data_9G9O
# 
_entry.id   9G9O 
# 
_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   9G9O         pdb_00009g9o 10.2210/pdb9g9o/pdb 
WWPDB D_1292140429 ?            ?                   
# 
_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                        9G9O 
_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 
PDB . 9G9N 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   0   MET MET A . n 
A 1 2   VAL 2   1   1   VAL VAL A . n 
A 1 3   SER 3   2   2   SER SER A . n 
A 1 4   LEU 4   3   3   LEU LEU A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   LYS 6   5   5   LYS LYS 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 ?   ?   ?   A . n 
A 1 417 ALA 417 416 ?   ?   ?   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   0   ALA ALA C . n 
C 3 3   GLN 3   1   1   GLN GLN 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'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    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                     9G9O 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.335 
_cell.length_a_esd                 ? 
_cell.length_b                     154.019 
_cell.length_b_esd                 ? 
_cell.length_c                     288.085 
_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                         9G9O 
_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                   9G9O 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          59.93 
_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    'sodium citrate, lithium sulfate, sodium chloride, PEG300, 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         2022-09-28 
_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   0.6702 
_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        0.6702 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G9O 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.69 
_reflns.d_resolution_low                               39.27 
_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                                     26959 
_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                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.1 
_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                                    2.69 
_reflns_shell.d_res_low                                     2.73 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           0.4 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1293 
_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                                  0.3 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                                 9G9O 
_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                            2.69 
_refine.ls_d_res_low                             38.50 
_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                     26804 
_refine.ls_number_reflns_R_free                  1295 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.30 
_refine.ls_percent_reflns_R_free                 4.83 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2822 
_refine.ls_R_factor_R_free                       0.3378 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2793 
_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                          1.33 
_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                 34.54 
_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                            0.53 
_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        5104 
_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               5104 
_refine_hist.d_res_high                       2.69 
_refine_hist.d_res_low                        38.50 
# 
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 ? 5221 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.451 ? 7098 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 3.755 ? 734  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.035 ? 811  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004 ? 881  ? 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' 2.69 2.80  . . 129 2739 98.00  . . . . 0.3801 . . . . . . . . . . . 0.3883 
'X-RAY DIFFRACTION' 2.80 2.92  . . 129 2784 100.00 . . . . 0.3561 . . . . . . . . . . . 0.4130 
'X-RAY DIFFRACTION' 2.92 3.08  . . 159 2813 100.00 . . . . 0.3407 . . . . . . . . . . . 0.3936 
'X-RAY DIFFRACTION' 3.08 3.27  . . 120 2845 100.00 . . . . 0.3153 . . . . . . . . . . . 0.3501 
'X-RAY DIFFRACTION' 3.27 3.52  . . 141 2830 100.00 . . . . 0.2916 . . . . . . . . . . . 0.3747 
'X-RAY DIFFRACTION' 3.52 3.88  . . 162 2813 100.00 . . . . 0.2515 . . . . . . . . . . . 0.3134 
'X-RAY DIFFRACTION' 3.88 4.44  . . 134 2838 99.00  . . . . 0.2777 . . . . . . . . . . . 0.3292 
'X-RAY DIFFRACTION' 4.44 5.59  . . 145 2835 98.00  . . . . 0.2745 . . . . . . . . . . . 0.3942 
'X-RAY DIFFRACTION' 5.59 38.50 . . 176 3012 100.00 . . . . 0.2280 . . . . . . . . . . . 0.2615 
# 
_struct.entry_id                     9G9O 
_struct.title                        
'Lipid III flippase WzxE with NB10 and NB7 nanobodies in outward-facing conformation - crystal 2' 
_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        9G9O 
_struct_keywords.text            'membrane protein, flippase, cell wall, enterobacterial common antigen, 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 9G9O       9G9O   ? 2 ? 1 
3 PDB 9G9O       9G9O   ? 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 9G9O A 3 ? 417 ? P0AAA7 2  ? 416 ? 2  416 
2 2 9G9O B 1 ? 140 ? 9G9O   -1 ? 138 ? -1 138 
3 3 9G9O C 1 ? 136 ? 9G9O   -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 9G9O MET A 1   ? UNP P0AAA7 ? ? 'initiating methionine' 0   1  
1 9G9O VAL A 2   ? UNP P0AAA7 ? ? 'cloning artifact'      1   2  
1 9G9O LEU A 418 ? UNP P0AAA7 ? ? 'expression tag'        417 3  
1 9G9O GLU A 419 ? UNP P0AAA7 ? ? 'expression tag'        418 4  
1 9G9O GLU A 420 ? UNP P0AAA7 ? ? 'expression tag'        419 5  
1 9G9O ASN A 421 ? UNP P0AAA7 ? ? 'expression tag'        420 6  
1 9G9O LEU A 422 ? UNP P0AAA7 ? ? 'expression tag'        421 7  
1 9G9O TYR A 423 ? UNP P0AAA7 ? ? 'expression tag'        422 8  
1 9G9O PHE A 424 ? UNP P0AAA7 ? ? 'expression tag'        423 9  
1 9G9O 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 3   ? ALA A 41  ? SER A 2   ALA A 40  1 ? 39 
HELX_P HELX_P2  AA2 ALA A 41  ? ALA A 55  ? ALA A 40  ALA A 54  1 ? 15 
HELX_P HELX_P3  AA3 ILE A 59  ? TYR A 70  ? ILE A 58  TYR A 69  1 ? 12 
HELX_P HELX_P4  AA4 ASN A 73  ? ALA A 102 ? ASN A 72  ALA A 101 1 ? 30 
HELX_P HELX_P5  AA5 ALA A 102 ? PHE A 111 ? ALA A 101 PHE A 110 1 ? 10 
HELX_P HELX_P6  AA6 TYR A 116 ? PHE A 143 ? TYR A 115 PHE A 142 1 ? 28 
HELX_P HELX_P7  AA7 ASP A 145 ? GLY A 172 ? ASP A 144 GLY A 171 1 ? 28 
HELX_P HELX_P8  AA8 GLY A 172 ? LEU A 186 ? GLY A 171 LEU A 185 1 ? 15 
HELX_P HELX_P9  AA9 VAL A 187 ? ARG A 198 ? VAL A 186 ARG A 197 1 ? 12 
HELX_P HELX_P10 AB1 PRO A 202 ? LYS A 207 ? PRO A 201 LYS A 206 5 ? 6  
HELX_P HELX_P11 AB2 ASP A 211 ? SER A 229 ? ASP A 210 SER A 228 1 ? 19 
HELX_P HELX_P12 AB3 VAL A 230 ? TYR A 247 ? VAL A 229 TYR A 246 1 ? 18 
HELX_P HELX_P13 AB4 SER A 248 ? SER A 274 ? SER A 247 SER A 273 1 ? 27 
HELX_P HELX_P14 AB5 TYR A 276 ? LEU A 284 ? TYR A 275 LEU A 283 1 ? 9  
HELX_P HELX_P15 AB6 GLU A 286 ? LEU A 315 ? GLU A 285 LEU A 314 1 ? 30 
HELX_P HELX_P16 AB7 LEU A 315 ? LEU A 322 ? LEU A 314 LEU A 321 1 ? 8  
HELX_P HELX_P17 AB8 PHE A 328 ? ARG A 332 ? PHE A 327 ARG A 331 5 ? 5  
HELX_P HELX_P18 AB9 ASP A 333 ? LYS A 358 ? ASP A 332 LYS A 357 1 ? 26 
HELX_P HELX_P19 AC1 SER A 360 ? ARG A 415 ? SER A 359 ARG A 414 1 ? 56 
HELX_P HELX_P20 AC2 THR B 30  ? TYR B 34  ? THR B 28  TYR B 32  5 ? 5  
HELX_P HELX_P21 AC3 ASN B 89  ? THR B 93  ? ASN B 87  THR B 91  5 ? 5  
HELX_P HELX_P22 AC4 LEU B 102 ? GLY B 107 ? LEU B 100 GLY B 105 1 ? 6  
HELX_P HELX_P23 AC5 ARG B 113 ? TYR B 117 ? ARG B 111 TYR B 115 5 ? 5  
HELX_P HELX_P24 AC6 THR C 30  ? TYR C 32  ? THR C 28  TYR C 30  5 ? 3  
HELX_P HELX_P25 AC7 ASP C 64  ? LYS C 67  ? ASP C 62  LYS C 65  5 ? 4  
HELX_P HELX_P26 AC8 LYS C 89  ? THR C 93  ? LYS C 87  THR C 91  5 ? 5  
HELX_P HELX_P27 AC9 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 ? ? ? ? ? ? ? 2.032 ? ? 
disulf2 disulf ? ? C CYS 24 SG ? ? ? 1_555 C CYS 98 SG ? ? C CYS 22 C CYS 96 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
# 
_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 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 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 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 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 LEU B 6   ? SER B 9   ? LEU B 4   SER B 7   
AA1 2 LEU B 20  ? ALA B 26  ? LEU B 18  ALA B 24  
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 B 13  ? VAL B 14  ? LEU B 11  VAL B 12  
AA3 2 THR B 124 ? VAL B 128 ? THR B 122 VAL B 126 
AA3 3 ALA B 94  ? THR B 101 ? ALA B 92  THR B 99  
AA3 4 TYR B 119 ? TRP B 120 ? TYR B 117 TRP B 118 
AA4 1 VAL C 4   ? SER C 9   ? VAL C 2   SER C 7   
AA4 2 LEU C 20  ? GLY C 28  ? LEU C 18  GLY C 26  
AA4 3 MET C 80  ? MET C 85  ? MET C 78  MET C 83  
AA4 4 PHE C 70  ? ASP C 75  ? PHE C 68  ASP C 73  
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 34  ? GLN C 41  ? TYR C 32  GLN C 39  
AA5 5 ARG C 47  ? ILE C 53  ? ARG C 45  ILE C 51  
AA5 6 THR C 60  ? TYR C 62  ? THR C 58  TYR C 60  
AA6 1 GLY C 12  ? GLN C 15  ? GLY C 10  GLN C 13  
AA6 2 THR C 120 ? SER C 125 ? THR C 118 SER C 123 
AA6 3 ALA C 94  ? PHE C 102 ? ALA C 92  PHE C 100 
AA6 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 SER B 9   ? N SER B 7   O SER B 23  ? O SER B 21  
AA1 2 3 N LEU B 20  ? N LEU B 18  O MET B 85  ? O MET B 83  
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 VAL B 14  ? N VAL B 12  O THR B 127 ? O THR B 125 
AA3 2 3 O THR B 124 ? O THR B 122 N TYR B 96  ? N TYR B 94  
AA3 3 4 N ALA B 100 ? N ALA B 98  O TYR B 119 ? O TYR B 117 
AA4 1 2 N VAL C 7   ? N VAL C 5   O ALA C 25  ? O ALA C 23  
AA4 2 3 N CYS C 24  ? N CYS C 22  O VAL C 81  ? O VAL C 79  
AA4 3 4 O TYR C 82  ? O TYR C 80  N SER C 73  ? N SER C 71  
AA5 1 2 N GLY C 12  ? N GLY C 10  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 O TYR C 97  ? O TYR C 95  N PHE C 39  ? N PHE C 37  
AA5 4 5 N TRP C 38  ? N TRP C 36  O ALA C 51  ? O ALA C 49  
AA5 5 6 N SER C 52  ? N SER C 50  O TYR C 61  ? O TYR C 59  
AA6 1 2 N GLY C 12  ? N GLY C 10  O THR C 123 ? O THR C 121 
AA6 2 3 O THR C 120 ? O THR C 118 N TYR C 96  ? N TYR C 94  
AA6 3 4 N ALA C 100 ? N ALA C 98  O TYR C 115 ? O TYR C 113 
# 
_pdbx_entry_details.entry_id                   9G9O 
_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 ALA A 101 ? ? -98.46  40.57   
2  1 VAL A 229 ? ? -133.70 -40.74  
3  1 THR A 230 ? ? -58.10  -75.57  
4  1 TYR A 246 ? ? -138.06 -148.51 
5  1 TYR A 275 ? ? -122.14 -53.45  
6  1 LEU A 321 ? ? -103.30 -69.75  
7  1 THR A 328 ? ? -65.09  2.05    
8  1 LYS B 43  ? ? -121.56 -156.16 
9  1 VAL B 48  ? ? -123.42 -68.29  
10 1 PRO C 41  ? ? -58.18  100.80  
11 1 VAL C 48  ? ? -120.06 -67.61  
# 
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 -4.6211 -34.6703 -46.4057 0.3634 ? 0.0013 ? 0.0315  ? 0.2938 ? 0.0129  ? 0.3998 ? 0.9364 ? -0.1642 
? 0.1805  ? 0.7700 ? -0.1653 ? 0.9206 ? -0.1087 ? -0.0596 ? -0.0950 ? 0.0853  ? 0.1245 ? 0.0700  ? -0.1149 ? -0.0741 ? -0.0153 ? 
2 'X-RAY DIFFRACTION' ? refined -7.1460 -5.9632  -13.0028 0.5642 ? 0.0055 ? -0.0705 ? 0.3530 ? 0.0027  ? 0.3358 ? 4.2843 ? -1.3184 
? -2.5813 ? 4.1301 ? 2.4463  ? 5.5310 ? -0.0353 ? 0.1339  ? -0.0369 ? -0.2854 ? 0.1137 ? -0.0882 ? 0.3123  ? 0.2168  ? -0.1214 ? 
3 'X-RAY DIFFRACTION' ? refined 5.1049  -53.6130 -6.0493  0.5857 ? 0.0623 ? 0.0022  ? 0.3090 ? -0.0042 ? 0.4831 ? 2.2613 ? 0.2261  
? 0.8959  ? 2.7678 ? -0.2350 ? 6.4389 ? -0.0125 ? -0.2784 ? 0.2839  ? 0.7549  ? 0.2335 ? 0.1762  ? -0.2420 ? -0.0953 ? -0.1942 ? 
# 
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 ? ? A 1 ? ? ? A 414 ? ? 
;(chain 'A' and resid 1 through 414)
;
2 'X-RAY DIFFRACTION' 2 ? ? B 2 ? ? ? B 127 ? ? 
;(chain 'B' and resid 2 through 127)
;
3 'X-RAY DIFFRACTION' 3 ? ? C 2 ? ? ? C 124 ? ? 
;(chain 'C' and resid 2 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 ARG 415 ? A ARG 416 
2  1 Y 1 A ALA 416 ? A ALA 417 
3  1 Y 1 A LEU 417 ? A LEU 418 
4  1 Y 1 A GLU 418 ? A GLU 419 
5  1 Y 1 A GLU 419 ? A GLU 420 
6  1 Y 1 A ASN 420 ? A ASN 421 
7  1 Y 1 A LEU 421 ? A LEU 422 
8  1 Y 1 A TYR 422 ? A TYR 423 
9  1 Y 1 A PHE 423 ? A PHE 424 
10 1 Y 1 A GLN 424 ? A GLN 425 
11 1 Y 1 B MET -1  ? B MET 1   
12 1 Y 1 B SER 128 ? B SER 130 
13 1 Y 1 B HIS 129 ? B HIS 131 
14 1 Y 1 B HIS 130 ? B HIS 132 
15 1 Y 1 B HIS 131 ? B HIS 133 
16 1 Y 1 B HIS 132 ? B HIS 134 
17 1 Y 1 B HIS 133 ? B HIS 135 
18 1 Y 1 B HIS 134 ? B HIS 136 
19 1 Y 1 B GLU 135 ? B GLU 137 
20 1 Y 1 B PRO 136 ? B PRO 138 
21 1 Y 1 B GLU 137 ? B GLU 139 
22 1 Y 1 B ALA 138 ? B ALA 140 
23 1 Y 1 C MET -1  ? C MET 1   
24 1 Y 1 C HIS 125 ? C HIS 127 
25 1 Y 1 C HIS 126 ? C HIS 128 
26 1 Y 1 C HIS 127 ? C HIS 129 
27 1 Y 1 C HIS 128 ? C HIS 130 
28 1 Y 1 C HIS 129 ? C HIS 131 
29 1 Y 1 C HIS 130 ? C HIS 132 
30 1 Y 1 C GLU 131 ? C GLU 133 
31 1 Y 1 C PRO 132 ? C PRO 134 
32 1 Y 1 C GLU 133 ? C GLU 135 
33 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                    9G9O 
_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]   0.023621 
_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]   0.006493 
_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]   0.003471 
_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   . MET A 1 1   ? 10.108  -36.614 -69.257 1.00 80.28  ? 0   MET A N   1 
ATOM 2    C CA  . MET A 1 1   ? 8.746   -37.127 -69.165 1.00 84.06  ? 0   MET A CA  1 
ATOM 3    C C   . MET A 1 1   ? 8.266   -37.099 -67.719 1.00 81.17  ? 0   MET A C   1 
ATOM 4    O O   . MET A 1 1   ? 9.072   -37.077 -66.789 1.00 81.84  ? 0   MET A O   1 
ATOM 5    C CB  . MET A 1 1   ? 8.665   -38.551 -69.729 1.00 85.18  ? 0   MET A CB  1 
ATOM 6    C CG  . MET A 1 1   ? 7.266   -38.989 -70.163 1.00 80.60  ? 0   MET A CG  1 
ATOM 7    S SD  . MET A 1 1   ? 6.251   -37.648 -70.820 1.00 80.77  ? 0   MET A SD  1 
ATOM 8    C CE  . MET A 1 1   ? 4.849   -38.555 -71.469 1.00 65.78  ? 0   MET A CE  1 
ATOM 9    N N   . VAL A 1 2   ? 6.953   -37.096 -67.537 1.00 81.77  ? 1   VAL A N   1 
ATOM 10   C CA  . VAL A 1 2   ? 6.343   -37.031 -66.215 1.00 79.33  ? 1   VAL A CA  1 
ATOM 11   C C   . VAL A 1 2   ? 6.130   -38.443 -65.692 1.00 74.26  ? 1   VAL A C   1 
ATOM 12   O O   . VAL A 1 2   ? 5.688   -39.336 -66.425 1.00 74.41  ? 1   VAL A O   1 
ATOM 13   C CB  . VAL A 1 2   ? 5.018   -36.248 -66.262 1.00 77.06  ? 1   VAL A CB  1 
ATOM 14   C CG1 . VAL A 1 2   ? 5.284   -34.752 -66.207 1.00 72.54  ? 1   VAL A CG1 1 
ATOM 15   C CG2 . VAL A 1 2   ? 4.238   -36.609 -67.517 1.00 77.86  ? 1   VAL A CG2 1 
ATOM 16   N N   . SER A 1 3   ? 6.449   -38.648 -64.417 1.00 68.82  ? 2   SER A N   1 
ATOM 17   C CA  . SER A 1 3   ? 6.265   -39.940 -63.775 1.00 67.41  ? 2   SER A CA  1 
ATOM 18   C C   . SER A 1 3   ? 6.032   -39.716 -62.289 1.00 61.20  ? 2   SER A C   1 
ATOM 19   O O   . SER A 1 3   ? 6.179   -38.604 -61.776 1.00 63.19  ? 2   SER A O   1 
ATOM 20   C CB  . SER A 1 3   ? 7.468   -40.861 -64.005 1.00 72.62  ? 2   SER A CB  1 
ATOM 21   O OG  . SER A 1 3   ? 8.560   -40.485 -63.185 1.00 65.35  ? 2   SER A OG  1 
ATOM 22   N N   . LEU A 1 4   ? 5.667   -40.796 -61.596 1.00 61.82  ? 3   LEU A N   1 
ATOM 23   C CA  . LEU A 1 4   ? 5.421   -40.696 -60.162 1.00 58.93  ? 3   LEU A CA  1 
ATOM 24   C C   . LEU A 1 4   ? 6.702   -40.405 -59.391 1.00 55.40  ? 3   LEU A C   1 
ATOM 25   O O   . LEU A 1 4   ? 6.653   -39.779 -58.326 1.00 58.03  ? 3   LEU A O   1 
ATOM 26   C CB  . LEU A 1 4   ? 4.767   -41.980 -59.653 1.00 54.21  ? 3   LEU A CB  1 
ATOM 27   C CG  . LEU A 1 4   ? 4.136   -41.943 -58.260 1.00 58.40  ? 3   LEU A CG  1 
ATOM 28   C CD1 . LEU A 1 4   ? 3.332   -40.668 -58.057 1.00 53.71  ? 3   LEU A CD1 1 
ATOM 29   C CD2 . LEU A 1 4   ? 3.259   -43.168 -58.054 1.00 56.94  ? 3   LEU A CD2 1 
ATOM 30   N N   . ALA A 1 5   ? 7.852   -40.838 -59.911 1.00 54.89  ? 4   ALA A N   1 
ATOM 31   C CA  . ALA A 1 5   ? 9.113   -40.599 -59.217 1.00 55.95  ? 4   ALA A CA  1 
ATOM 32   C C   . ALA A 1 5   ? 9.505   -39.128 -59.264 1.00 55.04  ? 4   ALA A C   1 
ATOM 33   O O   . ALA A 1 5   ? 9.955   -38.568 -58.258 1.00 54.41  ? 4   ALA A O   1 
ATOM 34   C CB  . ALA A 1 5   ? 10.217  -41.468 -59.818 1.00 64.87  ? 4   ALA A CB  1 
ATOM 35   N N   . LYS A 1 6   ? 9.346   -38.486 -60.425 1.00 55.66  ? 5   LYS A N   1 
ATOM 36   C CA  . LYS A 1 6   ? 9.670   -37.067 -60.531 1.00 57.32  ? 5   LYS A CA  1 
ATOM 37   C C   . LYS A 1 6   ? 8.738   -36.225 -59.667 1.00 56.85  ? 5   LYS A C   1 
ATOM 38   O O   . LYS A 1 6   ? 9.174   -35.253 -59.038 1.00 52.37  ? 5   LYS A O   1 
ATOM 39   C CB  . LYS A 1 6   ? 9.604   -36.621 -61.991 1.00 57.18  ? 5   LYS A CB  1 
ATOM 40   C CG  . LYS A 1 6   ? 10.092  -37.666 -62.985 1.00 65.65  ? 5   LYS A CG  1 
ATOM 41   C CD  . LYS A 1 6   ? 11.457  -37.309 -63.552 1.00 65.05  ? 5   LYS A CD  1 
ATOM 42   C CE  . LYS A 1 6   ? 11.921  -38.340 -64.572 1.00 59.47  ? 5   LYS A CE  1 
ATOM 43   N NZ  . LYS A 1 6   ? 13.169  -37.915 -65.267 1.00 64.30  ? 5   LYS A NZ  1 
ATOM 44   N N   . ALA A 1 7   ? 7.453   -36.585 -59.622 1.00 55.21  ? 6   ALA A N   1 
ATOM 45   C CA  . ALA A 1 7   ? 6.524   -35.884 -58.744 1.00 48.25  ? 6   ALA A CA  1 
ATOM 46   C C   . ALA A 1 7   ? 6.840   -36.143 -57.278 1.00 52.00  ? 6   ALA A C   1 
ATOM 47   O O   . ALA A 1 7   ? 6.660   -35.252 -56.441 1.00 56.13  ? 6   ALA A O   1 
ATOM 48   C CB  . ALA A 1 7   ? 5.087   -36.296 -59.059 1.00 47.89  ? 6   ALA A CB  1 
ATOM 49   N N   . SER A 1 8   ? 7.317   -37.346 -56.950 1.00 52.26  ? 7   SER A N   1 
ATOM 50   C CA  . SER A 1 8   ? 7.682   -37.645 -55.569 1.00 49.44  ? 7   SER A CA  1 
ATOM 51   C C   . SER A 1 8   ? 8.913   -36.863 -55.131 1.00 49.55  ? 7   SER A C   1 
ATOM 52   O O   . SER A 1 8   ? 9.036   -36.517 -53.951 1.00 52.44  ? 7   SER A O   1 
ATOM 53   C CB  . SER A 1 8   ? 7.919   -39.144 -55.399 1.00 52.75  ? 7   SER A CB  1 
ATOM 54   O OG  . SER A 1 8   ? 6.753   -39.881 -55.722 1.00 55.10  ? 7   SER A OG  1 
ATOM 55   N N   . LEU A 1 9   ? 9.831   -36.578 -56.058 1.00 51.58  ? 8   LEU A N   1 
ATOM 56   C CA  . LEU A 1 9   ? 11.005  -35.783 -55.711 1.00 46.05  ? 8   LEU A CA  1 
ATOM 57   C C   . LEU A 1 9   ? 10.619  -34.347 -55.384 1.00 47.58  ? 8   LEU A C   1 
ATOM 58   O O   . LEU A 1 9   ? 11.134  -33.763 -54.424 1.00 52.57  ? 8   LEU A O   1 
ATOM 59   C CB  . LEU A 1 9   ? 12.018  -35.811 -56.854 1.00 48.77  ? 8   LEU A CB  1 
ATOM 60   C CG  . LEU A 1 9   ? 13.209  -36.753 -56.689 1.00 51.25  ? 8   LEU A CG  1 
ATOM 61   C CD1 . LEU A 1 9   ? 13.934  -36.913 -58.015 1.00 43.49  ? 8   LEU A CD1 1 
ATOM 62   C CD2 . LEU A 1 9   ? 14.153  -36.250 -55.608 1.00 49.13  ? 8   LEU A CD2 1 
ATOM 63   N N   . TRP A 1 10  ? 9.721   -33.760 -56.176 1.00 48.34  ? 9   TRP A N   1 
ATOM 64   C CA  . TRP A 1 10  ? 9.239   -32.418 -55.873 1.00 47.46  ? 9   TRP A CA  1 
ATOM 65   C C   . TRP A 1 10  ? 8.355   -32.422 -54.636 1.00 48.46  ? 9   TRP A C   1 
ATOM 66   O O   . TRP A 1 10  ? 8.372   -31.467 -53.851 1.00 51.54  ? 9   TRP A O   1 
ATOM 67   C CB  . TRP A 1 10  ? 8.477   -31.853 -57.068 1.00 50.65  ? 9   TRP A CB  1 
ATOM 68   C CG  . TRP A 1 10  ? 9.357   -31.252 -58.105 1.00 50.17  ? 9   TRP A CG  1 
ATOM 69   C CD1 . TRP A 1 10  ? 9.488   -31.655 -59.401 1.00 52.35  ? 9   TRP A CD1 1 
ATOM 70   C CD2 . TRP A 1 10  ? 10.233  -30.131 -57.943 1.00 50.45  ? 9   TRP A CD2 1 
ATOM 71   N NE1 . TRP A 1 10  ? 10.391  -30.855 -60.057 1.00 51.40  ? 9   TRP A NE1 1 
ATOM 72   C CE2 . TRP A 1 10  ? 10.863  -29.911 -59.184 1.00 48.30  ? 9   TRP A CE2 1 
ATOM 73   C CE3 . TRP A 1 10  ? 10.545  -29.292 -56.869 1.00 48.99  ? 9   TRP A CE3 1 
ATOM 74   C CZ2 . TRP A 1 10  ? 11.786  -28.888 -59.381 1.00 46.95  ? 9   TRP A CZ2 1 
ATOM 75   C CZ3 . TRP A 1 10  ? 11.463  -28.279 -57.066 1.00 52.17  ? 9   TRP A CZ3 1 
ATOM 76   C CH2 . TRP A 1 10  ? 12.072  -28.083 -58.313 1.00 48.80  ? 9   TRP A CH2 1 
ATOM 77   N N   . THR A 1 11  ? 7.571   -33.484 -54.452 1.00 47.54  ? 10  THR A N   1 
ATOM 78   C CA  . THR A 1 11  ? 6.745   -33.600 -53.256 1.00 49.60  ? 10  THR A CA  1 
ATOM 79   C C   . THR A 1 11  ? 7.606   -33.759 -52.009 1.00 48.02  ? 10  THR A C   1 
ATOM 80   O O   . THR A 1 11  ? 7.321   -33.153 -50.970 1.00 51.60  ? 10  THR A O   1 
ATOM 81   C CB  . THR A 1 11  ? 5.778   -34.776 -53.404 1.00 54.98  ? 10  THR A CB  1 
ATOM 82   O OG1 . THR A 1 11  ? 4.642   -34.367 -54.177 1.00 52.65  ? 10  THR A OG1 1 
ATOM 83   C CG2 . THR A 1 11  ? 5.316   -35.282 -52.046 1.00 61.01  ? 10  THR A CG2 1 
ATOM 84   N N   . ALA A 1 12  ? 8.674   -34.557 -52.100 1.00 49.77  ? 11  ALA A N   1 
ATOM 85   C CA  . ALA A 1 12  ? 9.559   -34.743 -50.956 1.00 54.70  ? 11  ALA A CA  1 
ATOM 86   C C   . ALA A 1 12  ? 10.225  -33.439 -50.540 1.00 51.00  ? 11  ALA A C   1 
ATOM 87   O O   . ALA A 1 12  ? 10.506  -33.238 -49.353 1.00 51.49  ? 11  ALA A O   1 
ATOM 88   C CB  . ALA A 1 12  ? 10.618  -35.800 -51.273 1.00 49.02  ? 11  ALA A CB  1 
ATOM 89   N N   . ALA A 1 13  ? 10.485  -32.544 -51.494 1.00 47.87  ? 12  ALA A N   1 
ATOM 90   C CA  . ALA A 1 13  ? 11.078  -31.256 -51.152 1.00 46.39  ? 12  ALA A CA  1 
ATOM 91   C C   . ALA A 1 13  ? 10.081  -30.376 -50.409 1.00 48.08  ? 12  ALA A C   1 
ATOM 92   O O   . ALA A 1 13  ? 10.416  -29.772 -49.384 1.00 54.54  ? 12  ALA A O   1 
ATOM 93   C CB  . ALA A 1 13  ? 11.585  -30.557 -52.413 1.00 39.92  ? 12  ALA A CB  1 
ATOM 94   N N   . SER A 1 14  ? 8.845   -30.296 -50.908 1.00 52.34  ? 13  SER A N   1 
ATOM 95   C CA  . SER A 1 14  ? 7.835   -29.478 -50.242 1.00 50.29  ? 13  SER A CA  1 
ATOM 96   C C   . SER A 1 14  ? 7.436   -30.078 -48.900 1.00 47.85  ? 13  SER A C   1 
ATOM 97   O O   . SER A 1 14  ? 7.176   -29.344 -47.939 1.00 46.51  ? 13  SER A O   1 
ATOM 98   C CB  . SER A 1 14  ? 6.609   -29.309 -51.142 1.00 45.95  ? 13  SER A CB  1 
ATOM 99   O OG  . SER A 1 14  ? 5.932   -30.541 -51.322 1.00 52.11  ? 13  SER A OG  1 
ATOM 100  N N   . THR A 1 15  ? 7.380   -31.409 -48.812 1.00 56.24  ? 14  THR A N   1 
ATOM 101  C CA  . THR A 1 15  ? 7.060   -32.050 -47.541 1.00 54.28  ? 14  THR A CA  1 
ATOM 102  C C   . THR A 1 15  ? 8.168   -31.851 -46.517 1.00 52.64  ? 14  THR A C   1 
ATOM 103  O O   . THR A 1 15  ? 7.887   -31.720 -45.320 1.00 53.03  ? 14  THR A O   1 
ATOM 104  C CB  . THR A 1 15  ? 6.801   -33.543 -47.742 1.00 57.59  ? 14  THR A CB  1 
ATOM 105  O OG1 . THR A 1 15  ? 6.110   -33.752 -48.980 1.00 64.02  ? 14  THR A OG1 1 
ATOM 106  C CG2 . THR A 1 15  ? 5.969   -34.093 -46.596 1.00 58.99  ? 14  THR A CG2 1 
ATOM 107  N N   . LEU A 1 16  ? 9.426   -31.834 -46.961 1.00 51.49  ? 15  LEU A N   1 
ATOM 108  C CA  . LEU A 1 16  ? 10.528  -31.572 -46.041 1.00 48.20  ? 15  LEU A CA  1 
ATOM 109  C C   . LEU A 1 16  ? 10.410  -30.185 -45.425 1.00 51.34  ? 15  LEU A C   1 
ATOM 110  O O   . LEU A 1 16  ? 10.634  -30.012 -44.221 1.00 56.26  ? 15  LEU A O   1 
ATOM 111  C CB  . LEU A 1 16  ? 11.863  -31.729 -46.767 1.00 47.74  ? 15  LEU A CB  1 
ATOM 112  C CG  . LEU A 1 16  ? 13.121  -31.630 -45.907 1.00 43.08  ? 15  LEU A CG  1 
ATOM 113  C CD1 . LEU A 1 16  ? 13.304  -32.896 -45.090 1.00 51.80  ? 15  LEU A CD1 1 
ATOM 114  C CD2 . LEU A 1 16  ? 14.335  -31.377 -46.781 1.00 45.38  ? 15  LEU A CD2 1 
ATOM 115  N N   . VAL A 1 17  ? 10.049  -29.184 -46.232 1.00 48.15  ? 16  VAL A N   1 
ATOM 116  C CA  . VAL A 1 17  ? 9.887   -27.833 -45.704 1.00 50.63  ? 16  VAL A CA  1 
ATOM 117  C C   . VAL A 1 17  ? 8.608   -27.724 -44.883 1.00 48.34  ? 16  VAL A C   1 
ATOM 118  O O   . VAL A 1 17  ? 8.558   -26.981 -43.895 1.00 45.21  ? 16  VAL A O   1 
ATOM 119  C CB  . VAL A 1 17  ? 9.910   -26.804 -46.851 1.00 47.35  ? 16  VAL A CB  1 
ATOM 120  C CG1 . VAL A 1 17  ? 9.897   -25.385 -46.300 1.00 41.73  ? 16  VAL A CG1 1 
ATOM 121  C CG2 . VAL A 1 17  ? 11.125  -27.023 -47.737 1.00 46.33  ? 16  VAL A CG2 1 
ATOM 122  N N   . LYS A 1 18  ? 7.563   -28.462 -45.264 1.00 46.48  ? 17  LYS A N   1 
ATOM 123  C CA  . LYS A 1 18  ? 6.292   -28.384 -44.550 1.00 46.69  ? 17  LYS A CA  1 
ATOM 124  C C   . LYS A 1 18  ? 6.413   -28.951 -43.140 1.00 48.45  ? 17  LYS A C   1 
ATOM 125  O O   . LYS A 1 18  ? 5.985   -28.319 -42.167 1.00 46.00  ? 17  LYS A O   1 
ATOM 126  C CB  . LYS A 1 18  ? 5.206   -29.119 -45.337 1.00 49.33  ? 17  LYS A CB  1 
ATOM 127  C CG  . LYS A 1 18  ? 3.850   -29.154 -44.650 1.00 46.87  ? 17  LYS A CG  1 
ATOM 128  C CD  . LYS A 1 18  ? 2.793   -29.779 -45.545 1.00 50.54  ? 17  LYS A CD  1 
ATOM 129  C CE  . LYS A 1 18  ? 1.488   -29.976 -44.796 1.00 52.75  ? 17  LYS A CE  1 
ATOM 130  N NZ  . LYS A 1 18  ? 0.833   -28.675 -44.484 1.00 50.38  ? 17  LYS A NZ  1 
ATOM 131  N N   . ILE A 1 19  ? 6.991   -30.148 -43.007 1.00 52.14  ? 18  ILE A N   1 
ATOM 132  C CA  . ILE A 1 19  ? 7.152   -30.733 -41.680 1.00 48.34  ? 18  ILE A CA  1 
ATOM 133  C C   . ILE A 1 19  ? 8.197   -29.965 -40.881 1.00 49.28  ? 18  ILE A C   1 
ATOM 134  O O   . ILE A 1 19  ? 8.094   -29.862 -39.653 1.00 49.61  ? 18  ILE A O   1 
ATOM 135  C CB  . ILE A 1 19  ? 7.494   -32.235 -41.782 1.00 53.06  ? 18  ILE A CB  1 
ATOM 136  C CG1 . ILE A 1 19  ? 8.901   -32.451 -42.345 1.00 52.66  ? 18  ILE A CG1 1 
ATOM 137  C CG2 . ILE A 1 19  ? 6.457   -32.967 -42.626 1.00 51.96  ? 18  ILE A CG2 1 
ATOM 138  C CD1 . ILE A 1 19  ? 9.651   -33.593 -41.690 1.00 54.29  ? 18  ILE A CD1 1 
ATOM 139  N N   . GLY A 1 20  ? 9.203   -29.399 -41.553 1.00 50.97  ? 19  GLY A N   1 
ATOM 140  C CA  . GLY A 1 20  ? 10.188  -28.597 -40.847 1.00 53.02  ? 19  GLY A CA  1 
ATOM 141  C C   . GLY A 1 20  ? 9.602   -27.311 -40.296 1.00 55.05  ? 19  GLY A C   1 
ATOM 142  O O   . GLY A 1 20  ? 9.887   -26.925 -39.158 1.00 52.16  ? 19  GLY A O   1 
ATOM 143  N N   . ALA A 1 21  ? 8.774   -26.631 -41.093 1.00 48.01  ? 20  ALA A N   1 
ATOM 144  C CA  . ALA A 1 21  ? 8.105   -25.428 -40.611 1.00 45.92  ? 20  ALA A CA  1 
ATOM 145  C C   . ALA A 1 21  ? 7.084   -25.752 -39.531 1.00 47.18  ? 20  ALA A C   1 
ATOM 146  O O   . ALA A 1 21  ? 6.887   -24.953 -38.609 1.00 47.38  ? 20  ALA A O   1 
ATOM 147  C CB  . ALA A 1 21  ? 7.434   -24.698 -41.773 1.00 49.47  ? 20  ALA A CB  1 
ATOM 148  N N   . GLY A 1 22  ? 6.426   -26.909 -39.625 1.00 49.52  ? 21  GLY A N   1 
ATOM 149  C CA  . GLY A 1 22  ? 5.478   -27.293 -38.593 1.00 47.31  ? 21  GLY A CA  1 
ATOM 150  C C   . GLY A 1 22  ? 6.158   -27.661 -37.288 1.00 45.94  ? 21  GLY A C   1 
ATOM 151  O O   . GLY A 1 22  ? 5.629   -27.396 -36.205 1.00 43.96  ? 21  GLY A O   1 
ATOM 152  N N   . LEU A 1 23  ? 7.338   -28.278 -37.372 1.00 46.76  ? 22  LEU A N   1 
ATOM 153  C CA  . LEU A 1 23  ? 8.087   -28.601 -36.163 1.00 43.89  ? 22  LEU A CA  1 
ATOM 154  C C   . LEU A 1 23  ? 8.648   -27.343 -35.512 1.00 46.66  ? 22  LEU A C   1 
ATOM 155  O O   . LEU A 1 23  ? 8.676   -27.234 -34.280 1.00 46.88  ? 22  LEU A O   1 
ATOM 156  C CB  . LEU A 1 23  ? 9.212   -29.583 -36.488 1.00 46.47  ? 22  LEU A CB  1 
ATOM 157  C CG  . LEU A 1 23  ? 8.813   -31.033 -36.775 1.00 47.21  ? 22  LEU A CG  1 
ATOM 158  C CD1 . LEU A 1 23  ? 10.049  -31.902 -36.928 1.00 40.71  ? 22  LEU A CD1 1 
ATOM 159  C CD2 . LEU A 1 23  ? 7.896   -31.581 -35.689 1.00 45.31  ? 22  LEU A CD2 1 
ATOM 160  N N   . LEU A 1 24  ? 9.104   -26.387 -36.321 1.00 46.76  ? 23  LEU A N   1 
ATOM 161  C CA  . LEU A 1 24  ? 9.636   -25.145 -35.772 1.00 46.01  ? 23  LEU A CA  1 
ATOM 162  C C   . LEU A 1 24  ? 8.544   -24.340 -35.081 1.00 50.95  ? 23  LEU A C   1 
ATOM 163  O O   . LEU A 1 24  ? 8.709   -23.904 -33.936 1.00 52.32  ? 23  LEU A O   1 
ATOM 164  C CB  . LEU A 1 24  ? 10.292  -24.322 -36.880 1.00 45.11  ? 23  LEU A CB  1 
ATOM 165  C CG  . LEU A 1 24  ? 10.670  -22.888 -36.510 1.00 41.36  ? 23  LEU A CG  1 
ATOM 166  C CD1 . LEU A 1 24  ? 11.723  -22.874 -35.408 1.00 37.64  ? 23  LEU A CD1 1 
ATOM 167  C CD2 . LEU A 1 24  ? 11.157  -22.141 -37.741 1.00 36.50  ? 23  LEU A CD2 1 
ATOM 168  N N   . VAL A 1 25  ? 7.418   -24.135 -35.765 1.00 48.75  ? 24  VAL A N   1 
ATOM 169  C CA  . VAL A 1 25  ? 6.313   -23.387 -35.173 1.00 50.14  ? 24  VAL A CA  1 
ATOM 170  C C   . VAL A 1 25  ? 5.752   -24.126 -33.965 1.00 50.95  ? 24  VAL A C   1 
ATOM 171  O O   . VAL A 1 25  ? 5.460   -23.518 -32.928 1.00 53.01  ? 24  VAL A O   1 
ATOM 172  C CB  . VAL A 1 25  ? 5.230   -23.116 -36.233 1.00 40.10  ? 24  VAL A CB  1 
ATOM 173  C CG1 . VAL A 1 25  ? 4.039   -22.436 -35.603 1.00 44.16  ? 24  VAL A CG1 1 
ATOM 174  C CG2 . VAL A 1 25  ? 5.797   -22.256 -37.351 1.00 43.19  ? 24  VAL A CG2 1 
ATOM 175  N N   . GLY A 1 26  ? 5.610   -25.450 -34.071 1.00 51.48  ? 25  GLY A N   1 
ATOM 176  C CA  . GLY A 1 26  ? 5.074   -26.219 -32.958 1.00 53.59  ? 25  GLY A CA  1 
ATOM 177  C C   . GLY A 1 26  ? 5.922   -26.116 -31.704 1.00 50.24  ? 25  GLY A C   1 
ATOM 178  O O   . GLY A 1 26  ? 5.394   -26.013 -30.594 1.00 44.87  ? 25  GLY A O   1 
ATOM 179  N N   . LYS A 1 27  ? 7.246   -26.143 -31.861 1.00 48.04  ? 26  LYS A N   1 
ATOM 180  C CA  . LYS A 1 27  ? 8.124   -25.989 -30.706 1.00 48.80  ? 26  LYS A CA  1 
ATOM 181  C C   . LYS A 1 27  ? 8.012   -24.590 -30.115 1.00 54.16  ? 26  LYS A C   1 
ATOM 182  O O   . LYS A 1 27  ? 8.092   -24.419 -28.893 1.00 58.47  ? 26  LYS A O   1 
ATOM 183  C CB  . LYS A 1 27  ? 9.569   -26.296 -31.098 1.00 52.56  ? 26  LYS A CB  1 
ATOM 184  C CG  . LYS A 1 27  ? 10.543  -26.318 -29.928 1.00 56.62  ? 26  LYS A CG  1 
ATOM 185  C CD  . LYS A 1 27  ? 10.291  -27.512 -29.016 1.00 65.96  ? 26  LYS A CD  1 
ATOM 186  C CE  . LYS A 1 27  ? 10.585  -27.171 -27.562 1.00 59.06  ? 26  LYS A CE  1 
ATOM 187  N NZ  . LYS A 1 27  ? 10.571  -28.378 -26.688 1.00 49.29  ? 26  LYS A NZ  1 
ATOM 188  N N   . LEU A 1 28  ? 7.825   -23.577 -30.965 1.00 55.03  ? 27  LEU A N   1 
ATOM 189  C CA  . LEU A 1 28  ? 7.614   -22.223 -30.463 1.00 53.10  ? 27  LEU A CA  1 
ATOM 190  C C   . LEU A 1 28  ? 6.270   -22.088 -29.761 1.00 55.09  ? 27  LEU A C   1 
ATOM 191  O O   . LEU A 1 28  ? 6.136   -21.282 -28.834 1.00 55.05  ? 27  LEU A O   1 
ATOM 192  C CB  . LEU A 1 28  ? 7.714   -21.213 -31.604 1.00 50.30  ? 27  LEU A CB  1 
ATOM 193  C CG  . LEU A 1 28  ? 9.071   -21.097 -32.295 1.00 51.02  ? 27  LEU A CG  1 
ATOM 194  C CD1 . LEU A 1 28  ? 9.114   -19.854 -33.168 1.00 48.79  ? 27  LEU A CD1 1 
ATOM 195  C CD2 . LEU A 1 28  ? 10.197  -21.084 -31.275 1.00 48.13  ? 27  LEU A CD2 1 
ATOM 196  N N   . LEU A 1 29  ? 5.265   -22.853 -30.195 1.00 62.15  ? 28  LEU A N   1 
ATOM 197  C CA  . LEU A 1 29  ? 3.993   -22.876 -29.479 1.00 61.23  ? 28  LEU A CA  1 
ATOM 198  C C   . LEU A 1 29  ? 4.169   -23.395 -28.059 1.00 61.41  ? 28  LEU A C   1 
ATOM 199  O O   . LEU A 1 29  ? 3.558   -22.873 -27.119 1.00 60.95  ? 28  LEU A O   1 
ATOM 200  C CB  . LEU A 1 29  ? 2.974   -23.737 -30.229 1.00 60.91  ? 28  LEU A CB  1 
ATOM 201  C CG  . LEU A 1 29  ? 2.026   -23.107 -31.253 1.00 57.12  ? 28  LEU A CG  1 
ATOM 202  C CD1 . LEU A 1 29  ? 0.826   -22.474 -30.562 1.00 54.33  ? 28  LEU A CD1 1 
ATOM 203  C CD2 . LEU A 1 29  ? 2.735   -22.099 -32.135 1.00 57.25  ? 28  LEU A CD2 1 
ATOM 204  N N   . ALA A 1 30  ? 4.995   -24.428 -27.883 1.00 59.30  ? 29  ALA A N   1 
ATOM 205  C CA  . ALA A 1 30  ? 5.132   -25.034 -26.563 1.00 56.81  ? 29  ALA A CA  1 
ATOM 206  C C   . ALA A 1 30  ? 5.976   -24.168 -25.640 1.00 60.17  ? 29  ALA A C   1 
ATOM 207  O O   . ALA A 1 30  ? 5.638   -23.991 -24.464 1.00 64.35  ? 29  ALA A O   1 
ATOM 208  C CB  . ALA A 1 30  ? 5.725   -26.437 -26.685 1.00 51.14  ? 29  ALA A CB  1 
ATOM 209  N N   . VAL A 1 31  ? 7.073   -23.612 -26.154 1.00 57.77  ? 30  VAL A N   1 
ATOM 210  C CA  . VAL A 1 31  ? 7.935   -22.789 -25.315 1.00 57.81  ? 30  VAL A CA  1 
ATOM 211  C C   . VAL A 1 31  ? 7.227   -21.505 -24.904 1.00 57.21  ? 30  VAL A C   1 
ATOM 212  O O   . VAL A 1 31  ? 7.451   -20.991 -23.802 1.00 60.80  ? 30  VAL A O   1 
ATOM 213  C CB  . VAL A 1 31  ? 9.261   -22.502 -26.043 1.00 53.63  ? 30  VAL A CB  1 
ATOM 214  C CG1 . VAL A 1 31  ? 10.135  -21.564 -25.224 1.00 46.55  ? 30  VAL A CG1 1 
ATOM 215  C CG2 . VAL A 1 31  ? 9.985   -23.798 -26.335 1.00 51.96  ? 30  VAL A CG2 1 
ATOM 216  N N   . SER A 1 32  ? 6.351   -20.974 -25.753 1.00 60.22  ? 31  SER A N   1 
ATOM 217  C CA  . SER A 1 32  ? 5.761   -19.680 -25.434 1.00 60.63  ? 31  SER A CA  1 
ATOM 218  C C   . SER A 1 32  ? 4.527   -19.821 -24.552 1.00 57.28  ? 31  SER A C   1 
ATOM 219  O O   . SER A 1 32  ? 4.326   -19.021 -23.632 1.00 56.55  ? 31  SER A O   1 
ATOM 220  C CB  . SER A 1 32  ? 5.426   -18.933 -26.722 1.00 54.92  ? 31  SER A CB  1 
ATOM 221  O OG  . SER A 1 32  ? 6.525   -18.988 -27.616 1.00 55.30  ? 31  SER A OG  1 
ATOM 222  N N   . PHE A 1 33  ? 3.701   -20.837 -24.803 1.00 52.63  ? 32  PHE A N   1 
ATOM 223  C CA  . PHE A 1 33  ? 2.412   -20.962 -24.141 1.00 52.85  ? 32  PHE A CA  1 
ATOM 224  C C   . PHE A 1 33  ? 2.250   -22.224 -23.306 1.00 55.60  ? 32  PHE A C   1 
ATOM 225  O O   . PHE A 1 33  ? 1.410   -22.233 -22.397 1.00 53.81  ? 32  PHE A O   1 
ATOM 226  C CB  . PHE A 1 33  ? 1.278   -20.898 -25.175 1.00 53.46  ? 32  PHE A CB  1 
ATOM 227  C CG  . PHE A 1 33  ? 1.409   -19.751 -26.142 1.00 57.04  ? 32  PHE A CG  1 
ATOM 228  C CD1 . PHE A 1 33  ? 1.373   -18.440 -25.693 1.00 55.12  ? 32  PHE A CD1 1 
ATOM 229  C CD2 . PHE A 1 33  ? 1.571   -19.983 -27.497 1.00 53.86  ? 32  PHE A CD2 1 
ATOM 230  C CE1 . PHE A 1 33  ? 1.490   -17.384 -26.579 1.00 53.76  ? 32  PHE A CE1 1 
ATOM 231  C CE2 . PHE A 1 33  ? 1.690   -18.932 -28.386 1.00 53.17  ? 32  PHE A CE2 1 
ATOM 232  C CZ  . PHE A 1 33  ? 1.648   -17.630 -27.926 1.00 48.33  ? 32  PHE A CZ  1 
ATOM 233  N N   . GLY A 1 34  ? 3.012   -23.279 -23.580 1.00 51.25  ? 33  GLY A N   1 
ATOM 234  C CA  . GLY A 1 34  ? 2.970   -24.474 -22.773 1.00 51.17  ? 33  GLY A CA  1 
ATOM 235  C C   . GLY A 1 34  ? 1.714   -25.292 -22.987 1.00 55.27  ? 33  GLY A C   1 
ATOM 236  O O   . GLY A 1 34  ? 0.963   -25.089 -23.947 1.00 60.51  ? 33  GLY A O   1 
ATOM 237  N N   . PRO A 1 35  ? 1.464   -26.244 -22.084 1.00 51.87  ? 34  PRO A N   1 
ATOM 238  C CA  . PRO A 1 35  ? 0.287   -27.113 -22.245 1.00 51.85  ? 34  PRO A CA  1 
ATOM 239  C C   . PRO A 1 35  ? -1.035  -26.381 -22.097 1.00 53.93  ? 34  PRO A C   1 
ATOM 240  O O   . PRO A 1 35  ? -2.037  -26.822 -22.673 1.00 54.39  ? 34  PRO A O   1 
ATOM 241  C CB  . PRO A 1 35  ? 0.473   -28.164 -21.140 1.00 58.05  ? 34  PRO A CB  1 
ATOM 242  C CG  . PRO A 1 35  ? 1.928   -28.088 -20.768 1.00 55.18  ? 34  PRO A CG  1 
ATOM 243  C CD  . PRO A 1 35  ? 2.297   -26.650 -20.941 1.00 50.83  ? 34  PRO A CD  1 
ATOM 244  N N   . ALA A 1 36  ? -1.072  -25.282 -21.340 1.00 61.76  ? 35  ALA A N   1 
ATOM 245  C CA  . ALA A 1 36  ? -2.319  -24.543 -21.166 1.00 54.92  ? 35  ALA A CA  1 
ATOM 246  C C   . ALA A 1 36  ? -2.776  -23.925 -22.481 1.00 56.55  ? 35  ALA A C   1 
ATOM 247  O O   . ALA A 1 36  ? -3.930  -24.094 -22.891 1.00 62.66  ? 35  ALA A O   1 
ATOM 248  C CB  . ALA A 1 36  ? -2.147  -23.466 -20.096 1.00 54.47  ? 35  ALA A CB  1 
ATOM 249  N N   . GLY A 1 37  ? -1.880  -23.203 -23.157 1.00 52.41  ? 36  GLY A N   1 
ATOM 250  C CA  . GLY A 1 37  ? -2.218  -22.651 -24.456 1.00 55.86  ? 36  GLY A CA  1 
ATOM 251  C C   . GLY A 1 37  ? -2.423  -23.712 -25.517 1.00 50.91  ? 36  GLY A C   1 
ATOM 252  O O   . GLY A 1 37  ? -3.255  -23.544 -26.413 1.00 52.33  ? 36  GLY A O   1 
ATOM 253  N N   . LEU A 1 38  ? -1.677  -24.816 -25.434 1.00 50.42  ? 37  LEU A N   1 
ATOM 254  C CA  . LEU A 1 38  ? -1.850  -25.894 -26.400 1.00 50.78  ? 37  LEU A CA  1 
ATOM 255  C C   . LEU A 1 38  ? -3.208  -26.567 -26.250 1.00 50.82  ? 37  LEU A C   1 
ATOM 256  O O   . LEU A 1 38  ? -3.769  -27.055 -27.237 1.00 54.53  ? 37  LEU A O   1 
ATOM 257  C CB  . LEU A 1 38  ? -0.725  -26.919 -26.253 1.00 48.77  ? 37  LEU A CB  1 
ATOM 258  C CG  . LEU A 1 38  ? 0.399   -26.824 -27.286 1.00 52.18  ? 37  LEU A CG  1 
ATOM 259  C CD1 . LEU A 1 38  ? 1.135   -25.500 -27.154 1.00 56.30  ? 37  LEU A CD1 1 
ATOM 260  C CD2 . LEU A 1 38  ? 1.365   -27.993 -27.155 1.00 50.80  ? 37  LEU A CD2 1 
ATOM 261  N N   . GLY A 1 39  ? -3.754  -26.597 -25.031 1.00 50.15  ? 38  GLY A N   1 
ATOM 262  C CA  . GLY A 1 39  ? -5.069  -27.180 -24.829 1.00 51.17  ? 38  GLY A CA  1 
ATOM 263  C C   . GLY A 1 39  ? -6.203  -26.282 -25.269 1.00 55.43  ? 38  GLY A C   1 
ATOM 264  O O   . GLY A 1 39  ? -7.242  -26.772 -25.722 1.00 59.76  ? 38  GLY A O   1 
ATOM 265  N N   . LEU A 1 40  ? -6.029  -24.963 -25.142 1.00 53.95  ? 39  LEU A N   1 
ATOM 266  C CA  . LEU A 1 40  ? -7.047  -24.029 -25.610 1.00 54.26  ? 39  LEU A CA  1 
ATOM 267  C C   . LEU A 1 40  ? -7.113  -23.976 -27.130 1.00 55.68  ? 39  LEU A C   1 
ATOM 268  O O   . LEU A 1 40  ? -8.201  -23.814 -27.695 1.00 54.56  ? 39  LEU A O   1 
ATOM 269  C CB  . LEU A 1 40  ? -6.775  -22.631 -25.058 1.00 50.82  ? 39  LEU A CB  1 
ATOM 270  C CG  . LEU A 1 40  ? -7.329  -22.303 -23.676 1.00 47.81  ? 39  LEU A CG  1 
ATOM 271  C CD1 . LEU A 1 40  ? -6.759  -20.980 -23.195 1.00 44.70  ? 39  LEU A CD1 1 
ATOM 272  C CD2 . LEU A 1 40  ? -8.846  -22.265 -23.708 1.00 44.31  ? 39  LEU A CD2 1 
ATOM 273  N N   . ALA A 1 41  ? -5.973  -24.107 -27.803 1.00 51.20  ? 40  ALA A N   1 
ATOM 274  C CA  . ALA A 1 41  ? -5.902  -24.030 -29.254 1.00 48.71  ? 40  ALA A CA  1 
ATOM 275  C C   . ALA A 1 41  ? -6.142  -25.371 -29.932 1.00 51.94  ? 40  ALA A C   1 
ATOM 276  O O   . ALA A 1 41  ? -5.975  -25.472 -31.151 1.00 56.24  ? 40  ALA A O   1 
ATOM 277  C CB  . ALA A 1 41  ? -4.544  -23.473 -29.684 1.00 48.03  ? 40  ALA A CB  1 
ATOM 278  N N   . ALA A 1 42  ? -6.525  -26.400 -29.175 1.00 55.81  ? 41  ALA A N   1 
ATOM 279  C CA  . ALA A 1 42  ? -6.742  -27.714 -29.772 1.00 51.92  ? 41  ALA A CA  1 
ATOM 280  C C   . ALA A 1 42  ? -7.920  -27.692 -30.738 1.00 54.56  ? 41  ALA A C   1 
ATOM 281  O O   . ALA A 1 42  ? -7.805  -28.146 -31.883 1.00 59.62  ? 41  ALA A O   1 
ATOM 282  C CB  . ALA A 1 42  ? -6.956  -28.759 -28.677 1.00 52.92  ? 41  ALA A CB  1 
ATOM 283  N N   . ASN A 1 43  ? -9.063  -27.163 -30.296 1.00 46.61  ? 42  ASN A N   1 
ATOM 284  C CA  . ASN A 1 43  ? -10.231 -27.100 -31.169 1.00 48.89  ? 42  ASN A CA  1 
ATOM 285  C C   . ASN A 1 43  ? -10.044 -26.090 -32.291 1.00 53.94  ? 42  ASN A C   1 
ATOM 286  O O   . ASN A 1 43  ? -10.596 -26.267 -33.382 1.00 51.56  ? 42  ASN A O   1 
ATOM 287  C CB  . ASN A 1 43  ? -11.477 -26.758 -30.357 1.00 48.65  ? 42  ASN A CB  1 
ATOM 288  C CG  . ASN A 1 43  ? -11.799 -27.809 -29.325 1.00 46.77  ? 42  ASN A CG  1 
ATOM 289  O OD1 . ASN A 1 43  ? -11.173 -28.867 -29.289 1.00 51.05  ? 42  ASN A OD1 1 
ATOM 290  N ND2 . ASN A 1 43  ? -12.788 -27.532 -28.484 1.00 43.64  ? 42  ASN A ND2 1 
ATOM 291  N N   . PHE A 1 44  ? -9.279  -25.028 -32.042 1.00 55.01  ? 43  PHE A N   1 
ATOM 292  C CA  . PHE A 1 44  ? -9.044  -24.034 -33.080 1.00 47.06  ? 43  PHE A CA  1 
ATOM 293  C C   . PHE A 1 44  ? -8.165  -24.598 -34.190 1.00 48.59  ? 43  PHE A C   1 
ATOM 294  O O   . PHE A 1 44  ? -8.476  -24.439 -35.376 1.00 49.26  ? 43  PHE A O   1 
ATOM 295  C CB  . PHE A 1 44  ? -8.414  -22.787 -32.462 1.00 41.26  ? 43  PHE A CB  1 
ATOM 296  C CG  . PHE A 1 44  ? -8.093  -21.713 -33.452 1.00 40.42  ? 43  PHE A CG  1 
ATOM 297  C CD1 . PHE A 1 44  ? -9.088  -20.879 -33.935 1.00 38.61  ? 43  PHE A CD1 1 
ATOM 298  C CD2 . PHE A 1 44  ? -6.795  -21.527 -33.893 1.00 41.39  ? 43  PHE A CD2 1 
ATOM 299  C CE1 . PHE A 1 44  ? -8.794  -19.883 -34.843 1.00 41.66  ? 43  PHE A CE1 1 
ATOM 300  C CE2 . PHE A 1 44  ? -6.494  -20.533 -34.800 1.00 42.62  ? 43  PHE A CE2 1 
ATOM 301  C CZ  . PHE A 1 44  ? -7.494  -19.709 -35.276 1.00 42.85  ? 43  PHE A CZ  1 
ATOM 302  N N   . ARG A 1 45  ? -7.072  -25.272 -33.825 1.00 49.49  ? 44  ARG A N   1 
ATOM 303  C CA  . ARG A 1 45  ? -6.182  -25.837 -34.834 1.00 51.45  ? 44  ARG A CA  1 
ATOM 304  C C   . ARG A 1 45  ? -6.873  -26.921 -35.652 1.00 53.09  ? 44  ARG A C   1 
ATOM 305  O O   . ARG A 1 45  ? -6.601  -27.059 -36.850 1.00 52.13  ? 44  ARG A O   1 
ATOM 306  C CB  . ARG A 1 45  ? -4.916  -26.383 -34.174 1.00 46.38  ? 44  ARG A CB  1 
ATOM 307  C CG  . ARG A 1 45  ? -4.007  -25.300 -33.614 1.00 49.65  ? 44  ARG A CG  1 
ATOM 308  C CD  . ARG A 1 45  ? -2.880  -25.888 -32.783 1.00 53.13  ? 44  ARG A CD  1 
ATOM 309  N NE  . ARG A 1 45  ? -1.786  -26.367 -33.620 1.00 60.38  ? 44  ARG A NE  1 
ATOM 310  C CZ  . ARG A 1 45  ? -0.719  -27.009 -33.164 1.00 58.23  ? 44  ARG A CZ  1 
ATOM 311  N NH1 . ARG A 1 45  ? -0.565  -27.263 -31.875 1.00 51.53  ? 44  ARG A NH1 1 
ATOM 312  N NH2 . ARG A 1 45  ? 0.214   -27.409 -34.023 1.00 65.93  ? 44  ARG A NH2 1 
ATOM 313  N N   . GLN A 1 46  ? -7.768  -27.693 -35.031 1.00 57.26  ? 45  GLN A N   1 
ATOM 314  C CA  . GLN A 1 46  ? -8.551  -28.659 -35.792 1.00 55.93  ? 45  GLN A CA  1 
ATOM 315  C C   . GLN A 1 46  ? -9.498  -27.964 -36.760 1.00 51.27  ? 45  GLN A C   1 
ATOM 316  O O   . GLN A 1 46  ? -9.780  -28.497 -37.839 1.00 51.31  ? 45  GLN A O   1 
ATOM 317  C CB  . GLN A 1 46  ? -9.331  -29.571 -34.844 1.00 61.92  ? 45  GLN A CB  1 
ATOM 318  C CG  . GLN A 1 46  ? -9.641  -30.948 -35.412 1.00 61.18  ? 45  GLN A CG  1 
ATOM 319  C CD  . GLN A 1 46  ? -8.527  -31.488 -36.291 1.00 71.85  ? 45  GLN A CD  1 
ATOM 320  O OE1 . GLN A 1 46  ? -8.601  -31.421 -37.519 1.00 63.25  ? 45  GLN A OE1 1 
ATOM 321  N NE2 . GLN A 1 46  ? -7.485  -32.024 -35.664 1.00 83.06  ? 45  GLN A NE2 1 
ATOM 322  N N   . LEU A 1 47  ? -9.998  -26.781 -36.393 1.00 49.64  ? 46  LEU A N   1 
ATOM 323  C CA  . LEU A 1 47  ? -10.835 -26.017 -37.311 1.00 47.93  ? 46  LEU A CA  1 
ATOM 324  C C   . LEU A 1 47  ? -10.037 -25.557 -38.523 1.00 46.86  ? 46  LEU A C   1 
ATOM 325  O O   . LEU A 1 47  ? -10.552 -25.546 -39.646 1.00 51.08  ? 46  LEU A O   1 
ATOM 326  C CB  . LEU A 1 47  ? -11.451 -24.820 -36.590 1.00 46.40  ? 46  LEU A CB  1 
ATOM 327  C CG  . LEU A 1 47  ? -12.035 -23.729 -37.490 1.00 45.15  ? 46  LEU A CG  1 
ATOM 328  C CD1 . LEU A 1 47  ? -13.462 -24.071 -37.901 1.00 44.25  ? 46  LEU A CD1 1 
ATOM 329  C CD2 . LEU A 1 47  ? -11.972 -22.373 -36.808 1.00 43.61  ? 46  LEU A CD2 1 
ATOM 330  N N   . ILE A 1 48  ? -8.776  -25.178 -38.315 1.00 45.58  ? 47  ILE A N   1 
ATOM 331  C CA  . ILE A 1 48  ? -7.928  -24.796 -39.437 1.00 44.51  ? 47  ILE A CA  1 
ATOM 332  C C   . ILE A 1 48  ? -7.668  -25.998 -40.338 1.00 49.20  ? 47  ILE A C   1 
ATOM 333  O O   . ILE A 1 48  ? -7.634  -25.873 -41.568 1.00 50.80  ? 47  ILE A O   1 
ATOM 334  C CB  . ILE A 1 48  ? -6.623  -24.165 -38.920 1.00 45.82  ? 47  ILE A CB  1 
ATOM 335  C CG1 . ILE A 1 48  ? -6.941  -22.938 -38.065 1.00 48.96  ? 47  ILE A CG1 1 
ATOM 336  C CG2 . ILE A 1 48  ? -5.715  -23.778 -40.074 1.00 45.81  ? 47  ILE A CG2 1 
ATOM 337  C CD1 . ILE A 1 48  ? -7.969  -22.009 -38.691 1.00 48.77  ? 47  ILE A CD1 1 
ATOM 338  N N   . THR A 1 49  ? -7.511  -27.183 -39.744 1.00 48.95  ? 48  THR A N   1 
ATOM 339  C CA  . THR A 1 49  ? -7.287  -28.387 -40.539 1.00 46.26  ? 48  THR A CA  1 
ATOM 340  C C   . THR A 1 49  ? -8.510  -28.726 -41.383 1.00 49.35  ? 48  THR A C   1 
ATOM 341  O O   . THR A 1 49  ? -8.388  -29.030 -42.575 1.00 54.02  ? 48  THR A O   1 
ATOM 342  C CB  . THR A 1 49  ? -6.920  -29.560 -39.629 1.00 51.43  ? 48  THR A CB  1 
ATOM 343  O OG1 . THR A 1 49  ? -5.661  -29.300 -38.998 1.00 57.15  ? 48  THR A OG1 1 
ATOM 344  C CG2 . THR A 1 49  ? -6.814  -30.848 -40.436 1.00 49.61  ? 48  THR A CG2 1 
ATOM 345  N N   . VAL A 1 50  ? -9.704  -28.682 -40.784 1.00 48.81  ? 49  VAL A N   1 
ATOM 346  C CA  . VAL A 1 50  ? -10.905 -28.975 -41.556 1.00 49.00  ? 49  VAL A CA  1 
ATOM 347  C C   . VAL A 1 50  ? -11.228 -27.849 -42.526 1.00 54.02  ? 49  VAL A C   1 
ATOM 348  O O   . VAL A 1 50  ? -11.915 -28.079 -43.527 1.00 56.42  ? 49  VAL A O   1 
ATOM 349  C CB  . VAL A 1 50  ? -12.107 -29.262 -40.636 1.00 45.47  ? 49  VAL A CB  1 
ATOM 350  C CG1 . VAL A 1 50  ? -11.752 -30.333 -39.614 1.00 49.74  ? 49  VAL A CG1 1 
ATOM 351  C CG2 . VAL A 1 50  ? -12.580 -27.995 -39.951 1.00 45.81  ? 49  VAL A CG2 1 
ATOM 352  N N   . LEU A 1 51  ? -10.742 -26.633 -42.263 1.00 52.23  ? 50  LEU A N   1 
ATOM 353  C CA  . LEU A 1 51  ? -10.930 -25.549 -43.219 1.00 50.59  ? 50  LEU A CA  1 
ATOM 354  C C   . LEU A 1 51  ? -10.080 -25.750 -44.466 1.00 55.12  ? 50  LEU A C   1 
ATOM 355  O O   . LEU A 1 51  ? -10.434 -25.256 -45.541 1.00 55.02  ? 50  LEU A O   1 
ATOM 356  C CB  . LEU A 1 51  ? -10.611 -24.205 -42.566 1.00 46.75  ? 50  LEU A CB  1 
ATOM 357  C CG  . LEU A 1 51  ? -11.782 -23.557 -41.827 1.00 51.90  ? 50  LEU A CG  1 
ATOM 358  C CD1 . LEU A 1 51  ? -11.304 -22.421 -40.933 1.00 52.62  ? 50  LEU A CD1 1 
ATOM 359  C CD2 . LEU A 1 51  ? -12.817 -23.062 -42.822 1.00 56.49  ? 50  LEU A CD2 1 
ATOM 360  N N   . GLY A 1 52  ? -8.967  -26.474 -44.351 1.00 51.06  ? 51  GLY A N   1 
ATOM 361  C CA  . GLY A 1 52  ? -8.162  -26.774 -45.523 1.00 53.07  ? 51  GLY A CA  1 
ATOM 362  C C   . GLY A 1 52  ? -8.818  -27.722 -46.505 1.00 55.78  ? 51  GLY A C   1 
ATOM 363  O O   . GLY A 1 52  ? -8.280  -27.923 -47.599 1.00 53.22  ? 51  GLY A O   1 
ATOM 364  N N   . VAL A 1 53  ? -9.962  -28.299 -46.142 1.00 61.21  ? 52  VAL A N   1 
ATOM 365  C CA  . VAL A 1 53  ? -10.661 -29.269 -46.975 1.00 54.26  ? 52  VAL A CA  1 
ATOM 366  C C   . VAL A 1 53  ? -12.073 -28.767 -47.249 1.00 53.35  ? 52  VAL A C   1 
ATOM 367  O O   . VAL A 1 53  ? -12.655 -29.058 -48.299 1.00 63.12  ? 52  VAL A O   1 
ATOM 368  C CB  . VAL A 1 53  ? -10.687 -30.655 -46.300 1.00 52.12  ? 52  VAL A CB  1 
ATOM 369  C CG1 . VAL A 1 53  ? -11.415 -31.674 -47.167 1.00 55.31  ? 52  VAL A CG1 1 
ATOM 370  C CG2 . VAL A 1 53  ? -9.270  -31.123 -45.994 1.00 45.50  ? 52  VAL A CG2 1 
ATOM 371  N N   . LEU A 1 54  ? -12.628 -27.997 -46.316 1.00 59.02  ? 53  LEU A N   1 
ATOM 372  C CA  . LEU A 1 54  ? -14.030 -27.608 -46.372 1.00 60.63  ? 53  LEU A CA  1 
ATOM 373  C C   . LEU A 1 54  ? -14.247 -26.141 -46.723 1.00 63.72  ? 53  LEU A C   1 
ATOM 374  O O   . LEU A 1 54  ? -15.401 -25.711 -46.817 1.00 69.24  ? 53  LEU A O   1 
ATOM 375  C CB  . LEU A 1 54  ? -14.716 -27.926 -45.034 1.00 65.06  ? 53  LEU A CB  1 
ATOM 376  C CG  . LEU A 1 54  ? -15.461 -29.261 -44.890 1.00 68.20  ? 53  LEU A CG  1 
ATOM 377  C CD1 . LEU A 1 54  ? -14.646 -30.429 -45.436 1.00 62.47  ? 53  LEU A CD1 1 
ATOM 378  C CD2 . LEU A 1 54  ? -15.845 -29.513 -43.437 1.00 58.83  ? 53  LEU A CD2 1 
ATOM 379  N N   . ALA A 1 55  ? -13.182 -25.358 -46.922 1.00 66.70  ? 54  ALA A N   1 
ATOM 380  C CA  . ALA A 1 55  ? -13.372 -23.947 -47.251 1.00 69.95  ? 54  ALA A CA  1 
ATOM 381  C C   . ALA A 1 55  ? -13.904 -23.774 -48.669 1.00 73.67  ? 54  ALA A C   1 
ATOM 382  O O   . ALA A 1 55  ? -14.782 -22.937 -48.911 1.00 72.97  ? 54  ALA A O   1 
ATOM 383  C CB  . ALA A 1 55  ? -12.066 -23.175 -47.073 1.00 60.71  ? 54  ALA A CB  1 
ATOM 384  N N   . GLY A 1 56  ? -13.386 -24.550 -49.618 1.00 73.35  ? 55  GLY A N   1 
ATOM 385  C CA  . GLY A 1 56  ? -13.853 -24.477 -50.987 1.00 70.41  ? 55  GLY A CA  1 
ATOM 386  C C   . GLY A 1 56  ? -14.796 -25.607 -51.343 1.00 71.29  ? 55  GLY A C   1 
ATOM 387  O O   . GLY A 1 56  ? -14.795 -26.092 -52.479 1.00 81.95  ? 55  GLY A O   1 
ATOM 388  N N   . ALA A 1 57  ? -15.595 -26.040 -50.366 1.00 57.79  ? 56  ALA A N   1 
ATOM 389  C CA  . ALA A 1 57  ? -16.582 -27.109 -50.523 1.00 55.10  ? 56  ALA A CA  1 
ATOM 390  C C   . ALA A 1 57  ? -15.952 -28.441 -50.922 1.00 56.22  ? 56  ALA A C   1 
ATOM 391  O O   . ALA A 1 57  ? -16.651 -29.340 -51.401 1.00 55.62  ? 56  ALA A O   1 
ATOM 392  C CB  . ALA A 1 57  ? -17.673 -26.720 -51.526 1.00 53.64  ? 56  ALA A CB  1 
ATOM 393  N N   . GLY A 1 58  ? -14.642 -28.591 -50.732 1.00 54.38  ? 57  GLY A N   1 
ATOM 394  C CA  . GLY A 1 58  ? -13.981 -29.855 -51.007 1.00 54.39  ? 57  GLY A CA  1 
ATOM 395  C C   . GLY A 1 58  ? -13.982 -30.286 -52.456 1.00 51.85  ? 57  GLY A C   1 
ATOM 396  O O   . GLY A 1 58  ? -13.864 -31.484 -52.738 1.00 48.71  ? 57  GLY A O   1 
ATOM 397  N N   . ILE A 1 59  ? -14.108 -29.339 -53.392 1.00 48.92  ? 58  ILE A N   1 
ATOM 398  C CA  . ILE A 1 59  ? -14.141 -29.670 -54.811 1.00 48.43  ? 58  ILE A CA  1 
ATOM 399  C C   . ILE A 1 59  ? -12.751 -29.794 -55.417 1.00 49.83  ? 58  ILE A C   1 
ATOM 400  O O   . ILE A 1 59  ? -12.633 -30.033 -56.626 1.00 52.86  ? 58  ILE A O   1 
ATOM 401  C CB  . ILE A 1 59  ? -14.951 -28.619 -55.596 1.00 45.08  ? 58  ILE A CB  1 
ATOM 402  C CG1 . ILE A 1 59  ? -14.220 -27.274 -55.593 1.00 41.12  ? 58  ILE A CG1 1 
ATOM 403  C CG2 . ILE A 1 59  ? -16.338 -28.466 -55.003 1.00 43.60  ? 58  ILE A CG2 1 
ATOM 404  C CD1 . ILE A 1 59  ? -14.860 -26.228 -56.481 1.00 43.57  ? 58  ILE A CD1 1 
ATOM 405  N N   . PHE A 1 60  ? -11.694 -29.656 -54.611 1.00 49.56  ? 59  PHE A N   1 
ATOM 406  C CA  . PHE A 1 60  ? -10.340 -29.585 -55.156 1.00 46.48  ? 59  PHE A CA  1 
ATOM 407  C C   . PHE A 1 60  ? -9.946  -30.877 -55.860 1.00 42.16  ? 59  PHE A C   1 
ATOM 408  O O   . PHE A 1 60  ? -9.292  -30.841 -56.909 1.00 44.69  ? 59  PHE A O   1 
ATOM 409  C CB  . PHE A 1 60  ? -9.357  -29.249 -54.038 1.00 44.58  ? 59  PHE A CB  1 
ATOM 410  C CG  . PHE A 1 60  ? -9.859  -28.191 -53.099 1.00 54.56  ? 59  PHE A CG  1 
ATOM 411  C CD1 . PHE A 1 60  ? -10.089 -26.899 -53.549 1.00 52.77  ? 59  PHE A CD1 1 
ATOM 412  C CD2 . PHE A 1 60  ? -10.128 -28.491 -51.773 1.00 55.38  ? 59  PHE A CD2 1 
ATOM 413  C CE1 . PHE A 1 60  ? -10.558 -25.924 -52.690 1.00 48.19  ? 59  PHE A CE1 1 
ATOM 414  C CE2 . PHE A 1 60  ? -10.599 -27.520 -50.911 1.00 56.72  ? 59  PHE A CE2 1 
ATOM 415  C CZ  . PHE A 1 60  ? -10.814 -26.235 -51.370 1.00 56.77  ? 59  PHE A CZ  1 
ATOM 416  N N   . ASN A 1 61  ? -10.334 -32.028 -55.308 1.00 41.09  ? 60  ASN A N   1 
ATOM 417  C CA  . ASN A 1 61  ? -10.046 -33.287 -55.984 1.00 42.49  ? 60  ASN A CA  1 
ATOM 418  C C   . ASN A 1 61  ? -10.851 -33.426 -57.269 1.00 46.03  ? 60  ASN A C   1 
ATOM 419  O O   . ASN A 1 61  ? -10.387 -34.060 -58.224 1.00 47.74  ? 60  ASN A O   1 
ATOM 420  C CB  . ASN A 1 61  ? -10.316 -34.465 -55.050 1.00 40.90  ? 60  ASN A CB  1 
ATOM 421  C CG  . ASN A 1 61  ? -9.090  -34.865 -54.259 1.00 39.93  ? 60  ASN A CG  1 
ATOM 422  O OD1 . ASN A 1 61  ? -7.980  -34.414 -54.547 1.00 37.27  ? 60  ASN A OD1 1 
ATOM 423  N ND2 . ASN A 1 61  ? -9.280  -35.718 -53.260 1.00 40.56  ? 60  ASN A ND2 1 
ATOM 424  N N   . GLY A 1 62  ? -12.051 -32.844 -57.314 1.00 44.73  ? 61  GLY A N   1 
ATOM 425  C CA  . GLY A 1 62  ? -12.790 -32.786 -58.561 1.00 43.37  ? 61  GLY A CA  1 
ATOM 426  C C   . GLY A 1 62  ? -12.243 -31.759 -59.525 1.00 44.92  ? 61  GLY A C   1 
ATOM 427  O O   . GLY A 1 62  ? -12.322 -31.945 -60.744 1.00 43.61  ? 61  GLY A O   1 
ATOM 428  N N   . VAL A 1 63  ? -11.688 -30.663 -59.003 1.00 43.40  ? 62  VAL A N   1 
ATOM 429  C CA  . VAL A 1 63  ? -11.035 -29.680 -59.863 1.00 43.00  ? 62  VAL A CA  1 
ATOM 430  C C   . VAL A 1 63  ? -9.845  -30.314 -60.570 1.00 41.67  ? 62  VAL A C   1 
ATOM 431  O O   . VAL A 1 63  ? -9.683  -30.187 -61.788 1.00 48.17  ? 62  VAL A O   1 
ATOM 432  C CB  . VAL A 1 63  ? -10.620 -28.442 -59.046 1.00 39.80  ? 62  VAL A CB  1 
ATOM 433  C CG1 . VAL A 1 63  ? -9.642  -27.581 -59.834 1.00 41.00  ? 62  VAL A CG1 1 
ATOM 434  C CG2 . VAL A 1 63  ? -11.844 -27.634 -58.653 1.00 37.43  ? 62  VAL A CG2 1 
ATOM 435  N N   . THR A 1 64  ? -9.005  -31.026 -59.815 1.00 39.03  ? 63  THR A N   1 
ATOM 436  C CA  . THR A 1 64  ? -7.852  -31.691 -60.413 1.00 40.71  ? 63  THR A CA  1 
ATOM 437  C C   . THR A 1 64  ? -8.285  -32.757 -61.414 1.00 45.20  ? 63  THR A C   1 
ATOM 438  O O   . THR A 1 64  ? -7.667  -32.911 -62.475 1.00 48.75  ? 63  THR A O   1 
ATOM 439  C CB  . THR A 1 64  ? -6.974  -32.299 -59.317 1.00 39.60  ? 63  THR A CB  1 
ATOM 440  O OG1 . THR A 1 64  ? -6.414  -31.250 -58.517 1.00 40.64  ? 63  THR A OG1 1 
ATOM 441  C CG2 . THR A 1 64  ? -5.845  -33.125 -59.917 1.00 39.68  ? 63  THR A CG2 1 
ATOM 442  N N   . LYS A 1 65  ? -9.360  -33.488 -61.108 1.00 42.72  ? 64  LYS A N   1 
ATOM 443  C CA  . LYS A 1 65  ? -9.798  -34.559 -62.000 1.00 46.99  ? 64  LYS A CA  1 
ATOM 444  C C   . LYS A 1 65  ? -10.313 -34.010 -63.326 1.00 45.79  ? 64  LYS A C   1 
ATOM 445  O O   . LYS A 1 65  ? -10.001 -34.556 -64.391 1.00 46.84  ? 64  LYS A O   1 
ATOM 446  C CB  . LYS A 1 65  ? -10.873 -35.408 -61.320 1.00 44.64  ? 64  LYS A CB  1 
ATOM 447  C CG  . LYS A 1 65  ? -11.407 -36.538 -62.194 1.00 44.35  ? 64  LYS A CG  1 
ATOM 448  C CD  . LYS A 1 65  ? -12.899 -36.387 -62.444 1.00 43.14  ? 64  LYS A CD  1 
ATOM 449  C CE  . LYS A 1 65  ? -13.457 -37.545 -63.260 1.00 42.42  ? 64  LYS A CE  1 
ATOM 450  N NZ  . LYS A 1 65  ? -12.662 -37.816 -64.493 1.00 45.58  ? 64  LYS A NZ  1 
ATOM 451  N N   . TYR A 1 66  ? -11.099 -32.933 -63.287 1.00 46.70  ? 65  TYR A N   1 
ATOM 452  C CA  . TYR A 1 66  ? -11.717 -32.410 -64.500 1.00 44.95  ? 65  TYR A CA  1 
ATOM 453  C C   . TYR A 1 66  ? -10.825 -31.442 -65.265 1.00 42.17  ? 65  TYR A C   1 
ATOM 454  O O   . TYR A 1 66  ? -10.977 -31.321 -66.486 1.00 42.74  ? 65  TYR A O   1 
ATOM 455  C CB  . TYR A 1 66  ? -13.053 -31.743 -64.159 1.00 41.88  ? 65  TYR A CB  1 
ATOM 456  C CG  . TYR A 1 66  ? -14.121 -32.752 -63.798 1.00 43.19  ? 65  TYR A CG  1 
ATOM 457  C CD1 . TYR A 1 66  ? -14.496 -33.739 -64.700 1.00 46.21  ? 65  TYR A CD1 1 
ATOM 458  C CD2 . TYR A 1 66  ? -14.736 -32.735 -62.553 1.00 43.63  ? 65  TYR A CD2 1 
ATOM 459  C CE1 . TYR A 1 66  ? -15.462 -34.673 -64.380 1.00 46.62  ? 65  TYR A CE1 1 
ATOM 460  C CE2 . TYR A 1 66  ? -15.703 -33.669 -62.222 1.00 49.92  ? 65  TYR A CE2 1 
ATOM 461  C CZ  . TYR A 1 66  ? -16.062 -34.634 -63.141 1.00 48.56  ? 65  TYR A CZ  1 
ATOM 462  O OH  . TYR A 1 66  ? -17.020 -35.566 -62.818 1.00 48.15  ? 65  TYR A OH  1 
ATOM 463  N N   . VAL A 1 67  ? -9.899  -30.759 -64.590 1.00 44.57  ? 66  VAL A N   1 
ATOM 464  C CA  . VAL A 1 67  ? -8.908  -29.962 -65.306 1.00 42.06  ? 66  VAL A CA  1 
ATOM 465  C C   . VAL A 1 67  ? -7.999  -30.867 -66.129 1.00 46.04  ? 66  VAL A C   1 
ATOM 466  O O   . VAL A 1 67  ? -7.659  -30.555 -67.276 1.00 52.74  ? 66  VAL A O   1 
ATOM 467  C CB  . VAL A 1 67  ? -8.106  -29.092 -64.321 1.00 37.70  ? 66  VAL A CB  1 
ATOM 468  C CG1 . VAL A 1 67  ? -6.756  -28.714 -64.910 1.00 42.84  ? 66  VAL A CG1 1 
ATOM 469  C CG2 . VAL A 1 67  ? -8.897  -27.852 -63.941 1.00 39.67  ? 66  VAL A CG2 1 
ATOM 470  N N   . ALA A 1 68  ? -7.602  -32.009 -65.560 1.00 44.72  ? 67  ALA A N   1 
ATOM 471  C CA  . ALA A 1 68  ? -6.795  -32.970 -66.305 1.00 46.90  ? 67  ALA A CA  1 
ATOM 472  C C   . ALA A 1 68  ? -7.586  -33.583 -67.452 1.00 49.53  ? 67  ALA A C   1 
ATOM 473  O O   . ALA A 1 68  ? -7.050  -33.782 -68.548 1.00 49.20  ? 67  ALA A O   1 
ATOM 474  C CB  . ALA A 1 68  ? -6.286  -34.063 -65.367 1.00 47.34  ? 67  ALA A CB  1 
ATOM 475  N N   . GLN A 1 69  ? -8.864  -33.888 -67.213 1.00 47.32  ? 68  GLN A N   1 
ATOM 476  C CA  . GLN A 1 69  ? -9.704  -34.464 -68.257 1.00 44.17  ? 68  GLN A CA  1 
ATOM 477  C C   . GLN A 1 69  ? -9.853  -33.509 -69.434 1.00 49.86  ? 68  GLN A C   1 
ATOM 478  O O   . GLN A 1 69  ? -9.755  -33.921 -70.596 1.00 54.29  ? 68  GLN A O   1 
ATOM 479  C CB  . GLN A 1 69  ? -11.071 -34.821 -67.677 1.00 44.98  ? 68  GLN A CB  1 
ATOM 480  C CG  . GLN A 1 69  ? -11.839 -35.872 -68.452 1.00 41.82  ? 68  GLN A CG  1 
ATOM 481  C CD  . GLN A 1 69  ? -13.185 -36.177 -67.824 1.00 45.79  ? 68  GLN A CD  1 
ATOM 482  O OE1 . GLN A 1 69  ? -13.420 -37.283 -67.338 1.00 53.95  ? 68  GLN A OE1 1 
ATOM 483  N NE2 . GLN A 1 69  ? -14.076 -35.193 -67.828 1.00 45.24  ? 68  GLN A NE2 1 
ATOM 484  N N   . TYR A 1 70  ? -10.086 -32.228 -69.154 1.00 46.99  ? 69  TYR A N   1 
ATOM 485  C CA  . TYR A 1 70  ? -10.233 -31.202 -70.183 1.00 47.66  ? 69  TYR A CA  1 
ATOM 486  C C   . TYR A 1 70  ? -8.975  -30.355 -70.327 1.00 54.13  ? 69  TYR A C   1 
ATOM 487  O O   . TYR A 1 70  ? -9.054  -29.151 -70.587 1.00 54.56  ? 69  TYR A O   1 
ATOM 488  C CB  . TYR A 1 70  ? -11.442 -30.323 -69.879 1.00 45.18  ? 69  TYR A CB  1 
ATOM 489  C CG  . TYR A 1 70  ? -12.754 -31.075 -69.868 1.00 44.94  ? 69  TYR A CG  1 
ATOM 490  C CD1 . TYR A 1 70  ? -13.136 -31.862 -70.947 1.00 47.02  ? 69  TYR A CD1 1 
ATOM 491  C CD2 . TYR A 1 70  ? -13.609 -31.001 -68.777 1.00 45.19  ? 69  TYR A CD2 1 
ATOM 492  C CE1 . TYR A 1 70  ? -14.334 -32.551 -70.940 1.00 45.34  ? 69  TYR A CE1 1 
ATOM 493  C CE2 . TYR A 1 70  ? -14.807 -31.687 -68.761 1.00 45.79  ? 69  TYR A CE2 1 
ATOM 494  C CZ  . TYR A 1 70  ? -15.165 -32.459 -69.844 1.00 47.75  ? 69  TYR A CZ  1 
ATOM 495  O OH  . TYR A 1 70  ? -16.358 -33.141 -69.828 1.00 57.30  ? 69  TYR A OH  1 
ATOM 496  N N   . HIS A 1 71  ? -7.797  -30.964 -70.160 1.00 58.08  ? 70  HIS A N   1 
ATOM 497  C CA  . HIS A 1 71  ? -6.543  -30.240 -70.332 1.00 58.16  ? 70  HIS A CA  1 
ATOM 498  C C   . HIS A 1 71  ? -6.332  -29.781 -71.767 1.00 67.11  ? 70  HIS A C   1 
ATOM 499  O O   . HIS A 1 71  ? -5.596  -28.815 -71.994 1.00 68.98  ? 70  HIS A O   1 
ATOM 500  C CB  . HIS A 1 71  ? -5.362  -31.112 -69.895 1.00 55.58  ? 70  HIS A CB  1 
ATOM 501  C CG  . HIS A 1 71  ? -4.952  -32.129 -70.916 1.00 63.58  ? 70  HIS A CG  1 
ATOM 502  N ND1 . HIS A 1 71  ? -5.619  -33.323 -71.090 1.00 65.04  ? 70  HIS A ND1 1 
ATOM 503  C CD2 . HIS A 1 71  ? -3.944  -32.128 -71.821 1.00 69.21  ? 70  HIS A CD2 1 
ATOM 504  C CE1 . HIS A 1 71  ? -5.040  -34.014 -72.055 1.00 69.46  ? 70  HIS A CE1 1 
ATOM 505  N NE2 . HIS A 1 71  ? -4.020  -33.312 -72.515 1.00 73.39  ? 70  HIS A NE2 1 
ATOM 506  N N   . ASP A 1 72  ? -6.953  -30.452 -72.738 1.00 76.76  ? 71  ASP A N   1 
ATOM 507  C CA  . ASP A 1 72  ? -6.807  -30.097 -74.143 1.00 73.65  ? 71  ASP A CA  1 
ATOM 508  C C   . ASP A 1 72  ? -7.909  -29.151 -74.611 1.00 72.10  ? 71  ASP A C   1 
ATOM 509  O O   . ASP A 1 72  ? -7.624  -28.132 -75.248 1.00 74.45  ? 71  ASP A O   1 
ATOM 510  C CB  . ASP A 1 72  ? -6.788  -31.365 -75.005 1.00 75.50  ? 71  ASP A CB  1 
ATOM 511  C CG  . ASP A 1 72  ? -7.810  -32.395 -74.555 1.00 79.88  ? 71  ASP A CG  1 
ATOM 512  O OD1 . ASP A 1 72  ? -8.529  -32.136 -73.567 1.00 75.85  ? 71  ASP A OD1 1 
ATOM 513  O OD2 . ASP A 1 72  ? -7.895  -33.466 -75.192 1.00 87.32  ? 71  ASP A OD2 1 
ATOM 514  N N   . ASN A 1 73  ? -9.158  -29.468 -74.303 1.00 60.05  ? 72  ASN A N   1 
ATOM 515  C CA  . ASN A 1 73  ? -10.295 -28.648 -74.709 1.00 57.45  ? 72  ASN A CA  1 
ATOM 516  C C   . ASN A 1 73  ? -10.279 -27.315 -73.973 1.00 58.23  ? 72  ASN A C   1 
ATOM 517  O O   . ASN A 1 73  ? -10.483 -27.297 -72.752 1.00 58.25  ? 72  ASN A O   1 
ATOM 518  C CB  . ASN A 1 73  ? -11.601 -29.389 -74.429 1.00 50.77  ? 72  ASN A CB  1 
ATOM 519  C CG  . ASN A 1 73  ? -12.746 -28.903 -75.296 1.00 57.86  ? 72  ASN A CG  1 
ATOM 520  O OD1 . ASN A 1 73  ? -12.617 -27.914 -76.021 1.00 57.59  ? 72  ASN A OD1 1 
ATOM 521  N ND2 . ASN A 1 73  ? -13.878 -29.596 -75.221 1.00 54.50  ? 72  ASN A ND2 1 
ATOM 522  N N   . PRO A 1 74  ? -10.051 -26.186 -74.653 1.00 59.00  ? 73  PRO A N   1 
ATOM 523  C CA  . PRO A 1 74  ? -10.000 -24.910 -73.922 1.00 54.85  ? 73  PRO A CA  1 
ATOM 524  C C   . PRO A 1 74  ? -11.366 -24.438 -73.466 1.00 52.11  ? 73  PRO A C   1 
ATOM 525  O O   . PRO A 1 74  ? -11.481 -23.842 -72.388 1.00 52.40  ? 73  PRO A O   1 
ATOM 526  C CB  . PRO A 1 74  ? -9.373  -23.941 -74.938 1.00 48.57  ? 73  PRO A CB  1 
ATOM 527  C CG  . PRO A 1 74  ? -8.938  -24.795 -76.113 1.00 54.82  ? 73  PRO A CG  1 
ATOM 528  C CD  . PRO A 1 74  ? -9.819  -25.998 -76.092 1.00 57.98  ? 73  PRO A CD  1 
ATOM 529  N N   . GLN A 1 75  ? -12.411 -24.691 -74.257 1.00 55.17  ? 74  GLN A N   1 
ATOM 530  C CA  . GLN A 1 75  ? -13.744 -24.215 -73.901 1.00 54.32  ? 74  GLN A CA  1 
ATOM 531  C C   . GLN A 1 75  ? -14.256 -24.899 -72.640 1.00 51.16  ? 74  GLN A C   1 
ATOM 532  O O   . GLN A 1 75  ? -14.746 -24.240 -71.716 1.00 48.86  ? 74  GLN A O   1 
ATOM 533  C CB  . GLN A 1 75  ? -14.713 -24.439 -75.058 1.00 48.55  ? 74  GLN A CB  1 
ATOM 534  C CG  . GLN A 1 75  ? -16.139 -24.038 -74.721 1.00 50.15  ? 74  GLN A CG  1 
ATOM 535  C CD  . GLN A 1 75  ? -17.143 -24.550 -75.722 1.00 44.92  ? 74  GLN A CD  1 
ATOM 536  O OE1 . GLN A 1 75  ? -17.279 -25.757 -75.920 1.00 46.10  ? 74  GLN A OE1 1 
ATOM 537  N NE2 . GLN A 1 75  ? -17.856 -23.634 -76.364 1.00 47.58  ? 74  GLN A NE2 1 
ATOM 538  N N   . GLN A 1 76  ? -14.166 -26.230 -72.590 1.00 49.27  ? 75  GLN A N   1 
ATOM 539  C CA  . GLN A 1 76  ? -14.599 -26.938 -71.393 1.00 47.18  ? 75  GLN A CA  1 
ATOM 540  C C   . GLN A 1 76  ? -13.696 -26.629 -70.206 1.00 47.82  ? 75  GLN A C   1 
ATOM 541  O O   . GLN A 1 76  ? -14.149 -26.679 -69.057 1.00 46.88  ? 75  GLN A O   1 
ATOM 542  C CB  . GLN A 1 76  ? -14.653 -28.442 -71.661 1.00 43.63  ? 75  GLN A CB  1 
ATOM 543  C CG  . GLN A 1 76  ? -15.847 -28.876 -72.499 1.00 47.14  ? 75  GLN A CG  1 
ATOM 544  C CD  . GLN A 1 76  ? -17.160 -28.812 -71.734 1.00 49.96  ? 75  GLN A CD  1 
ATOM 545  O OE1 . GLN A 1 76  ? -17.173 -28.668 -70.511 1.00 52.79  ? 75  GLN A OE1 1 
ATOM 546  N NE2 . GLN A 1 76  ? -18.273 -28.923 -72.455 1.00 43.98  ? 75  GLN A NE2 1 
ATOM 547  N N   . LEU A 1 77  ? -12.428 -26.290 -70.462 1.00 50.16  ? 76  LEU A N   1 
ATOM 548  C CA  . LEU A 1 77  ? -11.531 -25.899 -69.379 1.00 45.74  ? 76  LEU A CA  1 
ATOM 549  C C   . LEU A 1 77  ? -11.974 -24.590 -68.736 1.00 48.06  ? 76  LEU A C   1 
ATOM 550  O O   . LEU A 1 77  ? -11.877 -24.431 -67.514 1.00 44.93  ? 76  LEU A O   1 
ATOM 551  C CB  . LEU A 1 77  ? -10.097 -25.782 -69.897 1.00 49.87  ? 76  LEU A CB  1 
ATOM 552  C CG  . LEU A 1 77  ? -9.000  -25.666 -68.838 1.00 50.49  ? 76  LEU A CG  1 
ATOM 553  C CD1 . LEU A 1 77  ? -8.935  -26.930 -68.000 1.00 54.41  ? 76  LEU A CD1 1 
ATOM 554  C CD2 . LEU A 1 77  ? -7.651  -25.373 -69.481 1.00 50.70  ? 76  LEU A CD2 1 
ATOM 555  N N   . ARG A 1 78  ? -12.451 -23.636 -69.542 1.00 55.61  ? 77  ARG A N   1 
ATOM 556  C CA  . ARG A 1 78  ? -13.004 -22.409 -68.976 1.00 54.27  ? 77  ARG A CA  1 
ATOM 557  C C   . ARG A 1 78  ? -14.191 -22.715 -68.075 1.00 52.46  ? 77  ARG A C   1 
ATOM 558  O O   . ARG A 1 78  ? -14.353 -22.100 -67.014 1.00 52.65  ? 77  ARG A O   1 
ATOM 559  C CB  . ARG A 1 78  ? -13.425 -21.446 -70.088 1.00 53.62  ? 77  ARG A CB  1 
ATOM 560  C CG  . ARG A 1 78  ? -12.343 -21.116 -71.098 1.00 53.42  ? 77  ARG A CG  1 
ATOM 561  C CD  . ARG A 1 78  ? -12.899 -20.269 -72.235 1.00 58.80  ? 77  ARG A CD  1 
ATOM 562  N NE  . ARG A 1 78  ? -12.718 -20.903 -73.536 1.00 54.57  ? 77  ARG A NE  1 
ATOM 563  C CZ  . ARG A 1 78  ? -13.473 -20.659 -74.598 1.00 64.09  ? 77  ARG A CZ  1 
ATOM 564  N NH1 . ARG A 1 78  ? -14.476 -19.797 -74.551 1.00 69.46  ? 77  ARG A NH1 1 
ATOM 565  N NH2 . ARG A 1 78  ? -13.214 -21.294 -75.738 1.00 68.80  ? 77  ARG A NH2 1 
ATOM 566  N N   . ARG A 1 79  ? -15.030 -23.672 -68.480 1.00 46.83  ? 78  ARG A N   1 
ATOM 567  C CA  . ARG A 1 79  ? -16.213 -24.003 -67.696 1.00 47.80  ? 78  ARG A CA  1 
ATOM 568  C C   . ARG A 1 79  ? -15.853 -24.764 -66.427 1.00 50.11  ? 78  ARG A C   1 
ATOM 569  O O   . ARG A 1 79  ? -16.574 -24.672 -65.426 1.00 48.34  ? 78  ARG A O   1 
ATOM 570  C CB  . ARG A 1 79  ? -17.194 -24.802 -68.552 1.00 44.84  ? 78  ARG A CB  1 
ATOM 571  C CG  . ARG A 1 79  ? -17.701 -24.033 -69.765 1.00 43.75  ? 78  ARG A CG  1 
ATOM 572  C CD  . ARG A 1 79  ? -18.440 -24.935 -70.737 1.00 48.10  ? 78  ARG A CD  1 
ATOM 573  N NE  . ARG A 1 79  ? -18.896 -24.208 -71.916 1.00 45.10  ? 78  ARG A NE  1 
ATOM 574  C CZ  . ARG A 1 79  ? -19.515 -24.766 -72.947 1.00 45.59  ? 78  ARG A CZ  1 
ATOM 575  N NH1 . ARG A 1 79  ? -19.781 -26.062 -72.974 1.00 46.57  ? 78  ARG A NH1 1 
ATOM 576  N NH2 . ARG A 1 79  ? -19.876 -24.006 -73.977 1.00 46.34  ? 78  ARG A NH2 1 
ATOM 577  N N   . VAL A 1 80  ? -14.750 -25.513 -66.443 1.00 49.14  ? 79  VAL A N   1 
ATOM 578  C CA  . VAL A 1 80  ? -14.293 -26.184 -65.230 1.00 46.32  ? 79  VAL A CA  1 
ATOM 579  C C   . VAL A 1 80  ? -13.774 -25.163 -64.224 1.00 49.06  ? 79  VAL A C   1 
ATOM 580  O O   . VAL A 1 80  ? -14.179 -25.157 -63.056 1.00 50.84  ? 79  VAL A O   1 
ATOM 581  C CB  . VAL A 1 80  ? -13.226 -27.239 -65.569 1.00 41.68  ? 79  VAL A CB  1 
ATOM 582  C CG1 . VAL A 1 80  ? -12.555 -27.741 -64.304 1.00 45.40  ? 79  VAL A CG1 1 
ATOM 583  C CG2 . VAL A 1 80  ? -13.852 -28.394 -66.322 1.00 41.05  ? 79  VAL A CG2 1 
ATOM 584  N N   . VAL A 1 81  ? -12.874 -24.280 -64.663 1.00 47.56  ? 80  VAL A N   1 
ATOM 585  C CA  . VAL A 1 81  ? -12.343 -23.266 -63.759 1.00 45.61  ? 80  VAL A CA  1 
ATOM 586  C C   . VAL A 1 81  ? -13.415 -22.244 -63.403 1.00 45.36  ? 80  VAL A C   1 
ATOM 587  O O   . VAL A 1 81  ? -13.462 -21.752 -62.269 1.00 44.30  ? 80  VAL A O   1 
ATOM 588  C CB  . VAL A 1 81  ? -11.105 -22.594 -64.382 1.00 45.75  ? 80  VAL A CB  1 
ATOM 589  C CG1 . VAL A 1 81  ? -10.403 -21.718 -63.359 1.00 48.57  ? 80  VAL A CG1 1 
ATOM 590  C CG2 . VAL A 1 81  ? -10.152 -23.644 -64.923 1.00 47.55  ? 80  VAL A CG2 1 
ATOM 591  N N   . GLY A 1 82  ? -14.300 -21.921 -64.348 1.00 47.81  ? 81  GLY A N   1 
ATOM 592  C CA  . GLY A 1 82  ? -15.331 -20.933 -64.078 1.00 45.27  ? 81  GLY A CA  1 
ATOM 593  C C   . GLY A 1 82  ? -16.334 -21.393 -63.036 1.00 47.88  ? 81  GLY A C   1 
ATOM 594  O O   . GLY A 1 82  ? -16.717 -20.623 -62.152 1.00 51.65  ? 81  GLY A O   1 
ATOM 595  N N   . THR A 1 83  ? -16.773 -22.651 -63.125 1.00 48.89  ? 82  THR A N   1 
ATOM 596  C CA  . THR A 1 83  ? -17.710 -23.173 -62.133 1.00 48.76  ? 82  THR A CA  1 
ATOM 597  C C   . THR A 1 83  ? -17.023 -23.400 -60.792 1.00 49.43  ? 82  THR A C   1 
ATOM 598  O O   . THR A 1 83  ? -17.619 -23.162 -59.734 1.00 47.15  ? 82  THR A O   1 
ATOM 599  C CB  . THR A 1 83  ? -18.344 -24.471 -62.634 1.00 47.04  ? 82  THR A CB  1 
ATOM 600  O OG1 . THR A 1 83  ? -18.798 -24.296 -63.982 1.00 43.30  ? 82  THR A OG1 1 
ATOM 601  C CG2 . THR A 1 83  ? -19.522 -24.861 -61.754 1.00 45.91  ? 82  THR A CG2 1 
ATOM 602  N N   . SER A 1 84  ? -15.770 -23.861 -60.818 1.00 47.35  ? 83  SER A N   1 
ATOM 603  C CA  . SER A 1 84  ? -15.026 -24.056 -59.578 1.00 46.09  ? 83  SER A CA  1 
ATOM 604  C C   . SER A 1 84  ? -14.764 -22.728 -58.880 1.00 41.97  ? 83  SER A C   1 
ATOM 605  O O   . SER A 1 84  ? -14.807 -22.649 -57.647 1.00 39.34  ? 83  SER A O   1 
ATOM 606  C CB  . SER A 1 84  ? -13.710 -24.777 -59.864 1.00 45.09  ? 83  SER A CB  1 
ATOM 607  O OG  . SER A 1 84  ? -13.922 -25.946 -60.635 1.00 40.79  ? 83  SER A OG  1 
ATOM 608  N N   . SER A 1 85  ? -14.483 -21.677 -59.650 1.00 43.36  ? 84  SER A N   1 
ATOM 609  C CA  . SER A 1 85  ? -14.248 -20.368 -59.053 1.00 43.01  ? 84  SER A CA  1 
ATOM 610  C C   . SER A 1 85  ? -15.513 -19.823 -58.404 1.00 46.54  ? 84  SER A C   1 
ATOM 611  O O   . SER A 1 85  ? -15.449 -19.191 -57.343 1.00 48.90  ? 84  SER A O   1 
ATOM 612  C CB  . SER A 1 85  ? -13.724 -19.400 -60.112 1.00 45.60  ? 84  SER A CB  1 
ATOM 613  O OG  . SER A 1 85  ? -13.801 -18.059 -59.664 1.00 52.08  ? 84  SER A OG  1 
ATOM 614  N N   . ALA A 1 86  ? -16.672 -20.067 -59.021 1.00 46.92  ? 85  ALA A N   1 
ATOM 615  C CA  . ALA A 1 86  ? -17.929 -19.572 -58.467 1.00 45.28  ? 85  ALA A CA  1 
ATOM 616  C C   . ALA A 1 86  ? -18.315 -20.328 -57.203 1.00 46.37  ? 85  ALA A C   1 
ATOM 617  O O   . ALA A 1 86  ? -18.861 -19.738 -56.263 1.00 47.37  ? 85  ALA A O   1 
ATOM 618  C CB  . ALA A 1 86  ? -19.040 -19.673 -59.510 1.00 42.45  ? 85  ALA A CB  1 
ATOM 619  N N   . MET A 1 87  ? -18.048 -21.635 -57.160 1.00 46.70  ? 86  MET A N   1 
ATOM 620  C CA  . MET A 1 87  ? -18.363 -22.405 -55.962 1.00 44.94  ? 86  MET A CA  1 
ATOM 621  C C   . MET A 1 87  ? -17.447 -22.018 -54.808 1.00 42.86  ? 86  MET A C   1 
ATOM 622  O O   . MET A 1 87  ? -17.903 -21.878 -53.667 1.00 41.99  ? 86  MET A O   1 
ATOM 623  C CB  . MET A 1 87  ? -18.260 -23.903 -56.252 1.00 45.04  ? 86  MET A CB  1 
ATOM 624  C CG  . MET A 1 87  ? -19.479 -24.478 -56.955 1.00 45.86  ? 86  MET A CG  1 
ATOM 625  S SD  . MET A 1 87  ? -19.113 -25.920 -57.976 1.00 42.73  ? 86  MET A SD  1 
ATOM 626  C CE  . MET A 1 87  ? -19.300 -27.230 -56.771 1.00 43.23  ? 86  MET A CE  1 
ATOM 627  N N   . VAL A 1 88  ? -16.154 -21.837 -55.086 1.00 44.07  ? 87  VAL A N   1 
ATOM 628  C CA  . VAL A 1 88  ? -15.225 -21.400 -54.048 1.00 44.34  ? 87  VAL A CA  1 
ATOM 629  C C   . VAL A 1 88  ? -15.593 -20.005 -53.561 1.00 46.77  ? 87  VAL A C   1 
ATOM 630  O O   . VAL A 1 88  ? -15.555 -19.722 -52.358 1.00 48.96  ? 87  VAL A O   1 
ATOM 631  C CB  . VAL A 1 88  ? -13.776 -21.457 -54.569 1.00 44.88  ? 87  VAL A CB  1 
ATOM 632  C CG1 . VAL A 1 88  ? -12.833 -20.716 -53.625 1.00 48.03  ? 87  VAL A CG1 1 
ATOM 633  C CG2 . VAL A 1 88  ? -13.331 -22.899 -54.759 1.00 43.16  ? 87  VAL A CG2 1 
ATOM 634  N N   . LEU A 1 89  ? -15.966 -19.114 -54.483 1.00 47.69  ? 88  LEU A N   1 
ATOM 635  C CA  . LEU A 1 89  ? -16.331 -17.754 -54.098 1.00 47.91  ? 88  LEU A CA  1 
ATOM 636  C C   . LEU A 1 89  ? -17.613 -17.741 -53.274 1.00 51.37  ? 88  LEU A C   1 
ATOM 637  O O   . LEU A 1 89  ? -17.688 -17.078 -52.233 1.00 56.40  ? 88  LEU A O   1 
ATOM 638  C CB  . LEU A 1 89  ? -16.481 -16.880 -55.343 1.00 43.46  ? 88  LEU A CB  1 
ATOM 639  C CG  . LEU A 1 89  ? -16.521 -15.366 -55.124 1.00 47.71  ? 88  LEU A CG  1 
ATOM 640  C CD1 . LEU A 1 89  ? -15.114 -14.798 -55.011 1.00 49.09  ? 88  LEU A CD1 1 
ATOM 641  C CD2 . LEU A 1 89  ? -17.290 -14.680 -56.243 1.00 47.20  ? 88  LEU A CD2 1 
ATOM 642  N N   . GLY A 1 90  ? -18.632 -18.475 -53.722 1.00 50.02  ? 89  GLY A N   1 
ATOM 643  C CA  . GLY A 1 90  ? -19.909 -18.450 -53.028 1.00 46.60  ? 89  GLY A CA  1 
ATOM 644  C C   . GLY A 1 90  ? -19.867 -19.146 -51.681 1.00 46.97  ? 89  GLY A C   1 
ATOM 645  O O   . GLY A 1 90  ? -20.476 -18.681 -50.715 1.00 52.56  ? 89  GLY A O   1 
ATOM 646  N N   . PHE A 1 91  ? -19.149 -20.268 -51.595 1.00 48.16  ? 90  PHE A N   1 
ATOM 647  C CA  . PHE A 1 91  ? -19.111 -21.018 -50.343 1.00 48.77  ? 90  PHE A CA  1 
ATOM 648  C C   . PHE A 1 91  ? -18.266 -20.306 -49.293 1.00 52.18  ? 90  PHE A C   1 
ATOM 649  O O   . PHE A 1 91  ? -18.639 -20.262 -48.115 1.00 53.13  ? 90  PHE A O   1 
ATOM 650  C CB  . PHE A 1 91  ? -18.582 -22.430 -50.589 1.00 48.02  ? 90  PHE A CB  1 
ATOM 651  C CG  . PHE A 1 91  ? -18.853 -23.382 -49.461 1.00 49.58  ? 90  PHE A CG  1 
ATOM 652  C CD1 . PHE A 1 91  ? -17.949 -23.516 -48.420 1.00 54.61  ? 90  PHE A CD1 1 
ATOM 653  C CD2 . PHE A 1 91  ? -20.008 -24.144 -49.442 1.00 51.40  ? 90  PHE A CD2 1 
ATOM 654  C CE1 . PHE A 1 91  ? -18.195 -24.388 -47.379 1.00 53.04  ? 90  PHE A CE1 1 
ATOM 655  C CE2 . PHE A 1 91  ? -20.259 -25.021 -48.403 1.00 55.31  ? 90  PHE A CE2 1 
ATOM 656  C CZ  . PHE A 1 91  ? -19.350 -25.143 -47.370 1.00 55.13  ? 90  PHE A CZ  1 
ATOM 657  N N   . SER A 1 92  ? -17.123 -19.748 -49.696 1.00 51.80  ? 91  SER A N   1 
ATOM 658  C CA  . SER A 1 92  ? -16.262 -19.062 -48.739 1.00 53.87  ? 91  SER A CA  1 
ATOM 659  C C   . SER A 1 92  ? -16.878 -17.752 -48.258 1.00 57.59  ? 91  SER A C   1 
ATOM 660  O O   . SER A 1 92  ? -16.677 -17.365 -47.101 1.00 60.82  ? 91  SER A O   1 
ATOM 661  C CB  . SER A 1 92  ? -14.887 -18.820 -49.358 1.00 55.66  ? 91  SER A CB  1 
ATOM 662  O OG  . SER A 1 92  ? -14.966 -17.868 -50.402 1.00 62.40  ? 91  SER A OG  1 
ATOM 663  N N   . THR A 1 93  ? -17.627 -17.058 -49.116 1.00 51.56  ? 92  THR A N   1 
ATOM 664  C CA  . THR A 1 93  ? -18.331 -15.863 -48.659 1.00 53.86  ? 92  THR A CA  1 
ATOM 665  C C   . THR A 1 93  ? -19.465 -16.227 -47.707 1.00 53.56  ? 92  THR A C   1 
ATOM 666  O O   . THR A 1 93  ? -19.739 -15.495 -46.749 1.00 55.17  ? 92  THR A O   1 
ATOM 667  C CB  . THR A 1 93  ? -18.860 -15.069 -49.854 1.00 53.49  ? 92  THR A CB  1 
ATOM 668  O OG1 . THR A 1 93  ? -19.465 -15.962 -50.798 1.00 54.99  ? 92  THR A OG1 1 
ATOM 669  C CG2 . THR A 1 93  ? -17.724 -14.310 -50.529 1.00 50.15  ? 92  THR A CG2 1 
ATOM 670  N N   . LEU A 1 94  ? -20.129 -17.359 -47.952 1.00 53.59  ? 93  LEU A N   1 
ATOM 671  C CA  . LEU A 1 94  ? -21.149 -17.834 -47.023 1.00 52.98  ? 93  LEU A CA  1 
ATOM 672  C C   . LEU A 1 94  ? -20.525 -18.270 -45.705 1.00 51.92  ? 93  LEU A C   1 
ATOM 673  O O   . LEU A 1 94  ? -21.102 -18.050 -44.634 1.00 51.69  ? 93  LEU A O   1 
ATOM 674  C CB  . LEU A 1 94  ? -21.934 -18.985 -47.652 1.00 46.60  ? 93  LEU A CB  1 
ATOM 675  C CG  . LEU A 1 94  ? -23.301 -19.297 -47.045 1.00 51.66  ? 93  LEU A CG  1 
ATOM 676  C CD1 . LEU A 1 94  ? -24.355 -19.400 -48.136 1.00 47.53  ? 93  LEU A CD1 1 
ATOM 677  C CD2 . LEU A 1 94  ? -23.248 -20.577 -46.222 1.00 48.61  ? 93  LEU A CD2 1 
ATOM 678  N N   . MET A 1 95  ? -19.347 -18.893 -45.765 1.00 50.43  ? 94  MET A N   1 
ATOM 679  C CA  . MET A 1 95  ? -18.635 -19.246 -44.544 1.00 50.60  ? 94  MET A CA  1 
ATOM 680  C C   . MET A 1 95  ? -18.178 -18.001 -43.798 1.00 57.51  ? 94  MET A C   1 
ATOM 681  O O   . MET A 1 95  ? -18.239 -17.953 -42.564 1.00 55.44  ? 94  MET A O   1 
ATOM 682  C CB  . MET A 1 95  ? -17.440 -20.141 -44.871 1.00 53.97  ? 94  MET A CB  1 
ATOM 683  C CG  . MET A 1 95  ? -17.743 -21.632 -44.847 1.00 59.52  ? 94  MET A CG  1 
ATOM 684  S SD  . MET A 1 95  ? -18.995 -22.088 -43.628 1.00 85.37  ? 94  MET A SD  1 
ATOM 685  C CE  . MET A 1 95  ? -20.450 -22.291 -44.659 1.00 53.58  ? 94  MET A CE  1 
ATOM 686  N N   . ALA A 1 96  ? -17.720 -16.983 -44.531 1.00 57.55  ? 95  ALA A N   1 
ATOM 687  C CA  . ALA A 1 96  ? -17.286 -15.745 -43.892 1.00 52.62  ? 95  ALA A CA  1 
ATOM 688  C C   . ALA A 1 96  ? -18.443 -15.057 -43.179 1.00 56.34  ? 95  ALA A C   1 
ATOM 689  O O   . ALA A 1 96  ? -18.264 -14.483 -42.098 1.00 59.07  ? 95  ALA A O   1 
ATOM 690  C CB  . ALA A 1 96  ? -16.658 -14.812 -44.927 1.00 48.29  ? 95  ALA A CB  1 
ATOM 691  N N   . LEU A 1 97  ? -19.641 -15.106 -43.768 1.00 55.99  ? 96  LEU A N   1 
ATOM 692  C CA  . LEU A 1 97  ? -20.807 -14.518 -43.118 1.00 55.94  ? 96  LEU A CA  1 
ATOM 693  C C   . LEU A 1 97  ? -21.185 -15.291 -41.862 1.00 58.72  ? 96  LEU A C   1 
ATOM 694  O O   . LEU A 1 97  ? -21.574 -14.695 -40.851 1.00 55.77  ? 96  LEU A O   1 
ATOM 695  C CB  . LEU A 1 97  ? -21.984 -14.474 -44.092 1.00 54.06  ? 96  LEU A CB  1 
ATOM 696  C CG  . LEU A 1 97  ? -22.888 -13.245 -44.004 1.00 60.83  ? 96  LEU A CG  1 
ATOM 697  C CD1 . LEU A 1 97  ? -22.256 -12.062 -44.723 1.00 60.07  ? 96  LEU A CD1 1 
ATOM 698  C CD2 . LEU A 1 97  ? -24.265 -13.552 -44.571 1.00 64.31  ? 96  LEU A CD2 1 
ATOM 699  N N   . VAL A 1 98  ? -21.074 -16.620 -41.909 1.00 56.25  ? 97  VAL A N   1 
ATOM 700  C CA  . VAL A 1 98  ? -21.382 -17.438 -40.741 1.00 56.29  ? 97  VAL A CA  1 
ATOM 701  C C   . VAL A 1 98  ? -20.386 -17.167 -39.619 1.00 59.93  ? 97  VAL A C   1 
ATOM 702  O O   . VAL A 1 98  ? -20.762 -17.083 -38.443 1.00 60.75  ? 97  VAL A O   1 
ATOM 703  C CB  . VAL A 1 98  ? -21.413 -18.926 -41.139 1.00 50.56  ? 97  VAL A CB  1 
ATOM 704  C CG1 . VAL A 1 98  ? -21.195 -19.820 -39.930 1.00 47.59  ? 97  VAL A CG1 1 
ATOM 705  C CG2 . VAL A 1 98  ? -22.730 -19.260 -41.822 1.00 49.90  ? 97  VAL A CG2 1 
ATOM 706  N N   . PHE A 1 99  ? -19.106 -17.006 -39.963 1.00 57.95  ? 98  PHE A N   1 
ATOM 707  C CA  . PHE A 1 99  ? -18.088 -16.800 -38.937 1.00 58.31  ? 98  PHE A CA  1 
ATOM 708  C C   . PHE A 1 99  ? -18.183 -15.407 -38.329 1.00 63.40  ? 98  PHE A C   1 
ATOM 709  O O   . PHE A 1 99  ? -17.946 -15.231 -37.129 1.00 64.58  ? 98  PHE A O   1 
ATOM 710  C CB  . PHE A 1 99  ? -16.696 -17.031 -39.523 1.00 57.06  ? 98  PHE A CB  1 
ATOM 711  C CG  . PHE A 1 99  ? -16.268 -18.470 -39.527 1.00 58.71  ? 98  PHE A CG  1 
ATOM 712  C CD1 . PHE A 1 99  ? -17.022 -19.432 -40.180 1.00 58.85  ? 98  PHE A CD1 1 
ATOM 713  C CD2 . PHE A 1 99  ? -15.111 -18.863 -38.875 1.00 59.64  ? 98  PHE A CD2 1 
ATOM 714  C CE1 . PHE A 1 99  ? -16.629 -20.756 -40.186 1.00 57.93  ? 98  PHE A CE1 1 
ATOM 715  C CE2 . PHE A 1 99  ? -14.714 -20.187 -38.877 1.00 61.38  ? 98  PHE A CE2 1 
ATOM 716  C CZ  . PHE A 1 99  ? -15.473 -21.134 -39.534 1.00 56.77  ? 98  PHE A CZ  1 
ATOM 717  N N   . VAL A 1 100 ? -18.525 -14.406 -39.139 1.00 72.47  ? 99  VAL A N   1 
ATOM 718  C CA  . VAL A 1 100 ? -18.577 -13.041 -38.628 1.00 72.74  ? 99  VAL A CA  1 
ATOM 719  C C   . VAL A 1 100 ? -19.854 -12.794 -37.833 1.00 69.51  ? 99  VAL A C   1 
ATOM 720  O O   . VAL A 1 100 ? -19.866 -11.965 -36.917 1.00 75.99  ? 99  VAL A O   1 
ATOM 721  C CB  . VAL A 1 100 ? -18.425 -12.031 -39.781 1.00 66.55  ? 99  VAL A CB  1 
ATOM 722  C CG1 . VAL A 1 100 ? -19.695 -11.974 -40.623 1.00 66.03  ? 99  VAL A CG1 1 
ATOM 723  C CG2 . VAL A 1 100 ? -18.060 -10.654 -39.243 1.00 62.25  ? 99  VAL A CG2 1 
ATOM 724  N N   . LEU A 1 101 ? -20.943 -13.495 -38.148 1.00 63.74  ? 100 LEU A N   1 
ATOM 725  C CA  . LEU A 1 101 ? -22.187 -13.244 -37.431 1.00 63.00  ? 100 LEU A CA  1 
ATOM 726  C C   . LEU A 1 101 ? -22.256 -14.046 -36.140 1.00 66.67  ? 100 LEU A C   1 
ATOM 727  O O   . LEU A 1 101 ? -22.656 -13.517 -35.097 1.00 73.17  ? 100 LEU A O   1 
ATOM 728  C CB  . LEU A 1 101 ? -23.385 -13.561 -38.327 1.00 62.60  ? 100 LEU A CB  1 
ATOM 729  C CG  . LEU A 1 101 ? -23.643 -12.608 -39.495 1.00 57.48  ? 100 LEU A CG  1 
ATOM 730  C CD1 . LEU A 1 101 ? -24.902 -13.024 -40.228 1.00 52.45  ? 100 LEU A CD1 1 
ATOM 731  C CD2 . LEU A 1 101 ? -23.760 -11.169 -39.006 1.00 52.68  ? 100 LEU A CD2 1 
ATOM 732  N N   . ALA A 1 102 ? -21.872 -15.317 -36.193 1.00 69.22  ? 101 ALA A N   1 
ATOM 733  C CA  . ALA A 1 102 ? -21.909 -16.208 -35.037 1.00 73.96  ? 101 ALA A CA  1 
ATOM 734  C C   . ALA A 1 102 ? -20.546 -16.328 -34.372 1.00 70.83  ? 101 ALA A C   1 
ATOM 735  O O   . ALA A 1 102 ? -20.148 -17.416 -33.955 1.00 71.67  ? 101 ALA A O   1 
ATOM 736  C CB  . ALA A 1 102 ? -22.429 -17.582 -35.447 1.00 75.99  ? 101 ALA A CB  1 
ATOM 737  N N   . ALA A 1 103 ? -19.812 -15.217 -34.255 1.00 61.41  ? 102 ALA A N   1 
ATOM 738  C CA  . ALA A 1 103 ? -18.473 -15.275 -33.674 1.00 59.33  ? 102 ALA A CA  1 
ATOM 739  C C   . ALA A 1 103 ? -18.498 -15.730 -32.219 1.00 59.56  ? 102 ALA A C   1 
ATOM 740  O O   . ALA A 1 103 ? -17.522 -16.322 -31.743 1.00 57.47  ? 102 ALA A O   1 
ATOM 741  C CB  . ALA A 1 103 ? -17.785 -13.915 -33.791 1.00 62.57  ? 102 ALA A CB  1 
ATOM 742  N N   . ALA A 1 104 ? -19.597 -15.472 -31.502 1.00 58.70  ? 103 ALA A N   1 
ATOM 743  C CA  . ALA A 1 104 ? -19.717 -15.821 -30.091 1.00 55.68  ? 103 ALA A CA  1 
ATOM 744  C C   . ALA A 1 104 ? -19.971 -17.314 -29.895 1.00 57.63  ? 103 ALA A C   1 
ATOM 745  O O   . ALA A 1 104 ? -19.282 -17.944 -29.081 1.00 58.28  ? 103 ALA A O   1 
ATOM 746  C CB  . ALA A 1 104 ? -20.819 -14.992 -29.423 1.00 57.13  ? 103 ALA A CB  1 
ATOM 747  N N   . PRO A 1 105 ? -20.937 -17.923 -30.600 1.00 55.54  ? 104 PRO A N   1 
ATOM 748  C CA  . PRO A 1 105 ? -21.117 -19.380 -30.449 1.00 52.69  ? 104 PRO A CA  1 
ATOM 749  C C   . PRO A 1 105 ? -19.896 -20.196 -30.844 1.00 57.82  ? 104 PRO A C   1 
ATOM 750  O O   . PRO A 1 105 ? -19.551 -21.157 -30.142 1.00 53.88  ? 104 PRO A O   1 
ATOM 751  C CB  . PRO A 1 105 ? -22.320 -19.670 -31.357 1.00 55.53  ? 104 PRO A CB  1 
ATOM 752  C CG  . PRO A 1 105 ? -23.071 -18.391 -31.381 1.00 52.41  ? 104 PRO A CG  1 
ATOM 753  C CD  . PRO A 1 105 ? -22.022 -17.336 -31.410 1.00 54.56  ? 104 PRO A CD  1 
ATOM 754  N N   . ILE A 1 106 ? -19.223 -19.845 -31.943 1.00 62.29  ? 105 ILE A N   1 
ATOM 755  C CA  . ILE A 1 106 ? -18.041 -20.607 -32.344 1.00 60.44  ? 105 ILE A CA  1 
ATOM 756  C C   . ILE A 1 106 ? -16.933 -20.468 -31.307 1.00 53.62  ? 105 ILE A C   1 
ATOM 757  O O   . ILE A 1 106 ? -16.269 -21.452 -30.959 1.00 52.46  ? 105 ILE A O   1 
ATOM 758  C CB  . ILE A 1 106 ? -17.567 -20.187 -33.749 1.00 54.65  ? 105 ILE A CB  1 
ATOM 759  C CG1 . ILE A 1 106 ? -18.755 -19.954 -34.681 1.00 56.07  ? 105 ILE A CG1 1 
ATOM 760  C CG2 . ILE A 1 106 ? -16.626 -21.233 -34.328 1.00 59.22  ? 105 ILE A CG2 1 
ATOM 761  C CD1 . ILE A 1 106 ? -18.367 -19.341 -36.008 1.00 58.03  ? 105 ILE A CD1 1 
ATOM 762  N N   . SER A 1 107 ? -16.718 -19.255 -30.793 1.00 49.86  ? 106 SER A N   1 
ATOM 763  C CA  . SER A 1 107 ? -15.725 -19.074 -29.738 1.00 55.83  ? 106 SER A CA  1 
ATOM 764  C C   . SER A 1 107 ? -16.104 -19.841 -28.477 1.00 58.60  ? 106 SER A C   1 
ATOM 765  O O   . SER A 1 107 ? -15.227 -20.356 -27.772 1.00 54.68  ? 106 SER A O   1 
ATOM 766  C CB  . SER A 1 107 ? -15.556 -17.585 -29.432 1.00 56.43  ? 106 SER A CB  1 
ATOM 767  O OG  . SER A 1 107 ? -14.652 -17.377 -28.363 1.00 57.22  ? 106 SER A OG  1 
ATOM 768  N N   . GLN A 1 108 ? -17.403 -19.932 -28.179 1.00 58.60  ? 107 GLN A N   1 
ATOM 769  C CA  . GLN A 1 108 ? -17.857 -20.685 -27.016 1.00 53.31  ? 107 GLN A CA  1 
ATOM 770  C C   . GLN A 1 108 ? -17.566 -22.174 -27.155 1.00 55.02  ? 107 GLN A C   1 
ATOM 771  O O   . GLN A 1 108 ? -17.284 -22.845 -26.156 1.00 59.60  ? 107 GLN A O   1 
ATOM 772  C CB  . GLN A 1 108 ? -19.353 -20.456 -26.801 1.00 55.41  ? 107 GLN A CB  1 
ATOM 773  C CG  . GLN A 1 108 ? -19.913 -21.104 -25.547 1.00 64.32  ? 107 GLN A CG  1 
ATOM 774  C CD  . GLN A 1 108 ? -19.457 -20.409 -24.280 1.00 61.28  ? 107 GLN A CD  1 
ATOM 775  O OE1 . GLN A 1 108 ? -19.855 -19.276 -24.000 1.00 57.39  ? 107 GLN A OE1 1 
ATOM 776  N NE2 . GLN A 1 108 ? -18.612 -21.083 -23.509 1.00 55.77  ? 107 GLN A NE2 1 
ATOM 777  N N   . GLY A 1 109 ? -17.625 -22.705 -28.372 1.00 56.35  ? 108 GLY A N   1 
ATOM 778  C CA  . GLY A 1 109 ? -17.398 -24.121 -28.580 1.00 52.44  ? 108 GLY A CA  1 
ATOM 779  C C   . GLY A 1 109 ? -15.939 -24.463 -28.790 1.00 50.19  ? 108 GLY A C   1 
ATOM 780  O O   . GLY A 1 109 ? -15.494 -25.560 -28.441 1.00 54.08  ? 108 GLY A O   1 
ATOM 781  N N   . LEU A 1 110 ? -15.181 -23.528 -29.359 1.00 49.43  ? 109 LEU A N   1 
ATOM 782  C CA  . LEU A 1 110 ? -13.777 -23.775 -29.661 1.00 50.14  ? 109 LEU A CA  1 
ATOM 783  C C   . LEU A 1 110 ? -12.867 -23.510 -28.468 1.00 53.20  ? 109 LEU A C   1 
ATOM 784  O O   . LEU A 1 110 ? -11.868 -24.215 -28.284 1.00 49.32  ? 109 LEU A O   1 
ATOM 785  C CB  . LEU A 1 110 ? -13.337 -22.916 -30.850 1.00 47.24  ? 109 LEU A CB  1 
ATOM 786  C CG  . LEU A 1 110 ? -13.899 -23.299 -32.221 1.00 48.52  ? 109 LEU A CG  1 
ATOM 787  C CD1 . LEU A 1 110 ? -13.281 -22.433 -33.306 1.00 49.04  ? 109 LEU A CD1 1 
ATOM 788  C CD2 . LEU A 1 110 ? -13.658 -24.774 -32.512 1.00 44.99  ? 109 LEU A CD2 1 
ATOM 789  N N   . PHE A 1 111 ? -13.195 -22.507 -27.649 1.00 51.33  ? 110 PHE A N   1 
ATOM 790  C CA  . PHE A 1 111 ? -12.353 -22.109 -26.532 1.00 53.42  ? 110 PHE A CA  1 
ATOM 791  C C   . PHE A 1 111 ? -13.037 -22.174 -25.175 1.00 60.97  ? 110 PHE A C   1 
ATOM 792  O O   . PHE A 1 111 ? -12.339 -22.161 -24.155 1.00 55.27  ? 110 PHE A O   1 
ATOM 793  C CB  . PHE A 1 111 ? -11.831 -20.678 -26.738 1.00 49.20  ? 110 PHE A CB  1 
ATOM 794  C CG  . PHE A 1 111 ? -10.949 -20.519 -27.943 1.00 51.28  ? 110 PHE A CG  1 
ATOM 795  C CD1 . PHE A 1 111 ? -9.606  -20.850 -27.882 1.00 52.52  ? 110 PHE A CD1 1 
ATOM 796  C CD2 . PHE A 1 111 ? -11.462 -20.037 -29.136 1.00 51.37  ? 110 PHE A CD2 1 
ATOM 797  C CE1 . PHE A 1 111 ? -8.790  -20.703 -28.987 1.00 48.11  ? 110 PHE A CE1 1 
ATOM 798  C CE2 . PHE A 1 111 ? -10.651 -19.887 -30.245 1.00 43.74  ? 110 PHE A CE2 1 
ATOM 799  C CZ  . PHE A 1 111 ? -9.313  -20.221 -30.169 1.00 44.45  ? 110 PHE A CZ  1 
ATOM 800  N N   . GLY A 1 112 ? -14.366 -22.236 -25.128 1.00 60.68  ? 111 GLY A N   1 
ATOM 801  C CA  . GLY A 1 112 ? -15.087 -22.239 -23.878 1.00 57.94  ? 111 GLY A CA  1 
ATOM 802  C C   . GLY A 1 112 ? -15.519 -20.876 -23.387 1.00 64.51  ? 111 GLY A C   1 
ATOM 803  O O   . GLY A 1 112 ? -16.332 -20.802 -22.458 1.00 71.63  ? 111 GLY A O   1 
ATOM 804  N N   . ASN A 1 113 ? -15.004 -19.799 -23.976 1.00 71.81  ? 112 ASN A N   1 
ATOM 805  C CA  . ASN A 1 113 ? -15.351 -18.436 -23.598 1.00 72.88  ? 112 ASN A CA  1 
ATOM 806  C C   . ASN A 1 113 ? -15.790 -17.671 -24.841 1.00 71.28  ? 112 ASN A C   1 
ATOM 807  O O   . ASN A 1 113 ? -15.866 -18.219 -25.944 1.00 69.31  ? 112 ASN A O   1 
ATOM 808  C CB  . ASN A 1 113 ? -14.171 -17.727 -22.924 1.00 72.53  ? 112 ASN A CB  1 
ATOM 809  C CG  . ASN A 1 113 ? -13.368 -18.650 -22.033 1.00 93.94  ? 112 ASN A CG  1 
ATOM 810  O OD1 . ASN A 1 113 ? -13.925 -19.384 -21.215 1.00 106.70 ? 112 ASN A OD1 1 
ATOM 811  N ND2 . ASN A 1 113 ? -12.050 -18.626 -22.194 1.00 97.21  ? 112 ASN A ND2 1 
ATOM 812  N N   . THR A 1 114 ? -16.072 -16.383 -24.658 1.00 64.46  ? 113 THR A N   1 
ATOM 813  C CA  . THR A 1 114 ? -16.430 -15.494 -25.754 1.00 62.75  ? 113 THR A CA  1 
ATOM 814  C C   . THR A 1 114 ? -15.349 -14.457 -26.035 1.00 67.20  ? 113 THR A C   1 
ATOM 815  O O   . THR A 1 114 ? -15.599 -13.494 -26.766 1.00 65.05  ? 113 THR A O   1 
ATOM 816  C CB  . THR A 1 114 ? -17.763 -14.801 -25.458 1.00 68.79  ? 113 THR A CB  1 
ATOM 817  O OG1 . THR A 1 114 ? -18.198 -14.080 -26.617 1.00 74.45  ? 113 THR A OG1 1 
ATOM 818  C CG2 . THR A 1 114 ? -17.624 -13.842 -24.279 1.00 63.02  ? 113 THR A CG2 1 
ATOM 819  N N   . ASP A 1 115 ? -14.152 -14.638 -25.485 1.00 72.93  ? 114 ASP A N   1 
ATOM 820  C CA  . ASP A 1 115 ? -13.071 -13.671 -25.621 1.00 71.37  ? 114 ASP A CA  1 
ATOM 821  C C   . ASP A 1 115 ? -12.322 -13.786 -26.944 1.00 61.93  ? 114 ASP A C   1 
ATOM 822  O O   . ASP A 1 115 ? -11.301 -13.112 -27.116 1.00 68.29  ? 114 ASP A O   1 
ATOM 823  C CB  . ASP A 1 115 ? -12.088 -13.827 -24.458 1.00 65.55  ? 114 ASP A CB  1 
ATOM 824  C CG  . ASP A 1 115 ? -12.782 -13.886 -23.112 1.00 65.89  ? 114 ASP A CG  1 
ATOM 825  O OD1 . ASP A 1 115 ? -14.019 -13.709 -23.069 1.00 63.99  ? 114 ASP A OD1 1 
ATOM 826  O OD2 . ASP A 1 115 ? -12.091 -14.114 -22.097 1.00 63.37  ? 114 ASP A OD2 1 
ATOM 827  N N   . TYR A 1 116 ? -12.793 -14.613 -27.875 1.00 57.51  ? 115 TYR A N   1 
ATOM 828  C CA  . TYR A 1 116 ? -12.109 -14.837 -29.143 1.00 55.54  ? 115 TYR A CA  1 
ATOM 829  C C   . TYR A 1 116 ? -13.025 -14.577 -30.335 1.00 58.63  ? 115 TYR A C   1 
ATOM 830  O O   . TYR A 1 116 ? -12.899 -15.228 -31.373 1.00 59.10  ? 115 TYR A O   1 
ATOM 831  C CB  . TYR A 1 116 ? -11.548 -16.256 -29.208 1.00 50.98  ? 115 TYR A CB  1 
ATOM 832  C CG  . TYR A 1 116 ? -10.701 -16.634 -28.017 1.00 55.32  ? 115 TYR A CG  1 
ATOM 833  C CD1 . TYR A 1 116 ? -9.334  -16.378 -27.999 1.00 53.74  ? 115 TYR A CD1 1 
ATOM 834  C CD2 . TYR A 1 116 ? -11.272 -17.228 -26.900 1.00 59.48  ? 115 TYR A CD2 1 
ATOM 835  C CE1 . TYR A 1 116 ? -8.559  -16.722 -26.908 1.00 53.07  ? 115 TYR A CE1 1 
ATOM 836  C CE2 . TYR A 1 116 ? -10.508 -17.569 -25.803 1.00 58.98  ? 115 TYR A CE2 1 
ATOM 837  C CZ  . TYR A 1 116 ? -9.154  -17.315 -25.812 1.00 58.04  ? 115 TYR A CZ  1 
ATOM 838  O OH  . TYR A 1 116 ? -8.393  -17.656 -24.721 1.00 62.12  ? 115 TYR A OH  1 
ATOM 839  N N   . GLN A 1 117 ? -13.954 -13.626 -30.199 1.00 60.27  ? 116 GLN A N   1 
ATOM 840  C CA  . GLN A 1 117 ? -14.830 -13.289 -31.317 1.00 54.78  ? 116 GLN A CA  1 
ATOM 841  C C   . GLN A 1 117 ? -14.048 -12.628 -32.444 1.00 54.25  ? 116 GLN A C   1 
ATOM 842  O O   . GLN A 1 117 ? -14.233 -12.961 -33.620 1.00 58.31  ? 116 GLN A O   1 
ATOM 843  C CB  . GLN A 1 117 ? -15.957 -12.372 -30.847 1.00 55.21  ? 116 GLN A CB  1 
ATOM 844  C CG  . GLN A 1 117 ? -16.676 -12.844 -29.607 1.00 58.90  ? 116 GLN A CG  1 
ATOM 845  C CD  . GLN A 1 117 ? -17.966 -12.088 -29.368 1.00 65.06  ? 116 GLN A CD  1 
ATOM 846  O OE1 . GLN A 1 117 ? -18.222 -11.062 -29.999 1.00 65.81  ? 116 GLN A OE1 1 
ATOM 847  N NE2 . GLN A 1 117 ? -18.776 -12.578 -28.438 1.00 65.93  ? 116 GLN A NE2 1 
ATOM 848  N N   . GLY A 1 118 ? -13.176 -11.676 -32.101 1.00 52.56  ? 117 GLY A N   1 
ATOM 849  C CA  . GLY A 1 118 ? -12.376 -11.015 -33.115 1.00 51.05  ? 117 GLY A CA  1 
ATOM 850  C C   . GLY A 1 118 ? -11.472 -11.968 -33.867 1.00 55.96  ? 117 GLY A C   1 
ATOM 851  O O   . GLY A 1 118 ? -11.207 -11.770 -35.056 1.00 64.10  ? 117 GLY A O   1 
ATOM 852  N N   . LEU A 1 119 ? -10.991 -13.015 -33.194 1.00 50.73  ? 118 LEU A N   1 
ATOM 853  C CA  . LEU A 1 119 ? -10.195 -14.020 -33.888 1.00 55.53  ? 118 LEU A CA  1 
ATOM 854  C C   . LEU A 1 119 ? -11.040 -14.781 -34.903 1.00 55.75  ? 118 LEU A C   1 
ATOM 855  O O   . LEU A 1 119 ? -10.580 -15.059 -36.017 1.00 53.68  ? 118 LEU A O   1 
ATOM 856  C CB  . LEU A 1 119 ? -9.557  -14.973 -32.877 1.00 51.26  ? 118 LEU A CB  1 
ATOM 857  C CG  . LEU A 1 119 ? -8.908  -16.244 -33.426 1.00 47.54  ? 118 LEU A CG  1 
ATOM 858  C CD1 . LEU A 1 119 ? -7.524  -15.948 -33.981 1.00 49.56  ? 118 LEU A CD1 1 
ATOM 859  C CD2 . LEU A 1 119 ? -8.831  -17.296 -32.336 1.00 48.19  ? 118 LEU A CD2 1 
ATOM 860  N N   . VAL A 1 120 ? -12.286 -15.105 -34.547 1.00 56.13  ? 119 VAL A N   1 
ATOM 861  C CA  . VAL A 1 120 ? -13.159 -15.827 -35.469 1.00 60.31  ? 119 VAL A CA  1 
ATOM 862  C C   . VAL A 1 120 ? -13.504 -14.959 -36.673 1.00 60.41  ? 119 VAL A C   1 
ATOM 863  O O   . VAL A 1 120 ? -13.557 -15.443 -37.810 1.00 62.57  ? 119 VAL A O   1 
ATOM 864  C CB  . VAL A 1 120 ? -14.424 -16.313 -34.739 1.00 58.37  ? 119 VAL A CB  1 
ATOM 865  C CG1 . VAL A 1 120 ? -15.372 -17.000 -35.713 1.00 62.18  ? 119 VAL A CG1 1 
ATOM 866  C CG2 . VAL A 1 120 ? -14.052 -17.249 -33.604 1.00 50.50  ? 119 VAL A CG2 1 
ATOM 867  N N   . ARG A 1 121 ? -13.745 -13.664 -36.446 1.00 58.22  ? 120 ARG A N   1 
ATOM 868  C CA  . ARG A 1 121 ? -14.006 -12.759 -37.560 1.00 59.94  ? 120 ARG A CA  1 
ATOM 869  C C   . ARG A 1 121 ? -12.784 -12.612 -38.455 1.00 55.71  ? 120 ARG A C   1 
ATOM 870  O O   . ARG A 1 121 ? -12.921 -12.350 -39.655 1.00 58.73  ? 120 ARG A O   1 
ATOM 871  C CB  . ARG A 1 121 ? -14.450 -11.393 -37.039 1.00 57.95  ? 120 ARG A CB  1 
ATOM 872  C CG  . ARG A 1 121 ? -15.800 -11.408 -36.344 1.00 56.61  ? 120 ARG A CG  1 
ATOM 873  C CD  . ARG A 1 121 ? -16.202 -10.013 -35.900 1.00 62.20  ? 120 ARG A CD  1 
ATOM 874  N NE  . ARG A 1 121 ? -17.207 -10.047 -34.845 1.00 57.40  ? 120 ARG A NE  1 
ATOM 875  C CZ  . ARG A 1 121 ? -16.971 -9.727  -33.580 1.00 55.44  ? 120 ARG A CZ  1 
ATOM 876  N NH1 . ARG A 1 121 ? -15.769 -9.349  -33.177 1.00 57.69  ? 120 ARG A NH1 1 
ATOM 877  N NH2 . ARG A 1 121 ? -17.964 -9.789  -32.699 1.00 57.49  ? 120 ARG A NH2 1 
ATOM 878  N N   . LEU A 1 122 ? -11.586 -12.776 -37.894 1.00 57.16  ? 121 LEU A N   1 
ATOM 879  C CA  . LEU A 1 122 ? -10.380 -12.776 -38.713 1.00 58.44  ? 121 LEU A CA  1 
ATOM 880  C C   . LEU A 1 122 ? -10.214 -14.088 -39.470 1.00 61.51  ? 121 LEU A C   1 
ATOM 881  O O   . LEU A 1 122 ? -9.602  -14.106 -40.544 1.00 63.76  ? 121 LEU A O   1 
ATOM 882  C CB  . LEU A 1 122 ? -9.151  -12.499 -37.844 1.00 50.23  ? 121 LEU A CB  1 
ATOM 883  C CG  . LEU A 1 122 ? -8.707  -11.037 -37.703 1.00 52.06  ? 121 LEU A CG  1 
ATOM 884  C CD1 . LEU A 1 122 ? -7.812  -10.635 -38.866 1.00 61.65  ? 121 LEU A CD1 1 
ATOM 885  C CD2 . LEU A 1 122 ? -9.892  -10.083 -37.588 1.00 51.20  ? 121 LEU A CD2 1 
ATOM 886  N N   . VAL A 1 123 ? -10.753 -15.187 -38.935 1.00 57.84  ? 122 VAL A N   1 
ATOM 887  C CA  . VAL A 1 123 ? -10.720 -16.456 -39.654 1.00 56.10  ? 122 VAL A CA  1 
ATOM 888  C C   . VAL A 1 123 ? -11.570 -16.379 -40.916 1.00 55.92  ? 122 VAL A C   1 
ATOM 889  O O   . VAL A 1 123 ? -11.259 -17.028 -41.923 1.00 58.05  ? 122 VAL A O   1 
ATOM 890  C CB  . VAL A 1 123 ? -11.170 -17.601 -38.724 1.00 53.02  ? 122 VAL A CB  1 
ATOM 891  C CG1 . VAL A 1 123 ? -11.464 -18.867 -39.513 1.00 50.03  ? 122 VAL A CG1 1 
ATOM 892  C CG2 . VAL A 1 123 ? -10.107 -17.872 -37.676 1.00 53.50  ? 122 VAL A CG2 1 
ATOM 893  N N   . ALA A 1 124 ? -12.637 -15.575 -40.892 1.00 55.91  ? 123 ALA A N   1 
ATOM 894  C CA  . ALA A 1 124 ? -13.486 -15.415 -42.070 1.00 56.85  ? 123 ALA A CA  1 
ATOM 895  C C   . ALA A 1 124 ? -12.679 -14.962 -43.280 1.00 56.89  ? 123 ALA A C   1 
ATOM 896  O O   . ALA A 1 124 ? -12.882 -15.462 -44.393 1.00 60.23  ? 123 ALA A O   1 
ATOM 897  C CB  . ALA A 1 124 ? -14.610 -14.424 -41.772 1.00 52.12  ? 123 ALA A CB  1 
ATOM 898  N N   . LEU A 1 125 ? -11.759 -14.016 -43.085 1.00 55.36  ? 124 LEU A N   1 
ATOM 899  C CA  . LEU A 1 125 ? -10.867 -13.631 -44.173 1.00 57.55  ? 124 LEU A CA  1 
ATOM 900  C C   . LEU A 1 125 ? -9.776  -14.671 -44.392 1.00 55.24  ? 124 LEU A C   1 
ATOM 901  O O   . LEU A 1 125 ? -9.304  -14.845 -45.522 1.00 59.33  ? 124 LEU A O   1 
ATOM 902  C CB  . LEU A 1 125 ? -10.253 -12.258 -43.890 1.00 57.23  ? 124 LEU A CB  1 
ATOM 903  C CG  . LEU A 1 125 ? -9.212  -11.740 -44.888 1.00 61.31  ? 124 LEU A CG  1 
ATOM 904  C CD1 . LEU A 1 125 ? -9.814  -11.572 -46.277 1.00 59.30  ? 124 LEU A CD1 1 
ATOM 905  C CD2 . LEU A 1 125 ? -8.603  -10.433 -44.402 1.00 61.60  ? 124 LEU A CD2 1 
ATOM 906  N N   . VAL A 1 126 ? -9.376  -15.380 -43.335 1.00 52.40  ? 125 VAL A N   1 
ATOM 907  C CA  . VAL A 1 126 ? -8.313  -16.374 -43.462 1.00 54.22  ? 125 VAL A CA  1 
ATOM 908  C C   . VAL A 1 126 ? -8.779  -17.551 -44.311 1.00 52.67  ? 125 VAL A C   1 
ATOM 909  O O   . VAL A 1 126 ? -8.072  -17.996 -45.222 1.00 56.22  ? 125 VAL A O   1 
ATOM 910  C CB  . VAL A 1 126 ? -7.839  -16.831 -42.071 1.00 55.52  ? 125 VAL A CB  1 
ATOM 911  C CG1 . VAL A 1 126 ? -7.271  -18.242 -42.139 1.00 52.83  ? 125 VAL A CG1 1 
ATOM 912  C CG2 . VAL A 1 126 ? -6.809  -15.859 -41.517 1.00 49.65  ? 125 VAL A CG2 1 
ATOM 913  N N   . GLN A 1 127 ? -9.975  -18.074 -44.027 1.00 56.16  ? 126 GLN A N   1 
ATOM 914  C CA  . GLN A 1 127 ? -10.489 -19.203 -44.796 1.00 59.34  ? 126 GLN A CA  1 
ATOM 915  C C   . GLN A 1 127 ? -10.776 -18.832 -46.244 1.00 61.01  ? 126 GLN A C   1 
ATOM 916  O O   . GLN A 1 127 ? -10.835 -19.722 -47.098 1.00 64.76  ? 126 GLN A O   1 
ATOM 917  C CB  . GLN A 1 127 ? -11.750 -19.767 -44.137 1.00 59.07  ? 126 GLN A CB  1 
ATOM 918  C CG  . GLN A 1 127 ? -12.901 -18.778 -44.009 1.00 58.21  ? 126 GLN A CG  1 
ATOM 919  C CD  . GLN A 1 127 ? -13.872 -18.849 -45.173 1.00 59.97  ? 126 GLN A CD  1 
ATOM 920  O OE1 . GLN A 1 127 ? -14.203 -19.934 -45.657 1.00 60.09  ? 126 GLN A OE1 1 
ATOM 921  N NE2 . GLN A 1 127 ? -14.343 -17.690 -45.620 1.00 57.64  ? 126 GLN A NE2 1 
ATOM 922  N N   . MET A 1 128 ? -10.961 -17.542 -46.535 1.00 57.60  ? 127 MET A N   1 
ATOM 923  C CA  . MET A 1 128 ? -11.086 -17.109 -47.922 1.00 54.85  ? 127 MET A CA  1 
ATOM 924  C C   . MET A 1 128 ? -9.783  -17.332 -48.682 1.00 54.52  ? 127 MET A C   1 
ATOM 925  O O   . MET A 1 128 ? -9.797  -17.801 -49.827 1.00 58.91  ? 127 MET A O   1 
ATOM 926  C CB  . MET A 1 128 ? -11.502 -15.640 -47.970 1.00 54.06  ? 127 MET A CB  1 
ATOM 927  C CG  . MET A 1 128 ? -12.969 -15.405 -47.647 1.00 57.84  ? 127 MET A CG  1 
ATOM 928  S SD  . MET A 1 128 ? -13.715 -14.109 -48.652 1.00 77.65  ? 127 MET A SD  1 
ATOM 929  C CE  . MET A 1 128 ? -13.794 -14.907 -50.255 1.00 56.99  ? 127 MET A CE  1 
ATOM 930  N N   . GLY A 1 129 ? -8.647  -17.010 -48.059 1.00 50.61  ? 128 GLY A N   1 
ATOM 931  C CA  . GLY A 1 129 ? -7.367  -17.270 -48.692 1.00 49.36  ? 128 GLY A CA  1 
ATOM 932  C C   . GLY A 1 129 ? -7.020  -18.743 -48.737 1.00 52.17  ? 128 GLY A C   1 
ATOM 933  O O   . GLY A 1 129 ? -6.314  -19.192 -49.645 1.00 53.80  ? 128 GLY A O   1 
ATOM 934  N N   . ILE A 1 130 ? -7.505  -19.514 -47.763 1.00 54.92  ? 129 ILE A N   1 
ATOM 935  C CA  . ILE A 1 130 ? -7.277  -20.954 -47.770 1.00 52.89  ? 129 ILE A CA  1 
ATOM 936  C C   . ILE A 1 130 ? -8.020  -21.603 -48.930 1.00 50.42  ? 129 ILE A C   1 
ATOM 937  O O   . ILE A 1 130 ? -7.471  -22.455 -49.638 1.00 52.47  ? 129 ILE A O   1 
ATOM 938  C CB  . ILE A 1 130 ? -7.688  -21.561 -46.416 1.00 52.72  ? 129 ILE A CB  1 
ATOM 939  C CG1 . ILE A 1 130 ? -6.635  -21.250 -45.350 1.00 55.13  ? 129 ILE A CG1 1 
ATOM 940  C CG2 . ILE A 1 130 ? -7.901  -23.060 -46.539 1.00 55.15  ? 129 ILE A CG2 1 
ATOM 941  C CD1 . ILE A 1 130 ? -6.963  -21.804 -43.979 1.00 44.90  ? 129 ILE A CD1 1 
ATOM 942  N N   . ALA A 1 131 ? -9.274  -21.199 -49.154 1.00 52.11  ? 130 ALA A N   1 
ATOM 943  C CA  . ALA A 1 131 ? -10.060 -21.777 -50.240 1.00 57.65  ? 130 ALA A CA  1 
ATOM 944  C C   . ALA A 1 131 ? -9.484  -21.413 -51.603 1.00 54.87  ? 130 ALA A C   1 
ATOM 945  O O   . ALA A 1 131 ? -9.399  -22.266 -52.495 1.00 47.34  ? 130 ALA A O   1 
ATOM 946  C CB  . ALA A 1 131 ? -11.515 -21.320 -50.133 1.00 56.01  ? 130 ALA A CB  1 
ATOM 947  N N   . TRP A 1 132 ? -9.084  -20.152 -51.784 1.00 54.47  ? 131 TRP A N   1 
ATOM 948  C CA  . TRP A 1 132 ? -8.544  -19.732 -53.073 1.00 54.56  ? 131 TRP A CA  1 
ATOM 949  C C   . TRP A 1 132 ? -7.170  -20.339 -53.323 1.00 50.07  ? 131 TRP A C   1 
ATOM 950  O O   . TRP A 1 132 ? -6.865  -20.755 -54.446 1.00 52.19  ? 131 TRP A O   1 
ATOM 951  C CB  . TRP A 1 132 ? -8.492  -18.205 -53.145 1.00 57.07  ? 131 TRP A CB  1 
ATOM 952  C CG  . TRP A 1 132 ? -9.788  -17.610 -53.602 1.00 64.46  ? 131 TRP A CG  1 
ATOM 953  C CD1 . TRP A 1 132 ? -10.704 -16.950 -52.835 1.00 70.54  ? 131 TRP A CD1 1 
ATOM 954  C CD2 . TRP A 1 132 ? -10.325 -17.640 -54.930 1.00 56.40  ? 131 TRP A CD2 1 
ATOM 955  N NE1 . TRP A 1 132 ? -11.774 -16.561 -53.605 1.00 70.96  ? 131 TRP A NE1 1 
ATOM 956  C CE2 . TRP A 1 132 ? -11.565 -16.973 -54.895 1.00 62.21  ? 131 TRP A CE2 1 
ATOM 957  C CE3 . TRP A 1 132 ? -9.874  -18.161 -56.147 1.00 54.08  ? 131 TRP A CE3 1 
ATOM 958  C CZ2 . TRP A 1 132 ? -12.360 -16.813 -56.028 1.00 62.90  ? 131 TRP A CZ2 1 
ATOM 959  C CZ3 . TRP A 1 132 ? -10.664 -18.002 -57.270 1.00 59.47  ? 131 TRP A CZ3 1 
ATOM 960  C CH2 . TRP A 1 132 ? -11.893 -17.334 -57.204 1.00 59.53  ? 131 TRP A CH2 1 
ATOM 961  N N   . GLY A 1 133 ? -6.328  -20.403 -52.290 1.00 49.73  ? 132 GLY A N   1 
ATOM 962  C CA  . GLY A 1 133 ? -5.033  -21.043 -52.448 1.00 48.17  ? 132 GLY A CA  1 
ATOM 963  C C   . GLY A 1 133 ? -5.149  -22.514 -52.801 1.00 51.18  ? 132 GLY A C   1 
ATOM 964  O O   . GLY A 1 133 ? -4.432  -23.011 -53.673 1.00 50.26  ? 132 GLY A O   1 
ATOM 965  N N   . ASN A 1 134 ? -6.058  -23.229 -52.133 1.00 57.60  ? 133 ASN A N   1 
ATOM 966  C CA  . ASN A 1 134 ? -6.257  -24.642 -52.435 1.00 54.02  ? 133 ASN A CA  1 
ATOM 967  C C   . ASN A 1 134 ? -6.805  -24.845 -53.841 1.00 54.34  ? 133 ASN A C   1 
ATOM 968  O O   . ASN A 1 134 ? -6.505  -25.860 -54.481 1.00 57.39  ? 133 ASN A O   1 
ATOM 969  C CB  . ASN A 1 134 ? -7.191  -25.274 -51.405 1.00 58.51  ? 133 ASN A CB  1 
ATOM 970  C CG  . ASN A 1 134 ? -6.521  -25.483 -50.059 1.00 61.00  ? 133 ASN A CG  1 
ATOM 971  O OD1 . ASN A 1 134 ? -5.316  -25.269 -49.912 1.00 60.87  ? 133 ASN A OD1 1 
ATOM 972  N ND2 . ASN A 1 134 ? -7.301  -25.901 -49.067 1.00 53.51  ? 133 ASN A ND2 1 
ATOM 973  N N   . LEU A 1 135 ? -7.604  -23.898 -54.336 1.00 50.20  ? 134 LEU A N   1 
ATOM 974  C CA  . LEU A 1 135 ? -8.102  -23.987 -55.705 1.00 51.03  ? 134 LEU A CA  1 
ATOM 975  C C   . LEU A 1 135 ? -6.968  -23.851 -56.713 1.00 47.00  ? 134 LEU A C   1 
ATOM 976  O O   . LEU A 1 135 ? -6.880  -24.628 -57.670 1.00 47.11  ? 134 LEU A O   1 
ATOM 977  C CB  . LEU A 1 135 ? -9.169  -22.919 -55.945 1.00 52.35  ? 134 LEU A CB  1 
ATOM 978  C CG  . LEU A 1 135 ? -9.711  -22.836 -57.373 1.00 41.46  ? 134 LEU A CG  1 
ATOM 979  C CD1 . LEU A 1 135 ? -10.362 -24.148 -57.775 1.00 32.97  ? 134 LEU A CD1 1 
ATOM 980  C CD2 . LEU A 1 135 ? -10.694 -21.684 -57.502 1.00 42.42  ? 134 LEU A CD2 1 
ATOM 981  N N   . LEU A 1 136 ? -6.088  -22.866 -56.513 1.00 46.57  ? 135 LEU A N   1 
ATOM 982  C CA  . LEU A 1 136 ? -4.972  -22.676 -57.435 1.00 45.48  ? 135 LEU A CA  1 
ATOM 983  C C   . LEU A 1 136 ? -4.025  -23.867 -57.407 1.00 46.21  ? 135 LEU A C   1 
ATOM 984  O O   . LEU A 1 136 ? -3.464  -24.247 -58.442 1.00 44.03  ? 135 LEU A O   1 
ATOM 985  C CB  . LEU A 1 136 ? -4.222  -21.390 -57.095 1.00 45.29  ? 135 LEU A CB  1 
ATOM 986  C CG  . LEU A 1 136 ? -5.067  -20.119 -57.066 1.00 45.13  ? 135 LEU A CG  1 
ATOM 987  C CD1 . LEU A 1 136 ? -4.196  -18.917 -56.755 1.00 45.93  ? 135 LEU A CD1 1 
ATOM 988  C CD2 . LEU A 1 136 ? -5.805  -19.934 -58.382 1.00 39.43  ? 135 LEU A CD2 1 
ATOM 989  N N   . LEU A 1 137 ? -3.828  -24.465 -56.231 1.00 46.22  ? 136 LEU A N   1 
ATOM 990  C CA  . LEU A 1 137 ? -3.004  -25.665 -56.156 1.00 43.63  ? 136 LEU A CA  1 
ATOM 991  C C   . LEU A 1 137 ? -3.688  -26.847 -56.830 1.00 44.06  ? 136 LEU A C   1 
ATOM 992  O O   . LEU A 1 137 ? -3.012  -27.763 -57.311 1.00 46.11  ? 136 LEU A O   1 
ATOM 993  C CB  . LEU A 1 137 ? -2.677  -25.992 -54.699 1.00 44.24  ? 136 LEU A CB  1 
ATOM 994  C CG  . LEU A 1 137 ? -1.910  -24.935 -53.899 1.00 40.40  ? 136 LEU A CG  1 
ATOM 995  C CD1 . LEU A 1 137 ? -1.969  -25.255 -52.413 1.00 42.50  ? 136 LEU A CD1 1 
ATOM 996  C CD2 . LEU A 1 137 ? -0.470  -24.819 -54.363 1.00 37.79  ? 136 LEU A CD2 1 
ATOM 997  N N   . ALA A 1 138 ? -5.022  -26.839 -56.884 1.00 43.33  ? 137 ALA A N   1 
ATOM 998  C CA  . ALA A 1 138 ? -5.740  -27.914 -57.560 1.00 41.04  ? 137 ALA A CA  1 
ATOM 999  C C   . ALA A 1 138 ? -5.604  -27.804 -59.074 1.00 41.46  ? 137 ALA A C   1 
ATOM 1000 O O   . ALA A 1 138 ? -5.492  -28.823 -59.765 1.00 41.83  ? 137 ALA A O   1 
ATOM 1001 C CB  . ALA A 1 138 ? -7.212  -27.903 -57.148 1.00 41.79  ? 137 ALA A CB  1 
ATOM 1002 N N   . LEU A 1 139 ? -5.612  -26.579 -59.610 1.00 40.89  ? 138 LEU A N   1 
ATOM 1003 C CA  . LEU A 1 139 ? -5.433  -26.406 -61.050 1.00 40.95  ? 138 LEU A CA  1 
ATOM 1004 C C   . LEU A 1 139 ? -4.037  -26.827 -61.488 1.00 44.95  ? 138 LEU A C   1 
ATOM 1005 O O   . LEU A 1 139 ? -3.875  -27.460 -62.538 1.00 50.94  ? 138 LEU A O   1 
ATOM 1006 C CB  . LEU A 1 139 ? -5.696  -24.955 -61.453 1.00 39.18  ? 138 LEU A CB  1 
ATOM 1007 C CG  . LEU A 1 139 ? -6.850  -24.220 -60.777 1.00 43.24  ? 138 LEU A CG  1 
ATOM 1008 C CD1 . LEU A 1 139 ? -6.587  -22.725 -60.774 1.00 48.66  ? 138 LEU A CD1 1 
ATOM 1009 C CD2 . LEU A 1 139 ? -8.164  -24.534 -61.476 1.00 42.85  ? 138 LEU A CD2 1 
ATOM 1010 N N   . MET A 1 140 ? -3.015  -26.479 -60.703 1.00 43.12  ? 139 MET A N   1 
ATOM 1011 C CA  . MET A 1 140 ? -1.660  -26.905 -61.032 1.00 41.87  ? 139 MET A CA  1 
ATOM 1012 C C   . MET A 1 140 ? -1.506  -28.416 -60.921 1.00 44.97  ? 139 MET A C   1 
ATOM 1013 O O   . MET A 1 140 ? -0.714  -29.011 -61.659 1.00 51.37  ? 139 MET A O   1 
ATOM 1014 C CB  . MET A 1 140 ? -0.650  -26.196 -60.132 1.00 41.65  ? 139 MET A CB  1 
ATOM 1015 C CG  . MET A 1 140 ? -0.231  -24.828 -60.646 1.00 53.85  ? 139 MET A CG  1 
ATOM 1016 S SD  . MET A 1 140 ? 0.686   -23.863 -59.429 1.00 55.06  ? 139 MET A SD  1 
ATOM 1017 C CE  . MET A 1 140 ? -0.034  -24.465 -57.908 1.00 46.97  ? 139 MET A CE  1 
ATOM 1018 N N   . LYS A 1 141 ? -2.249  -29.052 -60.013 1.00 42.80  ? 140 LYS A N   1 
ATOM 1019 C CA  . LYS A 1 141 ? -2.227  -30.507 -59.944 1.00 41.63  ? 140 LYS A CA  1 
ATOM 1020 C C   . LYS A 1 141 ? -2.882  -31.131 -61.171 1.00 43.81  ? 140 LYS A C   1 
ATOM 1021 O O   . LYS A 1 141 ? -2.431  -32.181 -61.645 1.00 41.41  ? 140 LYS A O   1 
ATOM 1022 C CB  . LYS A 1 141 ? -2.919  -30.984 -58.667 1.00 41.28  ? 140 LYS A CB  1 
ATOM 1023 C CG  . LYS A 1 141 ? -2.045  -30.904 -57.427 1.00 46.34  ? 140 LYS A CG  1 
ATOM 1024 C CD  . LYS A 1 141 ? -2.797  -31.358 -56.187 1.00 42.05  ? 140 LYS A CD  1 
ATOM 1025 C CE  . LYS A 1 141 ? -2.048  -30.984 -54.923 1.00 39.66  ? 140 LYS A CE  1 
ATOM 1026 N NZ  . LYS A 1 141 ? -2.913  -31.133 -53.726 1.00 44.12  ? 140 LYS A NZ  1 
ATOM 1027 N N   . GLY A 1 142 ? -3.931  -30.497 -61.701 1.00 44.13  ? 141 GLY A N   1 
ATOM 1028 C CA  . GLY A 1 142 ? -4.612  -31.044 -62.862 1.00 41.47  ? 141 GLY A CA  1 
ATOM 1029 C C   . GLY A 1 142 ? -3.737  -31.099 -64.096 1.00 44.25  ? 141 GLY A C   1 
ATOM 1030 O O   . GLY A 1 142 ? -3.933  -31.954 -64.963 1.00 44.18  ? 141 GLY A O   1 
ATOM 1031 N N   . PHE A 1 143 ? -2.764  -30.197 -64.196 1.00 42.87  ? 142 PHE A N   1 
ATOM 1032 C CA  . PHE A 1 143 ? -1.803  -30.205 -65.288 1.00 42.41  ? 142 PHE A CA  1 
ATOM 1033 C C   . PHE A 1 143 ? -0.522  -30.951 -64.936 1.00 43.36  ? 142 PHE A C   1 
ATOM 1034 O O   . PHE A 1 143 ? 0.462   -30.850 -65.677 1.00 39.95  ? 142 PHE A O   1 
ATOM 1035 C CB  . PHE A 1 143 ? -1.478  -28.771 -65.708 1.00 41.84  ? 142 PHE A CB  1 
ATOM 1036 C CG  . PHE A 1 143 ? -2.627  -28.062 -66.358 1.00 45.26  ? 142 PHE A CG  1 
ATOM 1037 C CD1 . PHE A 1 143 ? -3.089  -28.462 -67.600 1.00 42.55  ? 142 PHE A CD1 1 
ATOM 1038 C CD2 . PHE A 1 143 ? -3.253  -27.003 -65.723 1.00 47.62  ? 142 PHE A CD2 1 
ATOM 1039 C CE1 . PHE A 1 143 ? -4.151  -27.818 -68.200 1.00 46.41  ? 142 PHE A CE1 1 
ATOM 1040 C CE2 . PHE A 1 143 ? -4.315  -26.353 -66.319 1.00 49.94  ? 142 PHE A CE2 1 
ATOM 1041 C CZ  . PHE A 1 143 ? -4.766  -26.761 -67.559 1.00 49.35  ? 142 PHE A CZ  1 
ATOM 1042 N N   . ARG A 1 144 ? -0.516  -31.688 -63.822 1.00 41.64  ? 143 ARG A N   1 
ATOM 1043 C CA  . ARG A 1 144 ? 0.631   -32.496 -63.405 1.00 43.16  ? 143 ARG A CA  1 
ATOM 1044 C C   . ARG A 1 144 ? 1.889   -31.642 -63.250 1.00 41.62  ? 143 ARG A C   1 
ATOM 1045 O O   . ARG A 1 144 ? 2.998   -32.069 -63.579 1.00 38.99  ? 143 ARG A O   1 
ATOM 1046 C CB  . ARG A 1 144 ? 0.871   -33.656 -64.375 1.00 48.27  ? 143 ARG A CB  1 
ATOM 1047 C CG  . ARG A 1 144 ? -0.350  -34.542 -64.596 1.00 46.81  ? 143 ARG A CG  1 
ATOM 1048 C CD  . ARG A 1 144 ? 0.033   -35.870 -65.234 1.00 47.02  ? 143 ARG A CD  1 
ATOM 1049 N NE  . ARG A 1 144 ? 0.390   -35.722 -66.640 1.00 51.89  ? 143 ARG A NE  1 
ATOM 1050 C CZ  . ARG A 1 144 ? 0.763   -36.723 -67.426 1.00 55.72  ? 143 ARG A CZ  1 
ATOM 1051 N NH1 . ARG A 1 144 ? 0.854   -37.962 -66.972 1.00 56.26  ? 143 ARG A NH1 1 
ATOM 1052 N NH2 . ARG A 1 144 ? 1.056   -36.473 -68.700 1.00 57.29  ? 143 ARG A NH2 1 
ATOM 1053 N N   . ASP A 1 145 ? 1.714   -30.423 -62.740 1.00 44.74  ? 144 ASP A N   1 
ATOM 1054 C CA  . ASP A 1 145 ? 2.821   -29.494 -62.515 1.00 43.97  ? 144 ASP A CA  1 
ATOM 1055 C C   . ASP A 1 145 ? 3.340   -29.715 -61.099 1.00 51.96  ? 144 ASP A C   1 
ATOM 1056 O O   . ASP A 1 145 ? 2.909   -29.063 -60.145 1.00 51.39  ? 144 ASP A O   1 
ATOM 1057 C CB  . ASP A 1 145 ? 2.368   -28.055 -62.735 1.00 38.17  ? 144 ASP A CB  1 
ATOM 1058 C CG  . ASP A 1 145 ? 3.529   -27.081 -62.813 1.00 48.05  ? 144 ASP A CG  1 
ATOM 1059 O OD1 . ASP A 1 145 ? 4.693   -27.534 -62.861 1.00 50.80  ? 144 ASP A OD1 1 
ATOM 1060 O OD2 . ASP A 1 145 ? 3.276   -25.858 -62.825 1.00 51.66  ? 144 ASP A OD2 1 
ATOM 1061 N N   . ALA A 1 146 ? 4.280   -30.654 -60.960 1.00 47.86  ? 145 ALA A N   1 
ATOM 1062 C CA  . ALA A 1 146 ? 4.828   -30.961 -59.642 1.00 45.36  ? 145 ALA A CA  1 
ATOM 1063 C C   . ALA A 1 146 ? 5.707   -29.829 -59.126 1.00 47.68  ? 145 ALA A C   1 
ATOM 1064 O O   . ALA A 1 146 ? 5.712   -29.540 -57.924 1.00 53.62  ? 145 ALA A O   1 
ATOM 1065 C CB  . ALA A 1 146 ? 5.613   -32.271 -59.693 1.00 44.44  ? 145 ALA A CB  1 
ATOM 1066 N N   . ALA A 1 147 ? 6.460   -29.178 -60.016 1.00 48.84  ? 146 ALA A N   1 
ATOM 1067 C CA  . ALA A 1 147 ? 7.343   -28.099 -59.584 1.00 48.05  ? 146 ALA A CA  1 
ATOM 1068 C C   . ALA A 1 147 ? 6.550   -26.871 -59.154 1.00 46.99  ? 146 ALA A C   1 
ATOM 1069 O O   . ALA A 1 147 ? 6.899   -26.216 -58.166 1.00 47.51  ? 146 ALA A O   1 
ATOM 1070 C CB  . ALA A 1 147 ? 8.323   -27.739 -60.700 1.00 48.82  ? 146 ALA A CB  1 
ATOM 1071 N N   . GLY A 1 148 ? 5.486   -26.539 -59.887 1.00 49.84  ? 147 GLY A N   1 
ATOM 1072 C CA  . GLY A 1 148 ? 4.679   -25.390 -59.514 1.00 50.58  ? 147 GLY A CA  1 
ATOM 1073 C C   . GLY A 1 148 ? 3.996   -25.573 -58.173 1.00 48.43  ? 147 GLY A C   1 
ATOM 1074 O O   . GLY A 1 148 ? 3.905   -24.634 -57.378 1.00 49.01  ? 147 GLY A O   1 
ATOM 1075 N N   . ASN A 1 149 ? 3.514   -26.786 -57.900 1.00 48.28  ? 148 ASN A N   1 
ATOM 1076 C CA  . ASN A 1 149 ? 2.863   -27.055 -56.623 1.00 45.57  ? 148 ASN A CA  1 
ATOM 1077 C C   . ASN A 1 149 ? 3.875   -27.078 -55.485 1.00 42.36  ? 148 ASN A C   1 
ATOM 1078 O O   . ASN A 1 149 ? 3.618   -26.533 -54.406 1.00 39.62  ? 148 ASN A O   1 
ATOM 1079 C CB  . ASN A 1 149 ? 2.103   -28.379 -56.700 1.00 42.92  ? 148 ASN A CB  1 
ATOM 1080 C CG  . ASN A 1 149 ? 1.287   -28.656 -55.458 1.00 44.22  ? 148 ASN A CG  1 
ATOM 1081 O OD1 . ASN A 1 149 ? 0.356   -27.919 -55.138 1.00 43.46  ? 148 ASN A OD1 1 
ATOM 1082 N ND2 . ASN A 1 149 ? 1.626   -29.731 -54.755 1.00 48.72  ? 148 ASN A ND2 1 
ATOM 1083 N N   . ALA A 1 150 ? 5.036   -27.697 -55.713 1.00 40.73  ? 149 ALA A N   1 
ATOM 1084 C CA  . ALA A 1 150 ? 6.054   -27.774 -54.671 1.00 42.25  ? 149 ALA A CA  1 
ATOM 1085 C C   . ALA A 1 150 ? 6.616   -26.397 -54.339 1.00 46.84  ? 149 ALA A C   1 
ATOM 1086 O O   . ALA A 1 150 ? 6.771   -26.053 -53.161 1.00 49.94  ? 149 ALA A O   1 
ATOM 1087 C CB  . ALA A 1 150 ? 7.172   -28.723 -55.103 1.00 46.87  ? 149 ALA A CB  1 
ATOM 1088 N N   . LEU A 1 151 ? 6.925   -25.595 -55.361 1.00 44.79  ? 150 LEU A N   1 
ATOM 1089 C CA  . LEU A 1 151 ? 7.485   -24.268 -55.120 1.00 45.06  ? 150 LEU A CA  1 
ATOM 1090 C C   . LEU A 1 151 ? 6.496   -23.356 -54.405 1.00 46.87  ? 150 LEU A C   1 
ATOM 1091 O O   . LEU A 1 151 ? 6.904   -22.516 -53.595 1.00 45.51  ? 150 LEU A O   1 
ATOM 1092 C CB  . LEU A 1 151 ? 7.927   -23.630 -56.437 1.00 46.34  ? 150 LEU A CB  1 
ATOM 1093 C CG  . LEU A 1 151 ? 9.410   -23.740 -56.796 1.00 44.66  ? 150 LEU A CG  1 
ATOM 1094 C CD1 . LEU A 1 151 ? 10.242  -22.809 -55.926 1.00 48.76  ? 150 LEU A CD1 1 
ATOM 1095 C CD2 . LEU A 1 151 ? 9.894   -25.173 -56.666 1.00 47.66  ? 150 LEU A CD2 1 
ATOM 1096 N N   . SER A 1 152 ? 5.200   -23.502 -54.692 1.00 48.01  ? 151 SER A N   1 
ATOM 1097 C CA  . SER A 1 152 ? 4.197   -22.692 -54.009 1.00 46.58  ? 151 SER A CA  1 
ATOM 1098 C C   . SER A 1 152 ? 4.090   -23.067 -52.537 1.00 46.05  ? 151 SER A C   1 
ATOM 1099 O O   . SER A 1 152 ? 3.889   -22.196 -51.683 1.00 50.49  ? 151 SER A O   1 
ATOM 1100 C CB  . SER A 1 152 ? 2.841   -22.840 -54.700 1.00 44.26  ? 151 SER A CB  1 
ATOM 1101 O OG  . SER A 1 152 ? 2.925   -22.499 -56.072 1.00 48.31  ? 151 SER A OG  1 
ATOM 1102 N N   . LEU A 1 153 ? 4.219   -24.356 -52.218 1.00 45.65  ? 152 LEU A N   1 
ATOM 1103 C CA  . LEU A 1 153 ? 4.127   -24.780 -50.825 1.00 42.64  ? 152 LEU A CA  1 
ATOM 1104 C C   . LEU A 1 153 ? 5.376   -24.390 -50.045 1.00 48.06  ? 152 LEU A C   1 
ATOM 1105 O O   . LEU A 1 153 ? 5.289   -24.032 -48.864 1.00 49.76  ? 152 LEU A O   1 
ATOM 1106 C CB  . LEU A 1 153 ? 3.890   -26.290 -50.749 1.00 42.07  ? 152 LEU A CB  1 
ATOM 1107 C CG  . LEU A 1 153 ? 2.563   -26.805 -51.316 1.00 41.45  ? 152 LEU A CG  1 
ATOM 1108 C CD1 . LEU A 1 153 ? 2.479   -28.319 -51.216 1.00 37.89  ? 152 LEU A CD1 1 
ATOM 1109 C CD2 . LEU A 1 153 ? 1.382   -26.153 -50.612 1.00 37.50  ? 152 LEU A CD2 1 
ATOM 1110 N N   . ILE A 1 154 ? 6.545   -24.446 -50.687 1.00 47.84  ? 153 ILE A N   1 
ATOM 1111 C CA  . ILE A 1 154 ? 7.788   -24.106 -49.999 1.00 50.70  ? 153 ILE A CA  1 
ATOM 1112 C C   . ILE A 1 154 ? 7.834   -22.615 -49.688 1.00 49.06  ? 153 ILE A C   1 
ATOM 1113 O O   . ILE A 1 154 ? 8.119   -22.210 -48.555 1.00 53.11  ? 153 ILE A O   1 
ATOM 1114 C CB  . ILE A 1 154 ? 9.002   -24.550 -50.836 1.00 45.47  ? 153 ILE A CB  1 
ATOM 1115 C CG1 . ILE A 1 154 ? 9.087   -26.075 -50.882 1.00 45.46  ? 153 ILE A CG1 1 
ATOM 1116 C CG2 . ILE A 1 154 ? 10.287  -23.974 -50.260 1.00 35.97  ? 153 ILE A CG2 1 
ATOM 1117 C CD1 . ILE A 1 154 ? 10.019  -26.601 -51.950 1.00 51.10  ? 153 ILE A CD1 1 
ATOM 1118 N N   . VAL A 1 155 ? 7.552   -21.775 -50.688 1.00 48.78  ? 154 VAL A N   1 
ATOM 1119 C CA  . VAL A 1 155 ? 7.536   -20.332 -50.460 1.00 46.16  ? 154 VAL A CA  1 
ATOM 1120 C C   . VAL A 1 155 ? 6.449   -19.965 -49.457 1.00 46.61  ? 154 VAL A C   1 
ATOM 1121 O O   . VAL A 1 155 ? 6.659   -19.128 -48.572 1.00 47.61  ? 154 VAL A O   1 
ATOM 1122 C CB  . VAL A 1 155 ? 7.360   -19.580 -51.793 1.00 44.88  ? 154 VAL A CB  1 
ATOM 1123 C CG1 . VAL A 1 155 ? 7.219   -18.085 -51.550 1.00 45.70  ? 154 VAL A CG1 1 
ATOM 1124 C CG2 . VAL A 1 155 ? 8.532   -19.859 -52.716 1.00 44.52  ? 154 VAL A CG2 1 
ATOM 1125 N N   . GLY A 1 156 ? 5.277   -20.597 -49.567 1.00 45.16  ? 155 GLY A N   1 
ATOM 1126 C CA  . GLY A 1 156 ? 4.199   -20.311 -48.636 1.00 48.59  ? 155 GLY A CA  1 
ATOM 1127 C C   . GLY A 1 156 ? 4.500   -20.755 -47.218 1.00 50.67  ? 155 GLY A C   1 
ATOM 1128 O O   . GLY A 1 156 ? 3.973   -20.180 -46.260 1.00 48.10  ? 155 GLY A O   1 
ATOM 1129 N N   . SER A 1 157 ? 5.341   -21.780 -47.064 1.00 49.10  ? 156 SER A N   1 
ATOM 1130 C CA  . SER A 1 157 ? 5.752   -22.239 -45.744 1.00 47.63  ? 156 SER A CA  1 
ATOM 1131 C C   . SER A 1 157 ? 6.769   -21.303 -45.106 1.00 51.65  ? 156 SER A C   1 
ATOM 1132 O O   . SER A 1 157 ? 6.803   -21.175 -43.877 1.00 51.09  ? 156 SER A O   1 
ATOM 1133 C CB  . SER A 1 157 ? 6.337   -23.649 -45.836 1.00 44.41  ? 156 SER A CB  1 
ATOM 1134 O OG  . SER A 1 157 ? 5.396   -24.560 -46.374 1.00 45.86  ? 156 SER A OG  1 
ATOM 1135 N N   . LEU A 1 158 ? 7.603   -20.649 -45.916 1.00 52.48  ? 157 LEU A N   1 
ATOM 1136 C CA  . LEU A 1 158 ? 8.587   -19.721 -45.368 1.00 58.37  ? 157 LEU A CA  1 
ATOM 1137 C C   . LEU A 1 158 ? 7.920   -18.436 -44.892 1.00 58.36  ? 157 LEU A C   1 
ATOM 1138 O O   . LEU A 1 158 ? 8.169   -17.973 -43.772 1.00 57.94  ? 157 LEU A O   1 
ATOM 1139 C CB  . LEU A 1 158 ? 9.661   -19.424 -46.414 1.00 57.99  ? 157 LEU A CB  1 
ATOM 1140 C CG  . LEU A 1 158 ? 10.467  -20.633 -46.892 1.00 50.56  ? 157 LEU A CG  1 
ATOM 1141 C CD1 . LEU A 1 158 ? 11.437  -20.233 -47.992 1.00 51.64  ? 157 LEU A CD1 1 
ATOM 1142 C CD2 . LEU A 1 158 ? 11.203  -21.287 -45.734 1.00 51.67  ? 157 LEU A CD2 1 
ATOM 1143 N N   . ILE A 1 159 ? 7.063   -17.846 -45.729 1.00 50.34  ? 158 ILE A N   1 
ATOM 1144 C CA  . ILE A 1 159 ? 6.346   -16.644 -45.325 1.00 47.16  ? 158 ILE A CA  1 
ATOM 1145 C C   . ILE A 1 159 ? 5.287   -16.953 -44.279 1.00 48.08  ? 158 ILE A C   1 
ATOM 1146 O O   . ILE A 1 159 ? 4.841   -16.046 -43.568 1.00 48.03  ? 158 ILE A O   1 
ATOM 1147 C CB  . ILE A 1 159 ? 5.706   -15.950 -46.541 1.00 50.73  ? 158 ILE A CB  1 
ATOM 1148 C CG1 . ILE A 1 159 ? 4.779   -16.917 -47.281 1.00 48.11  ? 158 ILE A CG1 1 
ATOM 1149 C CG2 . ILE A 1 159 ? 6.782   -15.410 -47.470 1.00 50.92  ? 158 ILE A CG2 1 
ATOM 1150 C CD1 . ILE A 1 159 ? 4.469   -16.506 -48.707 1.00 49.92  ? 158 ILE A CD1 1 
ATOM 1151 N N   . GLY A 1 160 ? 4.860   -18.213 -44.172 1.00 49.29  ? 159 GLY A N   1 
ATOM 1152 C CA  . GLY A 1 160 ? 3.935   -18.579 -43.113 1.00 49.43  ? 159 GLY A CA  1 
ATOM 1153 C C   . GLY A 1 160 ? 4.601   -18.597 -41.751 1.00 51.47  ? 159 GLY A C   1 
ATOM 1154 O O   . GLY A 1 160 ? 3.987   -18.235 -40.743 1.00 57.21  ? 159 GLY A O   1 
ATOM 1155 N N   . VAL A 1 161 ? 5.866   -19.018 -41.700 1.00 47.10  ? 160 VAL A N   1 
ATOM 1156 C CA  . VAL A 1 161 ? 6.614   -18.962 -40.450 1.00 45.58  ? 160 VAL A CA  1 
ATOM 1157 C C   . VAL A 1 161 ? 6.917   -17.516 -40.081 1.00 51.12  ? 160 VAL A C   1 
ATOM 1158 O O   . VAL A 1 161 ? 6.793   -17.119 -38.916 1.00 50.96  ? 160 VAL A O   1 
ATOM 1159 C CB  . VAL A 1 161 ? 7.898   -19.802 -40.558 1.00 43.40  ? 160 VAL A CB  1 
ATOM 1160 C CG1 . VAL A 1 161 ? 8.825   -19.513 -39.388 1.00 45.49  ? 160 VAL A CG1 1 
ATOM 1161 C CG2 . VAL A 1 161 ? 7.554   -21.277 -40.615 1.00 46.37  ? 160 VAL A CG2 1 
ATOM 1162 N N   . LEU A 1 162 ? 7.314   -16.706 -41.065 1.00 46.39  ? 161 LEU A N   1 
ATOM 1163 C CA  . LEU A 1 162 ? 7.557   -15.292 -40.804 1.00 42.03  ? 161 LEU A CA  1 
ATOM 1164 C C   . LEU A 1 162 ? 6.285   -14.593 -40.341 1.00 42.79  ? 161 LEU A C   1 
ATOM 1165 O O   . LEU A 1 162 ? 6.331   -13.723 -39.463 1.00 51.09  ? 161 LEU A O   1 
ATOM 1166 C CB  . LEU A 1 162 ? 8.117   -14.615 -42.056 1.00 49.06  ? 161 LEU A CB  1 
ATOM 1167 C CG  . LEU A 1 162 ? 8.172   -13.085 -42.041 1.00 49.51  ? 161 LEU A CG  1 
ATOM 1168 C CD1 . LEU A 1 162 ? 9.364   -12.593 -41.231 1.00 45.53  ? 161 LEU A CD1 1 
ATOM 1169 C CD2 . LEU A 1 162 ? 8.213   -12.530 -43.457 1.00 44.72  ? 161 LEU A CD2 1 
ATOM 1170 N N   . ALA A 1 163 ? 5.138   -14.967 -40.911 1.00 42.81  ? 162 ALA A N   1 
ATOM 1171 C CA  . ALA A 1 163 ? 3.883   -14.340 -40.508 1.00 46.01  ? 162 ALA A CA  1 
ATOM 1172 C C   . ALA A 1 163 ? 3.482   -14.761 -39.101 1.00 48.87  ? 162 ALA A C   1 
ATOM 1173 O O   . ALA A 1 163 ? 2.969   -13.944 -38.327 1.00 51.18  ? 162 ALA A O   1 
ATOM 1174 C CB  . ALA A 1 163 ? 2.776   -14.682 -41.500 1.00 42.75  ? 162 ALA A CB  1 
ATOM 1175 N N   . TYR A 1 164 ? 3.697   -16.032 -38.755 1.00 48.21  ? 163 TYR A N   1 
ATOM 1176 C CA  . TYR A 1 164 ? 3.414   -16.473 -37.394 1.00 47.50  ? 163 TYR A CA  1 
ATOM 1177 C C   . TYR A 1 164 ? 4.280   -15.719 -36.393 1.00 47.31  ? 163 TYR A C   1 
ATOM 1178 O O   . TYR A 1 164 ? 3.782   -15.216 -35.381 1.00 49.07  ? 163 TYR A O   1 
ATOM 1179 C CB  . TYR A 1 164 ? 3.633   -17.982 -37.266 1.00 44.91  ? 163 TYR A CB  1 
ATOM 1180 C CG  . TYR A 1 164 ? 3.867   -18.417 -35.839 1.00 45.36  ? 163 TYR A CG  1 
ATOM 1181 C CD1 . TYR A 1 164 ? 2.813   -18.509 -34.940 1.00 45.33  ? 163 TYR A CD1 1 
ATOM 1182 C CD2 . TYR A 1 164 ? 5.145   -18.708 -35.383 1.00 47.59  ? 163 TYR A CD2 1 
ATOM 1183 C CE1 . TYR A 1 164 ? 3.024   -18.894 -33.631 1.00 46.94  ? 163 TYR A CE1 1 
ATOM 1184 C CE2 . TYR A 1 164 ? 5.366   -19.091 -34.075 1.00 50.92  ? 163 TYR A CE2 1 
ATOM 1185 C CZ  . TYR A 1 164 ? 4.303   -19.183 -33.203 1.00 52.82  ? 163 TYR A CZ  1 
ATOM 1186 O OH  . TYR A 1 164 ? 4.522   -19.564 -31.897 1.00 60.00  ? 163 TYR A OH  1 
ATOM 1187 N N   . TYR A 1 165 ? 5.583   -15.620 -36.672 1.00 46.68  ? 164 TYR A N   1 
ATOM 1188 C CA  . TYR A 1 165 ? 6.491   -14.936 -35.756 1.00 45.89  ? 164 TYR A CA  1 
ATOM 1189 C C   . TYR A 1 165 ? 6.139   -13.460 -35.623 1.00 49.39  ? 164 TYR A C   1 
ATOM 1190 O O   . TYR A 1 165 ? 6.239   -12.885 -34.532 1.00 46.54  ? 164 TYR A O   1 
ATOM 1191 C CB  . TYR A 1 165 ? 7.934   -15.101 -36.231 1.00 45.13  ? 164 TYR A CB  1 
ATOM 1192 C CG  . TYR A 1 165 ? 8.969   -14.764 -35.183 1.00 51.77  ? 164 TYR A CG  1 
ATOM 1193 C CD1 . TYR A 1 165 ? 8.998   -15.431 -33.965 1.00 53.35  ? 164 TYR A CD1 1 
ATOM 1194 C CD2 . TYR A 1 165 ? 9.913   -13.773 -35.409 1.00 54.68  ? 164 TYR A CD2 1 
ATOM 1195 C CE1 . TYR A 1 165 ? 9.945   -15.124 -33.005 1.00 54.48  ? 164 TYR A CE1 1 
ATOM 1196 C CE2 . TYR A 1 165 ? 10.860  -13.457 -34.456 1.00 52.72  ? 164 TYR A CE2 1 
ATOM 1197 C CZ  . TYR A 1 165 ? 10.873  -14.134 -33.258 1.00 57.34  ? 164 TYR A CZ  1 
ATOM 1198 O OH  . TYR A 1 165 ? 11.820  -13.816 -32.312 1.00 67.97  ? 164 TYR A OH  1 
ATOM 1199 N N   . VAL A 1 166 ? 5.726   -12.827 -36.722 1.00 47.55  ? 165 VAL A N   1 
ATOM 1200 C CA  . VAL A 1 166 ? 5.320   -11.426 -36.666 1.00 46.34  ? 165 VAL A CA  1 
ATOM 1201 C C   . VAL A 1 166 ? 4.037   -11.278 -35.856 1.00 51.33  ? 165 VAL A C   1 
ATOM 1202 O O   . VAL A 1 166 ? 3.931   -10.406 -34.985 1.00 53.57  ? 165 VAL A O   1 
ATOM 1203 C CB  . VAL A 1 166 ? 5.166   -10.857 -38.089 1.00 49.77  ? 165 VAL A CB  1 
ATOM 1204 C CG1 . VAL A 1 166 ? 4.177   -9.700  -38.109 1.00 43.00  ? 165 VAL A CG1 1 
ATOM 1205 C CG2 . VAL A 1 166 ? 6.519   -10.411 -38.630 1.00 41.61  ? 165 VAL A CG2 1 
ATOM 1206 N N   . SER A 1 167 ? 3.051   -12.140 -36.116 1.00 55.91  ? 166 SER A N   1 
ATOM 1207 C CA  . SER A 1 167 ? 1.774   -12.037 -35.418 1.00 57.97  ? 166 SER A CA  1 
ATOM 1208 C C   . SER A 1 167 ? 1.899   -12.452 -33.956 1.00 58.34  ? 166 SER A C   1 
ATOM 1209 O O   . SER A 1 167 ? 1.240   -11.873 -33.085 1.00 58.85  ? 166 SER A O   1 
ATOM 1210 C CB  . SER A 1 167 ? 0.721   -12.890 -36.123 1.00 58.99  ? 166 SER A CB  1 
ATOM 1211 O OG  . SER A 1 167 ? 1.073   -14.261 -36.076 1.00 55.07  ? 166 SER A OG  1 
ATOM 1212 N N   . TYR A 1 168 ? 2.731   -13.458 -33.667 1.00 53.09  ? 167 TYR A N   1 
ATOM 1213 C CA  . TYR A 1 168 ? 2.898   -13.901 -32.285 1.00 51.61  ? 167 TYR A CA  1 
ATOM 1214 C C   . TYR A 1 168 ? 3.665   -12.872 -31.465 1.00 50.96  ? 167 TYR A C   1 
ATOM 1215 O O   . TYR A 1 168 ? 3.297   -12.586 -30.320 1.00 56.97  ? 167 TYR A O   1 
ATOM 1216 C CB  . TYR A 1 168 ? 3.603   -15.259 -32.240 1.00 51.12  ? 167 TYR A CB  1 
ATOM 1217 C CG  . TYR A 1 168 ? 4.596   -15.422 -31.104 1.00 54.00  ? 167 TYR A CG  1 
ATOM 1218 C CD1 . TYR A 1 168 ? 4.165   -15.642 -29.799 1.00 58.05  ? 167 TYR A CD1 1 
ATOM 1219 C CD2 . TYR A 1 168 ? 5.964   -15.363 -31.339 1.00 54.94  ? 167 TYR A CD2 1 
ATOM 1220 C CE1 . TYR A 1 168 ? 5.071   -15.793 -28.760 1.00 58.59  ? 167 TYR A CE1 1 
ATOM 1221 C CE2 . TYR A 1 168 ? 6.877   -15.513 -30.306 1.00 57.15  ? 167 TYR A CE2 1 
ATOM 1222 C CZ  . TYR A 1 168 ? 6.425   -15.728 -29.020 1.00 58.95  ? 167 TYR A CZ  1 
ATOM 1223 O OH  . TYR A 1 168 ? 7.327   -15.877 -27.989 1.00 60.79  ? 167 TYR A OH  1 
ATOM 1224 N N   . ARG A 1 169 ? 4.732   -12.305 -32.026 1.00 51.47  ? 168 ARG A N   1 
ATOM 1225 C CA  . ARG A 1 169 ? 5.490   -11.307 -31.281 1.00 55.49  ? 168 ARG A CA  1 
ATOM 1226 C C   . ARG A 1 169 ? 4.741   -9.990  -31.135 1.00 61.77  ? 168 ARG A C   1 
ATOM 1227 O O   . ARG A 1 169 ? 5.128   -9.168  -30.298 1.00 62.46  ? 168 ARG A O   1 
ATOM 1228 C CB  . ARG A 1 169 ? 6.845   -11.071 -31.948 1.00 51.94  ? 168 ARG A CB  1 
ATOM 1229 C CG  . ARG A 1 169 ? 7.946   -11.970 -31.413 1.00 53.80  ? 168 ARG A CG  1 
ATOM 1230 C CD  . ARG A 1 169 ? 8.594   -11.368 -30.179 1.00 54.99  ? 168 ARG A CD  1 
ATOM 1231 N NE  . ARG A 1 169 ? 9.729   -10.524 -30.526 1.00 62.28  ? 168 ARG A NE  1 
ATOM 1232 C CZ  . ARG A 1 169 ? 10.948  -10.979 -30.780 1.00 65.94  ? 168 ARG A CZ  1 
ATOM 1233 N NH1 . ARG A 1 169 ? 11.229  -12.271 -30.722 1.00 58.61  ? 168 ARG A NH1 1 
ATOM 1234 N NH2 . ARG A 1 169 ? 11.909  -10.117 -31.100 1.00 71.57  ? 168 ARG A NH2 1 
ATOM 1235 N N   . LEU A 1 170 ? 3.677   -9.778  -31.911 1.00 57.50  ? 169 LEU A N   1 
ATOM 1236 C CA  . LEU A 1 170 ? 2.872   -8.565  -31.842 1.00 56.41  ? 169 LEU A CA  1 
ATOM 1237 C C   . LEU A 1 170 ? 1.594   -8.756  -31.032 1.00 56.20  ? 169 LEU A C   1 
ATOM 1238 O O   . LEU A 1 170 ? 1.360   -8.026  -30.065 1.00 52.83  ? 169 LEU A O   1 
ATOM 1239 C CB  . LEU A 1 170 ? 2.530   -8.089  -33.259 1.00 56.01  ? 169 LEU A CB  1 
ATOM 1240 C CG  . LEU A 1 170 ? 3.381   -6.958  -33.841 1.00 52.84  ? 169 LEU A CG  1 
ATOM 1241 C CD1 . LEU A 1 170 ? 4.845   -7.365  -33.939 1.00 47.14  ? 169 LEU A CD1 1 
ATOM 1242 C CD2 . LEU A 1 170 ? 2.844   -6.558  -35.204 1.00 47.79  ? 169 LEU A CD2 1 
ATOM 1243 N N   . GLY A 1 171 ? 0.764   -9.729  -31.402 1.00 54.69  ? 170 GLY A N   1 
ATOM 1244 C CA  . GLY A 1 171 ? -0.499  -9.947  -30.722 1.00 49.74  ? 170 GLY A CA  1 
ATOM 1245 C C   . GLY A 1 171 ? -0.448  -10.986 -29.620 1.00 50.79  ? 170 GLY A C   1 
ATOM 1246 O O   . GLY A 1 171 ? -1.379  -11.091 -28.817 1.00 55.81  ? 170 GLY A O   1 
ATOM 1247 N N   . GLY A 1 172 ? 0.624   -11.767 -29.577 1.00 49.21  ? 171 GLY A N   1 
ATOM 1248 C CA  . GLY A 1 172 ? 0.780   -12.746 -28.511 1.00 47.14  ? 171 GLY A CA  1 
ATOM 1249 C C   . GLY A 1 172 ? 0.040   -14.030 -28.810 1.00 53.40  ? 171 GLY A C   1 
ATOM 1250 O O   . GLY A 1 172 ? 0.199   -14.619 -29.884 1.00 57.76  ? 171 GLY A O   1 
ATOM 1251 N N   . TYR A 1 173 ? -0.773  -14.477 -27.848 1.00 50.77  ? 172 TYR A N   1 
ATOM 1252 C CA  . TYR A 1 173 ? -1.482  -15.745 -28.002 1.00 47.19  ? 172 TYR A CA  1 
ATOM 1253 C C   . TYR A 1 173 ? -2.510  -15.668 -29.124 1.00 48.77  ? 172 TYR A C   1 
ATOM 1254 O O   . TYR A 1 173 ? -2.546  -16.536 -30.003 1.00 51.69  ? 172 TYR A O   1 
ATOM 1255 C CB  . TYR A 1 173 ? -2.150  -16.142 -26.685 1.00 46.68  ? 172 TYR A CB  1 
ATOM 1256 C CG  . TYR A 1 173 ? -2.710  -17.546 -26.687 1.00 45.04  ? 172 TYR A CG  1 
ATOM 1257 C CD1 . TYR A 1 173 ? -1.876  -18.646 -26.849 1.00 46.42  ? 172 TYR A CD1 1 
ATOM 1258 C CD2 . TYR A 1 173 ? -4.072  -17.774 -26.530 1.00 44.66  ? 172 TYR A CD2 1 
ATOM 1259 C CE1 . TYR A 1 173 ? -2.383  -19.933 -26.854 1.00 46.45  ? 172 TYR A CE1 1 
ATOM 1260 C CE2 . TYR A 1 173 ? -4.588  -19.059 -26.533 1.00 44.30  ? 172 TYR A CE2 1 
ATOM 1261 C CZ  . TYR A 1 173 ? -3.738  -20.132 -26.695 1.00 44.41  ? 172 TYR A CZ  1 
ATOM 1262 O OH  . TYR A 1 173 ? -4.243  -21.410 -26.700 1.00 46.28  ? 172 TYR A OH  1 
ATOM 1263 N N   . GLU A 1 174 ? -3.358  -14.635 -29.111 1.00 48.87  ? 173 GLU A N   1 
ATOM 1264 C CA  . GLU A 1 174 ? -4.303  -14.455 -30.208 1.00 48.91  ? 173 GLU A CA  1 
ATOM 1265 C C   . GLU A 1 174 ? -3.583  -14.193 -31.523 1.00 47.12  ? 173 GLU A C   1 
ATOM 1266 O O   . GLU A 1 174 ? -4.086  -14.559 -32.592 1.00 47.22  ? 173 GLU A O   1 
ATOM 1267 C CB  . GLU A 1 174 ? -5.274  -13.316 -29.894 1.00 44.55  ? 173 GLU A CB  1 
ATOM 1268 C CG  . GLU A 1 174 ? -6.484  -13.745 -29.078 1.00 49.04  ? 173 GLU A CG  1 
ATOM 1269 C CD  . GLU A 1 174 ? -7.452  -12.607 -28.815 1.00 56.41  ? 173 GLU A CD  1 
ATOM 1270 O OE1 . GLU A 1 174 ? -7.923  -11.983 -29.790 1.00 55.50  ? 173 GLU A OE1 1 
ATOM 1271 O OE2 . GLU A 1 174 ? -7.744  -12.336 -27.630 1.00 61.89  ? 173 GLU A OE2 1 
ATOM 1272 N N   . GLY A 1 175 ? -2.409  -13.562 -31.469 1.00 49.39  ? 174 GLY A N   1 
ATOM 1273 C CA  . GLY A 1 175 ? -1.618  -13.397 -32.676 1.00 46.88  ? 174 GLY A CA  1 
ATOM 1274 C C   . GLY A 1 175 ? -1.032  -14.707 -33.163 1.00 49.50  ? 174 GLY A C   1 
ATOM 1275 O O   . GLY A 1 175 ? -0.972  -14.961 -34.369 1.00 53.89  ? 174 GLY A O   1 
ATOM 1276 N N   . ALA A 1 176 ? -0.593  -15.560 -32.233 1.00 48.27  ? 175 ALA A N   1 
ATOM 1277 C CA  . ALA A 1 176 ? -0.091  -16.873 -32.618 1.00 43.93  ? 175 ALA A CA  1 
ATOM 1278 C C   . ALA A 1 176 ? -1.196  -17.746 -33.196 1.00 43.81  ? 175 ALA A C   1 
ATOM 1279 O O   . ALA A 1 176 ? -0.935  -18.575 -34.074 1.00 47.26  ? 175 ALA A O   1 
ATOM 1280 C CB  . ALA A 1 176 ? 0.561   -17.562 -31.421 1.00 45.99  ? 175 ALA A CB  1 
ATOM 1281 N N   . LEU A 1 177 ? -2.430  -17.580 -32.717 1.00 43.26  ? 176 LEU A N   1 
ATOM 1282 C CA  . LEU A 1 177 ? -3.548  -18.297 -33.317 1.00 42.67  ? 176 LEU A CA  1 
ATOM 1283 C C   . LEU A 1 177 ? -3.822  -17.792 -34.728 1.00 46.79  ? 176 LEU A C   1 
ATOM 1284 O O   . LEU A 1 177 ? -4.031  -18.590 -35.649 1.00 51.44  ? 176 LEU A O   1 
ATOM 1285 C CB  . LEU A 1 177 ? -4.791  -18.164 -32.438 1.00 41.48  ? 176 LEU A CB  1 
ATOM 1286 C CG  . LEU A 1 177 ? -4.648  -18.657 -30.995 1.00 38.24  ? 176 LEU A CG  1 
ATOM 1287 C CD1 . LEU A 1 177 ? -5.992  -18.660 -30.284 1.00 40.44  ? 176 LEU A CD1 1 
ATOM 1288 C CD2 . LEU A 1 177 ? -4.006  -20.038 -30.943 1.00 38.52  ? 176 LEU A CD2 1 
ATOM 1289 N N   . LEU A 1 178 ? -3.813  -16.469 -34.918 1.00 44.70  ? 177 LEU A N   1 
ATOM 1290 C CA  . LEU A 1 178 ? -3.989  -15.913 -36.255 1.00 44.36  ? 177 LEU A CA  1 
ATOM 1291 C C   . LEU A 1 178 ? -2.866  -16.355 -37.185 1.00 46.07  ? 177 LEU A C   1 
ATOM 1292 O O   . LEU A 1 178 ? -3.099  -16.622 -38.370 1.00 47.83  ? 177 LEU A O   1 
ATOM 1293 C CB  . LEU A 1 178 ? -4.062  -14.387 -36.186 1.00 45.26  ? 177 LEU A CB  1 
ATOM 1294 C CG  . LEU A 1 178 ? -4.189  -13.649 -37.521 1.00 44.27  ? 177 LEU A CG  1 
ATOM 1295 C CD1 . LEU A 1 178 ? -5.610  -13.752 -38.051 1.00 48.34  ? 177 LEU A CD1 1 
ATOM 1296 C CD2 . LEU A 1 178 ? -3.773  -12.196 -37.376 1.00 38.53  ? 177 LEU A CD2 1 
ATOM 1297 N N   . GLY A 1 179 ? -1.641  -16.443 -36.664 1.00 43.37  ? 178 GLY A N   1 
ATOM 1298 C CA  . GLY A 1 179 ? -0.533  -16.912 -37.480 1.00 45.15  ? 178 GLY A CA  1 
ATOM 1299 C C   . GLY A 1 179 ? -0.671  -18.372 -37.864 1.00 48.74  ? 178 GLY A C   1 
ATOM 1300 O O   . GLY A 1 179 ? -0.317  -18.765 -38.979 1.00 48.61  ? 178 GLY A O   1 
ATOM 1301 N N   . LEU A 1 180 ? -1.187  -19.196 -36.948 1.00 46.54  ? 179 LEU A N   1 
ATOM 1302 C CA  . LEU A 1 180 ? -1.424  -20.598 -37.272 1.00 45.83  ? 179 LEU A CA  1 
ATOM 1303 C C   . LEU A 1 180 ? -2.478  -20.745 -38.361 1.00 48.29  ? 179 LEU A C   1 
ATOM 1304 O O   . LEU A 1 180 ? -2.385  -21.649 -39.200 1.00 44.86  ? 179 LEU A O   1 
ATOM 1305 C CB  . LEU A 1 180 ? -1.839  -21.363 -36.016 1.00 37.46  ? 179 LEU A CB  1 
ATOM 1306 C CG  . LEU A 1 180 ? -0.689  -21.883 -35.153 1.00 42.98  ? 179 LEU A CG  1 
ATOM 1307 C CD1 . LEU A 1 180 ? -1.131  -23.090 -34.350 1.00 52.87  ? 179 LEU A CD1 1 
ATOM 1308 C CD2 . LEU A 1 180 ? 0.515   -22.226 -36.011 1.00 40.69  ? 179 LEU A CD2 1 
ATOM 1309 N N   . ALA A 1 181 ? -3.480  -19.866 -38.368 1.00 44.87  ? 180 ALA A N   1 
ATOM 1310 C CA  . ALA A 1 181 ? -4.468  -19.875 -39.437 1.00 47.84  ? 180 ALA A CA  1 
ATOM 1311 C C   . ALA A 1 181 ? -3.920  -19.270 -40.723 1.00 47.58  ? 180 ALA A C   1 
ATOM 1312 O O   . ALA A 1 181 ? -4.361  -19.644 -41.815 1.00 46.97  ? 180 ALA A O   1 
ATOM 1313 C CB  . ALA A 1 181 ? -5.725  -19.125 -38.995 1.00 42.32  ? 180 ALA A CB  1 
ATOM 1314 N N   . LEU A 1 182 ? -2.960  -18.349 -40.621 1.00 46.17  ? 181 LEU A N   1 
ATOM 1315 C CA  . LEU A 1 182 ? -2.427  -17.687 -41.805 1.00 47.15  ? 181 LEU A CA  1 
ATOM 1316 C C   . LEU A 1 182 ? -1.436  -18.551 -42.573 1.00 45.03  ? 181 LEU A C   1 
ATOM 1317 O O   . LEU A 1 182 ? -1.195  -18.285 -43.754 1.00 51.02  ? 181 LEU A O   1 
ATOM 1318 C CB  . LEU A 1 182 ? -1.760  -16.367 -41.415 1.00 41.68  ? 181 LEU A CB  1 
ATOM 1319 C CG  . LEU A 1 182 ? -2.660  -15.131 -41.400 1.00 38.54  ? 181 LEU A CG  1 
ATOM 1320 C CD1 . LEU A 1 182 ? -1.888  -13.926 -40.895 1.00 40.14  ? 181 LEU A CD1 1 
ATOM 1321 C CD2 . LEU A 1 182 ? -3.232  -14.864 -42.778 1.00 43.03  ? 181 LEU A CD2 1 
ATOM 1322 N N   . ILE A 1 183 ? -0.857  -19.570 -41.932 1.00 46.02  ? 182 ILE A N   1 
ATOM 1323 C CA  . ILE A 1 183 ? 0.099   -20.433 -42.628 1.00 50.11  ? 182 ILE A CA  1 
ATOM 1324 C C   . ILE A 1 183 ? -0.535  -21.158 -43.810 1.00 51.10  ? 182 ILE A C   1 
ATOM 1325 O O   . ILE A 1 183 ? 0.045   -21.134 -44.905 1.00 50.26  ? 182 ILE A O   1 
ATOM 1326 C CB  . ILE A 1 183 ? 0.772   -21.392 -41.623 1.00 50.28  ? 182 ILE A CB  1 
ATOM 1327 C CG1 . ILE A 1 183 ? 1.751   -20.618 -40.734 1.00 45.51  ? 182 ILE A CG1 1 
ATOM 1328 C CG2 . ILE A 1 183 ? 1.458   -22.540 -42.349 1.00 48.04  ? 182 ILE A CG2 1 
ATOM 1329 C CD1 . ILE A 1 183 ? 2.057   -21.298 -39.414 1.00 40.84  ? 182 ILE A CD1 1 
ATOM 1330 N N   . PRO A 1 184 ? -1.707  -21.800 -43.676 1.00 48.64  ? 183 PRO A N   1 
ATOM 1331 C CA  . PRO A 1 184 ? -2.362  -22.353 -44.874 1.00 48.28  ? 183 PRO A CA  1 
ATOM 1332 C C   . PRO A 1 184 ? -2.971  -21.293 -45.770 1.00 48.01  ? 183 PRO A C   1 
ATOM 1333 O O   . PRO A 1 184 ? -3.278  -21.590 -46.932 1.00 48.82  ? 183 PRO A O   1 
ATOM 1334 C CB  . PRO A 1 184 ? -3.451  -23.269 -44.293 1.00 45.28  ? 183 PRO A CB  1 
ATOM 1335 C CG  . PRO A 1 184 ? -3.101  -23.440 -42.848 1.00 51.37  ? 183 PRO A CG  1 
ATOM 1336 C CD  . PRO A 1 184 ? -2.451  -22.160 -42.459 1.00 46.81  ? 183 PRO A CD  1 
ATOM 1337 N N   . ALA A 1 185 ? -3.163  -20.074 -45.271 1.00 45.68  ? 184 ALA A N   1 
ATOM 1338 C CA  . ALA A 1 185 ? -3.842  -19.038 -46.037 1.00 48.80  ? 184 ALA A CA  1 
ATOM 1339 C C   . ALA A 1 185 ? -2.896  -18.275 -46.951 1.00 50.13  ? 184 ALA A C   1 
ATOM 1340 O O   . ALA A 1 185 ? -3.290  -17.873 -48.051 1.00 50.81  ? 184 ALA A O   1 
ATOM 1341 C CB  . ALA A 1 185 ? -4.547  -18.062 -45.091 1.00 47.99  ? 184 ALA A CB  1 
ATOM 1342 N N   . LEU A 1 186 ? -1.653  -18.068 -46.523 1.00 50.29  ? 185 LEU A N   1 
ATOM 1343 C CA  . LEU A 1 186 ? -0.710  -17.273 -47.298 1.00 51.63  ? 185 LEU A CA  1 
ATOM 1344 C C   . LEU A 1 186 ? -0.115  -18.028 -48.476 1.00 54.21  ? 185 LEU A C   1 
ATOM 1345 O O   . LEU A 1 186 ? 0.721   -17.463 -49.190 1.00 55.72  ? 185 LEU A O   1 
ATOM 1346 C CB  . LEU A 1 186 ? 0.411   -16.756 -46.396 1.00 45.89  ? 185 LEU A CB  1 
ATOM 1347 C CG  . LEU A 1 186 ? -0.037  -15.718 -45.369 1.00 41.36  ? 185 LEU A CG  1 
ATOM 1348 C CD1 . LEU A 1 186 ? 1.141   -15.268 -44.539 1.00 44.80  ? 185 LEU A CD1 1 
ATOM 1349 C CD2 . LEU A 1 186 ? -0.700  -14.536 -46.057 1.00 42.56  ? 185 LEU A CD2 1 
ATOM 1350 N N   . VAL A 1 187 ? -0.516  -19.282 -48.700 1.00 60.48  ? 186 VAL A N   1 
ATOM 1351 C CA  . VAL A 1 187 ? -0.079  -20.006 -49.887 1.00 55.67  ? 186 VAL A CA  1 
ATOM 1352 C C   . VAL A 1 187 ? -0.729  -19.472 -51.153 1.00 58.09  ? 186 VAL A C   1 
ATOM 1353 O O   . VAL A 1 187 ? -0.298  -19.820 -52.258 1.00 55.13  ? 186 VAL A O   1 
ATOM 1354 C CB  . VAL A 1 187 ? -0.373  -21.512 -49.725 1.00 53.85  ? 186 VAL A CB  1 
ATOM 1355 C CG1 . VAL A 1 187 ? -1.832  -21.811 -50.047 1.00 58.49  ? 186 VAL A CG1 1 
ATOM 1356 C CG2 . VAL A 1 187 ? 0.569   -22.343 -50.588 1.00 54.73  ? 186 VAL A CG2 1 
ATOM 1357 N N   . VAL A 1 188 ? -1.751  -18.622 -51.017 1.00 54.97  ? 187 VAL A N   1 
ATOM 1358 C CA  . VAL A 1 188 ? -2.429  -18.062 -52.178 1.00 50.67  ? 187 VAL A CA  1 
ATOM 1359 C C   . VAL A 1 188 ? -1.536  -17.095 -52.944 1.00 55.63  ? 187 VAL A C   1 
ATOM 1360 O O   . VAL A 1 188 ? -1.761  -16.864 -54.139 1.00 55.87  ? 187 VAL A O   1 
ATOM 1361 C CB  . VAL A 1 188 ? -3.738  -17.374 -51.742 1.00 46.79  ? 187 VAL A CB  1 
ATOM 1362 C CG1 . VAL A 1 188 ? -3.442  -16.061 -51.030 1.00 42.75  ? 187 VAL A CG1 1 
ATOM 1363 C CG2 . VAL A 1 188 ? -4.656  -17.153 -52.936 1.00 51.67  ? 187 VAL A CG2 1 
ATOM 1364 N N   . ILE A 1 189 ? -0.522  -16.527 -52.297 1.00 57.60  ? 188 ILE A N   1 
ATOM 1365 C CA  . ILE A 1 189 ? 0.383   -15.590 -52.960 1.00 58.95  ? 188 ILE A CA  1 
ATOM 1366 C C   . ILE A 1 189 ? 1.365   -16.349 -53.850 1.00 62.70  ? 188 ILE A C   1 
ATOM 1367 O O   . ILE A 1 189 ? 1.503   -15.994 -55.031 1.00 59.75  ? 188 ILE A O   1 
ATOM 1368 C CB  . ILE A 1 189 ? 1.107   -14.693 -51.941 1.00 48.54  ? 188 ILE A CB  1 
ATOM 1369 C CG1 . ILE A 1 189 ? 0.122   -13.701 -51.320 1.00 48.84  ? 188 ILE A CG1 1 
ATOM 1370 C CG2 . ILE A 1 189 ? 2.273   -13.963 -52.598 1.00 50.47  ? 188 ILE A CG2 1 
ATOM 1371 C CD1 . ILE A 1 189 ? -0.009  -12.404 -52.095 1.00 59.28  ? 188 ILE A CD1 1 
ATOM 1372 N N   . PRO A 1 190 ? 2.064   -17.386 -53.364 1.00 54.52  ? 189 PRO A N   1 
ATOM 1373 C CA  . PRO A 1 190 ? 2.937   -18.137 -54.279 1.00 52.42  ? 189 PRO A CA  1 
ATOM 1374 C C   . PRO A 1 190 ? 2.166   -18.937 -55.311 1.00 53.34  ? 189 PRO A C   1 
ATOM 1375 O O   . PRO A 1 190 ? 2.663   -19.126 -56.428 1.00 52.20  ? 189 PRO A O   1 
ATOM 1376 C CB  . PRO A 1 190 ? 3.732   -19.057 -53.339 1.00 51.18  ? 189 PRO A CB  1 
ATOM 1377 C CG  . PRO A 1 190 ? 3.566   -18.466 -51.982 1.00 52.30  ? 189 PRO A CG  1 
ATOM 1378 C CD  . PRO A 1 190 ? 2.193   -17.894 -51.988 1.00 51.57  ? 189 PRO A CD  1 
ATOM 1379 N N   . ALA A 1 191 ? 0.968   -19.417 -54.968 1.00 54.13  ? 190 ALA A N   1 
ATOM 1380 C CA  . ALA A 1 191 ? 0.180   -20.190 -55.921 1.00 51.07  ? 190 ALA A CA  1 
ATOM 1381 C C   . ALA A 1 191 ? -0.287  -19.322 -57.082 1.00 50.61  ? 190 ALA A C   1 
ATOM 1382 O O   . ALA A 1 191 ? -0.259  -19.758 -58.239 1.00 51.26  ? 190 ALA A O   1 
ATOM 1383 C CB  . ALA A 1 191 ? -1.014  -20.832 -55.217 1.00 47.07  ? 190 ALA A CB  1 
ATOM 1384 N N   . ALA A 1 192 ? -0.719  -18.092 -56.794 1.00 51.05  ? 191 ALA A N   1 
ATOM 1385 C CA  . ALA A 1 192 ? -1.143  -17.193 -57.862 1.00 50.96  ? 191 ALA A CA  1 
ATOM 1386 C C   . ALA A 1 192 ? 0.042   -16.742 -58.705 1.00 55.89  ? 191 ALA A C   1 
ATOM 1387 O O   . ALA A 1 192 ? -0.058  -16.663 -59.935 1.00 59.49  ? 191 ALA A O   1 
ATOM 1388 C CB  . ALA A 1 192 ? -1.875  -15.986 -57.277 1.00 46.32  ? 191 ALA A CB  1 
ATOM 1389 N N   . ILE A 1 193 ? 1.173   -16.443 -58.062 1.00 55.76  ? 192 ILE A N   1 
ATOM 1390 C CA  . ILE A 1 193 ? 2.357   -16.018 -58.801 1.00 51.41  ? 192 ILE A CA  1 
ATOM 1391 C C   . ILE A 1 193 ? 2.859   -17.147 -59.693 1.00 55.59  ? 192 ILE A C   1 
ATOM 1392 O O   . ILE A 1 193 ? 3.247   -16.922 -60.845 1.00 63.22  ? 192 ILE A O   1 
ATOM 1393 C CB  . ILE A 1 193 ? 3.442   -15.525 -57.824 1.00 51.45  ? 192 ILE A CB  1 
ATOM 1394 C CG1 . ILE A 1 193 ? 3.379   -14.002 -57.682 1.00 53.07  ? 192 ILE A CG1 1 
ATOM 1395 C CG2 . ILE A 1 193 ? 4.830   -15.958 -58.278 1.00 55.04  ? 192 ILE A CG2 1 
ATOM 1396 C CD1 . ILE A 1 193 ? 2.059   -13.485 -57.150 1.00 50.85  ? 192 ILE A CD1 1 
ATOM 1397 N N   . MET A 1 194 ? 2.838   -18.382 -59.185 1.00 60.31  ? 193 MET A N   1 
ATOM 1398 C CA  . MET A 1 194 ? 3.233   -19.529 -59.992 1.00 55.91  ? 193 MET A CA  1 
ATOM 1399 C C   . MET A 1 194 ? 2.212   -19.857 -61.071 1.00 64.41  ? 193 MET A C   1 
ATOM 1400 O O   . MET A 1 194 ? 2.563   -20.503 -62.063 1.00 72.53  ? 193 MET A O   1 
ATOM 1401 C CB  . MET A 1 194 ? 3.447   -20.753 -59.100 1.00 55.20  ? 193 MET A CB  1 
ATOM 1402 C CG  . MET A 1 194 ? 4.569   -21.668 -59.553 1.00 62.78  ? 193 MET A CG  1 
ATOM 1403 S SD  . MET A 1 194 ? 6.169   -21.189 -58.876 1.00 78.14  ? 193 MET A SD  1 
ATOM 1404 C CE  . MET A 1 194 ? 6.847   -20.238 -60.236 1.00 75.62  ? 193 MET A CE  1 
ATOM 1405 N N   . LEU A 1 195 ? 0.959   -19.430 -60.900 1.00 60.07  ? 194 LEU A N   1 
ATOM 1406 C CA  . LEU A 1 195 ? -0.072  -19.729 -61.888 1.00 61.21  ? 194 LEU A CA  1 
ATOM 1407 C C   . LEU A 1 195 ? 0.050   -18.839 -63.119 1.00 64.36  ? 194 LEU A C   1 
ATOM 1408 O O   . LEU A 1 195 ? -0.205  -19.291 -64.241 1.00 65.56  ? 194 LEU A O   1 
ATOM 1409 C CB  . LEU A 1 195 ? -1.458  -19.581 -61.259 1.00 55.99  ? 194 LEU A CB  1 
ATOM 1410 C CG  . LEU A 1 195 ? -2.615  -20.311 -61.946 1.00 57.33  ? 194 LEU A CG  1 
ATOM 1411 C CD1 . LEU A 1 195 ? -2.661  -21.769 -61.524 1.00 51.57  ? 194 LEU A CD1 1 
ATOM 1412 C CD2 . LEU A 1 195 ? -3.934  -19.619 -61.636 1.00 50.30  ? 194 LEU A CD2 1 
ATOM 1413 N N   . ILE A 1 196 ? 0.439   -17.576 -62.934 1.00 62.93  ? 195 ILE A N   1 
ATOM 1414 C CA  . ILE A 1 196 ? 0.542   -16.654 -64.060 1.00 66.38  ? 195 ILE A CA  1 
ATOM 1415 C C   . ILE A 1 196 ? 1.941   -16.603 -64.665 1.00 66.44  ? 195 ILE A C   1 
ATOM 1416 O O   . ILE A 1 196 ? 2.083   -16.215 -65.834 1.00 67.72  ? 195 ILE A O   1 
ATOM 1417 C CB  . ILE A 1 196 ? 0.094   -15.236 -63.655 1.00 68.49  ? 195 ILE A CB  1 
ATOM 1418 C CG1 . ILE A 1 196 ? 1.261   -14.434 -63.070 1.00 61.76  ? 195 ILE A CG1 1 
ATOM 1419 C CG2 . ILE A 1 196 ? -1.068  -15.302 -62.675 1.00 70.45  ? 195 ILE A CG2 1 
ATOM 1420 C CD1 . ILE A 1 196 ? 0.890   -13.019 -62.674 1.00 59.65  ? 195 ILE A CD1 1 
ATOM 1421 N N   . LYS A 1 197 ? 2.975   -16.986 -63.915 1.00 67.17  ? 196 LYS A N   1 
ATOM 1422 C CA  . LYS A 1 197 ? 4.323   -16.989 -64.475 1.00 69.97  ? 196 LYS A CA  1 
ATOM 1423 C C   . LYS A 1 197 ? 4.506   -18.152 -65.440 1.00 68.61  ? 196 LYS A C   1 
ATOM 1424 O O   . LYS A 1 197 ? 4.979   -17.970 -66.567 1.00 76.18  ? 196 LYS A O   1 
ATOM 1425 C CB  . LYS A 1 197 ? 5.363   -17.047 -63.356 1.00 72.70  ? 196 LYS A CB  1 
ATOM 1426 C CG  . LYS A 1 197 ? 6.799   -16.961 -63.849 1.00 72.52  ? 196 LYS A CG  1 
ATOM 1427 C CD  . LYS A 1 197 ? 7.788   -17.302 -62.748 1.00 72.04  ? 196 LYS A CD  1 
ATOM 1428 C CE  . LYS A 1 197 ? 7.860   -16.198 -61.707 1.00 67.08  ? 196 LYS A CE  1 
ATOM 1429 N NZ  . LYS A 1 197 ? 8.965   -16.422 -60.733 1.00 64.06  ? 196 LYS A NZ  1 
ATOM 1430 N N   . ARG A 1 198 ? 4.134   -19.359 -65.013 1.00 67.81  ? 197 ARG A N   1 
ATOM 1431 C CA  . ARG A 1 198 ? 4.194   -20.519 -65.891 1.00 71.46  ? 197 ARG A CA  1 
ATOM 1432 C C   . ARG A 1 198 ? 3.104   -20.503 -66.954 1.00 74.44  ? 197 ARG A C   1 
ATOM 1433 O O   . ARG A 1 198 ? 3.201   -21.261 -67.926 1.00 80.46  ? 197 ARG A O   1 
ATOM 1434 C CB  . ARG A 1 198 ? 4.108   -21.801 -65.060 1.00 75.13  ? 197 ARG A CB  1 
ATOM 1435 C CG  . ARG A 1 198 ? 5.070   -21.822 -63.875 1.00 66.75  ? 197 ARG A CG  1 
ATOM 1436 C CD  . ARG A 1 198 ? 4.961   -23.112 -63.076 1.00 58.87  ? 197 ARG A CD  1 
ATOM 1437 N NE  . ARG A 1 198 ? 5.831   -24.160 -63.599 1.00 57.61  ? 197 ARG A NE  1 
ATOM 1438 C CZ  . ARG A 1 198 ? 7.141   -24.216 -63.403 1.00 60.20  ? 197 ARG A CZ  1 
ATOM 1439 N NH1 . ARG A 1 198 ? 7.775   -23.296 -62.696 1.00 62.14  ? 197 ARG A NH1 1 
ATOM 1440 N NH2 . ARG A 1 198 ? 7.834   -25.222 -63.932 1.00 60.59  ? 197 ARG A NH2 1 
ATOM 1441 N N   . GLY A 1 199 ? 2.087   -19.661 -66.798 1.00 72.15  ? 198 GLY A N   1 
ATOM 1442 C CA  . GLY A 1 199 ? 1.051   -19.524 -67.810 1.00 73.43  ? 198 GLY A CA  1 
ATOM 1443 C C   . GLY A 1 199 ? 0.259   -20.787 -68.066 1.00 74.66  ? 198 GLY A C   1 
ATOM 1444 O O   . GLY A 1 199 ? -0.044  -21.101 -69.224 1.00 81.76  ? 198 GLY A O   1 
ATOM 1445 N N   . VAL A 1 200 ? -0.087  -21.522 -67.008 1.00 75.91  ? 199 VAL A N   1 
ATOM 1446 C CA  . VAL A 1 200 ? -0.835  -22.762 -67.193 1.00 78.22  ? 199 VAL A CA  1 
ATOM 1447 C C   . VAL A 1 200 ? -2.267  -22.467 -67.622 1.00 67.79  ? 199 VAL A C   1 
ATOM 1448 O O   . VAL A 1 200 ? -2.829  -23.166 -68.473 1.00 71.04  ? 199 VAL A O   1 
ATOM 1449 C CB  . VAL A 1 200 ? -0.777  -23.620 -65.914 1.00 79.64  ? 199 VAL A CB  1 
ATOM 1450 C CG1 . VAL A 1 200 ? 0.646   -24.094 -65.667 1.00 85.12  ? 199 VAL A CG1 1 
ATOM 1451 C CG2 . VAL A 1 200 ? -1.278  -22.837 -64.712 1.00 72.65  ? 199 VAL A CG2 1 
ATOM 1452 N N   . ILE A 1 201 ? -2.876  -21.430 -67.055 1.00 60.75  ? 200 ILE A N   1 
ATOM 1453 C CA  . ILE A 1 201 ? -4.214  -20.993 -67.443 1.00 59.61  ? 200 ILE A CA  1 
ATOM 1454 C C   . ILE A 1 201 ? -4.237  -19.470 -67.465 1.00 60.30  ? 200 ILE A C   1 
ATOM 1455 O O   . ILE A 1 201 ? -3.556  -18.830 -66.650 1.00 63.30  ? 200 ILE A O   1 
ATOM 1456 C CB  . ILE A 1 201 ? -5.292  -21.541 -66.493 1.00 56.91  ? 200 ILE A CB  1 
ATOM 1457 C CG1 . ILE A 1 201 ? -4.958  -21.185 -65.043 1.00 58.86  ? 200 ILE A CG1 1 
ATOM 1458 C CG2 . ILE A 1 201 ? -5.469  -23.042 -66.669 1.00 62.40  ? 200 ILE A CG2 1 
ATOM 1459 C CD1 . ILE A 1 201 ? -6.157  -21.187 -64.130 1.00 57.89  ? 200 ILE A CD1 1 
ATOM 1460 N N   . PRO A 1 202 ? -4.978  -18.848 -68.379 1.00 59.28  ? 201 PRO A N   1 
ATOM 1461 C CA  . PRO A 1 202 ? -5.157  -17.395 -68.307 1.00 54.87  ? 201 PRO A CA  1 
ATOM 1462 C C   . PRO A 1 202 ? -5.971  -17.012 -67.082 1.00 50.23  ? 201 PRO A C   1 
ATOM 1463 O O   . PRO A 1 202 ? -6.783  -17.790 -66.576 1.00 52.20  ? 201 PRO A O   1 
ATOM 1464 C CB  . PRO A 1 202 ? -5.904  -17.060 -69.604 1.00 51.34  ? 201 PRO A CB  1 
ATOM 1465 C CG  . PRO A 1 202 ? -5.644  -18.229 -70.510 1.00 56.29  ? 201 PRO A CG  1 
ATOM 1466 C CD  . PRO A 1 202 ? -5.568  -19.417 -69.601 1.00 54.91  ? 201 PRO A CD  1 
ATOM 1467 N N   . LEU A 1 203 ? -5.735  -15.790 -66.600 1.00 48.10  ? 202 LEU A N   1 
ATOM 1468 C CA  . LEU A 1 203 ? -6.438  -15.317 -65.413 1.00 50.04  ? 202 LEU A CA  1 
ATOM 1469 C C   . LEU A 1 203 ? -7.930  -15.144 -65.671 1.00 51.22  ? 202 LEU A C   1 
ATOM 1470 O O   . LEU A 1 203 ? -8.733  -15.245 -64.736 1.00 55.84  ? 202 LEU A O   1 
ATOM 1471 C CB  . LEU A 1 203 ? -5.825  -14.002 -64.929 1.00 53.15  ? 202 LEU A CB  1 
ATOM 1472 C CG  . LEU A 1 203 ? -6.408  -13.385 -63.657 1.00 53.63  ? 202 LEU A CG  1 
ATOM 1473 C CD1 . LEU A 1 203 ? -5.323  -13.207 -62.609 1.00 55.49  ? 202 LEU A CD1 1 
ATOM 1474 C CD2 . LEU A 1 203 ? -7.090  -12.058 -63.965 1.00 56.22  ? 202 LEU A CD2 1 
ATOM 1475 N N   . SER A 1 204 ? -8.321  -14.890 -66.923 1.00 50.49  ? 203 SER A N   1 
ATOM 1476 C CA  . SER A 1 204 ? -9.739  -14.760 -67.239 1.00 50.65  ? 203 SER A CA  1 
ATOM 1477 C C   . SER A 1 204 ? -10.497 -16.060 -67.010 1.00 49.58  ? 203 SER A C   1 
ATOM 1478 O O   . SER A 1 204 ? -11.724 -16.033 -66.870 1.00 51.38  ? 203 SER A O   1 
ATOM 1479 C CB  . SER A 1 204 ? -9.921  -14.290 -68.686 1.00 46.42  ? 203 SER A CB  1 
ATOM 1480 O OG  . SER A 1 204 ? -9.368  -15.215 -69.607 1.00 45.15  ? 203 SER A OG  1 
ATOM 1481 N N   . TYR A 1 205 ? -9.795  -17.197 -66.962 1.00 50.11  ? 204 TYR A N   1 
ATOM 1482 C CA  . TYR A 1 205 ? -10.455 -18.467 -66.678 1.00 51.52  ? 204 TYR A CA  1 
ATOM 1483 C C   . TYR A 1 205 ? -11.017 -18.501 -65.262 1.00 51.03  ? 204 TYR A C   1 
ATOM 1484 O O   . TYR A 1 205 ? -11.999 -19.204 -65.002 1.00 49.45  ? 204 TYR A O   1 
ATOM 1485 C CB  . TYR A 1 205 ? -9.482  -19.629 -66.892 1.00 48.43  ? 204 TYR A CB  1 
ATOM 1486 C CG  . TYR A 1 205 ? -9.294  -20.032 -68.342 1.00 53.43  ? 204 TYR A CG  1 
ATOM 1487 C CD1 . TYR A 1 205 ? -9.253  -19.080 -69.353 1.00 54.03  ? 204 TYR A CD1 1 
ATOM 1488 C CD2 . TYR A 1 205 ? -9.150  -21.367 -68.698 1.00 52.93  ? 204 TYR A CD2 1 
ATOM 1489 C CE1 . TYR A 1 205 ? -9.081  -19.445 -70.675 1.00 50.97  ? 204 TYR A CE1 1 
ATOM 1490 C CE2 . TYR A 1 205 ? -8.975  -21.741 -70.020 1.00 52.64  ? 204 TYR A CE2 1 
ATOM 1491 C CZ  . TYR A 1 205 ? -8.941  -20.775 -71.002 1.00 48.87  ? 204 TYR A CZ  1 
ATOM 1492 O OH  . TYR A 1 205 ? -8.769  -21.141 -72.317 1.00 50.59  ? 204 TYR A OH  1 
ATOM 1493 N N   . LEU A 1 206 ? -10.416 -17.748 -64.340 1.00 50.09  ? 205 LEU A N   1 
ATOM 1494 C CA  . LEU A 1 206 ? -10.885 -17.687 -62.962 1.00 53.41  ? 205 LEU A CA  1 
ATOM 1495 C C   . LEU A 1 206 ? -12.151 -16.854 -62.794 1.00 52.65  ? 205 LEU A C   1 
ATOM 1496 O O   . LEU A 1 206 ? -12.680 -16.786 -61.679 1.00 50.98  ? 205 LEU A O   1 
ATOM 1497 C CB  . LEU A 1 206 ? -9.780  -17.133 -62.055 1.00 47.53  ? 205 LEU A CB  1 
ATOM 1498 C CG  . LEU A 1 206 ? -8.531  -18.006 -61.905 1.00 44.97  ? 205 LEU A CG  1 
ATOM 1499 C CD1 . LEU A 1 206 ? -7.401  -17.234 -61.248 1.00 43.15  ? 205 LEU A CD1 1 
ATOM 1500 C CD2 . LEU A 1 206 ? -8.853  -19.261 -61.118 1.00 41.82  ? 205 LEU A CD2 1 
ATOM 1501 N N   . LYS A 1 207 ? -12.642 -16.222 -63.857 1.00 54.19  ? 206 LYS A N   1 
ATOM 1502 C CA  . LYS A 1 207 ? -13.865 -15.437 -63.763 1.00 54.25  ? 206 LYS A CA  1 
ATOM 1503 C C   . LYS A 1 207 ? -15.034 -16.352 -63.409 1.00 56.04  ? 206 LYS A C   1 
ATOM 1504 O O   . LYS A 1 207 ? -15.160 -17.440 -63.988 1.00 60.94  ? 206 LYS A O   1 
ATOM 1505 C CB  . LYS A 1 207 ? -14.136 -14.708 -65.078 1.00 58.68  ? 206 LYS A CB  1 
ATOM 1506 C CG  . LYS A 1 207 ? -14.994 -13.462 -64.932 1.00 63.59  ? 206 LYS A CG  1 
ATOM 1507 C CD  . LYS A 1 207 ? -16.031 -13.352 -66.042 1.00 64.15  ? 206 LYS A CD  1 
ATOM 1508 C CE  . LYS A 1 207 ? -17.335 -14.026 -65.648 1.00 68.48  ? 206 LYS A CE  1 
ATOM 1509 N NZ  . LYS A 1 207 ? -17.958 -13.383 -64.458 1.00 77.68  ? 206 LYS A NZ  1 
ATOM 1510 N N   . PRO A 1 208 ? -15.887 -15.971 -62.459 1.00 57.57  ? 207 PRO A N   1 
ATOM 1511 C CA  . PRO A 1 208 ? -16.944 -16.891 -62.009 1.00 57.50  ? 207 PRO A CA  1 
ATOM 1512 C C   . PRO A 1 208 ? -17.967 -17.156 -63.103 1.00 57.59  ? 207 PRO A C   1 
ATOM 1513 O O   . PRO A 1 208 ? -18.554 -16.234 -63.677 1.00 58.04  ? 207 PRO A O   1 
ATOM 1514 C CB  . PRO A 1 208 ? -17.560 -16.162 -60.807 1.00 54.45  ? 207 PRO A CB  1 
ATOM 1515 C CG  . PRO A 1 208 ? -16.508 -15.198 -60.358 1.00 50.99  ? 207 PRO A CG  1 
ATOM 1516 C CD  . PRO A 1 208 ? -15.813 -14.765 -61.617 1.00 58.40  ? 207 PRO A CD  1 
ATOM 1517 N N   . SER A 1 209 ? -18.163 -18.438 -63.400 1.00 60.90  ? 208 SER A N   1 
ATOM 1518 C CA  . SER A 1 209 ? -19.174 -18.920 -64.330 1.00 58.44  ? 208 SER A CA  1 
ATOM 1519 C C   . SER A 1 209 ? -19.919 -20.075 -63.669 1.00 56.56  ? 208 SER A C   1 
ATOM 1520 O O   . SER A 1 209 ? -19.576 -20.508 -62.565 1.00 58.05  ? 208 SER A O   1 
ATOM 1521 C CB  . SER A 1 209 ? -18.546 -19.353 -65.662 1.00 53.84  ? 208 SER A CB  1 
ATOM 1522 O OG  . SER A 1 209 ? -19.428 -20.181 -66.402 1.00 55.78  ? 208 SER A OG  1 
ATOM 1523 N N   . TRP A 1 210 ? -20.949 -20.583 -64.343 1.00 53.18  ? 209 TRP A N   1 
ATOM 1524 C CA  . TRP A 1 210 ? -21.757 -21.665 -63.788 1.00 51.54  ? 209 TRP A CA  1 
ATOM 1525 C C   . TRP A 1 210 ? -22.168 -22.623 -64.894 1.00 47.55  ? 209 TRP A C   1 
ATOM 1526 O O   . TRP A 1 210 ? -22.920 -22.246 -65.798 1.00 50.03  ? 209 TRP A O   1 
ATOM 1527 C CB  . TRP A 1 210 ? -22.995 -21.123 -63.067 1.00 49.73  ? 209 TRP A CB  1 
ATOM 1528 C CG  . TRP A 1 210 ? -23.598 -22.110 -62.116 1.00 50.39  ? 209 TRP A CG  1 
ATOM 1529 C CD1 . TRP A 1 210 ? -24.717 -22.862 -62.317 1.00 53.13  ? 209 TRP A CD1 1 
ATOM 1530 C CD2 . TRP A 1 210 ? -23.109 -22.458 -60.815 1.00 53.61  ? 209 TRP A CD2 1 
ATOM 1531 N NE1 . TRP A 1 210 ? -24.958 -23.657 -61.222 1.00 57.12  ? 209 TRP A NE1 1 
ATOM 1532 C CE2 . TRP A 1 210 ? -23.985 -23.427 -60.285 1.00 56.92  ? 209 TRP A CE2 1 
ATOM 1533 C CE3 . TRP A 1 210 ? -22.018 -22.043 -60.045 1.00 54.31  ? 209 TRP A CE3 1 
ATOM 1534 C CZ2 . TRP A 1 210 ? -23.805 -23.987 -59.021 1.00 52.50  ? 209 TRP A CZ2 1 
ATOM 1535 C CZ3 . TRP A 1 210 ? -21.840 -22.601 -58.791 1.00 50.30  ? 209 TRP A CZ3 1 
ATOM 1536 C CH2 . TRP A 1 210 ? -22.729 -23.562 -58.292 1.00 46.00  ? 209 TRP A CH2 1 
ATOM 1537 N N   . ASP A 1 211 ? -21.679 -23.857 -64.812 1.00 45.76  ? 210 ASP A N   1 
ATOM 1538 C CA  . ASP A 1 211 ? -22.100 -24.951 -65.679 1.00 43.12  ? 210 ASP A CA  1 
ATOM 1539 C C   . ASP A 1 211 ? -22.866 -25.959 -64.833 1.00 46.58  ? 210 ASP A C   1 
ATOM 1540 O O   . ASP A 1 211 ? -22.300 -26.556 -63.911 1.00 47.62  ? 210 ASP A O   1 
ATOM 1541 C CB  . ASP A 1 211 ? -20.901 -25.614 -66.355 1.00 45.27  ? 210 ASP A CB  1 
ATOM 1542 C CG  . ASP A 1 211 ? -21.302 -26.490 -67.526 1.00 49.60  ? 210 ASP A CG  1 
ATOM 1543 O OD1 . ASP A 1 211 ? -21.977 -27.519 -67.303 1.00 48.27  ? 210 ASP A OD1 1 
ATOM 1544 O OD2 . ASP A 1 211 ? -20.947 -26.144 -68.673 1.00 52.61  ? 210 ASP A OD2 1 
ATOM 1545 N N   . ASN A 1 212 ? -24.147 -26.148 -65.155 1.00 45.51  ? 211 ASN A N   1 
ATOM 1546 C CA  . ASN A 1 212 ? -25.009 -26.992 -64.333 1.00 44.38  ? 211 ASN A CA  1 
ATOM 1547 C C   . ASN A 1 212 ? -24.488 -28.422 -64.267 1.00 48.80  ? 211 ASN A C   1 
ATOM 1548 O O   . ASN A 1 212 ? -24.350 -28.995 -63.180 1.00 51.29  ? 211 ASN A O   1 
ATOM 1549 C CB  . ASN A 1 212 ? -26.436 -26.961 -64.880 1.00 50.29  ? 211 ASN A CB  1 
ATOM 1550 C CG  . ASN A 1 212 ? -27.081 -25.601 -64.731 1.00 55.19  ? 211 ASN A CG  1 
ATOM 1551 O OD1 . ASN A 1 212 ? -26.556 -24.729 -64.038 1.00 53.62  ? 211 ASN A OD1 1 
ATOM 1552 N ND2 . ASN A 1 212 ? -28.222 -25.409 -65.385 1.00 64.70  ? 211 ASN A ND2 1 
ATOM 1553 N N   . GLY A 1 213 ? -24.193 -29.018 -65.425 1.00 46.92  ? 212 GLY A N   1 
ATOM 1554 C CA  . GLY A 1 213 ? -23.701 -30.386 -65.435 1.00 47.03  ? 212 GLY A CA  1 
ATOM 1555 C C   . GLY A 1 213 ? -22.351 -30.539 -64.766 1.00 47.00  ? 212 GLY A C   1 
ATOM 1556 O O   . GLY A 1 213 ? -22.038 -31.602 -64.223 1.00 48.74  ? 212 GLY A O   1 
ATOM 1557 N N   . LEU A 1 214 ? -21.535 -29.486 -64.788 1.00 46.29  ? 213 LEU A N   1 
ATOM 1558 C CA  . LEU A 1 214 ? -20.229 -29.547 -64.146 1.00 48.23  ? 213 LEU A CA  1 
ATOM 1559 C C   . LEU A 1 214 ? -20.314 -29.236 -62.657 1.00 46.40  ? 213 LEU A C   1 
ATOM 1560 O O   . LEU A 1 214 ? -19.491 -29.729 -61.878 1.00 47.22  ? 213 LEU A O   1 
ATOM 1561 C CB  . LEU A 1 214 ? -19.262 -28.583 -64.836 1.00 48.98  ? 213 LEU A CB  1 
ATOM 1562 C CG  . LEU A 1 214 ? -18.455 -29.135 -66.014 1.00 46.56  ? 213 LEU A CG  1 
ATOM 1563 C CD1 . LEU A 1 214 ? -19.361 -29.503 -67.181 1.00 50.57  ? 213 LEU A CD1 1 
ATOM 1564 C CD2 . LEU A 1 214 ? -17.419 -28.119 -66.452 1.00 45.34  ? 213 LEU A CD2 1 
ATOM 1565 N N   . ALA A 1 215 ? -21.297 -28.430 -62.245 1.00 46.74  ? 214 ALA A N   1 
ATOM 1566 C CA  . ALA A 1 215 ? -21.461 -28.128 -60.826 1.00 45.58  ? 214 ALA A CA  1 
ATOM 1567 C C   . ALA A 1 215 ? -21.958 -29.339 -60.049 1.00 46.61  ? 214 ALA A C   1 
ATOM 1568 O O   . ALA A 1 215 ? -21.581 -29.526 -58.887 1.00 45.05  ? 214 ALA A O   1 
ATOM 1569 C CB  . ALA A 1 215 ? -22.420 -26.954 -60.642 1.00 40.78  ? 214 ALA A CB  1 
ATOM 1570 N N   . GLY A 1 216 ? -22.804 -30.165 -60.668 1.00 46.25  ? 215 GLY A N   1 
ATOM 1571 C CA  . GLY A 1 216 ? -23.261 -31.373 -60.008 1.00 43.23  ? 215 GLY A CA  1 
ATOM 1572 C C   . GLY A 1 216 ? -22.175 -32.418 -59.868 1.00 46.29  ? 215 GLY A C   1 
ATOM 1573 O O   . GLY A 1 216 ? -22.145 -33.157 -58.880 1.00 49.94  ? 215 GLY A O   1 
ATOM 1574 N N   . GLN A 1 217 ? -21.271 -32.499 -60.847 1.00 50.36  ? 216 GLN A N   1 
ATOM 1575 C CA  . GLN A 1 217 ? -20.174 -33.456 -60.753 1.00 49.72  ? 216 GLN A CA  1 
ATOM 1576 C C   . GLN A 1 217 ? -19.185 -33.050 -59.669 1.00 49.85  ? 216 GLN A C   1 
ATOM 1577 O O   . GLN A 1 217 ? -18.707 -33.899 -58.907 1.00 51.82  ? 216 GLN A O   1 
ATOM 1578 C CB  . GLN A 1 217 ? -19.471 -33.586 -62.101 1.00 53.80  ? 216 GLN A CB  1 
ATOM 1579 C CG  . GLN A 1 217 ? -20.065 -34.650 -63.001 1.00 53.71  ? 216 GLN A CG  1 
ATOM 1580 C CD  . GLN A 1 217 ? -19.868 -34.339 -64.471 1.00 60.48  ? 216 GLN A CD  1 
ATOM 1581 O OE1 . GLN A 1 217 ? -19.149 -33.406 -64.828 1.00 61.57  ? 216 GLN A OE1 1 
ATOM 1582 N NE2 . GLN A 1 217 ? -20.503 -35.125 -65.333 1.00 65.33  ? 216 GLN A NE2 1 
ATOM 1583 N N   . LEU A 1 218 ? -18.865 -31.756 -59.587 1.00 46.01  ? 217 LEU A N   1 
ATOM 1584 C CA  . LEU A 1 218 ? -18.044 -31.274 -58.483 1.00 46.88  ? 217 LEU A CA  1 
ATOM 1585 C C   . LEU A 1 218 ? -18.769 -31.417 -57.151 1.00 46.28  ? 217 LEU A C   1 
ATOM 1586 O O   . LEU A 1 218 ? -18.122 -31.550 -56.106 1.00 46.18  ? 217 LEU A O   1 
ATOM 1587 C CB  . LEU A 1 218 ? -17.641 -29.819 -58.720 1.00 45.87  ? 217 LEU A CB  1 
ATOM 1588 C CG  . LEU A 1 218 ? -16.698 -29.557 -59.895 1.00 41.78  ? 217 LEU A CG  1 
ATOM 1589 C CD1 . LEU A 1 218 ? -16.705 -28.083 -60.265 1.00 42.38  ? 217 LEU A CD1 1 
ATOM 1590 C CD2 . LEU A 1 218 ? -15.290 -30.026 -59.568 1.00 42.51  ? 217 LEU A CD2 1 
ATOM 1591 N N   . SER A 1 219 ? -20.104 -31.392 -57.167 1.00 41.54  ? 218 SER A N   1 
ATOM 1592 C CA  . SER A 1 219 ? -20.863 -31.642 -55.947 1.00 45.62  ? 218 SER A CA  1 
ATOM 1593 C C   . SER A 1 219 ? -20.692 -33.077 -55.468 1.00 47.65  ? 218 SER A C   1 
ATOM 1594 O O   . SER A 1 219 ? -20.743 -33.335 -54.261 1.00 50.84  ? 218 SER A O   1 
ATOM 1595 C CB  . SER A 1 219 ? -22.344 -31.333 -56.168 1.00 41.53  ? 218 SER A CB  1 
ATOM 1596 O OG  . SER A 1 219 ? -22.551 -29.950 -56.396 1.00 48.07  ? 218 SER A OG  1 
ATOM 1597 N N   . LYS A 1 220 ? -20.500 -34.023 -56.390 1.00 47.24  ? 219 LYS A N   1 
ATOM 1598 C CA  . LYS A 1 220 ? -20.226 -35.395 -55.981 1.00 47.11  ? 219 LYS A CA  1 
ATOM 1599 C C   . LYS A 1 220 ? -18.869 -35.507 -55.302 1.00 45.01  ? 219 LYS A C   1 
ATOM 1600 O O   . LYS A 1 220 ? -18.699 -36.318 -54.384 1.00 45.58  ? 219 LYS A O   1 
ATOM 1601 C CB  . LYS A 1 220 ? -20.306 -36.331 -57.188 1.00 49.13  ? 219 LYS A CB  1 
ATOM 1602 C CG  . LYS A 1 220 ? -21.696 -36.423 -57.805 1.00 55.20  ? 219 LYS A CG  1 
ATOM 1603 C CD  . LYS A 1 220 ? -22.717 -36.954 -56.806 1.00 53.38  ? 219 LYS A CD  1 
ATOM 1604 C CE  . LYS A 1 220 ? -24.142 -36.619 -57.228 1.00 52.34  ? 219 LYS A CE  1 
ATOM 1605 N NZ  . LYS A 1 220 ? -24.536 -35.234 -56.839 1.00 42.87  ? 219 LYS A NZ  1 
ATOM 1606 N N   . PHE A 1 221 ? -17.895 -34.702 -55.734 1.00 44.60  ? 220 PHE A N   1 
ATOM 1607 C CA  . PHE A 1 221 ? -16.617 -34.647 -55.034 1.00 46.28  ? 220 PHE A CA  1 
ATOM 1608 C C   . PHE A 1 221 ? -16.753 -33.944 -53.691 1.00 46.88  ? 220 PHE A C   1 
ATOM 1609 O O   . PHE A 1 221 ? -15.975 -34.214 -52.769 1.00 46.44  ? 220 PHE A O   1 
ATOM 1610 C CB  . PHE A 1 221 ? -15.573 -33.945 -55.900 1.00 46.26  ? 220 PHE A CB  1 
ATOM 1611 C CG  . PHE A 1 221 ? -15.025 -34.803 -57.002 1.00 48.96  ? 220 PHE A CG  1 
ATOM 1612 C CD1 . PHE A 1 221 ? -15.677 -34.887 -58.221 1.00 46.57  ? 220 PHE A CD1 1 
ATOM 1613 C CD2 . PHE A 1 221 ? -13.854 -35.522 -56.821 1.00 48.63  ? 220 PHE A CD2 1 
ATOM 1614 C CE1 . PHE A 1 221 ? -15.174 -35.676 -59.239 1.00 47.60  ? 220 PHE A CE1 1 
ATOM 1615 C CE2 . PHE A 1 221 ? -13.346 -36.312 -57.835 1.00 49.28  ? 220 PHE A CE2 1 
ATOM 1616 C CZ  . PHE A 1 221 ? -14.007 -36.388 -59.046 1.00 48.42  ? 220 PHE A CZ  1 
ATOM 1617 N N   . THR A 1 222 ? -17.725 -33.037 -53.566 1.00 47.90  ? 221 THR A N   1 
ATOM 1618 C CA  . THR A 1 222 ? -18.014 -32.433 -52.270 1.00 47.08  ? 221 THR A CA  1 
ATOM 1619 C C   . THR A 1 222 ? -18.548 -33.472 -51.293 1.00 49.41  ? 221 THR A C   1 
ATOM 1620 O O   . THR A 1 222 ? -18.145 -33.499 -50.124 1.00 51.57  ? 221 THR A O   1 
ATOM 1621 C CB  . THR A 1 222 ? -19.017 -31.290 -52.437 1.00 47.11  ? 221 THR A CB  1 
ATOM 1622 O OG1 . THR A 1 222 ? -18.383 -30.185 -53.093 1.00 48.49  ? 221 THR A OG1 1 
ATOM 1623 C CG2 . THR A 1 222 ? -19.542 -30.833 -51.085 1.00 43.70  ? 221 THR A CG2 1 
ATOM 1624 N N   . LEU A 1 223 ? -19.448 -34.342 -51.759 1.00 51.90  ? 222 LEU A N   1 
ATOM 1625 C CA  . LEU A 1 223 ? -19.975 -35.397 -50.899 1.00 52.44  ? 222 LEU A CA  1 
ATOM 1626 C C   . LEU A 1 223 ? -18.870 -36.348 -50.457 1.00 51.40  ? 222 LEU A C   1 
ATOM 1627 O O   . LEU A 1 223 ? -18.847 -36.792 -49.303 1.00 51.39  ? 222 LEU A O   1 
ATOM 1628 C CB  . LEU A 1 223 ? -21.081 -36.162 -51.626 1.00 54.03  ? 222 LEU A CB  1 
ATOM 1629 C CG  . LEU A 1 223 ? -22.313 -35.352 -52.034 1.00 54.60  ? 222 LEU A CG  1 
ATOM 1630 C CD1 . LEU A 1 223 ? -23.350 -36.249 -52.694 1.00 57.19  ? 222 LEU A CD1 1 
ATOM 1631 C CD2 . LEU A 1 223 ? -22.908 -34.627 -50.837 1.00 58.94  ? 222 LEU A CD2 1 
ATOM 1632 N N   . MET A 1 224 ? -17.940 -36.669 -51.361 1.00 48.20  ? 223 MET A N   1 
ATOM 1633 C CA  . MET A 1 224 ? -16.832 -37.546 -50.997 1.00 47.74  ? 223 MET A CA  1 
ATOM 1634 C C   . MET A 1 224 ? -15.914 -36.879 -49.980 1.00 47.07  ? 223 MET A C   1 
ATOM 1635 O O   . MET A 1 224 ? -15.431 -37.533 -49.048 1.00 46.74  ? 223 MET A O   1 
ATOM 1636 C CB  . MET A 1 224 ? -16.047 -37.954 -52.245 1.00 48.41  ? 223 MET A CB  1 
ATOM 1637 C CG  . MET A 1 224 ? -16.763 -38.961 -53.140 1.00 50.82  ? 223 MET A CG  1 
ATOM 1638 S SD  . MET A 1 224 ? -16.019 -39.150 -54.779 1.00 54.35  ? 223 MET A SD  1 
ATOM 1639 C CE  . MET A 1 224 ? -14.571 -38.108 -54.629 1.00 45.96  ? 223 MET A CE  1 
ATOM 1640 N N   . ALA A 1 225 ? -15.664 -35.575 -50.140 1.00 47.95  ? 224 ALA A N   1 
ATOM 1641 C CA  . ALA A 1 225 ? -14.848 -34.849 -49.171 1.00 46.66  ? 224 ALA A CA  1 
ATOM 1642 C C   . ALA A 1 225 ? -15.542 -34.741 -47.821 1.00 51.37  ? 224 ALA A C   1 
ATOM 1643 O O   . ALA A 1 225 ? -14.875 -34.720 -46.780 1.00 50.32  ? 224 ALA A O   1 
ATOM 1644 C CB  . ALA A 1 225 ? -14.511 -33.456 -49.699 1.00 43.86  ? 224 ALA A CB  1 
ATOM 1645 N N   . LEU A 1 226 ? -16.873 -34.661 -47.818 1.00 50.31  ? 225 LEU A N   1 
ATOM 1646 C CA  . LEU A 1 226 ? -17.604 -34.631 -46.557 1.00 48.40  ? 225 LEU A CA  1 
ATOM 1647 C C   . LEU A 1 226 ? -17.599 -35.992 -45.878 1.00 49.89  ? 225 LEU A C   1 
ATOM 1648 O O   . LEU A 1 226 ? -17.703 -36.070 -44.650 1.00 52.44  ? 225 LEU A O   1 
ATOM 1649 C CB  . LEU A 1 226 ? -19.037 -34.161 -46.796 1.00 44.04  ? 225 LEU A CB  1 
ATOM 1650 C CG  . LEU A 1 226 ? -19.731 -33.520 -45.597 1.00 45.53  ? 225 LEU A CG  1 
ATOM 1651 C CD1 . LEU A 1 226 ? -19.188 -32.120 -45.372 1.00 50.77  ? 225 LEU A CD1 1 
ATOM 1652 C CD2 . LEU A 1 226 ? -21.235 -33.487 -45.809 1.00 44.40  ? 225 LEU A CD2 1 
ATOM 1653 N N   . ILE A 1 227 ? -17.471 -37.070 -46.653 1.00 51.36  ? 226 ILE A N   1 
ATOM 1654 C CA  . ILE A 1 227 ? -17.503 -38.409 -46.077 1.00 46.77  ? 226 ILE A CA  1 
ATOM 1655 C C   . ILE A 1 227 ? -16.203 -38.713 -45.345 1.00 46.20  ? 226 ILE A C   1 
ATOM 1656 O O   . ILE A 1 227 ? -16.216 -39.243 -44.228 1.00 51.78  ? 226 ILE A O   1 
ATOM 1657 C CB  . ILE A 1 227 ? -17.797 -39.450 -47.173 1.00 46.69  ? 226 ILE A CB  1 
ATOM 1658 C CG1 . ILE A 1 227 ? -19.287 -39.452 -47.517 1.00 45.25  ? 226 ILE A CG1 1 
ATOM 1659 C CG2 . ILE A 1 227 ? -17.337 -40.834 -46.741 1.00 48.73  ? 226 ILE A CG2 1 
ATOM 1660 C CD1 . ILE A 1 227 ? -19.617 -40.161 -48.811 1.00 46.74  ? 226 ILE A CD1 1 
ATOM 1661 N N   . THR A 1 228 ? -15.062 -38.384 -45.953 1.00 46.40  ? 227 THR A N   1 
ATOM 1662 C CA  . THR A 1 228 ? -13.782 -38.669 -45.312 1.00 50.78  ? 227 THR A CA  1 
ATOM 1663 C C   . THR A 1 228 ? -13.569 -37.819 -44.066 1.00 52.26  ? 227 THR A C   1 
ATOM 1664 O O   . THR A 1 228 ? -12.829 -38.224 -43.163 1.00 53.17  ? 227 THR A O   1 
ATOM 1665 C CB  . THR A 1 228 ? -12.635 -38.447 -46.295 1.00 50.13  ? 227 THR A CB  1 
ATOM 1666 O OG1 . THR A 1 228 ? -12.393 -37.042 -46.440 1.00 54.72  ? 227 THR A OG1 1 
ATOM 1667 C CG2 . THR A 1 228 ? -12.983 -39.035 -47.641 1.00 47.10  ? 227 THR A CG2 1 
ATOM 1668 N N   . SER A 1 229 ? -14.204 -36.651 -43.993 1.00 51.43  ? 228 SER A N   1 
ATOM 1669 C CA  . SER A 1 229 ? -14.033 -35.784 -42.835 1.00 51.01  ? 228 SER A CA  1 
ATOM 1670 C C   . SER A 1 229 ? -14.771 -36.282 -41.605 1.00 49.96  ? 228 SER A C   1 
ATOM 1671 O O   . SER A 1 229 ? -14.666 -35.646 -40.552 1.00 56.42  ? 228 SER A O   1 
ATOM 1672 C CB  . SER A 1 229 ? -14.499 -34.364 -43.164 1.00 49.21  ? 228 SER A CB  1 
ATOM 1673 O OG  . SER A 1 229 ? -14.199 -34.024 -44.505 1.00 61.10  ? 228 SER A OG  1 
ATOM 1674 N N   . VAL A 1 230 ? -15.513 -37.384 -41.699 1.00 54.76  ? 229 VAL A N   1 
ATOM 1675 C CA  . VAL A 1 230 ? -16.282 -37.863 -40.557 1.00 56.86  ? 229 VAL A CA  1 
ATOM 1676 C C   . VAL A 1 230 ? -16.092 -39.363 -40.369 1.00 60.54  ? 229 VAL A C   1 
ATOM 1677 O O   . VAL A 1 230 ? -15.949 -39.833 -39.237 1.00 67.94  ? 229 VAL A O   1 
ATOM 1678 C CB  . VAL A 1 230 ? -17.775 -37.509 -40.704 1.00 53.78  ? 229 VAL A CB  1 
ATOM 1679 C CG1 . VAL A 1 230 ? -17.998 -36.029 -40.435 1.00 58.27  ? 229 VAL A CG1 1 
ATOM 1680 C CG2 . VAL A 1 230 ? -18.286 -37.881 -42.087 1.00 55.08  ? 229 VAL A CG2 1 
ATOM 1681 N N   . THR A 1 231 ? -16.071 -40.120 -41.467 1.00 55.32  ? 230 THR A N   1 
ATOM 1682 C CA  . THR A 1 231 ? -16.114 -41.579 -41.394 1.00 49.65  ? 230 THR A CA  1 
ATOM 1683 C C   . THR A 1 231 ? -14.963 -42.153 -40.576 1.00 52.04  ? 230 THR A C   1 
ATOM 1684 O O   . THR A 1 231 ? -15.160 -42.580 -39.434 1.00 51.72  ? 230 THR A O   1 
ATOM 1685 C CB  . THR A 1 231 ? -16.103 -42.191 -42.796 1.00 48.99  ? 230 THR A CB  1 
ATOM 1686 O OG1 . THR A 1 231 ? -17.172 -41.634 -43.570 1.00 50.72  ? 230 THR A OG1 1 
ATOM 1687 C CG2 . THR A 1 231 ? -16.282 -43.700 -42.716 1.00 45.12  ? 230 THR A CG2 1 
ATOM 1688 N N   . LEU A 1 232 ? -13.766 -42.175 -41.148 1.00 49.75  ? 231 LEU A N   1 
ATOM 1689 C CA  . LEU A 1 232 ? -12.617 -42.763 -40.469 1.00 50.69  ? 231 LEU A CA  1 
ATOM 1690 C C   . LEU A 1 232 ? -12.177 -41.970 -39.238 1.00 55.44  ? 231 LEU A C   1 
ATOM 1691 O O   . LEU A 1 232 ? -11.765 -42.585 -38.246 1.00 59.35  ? 231 LEU A O   1 
ATOM 1692 C CB  . LEU A 1 232 ? -11.449 -42.917 -41.445 1.00 56.96  ? 231 LEU A CB  1 
ATOM 1693 C CG  . LEU A 1 232 ? -11.482 -44.181 -42.308 1.00 51.87  ? 231 LEU A CG  1 
ATOM 1694 C CD1 . LEU A 1 232 ? -10.106 -44.463 -42.885 1.00 51.93  ? 231 LEU A CD1 1 
ATOM 1695 C CD2 . LEU A 1 232 ? -11.987 -45.373 -41.508 1.00 49.67  ? 231 LEU A CD2 1 
ATOM 1696 N N   . PRO A 1 233 ? -12.219 -40.627 -39.247 1.00 55.01  ? 232 PRO A N   1 
ATOM 1697 C CA  . PRO A 1 233 ? -11.881 -39.900 -38.008 1.00 55.73  ? 232 PRO A CA  1 
ATOM 1698 C C   . PRO A 1 233 ? -12.753 -40.276 -36.822 1.00 49.33  ? 232 PRO A C   1 
ATOM 1699 O O   . PRO A 1 233 ? -12.245 -40.387 -35.699 1.00 50.00  ? 232 PRO A O   1 
ATOM 1700 C CB  . PRO A 1 233 ? -12.066 -38.432 -38.412 1.00 51.87  ? 232 PRO A CB  1 
ATOM 1701 C CG  . PRO A 1 233 ? -11.744 -38.419 -39.851 1.00 45.95  ? 232 PRO A CG  1 
ATOM 1702 C CD  . PRO A 1 233 ? -12.302 -39.702 -40.395 1.00 47.76  ? 232 PRO A CD  1 
ATOM 1703 N N   . VAL A 1 234 ? -14.056 -40.473 -37.035 1.00 46.60  ? 233 VAL A N   1 
ATOM 1704 C CA  . VAL A 1 234 ? -14.925 -40.896 -35.941 1.00 47.70  ? 233 VAL A CA  1 
ATOM 1705 C C   . VAL A 1 234 ? -14.549 -42.297 -35.478 1.00 49.84  ? 233 VAL A C   1 
ATOM 1706 O O   . VAL A 1 234 ? -14.560 -42.592 -34.277 1.00 52.75  ? 233 VAL A O   1 
ATOM 1707 C CB  . VAL A 1 234 ? -16.402 -40.809 -36.369 1.00 45.66  ? 233 VAL A CB  1 
ATOM 1708 C CG1 . VAL A 1 234 ? -17.258 -41.815 -35.611 1.00 49.69  ? 233 VAL A CG1 1 
ATOM 1709 C CG2 . VAL A 1 234 ? -16.927 -39.392 -36.176 1.00 45.00  ? 233 VAL A CG2 1 
ATOM 1710 N N   . ALA A 1 235 ? -14.200 -43.179 -36.418 1.00 44.67  ? 234 ALA A N   1 
ATOM 1711 C CA  . ALA A 1 235 ? -13.740 -44.514 -36.051 1.00 48.42  ? 234 ALA A CA  1 
ATOM 1712 C C   . ALA A 1 235 ? -12.528 -44.436 -35.132 1.00 53.54  ? 234 ALA A C   1 
ATOM 1713 O O   . ALA A 1 235 ? -12.467 -45.118 -34.102 1.00 53.99  ? 234 ALA A O   1 
ATOM 1714 C CB  . ALA A 1 235 ? -13.415 -45.322 -37.307 1.00 46.20  ? 234 ALA A CB  1 
ATOM 1715 N N   . TYR A 1 236 ? -11.557 -43.592 -35.481 1.00 52.40  ? 235 TYR A N   1 
ATOM 1716 C CA  . TYR A 1 236 ? -10.389 -43.426 -34.625 1.00 52.17  ? 235 TYR A CA  1 
ATOM 1717 C C   . TYR A 1 236 ? -10.769 -42.804 -33.287 1.00 50.68  ? 235 TYR A C   1 
ATOM 1718 O O   . TYR A 1 236 ? -10.232 -43.193 -32.244 1.00 52.87  ? 235 TYR A O   1 
ATOM 1719 C CB  . TYR A 1 236 ? -9.334  -42.588 -35.342 1.00 47.20  ? 235 TYR A CB  1 
ATOM 1720 C CG  . TYR A 1 236 ? -8.504  -43.392 -36.314 1.00 51.35  ? 235 TYR A CG  1 
ATOM 1721 C CD1 . TYR A 1 236 ? -7.587  -44.328 -35.859 1.00 54.54  ? 235 TYR A CD1 1 
ATOM 1722 C CD2 . TYR A 1 236 ? -8.649  -43.230 -37.687 1.00 52.37  ? 235 TYR A CD2 1 
ATOM 1723 C CE1 . TYR A 1 236 ? -6.826  -45.072 -36.739 1.00 54.60  ? 235 TYR A CE1 1 
ATOM 1724 C CE2 . TYR A 1 236 ? -7.892  -43.972 -38.577 1.00 52.21  ? 235 TYR A CE2 1 
ATOM 1725 C CZ  . TYR A 1 236 ? -6.983  -44.892 -38.095 1.00 50.73  ? 235 TYR A CZ  1 
ATOM 1726 O OH  . TYR A 1 236 ? -6.224  -45.636 -38.969 1.00 52.23  ? 235 TYR A OH  1 
ATOM 1727 N N   . ILE A 1 237 ? -11.703 -41.849 -33.296 1.00 54.32  ? 236 ILE A N   1 
ATOM 1728 C CA  . ILE A 1 237 ? -12.170 -41.243 -32.050 1.00 50.51  ? 236 ILE A CA  1 
ATOM 1729 C C   . ILE A 1 237 ? -12.741 -42.306 -31.121 1.00 50.55  ? 236 ILE A C   1 
ATOM 1730 O O   . ILE A 1 237 ? -12.460 -42.315 -29.916 1.00 54.36  ? 236 ILE A O   1 
ATOM 1731 C CB  . ILE A 1 237 ? -13.203 -40.140 -32.349 1.00 48.00  ? 236 ILE A CB  1 
ATOM 1732 C CG1 . ILE A 1 237 ? -12.499 -38.847 -32.765 1.00 52.65  ? 236 ILE A CG1 1 
ATOM 1733 C CG2 . ILE A 1 237 ? -14.103 -39.906 -31.144 1.00 46.80  ? 236 ILE A CG2 1 
ATOM 1734 C CD1 . ILE A 1 237 ? -13.394 -37.628 -32.748 1.00 48.07  ? 236 ILE A CD1 1 
ATOM 1735 N N   . MET A 1 238 ? -13.548 -43.219 -31.666 1.00 47.42  ? 237 MET A N   1 
ATOM 1736 C CA  . MET A 1 238 ? -14.066 -44.322 -30.865 1.00 50.72  ? 237 MET A CA  1 
ATOM 1737 C C   . MET A 1 238 ? -12.945 -45.214 -30.350 1.00 50.60  ? 237 MET A C   1 
ATOM 1738 O O   . MET A 1 238 ? -13.065 -45.803 -29.269 1.00 54.00  ? 237 MET A O   1 
ATOM 1739 C CB  . MET A 1 238 ? -15.064 -45.139 -31.687 1.00 53.13  ? 237 MET A CB  1 
ATOM 1740 C CG  . MET A 1 238 ? -16.362 -44.408 -32.005 1.00 53.88  ? 237 MET A CG  1 
ATOM 1741 S SD  . MET A 1 238 ? -17.612 -45.494 -32.726 1.00 60.08  ? 237 MET A SD  1 
ATOM 1742 C CE  . MET A 1 238 ? -18.815 -44.307 -33.318 1.00 38.28  ? 237 MET A CE  1 
ATOM 1743 N N   . MET A 1 239 ? -11.846 -45.318 -31.100 1.00 54.28  ? 238 MET A N   1 
ATOM 1744 C CA  . MET A 1 239 ? -10.735 -46.162 -30.672 1.00 52.89  ? 238 MET A CA  1 
ATOM 1745 C C   . MET A 1 239 ? -10.012 -45.560 -29.473 1.00 55.49  ? 238 MET A C   1 
ATOM 1746 O O   . MET A 1 239 ? -9.672  -46.277 -28.525 1.00 58.06  ? 238 MET A O   1 
ATOM 1747 C CB  . MET A 1 239 ? -9.769  -46.382 -31.836 1.00 55.16  ? 238 MET A CB  1 
ATOM 1748 C CG  . MET A 1 239 ? -10.217 -47.458 -32.813 1.00 55.58  ? 238 MET A CG  1 
ATOM 1749 S SD  . MET A 1 239 ? -9.270  -47.457 -34.348 1.00 55.83  ? 238 MET A SD  1 
ATOM 1750 C CE  . MET A 1 239 ? -8.078  -48.753 -34.010 1.00 51.35  ? 238 MET A CE  1 
ATOM 1751 N N   . ARG A 1 240 ? -9.771  -44.245 -29.492 1.00 51.53  ? 239 ARG A N   1 
ATOM 1752 C CA  . ARG A 1 240 ? -9.113  -43.606 -28.357 1.00 52.23  ? 239 ARG A CA  1 
ATOM 1753 C C   . ARG A 1 240 ? -9.979  -43.646 -27.103 1.00 50.91  ? 239 ARG A C   1 
ATOM 1754 O O   . ARG A 1 240 ? -9.448  -43.752 -25.992 1.00 49.39  ? 239 ARG A O   1 
ATOM 1755 C CB  . ARG A 1 240 ? -8.738  -42.161 -28.696 1.00 51.16  ? 239 ARG A CB  1 
ATOM 1756 C CG  . ARG A 1 240 ? -8.381  -41.921 -30.152 1.00 51.47  ? 239 ARG A CG  1 
ATOM 1757 C CD  . ARG A 1 240 ? -7.894  -40.498 -30.384 1.00 58.03  ? 239 ARG A CD  1 
ATOM 1758 N NE  . ARG A 1 240 ? -8.969  -39.525 -30.227 1.00 68.67  ? 239 ARG A NE  1 
ATOM 1759 C CZ  . ARG A 1 240 ? -8.950  -38.516 -29.366 1.00 71.78  ? 239 ARG A CZ  1 
ATOM 1760 N NH1 . ARG A 1 240 ? -7.911  -38.302 -28.574 1.00 66.30  ? 239 ARG A NH1 1 
ATOM 1761 N NH2 . ARG A 1 240 ? -10.000 -37.702 -29.296 1.00 60.23  ? 239 ARG A NH2 1 
ATOM 1762 N N   . LYS A 1 241 ? -11.304 -43.563 -27.253 1.00 53.19  ? 240 LYS A N   1 
ATOM 1763 C CA  . LYS A 1 241 ? -12.182 -43.641 -26.089 1.00 54.09  ? 240 LYS A CA  1 
ATOM 1764 C C   . LYS A 1 241 ? -12.175 -45.040 -25.490 1.00 61.25  ? 240 LYS A C   1 
ATOM 1765 O O   . LYS A 1 241 ? -12.141 -45.196 -24.263 1.00 65.64  ? 240 LYS A O   1 
ATOM 1766 C CB  . LYS A 1 241 ? -13.605 -43.229 -26.467 1.00 56.28  ? 240 LYS A CB  1 
ATOM 1767 C CG  . LYS A 1 241 ? -13.719 -41.825 -27.029 1.00 59.95  ? 240 LYS A CG  1 
ATOM 1768 C CD  . LYS A 1 241 ? -13.906 -40.796 -25.930 1.00 58.23  ? 240 LYS A CD  1 
ATOM 1769 C CE  . LYS A 1 241 ? -13.868 -39.388 -26.499 1.00 58.36  ? 240 LYS A CE  1 
ATOM 1770 N NZ  . LYS A 1 241 ? -12.617 -39.142 -27.271 1.00 53.38  ? 240 LYS A NZ  1 
ATOM 1771 N N   . LEU A 1 242 ? -12.209 -46.071 -26.338 1.00 54.14  ? 241 LEU A N   1 
ATOM 1772 C CA  . LEU A 1 242 ? -12.100 -47.435 -25.836 1.00 52.13  ? 241 LEU A CA  1 
ATOM 1773 C C   . LEU A 1 242 ? -10.740 -47.678 -25.189 1.00 54.18  ? 241 LEU A C   1 
ATOM 1774 O O   . LEU A 1 242 ? -10.653 -48.351 -24.156 1.00 53.36  ? 241 LEU A O   1 
ATOM 1775 C CB  . LEU A 1 242 ? -12.352 -48.436 -26.963 1.00 48.10  ? 241 LEU A CB  1 
ATOM 1776 C CG  . LEU A 1 242 ? -12.502 -49.889 -26.509 1.00 49.29  ? 241 LEU A CG  1 
ATOM 1777 C CD1 . LEU A 1 242 ? -13.428 -49.994 -25.303 1.00 50.50  ? 241 LEU A CD1 1 
ATOM 1778 C CD2 . LEU A 1 242 ? -12.999 -50.765 -27.644 1.00 60.15  ? 241 LEU A CD2 1 
ATOM 1779 N N   . LEU A 1 243 ? -9.666  -47.136 -25.773 1.00 53.30  ? 242 LEU A N   1 
ATOM 1780 C CA  . LEU A 1 243 ? -8.352  -47.269 -25.147 1.00 53.12  ? 242 LEU A CA  1 
ATOM 1781 C C   . LEU A 1 243 ? -8.307  -46.495 -23.831 1.00 54.22  ? 242 LEU A C   1 
ATOM 1782 O O   . LEU A 1 243 ? -7.871  -47.029 -22.804 1.00 53.11  ? 242 LEU A O   1 
ATOM 1783 C CB  . LEU A 1 243 ? -7.249  -46.805 -26.111 1.00 46.03  ? 242 LEU A CB  1 
ATOM 1784 C CG  . LEU A 1 243 ? -5.797  -47.318 -26.070 1.00 41.71  ? 242 LEU A CG  1 
ATOM 1785 C CD1 . LEU A 1 243 ? -5.009  -46.730 -27.245 1.00 49.02  ? 242 LEU A CD1 1 
ATOM 1786 C CD2 . LEU A 1 243 ? -5.101  -47.011 -24.756 1.00 55.21  ? 242 LEU A CD2 1 
ATOM 1787 N N   . ALA A 1 244 ? -8.800  -45.251 -23.827 1.00 54.87  ? 243 ALA A N   1 
ATOM 1788 C CA  . ALA A 1 244 ? -8.758  -44.466 -22.596 1.00 54.89  ? 243 ALA A CA  1 
ATOM 1789 C C   . ALA A 1 244 ? -9.613  -45.078 -21.497 1.00 55.32  ? 243 ALA A C   1 
ATOM 1790 O O   . ALA A 1 244 ? -9.439  -44.728 -20.325 1.00 55.88  ? 243 ALA A O   1 
ATOM 1791 C CB  . ALA A 1 244 ? -9.199  -43.024 -22.854 1.00 47.71  ? 243 ALA A CB  1 
ATOM 1792 N N   . ALA A 1 245 ? -10.532 -45.978 -21.845 1.00 56.71  ? 244 ALA A N   1 
ATOM 1793 C CA  . ALA A 1 245 ? -11.356 -46.658 -20.856 1.00 49.84  ? 244 ALA A CA  1 
ATOM 1794 C C   . ALA A 1 245 ? -10.637 -47.865 -20.259 1.00 53.06  ? 244 ALA A C   1 
ATOM 1795 O O   . ALA A 1 245 ? -10.520 -47.980 -19.035 1.00 63.14  ? 244 ALA A O   1 
ATOM 1796 C CB  . ALA A 1 245 ? -12.689 -47.077 -21.488 1.00 43.67  ? 244 ALA A CB  1 
ATOM 1797 N N   . GLN A 1 246 ? -10.138 -48.764 -21.109 1.00 54.15  ? 245 GLN A N   1 
ATOM 1798 C CA  . GLN A 1 246 ? -9.425  -49.937 -20.618 1.00 53.23  ? 245 GLN A CA  1 
ATOM 1799 C C   . GLN A 1 246 ? -8.052  -49.590 -20.059 1.00 55.02  ? 245 GLN A C   1 
ATOM 1800 O O   . GLN A 1 246 ? -7.509  -50.363 -19.262 1.00 57.07  ? 245 GLN A O   1 
ATOM 1801 C CB  . GLN A 1 246 ? -9.289  -50.971 -21.736 1.00 53.57  ? 245 GLN A CB  1 
ATOM 1802 C CG  . GLN A 1 246 ? -10.583 -51.241 -22.484 1.00 54.24  ? 245 GLN A CG  1 
ATOM 1803 C CD  . GLN A 1 246 ? -11.526 -52.133 -21.705 1.00 57.32  ? 245 GLN A CD  1 
ATOM 1804 O OE1 . GLN A 1 246 ? -11.190 -53.271 -21.376 1.00 56.49  ? 245 GLN A OE1 1 
ATOM 1805 N NE2 . GLN A 1 246 ? -12.716 -51.622 -21.407 1.00 56.26  ? 245 GLN A NE2 1 
ATOM 1806 N N   . TYR A 1 247 ? -7.479  -48.454 -20.461 1.00 54.54  ? 246 TYR A N   1 
ATOM 1807 C CA  . TYR A 1 247 ? -6.162  -48.038 -19.992 1.00 56.19  ? 246 TYR A CA  1 
ATOM 1808 C C   . TYR A 1 247 ? -6.163  -46.544 -19.688 1.00 58.72  ? 246 TYR A C   1 
ATOM 1809 O O   . TYR A 1 247 ? -7.193  -45.995 -19.286 1.00 63.30  ? 246 TYR A O   1 
ATOM 1810 C CB  . TYR A 1 247 ? -5.089  -48.393 -21.027 1.00 55.14  ? 246 TYR A CB  1 
ATOM 1811 C CG  . TYR A 1 247 ? -4.984  -49.881 -21.284 1.00 47.60  ? 246 TYR A CG  1 
ATOM 1812 C CD1 . TYR A 1 247 ? -5.792  -50.500 -22.228 1.00 48.40  ? 246 TYR A CD1 1 
ATOM 1813 C CD2 . TYR A 1 247 ? -4.087  -50.668 -20.575 1.00 50.87  ? 246 TYR A CD2 1 
ATOM 1814 C CE1 . TYR A 1 247 ? -5.714  -51.858 -22.457 1.00 47.15  ? 246 TYR A CE1 1 
ATOM 1815 C CE2 . TYR A 1 247 ? -3.997  -52.030 -20.803 1.00 52.85  ? 246 TYR A CE2 1 
ATOM 1816 C CZ  . TYR A 1 247 ? -4.813  -52.618 -21.747 1.00 45.44  ? 246 TYR A CZ  1 
ATOM 1817 O OH  . TYR A 1 247 ? -4.735  -53.971 -21.986 1.00 43.20  ? 246 TYR A OH  1 
ATOM 1818 N N   . SER A 1 248 ? -5.029  -45.877 -19.874 1.00 67.46  ? 247 SER A N   1 
ATOM 1819 C CA  . SER A 1 248 ? -4.904  -44.462 -19.557 1.00 70.44  ? 247 SER A CA  1 
ATOM 1820 C C   . SER A 1 248 ? -4.985  -43.605 -20.815 1.00 69.62  ? 247 SER A C   1 
ATOM 1821 O O   . SER A 1 248 ? -4.827  -44.087 -21.939 1.00 67.15  ? 247 SER A O   1 
ATOM 1822 C CB  . SER A 1 248 ? -3.586  -44.182 -18.828 1.00 70.45  ? 247 SER A CB  1 
ATOM 1823 O OG  . SER A 1 248 ? -3.525  -42.834 -18.392 1.00 71.16  ? 247 SER A OG  1 
ATOM 1824 N N   . TRP A 1 249 ? -5.240  -42.310 -20.605 1.00 61.73  ? 248 TRP A N   1 
ATOM 1825 C CA  . TRP A 1 249 ? -5.195  -41.366 -21.716 1.00 53.49  ? 248 TRP A CA  1 
ATOM 1826 C C   . TRP A 1 249 ? -3.773  -41.182 -22.226 1.00 55.60  ? 248 TRP A C   1 
ATOM 1827 O O   . TRP A 1 249 ? -3.573  -40.883 -23.409 1.00 57.32  ? 248 TRP A O   1 
ATOM 1828 C CB  . TRP A 1 249 ? -5.789  -40.021 -21.296 1.00 45.75  ? 248 TRP A CB  1 
ATOM 1829 C CG  . TRP A 1 249 ? -7.227  -39.855 -21.686 1.00 50.46  ? 248 TRP A CG  1 
ATOM 1830 C CD1 . TRP A 1 249 ? -8.299  -39.778 -20.845 1.00 43.66  ? 248 TRP A CD1 1 
ATOM 1831 C CD2 . TRP A 1 249 ? -7.752  -39.743 -23.017 1.00 56.34  ? 248 TRP A CD2 1 
ATOM 1832 N NE1 . TRP A 1 249 ? -9.458  -39.629 -21.568 1.00 46.74  ? 248 TRP A NE1 1 
ATOM 1833 C CE2 . TRP A 1 249 ? -9.150  -39.602 -22.903 1.00 53.99  ? 248 TRP A CE2 1 
ATOM 1834 C CE3 . TRP A 1 249 ? -7.176  -39.748 -24.293 1.00 44.33  ? 248 TRP A CE3 1 
ATOM 1835 C CZ2 . TRP A 1 249 ? -9.980  -39.470 -24.015 1.00 45.81  ? 248 TRP A CZ2 1 
ATOM 1836 C CZ3 . TRP A 1 249 ? -8.001  -39.615 -25.393 1.00 46.96  ? 248 TRP A CZ3 1 
ATOM 1837 C CH2 . TRP A 1 249 ? -9.388  -39.478 -25.247 1.00 49.63  ? 248 TRP A CH2 1 
ATOM 1838 N N   . ASP A 1 250 ? -2.778  -41.358 -21.354 1.00 57.73  ? 249 ASP A N   1 
ATOM 1839 C CA  . ASP A 1 250 ? -1.390  -41.323 -21.800 1.00 56.02  ? 249 ASP A CA  1 
ATOM 1840 C C   . ASP A 1 250 ? -1.053  -42.528 -22.667 1.00 52.47  ? 249 ASP A C   1 
ATOM 1841 O O   . ASP A 1 250 ? -0.204  -42.428 -23.560 1.00 53.27  ? 249 ASP A O   1 
ATOM 1842 C CB  . ASP A 1 250 ? -0.452  -41.246 -20.595 1.00 56.36  ? 249 ASP A CB  1 
ATOM 1843 C CG  . ASP A 1 250 ? -0.491  -39.890 -19.915 1.00 58.36  ? 249 ASP A CG  1 
ATOM 1844 O OD1 . ASP A 1 250 ? -0.529  -38.868 -20.633 1.00 62.71  ? 249 ASP A OD1 1 
ATOM 1845 O OD2 . ASP A 1 250 ? -0.483  -39.843 -18.667 1.00 59.51  ? 249 ASP A OD2 1 
ATOM 1846 N N   . GLU A 1 251 ? -1.701  -43.670 -22.423 1.00 53.41  ? 250 GLU A N   1 
ATOM 1847 C CA  . GLU A 1 251 ? -1.544  -44.807 -23.323 1.00 52.66  ? 250 GLU A CA  1 
ATOM 1848 C C   . GLU A 1 251 ? -2.126  -44.504 -24.697 1.00 49.93  ? 250 GLU A C   1 
ATOM 1849 O O   . GLU A 1 251 ? -1.642  -45.028 -25.706 1.00 48.74  ? 250 GLU A O   1 
ATOM 1850 C CB  . GLU A 1 251 ? -2.194  -46.052 -22.716 1.00 52.56  ? 250 GLU A CB  1 
ATOM 1851 C CG  . GLU A 1 251 ? -2.017  -47.326 -23.531 1.00 46.48  ? 250 GLU A CG  1 
ATOM 1852 C CD  . GLU A 1 251 ? -0.696  -48.013 -23.299 1.00 48.78  ? 250 GLU A CD  1 
ATOM 1853 O OE1 . GLU A 1 251 ? 0.135   -47.471 -22.543 1.00 54.47  ? 250 GLU A OE1 1 
ATOM 1854 O OE2 . GLU A 1 251 ? -0.495  -49.104 -23.872 1.00 50.76  ? 250 GLU A OE2 1 
ATOM 1855 N N   . VAL A 1 252 ? -3.161  -43.661 -24.755 1.00 51.99  ? 251 VAL A N   1 
ATOM 1856 C CA  . VAL A 1 252 ? -3.612  -43.130 -26.037 1.00 48.88  ? 251 VAL A CA  1 
ATOM 1857 C C   . VAL A 1 252 ? -2.566  -42.182 -26.607 1.00 50.69  ? 251 VAL A C   1 
ATOM 1858 O O   . VAL A 1 252 ? -2.427  -42.056 -27.830 1.00 51.37  ? 251 VAL A O   1 
ATOM 1859 C CB  . VAL A 1 252 ? -4.974  -42.428 -25.879 1.00 48.74  ? 251 VAL A CB  1 
ATOM 1860 C CG1 . VAL A 1 252 ? -5.451  -41.871 -27.216 1.00 54.99  ? 251 VAL A CG1 1 
ATOM 1861 C CG2 . VAL A 1 252 ? -6.005  -43.371 -25.272 1.00 45.81  ? 251 VAL A CG2 1 
ATOM 1862 N N   . GLY A 1 253 ? -1.808  -41.510 -25.737 1.00 45.87  ? 252 GLY A N   1 
ATOM 1863 C CA  . GLY A 1 253 ? -0.826  -40.550 -26.209 1.00 44.01  ? 252 GLY A CA  1 
ATOM 1864 C C   . GLY A 1 253 ? 0.336   -41.199 -26.935 1.00 49.79  ? 252 GLY A C   1 
ATOM 1865 O O   . GLY A 1 253 ? 0.855   -40.646 -27.909 1.00 55.84  ? 252 GLY A O   1 
ATOM 1866 N N   . ILE A 1 254 ? 0.767   -42.375 -26.473 1.00 44.51  ? 253 ILE A N   1 
ATOM 1867 C CA  . ILE A 1 254 ? 1.863   -43.054 -27.157 1.00 49.65  ? 253 ILE A CA  1 
ATOM 1868 C C   . ILE A 1 254 ? 1.394   -43.631 -28.486 1.00 49.05  ? 253 ILE A C   1 
ATOM 1869 O O   . ILE A 1 254 ? 2.192   -43.784 -29.418 1.00 49.30  ? 253 ILE A O   1 
ATOM 1870 C CB  . ILE A 1 254 ? 2.486   -44.137 -26.256 1.00 47.25  ? 253 ILE A CB  1 
ATOM 1871 C CG1 . ILE A 1 254 ? 1.491   -45.267 -25.998 1.00 47.87  ? 253 ILE A CG1 1 
ATOM 1872 C CG2 . ILE A 1 254 ? 2.957   -43.532 -24.945 1.00 51.41  ? 253 ILE A CG2 1 
ATOM 1873 C CD1 . ILE A 1 254 ? 2.107   -46.480 -25.343 1.00 48.39  ? 253 ILE A CD1 1 
ATOM 1874 N N   . TRP A 1 255 ? 0.104   -43.958 -28.604 1.00 48.88  ? 254 TRP A N   1 
ATOM 1875 C CA  . TRP A 1 255 ? -0.424  -44.387 -29.895 1.00 48.70  ? 254 TRP A CA  1 
ATOM 1876 C C   . TRP A 1 255 ? -0.606  -43.206 -30.836 1.00 50.90  ? 254 TRP A C   1 
ATOM 1877 O O   . TRP A 1 255 ? -0.412  -43.344 -32.050 1.00 52.54  ? 254 TRP A O   1 
ATOM 1878 C CB  . TRP A 1 255 ? -1.746  -45.131 -29.707 1.00 47.69  ? 254 TRP A CB  1 
ATOM 1879 C CG  . TRP A 1 255 ? -2.368  -45.594 -30.998 1.00 52.91  ? 254 TRP A CG  1 
ATOM 1880 C CD1 . TRP A 1 255 ? -1.735  -46.207 -32.043 1.00 51.80  ? 254 TRP A CD1 1 
ATOM 1881 C CD2 . TRP A 1 255 ? -3.745  -45.476 -31.377 1.00 52.82  ? 254 TRP A CD2 1 
ATOM 1882 N NE1 . TRP A 1 255 ? -2.633  -46.479 -33.048 1.00 48.68  ? 254 TRP A NE1 1 
ATOM 1883 C CE2 . TRP A 1 255 ? -3.874  -46.040 -32.663 1.00 49.35  ? 254 TRP A CE2 1 
ATOM 1884 C CE3 . TRP A 1 255 ? -4.880  -44.951 -30.754 1.00 50.02  ? 254 TRP A CE3 1 
ATOM 1885 C CZ2 . TRP A 1 255 ? -5.093  -46.093 -33.335 1.00 47.19  ? 254 TRP A CZ2 1 
ATOM 1886 C CZ3 . TRP A 1 255 ? -6.089  -45.004 -31.423 1.00 47.57  ? 254 TRP A CZ3 1 
ATOM 1887 C CH2 . TRP A 1 255 ? -6.185  -45.571 -32.700 1.00 47.67  ? 254 TRP A CH2 1 
ATOM 1888 N N   . GLN A 1 256 ? -0.971  -42.041 -30.298 1.00 51.11  ? 255 GLN A N   1 
ATOM 1889 C CA  . GLN A 1 256 ? -1.073  -40.843 -31.122 1.00 54.44  ? 255 GLN A CA  1 
ATOM 1890 C C   . GLN A 1 256 ? 0.298   -40.373 -31.597 1.00 51.66  ? 255 GLN A C   1 
ATOM 1891 O O   . GLN A 1 256 ? 0.418   -39.849 -32.710 1.00 53.63  ? 255 GLN A O   1 
ATOM 1892 C CB  . GLN A 1 256 ? -1.785  -39.733 -30.345 1.00 56.95  ? 255 GLN A CB  1 
ATOM 1893 C CG  . GLN A 1 256 ? -3.296  -39.913 -30.239 1.00 60.24  ? 255 GLN A CG  1 
ATOM 1894 C CD  . GLN A 1 256 ? -3.957  -38.845 -29.387 1.00 60.70  ? 255 GLN A CD  1 
ATOM 1895 O OE1 . GLN A 1 256 ? -5.182  -38.807 -29.256 1.00 59.89  ? 255 GLN A OE1 1 
ATOM 1896 N NE2 . GLN A 1 256 ? -3.147  -37.971 -28.802 1.00 58.87  ? 255 GLN A NE2 1 
ATOM 1897 N N   . GLY A 1 257 ? 1.337   -40.557 -30.779 1.00 47.15  ? 256 GLY A N   1 
ATOM 1898 C CA  . GLY A 1 257 ? 2.669   -40.139 -31.185 1.00 47.50  ? 256 GLY A CA  1 
ATOM 1899 C C   . GLY A 1 257 ? 3.231   -40.973 -32.322 1.00 56.79  ? 256 GLY A C   1 
ATOM 1900 O O   . GLY A 1 257 ? 3.845   -40.438 -33.250 1.00 61.88  ? 256 GLY A O   1 
ATOM 1901 N N   . VAL A 1 258 ? 3.034   -42.292 -32.266 1.00 54.70  ? 257 VAL A N   1 
ATOM 1902 C CA  . VAL A 1 258 ? 3.504   -43.157 -33.343 1.00 52.16  ? 257 VAL A CA  1 
ATOM 1903 C C   . VAL A 1 258 ? 2.757   -42.850 -34.636 1.00 54.72  ? 257 VAL A C   1 
ATOM 1904 O O   . VAL A 1 258 ? 3.354   -42.800 -35.718 1.00 55.29  ? 257 VAL A O   1 
ATOM 1905 C CB  . VAL A 1 258 ? 3.364   -44.637 -32.937 1.00 51.41  ? 257 VAL A CB  1 
ATOM 1906 C CG1 . VAL A 1 258 ? 3.787   -45.552 -34.076 1.00 50.70  ? 257 VAL A CG1 1 
ATOM 1907 C CG2 . VAL A 1 258 ? 4.184   -44.923 -31.688 1.00 48.09  ? 257 VAL A CG2 1 
ATOM 1908 N N   . SER A 1 259 ? 1.443   -42.621 -34.542 1.00 55.24  ? 258 SER A N   1 
ATOM 1909 C CA  . SER A 1 259 ? 0.657   -42.292 -35.727 1.00 53.68  ? 258 SER A CA  1 
ATOM 1910 C C   . SER A 1 259 ? 0.976   -40.898 -36.250 1.00 56.35  ? 258 SER A C   1 
ATOM 1911 O O   . SER A 1 259 ? 0.838   -40.644 -37.451 1.00 64.49  ? 258 SER A O   1 
ATOM 1912 C CB  . SER A 1 259 ? -0.837  -42.401 -35.420 1.00 53.90  ? 258 SER A CB  1 
ATOM 1913 O OG  . SER A 1 259 ? -1.102  -43.472 -34.533 1.00 54.26  ? 258 SER A OG  1 
ATOM 1914 N N   . SER A 1 260 ? 1.386   -39.982 -35.369 1.00 55.65  ? 259 SER A N   1 
ATOM 1915 C CA  . SER A 1 260 ? 1.703   -38.626 -35.806 1.00 62.05  ? 259 SER A CA  1 
ATOM 1916 C C   . SER A 1 260 ? 2.924   -38.617 -36.717 1.00 60.59  ? 259 SER A C   1 
ATOM 1917 O O   . SER A 1 260 ? 2.885   -38.058 -37.820 1.00 61.63  ? 259 SER A O   1 
ATOM 1918 C CB  . SER A 1 260 ? 1.927   -37.722 -34.593 1.00 59.54  ? 259 SER A CB  1 
ATOM 1919 O OG  . SER A 1 260 ? 3.119   -38.071 -33.913 1.00 58.14  ? 259 SER A OG  1 
ATOM 1920 N N   . ILE A 1 261 ? 4.021   -39.235 -36.271 1.00 57.49  ? 260 ILE A N   1 
ATOM 1921 C CA  . ILE A 1 261 ? 5.210   -39.316 -37.107 1.00 58.44  ? 260 ILE A CA  1 
ATOM 1922 C C   . ILE A 1 261 ? 4.991   -40.237 -38.298 1.00 65.90  ? 260 ILE A C   1 
ATOM 1923 O O   . ILE A 1 261 ? 5.711   -40.134 -39.298 1.00 65.83  ? 260 ILE A O   1 
ATOM 1924 C CB  . ILE A 1 261 ? 6.424   -39.771 -36.276 1.00 54.23  ? 260 ILE A CB  1 
ATOM 1925 C CG1 . ILE A 1 261 ? 6.349   -41.269 -35.994 1.00 52.13  ? 260 ILE A CG1 1 
ATOM 1926 C CG2 . ILE A 1 261 ? 6.504   -38.991 -34.974 1.00 59.48  ? 260 ILE A CG2 1 
ATOM 1927 C CD1 . ILE A 1 261 ? 7.582   -41.801 -35.325 1.00 56.61  ? 260 ILE A CD1 1 
ATOM 1928 N N   . SER A 1 262 ? 4.009   -41.138 -38.220 1.00 66.76  ? 261 SER A N   1 
ATOM 1929 C CA  . SER A 1 262 ? 3.654   -41.938 -39.387 1.00 60.34  ? 261 SER A CA  1 
ATOM 1930 C C   . SER A 1 262 ? 3.010   -41.076 -40.464 1.00 63.24  ? 261 SER A C   1 
ATOM 1931 O O   . SER A 1 262 ? 3.288   -41.251 -41.655 1.00 62.81  ? 261 SER A O   1 
ATOM 1932 C CB  . SER A 1 262 ? 2.723   -43.079 -38.980 1.00 61.32  ? 261 SER A CB  1 
ATOM 1933 O OG  . SER A 1 262 ? 3.321   -43.889 -37.983 1.00 64.91  ? 261 SER A OG  1 
ATOM 1934 N N   . ASP A 1 263 ? 2.156   -40.130 -40.062 1.00 72.43  ? 262 ASP A N   1 
ATOM 1935 C CA  . ASP A 1 263 ? 1.528   -39.237 -41.030 1.00 76.33  ? 262 ASP A CA  1 
ATOM 1936 C C   . ASP A 1 263 ? 2.546   -38.324 -41.697 1.00 70.68  ? 262 ASP A C   1 
ATOM 1937 O O   . ASP A 1 263 ? 2.366   -37.939 -42.858 1.00 74.37  ? 262 ASP A O   1 
ATOM 1938 C CB  . ASP A 1 263 ? 0.447   -38.397 -40.349 1.00 75.49  ? 262 ASP A CB  1 
ATOM 1939 C CG  . ASP A 1 263 ? -0.786  -39.203 -40.000 1.00 88.42  ? 262 ASP A CG  1 
ATOM 1940 O OD1 . ASP A 1 263 ? -0.997  -40.270 -40.615 1.00 87.01  ? 262 ASP A OD1 1 
ATOM 1941 O OD2 . ASP A 1 263 ? -1.544  -38.770 -39.106 1.00 97.52  ? 262 ASP A OD2 1 
ATOM 1942 N N   . ALA A 1 264 ? 3.614   -37.964 -40.984 1.00 63.30  ? 263 ALA A N   1 
ATOM 1943 C CA  . ALA A 1 264 ? 4.594   -37.037 -41.538 1.00 64.51  ? 263 ALA A CA  1 
ATOM 1944 C C   . ALA A 1 264 ? 5.431   -37.704 -42.621 1.00 61.87  ? 263 ALA A C   1 
ATOM 1945 O O   . ALA A 1 264 ? 5.545   -37.188 -43.738 1.00 62.94  ? 263 ALA A O   1 
ATOM 1946 C CB  . ALA A 1 264 ? 5.486   -36.492 -40.423 1.00 61.57  ? 263 ALA A CB  1 
ATOM 1947 N N   . TYR A 1 265 ? 6.021   -38.860 -42.310 1.00 59.38  ? 264 TYR A N   1 
ATOM 1948 C CA  . TYR A 1 265 ? 6.893   -39.524 -43.271 1.00 59.12  ? 264 TYR A CA  1 
ATOM 1949 C C   . TYR A 1 265 ? 6.120   -40.174 -44.412 1.00 62.36  ? 264 TYR A C   1 
ATOM 1950 O O   . TYR A 1 265 ? 6.691   -40.382 -45.486 1.00 63.14  ? 264 TYR A O   1 
ATOM 1951 C CB  . TYR A 1 265 ? 7.776   -40.552 -42.554 1.00 55.76  ? 264 TYR A CB  1 
ATOM 1952 C CG  . TYR A 1 265 ? 7.244   -41.970 -42.544 1.00 57.88  ? 264 TYR A CG  1 
ATOM 1953 C CD1 . TYR A 1 265 ? 6.330   -42.382 -41.585 1.00 57.48  ? 264 TYR A CD1 1 
ATOM 1954 C CD2 . TYR A 1 265 ? 7.681   -42.904 -43.477 1.00 60.72  ? 264 TYR A CD2 1 
ATOM 1955 C CE1 . TYR A 1 265 ? 5.851   -43.681 -41.565 1.00 56.50  ? 264 TYR A CE1 1 
ATOM 1956 C CE2 . TYR A 1 265 ? 7.207   -44.203 -43.467 1.00 56.60  ? 264 TYR A CE2 1 
ATOM 1957 C CZ  . TYR A 1 265 ? 6.294   -44.586 -42.508 1.00 58.54  ? 264 TYR A CZ  1 
ATOM 1958 O OH  . TYR A 1 265 ? 5.820   -45.878 -42.492 1.00 58.49  ? 264 TYR A OH  1 
ATOM 1959 N N   . LEU A 1 266 ? 4.840   -40.498 -44.215 1.00 60.97  ? 265 LEU A N   1 
ATOM 1960 C CA  . LEU A 1 266 ? 4.043   -41.004 -45.328 1.00 60.66  ? 265 LEU A CA  1 
ATOM 1961 C C   . LEU A 1 266 ? 3.641   -39.898 -46.295 1.00 65.10  ? 265 LEU A C   1 
ATOM 1962 O O   . LEU A 1 266 ? 3.288   -40.193 -47.441 1.00 66.83  ? 265 LEU A O   1 
ATOM 1963 C CB  . LEU A 1 266 ? 2.794   -41.723 -44.815 1.00 63.76  ? 265 LEU A CB  1 
ATOM 1964 C CG  . LEU A 1 266 ? 2.972   -43.110 -44.194 1.00 57.14  ? 265 LEU A CG  1 
ATOM 1965 C CD1 . LEU A 1 266 ? 1.626   -43.797 -44.070 1.00 45.75  ? 265 LEU A CD1 1 
ATOM 1966 C CD2 . LEU A 1 266 ? 3.929   -43.954 -45.018 1.00 58.05  ? 265 LEU A CD2 1 
ATOM 1967 N N   . GLN A 1 267 ? 3.690   -38.637 -45.860 1.00 61.76  ? 266 GLN A N   1 
ATOM 1968 C CA  . GLN A 1 267 ? 3.310   -37.531 -46.728 1.00 60.13  ? 266 GLN A CA  1 
ATOM 1969 C C   . GLN A 1 267 ? 4.300   -37.319 -47.868 1.00 66.82  ? 266 GLN A C   1 
ATOM 1970 O O   . GLN A 1 267 ? 3.972   -36.624 -48.836 1.00 64.21  ? 266 GLN A O   1 
ATOM 1971 C CB  . GLN A 1 267 ? 3.168   -36.252 -45.903 1.00 59.92  ? 266 GLN A CB  1 
ATOM 1972 C CG  . GLN A 1 267 ? 2.067   -35.322 -46.374 1.00 63.08  ? 266 GLN A CG  1 
ATOM 1973 C CD  . GLN A 1 267 ? 1.918   -34.108 -45.480 1.00 61.91  ? 266 GLN A CD  1 
ATOM 1974 O OE1 . GLN A 1 267 ? 2.674   -33.931 -44.524 1.00 57.86  ? 266 GLN A OE1 1 
ATOM 1975 N NE2 . GLN A 1 267 ? 0.948   -33.256 -45.794 1.00 61.46  ? 266 GLN A NE2 1 
ATOM 1976 N N   . PHE A 1 268 ? 5.500   -37.897 -47.777 1.00 69.68  ? 267 PHE A N   1 
ATOM 1977 C CA  . PHE A 1 268 ? 6.450   -37.828 -48.882 1.00 68.81  ? 267 PHE A CA  1 
ATOM 1978 C C   . PHE A 1 268 ? 5.957   -38.578 -50.110 1.00 71.11  ? 267 PHE A C   1 
ATOM 1979 O O   . PHE A 1 268 ? 6.392   -38.272 -51.225 1.00 71.51  ? 267 PHE A O   1 
ATOM 1980 C CB  . PHE A 1 268 ? 7.807   -38.387 -48.451 1.00 67.45  ? 267 PHE A CB  1 
ATOM 1981 C CG  . PHE A 1 268 ? 8.519   -37.538 -47.438 1.00 65.05  ? 267 PHE A CG  1 
ATOM 1982 C CD1 . PHE A 1 268 ? 9.113   -36.344 -47.810 1.00 63.67  ? 267 PHE A CD1 1 
ATOM 1983 C CD2 . PHE A 1 268 ? 8.593   -37.932 -46.114 1.00 60.12  ? 267 PHE A CD2 1 
ATOM 1984 C CE1 . PHE A 1 268 ? 9.769   -35.559 -46.881 1.00 58.20  ? 267 PHE A CE1 1 
ATOM 1985 C CE2 . PHE A 1 268 ? 9.246   -37.152 -45.179 1.00 61.75  ? 267 PHE A CE2 1 
ATOM 1986 C CZ  . PHE A 1 268 ? 9.835   -35.965 -45.564 1.00 59.89  ? 267 PHE A CZ  1 
ATOM 1987 N N   . ILE A 1 269 ? 5.061   -39.545 -49.930 1.00 81.06  ? 268 ILE A N   1 
ATOM 1988 C CA  . ILE A 1 269 ? 4.541   -40.350 -51.022 1.00 82.74  ? 268 ILE A CA  1 
ATOM 1989 C C   . ILE A 1 269 ? 3.074   -40.045 -51.298 1.00 80.44  ? 268 ILE A C   1 
ATOM 1990 O O   . ILE A 1 269 ? 2.671   -39.919 -52.457 1.00 81.93  ? 268 ILE A O   1 
ATOM 1991 C CB  . ILE A 1 269 ? 4.751   -41.854 -50.733 1.00 78.92  ? 268 ILE A CB  1 
ATOM 1992 C CG1 . ILE A 1 269 ? 6.195   -42.259 -51.035 1.00 80.95  ? 268 ILE A CG1 1 
ATOM 1993 C CG2 . ILE A 1 269 ? 3.780   -42.708 -51.533 1.00 78.91  ? 268 ILE A CG2 1 
ATOM 1994 C CD1 . ILE A 1 269 ? 6.812   -43.157 -49.987 1.00 79.69  ? 268 ILE A CD1 1 
ATOM 1995 N N   . THR A 1 270 ? 2.264   -39.903 -50.247 1.00 67.32  ? 269 THR A N   1 
ATOM 1996 C CA  . THR A 1 270 ? 0.829   -39.711 -50.437 1.00 64.23  ? 269 THR A CA  1 
ATOM 1997 C C   . THR A 1 270 ? 0.511   -38.369 -51.087 1.00 61.78  ? 269 THR A C   1 
ATOM 1998 O O   . THR A 1 270 ? -0.499  -38.249 -51.790 1.00 57.83  ? 269 THR A O   1 
ATOM 1999 C CB  . THR A 1 270 ? 0.102   -39.827 -49.099 1.00 67.12  ? 269 THR A CB  1 
ATOM 2000 O OG1 . THR A 1 270 ? 0.723   -38.962 -48.141 1.00 70.25  ? 269 THR A OG1 1 
ATOM 2001 C CG2 . THR A 1 270 ? 0.163   -41.254 -48.587 1.00 63.29  ? 269 THR A CG2 1 
ATOM 2002 N N   . ALA A 1 271 ? 1.349   -37.353 -50.864 1.00 62.62  ? 270 ALA A N   1 
ATOM 2003 C CA  . ALA A 1 271 ? 1.081   -36.038 -51.433 1.00 58.56  ? 270 ALA A CA  1 
ATOM 2004 C C   . ALA A 1 271 ? 1.351   -35.986 -52.929 1.00 58.59  ? 270 ALA A C   1 
ATOM 2005 O O   . ALA A 1 271 ? 0.863   -35.071 -53.601 1.00 59.30  ? 270 ALA A O   1 
ATOM 2006 C CB  . ALA A 1 271 ? 1.910   -34.972 -50.718 1.00 58.89  ? 270 ALA A CB  1 
ATOM 2007 N N   . SER A 1 272 ? 2.115   -36.938 -53.464 1.00 58.97  ? 271 SER A N   1 
ATOM 2008 C CA  . SER A 1 272 ? 2.368   -37.004 -54.897 1.00 54.00  ? 271 SER A CA  1 
ATOM 2009 C C   . SER A 1 272 ? 1.273   -37.738 -55.660 1.00 52.44  ? 271 SER A C   1 
ATOM 2010 O O   . SER A 1 272 ? 1.235   -37.654 -56.892 1.00 53.90  ? 271 SER A O   1 
ATOM 2011 C CB  . SER A 1 272 ? 3.719   -37.677 -55.170 1.00 53.23  ? 271 SER A CB  1 
ATOM 2012 O OG  . SER A 1 272 ? 3.995   -38.687 -54.216 1.00 60.80  ? 271 SER A OG  1 
ATOM 2013 N N   . PHE A 1 273 ? 0.386   -38.454 -54.964 1.00 50.00  ? 272 PHE A N   1 
ATOM 2014 C CA  . PHE A 1 273 ? -0.706  -39.133 -55.652 1.00 50.64  ? 272 PHE A CA  1 
ATOM 2015 C C   . PHE A 1 273 ? -1.704  -38.138 -56.227 1.00 48.32  ? 272 PHE A C   1 
ATOM 2016 O O   . PHE A 1 273 ? -2.315  -38.404 -57.268 1.00 51.73  ? 272 PHE A O   1 
ATOM 2017 C CB  . PHE A 1 273 ? -1.413  -40.100 -54.702 1.00 54.78  ? 272 PHE A CB  1 
ATOM 2018 C CG  . PHE A 1 273 ? -0.602  -41.319 -54.352 1.00 53.70  ? 272 PHE A CG  1 
ATOM 2019 C CD1 . PHE A 1 273 ? 0.631   -41.548 -54.941 1.00 54.67  ? 272 PHE A CD1 1 
ATOM 2020 C CD2 . PHE A 1 273 ? -1.080  -42.239 -53.434 1.00 51.64  ? 272 PHE A CD2 1 
ATOM 2021 C CE1 . PHE A 1 273 ? 1.372   -42.669 -54.616 1.00 55.65  ? 272 PHE A CE1 1 
ATOM 2022 C CE2 . PHE A 1 273 ? -0.345  -43.361 -53.106 1.00 47.11  ? 272 PHE A CE2 1 
ATOM 2023 C CZ  . PHE A 1 273 ? 0.883   -43.576 -53.698 1.00 52.53  ? 272 PHE A CZ  1 
ATOM 2024 N N   . SER A 1 274 ? -1.883  -36.993 -55.570 1.00 45.99  ? 273 SER A N   1 
ATOM 2025 C CA  . SER A 1 274 ? -2.772  -35.956 -56.073 1.00 48.52  ? 273 SER A CA  1 
ATOM 2026 C C   . SER A 1 274 ? -2.137  -35.117 -57.171 1.00 46.91  ? 273 SER A C   1 
ATOM 2027 O O   . SER A 1 274 ? -2.837  -34.313 -57.798 1.00 46.02  ? 273 SER A O   1 
ATOM 2028 C CB  . SER A 1 274 ? -3.209  -35.043 -54.926 1.00 49.26  ? 273 SER A CB  1 
ATOM 2029 O OG  . SER A 1 274 ? -3.698  -35.802 -53.834 1.00 59.88  ? 273 SER A OG  1 
ATOM 2030 N N   . VAL A 1 275 ? -0.839  -35.282 -57.419 1.00 49.10  ? 274 VAL A N   1 
ATOM 2031 C CA  . VAL A 1 275 ? -0.133  -34.471 -58.403 1.00 47.81  ? 274 VAL A CA  1 
ATOM 2032 C C   . VAL A 1 275 ? 0.039   -35.262 -59.692 1.00 51.97  ? 274 VAL A C   1 
ATOM 2033 O O   . VAL A 1 275 ? 0.038   -34.689 -60.787 1.00 52.59  ? 274 VAL A O   1 
ATOM 2034 C CB  . VAL A 1 275 ? 1.228   -34.000 -57.863 1.00 46.09  ? 274 VAL A CB  1 
ATOM 2035 C CG1 . VAL A 1 275 ? 1.833   -32.961 -58.790 1.00 45.61  ? 274 VAL A CG1 1 
ATOM 2036 C CG2 . VAL A 1 275 ? 1.075   -33.440 -56.457 1.00 48.88  ? 274 VAL A CG2 1 
ATOM 2037 N N   . TYR A 1 276 ? 0.190   -36.581 -59.574 1.00 57.61  ? 275 TYR A N   1 
ATOM 2038 C CA  . TYR A 1 276 ? 0.398   -37.436 -60.738 1.00 59.50  ? 275 TYR A CA  1 
ATOM 2039 C C   . TYR A 1 276 ? -0.655  -38.523 -60.871 1.00 60.78  ? 275 TYR A C   1 
ATOM 2040 O O   . TYR A 1 276 ? -1.276  -38.646 -61.933 1.00 63.65  ? 275 TYR A O   1 
ATOM 2041 C CB  . TYR A 1 276 ? 1.794   -38.077 -60.692 1.00 61.74  ? 275 TYR A CB  1 
ATOM 2042 C CG  . TYR A 1 276 ? 2.046   -39.043 -61.830 1.00 63.77  ? 275 TYR A CG  1 
ATOM 2043 C CD1 . TYR A 1 276 ? 2.270   -38.581 -63.121 1.00 64.89  ? 275 TYR A CD1 1 
ATOM 2044 C CD2 . TYR A 1 276 ? 2.048   -40.417 -61.616 1.00 65.36  ? 275 TYR A CD2 1 
ATOM 2045 C CE1 . TYR A 1 276 ? 2.496   -39.458 -64.166 1.00 66.86  ? 275 TYR A CE1 1 
ATOM 2046 C CE2 . TYR A 1 276 ? 2.273   -41.303 -62.658 1.00 68.46  ? 275 TYR A CE2 1 
ATOM 2047 C CZ  . TYR A 1 276 ? 2.496   -40.816 -63.931 1.00 68.58  ? 275 TYR A CZ  1 
ATOM 2048 O OH  . TYR A 1 276 ? 2.720   -41.686 -64.974 1.00 69.41  ? 275 TYR A OH  1 
ATOM 2049 N N   . LEU A 1 277 ? -0.874  -39.322 -59.824 1.00 50.07  ? 276 LEU A N   1 
ATOM 2050 C CA  . LEU A 1 277 ? -1.747  -40.485 -59.956 1.00 43.86  ? 276 LEU A CA  1 
ATOM 2051 C C   . LEU A 1 277 ? -3.188  -40.076 -60.234 1.00 48.67  ? 276 LEU A C   1 
ATOM 2052 O O   . LEU A 1 277 ? -3.856  -40.684 -61.078 1.00 49.16  ? 276 LEU A O   1 
ATOM 2053 C CB  . LEU A 1 277 ? -1.661  -41.350 -58.699 1.00 47.35  ? 276 LEU A CB  1 
ATOM 2054 C CG  . LEU A 1 277 ? -2.498  -42.630 -58.683 1.00 43.97  ? 276 LEU A CG  1 
ATOM 2055 C CD1 . LEU A 1 277 ? -1.935  -43.643 -59.661 1.00 44.46  ? 276 LEU A CD1 1 
ATOM 2056 C CD2 . LEU A 1 277 ? -2.547  -43.215 -57.281 1.00 48.32  ? 276 LEU A CD2 1 
ATOM 2057 N N   . LEU A 1 278 ? -3.687  -39.046 -59.541 1.00 39.07  ? 277 LEU A N   1 
ATOM 2058 C CA  . LEU A 1 278 ? -5.072  -38.629 -59.761 1.00 41.70  ? 277 LEU A CA  1 
ATOM 2059 C C   . LEU A 1 278 ? -5.289  -38.058 -61.159 1.00 45.21  ? 277 LEU A C   1 
ATOM 2060 O O   . LEU A 1 278 ? -6.247  -38.480 -61.831 1.00 45.92  ? 277 LEU A O   1 
ATOM 2061 C CB  . LEU A 1 278 ? -5.504  -37.650 -58.663 1.00 43.83  ? 277 LEU A CB  1 
ATOM 2062 C CG  . LEU A 1 278 ? -6.834  -36.913 -58.850 1.00 42.63  ? 277 LEU A CG  1 
ATOM 2063 C CD1 . LEU A 1 278 ? -7.998  -37.890 -58.872 1.00 41.96  ? 277 LEU A CD1 1 
ATOM 2064 C CD2 . LEU A 1 278 ? -7.034  -35.873 -57.756 1.00 41.40  ? 277 LEU A CD2 1 
ATOM 2065 N N   . PRO A 1 279 ? -4.472  -37.123 -61.663 1.00 43.39  ? 278 PRO A N   1 
ATOM 2066 C CA  . PRO A 1 279 ? -4.728  -36.620 -63.024 1.00 45.32  ? 278 PRO A CA  1 
ATOM 2067 C C   . PRO A 1 279 ? -4.447  -37.640 -64.116 1.00 48.54  ? 278 PRO A C   1 
ATOM 2068 O O   . PRO A 1 279 ? -5.166  -37.669 -65.123 1.00 44.62  ? 278 PRO A O   1 
ATOM 2069 C CB  . PRO A 1 279 ? -3.800  -35.401 -63.127 1.00 44.95  ? 278 PRO A CB  1 
ATOM 2070 C CG  . PRO A 1 279 ? -2.732  -35.654 -62.136 1.00 45.49  ? 278 PRO A CG  1 
ATOM 2071 C CD  . PRO A 1 279 ? -3.394  -36.364 -61.002 1.00 46.06  ? 278 PRO A CD  1 
ATOM 2072 N N   . THR A 1 280 ? -3.418  -38.477 -63.952 1.00 50.73  ? 279 THR A N   1 
ATOM 2073 C CA  . THR A 1 280 ? -3.101  -39.466 -64.979 1.00 46.14  ? 279 THR A CA  1 
ATOM 2074 C C   . THR A 1 280 ? -4.221  -40.487 -65.129 1.00 47.97  ? 279 THR A C   1 
ATOM 2075 O O   . THR A 1 280 ? -4.630  -40.808 -66.252 1.00 50.52  ? 279 THR A O   1 
ATOM 2076 C CB  . THR A 1 280 ? -1.784  -40.168 -64.650 1.00 45.63  ? 279 THR A CB  1 
ATOM 2077 O OG1 . THR A 1 280 ? -0.773  -39.188 -64.384 1.00 48.40  ? 279 THR A OG1 1 
ATOM 2078 C CG2 . THR A 1 280 ? -1.341  -41.050 -65.809 1.00 44.59  ? 279 THR A CG2 1 
ATOM 2079 N N   . LEU A 1 281 ? -4.730  -41.007 -64.010 1.00 44.36  ? 280 LEU A N   1 
ATOM 2080 C CA  . LEU A 1 281 ? -5.812  -41.981 -64.074 1.00 44.38  ? 280 LEU A CA  1 
ATOM 2081 C C   . LEU A 1 281 ? -7.112  -41.367 -64.574 1.00 47.29  ? 280 LEU A C   1 
ATOM 2082 O O   . LEU A 1 281 ? -7.956  -42.090 -65.115 1.00 50.43  ? 280 LEU A O   1 
ATOM 2083 C CB  . LEU A 1 281 ? -6.024  -42.620 -62.701 1.00 38.23  ? 280 LEU A CB  1 
ATOM 2084 C CG  . LEU A 1 281 ? -4.927  -43.585 -62.247 1.00 35.47  ? 280 LEU A CG  1 
ATOM 2085 C CD1 . LEU A 1 281 ? -5.318  -44.275 -60.950 1.00 37.39  ? 280 LEU A CD1 1 
ATOM 2086 C CD2 . LEU A 1 281 ? -4.624  -44.606 -63.333 1.00 39.78  ? 280 LEU A CD2 1 
ATOM 2087 N N   . SER A 1 282 ? -7.291  -40.054 -64.417 1.00 44.49  ? 281 SER A N   1 
ATOM 2088 C CA  . SER A 1 282 ? -8.494  -39.414 -64.938 1.00 48.30  ? 281 SER A CA  1 
ATOM 2089 C C   . SER A 1 282 ? -8.461  -39.304 -66.458 1.00 48.44  ? 281 SER A C   1 
ATOM 2090 O O   . SER A 1 282 ? -9.514  -39.355 -67.103 1.00 49.23  ? 281 SER A O   1 
ATOM 2091 C CB  . SER A 1 282 ? -8.672  -38.035 -64.304 1.00 43.51  ? 281 SER A CB  1 
ATOM 2092 O OG  . SER A 1 282 ? -7.645  -37.153 -64.717 1.00 48.27  ? 281 SER A OG  1 
ATOM 2093 N N   . ARG A 1 283 ? -7.272  -39.152 -67.048 1.00 48.67  ? 282 ARG A N   1 
ATOM 2094 C CA  . ARG A 1 283 ? -7.170  -39.090 -68.502 1.00 49.14  ? 282 ARG A CA  1 
ATOM 2095 C C   . ARG A 1 283 ? -7.328  -40.462 -69.142 1.00 55.58  ? 282 ARG A C   1 
ATOM 2096 O O   . ARG A 1 283 ? -7.798  -40.559 -70.282 1.00 57.09  ? 282 ARG A O   1 
ATOM 2097 C CB  . ARG A 1 283 ? -5.829  -38.480 -68.919 1.00 55.15  ? 282 ARG A CB  1 
ATOM 2098 C CG  . ARG A 1 283 ? -5.502  -37.154 -68.255 1.00 52.19  ? 282 ARG A CG  1 
ATOM 2099 C CD  . ARG A 1 283 ? -5.085  -36.106 -69.275 1.00 60.44  ? 282 ARG A CD  1 
ATOM 2100 N NE  . ARG A 1 283 ? -3.890  -36.484 -70.021 1.00 64.50  ? 282 ARG A NE  1 
ATOM 2101 C CZ  . ARG A 1 283 ? -2.729  -35.847 -69.948 1.00 62.39  ? 282 ARG A CZ  1 
ATOM 2102 N NH1 . ARG A 1 283 ? -2.562  -34.805 -69.149 1.00 63.07  ? 282 ARG A NH1 1 
ATOM 2103 N NH2 . ARG A 1 283 ? -1.711  -36.264 -70.695 1.00 62.18  ? 282 ARG A NH2 1 
ATOM 2104 N N   . LEU A 1 284 ? -6.941  -41.520 -68.434 1.00 52.74  ? 283 LEU A N   1 
ATOM 2105 C CA  . LEU A 1 284 ? -7.042  -42.872 -68.963 1.00 48.57  ? 283 LEU A CA  1 
ATOM 2106 C C   . LEU A 1 284 ? -8.491  -43.340 -68.925 1.00 52.37  ? 283 LEU A C   1 
ATOM 2107 O O   . LEU A 1 284 ? -9.143  -43.286 -67.878 1.00 57.23  ? 283 LEU A O   1 
ATOM 2108 C CB  . LEU A 1 284 ? -6.158  -43.822 -68.159 1.00 46.97  ? 283 LEU A CB  1 
ATOM 2109 C CG  . LEU A 1 284 ? -4.656  -43.554 -68.249 1.00 46.66  ? 283 LEU A CG  1 
ATOM 2110 C CD1 . LEU A 1 284 ? -3.877  -44.624 -67.499 1.00 48.40  ? 283 LEU A CD1 1 
ATOM 2111 C CD2 . LEU A 1 284 ? -4.213  -43.471 -69.699 1.00 47.51  ? 283 LEU A CD2 1 
ATOM 2112 N N   . THR A 1 285 ? -8.993  -43.800 -70.070 1.00 56.34  ? 284 THR A N   1 
ATOM 2113 C CA  . THR A 1 285 ? -10.367 -44.268 -70.188 1.00 60.82  ? 284 THR A CA  1 
ATOM 2114 C C   . THR A 1 285 ? -10.468 -45.753 -70.505 1.00 65.39  ? 284 THR A C   1 
ATOM 2115 O O   . THR A 1 285 ? -11.581 -46.289 -70.544 1.00 67.97  ? 284 THR A O   1 
ATOM 2116 C CB  . THR A 1 285 ? -11.113 -43.465 -71.261 1.00 61.24  ? 284 THR A CB  1 
ATOM 2117 O OG1 . THR A 1 285 ? -10.414 -43.565 -72.509 1.00 53.41  ? 284 THR A OG1 1 
ATOM 2118 C CG2 . THR A 1 285 ? -11.217 -42.001 -70.857 1.00 58.17  ? 284 THR A CG2 1 
ATOM 2119 N N   . GLU A 1 286 ? -9.346  -46.430 -70.736 1.00 66.77  ? 285 GLU A N   1 
ATOM 2120 C CA  . GLU A 1 286 ? -9.331  -47.855 -71.033 1.00 68.32  ? 285 GLU A CA  1 
ATOM 2121 C C   . GLU A 1 286 ? -8.810  -48.628 -69.830 1.00 67.18  ? 285 GLU A C   1 
ATOM 2122 O O   . GLU A 1 286 ? -7.845  -48.211 -69.181 1.00 66.91  ? 285 GLU A O   1 
ATOM 2123 C CB  . GLU A 1 286 ? -8.464  -48.156 -72.259 1.00 72.83  ? 285 GLU A CB  1 
ATOM 2124 C CG  . GLU A 1 286 ? -9.221  -48.131 -73.577 1.00 77.69  ? 285 GLU A CG  1 
ATOM 2125 C CD  . GLU A 1 286 ? -10.376 -49.115 -73.612 1.00 85.68  ? 285 GLU A CD  1 
ATOM 2126 O OE1 . GLU A 1 286 ? -10.257 -50.206 -73.010 1.00 85.88  ? 285 GLU A OE1 1 
ATOM 2127 O OE2 . GLU A 1 286 ? -11.407 -48.795 -74.239 1.00 84.67  ? 285 GLU A OE2 1 
ATOM 2128 N N   . LYS A 1 287 ? -9.453  -49.761 -69.540 1.00 64.91  ? 286 LYS A N   1 
ATOM 2129 C CA  . LYS A 1 287 ? -9.041  -50.580 -68.407 1.00 59.97  ? 286 LYS A CA  1 
ATOM 2130 C C   . LYS A 1 287 ? -7.656  -51.185 -68.601 1.00 57.70  ? 286 LYS A C   1 
ATOM 2131 O O   . LYS A 1 287 ? -6.997  -51.519 -67.611 1.00 59.41  ? 286 LYS A O   1 
ATOM 2132 C CB  . LYS A 1 287 ? -10.068 -51.686 -68.157 1.00 56.04  ? 286 LYS A CB  1 
ATOM 2133 C CG  . LYS A 1 287 ? -11.335 -51.206 -67.464 1.00 54.50  ? 286 LYS A CG  1 
ATOM 2134 C CD  . LYS A 1 287 ? -12.059 -52.348 -66.762 1.00 57.63  ? 286 LYS A CD  1 
ATOM 2135 C CE  . LYS A 1 287 ? -13.359 -52.703 -67.473 1.00 57.94  ? 286 LYS A CE  1 
ATOM 2136 N NZ  . LYS A 1 287 ? -13.658 -54.164 -67.418 1.00 58.22  ? 286 LYS A NZ  1 
ATOM 2137 N N   . ARG A 1 288 ? -7.201  -51.328 -69.847 1.00 59.39  ? 287 ARG A N   1 
ATOM 2138 C CA  . ARG A 1 288 ? -5.861  -51.853 -70.092 1.00 59.51  ? 287 ARG A CA  1 
ATOM 2139 C C   . ARG A 1 288 ? -4.795  -50.874 -69.621 1.00 59.06  ? 287 ARG A C   1 
ATOM 2140 O O   . ARG A 1 288 ? -3.827  -51.263 -68.958 1.00 55.38  ? 287 ARG A O   1 
ATOM 2141 C CB  . ARG A 1 288 ? -5.683  -52.161 -71.578 1.00 62.28  ? 287 ARG A CB  1 
ATOM 2142 C CG  . ARG A 1 288 ? -6.857  -52.874 -72.209 1.00 58.09  ? 287 ARG A CG  1 
ATOM 2143 C CD  . ARG A 1 288 ? -6.643  -53.030 -73.711 1.00 60.21  ? 287 ARG A CD  1 
ATOM 2144 N NE  . ARG A 1 288 ? -7.371  -54.147 -74.309 1.00 65.72  ? 287 ARG A NE  1 
ATOM 2145 C CZ  . ARG A 1 288 ? -7.345  -55.405 -73.884 1.00 66.64  ? 287 ARG A CZ  1 
ATOM 2146 N NH1 . ARG A 1 288 ? -6.559  -55.792 -72.890 1.00 62.37  ? 287 ARG A NH1 1 
ATOM 2147 N NH2 . ARG A 1 288 ? -8.119  -56.306 -74.484 1.00 65.75  ? 287 ARG A NH2 1 
ATOM 2148 N N   . ASP A 1 289 ? -4.956  -49.594 -69.966 1.00 69.96  ? 288 ASP A N   1 
ATOM 2149 C CA  . ASP A 1 289 ? -4.008  -48.579 -69.524 1.00 67.95  ? 288 ASP A CA  1 
ATOM 2150 C C   . ASP A 1 289 ? -4.181  -48.258 -68.047 1.00 66.20  ? 288 ASP A C   1 
ATOM 2151 O O   . ASP A 1 289 ? -3.211  -47.885 -67.378 1.00 68.03  ? 288 ASP A O   1 
ATOM 2152 C CB  . ASP A 1 289 ? -4.167  -47.308 -70.359 1.00 67.63  ? 288 ASP A CB  1 
ATOM 2153 C CG  . ASP A 1 289 ? -4.256  -47.593 -71.846 1.00 76.73  ? 288 ASP A CG  1 
ATOM 2154 O OD1 . ASP A 1 289 ? -3.270  -48.104 -72.420 1.00 75.48  ? 288 ASP A OD1 1 
ATOM 2155 O OD2 . ASP A 1 289 ? -5.314  -47.301 -72.442 1.00 78.40  ? 288 ASP A OD2 1 
ATOM 2156 N N   . ILE A 1 290 ? -5.403  -48.385 -67.527 1.00 58.58  ? 289 ILE A N   1 
ATOM 2157 C CA  . ILE A 1 290 ? -5.622  -48.173 -66.101 1.00 53.64  ? 289 ILE A CA  1 
ATOM 2158 C C   . ILE A 1 290 ? -4.917  -49.255 -65.293 1.00 51.59  ? 289 ILE A C   1 
ATOM 2159 O O   . ILE A 1 290 ? -4.288  -48.972 -64.267 1.00 49.59  ? 289 ILE A O   1 
ATOM 2160 C CB  . ILE A 1 290 ? -7.130  -48.119 -65.795 1.00 55.00  ? 289 ILE A CB  1 
ATOM 2161 C CG1 . ILE A 1 290 ? -7.672  -46.713 -66.055 1.00 53.30  ? 289 ILE A CG1 1 
ATOM 2162 C CG2 . ILE A 1 290 ? -7.410  -48.529 -64.356 1.00 53.71  ? 289 ILE A CG2 1 
ATOM 2163 C CD1 . ILE A 1 290 ? -9.180  -46.633 -66.050 1.00 50.46  ? 289 ILE A CD1 1 
ATOM 2164 N N   . THR A 1 291 ? -4.997  -50.508 -65.750 1.00 49.83  ? 290 THR A N   1 
ATOM 2165 C CA  . THR A 1 291 ? -4.303  -51.592 -65.061 1.00 51.44  ? 290 THR A CA  1 
ATOM 2166 C C   . THR A 1 291 ? -2.792  -51.414 -65.132 1.00 50.19  ? 290 THR A C   1 
ATOM 2167 O O   . THR A 1 291 ? -2.081  -51.695 -64.161 1.00 48.72  ? 290 THR A O   1 
ATOM 2168 C CB  . THR A 1 291 ? -4.711  -52.940 -65.655 1.00 55.04  ? 290 THR A CB  1 
ATOM 2169 O OG1 . THR A 1 291 ? -6.119  -52.943 -65.922 1.00 58.33  ? 290 THR A OG1 1 
ATOM 2170 C CG2 . THR A 1 291 ? -4.374  -54.072 -64.694 1.00 54.77  ? 290 THR A CG2 1 
ATOM 2171 N N   . ARG A 1 292 ? -2.283  -50.945 -66.274 1.00 49.92  ? 291 ARG A N   1 
ATOM 2172 C CA  . ARG A 1 292 ? -0.846  -50.730 -66.407 1.00 49.89  ? 291 ARG A CA  1 
ATOM 2173 C C   . ARG A 1 292 ? -0.369  -49.608 -65.491 1.00 46.12  ? 291 ARG A C   1 
ATOM 2174 O O   . ARG A 1 292 ? 0.704   -49.709 -64.885 1.00 44.28  ? 291 ARG A O   1 
ATOM 2175 C CB  . ARG A 1 292 ? -0.496  -50.428 -67.866 1.00 50.22  ? 291 ARG A CB  1 
ATOM 2176 C CG  . ARG A 1 292 ? 0.881   -50.921 -68.302 1.00 49.90  ? 291 ARG A CG  1 
ATOM 2177 C CD  . ARG A 1 292 ? 0.828   -52.359 -68.810 1.00 54.01  ? 291 ARG A CD  1 
ATOM 2178 N NE  . ARG A 1 292 ? 2.153   -52.969 -68.852 1.00 53.90  ? 291 ARG A NE  1 
ATOM 2179 C CZ  . ARG A 1 292 ? 2.383   -54.254 -69.083 1.00 49.82  ? 291 ARG A CZ  1 
ATOM 2180 N NH1 . ARG A 1 292 ? 1.394   -55.104 -69.308 1.00 47.95  ? 291 ARG A NH1 1 
ATOM 2181 N NH2 . ARG A 1 292 ? 3.636   -54.699 -69.083 1.00 52.57  ? 291 ARG A NH2 1 
ATOM 2182 N N   . GLU A 1 293 ? -1.158  -48.538 -65.366 1.00 43.41  ? 292 GLU A N   1 
ATOM 2183 C CA  . GLU A 1 293 ? -0.749  -47.412 -64.532 1.00 47.04  ? 292 GLU A CA  1 
ATOM 2184 C C   . GLU A 1 293 ? -0.844  -47.754 -63.049 1.00 47.37  ? 292 GLU A C   1 
ATOM 2185 O O   . GLU A 1 293 ? 0.020   -47.357 -62.258 1.00 42.27  ? 292 GLU A O   1 
ATOM 2186 C CB  . GLU A 1 293 ? -1.600  -46.185 -64.858 1.00 47.38  ? 292 GLU A CB  1 
ATOM 2187 C CG  . GLU A 1 293 ? -0.993  -44.869 -64.400 1.00 51.17  ? 292 GLU A CG  1 
ATOM 2188 C CD  . GLU A 1 293 ? 0.193   -44.444 -65.247 1.00 57.54  ? 292 GLU A CD  1 
ATOM 2189 O OE1 . GLU A 1 293 ? 0.027   -44.293 -66.477 1.00 64.52  ? 292 GLU A OE1 1 
ATOM 2190 O OE2 . GLU A 1 293 ? 1.291   -44.260 -64.679 1.00 52.52  ? 292 GLU A OE2 1 
ATOM 2191 N N   . VAL A 1 294 ? -1.885  -48.488 -62.655 1.00 46.79  ? 293 VAL A N   1 
ATOM 2192 C CA  . VAL A 1 294 ? -2.043  -48.866 -61.255 1.00 40.38  ? 293 VAL A CA  1 
ATOM 2193 C C   . VAL A 1 294 ? -0.958  -49.851 -60.840 1.00 44.40  ? 293 VAL A C   1 
ATOM 2194 O O   . VAL A 1 294 ? -0.367  -49.727 -59.759 1.00 50.58  ? 293 VAL A O   1 
ATOM 2195 C CB  . VAL A 1 294 ? -3.452  -49.438 -61.016 1.00 43.63  ? 293 VAL A CB  1 
ATOM 2196 C CG1 . VAL A 1 294 ? -3.496  -50.228 -59.718 1.00 45.76  ? 293 VAL A CG1 1 
ATOM 2197 C CG2 . VAL A 1 294 ? -4.479  -48.316 -60.999 1.00 40.73  ? 293 VAL A CG2 1 
ATOM 2198 N N   . VAL A 1 295 ? -0.676  -50.844 -61.686 1.00 45.96  ? 294 VAL A N   1 
ATOM 2199 C CA  . VAL A 1 295 ? 0.375   -51.806 -61.370 1.00 44.04  ? 294 VAL A CA  1 
ATOM 2200 C C   . VAL A 1 295 ? 1.734   -51.116 -61.334 1.00 45.66  ? 294 VAL A C   1 
ATOM 2201 O O   . VAL A 1 295 ? 2.563   -51.393 -60.458 1.00 43.61  ? 294 VAL A O   1 
ATOM 2202 C CB  . VAL A 1 295 ? 0.346   -52.973 -62.375 1.00 39.41  ? 294 VAL A CB  1 
ATOM 2203 C CG1 . VAL A 1 295 ? 1.641   -53.768 -62.319 1.00 34.73  ? 294 VAL A CG1 1 
ATOM 2204 C CG2 . VAL A 1 295 ? -0.848  -53.876 -62.101 1.00 37.64  ? 294 VAL A CG2 1 
ATOM 2205 N N   . LYS A 1 296 ? 1.977   -50.193 -62.268 1.00 43.47  ? 295 LYS A N   1 
ATOM 2206 C CA  . LYS A 1 296 ? 3.252   -49.483 -62.284 1.00 44.49  ? 295 LYS A CA  1 
ATOM 2207 C C   . LYS A 1 296 ? 3.423   -48.632 -61.030 1.00 44.06  ? 295 LYS A C   1 
ATOM 2208 O O   . LYS A 1 296 ? 4.525   -48.544 -60.476 1.00 42.75  ? 295 LYS A O   1 
ATOM 2209 C CB  . LYS A 1 296 ? 3.360   -48.621 -63.543 1.00 40.86  ? 295 LYS A CB  1 
ATOM 2210 C CG  . LYS A 1 296 ? 4.436   -47.550 -63.473 1.00 46.76  ? 295 LYS A CG  1 
ATOM 2211 C CD  . LYS A 1 296 ? 4.866   -47.089 -64.855 1.00 50.84  ? 295 LYS A CD  1 
ATOM 2212 C CE  . LYS A 1 296 ? 3.909   -46.047 -65.406 1.00 52.19  ? 295 LYS A CE  1 
ATOM 2213 N NZ  . LYS A 1 296 ? 4.636   -44.869 -65.951 1.00 53.46  ? 295 LYS A NZ  1 
ATOM 2214 N N   . SER A 1 297 ? 2.340   -48.005 -60.563 1.00 45.43  ? 296 SER A N   1 
ATOM 2215 C CA  . SER A 1 297 ? 2.420   -47.207 -59.343 1.00 43.89  ? 296 SER A CA  1 
ATOM 2216 C C   . SER A 1 297 ? 2.693   -48.085 -58.128 1.00 43.84  ? 296 SER A C   1 
ATOM 2217 O O   . SER A 1 297 ? 3.464   -47.703 -57.240 1.00 44.98  ? 296 SER A O   1 
ATOM 2218 C CB  . SER A 1 297 ? 1.131   -46.406 -59.153 1.00 42.49  ? 296 SER A CB  1 
ATOM 2219 O OG  . SER A 1 297 ? 0.846   -45.619 -60.298 1.00 45.80  ? 296 SER A OG  1 
ATOM 2220 N N   . LEU A 1 298 ? 2.075   -49.268 -58.074 1.00 43.27  ? 297 LEU A N   1 
ATOM 2221 C CA  . LEU A 1 298 ? 2.333   -50.185 -56.970 1.00 43.70  ? 297 LEU A CA  1 
ATOM 2222 C C   . LEU A 1 298 ? 3.765   -50.706 -56.994 1.00 46.01  ? 297 LEU A C   1 
ATOM 2223 O O   . LEU A 1 298 ? 4.337   -50.989 -55.935 1.00 45.53  ? 297 LEU A O   1 
ATOM 2224 C CB  . LEU A 1 298 ? 1.341   -51.348 -57.013 1.00 41.56  ? 297 LEU A CB  1 
ATOM 2225 C CG  . LEU A 1 298 ? -0.083  -51.013 -56.567 1.00 45.86  ? 297 LEU A CG  1 
ATOM 2226 C CD1 . LEU A 1 298 ? -1.001  -52.206 -56.756 1.00 43.87  ? 297 LEU A CD1 1 
ATOM 2227 C CD2 . LEU A 1 298 ? -0.097  -50.545 -55.117 1.00 43.67  ? 297 LEU A CD2 1 
ATOM 2228 N N   . LYS A 1 299 ? 4.360   -50.835 -58.184 1.00 44.63  ? 298 LYS A N   1 
ATOM 2229 C CA  . LYS A 1 299 ? 5.741   -51.296 -58.288 1.00 44.43  ? 298 LYS A CA  1 
ATOM 2230 C C   . LYS A 1 299 ? 6.731   -50.301 -57.699 1.00 44.23  ? 298 LYS A C   1 
ATOM 2231 O O   . LYS A 1 299 ? 7.848   -50.692 -57.345 1.00 45.75  ? 298 LYS A O   1 
ATOM 2232 C CB  . LYS A 1 299 ? 6.104   -51.566 -59.750 1.00 51.65  ? 298 LYS A CB  1 
ATOM 2233 C CG  . LYS A 1 299 ? 6.064   -53.033 -60.163 1.00 49.28  ? 298 LYS A CG  1 
ATOM 2234 C CD  . LYS A 1 299 ? 6.329   -53.189 -61.656 1.00 48.07  ? 298 LYS A CD  1 
ATOM 2235 C CE  . LYS A 1 299 ? 5.213   -53.957 -62.350 1.00 51.17  ? 298 LYS A CE  1 
ATOM 2236 N NZ  . LYS A 1 299 ? 5.369   -53.963 -63.836 1.00 53.76  ? 298 LYS A NZ  1 
ATOM 2237 N N   . PHE A 1 300 ? 6.353   -49.029 -57.592 1.00 47.24  ? 299 PHE A N   1 
ATOM 2238 C CA  . PHE A 1 300 ? 7.235   -47.986 -57.084 1.00 50.04  ? 299 PHE A CA  1 
ATOM 2239 C C   . PHE A 1 300 ? 6.949   -47.635 -55.630 1.00 48.70  ? 299 PHE A C   1 
ATOM 2240 O O   . PHE A 1 300 ? 7.877   -47.536 -54.822 1.00 45.04  ? 299 PHE A O   1 
ATOM 2241 C CB  . PHE A 1 300 ? 7.115   -46.731 -57.957 1.00 52.81  ? 299 PHE A CB  1 
ATOM 2242 C CG  . PHE A 1 300 ? 7.664   -45.487 -57.314 1.00 55.89  ? 299 PHE A CG  1 
ATOM 2243 C CD1 . PHE A 1 300 ? 9.030   -45.295 -57.199 1.00 54.46  ? 299 PHE A CD1 1 
ATOM 2244 C CD2 . PHE A 1 300 ? 6.810   -44.509 -56.828 1.00 54.33  ? 299 PHE A CD2 1 
ATOM 2245 C CE1 . PHE A 1 300 ? 9.536   -44.152 -56.610 1.00 52.52  ? 299 PHE A CE1 1 
ATOM 2246 C CE2 . PHE A 1 300 ? 7.310   -43.364 -56.238 1.00 54.88  ? 299 PHE A CE2 1 
ATOM 2247 C CZ  . PHE A 1 300 ? 8.674   -43.185 -56.129 1.00 53.36  ? 299 PHE A CZ  1 
ATOM 2248 N N   . VAL A 1 301 ? 5.675   -47.450 -55.278 1.00 50.97  ? 300 VAL A N   1 
ATOM 2249 C CA  . VAL A 1 301 ? 5.348   -46.965 -53.943 1.00 51.30  ? 300 VAL A CA  1 
ATOM 2250 C C   . VAL A 1 301 ? 5.536   -48.057 -52.900 1.00 52.48  ? 300 VAL A C   1 
ATOM 2251 O O   . VAL A 1 301 ? 5.886   -47.766 -51.750 1.00 55.33  ? 300 VAL A O   1 
ATOM 2252 C CB  . VAL A 1 301 ? 3.918   -46.393 -53.917 1.00 51.19  ? 300 VAL A CB  1 
ATOM 2253 C CG1 . VAL A 1 301 ? 3.758   -45.335 -54.994 1.00 53.76  ? 300 VAL A CG1 1 
ATOM 2254 C CG2 . VAL A 1 301 ? 2.884   -47.497 -54.089 1.00 52.14  ? 300 VAL A CG2 1 
ATOM 2255 N N   . LEU A 1 302 ? 5.325   -49.326 -53.271 1.00 49.78  ? 301 LEU A N   1 
ATOM 2256 C CA  . LEU A 1 302 ? 5.446   -50.394 -52.280 1.00 47.07  ? 301 LEU A CA  1 
ATOM 2257 C C   . LEU A 1 302 ? 6.876   -50.554 -51.782 1.00 47.78  ? 301 LEU A C   1 
ATOM 2258 O O   . LEU A 1 302 ? 7.077   -50.591 -50.555 1.00 50.21  ? 301 LEU A O   1 
ATOM 2259 C CB  . LEU A 1 302 ? 4.879   -51.700 -52.843 1.00 44.18  ? 301 LEU A CB  1 
ATOM 2260 C CG  . LEU A 1 302 ? 3.355   -51.795 -52.860 1.00 43.64  ? 301 LEU A CG  1 
ATOM 2261 C CD1 . LEU A 1 302 ? 2.924   -53.166 -53.341 1.00 41.77  ? 301 LEU A CD1 1 
ATOM 2262 C CD2 . LEU A 1 302 ? 2.779   -51.497 -51.482 1.00 41.86  ? 301 LEU A CD2 1 
ATOM 2263 N N   . PRO A 1 303 ? 7.904   -50.646 -52.635 1.00 49.79  ? 302 PRO A N   1 
ATOM 2264 C CA  . PRO A 1 303 ? 9.270   -50.655 -52.092 1.00 49.02  ? 302 PRO A CA  1 
ATOM 2265 C C   . PRO A 1 303 ? 9.665   -49.328 -51.473 1.00 48.52  ? 302 PRO A C   1 
ATOM 2266 O O   . PRO A 1 303 ? 10.503  -49.307 -50.563 1.00 47.20  ? 302 PRO A O   1 
ATOM 2267 C CB  . PRO A 1 303 ? 10.140  -50.991 -53.314 1.00 44.89  ? 302 PRO A CB  1 
ATOM 2268 C CG  . PRO A 1 303 ? 9.197   -51.565 -54.321 1.00 47.53  ? 302 PRO A CG  1 
ATOM 2269 C CD  . PRO A 1 303 ? 7.914   -50.834 -54.097 1.00 47.17  ? 302 PRO A CD  1 
ATOM 2270 N N   . ALA A 1 304 ? 9.082   -48.218 -51.934 1.00 50.04  ? 303 ALA A N   1 
ATOM 2271 C CA  . ALA A 1 304 ? 9.429   -46.913 -51.381 1.00 49.75  ? 303 ALA A CA  1 
ATOM 2272 C C   . ALA A 1 304 ? 8.944   -46.781 -49.944 1.00 54.69  ? 303 ALA A C   1 
ATOM 2273 O O   . ALA A 1 304 ? 9.706   -46.384 -49.054 1.00 51.57  ? 303 ALA A O   1 
ATOM 2274 C CB  . ALA A 1 304 ? 8.844   -45.800 -52.250 1.00 48.35  ? 303 ALA A CB  1 
ATOM 2275 N N   . VAL A 1 305 ? 7.674   -47.109 -49.698 1.00 56.70  ? 304 VAL A N   1 
ATOM 2276 C CA  . VAL A 1 305 ? 7.153   -47.016 -48.340 1.00 56.13  ? 304 VAL A CA  1 
ATOM 2277 C C   . VAL A 1 305 ? 7.800   -48.070 -47.451 1.00 56.26  ? 304 VAL A C   1 
ATOM 2278 O O   . VAL A 1 305 ? 8.012   -47.835 -46.256 1.00 54.99  ? 304 VAL A O   1 
ATOM 2279 C CB  . VAL A 1 305 ? 5.616   -47.133 -48.340 1.00 57.51  ? 304 VAL A CB  1 
ATOM 2280 C CG1 . VAL A 1 305 ? 5.168   -48.521 -48.791 1.00 54.57  ? 304 VAL A CG1 1 
ATOM 2281 C CG2 . VAL A 1 305 ? 5.057   -46.799 -46.968 1.00 54.81  ? 304 VAL A CG2 1 
ATOM 2282 N N   . ALA A 1 306 ? 8.143   -49.233 -48.012 1.00 51.66  ? 305 ALA A N   1 
ATOM 2283 C CA  . ALA A 1 306 ? 8.782   -50.271 -47.211 1.00 51.41  ? 305 ALA A CA  1 
ATOM 2284 C C   . ALA A 1 306 ? 10.193  -49.862 -46.810 1.00 52.86  ? 305 ALA A C   1 
ATOM 2285 O O   . ALA A 1 306 ? 10.615  -50.100 -45.672 1.00 55.43  ? 305 ALA A O   1 
ATOM 2286 C CB  . ALA A 1 306 ? 8.799   -51.594 -47.975 1.00 45.20  ? 305 ALA A CB  1 
ATOM 2287 N N   . ALA A 1 307 ? 10.938  -49.244 -47.729 1.00 49.96  ? 306 ALA A N   1 
ATOM 2288 C CA  . ALA A 1 307 ? 12.267  -48.756 -47.384 1.00 50.58  ? 306 ALA A CA  1 
ATOM 2289 C C   . ALA A 1 307 ? 12.186  -47.600 -46.396 1.00 53.03  ? 306 ALA A C   1 
ATOM 2290 O O   . ALA A 1 307 ? 12.957  -47.547 -45.431 1.00 55.85  ? 306 ALA A O   1 
ATOM 2291 C CB  . ALA A 1 307 ? 13.021  -48.335 -48.645 1.00 45.77  ? 306 ALA A CB  1 
ATOM 2292 N N   . ALA A 1 308 ? 11.254  -46.669 -46.616 1.00 54.09  ? 307 ALA A N   1 
ATOM 2293 C CA  . ALA A 1 308 ? 11.101  -45.545 -45.697 1.00 54.10  ? 307 ALA A CA  1 
ATOM 2294 C C   . ALA A 1 308 ? 10.633  -46.012 -44.325 1.00 57.37  ? 307 ALA A C   1 
ATOM 2295 O O   . ALA A 1 308 ? 11.104  -45.508 -43.299 1.00 54.87  ? 307 ALA A O   1 
ATOM 2296 C CB  . ALA A 1 308 ? 10.128  -44.519 -46.276 1.00 48.10  ? 307 ALA A CB  1 
ATOM 2297 N N   . SER A 1 309 ? 9.708   -46.974 -44.284 1.00 63.81  ? 308 SER A N   1 
ATOM 2298 C CA  . SER A 1 309 ? 9.249   -47.490 -43.000 1.00 59.90  ? 308 SER A CA  1 
ATOM 2299 C C   . SER A 1 309 ? 10.373  -48.200 -42.258 1.00 56.94  ? 308 SER A C   1 
ATOM 2300 O O   . SER A 1 309 ? 10.542  -48.006 -41.049 1.00 58.77  ? 308 SER A O   1 
ATOM 2301 C CB  . SER A 1 309 ? 8.064   -48.432 -43.197 1.00 58.47  ? 308 SER A CB  1 
ATOM 2302 O OG  . SER A 1 309 ? 7.034   -47.799 -43.932 1.00 60.30  ? 308 SER A OG  1 
ATOM 2303 N N   . PHE A 1 310 ? 11.151  -49.024 -42.961 1.00 51.39  ? 309 PHE A N   1 
ATOM 2304 C CA  . PHE A 1 310 ? 12.233  -49.741 -42.295 1.00 51.08  ? 309 PHE A CA  1 
ATOM 2305 C C   . PHE A 1 310 ? 13.220  -48.768 -41.661 1.00 53.13  ? 309 PHE A C   1 
ATOM 2306 O O   . PHE A 1 310 ? 13.593  -48.922 -40.492 1.00 55.41  ? 309 PHE A O   1 
ATOM 2307 C CB  . PHE A 1 310 ? 12.939  -50.674 -43.278 1.00 48.95  ? 309 PHE A CB  1 
ATOM 2308 C CG  . PHE A 1 310 ? 13.884  -51.635 -42.617 1.00 51.63  ? 309 PHE A CG  1 
ATOM 2309 C CD1 . PHE A 1 310 ? 13.445  -52.468 -41.601 1.00 50.72  ? 309 PHE A CD1 1 
ATOM 2310 C CD2 . PHE A 1 310 ? 15.210  -51.702 -43.007 1.00 53.05  ? 309 PHE A CD2 1 
ATOM 2311 C CE1 . PHE A 1 310 ? 14.312  -53.353 -40.986 1.00 52.98  ? 309 PHE A CE1 1 
ATOM 2312 C CE2 . PHE A 1 310 ? 16.082  -52.586 -42.398 1.00 52.32  ? 309 PHE A CE2 1 
ATOM 2313 C CZ  . PHE A 1 310 ? 15.632  -53.412 -41.386 1.00 53.18  ? 309 PHE A CZ  1 
ATOM 2314 N N   . THR A 1 311 ? 13.628  -47.736 -42.407 1.00 49.64  ? 310 THR A N   1 
ATOM 2315 C CA  . THR A 1 311 ? 14.578  -46.768 -41.866 1.00 50.17  ? 310 THR A CA  1 
ATOM 2316 C C   . THR A 1 311 ? 13.995  -46.004 -40.684 1.00 53.34  ? 310 THR A C   1 
ATOM 2317 O O   . THR A 1 311 ? 14.729  -45.639 -39.758 1.00 49.69  ? 310 THR A O   1 
ATOM 2318 C CB  . THR A 1 311 ? 15.023  -45.797 -42.958 1.00 49.96  ? 310 THR A CB  1 
ATOM 2319 O OG1 . THR A 1 311 ? 13.880  -45.122 -43.497 1.00 59.42  ? 310 THR A OG1 1 
ATOM 2320 C CG2 . THR A 1 311 ? 15.738  -46.548 -44.071 1.00 47.34  ? 310 THR A CG2 1 
ATOM 2321 N N   . VAL A 1 312 ? 12.685  -45.752 -40.694 1.00 51.80  ? 311 VAL A N   1 
ATOM 2322 C CA  . VAL A 1 312 ? 12.043  -45.164 -39.524 1.00 49.95  ? 311 VAL A CA  1 
ATOM 2323 C C   . VAL A 1 312 ? 12.103  -46.135 -38.351 1.00 54.68  ? 311 VAL A C   1 
ATOM 2324 O O   . VAL A 1 312 ? 12.296  -45.729 -37.198 1.00 54.97  ? 311 VAL A O   1 
ATOM 2325 C CB  . VAL A 1 312 ? 10.596  -44.755 -39.862 1.00 48.91  ? 311 VAL A CB  1 
ATOM 2326 C CG1 . VAL A 1 312 ? 9.810   -44.441 -38.597 1.00 50.58  ? 311 VAL A CG1 1 
ATOM 2327 C CG2 . VAL A 1 312 ? 10.592  -43.562 -40.804 1.00 51.28  ? 311 VAL A CG2 1 
ATOM 2328 N N   . TRP A 1 313 ? 11.966  -47.435 -38.628 1.00 51.84  ? 312 TRP A N   1 
ATOM 2329 C CA  . TRP A 1 313 ? 12.085  -48.427 -37.566 1.00 47.36  ? 312 TRP A CA  1 
ATOM 2330 C C   . TRP A 1 313 ? 13.510  -48.490 -37.023 1.00 49.78  ? 312 TRP A C   1 
ATOM 2331 O O   . TRP A 1 313 ? 13.708  -48.643 -35.813 1.00 51.65  ? 312 TRP A O   1 
ATOM 2332 C CB  . TRP A 1 313 ? 11.634  -49.799 -38.070 1.00 45.73  ? 312 TRP A CB  1 
ATOM 2333 C CG  . TRP A 1 313 ? 11.674  -50.856 -37.008 1.00 47.87  ? 312 TRP A CG  1 
ATOM 2334 C CD1 . TRP A 1 313 ? 10.794  -51.017 -35.975 1.00 49.32  ? 312 TRP A CD1 1 
ATOM 2335 C CD2 . TRP A 1 313 ? 12.647  -51.899 -36.871 1.00 47.98  ? 312 TRP A CD2 1 
ATOM 2336 N NE1 . TRP A 1 313 ? 11.160  -52.094 -35.204 1.00 49.33  ? 312 TRP A NE1 1 
ATOM 2337 C CE2 . TRP A 1 313 ? 12.294  -52.653 -35.734 1.00 46.35  ? 312 TRP A CE2 1 
ATOM 2338 C CE3 . TRP A 1 313 ? 13.781  -52.269 -37.600 1.00 49.12  ? 312 TRP A CE3 1 
ATOM 2339 C CZ2 . TRP A 1 313 ? 13.035  -53.753 -35.310 1.00 47.01  ? 312 TRP A CZ2 1 
ATOM 2340 C CZ3 . TRP A 1 313 ? 14.514  -53.362 -37.178 1.00 47.64  ? 312 TRP A CZ3 1 
ATOM 2341 C CH2 . TRP A 1 313 ? 14.139  -54.090 -36.043 1.00 47.20  ? 312 TRP A CH2 1 
ATOM 2342 N N   . LEU A 1 314 ? 14.517  -48.366 -37.893 1.00 50.09  ? 313 LEU A N   1 
ATOM 2343 C CA  . LEU A 1 314 ? 15.895  -48.340 -37.406 1.00 48.60  ? 313 LEU A CA  1 
ATOM 2344 C C   . LEU A 1 314 ? 16.184  -47.081 -36.597 1.00 52.57  ? 313 LEU A C   1 
ATOM 2345 O O   . LEU A 1 314 ? 17.068  -47.090 -35.733 1.00 52.26  ? 313 LEU A O   1 
ATOM 2346 C CB  . LEU A 1 314 ? 16.886  -48.453 -38.567 1.00 50.14  ? 313 LEU A CB  1 
ATOM 2347 C CG  . LEU A 1 314 ? 16.603  -49.452 -39.689 1.00 49.74  ? 313 LEU A CG  1 
ATOM 2348 C CD1 . LEU A 1 314 ? 17.335  -49.061 -40.974 1.00 48.28  ? 313 LEU A CD1 1 
ATOM 2349 C CD2 . LEU A 1 314 ? 16.969  -50.860 -39.249 1.00 47.52  ? 313 LEU A CD2 1 
ATOM 2350 N N   . LEU A 1 315 ? 15.455  -45.996 -36.856 1.00 53.26  ? 314 LEU A N   1 
ATOM 2351 C CA  . LEU A 1 315 ? 15.642  -44.734 -36.152 1.00 51.71  ? 314 LEU A CA  1 
ATOM 2352 C C   . LEU A 1 315 ? 14.479  -44.427 -35.212 1.00 54.82  ? 314 LEU A C   1 
ATOM 2353 O O   . LEU A 1 315 ? 14.193  -43.261 -34.930 1.00 54.92  ? 314 LEU A O   1 
ATOM 2354 C CB  . LEU A 1 315 ? 15.837  -43.591 -37.148 1.00 54.85  ? 314 LEU A CB  1 
ATOM 2355 C CG  . LEU A 1 315 ? 17.256  -43.037 -37.298 1.00 59.86  ? 314 LEU A CG  1 
ATOM 2356 C CD1 . LEU A 1 315 ? 18.161  -44.031 -38.014 1.00 51.96  ? 314 LEU A CD1 1 
ATOM 2357 C CD2 . LEU A 1 315 ? 17.236  -41.701 -38.029 1.00 60.34  ? 314 LEU A CD2 1 
ATOM 2358 N N   . ARG A 1 316 ? 13.802  -45.467 -34.715 1.00 54.38  ? 315 ARG A N   1 
ATOM 2359 C CA  . ARG A 1 316 ? 12.656  -45.244 -33.839 1.00 51.93  ? 315 ARG A CA  1 
ATOM 2360 C C   . ARG A 1 316 ? 13.076  -44.660 -32.496 1.00 56.65  ? 315 ARG A C   1 
ATOM 2361 O O   . ARG A 1 316 ? 12.334  -43.862 -31.913 1.00 61.28  ? 315 ARG A O   1 
ATOM 2362 C CB  . ARG A 1 316 ? 11.872  -46.545 -33.641 1.00 47.66  ? 315 ARG A CB  1 
ATOM 2363 C CG  . ARG A 1 316 ? 12.627  -47.669 -32.945 1.00 48.15  ? 315 ARG A CG  1 
ATOM 2364 C CD  . ARG A 1 316 ? 11.936  -49.009 -33.182 1.00 46.49  ? 315 ARG A CD  1 
ATOM 2365 N NE  . ARG A 1 316 ? 12.601  -50.124 -32.515 1.00 46.76  ? 315 ARG A NE  1 
ATOM 2366 C CZ  . ARG A 1 316 ? 13.760  -50.648 -32.892 1.00 51.31  ? 315 ARG A CZ  1 
ATOM 2367 N NH1 . ARG A 1 316 ? 14.431  -50.174 -33.930 1.00 50.40  ? 315 ARG A NH1 1 
ATOM 2368 N NH2 . ARG A 1 316 ? 14.259  -51.676 -32.213 1.00 57.52  ? 315 ARG A NH2 1 
ATOM 2369 N N   . ASP A 1 317 ? 14.253  -45.034 -31.990 1.00 55.54  ? 316 ASP A N   1 
ATOM 2370 C CA  . ASP A 1 317 ? 14.754  -44.405 -30.773 1.00 54.96  ? 316 ASP A CA  1 
ATOM 2371 C C   . ASP A 1 317 ? 15.119  -42.947 -31.015 1.00 60.75  ? 316 ASP A C   1 
ATOM 2372 O O   . ASP A 1 317 ? 14.981  -42.114 -30.114 1.00 65.08  ? 316 ASP A O   1 
ATOM 2373 C CB  . ASP A 1 317 ? 15.962  -45.176 -30.242 1.00 57.18  ? 316 ASP A CB  1 
ATOM 2374 C CG  . ASP A 1 317 ? 15.656  -46.639 -29.984 1.00 55.44  ? 316 ASP A CG  1 
ATOM 2375 O OD1 . ASP A 1 317 ? 14.597  -47.117 -30.443 1.00 55.94  ? 316 ASP A OD1 1 
ATOM 2376 O OD2 . ASP A 1 317 ? 16.479  -47.314 -29.331 1.00 54.68  ? 316 ASP A OD2 1 
ATOM 2377 N N   . PHE A 1 318 ? 15.583  -42.624 -32.222 1.00 69.74  ? 317 PHE A N   1 
ATOM 2378 C CA  . PHE A 1 318 ? 15.900  -41.241 -32.559 1.00 69.11  ? 317 PHE A CA  1 
ATOM 2379 C C   . PHE A 1 318 ? 14.640  -40.382 -32.594 1.00 73.62  ? 317 PHE A C   1 
ATOM 2380 O O   . PHE A 1 318 ? 14.665  -39.212 -32.194 1.00 77.90  ? 317 PHE A O   1 
ATOM 2381 C CB  . PHE A 1 318 ? 16.647  -41.215 -33.895 1.00 71.55  ? 317 PHE A CB  1 
ATOM 2382 C CG  . PHE A 1 318 ? 16.883  -39.838 -34.451 1.00 77.73  ? 317 PHE A CG  1 
ATOM 2383 C CD1 . PHE A 1 318 ? 15.952  -39.242 -35.288 1.00 81.58  ? 317 PHE A CD1 1 
ATOM 2384 C CD2 . PHE A 1 318 ? 18.058  -39.157 -34.171 1.00 81.39  ? 317 PHE A CD2 1 
ATOM 2385 C CE1 . PHE A 1 318 ? 16.176  -37.984 -35.813 1.00 88.08  ? 317 PHE A CE1 1 
ATOM 2386 C CE2 . PHE A 1 318 ? 18.287  -37.898 -34.692 1.00 86.45  ? 317 PHE A CE2 1 
ATOM 2387 C CZ  . PHE A 1 318 ? 17.345  -37.313 -35.516 1.00 94.60  ? 317 PHE A CZ  1 
ATOM 2388 N N   . ALA A 1 319 ? 13.526  -40.955 -33.056 1.00 66.87  ? 318 ALA A N   1 
ATOM 2389 C CA  . ALA A 1 319 ? 12.277  -40.204 -33.142 1.00 64.98  ? 318 ALA A CA  1 
ATOM 2390 C C   . ALA A 1 319 ? 11.692  -39.936 -31.761 1.00 67.98  ? 318 ALA A C   1 
ATOM 2391 O O   . ALA A 1 319 ? 11.150  -38.853 -31.512 1.00 66.28  ? 318 ALA A O   1 
ATOM 2392 C CB  . ALA A 1 319 ? 11.275  -40.960 -34.015 1.00 60.57  ? 318 ALA A CB  1 
ATOM 2393 N N   . ILE A 1 320 ? 11.786  -40.910 -30.852 1.00 66.81  ? 319 ILE A N   1 
ATOM 2394 C CA  . ILE A 1 320 ? 11.253  -40.720 -29.506 1.00 67.88  ? 319 ILE A CA  1 
ATOM 2395 C C   . ILE A 1 320 ? 12.072  -39.685 -28.744 1.00 73.03  ? 319 ILE A C   1 
ATOM 2396 O O   . ILE A 1 320 ? 11.528  -38.928 -27.930 1.00 74.87  ? 319 ILE A O   1 
ATOM 2397 C CB  . ILE A 1 320 ? 11.195  -42.069 -28.759 1.00 66.60  ? 319 ILE A CB  1 
ATOM 2398 C CG1 . ILE A 1 320 ? 10.199  -43.016 -29.432 1.00 58.57  ? 319 ILE A CG1 1 
ATOM 2399 C CG2 . ILE A 1 320 ? 10.809  -41.877 -27.301 1.00 66.28  ? 319 ILE A CG2 1 
ATOM 2400 C CD1 . ILE A 1 320 ? 10.571  -44.480 -29.319 1.00 48.56  ? 319 ILE A CD1 1 
ATOM 2401 N N   . TRP A 1 321 ? 13.380  -39.615 -29.008 1.00 71.90  ? 320 TRP A N   1 
ATOM 2402 C CA  . TRP A 1 321 ? 14.231  -38.657 -28.309 1.00 74.43  ? 320 TRP A CA  1 
ATOM 2403 C C   . TRP A 1 321 ? 13.930  -37.225 -28.738 1.00 75.87  ? 320 TRP A C   1 
ATOM 2404 O O   . TRP A 1 321 ? 13.923  -36.311 -27.905 1.00 77.16  ? 320 TRP A O   1 
ATOM 2405 C CB  . TRP A 1 321 ? 15.704  -38.993 -28.549 1.00 72.12  ? 320 TRP A CB  1 
ATOM 2406 C CG  . TRP A 1 321 ? 16.656  -38.306 -27.611 1.00 73.31  ? 320 TRP A CG  1 
ATOM 2407 C CD1 . TRP A 1 321 ? 16.889  -36.964 -27.513 1.00 68.44  ? 320 TRP A CD1 1 
ATOM 2408 C CD2 . TRP A 1 321 ? 17.506  -38.931 -26.640 1.00 81.15  ? 320 TRP A CD2 1 
ATOM 2409 N NE1 . TRP A 1 321 ? 17.828  -36.715 -26.544 1.00 72.68  ? 320 TRP A NE1 1 
ATOM 2410 C CE2 . TRP A 1 321 ? 18.223  -37.905 -25.991 1.00 82.76  ? 320 TRP A CE2 1 
ATOM 2411 C CE3 . TRP A 1 321 ? 17.730  -40.257 -26.254 1.00 78.90  ? 320 TRP A CE3 1 
ATOM 2412 C CZ2 . TRP A 1 321 ? 19.147  -38.164 -24.980 1.00 79.70  ? 320 TRP A CZ2 1 
ATOM 2413 C CZ3 . TRP A 1 321 ? 18.647  -40.512 -25.250 1.00 69.44  ? 320 TRP A CZ3 1 
ATOM 2414 C CH2 . TRP A 1 321 ? 19.344  -39.471 -24.625 1.00 68.76  ? 320 TRP A CH2 1 
ATOM 2415 N N   . LEU A 1 322 ? 13.675  -37.007 -30.030 1.00 74.61  ? 321 LEU A N   1 
ATOM 2416 C CA  . LEU A 1 322 ? 13.479  -35.651 -30.534 1.00 73.58  ? 321 LEU A CA  1 
ATOM 2417 C C   . LEU A 1 322 ? 12.009  -35.334 -30.784 1.00 70.77  ? 321 LEU A C   1 
ATOM 2418 O O   . LEU A 1 322 ? 11.419  -34.521 -30.065 1.00 69.47  ? 321 LEU A O   1 
ATOM 2419 C CB  . LEU A 1 322 ? 14.280  -35.418 -31.820 1.00 75.86  ? 321 LEU A CB  1 
ATOM 2420 C CG  . LEU A 1 322 ? 15.730  -35.888 -31.971 1.00 78.68  ? 321 LEU A CG  1 
ATOM 2421 C CD1 . LEU A 1 322 ? 16.405  -35.099 -33.087 1.00 78.84  ? 321 LEU A CD1 1 
ATOM 2422 C CD2 . LEU A 1 322 ? 16.508  -35.740 -30.672 1.00 76.45  ? 321 LEU A CD2 1 
ATOM 2423 N N   . LEU A 1 323 ? 11.414  -35.961 -31.806 1.00 73.04  ? 322 LEU A N   1 
ATOM 2424 C CA  . LEU A 1 323 ? 10.040  -35.638 -32.189 1.00 70.51  ? 322 LEU A CA  1 
ATOM 2425 C C   . LEU A 1 323 ? 9.058   -35.882 -31.049 1.00 68.28  ? 322 LEU A C   1 
ATOM 2426 O O   . LEU A 1 323 ? 8.009   -35.232 -30.983 1.00 68.59  ? 322 LEU A O   1 
ATOM 2427 C CB  . LEU A 1 323 ? 9.632   -36.450 -33.420 1.00 66.37  ? 322 LEU A CB  1 
ATOM 2428 C CG  . LEU A 1 323 ? 10.327  -36.096 -34.736 1.00 56.83  ? 322 LEU A CG  1 
ATOM 2429 C CD1 . LEU A 1 323 ? 11.058  -37.305 -35.301 1.00 51.96  ? 322 LEU A CD1 1 
ATOM 2430 C CD2 . LEU A 1 323 ? 9.325   -35.550 -35.741 1.00 58.58  ? 322 LEU A CD2 1 
ATOM 2431 N N   . LEU A 1 324 ? 9.370   -36.812 -30.156 1.00 71.66  ? 323 LEU A N   1 
ATOM 2432 C CA  . LEU A 1 324 ? 8.591   -37.029 -28.948 1.00 72.03  ? 323 LEU A CA  1 
ATOM 2433 C C   . LEU A 1 324 ? 9.379   -36.541 -27.740 1.00 75.11  ? 323 LEU A C   1 
ATOM 2434 O O   . LEU A 1 324 ? 10.572  -36.234 -27.824 1.00 76.89  ? 323 LEU A O   1 
ATOM 2435 C CB  . LEU A 1 324 ? 8.215   -38.509 -28.792 1.00 68.64  ? 323 LEU A CB  1 
ATOM 2436 C CG  . LEU A 1 324 ? 7.251   -39.095 -29.832 1.00 60.67  ? 323 LEU A CG  1 
ATOM 2437 C CD1 . LEU A 1 324 ? 6.262   -38.044 -30.320 1.00 58.16  ? 323 LEU A CD1 1 
ATOM 2438 C CD2 . LEU A 1 324 ? 8.002   -39.719 -31.002 1.00 61.57  ? 323 LEU A CD2 1 
ATOM 2439 N N   . SER A 1 325 ? 8.693   -36.464 -26.604 1.00 75.88  ? 324 SER A N   1 
ATOM 2440 C CA  . SER A 1 325 ? 9.318   -35.969 -25.386 1.00 81.55  ? 324 SER A CA  1 
ATOM 2441 C C   . SER A 1 325 ? 10.180  -37.016 -24.693 1.00 78.70  ? 324 SER A C   1 
ATOM 2442 O O   . SER A 1 325 ? 10.743  -36.719 -23.634 1.00 79.30  ? 324 SER A O   1 
ATOM 2443 C CB  . SER A 1 325 ? 8.248   -35.453 -24.420 1.00 84.75  ? 324 SER A CB  1 
ATOM 2444 O OG  . SER A 1 325 ? 8.835   -34.750 -23.338 1.00 83.32  ? 324 SER A OG  1 
ATOM 2445 N N   . ASN A 1 326 ? 10.301  -38.218 -25.265 1.00 78.03  ? 325 ASN A N   1 
ATOM 2446 C CA  . ASN A 1 326 ? 11.080  -39.306 -24.670 1.00 80.08  ? 325 ASN A CA  1 
ATOM 2447 C C   . ASN A 1 326 ? 10.579  -39.636 -23.265 1.00 84.66  ? 325 ASN A C   1 
ATOM 2448 O O   . ASN A 1 326 ? 11.359  -39.955 -22.365 1.00 91.72  ? 325 ASN A O   1 
ATOM 2449 C CB  . ASN A 1 326 ? 12.575  -38.974 -24.653 1.00 81.96  ? 325 ASN A CB  1 
ATOM 2450 C CG  . ASN A 1 326 ? 13.450  -40.214 -24.612 1.00 78.82  ? 325 ASN A CG  1 
ATOM 2451 O OD1 . ASN A 1 326 ? 13.423  -41.039 -25.525 1.00 79.60  ? 325 ASN A OD1 1 
ATOM 2452 N ND2 . ASN A 1 326 ? 14.232  -40.350 -23.547 1.00 74.78  ? 325 ASN A ND2 1 
ATOM 2453 N N   . LYS A 1 327 ? 9.262   -39.556 -23.077 1.00 81.77  ? 326 LYS A N   1 
ATOM 2454 C CA  . LYS A 1 327 ? 8.659   -39.776 -21.767 1.00 85.30  ? 326 LYS A CA  1 
ATOM 2455 C C   . LYS A 1 327 ? 8.395   -41.253 -21.500 1.00 85.13  ? 326 LYS A C   1 
ATOM 2456 O O   . LYS A 1 327 ? 8.720   -41.759 -20.421 1.00 84.04  ? 326 LYS A O   1 
ATOM 2457 C CB  . LYS A 1 327 ? 7.360   -38.976 -21.647 1.00 80.50  ? 326 LYS A CB  1 
ATOM 2458 C CG  . LYS A 1 327 ? 7.573   -37.492 -21.406 1.00 84.77  ? 326 LYS A CG  1 
ATOM 2459 C CD  . LYS A 1 327 ? 6.267   -36.787 -21.074 1.00 85.77  ? 326 LYS A CD  1 
ATOM 2460 C CE  . LYS A 1 327 ? 6.391   -35.279 -21.238 1.00 78.11  ? 326 LYS A CE  1 
ATOM 2461 N NZ  . LYS A 1 327 ? 7.491   -34.709 -20.411 1.00 76.32  ? 326 LYS A NZ  1 
ATOM 2462 N N   . PHE A 1 328 ? 7.804   -41.953 -22.466 1.00 75.63  ? 327 PHE A N   1 
ATOM 2463 C CA  . PHE A 1 328 ? 7.529   -43.386 -22.370 1.00 66.91  ? 327 PHE A CA  1 
ATOM 2464 C C   . PHE A 1 328 ? 8.302   -44.078 -23.486 1.00 60.55  ? 327 PHE A C   1 
ATOM 2465 O O   . PHE A 1 328 ? 7.751   -44.394 -24.537 1.00 59.57  ? 327 PHE A O   1 
ATOM 2466 C CB  . PHE A 1 328 ? 6.021   -43.664 -22.470 1.00 64.36  ? 327 PHE A CB  1 
ATOM 2467 C CG  . PHE A 1 328 ? 5.185   -42.811 -21.560 1.00 67.68  ? 327 PHE A CG  1 
ATOM 2468 C CD1 . PHE A 1 328 ? 5.290   -42.929 -20.183 1.00 65.68  ? 327 PHE A CD1 1 
ATOM 2469 C CD2 . PHE A 1 328 ? 4.300   -41.883 -22.082 1.00 63.69  ? 327 PHE A CD2 1 
ATOM 2470 C CE1 . PHE A 1 328 ? 4.520   -42.139 -19.346 1.00 65.26  ? 327 PHE A CE1 1 
ATOM 2471 C CE2 . PHE A 1 328 ? 3.530   -41.091 -21.252 1.00 64.72  ? 327 PHE A CE2 1 
ATOM 2472 C CZ  . PHE A 1 328 ? 3.640   -41.218 -19.882 1.00 64.60  ? 327 PHE A CZ  1 
ATOM 2473 N N   . THR A 1 329 ? 9.588   -44.326 -23.253 1.00 58.85  ? 328 THR A N   1 
ATOM 2474 C CA  . THR A 1 329 ? 10.427  -44.944 -24.272 1.00 61.14  ? 328 THR A CA  1 
ATOM 2475 C C   . THR A 1 329 ? 10.023  -46.377 -24.627 1.00 60.11  ? 328 THR A C   1 
ATOM 2476 O O   . THR A 1 329 ? 10.709  -46.981 -25.457 1.00 58.11  ? 328 THR A O   1 
ATOM 2477 C CB  . THR A 1 329 ? 11.886  -44.931 -23.819 1.00 65.86  ? 328 THR A CB  1 
ATOM 2478 O OG1 . THR A 1 329 ? 12.100  -46.007 -22.903 1.00 64.80  ? 328 THR A OG1 1 
ATOM 2479 C CG2 . THR A 1 329 ? 12.230  -43.615 -23.105 1.00 69.09  ? 328 THR A CG2 1 
ATOM 2480 N N   . ALA A 1 330 ? 8.955   -46.941 -24.048 1.00 58.35  ? 329 ALA A N   1 
ATOM 2481 C CA  . ALA A 1 330 ? 8.525   -48.289 -24.404 1.00 51.62  ? 329 ALA A CA  1 
ATOM 2482 C C   . ALA A 1 330 ? 7.691   -48.337 -25.674 1.00 49.78  ? 329 ALA A C   1 
ATOM 2483 O O   . ALA A 1 330 ? 7.363   -49.438 -26.128 1.00 50.75  ? 329 ALA A O   1 
ATOM 2484 C CB  . ALA A 1 330 ? 7.717   -48.923 -23.272 1.00 51.49  ? 329 ALA A CB  1 
ATOM 2485 N N   . MET A 1 331 ? 7.331   -47.189 -26.254 1.00 49.48  ? 330 MET A N   1 
ATOM 2486 C CA  . MET A 1 331 ? 6.536   -47.213 -27.478 1.00 51.46  ? 330 MET A CA  1 
ATOM 2487 C C   . MET A 1 331 ? 7.334   -47.670 -28.687 1.00 45.87  ? 330 MET A C   1 
ATOM 2488 O O   . MET A 1 331 ? 6.759   -47.783 -29.775 1.00 44.85  ? 330 MET A O   1 
ATOM 2489 C CB  . MET A 1 331 ? 5.935   -45.834 -27.759 1.00 51.09  ? 330 MET A CB  1 
ATOM 2490 C CG  . MET A 1 331 ? 6.823   -44.670 -27.367 1.00 52.06  ? 330 MET A CG  1 
ATOM 2491 S SD  . MET A 1 331 ? 6.242   -43.087 -27.999 1.00 54.64  ? 330 MET A SD  1 
ATOM 2492 C CE  . MET A 1 331 ? 6.936   -41.985 -26.768 1.00 59.55  ? 330 MET A CE  1 
ATOM 2493 N N   . ARG A 1 332 ? 8.634   -47.931 -28.526 1.00 46.82  ? 331 ARG A N   1 
ATOM 2494 C CA  . ARG A 1 332 ? 9.441   -48.425 -29.633 1.00 48.64  ? 331 ARG A CA  1 
ATOM 2495 C C   . ARG A 1 332 ? 8.931   -49.759 -30.163 1.00 50.13  ? 331 ARG A C   1 
ATOM 2496 O O   . ARG A 1 332 ? 9.278   -50.138 -31.287 1.00 51.26  ? 331 ARG A O   1 
ATOM 2497 C CB  . ARG A 1 332 ? 10.902  -48.553 -29.198 1.00 47.10  ? 331 ARG A CB  1 
ATOM 2498 C CG  . ARG A 1 332 ? 11.103  -49.419 -27.969 1.00 51.13  ? 331 ARG A CG  1 
ATOM 2499 C CD  . ARG A 1 332 ? 12.493  -49.242 -27.385 1.00 52.38  ? 331 ARG A CD  1 
ATOM 2500 N NE  . ARG A 1 332 ? 13.543  -49.418 -28.382 1.00 50.08  ? 331 ARG A NE  1 
ATOM 2501 C CZ  . ARG A 1 332 ? 14.201  -50.553 -28.581 1.00 51.25  ? 331 ARG A CZ  1 
ATOM 2502 N NH1 . ARG A 1 332 ? 13.915  -51.648 -27.896 1.00 53.80  ? 331 ARG A NH1 1 
ATOM 2503 N NH2 . ARG A 1 332 ? 15.172  -50.589 -29.489 1.00 46.19  ? 331 ARG A NH2 1 
ATOM 2504 N N   . ASP A 1 333 ? 8.117   -50.477 -29.382 1.00 50.28  ? 332 ASP A N   1 
ATOM 2505 C CA  . ASP A 1 333 ? 7.505   -51.716 -29.846 1.00 48.11  ? 332 ASP A CA  1 
ATOM 2506 C C   . ASP A 1 333 ? 6.261   -51.476 -30.685 1.00 47.60  ? 332 ASP A C   1 
ATOM 2507 O O   . ASP A 1 333 ? 5.864   -52.364 -31.448 1.00 59.91  ? 332 ASP A O   1 
ATOM 2508 C CB  . ASP A 1 333 ? 7.143   -52.606 -28.657 1.00 45.09  ? 332 ASP A CB  1 
ATOM 2509 C CG  . ASP A 1 333 ? 8.341   -52.954 -27.804 1.00 49.46  ? 332 ASP A CG  1 
ATOM 2510 O OD1 . ASP A 1 333 ? 9.481   -52.651 -28.214 1.00 51.85  ? 332 ASP A OD1 1 
ATOM 2511 O OD2 . ASP A 1 333 ? 8.140   -53.533 -26.720 1.00 53.86  ? 332 ASP A OD2 1 
ATOM 2512 N N   . LEU A 1 334 ? 5.634   -50.307 -30.555 1.00 46.14  ? 333 LEU A N   1 
ATOM 2513 C CA  . LEU A 1 334 ? 4.470   -49.961 -31.359 1.00 47.74  ? 333 LEU A CA  1 
ATOM 2514 C C   . LEU A 1 334 ? 4.832   -49.576 -32.788 1.00 49.67  ? 333 LEU A C   1 
ATOM 2515 O O   . LEU A 1 334 ? 3.928   -49.405 -33.614 1.00 52.59  ? 333 LEU A O   1 
ATOM 2516 C CB  . LEU A 1 334 ? 3.700   -48.815 -30.694 1.00 43.11  ? 333 LEU A CB  1 
ATOM 2517 C CG  . LEU A 1 334 ? 2.651   -49.183 -29.641 1.00 49.79  ? 333 LEU A CG  1 
ATOM 2518 C CD1 . LEU A 1 334 ? 3.287   -49.413 -28.277 1.00 47.47  ? 333 LEU A CD1 1 
ATOM 2519 C CD2 . LEU A 1 334 ? 1.588   -48.103 -29.556 1.00 47.34  ? 333 LEU A CD2 1 
ATOM 2520 N N   . PHE A 1 335 ? 6.123   -49.449 -33.102 1.00 45.66  ? 334 PHE A N   1 
ATOM 2521 C CA  . PHE A 1 335 ? 6.530   -48.948 -34.411 1.00 52.32  ? 334 PHE A CA  1 
ATOM 2522 C C   . PHE A 1 335 ? 6.319   -49.991 -35.500 1.00 55.75  ? 334 PHE A C   1 
ATOM 2523 O O   . PHE A 1 335 ? 5.688   -49.711 -36.526 1.00 50.61  ? 334 PHE A O   1 
ATOM 2524 C CB  . PHE A 1 335 ? 7.995   -48.517 -34.374 1.00 52.24  ? 334 PHE A CB  1 
ATOM 2525 C CG  . PHE A 1 335 ? 8.201   -47.113 -33.902 1.00 47.60  ? 334 PHE A CG  1 
ATOM 2526 C CD1 . PHE A 1 335 ? 8.028   -46.786 -32.569 1.00 47.98  ? 334 PHE A CD1 1 
ATOM 2527 C CD2 . PHE A 1 335 ? 8.568   -46.120 -34.791 1.00 48.42  ? 334 PHE A CD2 1 
ATOM 2528 C CE1 . PHE A 1 335 ? 8.219   -45.493 -32.130 1.00 48.14  ? 334 PHE A CE1 1 
ATOM 2529 C CE2 . PHE A 1 335 ? 8.764   -44.827 -34.358 1.00 47.88  ? 334 PHE A CE2 1 
ATOM 2530 C CZ  . PHE A 1 335 ? 8.587   -44.511 -33.026 1.00 49.72  ? 334 PHE A CZ  1 
ATOM 2531 N N   . ALA A 1 336 ? 6.853   -51.200 -35.298 1.00 53.21  ? 335 ALA A N   1 
ATOM 2532 C CA  . ALA A 1 336 ? 6.856   -52.202 -36.359 1.00 48.83  ? 335 ALA A CA  1 
ATOM 2533 C C   . ALA A 1 336 ? 5.444   -52.528 -36.828 1.00 54.95  ? 335 ALA A C   1 
ATOM 2534 O O   . ALA A 1 336 ? 5.208   -52.714 -38.028 1.00 60.19  ? 335 ALA A O   1 
ATOM 2535 C CB  . ALA A 1 336 ? 7.569   -53.466 -35.882 1.00 45.30  ? 335 ALA A CB  1 
ATOM 2536 N N   . TRP A 1 337 ? 4.489   -52.590 -35.899 1.00 60.39  ? 336 TRP A N   1 
ATOM 2537 C CA  . TRP A 1 337 ? 3.110   -52.881 -36.277 1.00 60.56  ? 336 TRP A CA  1 
ATOM 2538 C C   . TRP A 1 337 ? 2.510   -51.740 -37.091 1.00 56.59  ? 336 TRP A C   1 
ATOM 2539 O O   . TRP A 1 337 ? 1.893   -51.969 -38.138 1.00 55.42  ? 336 TRP A O   1 
ATOM 2540 C CB  . TRP A 1 337 ? 2.274   -53.156 -35.027 1.00 58.74  ? 336 TRP A CB  1 
ATOM 2541 C CG  . TRP A 1 337 ? 2.829   -54.249 -34.172 1.00 62.21  ? 336 TRP A CG  1 
ATOM 2542 C CD1 . TRP A 1 337 ? 3.662   -54.108 -33.101 1.00 62.30  ? 336 TRP A CD1 1 
ATOM 2543 C CD2 . TRP A 1 337 ? 2.595   -55.654 -34.317 1.00 66.10  ? 336 TRP A CD2 1 
ATOM 2544 N NE1 . TRP A 1 337 ? 3.960   -55.338 -32.568 1.00 64.32  ? 336 TRP A NE1 1 
ATOM 2545 C CE2 . TRP A 1 337 ? 3.318   -56.305 -33.296 1.00 64.93  ? 336 TRP A CE2 1 
ATOM 2546 C CE3 . TRP A 1 337 ? 1.844   -56.425 -35.209 1.00 63.17  ? 336 TRP A CE3 1 
ATOM 2547 C CZ2 . TRP A 1 337 ? 3.312   -57.690 -33.143 1.00 64.99  ? 336 TRP A CZ2 1 
ATOM 2548 C CZ3 . TRP A 1 337 ? 1.839   -57.801 -35.055 1.00 71.67  ? 336 TRP A CZ3 1 
ATOM 2549 C CH2 . TRP A 1 337 ? 2.569   -58.419 -34.030 1.00 68.05  ? 336 TRP A CH2 1 
ATOM 2550 N N   . GLN A 1 338 ? 2.686   -50.501 -36.627 1.00 50.44  ? 337 GLN A N   1 
ATOM 2551 C CA  . GLN A 1 338 ? 2.148   -49.357 -37.356 1.00 51.17  ? 337 GLN A CA  1 
ATOM 2552 C C   . GLN A 1 338 ? 2.832   -49.187 -38.707 1.00 54.15  ? 337 GLN A C   1 
ATOM 2553 O O   . GLN A 1 338 ? 2.179   -48.852 -39.702 1.00 51.67  ? 337 GLN A O   1 
ATOM 2554 C CB  . GLN A 1 338 ? 2.291   -48.087 -36.515 1.00 48.79  ? 337 GLN A CB  1 
ATOM 2555 C CG  . GLN A 1 338 ? 1.975   -46.802 -37.265 1.00 52.18  ? 337 GLN A CG  1 
ATOM 2556 C CD  . GLN A 1 338 ? 0.578   -46.281 -36.980 1.00 53.98  ? 337 GLN A CD  1 
ATOM 2557 O OE1 . GLN A 1 338 ? -0.057  -46.669 -35.997 1.00 52.23  ? 337 GLN A OE1 1 
ATOM 2558 N NE2 . GLN A 1 338 ? 0.089   -45.398 -37.848 1.00 48.33  ? 337 GLN A NE2 1 
ATOM 2559 N N   . LEU A 1 339 ? 4.143   -49.432 -38.765 1.00 58.05  ? 338 LEU A N   1 
ATOM 2560 C CA  . LEU A 1 339 ? 4.888   -49.210 -40.000 1.00 55.65  ? 338 LEU A CA  1 
ATOM 2561 C C   . LEU A 1 339 ? 4.584   -50.275 -41.047 1.00 49.44  ? 338 LEU A C   1 
ATOM 2562 O O   . LEU A 1 339 ? 4.680   -50.003 -42.249 1.00 50.61  ? 338 LEU A O   1 
ATOM 2563 C CB  . LEU A 1 339 ? 6.382   -49.158 -39.692 1.00 54.42  ? 338 LEU A CB  1 
ATOM 2564 C CG  . LEU A 1 339 ? 6.793   -47.941 -38.857 1.00 53.48  ? 338 LEU A CG  1 
ATOM 2565 C CD1 . LEU A 1 339 ? 8.287   -47.720 -38.920 1.00 53.89  ? 338 LEU A CD1 1 
ATOM 2566 C CD2 . LEU A 1 339 ? 6.052   -46.690 -39.306 1.00 55.32  ? 338 LEU A CD2 1 
ATOM 2567 N N   . VAL A 1 340 ? 4.225   -51.488 -40.620 1.00 47.56  ? 339 VAL A N   1 
ATOM 2568 C CA  . VAL A 1 340 ? 3.751   -52.479 -41.579 1.00 46.32  ? 339 VAL A CA  1 
ATOM 2569 C C   . VAL A 1 340 ? 2.387   -52.074 -42.118 1.00 46.73  ? 339 VAL A C   1 
ATOM 2570 O O   . VAL A 1 340 ? 2.129   -52.161 -43.325 1.00 42.83  ? 339 VAL A O   1 
ATOM 2571 C CB  . VAL A 1 340 ? 3.722   -53.882 -40.945 1.00 47.99  ? 339 VAL A CB  1 
ATOM 2572 C CG1 . VAL A 1 340 ? 2.868   -54.824 -41.780 1.00 44.01  ? 339 VAL A CG1 1 
ATOM 2573 C CG2 . VAL A 1 340 ? 5.134   -54.432 -40.817 1.00 39.86  ? 339 VAL A CG2 1 
ATOM 2574 N N   . GLY A 1 341 ? 1.501   -51.602 -41.240 1.00 41.43  ? 340 GLY A N   1 
ATOM 2575 C CA  . GLY A 1 341 ? 0.206   -51.125 -41.692 1.00 44.36  ? 340 GLY A CA  1 
ATOM 2576 C C   . GLY A 1 341 ? 0.299   -49.878 -42.549 1.00 41.45  ? 340 GLY A C   1 
ATOM 2577 O O   . GLY A 1 341 ? -0.584  -49.619 -43.369 1.00 47.78  ? 340 GLY A O   1 
ATOM 2578 N N   . ASP A 1 342 ? 1.362   -49.087 -42.369 1.00 48.30  ? 341 ASP A N   1 
ATOM 2579 C CA  . ASP A 1 342 ? 1.590   -47.936 -43.237 1.00 49.15  ? 341 ASP A CA  1 
ATOM 2580 C C   . ASP A 1 342 ? 1.930   -48.367 -44.657 1.00 42.40  ? 341 ASP A C   1 
ATOM 2581 O O   . ASP A 1 342 ? 1.554   -47.686 -45.619 1.00 42.88  ? 341 ASP A O   1 
ATOM 2582 C CB  . ASP A 1 342 ? 2.718   -47.065 -42.681 1.00 44.44  ? 341 ASP A CB  1 
ATOM 2583 C CG  . ASP A 1 342 ? 2.323   -46.329 -41.415 1.00 47.96  ? 341 ASP A CG  1 
ATOM 2584 O OD1 . ASP A 1 342 ? 1.113   -46.258 -41.114 1.00 49.52  ? 341 ASP A OD1 1 
ATOM 2585 O OD2 . ASP A 1 342 ? 3.226   -45.817 -40.723 1.00 49.15  ? 341 ASP A OD2 1 
ATOM 2586 N N   . VAL A 1 343 ? 2.642   -49.485 -44.804 1.00 43.56  ? 342 VAL A N   1 
ATOM 2587 C CA  . VAL A 1 343 ? 3.033   -49.959 -46.127 1.00 43.85  ? 342 VAL A CA  1 
ATOM 2588 C C   . VAL A 1 343 ? 1.810   -50.424 -46.907 1.00 46.78  ? 342 VAL A C   1 
ATOM 2589 O O   . VAL A 1 343 ? 1.615   -50.051 -48.070 1.00 50.47  ? 342 VAL A O   1 
ATOM 2590 C CB  . VAL A 1 343 ? 4.083   -51.077 -46.003 1.00 41.62  ? 342 VAL A CB  1 
ATOM 2591 C CG1 . VAL A 1 343 ? 4.245   -51.807 -47.329 1.00 37.43  ? 342 VAL A CG1 1 
ATOM 2592 C CG2 . VAL A 1 343 ? 5.410   -50.507 -45.528 1.00 41.68  ? 342 VAL A CG2 1 
ATOM 2593 N N   . LEU A 1 344 ? 0.968   -51.245 -46.280 1.00 43.71  ? 343 LEU A N   1 
ATOM 2594 C CA  . LEU A 1 344 ? -0.219  -51.743 -46.962 1.00 40.04  ? 343 LEU A CA  1 
ATOM 2595 C C   . LEU A 1 344 ? -1.299  -50.681 -47.099 1.00 42.59  ? 343 LEU A C   1 
ATOM 2596 O O   . LEU A 1 344 ? -2.168  -50.812 -47.966 1.00 43.51  ? 343 LEU A O   1 
ATOM 2597 C CB  . LEU A 1 344 ? -0.775  -52.960 -46.228 1.00 41.24  ? 343 LEU A CB  1 
ATOM 2598 C CG  . LEU A 1 344 ? 0.084   -54.215 -46.369 1.00 43.64  ? 343 LEU A CG  1 
ATOM 2599 C CD1 . LEU A 1 344 ? 0.852   -54.484 -45.087 1.00 43.09  ? 343 LEU A CD1 1 
ATOM 2600 C CD2 . LEU A 1 344 ? -0.778  -55.406 -46.749 1.00 49.23  ? 343 LEU A CD2 1 
ATOM 2601 N N   . LYS A 1 345 ? -1.273  -49.639 -46.265 1.00 41.21  ? 344 LYS A N   1 
ATOM 2602 C CA  . LYS A 1 345 ? -2.224  -48.546 -46.437 1.00 44.59  ? 344 LYS A CA  1 
ATOM 2603 C C   . LYS A 1 345 ? -1.851  -47.683 -47.633 1.00 46.70  ? 344 LYS A C   1 
ATOM 2604 O O   . LYS A 1 345 ? -2.730  -47.169 -48.335 1.00 46.14  ? 344 LYS A O   1 
ATOM 2605 C CB  . LYS A 1 345 ? -2.297  -47.695 -45.170 1.00 36.56  ? 344 LYS A CB  1 
ATOM 2606 C CG  . LYS A 1 345 ? -3.387  -46.639 -45.206 1.00 41.29  ? 344 LYS A CG  1 
ATOM 2607 C CD  . LYS A 1 345 ? -3.401  -45.811 -43.937 1.00 42.29  ? 344 LYS A CD  1 
ATOM 2608 C CE  . LYS A 1 345 ? -2.327  -44.739 -43.964 1.00 40.82  ? 344 LYS A CE  1 
ATOM 2609 N NZ  . LYS A 1 345 ? -2.276  -43.995 -42.675 1.00 43.47  ? 344 LYS A NZ  1 
ATOM 2610 N N   . VAL A 1 346 ? -0.551  -47.509 -47.876 1.00 44.57  ? 345 VAL A N   1 
ATOM 2611 C CA  . VAL A 1 346 ? -0.102  -46.754 -49.041 1.00 46.02  ? 345 VAL A CA  1 
ATOM 2612 C C   . VAL A 1 346 ? -0.465  -47.493 -50.324 1.00 46.70  ? 345 VAL A C   1 
ATOM 2613 O O   . VAL A 1 346 ? -0.901  -46.881 -51.307 1.00 43.87  ? 345 VAL A O   1 
ATOM 2614 C CB  . VAL A 1 346 ? 1.411   -46.483 -48.941 1.00 45.74  ? 345 VAL A CB  1 
ATOM 2615 C CG1 . VAL A 1 346 ? 2.019   -46.260 -50.320 1.00 47.02  ? 345 VAL A CG1 1 
ATOM 2616 C CG2 . VAL A 1 346 ? 1.678   -45.292 -48.033 1.00 43.23  ? 345 VAL A CG2 1 
ATOM 2617 N N   . GLY A 1 347 ? -0.309  -48.819 -50.329 1.00 48.04  ? 346 GLY A N   1 
ATOM 2618 C CA  . GLY A 1 347 ? -0.671  -49.591 -51.506 1.00 49.69  ? 346 GLY A CA  1 
ATOM 2619 C C   . GLY A 1 347 ? -2.153  -49.521 -51.819 1.00 48.40  ? 346 GLY A C   1 
ATOM 2620 O O   . GLY A 1 347 ? -2.550  -49.488 -52.987 1.00 53.20  ? 346 GLY A O   1 
ATOM 2621 N N   . ALA A 1 348 ? -2.993  -49.498 -50.782 1.00 44.58  ? 347 ALA A N   1 
ATOM 2622 C CA  . ALA A 1 348 ? -4.429  -49.371 -50.997 1.00 43.60  ? 347 ALA A CA  1 
ATOM 2623 C C   . ALA A 1 348 ? -4.822  -47.971 -51.449 1.00 47.03  ? 347 ALA A C   1 
ATOM 2624 O O   . ALA A 1 348 ? -5.906  -47.800 -52.017 1.00 46.42  ? 347 ALA A O   1 
ATOM 2625 C CB  . ALA A 1 348 ? -5.188  -49.739 -49.722 1.00 42.84  ? 347 ALA A CB  1 
ATOM 2626 N N   . TYR A 1 349 ? -3.969  -46.970 -51.209 1.00 49.19  ? 348 TYR A N   1 
ATOM 2627 C CA  . TYR A 1 349 ? -4.269  -45.612 -51.651 1.00 45.91  ? 348 TYR A CA  1 
ATOM 2628 C C   . TYR A 1 349 ? -4.309  -45.512 -53.170 1.00 49.08  ? 348 TYR A C   1 
ATOM 2629 O O   . TYR A 1 349 ? -5.026  -44.666 -53.715 1.00 51.19  ? 348 TYR A O   1 
ATOM 2630 C CB  . TYR A 1 349 ? -3.237  -44.634 -51.088 1.00 45.67  ? 348 TYR A CB  1 
ATOM 2631 C CG  . TYR A 1 349 ? -3.604  -44.038 -49.748 1.00 50.47  ? 348 TYR A CG  1 
ATOM 2632 C CD1 . TYR A 1 349 ? -4.778  -44.402 -49.100 1.00 55.12  ? 348 TYR A CD1 1 
ATOM 2633 C CD2 . TYR A 1 349 ? -2.777  -43.108 -49.132 1.00 48.74  ? 348 TYR A CD2 1 
ATOM 2634 C CE1 . TYR A 1 349 ? -5.116  -43.856 -47.875 1.00 53.50  ? 348 TYR A CE1 1 
ATOM 2635 C CE2 . TYR A 1 349 ? -3.106  -42.557 -47.908 1.00 51.11  ? 348 TYR A CE2 1 
ATOM 2636 C CZ  . TYR A 1 349 ? -4.275  -42.933 -47.284 1.00 54.81  ? 348 TYR A CZ  1 
ATOM 2637 O OH  . TYR A 1 349 ? -4.604  -42.385 -46.064 1.00 52.42  ? 348 TYR A OH  1 
ATOM 2638 N N   . VAL A 1 350 ? -3.544  -46.360 -53.862 1.00 46.95  ? 349 VAL A N   1 
ATOM 2639 C CA  . VAL A 1 350 ? -3.558  -46.364 -55.322 1.00 41.67  ? 349 VAL A CA  1 
ATOM 2640 C C   . VAL A 1 350 ? -4.946  -46.714 -55.838 1.00 42.25  ? 349 VAL A C   1 
ATOM 2641 O O   . VAL A 1 350 ? -5.477  -46.053 -56.739 1.00 44.97  ? 349 VAL A O   1 
ATOM 2642 C CB  . VAL A 1 350 ? -2.492  -47.336 -55.860 1.00 39.21  ? 349 VAL A CB  1 
ATOM 2643 C CG1 . VAL A 1 350 ? -2.570  -47.427 -57.375 1.00 40.85  ? 349 VAL A CG1 1 
ATOM 2644 C CG2 . VAL A 1 350 ? -1.105  -46.905 -55.407 1.00 41.85  ? 349 VAL A CG2 1 
ATOM 2645 N N   . PHE A 1 351 ? -5.560  -47.755 -55.273 1.00 40.70  ? 350 PHE A N   1 
ATOM 2646 C CA  . PHE A 1 351 ? -6.925  -48.092 -55.657 1.00 38.91  ? 350 PHE A CA  1 
ATOM 2647 C C   . PHE A 1 351 ? -7.910  -47.023 -55.206 1.00 48.71  ? 350 PHE A C   1 
ATOM 2648 O O   . PHE A 1 351 ? -8.937  -46.812 -55.860 1.00 40.19  ? 350 PHE A O   1 
ATOM 2649 C CB  . PHE A 1 351 ? -7.310  -49.454 -55.082 1.00 38.95  ? 350 PHE A CB  1 
ATOM 2650 C CG  . PHE A 1 351 ? -6.419  -50.572 -55.538 1.00 46.80  ? 350 PHE A CG  1 
ATOM 2651 C CD1 . PHE A 1 351 ? -6.400  -50.961 -56.868 1.00 42.96  ? 350 PHE A CD1 1 
ATOM 2652 C CD2 . PHE A 1 351 ? -5.594  -51.228 -54.641 1.00 47.26  ? 350 PHE A CD2 1 
ATOM 2653 C CE1 . PHE A 1 351 ? -5.578  -51.985 -57.292 1.00 44.28  ? 350 PHE A CE1 1 
ATOM 2654 C CE2 . PHE A 1 351 ? -4.770  -52.256 -55.060 1.00 50.73  ? 350 PHE A CE2 1 
ATOM 2655 C CZ  . PHE A 1 351 ? -4.761  -52.634 -56.387 1.00 43.09  ? 350 PHE A CZ  1 
ATOM 2656 N N   . GLY A 1 352 ? -7.613  -46.336 -54.101 1.00 35.33  ? 351 GLY A N   1 
ATOM 2657 C CA  . GLY A 1 352 ? -8.503  -45.286 -53.637 1.00 36.20  ? 351 GLY A CA  1 
ATOM 2658 C C   . GLY A 1 352 ? -8.484  -44.067 -54.538 1.00 41.54  ? 351 GLY A C   1 
ATOM 2659 O O   . GLY A 1 352 ? -9.529  -43.472 -54.814 1.00 44.81  ? 351 GLY A O   1 
ATOM 2660 N N   . TYR A 1 353 ? -7.297  -43.678 -55.011 1.00 48.80  ? 352 TYR A N   1 
ATOM 2661 C CA  . TYR A 1 353 ? -7.203  -42.550 -55.932 1.00 48.13  ? 352 TYR A CA  1 
ATOM 2662 C C   . TYR A 1 353 ? -7.770  -42.898 -57.303 1.00 42.44  ? 352 TYR A C   1 
ATOM 2663 O O   . TYR A 1 353 ? -8.210  -42.005 -58.036 1.00 40.43  ? 352 TYR A O   1 
ATOM 2664 C CB  . TYR A 1 353 ? -5.750  -42.089 -56.051 1.00 44.77  ? 352 TYR A CB  1 
ATOM 2665 C CG  . TYR A 1 353 ? -5.368  -41.006 -55.065 1.00 47.29  ? 352 TYR A CG  1 
ATOM 2666 C CD1 . TYR A 1 353 ? -5.585  -39.664 -55.354 1.00 48.81  ? 352 TYR A CD1 1 
ATOM 2667 C CD2 . TYR A 1 353 ? -4.796  -41.327 -53.839 1.00 50.33  ? 352 TYR A CD2 1 
ATOM 2668 C CE1 . TYR A 1 353 ? -5.238  -38.671 -54.453 1.00 49.72  ? 352 TYR A CE1 1 
ATOM 2669 C CE2 . TYR A 1 353 ? -4.447  -40.343 -52.931 1.00 51.97  ? 352 TYR A CE2 1 
ATOM 2670 C CZ  . TYR A 1 353 ? -4.669  -39.018 -53.242 1.00 52.92  ? 352 TYR A CZ  1 
ATOM 2671 O OH  . TYR A 1 353 ? -4.321  -38.039 -52.339 1.00 54.40  ? 352 TYR A OH  1 
ATOM 2672 N N   . LEU A 1 354 ? -7.767  -44.181 -57.669 1.00 38.26  ? 353 LEU A N   1 
ATOM 2673 C CA  . LEU A 1 354 ? -8.440  -44.588 -58.897 1.00 40.88  ? 353 LEU A CA  1 
ATOM 2674 C C   . LEU A 1 354 ? -9.947  -44.400 -58.775 1.00 41.00  ? 353 LEU A C   1 
ATOM 2675 O O   . LEU A 1 354 ? -10.614 -44.018 -59.745 1.00 44.36  ? 353 LEU A O   1 
ATOM 2676 C CB  . LEU A 1 354 ? -8.094  -46.040 -59.230 1.00 42.40  ? 353 LEU A CB  1 
ATOM 2677 C CG  . LEU A 1 354 ? -9.036  -46.788 -60.175 1.00 34.61  ? 353 LEU A CG  1 
ATOM 2678 C CD1 . LEU A 1 354 ? -8.977  -46.205 -61.581 1.00 38.40  ? 353 LEU A CD1 1 
ATOM 2679 C CD2 . LEU A 1 354 ? -8.702  -48.271 -60.188 1.00 41.16  ? 353 LEU A CD2 1 
ATOM 2680 N N   . VAL A 1 355 ? -10.495 -44.652 -57.585 1.00 40.82  ? 354 VAL A N   1 
ATOM 2681 C CA  . VAL A 1 355 ? -11.913 -44.406 -57.340 1.00 39.47  ? 354 VAL A CA  1 
ATOM 2682 C C   . VAL A 1 355 ? -12.217 -42.914 -57.423 1.00 44.24  ? 354 VAL A C   1 
ATOM 2683 O O   . VAL A 1 355 ? -13.262 -42.506 -57.945 1.00 40.52  ? 354 VAL A O   1 
ATOM 2684 C CB  . VAL A 1 355 ? -12.318 -45.001 -55.979 1.00 35.31  ? 354 VAL A CB  1 
ATOM 2685 C CG1 . VAL A 1 355 ? -13.687 -44.495 -55.551 1.00 42.56  ? 354 VAL A CG1 1 
ATOM 2686 C CG2 . VAL A 1 355 ? -12.299 -46.522 -56.043 1.00 34.51  ? 354 VAL A CG2 1 
ATOM 2687 N N   . ILE A 1 356 ? -11.306 -42.077 -56.921 1.00 42.77  ? 355 ILE A N   1 
ATOM 2688 C CA  . ILE A 1 356 ? -11.487 -40.633 -57.024 1.00 42.76  ? 355 ILE A CA  1 
ATOM 2689 C C   . ILE A 1 356 ? -11.368 -40.183 -58.475 1.00 42.91  ? 355 ILE A C   1 
ATOM 2690 O O   . ILE A 1 356 ? -12.167 -39.369 -58.955 1.00 40.97  ? 355 ILE A O   1 
ATOM 2691 C CB  . ILE A 1 356 ? -10.478 -39.904 -56.117 1.00 40.24  ? 355 ILE A CB  1 
ATOM 2692 C CG1 . ILE A 1 356 ? -10.623 -40.379 -54.672 1.00 42.91  ? 355 ILE A CG1 1 
ATOM 2693 C CG2 . ILE A 1 356 ? -10.674 -38.396 -56.193 1.00 39.50  ? 355 ILE A CG2 1 
ATOM 2694 C CD1 . ILE A 1 356 ? -9.449  -40.015 -53.793 1.00 43.73  ? 355 ILE A CD1 1 
ATOM 2695 N N   . ALA A 1 357 ? -10.379 -40.715 -59.201 1.00 42.26  ? 356 ALA A N   1 
ATOM 2696 C CA  . ALA A 1 357 ? -10.171 -40.332 -60.593 1.00 38.27  ? 356 ALA A CA  1 
ATOM 2697 C C   . ALA A 1 357 ? -11.347 -40.705 -61.485 1.00 43.47  ? 356 ALA A C   1 
ATOM 2698 O O   . ALA A 1 357 ? -11.518 -40.098 -62.547 1.00 48.13  ? 356 ALA A O   1 
ATOM 2699 C CB  . ALA A 1 357 ? -8.889  -40.973 -61.129 1.00 36.88  ? 356 ALA A CB  1 
ATOM 2700 N N   . LYS A 1 358 ? -12.155 -41.684 -61.085 1.00 43.28  ? 357 LYS A N   1 
ATOM 2701 C CA  . LYS A 1 358 ? -13.327 -42.084 -61.849 1.00 38.24  ? 357 LYS A CA  1 
ATOM 2702 C C   . LYS A 1 358 ? -14.624 -41.533 -61.273 1.00 42.68  ? 357 LYS A C   1 
ATOM 2703 O O   . LYS A 1 358 ? -15.693 -41.811 -61.824 1.00 45.02  ? 357 LYS A O   1 
ATOM 2704 C CB  . LYS A 1 358 ? -13.404 -43.611 -61.938 1.00 40.08  ? 357 LYS A CB  1 
ATOM 2705 C CG  . LYS A 1 358 ? -12.230 -44.249 -62.666 1.00 43.28  ? 357 LYS A CG  1 
ATOM 2706 C CD  . LYS A 1 358 ? -12.212 -43.862 -64.138 1.00 50.42  ? 357 LYS A CD  1 
ATOM 2707 C CE  . LYS A 1 358 ? -11.004 -43.001 -64.479 1.00 43.93  ? 357 LYS A CE  1 
ATOM 2708 N NZ  . LYS A 1 358 ? -11.042 -42.540 -65.894 1.00 45.27  ? 357 LYS A NZ  1 
ATOM 2709 N N   . ALA A 1 359 ? -14.552 -40.765 -60.182 1.00 47.75  ? 358 ALA A N   1 
ATOM 2710 C CA  . ALA A 1 359 ? -15.718 -40.121 -59.570 1.00 48.86  ? 358 ALA A CA  1 
ATOM 2711 C C   . ALA A 1 359 ? -16.819 -41.135 -59.257 1.00 52.58  ? 358 ALA A C   1 
ATOM 2712 O O   . ALA A 1 359 ? -17.990 -40.944 -59.592 1.00 53.65  ? 358 ALA A O   1 
ATOM 2713 C CB  . ALA A 1 359 ? -16.250 -38.991 -60.456 1.00 51.51  ? 358 ALA A CB  1 
ATOM 2714 N N   . SER A 1 360 ? -16.433 -42.227 -58.599 1.00 46.40  ? 359 SER A N   1 
ATOM 2715 C CA  . SER A 1 360 ? -17.356 -43.310 -58.265 1.00 45.48  ? 359 SER A CA  1 
ATOM 2716 C C   . SER A 1 360 ? -17.746 -43.188 -56.797 1.00 46.51  ? 359 SER A C   1 
ATOM 2717 O O   . SER A 1 360 ? -17.033 -43.668 -55.912 1.00 51.99  ? 359 SER A O   1 
ATOM 2718 C CB  . SER A 1 360 ? -16.727 -44.667 -58.559 1.00 42.23  ? 359 SER A CB  1 
ATOM 2719 O OG  . SER A 1 360 ? -17.658 -45.712 -58.338 1.00 44.87  ? 359 SER A OG  1 
ATOM 2720 N N   . LEU A 1 361 ? -18.887 -42.546 -56.539 1.00 46.95  ? 360 LEU A N   1 
ATOM 2721 C CA  . LEU A 1 361 ? -19.387 -42.467 -55.171 1.00 47.25  ? 360 LEU A CA  1 
ATOM 2722 C C   . LEU A 1 361 ? -19.756 -43.845 -54.633 1.00 48.12  ? 360 LEU A C   1 
ATOM 2723 O O   . LEU A 1 361 ? -19.670 -44.079 -53.421 1.00 47.61  ? 360 LEU A O   1 
ATOM 2724 C CB  . LEU A 1 361 ? -20.588 -41.521 -55.108 1.00 41.92  ? 360 LEU A CB  1 
ATOM 2725 C CG  . LEU A 1 361 ? -21.129 -41.151 -53.726 1.00 52.24  ? 360 LEU A CG  1 
ATOM 2726 C CD1 . LEU A 1 361 ? -20.137 -40.282 -52.969 1.00 52.81  ? 360 LEU A CD1 1 
ATOM 2727 C CD2 . LEU A 1 361 ? -22.466 -40.441 -53.858 1.00 54.15  ? 360 LEU A CD2 1 
ATOM 2728 N N   . ARG A 1 362 ? -20.150 -44.767 -55.515 1.00 49.64  ? 361 ARG A N   1 
ATOM 2729 C CA  . ARG A 1 362 ? -20.494 -46.122 -55.091 1.00 46.22  ? 361 ARG A CA  1 
ATOM 2730 C C   . ARG A 1 362 ? -19.282 -46.842 -54.513 1.00 45.97  ? 361 ARG A C   1 
ATOM 2731 O O   . ARG A 1 362 ? -19.335 -47.373 -53.398 1.00 45.14  ? 361 ARG A O   1 
ATOM 2732 C CB  . ARG A 1 362 ? -21.074 -46.902 -56.272 1.00 43.20  ? 361 ARG A CB  1 
ATOM 2733 C CG  . ARG A 1 362 ? -22.279 -46.236 -56.914 1.00 45.21  ? 361 ARG A CG  1 
ATOM 2734 C CD  . ARG A 1 362 ? -22.218 -46.322 -58.431 1.00 42.78  ? 361 ARG A CD  1 
ATOM 2735 N NE  . ARG A 1 362 ? -21.193 -45.448 -58.991 1.00 47.03  ? 361 ARG A NE  1 
ATOM 2736 C CZ  . ARG A 1 362 ? -21.320 -44.137 -59.157 1.00 40.35  ? 361 ARG A CZ  1 
ATOM 2737 N NH1 . ARG A 1 362 ? -22.428 -43.499 -58.820 1.00 35.99  ? 361 ARG A NH1 1 
ATOM 2738 N NH2 . ARG A 1 362 ? -20.310 -43.449 -59.680 1.00 41.84  ? 361 ARG A NH2 1 
ATOM 2739 N N   . PHE A 1 363 ? -18.177 -46.873 -55.261 1.00 46.68  ? 362 PHE A N   1 
ATOM 2740 C CA  . PHE A 1 363 ? -16.963 -47.507 -54.761 1.00 45.88  ? 362 PHE A CA  1 
ATOM 2741 C C   . PHE A 1 363 ? -16.308 -46.700 -53.649 1.00 45.90  ? 362 PHE A C   1 
ATOM 2742 O O   . PHE A 1 363 ? -15.445 -47.230 -52.941 1.00 41.41  ? 362 PHE A O   1 
ATOM 2743 C CB  . PHE A 1 363 ? -15.971 -47.719 -55.906 1.00 45.33  ? 362 PHE A CB  1 
ATOM 2744 C CG  . PHE A 1 363 ? -16.185 -48.999 -56.659 1.00 42.97  ? 362 PHE A CG  1 
ATOM 2745 C CD1 . PHE A 1 363 ? -15.864 -50.218 -56.085 1.00 41.47  ? 362 PHE A CD1 1 
ATOM 2746 C CD2 . PHE A 1 363 ? -16.713 -48.984 -57.939 1.00 43.14  ? 362 PHE A CD2 1 
ATOM 2747 C CE1 . PHE A 1 363 ? -16.063 -51.399 -56.775 1.00 43.07  ? 362 PHE A CE1 1 
ATOM 2748 C CE2 . PHE A 1 363 ? -16.914 -50.159 -58.635 1.00 40.76  ? 362 PHE A CE2 1 
ATOM 2749 C CZ  . PHE A 1 363 ? -16.588 -51.368 -58.053 1.00 48.39  ? 362 PHE A CZ  1 
ATOM 2750 N N   . TYR A 1 364 ? -16.693 -45.434 -53.481 1.00 49.42  ? 363 TYR A N   1 
ATOM 2751 C CA  . TYR A 1 364 ? -16.131 -44.626 -52.406 1.00 51.65  ? 363 TYR A CA  1 
ATOM 2752 C C   . TYR A 1 364 ? -16.763 -44.979 -51.065 1.00 54.36  ? 363 TYR A C   1 
ATOM 2753 O O   . TYR A 1 364 ? -16.055 -45.188 -50.073 1.00 50.73  ? 363 TYR A O   1 
ATOM 2754 C CB  . TYR A 1 364 ? -16.315 -43.139 -52.711 1.00 52.13  ? 363 TYR A CB  1 
ATOM 2755 C CG  . TYR A 1 364 ? -15.232 -42.273 -52.114 1.00 48.36  ? 363 TYR A CG  1 
ATOM 2756 C CD1 . TYR A 1 364 ? -15.323 -41.809 -50.807 1.00 47.95  ? 363 TYR A CD1 1 
ATOM 2757 C CD2 . TYR A 1 364 ? -14.108 -41.934 -52.851 1.00 52.36  ? 363 TYR A CD2 1 
ATOM 2758 C CE1 . TYR A 1 364 ? -14.327 -41.023 -50.258 1.00 46.84  ? 363 TYR A CE1 1 
ATOM 2759 C CE2 . TYR A 1 364 ? -13.111 -41.151 -52.311 1.00 49.46  ? 363 TYR A CE2 1 
ATOM 2760 C CZ  . TYR A 1 364 ? -13.224 -40.698 -51.017 1.00 48.47  ? 363 TYR A CZ  1 
ATOM 2761 O OH  . TYR A 1 364 ? -12.222 -39.918 -50.492 1.00 54.14  ? 363 TYR A OH  1 
ATOM 2762 N N   . ILE A 1 365 ? -18.095 -45.045 -51.019 1.00 49.71  ? 364 ILE A N   1 
ATOM 2763 C CA  . ILE A 1 365 ? -18.779 -45.453 -49.796 1.00 45.63  ? 364 ILE A CA  1 
ATOM 2764 C C   . ILE A 1 365 ? -18.389 -46.876 -49.423 1.00 46.38  ? 364 ILE A C   1 
ATOM 2765 O O   . ILE A 1 365 ? -18.226 -47.204 -48.241 1.00 48.61  ? 364 ILE A O   1 
ATOM 2766 C CB  . ILE A 1 365 ? -20.303 -45.302 -49.964 1.00 40.57  ? 364 ILE A CB  1 
ATOM 2767 C CG1 . ILE A 1 365 ? -20.662 -43.833 -50.191 1.00 42.15  ? 364 ILE A CG1 1 
ATOM 2768 C CG2 . ILE A 1 365 ? -21.041 -45.855 -48.752 1.00 35.51  ? 364 ILE A CG2 1 
ATOM 2769 C CD1 . ILE A 1 365 ? -21.977 -43.624 -50.901 1.00 44.50  ? 364 ILE A CD1 1 
ATOM 2770 N N   . LEU A 1 366 ? -18.216 -47.741 -50.425 1.00 44.12  ? 365 LEU A N   1 
ATOM 2771 C CA  . LEU A 1 366 ? -17.791 -49.109 -50.155 1.00 43.95  ? 365 LEU A CA  1 
ATOM 2772 C C   . LEU A 1 366 ? -16.411 -49.139 -49.508 1.00 44.14  ? 365 LEU A C   1 
ATOM 2773 O O   . LEU A 1 366 ? -16.164 -49.928 -48.588 1.00 44.24  ? 365 LEU A O   1 
ATOM 2774 C CB  . LEU A 1 366 ? -17.801 -49.922 -51.449 1.00 42.64  ? 365 LEU A CB  1 
ATOM 2775 C CG  . LEU A 1 366 ? -17.487 -51.413 -51.330 1.00 41.46  ? 365 LEU A CG  1 
ATOM 2776 C CD1 . LEU A 1 366 ? -18.718 -52.181 -50.871 1.00 40.30  ? 365 LEU A CD1 1 
ATOM 2777 C CD2 . LEU A 1 366 ? -16.975 -51.952 -52.657 1.00 42.64  ? 365 LEU A CD2 1 
ATOM 2778 N N   . ALA A 1 367 ? -15.503 -48.274 -49.964 1.00 44.45  ? 366 ALA A N   1 
ATOM 2779 C CA  . ALA A 1 367 ? -14.149 -48.263 -49.420 1.00 44.32  ? 366 ALA A CA  1 
ATOM 2780 C C   . ALA A 1 367 ? -14.121 -47.702 -48.003 1.00 50.93  ? 366 ALA A C   1 
ATOM 2781 O O   . ALA A 1 367 ? -13.414 -48.229 -47.135 1.00 50.00  ? 366 ALA A O   1 
ATOM 2782 C CB  . ALA A 1 367 ? -13.224 -47.462 -50.333 1.00 35.78  ? 366 ALA A CB  1 
ATOM 2783 N N   . GLU A 1 368 ? -14.880 -46.633 -47.749 1.00 47.84  ? 367 GLU A N   1 
ATOM 2784 C CA  . GLU A 1 368 ? -14.879 -46.026 -46.422 1.00 43.74  ? 367 GLU A CA  1 
ATOM 2785 C C   . GLU A 1 368 ? -15.579 -46.917 -45.403 1.00 45.50  ? 367 GLU A C   1 
ATOM 2786 O O   . GLU A 1 368 ? -15.134 -47.025 -44.254 1.00 42.29  ? 367 GLU A O   1 
ATOM 2787 C CB  . GLU A 1 368 ? -15.541 -44.649 -46.476 1.00 45.04  ? 367 GLU A CB  1 
ATOM 2788 C CG  . GLU A 1 368 ? -14.795 -43.630 -47.324 1.00 50.87  ? 367 GLU A CG  1 
ATOM 2789 C CD  . GLU A 1 368 ? -13.667 -42.946 -46.569 1.00 55.43  ? 367 GLU A CD  1 
ATOM 2790 O OE1 . GLU A 1 368 ? -13.941 -42.322 -45.520 1.00 54.17  ? 367 GLU A OE1 1 
ATOM 2791 O OE2 . GLU A 1 368 ? -12.506 -43.030 -47.027 1.00 57.47  ? 367 GLU A OE2 1 
ATOM 2792 N N   . VAL A 1 369 ? -16.676 -47.564 -45.804 1.00 47.84  ? 368 VAL A N   1 
ATOM 2793 C CA  . VAL A 1 369 ? -17.396 -48.441 -44.886 1.00 44.97  ? 368 VAL A CA  1 
ATOM 2794 C C   . VAL A 1 369 ? -16.552 -49.664 -44.546 1.00 43.14  ? 368 VAL A C   1 
ATOM 2795 O O   . VAL A 1 369 ? -16.548 -50.133 -43.401 1.00 50.88  ? 368 VAL A O   1 
ATOM 2796 C CB  . VAL A 1 369 ? -18.760 -48.832 -45.488 1.00 41.32  ? 368 VAL A CB  1 
ATOM 2797 C CG1 . VAL A 1 369 ? -19.316 -50.082 -44.817 1.00 42.05  ? 368 VAL A CG1 1 
ATOM 2798 C CG2 . VAL A 1 369 ? -19.742 -47.675 -45.372 1.00 38.68  ? 368 VAL A CG2 1 
ATOM 2799 N N   . SER A 1 370 ? -15.813 -50.190 -45.524 1.00 43.21  ? 369 SER A N   1 
ATOM 2800 C CA  . SER A 1 370 ? -14.979 -51.362 -45.275 1.00 44.68  ? 369 SER A CA  1 
ATOM 2801 C C   . SER A 1 370 ? -13.890 -51.053 -44.255 1.00 48.81  ? 369 SER A C   1 
ATOM 2802 O O   . SER A 1 370 ? -13.669 -51.821 -43.312 1.00 47.67  ? 369 SER A O   1 
ATOM 2803 C CB  . SER A 1 370 ? -14.366 -51.857 -46.585 1.00 42.70  ? 369 SER A CB  1 
ATOM 2804 O OG  . SER A 1 370 ? -15.316 -51.819 -47.632 1.00 49.47  ? 369 SER A OG  1 
ATOM 2805 N N   . GLN A 1 371 ? -13.200 -49.924 -44.428 1.00 47.90  ? 370 GLN A N   1 
ATOM 2806 C CA  . GLN A 1 371 ? -12.161 -49.542 -43.478 1.00 46.04  ? 370 GLN A CA  1 
ATOM 2807 C C   . GLN A 1 371 ? -12.750 -49.236 -42.108 1.00 47.30  ? 370 GLN A C   1 
ATOM 2808 O O   . GLN A 1 371 ? -12.156 -49.581 -41.080 1.00 45.13  ? 370 GLN A O   1 
ATOM 2809 C CB  . GLN A 1 371 ? -11.387 -48.340 -44.011 1.00 44.74  ? 370 GLN A CB  1 
ATOM 2810 C CG  . GLN A 1 371 ? -10.701 -48.595 -45.335 1.00 46.25  ? 370 GLN A CG  1 
ATOM 2811 C CD  . GLN A 1 371 ? -10.077 -47.342 -45.907 1.00 48.52  ? 370 GLN A CD  1 
ATOM 2812 O OE1 . GLN A 1 371 ? -9.137  -46.789 -45.337 1.00 47.19  ? 370 GLN A OE1 1 
ATOM 2813 N NE2 . GLN A 1 371 ? -10.598 -46.886 -47.040 1.00 49.61  ? 370 GLN A NE2 1 
ATOM 2814 N N   . PHE A 1 372 ? -13.916 -48.588 -42.075 1.00 50.72  ? 371 PHE A N   1 
ATOM 2815 C CA  . PHE A 1 372 ? -14.588 -48.327 -40.806 1.00 44.22  ? 371 PHE A CA  1 
ATOM 2816 C C   . PHE A 1 372 ? -14.948 -49.631 -40.104 1.00 46.48  ? 371 PHE A C   1 
ATOM 2817 O O   . PHE A 1 372 ? -14.707 -49.789 -38.902 1.00 48.64  ? 371 PHE A O   1 
ATOM 2818 C CB  . PHE A 1 372 ? -15.839 -47.477 -41.045 1.00 40.61  ? 371 PHE A CB  1 
ATOM 2819 C CG  . PHE A 1 372 ? -16.480 -46.962 -39.784 1.00 41.81  ? 371 PHE A CG  1 
ATOM 2820 C CD1 . PHE A 1 372 ? -17.328 -47.765 -39.036 1.00 45.99  ? 371 PHE A CD1 1 
ATOM 2821 C CD2 . PHE A 1 372 ? -16.244 -45.668 -39.355 1.00 42.98  ? 371 PHE A CD2 1 
ATOM 2822 C CE1 . PHE A 1 372 ? -17.916 -47.290 -37.879 1.00 46.71  ? 371 PHE A CE1 1 
ATOM 2823 C CE2 . PHE A 1 372 ? -16.832 -45.185 -38.200 1.00 40.73  ? 371 PHE A CE2 1 
ATOM 2824 C CZ  . PHE A 1 372 ? -17.668 -45.997 -37.461 1.00 46.74  ? 371 PHE A CZ  1 
ATOM 2825 N N   . THR A 1 373 ? -15.528 -50.580 -40.844 1.00 46.01  ? 372 THR A N   1 
ATOM 2826 C CA  . THR A 1 373 ? -15.955 -51.837 -40.237 1.00 48.48  ? 372 THR A CA  1 
ATOM 2827 C C   . THR A 1 373 ? -14.760 -52.648 -39.754 1.00 51.22  ? 372 THR A C   1 
ATOM 2828 O O   . THR A 1 373 ? -14.756 -53.152 -38.625 1.00 56.07  ? 372 THR A O   1 
ATOM 2829 C CB  . THR A 1 373 ? -16.786 -52.653 -41.229 1.00 43.51  ? 372 THR A CB  1 
ATOM 2830 O OG1 . THR A 1 373 ? -17.702 -51.792 -41.915 1.00 40.84  ? 372 THR A OG1 1 
ATOM 2831 C CG2 . THR A 1 373 ? -17.568 -53.735 -40.498 1.00 41.67  ? 372 THR A CG2 1 
ATOM 2832 N N   . LEU A 1 374 ? -13.734 -52.785 -40.596 1.00 51.75  ? 373 LEU A N   1 
ATOM 2833 C CA  . LEU A 1 374 ? -12.568 -53.573 -40.208 1.00 55.19  ? 373 LEU A CA  1 
ATOM 2834 C C   . LEU A 1 374 ? -11.833 -52.936 -39.034 1.00 55.71  ? 373 LEU A C   1 
ATOM 2835 O O   . LEU A 1 374 ? -11.352 -53.644 -38.142 1.00 57.12  ? 373 LEU A O   1 
ATOM 2836 C CB  . LEU A 1 374 ? -11.634 -53.754 -41.405 1.00 58.90  ? 373 LEU A CB  1 
ATOM 2837 C CG  . LEU A 1 374 ? -12.191 -54.579 -42.570 1.00 57.24  ? 373 LEU A CG  1 
ATOM 2838 C CD1 . LEU A 1 374 ? -11.425 -54.287 -43.852 1.00 50.35  ? 373 LEU A CD1 1 
ATOM 2839 C CD2 . LEU A 1 374 ? -12.172 -56.068 -42.252 1.00 47.43  ? 373 LEU A CD2 1 
ATOM 2840 N N   . LEU A 1 375 ? -11.746 -51.603 -39.008 1.00 53.26  ? 374 LEU A N   1 
ATOM 2841 C CA  . LEU A 1 375 ? -11.085 -50.934 -37.891 1.00 49.23  ? 374 LEU A CA  1 
ATOM 2842 C C   . LEU A 1 375 ? -11.839 -51.164 -36.591 1.00 52.23  ? 374 LEU A C   1 
ATOM 2843 O O   . LEU A 1 375 ? -11.229 -51.298 -35.525 1.00 52.04  ? 374 LEU A O   1 
ATOM 2844 C CB  . LEU A 1 375 ? -10.957 -49.436 -38.168 1.00 45.06  ? 374 LEU A CB  1 
ATOM 2845 C CG  . LEU A 1 375 ? -9.651  -48.960 -38.805 1.00 42.70  ? 374 LEU A CG  1 
ATOM 2846 C CD1 . LEU A 1 375 ? -9.724  -47.477 -39.114 1.00 46.58  ? 374 LEU A CD1 1 
ATOM 2847 C CD2 . LEU A 1 375 ? -8.465  -49.263 -37.906 1.00 46.68  ? 374 LEU A CD2 1 
ATOM 2848 N N   . MET A 1 376 ? -13.168 -51.224 -36.661 1.00 51.33  ? 375 MET A N   1 
ATOM 2849 C CA  . MET A 1 376 ? -13.972 -51.382 -35.457 1.00 54.37  ? 375 MET A CA  1 
ATOM 2850 C C   . MET A 1 376 ? -13.973 -52.817 -34.949 1.00 58.93  ? 375 MET A C   1 
ATOM 2851 O O   . MET A 1 376 ? -14.037 -53.035 -33.735 1.00 60.91  ? 375 MET A O   1 
ATOM 2852 C CB  . MET A 1 376 ? -15.404 -50.918 -35.718 1.00 53.67  ? 375 MET A CB  1 
ATOM 2853 C CG  . MET A 1 376 ? -15.648 -49.424 -35.493 1.00 55.69  ? 375 MET A CG  1 
ATOM 2854 S SD  . MET A 1 376 ? -14.774 -48.699 -34.086 1.00 74.53  ? 375 MET A SD  1 
ATOM 2855 C CE  . MET A 1 376 ? -13.310 -48.016 -34.862 1.00 48.20  ? 375 MET A CE  1 
ATOM 2856 N N   . VAL A 1 377 ? -13.918 -53.801 -35.848 1.00 54.79  ? 376 VAL A N   1 
ATOM 2857 C CA  . VAL A 1 377 ? -13.859 -55.191 -35.410 1.00 56.74  ? 376 VAL A CA  1 
ATOM 2858 C C   . VAL A 1 377 ? -12.508 -55.494 -34.774 1.00 60.71  ? 376 VAL A C   1 
ATOM 2859 O O   . VAL A 1 377 ? -12.431 -56.153 -33.730 1.00 61.90  ? 376 VAL A O   1 
ATOM 2860 C CB  . VAL A 1 377 ? -14.158 -56.137 -36.587 1.00 55.70  ? 376 VAL A CB  1 
ATOM 2861 C CG1 . VAL A 1 377 ? -14.061 -57.584 -36.141 1.00 60.01  ? 376 VAL A CG1 1 
ATOM 2862 C CG2 . VAL A 1 377 ? -15.539 -55.854 -37.151 1.00 51.45  ? 376 VAL A CG2 1 
ATOM 2863 N N   . PHE A 1 378 ? -11.425 -55.009 -35.382 1.00 64.11  ? 377 PHE A N   1 
ATOM 2864 C CA  . PHE A 1 378 ? -10.093 -55.289 -34.858 1.00 68.76  ? 377 PHE A CA  1 
ATOM 2865 C C   . PHE A 1 378 ? -9.783  -54.477 -33.605 1.00 66.83  ? 377 PHE A C   1 
ATOM 2866 O O   . PHE A 1 378 ? -8.958  -54.901 -32.787 1.00 63.26  ? 377 PHE A O   1 
ATOM 2867 C CB  . PHE A 1 378 ? -9.042  -55.027 -35.938 1.00 59.70  ? 377 PHE A CB  1 
ATOM 2868 C CG  . PHE A 1 378 ? -9.011  -56.073 -37.021 1.00 57.62  ? 377 PHE A CG  1 
ATOM 2869 C CD1 . PHE A 1 378 ? -8.966  -57.419 -36.699 1.00 59.65  ? 377 PHE A CD1 1 
ATOM 2870 C CD2 . PHE A 1 378 ? -9.011  -55.710 -38.360 1.00 58.90  ? 377 PHE A CD2 1 
ATOM 2871 C CE1 . PHE A 1 378 ? -8.931  -58.383 -37.688 1.00 62.57  ? 377 PHE A CE1 1 
ATOM 2872 C CE2 . PHE A 1 378 ? -8.976  -56.673 -39.354 1.00 58.82  ? 377 PHE A CE2 1 
ATOM 2873 C CZ  . PHE A 1 378 ? -8.936  -58.010 -39.016 1.00 55.71  ? 377 PHE A CZ  1 
ATOM 2874 N N   . ALA A 1 379 ? -10.428 -53.319 -33.429 1.00 63.51  ? 378 ALA A N   1 
ATOM 2875 C CA  . ALA A 1 379 ? -10.194 -52.521 -32.228 1.00 60.17  ? 378 ALA A CA  1 
ATOM 2876 C C   . ALA A 1 379 ? -10.847 -53.161 -31.010 1.00 63.27  ? 378 ALA A C   1 
ATOM 2877 O O   . ALA A 1 379 ? -10.227 -53.276 -29.947 1.00 57.93  ? 378 ALA A O   1 
ATOM 2878 C CB  . ALA A 1 379 ? -10.711 -51.098 -32.428 1.00 53.59  ? 378 ALA A CB  1 
ATOM 2879 N N   . HIS A 1 380 ? -12.104 -53.586 -31.148 1.00 73.60  ? 379 HIS A N   1 
ATOM 2880 C CA  . HIS A 1 380 ? -12.809 -54.262 -30.067 1.00 69.93  ? 379 HIS A CA  1 
ATOM 2881 C C   . HIS A 1 380 ? -12.179 -55.600 -29.699 1.00 64.84  ? 379 HIS A C   1 
ATOM 2882 O O   . HIS A 1 380 ? -12.491 -56.139 -28.632 1.00 70.14  ? 379 HIS A O   1 
ATOM 2883 C CB  . HIS A 1 380 ? -14.275 -54.472 -30.451 1.00 75.78  ? 379 HIS A CB  1 
ATOM 2884 C CG  . HIS A 1 380 ? -15.091 -53.217 -30.428 1.00 85.48  ? 379 HIS A CG  1 
ATOM 2885 N ND1 . HIS A 1 380 ? -15.480 -52.561 -31.576 1.00 90.22  ? 379 HIS A ND1 1 
ATOM 2886 C CD2 . HIS A 1 380 ? -15.595 -52.500 -29.396 1.00 79.83  ? 379 HIS A CD2 1 
ATOM 2887 C CE1 . HIS A 1 380 ? -16.187 -51.492 -31.252 1.00 82.07  ? 379 HIS A CE1 1 
ATOM 2888 N NE2 . HIS A 1 380 ? -16.272 -51.433 -29.935 1.00 81.46  ? 379 HIS A NE2 1 
ATOM 2889 N N   . TRP A 1 381 ? -11.306 -56.142 -30.548 1.00 60.92  ? 380 TRP A N   1 
ATOM 2890 C CA  . TRP A 1 381 ? -10.668 -57.427 -30.297 1.00 58.49  ? 380 TRP A CA  1 
ATOM 2891 C C   . TRP A 1 381 ? -9.264  -57.300 -29.724 1.00 60.79  ? 380 TRP A C   1 
ATOM 2892 O O   . TRP A 1 381 ? -8.818  -58.204 -29.010 1.00 60.55  ? 380 TRP A O   1 
ATOM 2893 C CB  . TRP A 1 381 ? -10.613 -58.248 -31.593 1.00 61.18  ? 380 TRP A CB  1 
ATOM 2894 C CG  . TRP A 1 381 ? -9.930  -59.585 -31.454 1.00 67.10  ? 380 TRP A CG  1 
ATOM 2895 C CD1 . TRP A 1 381 ? -10.226 -60.571 -30.554 1.00 64.45  ? 380 TRP A CD1 1 
ATOM 2896 C CD2 . TRP A 1 381 ? -8.835  -60.077 -32.240 1.00 69.43  ? 380 TRP A CD2 1 
ATOM 2897 N NE1 . TRP A 1 381 ? -9.385  -61.644 -30.733 1.00 65.65  ? 380 TRP A NE1 1 
ATOM 2898 C CE2 . TRP A 1 381 ? -8.521  -61.365 -31.761 1.00 66.91  ? 380 TRP A CE2 1 
ATOM 2899 C CE3 . TRP A 1 381 ? -8.091  -59.554 -33.303 1.00 68.28  ? 380 TRP A CE3 1 
ATOM 2900 C CZ2 . TRP A 1 381 ? -7.495  -62.135 -32.307 1.00 69.04  ? 380 TRP A CZ2 1 
ATOM 2901 C CZ3 . TRP A 1 381 ? -7.073  -60.320 -33.843 1.00 62.65  ? 380 TRP A CZ3 1 
ATOM 2902 C CH2 . TRP A 1 381 ? -6.786  -61.596 -33.345 1.00 64.78  ? 380 TRP A CH2 1 
ATOM 2903 N N   . LEU A 1 382 ? -8.561  -56.200 -30.000 1.00 60.54  ? 381 LEU A N   1 
ATOM 2904 C CA  . LEU A 1 382 ? -7.164  -56.055 -29.612 1.00 54.28  ? 381 LEU A CA  1 
ATOM 2905 C C   . LEU A 1 382 ? -6.899  -54.940 -28.610 1.00 54.52  ? 381 LEU A C   1 
ATOM 2906 O O   . LEU A 1 382 ? -5.988  -55.079 -27.792 1.00 56.85  ? 381 LEU A O   1 
ATOM 2907 C CB  . LEU A 1 382 ? -6.290  -55.812 -30.852 1.00 53.84  ? 381 LEU A CB  1 
ATOM 2908 C CG  . LEU A 1 382 ? -6.176  -56.983 -31.829 1.00 57.79  ? 381 LEU A CG  1 
ATOM 2909 C CD1 . LEU A 1 382 ? -5.966  -56.470 -33.243 1.00 56.31  ? 381 LEU A CD1 1 
ATOM 2910 C CD2 . LEU A 1 382 ? -5.054  -57.929 -31.424 1.00 55.26  ? 381 LEU A CD2 1 
ATOM 2911 N N   . ILE A 1 383 ? -7.655  -53.846 -28.648 1.00 51.56  ? 382 ILE A N   1 
ATOM 2912 C CA  . ILE A 1 383 ? -7.411  -52.703 -27.766 1.00 50.43  ? 382 ILE A CA  1 
ATOM 2913 C C   . ILE A 1 383 ? -7.676  -53.050 -26.302 1.00 53.00  ? 382 ILE A C   1 
ATOM 2914 O O   . ILE A 1 383 ? -6.812  -52.774 -25.456 1.00 51.56  ? 382 ILE A O   1 
ATOM 2915 C CB  . ILE A 1 383 ? -8.240  -51.479 -28.193 1.00 54.95  ? 382 ILE A CB  1 
ATOM 2916 C CG1 . ILE A 1 383 ? -7.634  -50.833 -29.441 1.00 57.01  ? 382 ILE A CG1 1 
ATOM 2917 C CG2 . ILE A 1 383 ? -8.330  -50.470 -27.053 1.00 48.98  ? 382 ILE A CG2 1 
ATOM 2918 C CD1 . ILE A 1 383 ? -8.296  -49.530 -29.842 1.00 46.89  ? 382 ILE A CD1 1 
ATOM 2919 N N   . PRO A 1 384 ? -8.826  -53.635 -25.933 1.00 51.65  ? 383 PRO A N   1 
ATOM 2920 C CA  . PRO A 1 384 ? -9.072  -53.902 -24.504 1.00 54.42  ? 383 PRO A CA  1 
ATOM 2921 C C   . PRO A 1 384 ? -8.117  -54.913 -23.885 1.00 51.80  ? 383 PRO A C   1 
ATOM 2922 O O   . PRO A 1 384 ? -8.080  -55.020 -22.652 1.00 51.91  ? 383 PRO A O   1 
ATOM 2923 C CB  . PRO A 1 384 ? -10.515 -54.427 -24.484 1.00 52.22  ? 383 PRO A CB  1 
ATOM 2924 C CG  . PRO A 1 384 ? -11.111 -53.980 -25.776 1.00 51.99  ? 383 PRO A CG  1 
ATOM 2925 C CD  . PRO A 1 384 ? -9.986  -54.040 -26.749 1.00 51.70  ? 383 PRO A CD  1 
ATOM 2926 N N   . ALA A 1 385 ? -7.344  -55.644 -24.686 1.00 48.58  ? 384 ALA A N   1 
ATOM 2927 C CA  . ALA A 1 385 ? -6.445  -56.670 -24.178 1.00 43.55  ? 384 ALA A CA  1 
ATOM 2928 C C   . ALA A 1 385 ? -4.973  -56.347 -24.364 1.00 46.19  ? 384 ALA A C   1 
ATOM 2929 O O   . ALA A 1 385 ? -4.157  -56.757 -23.537 1.00 44.16  ? 384 ALA A O   1 
ATOM 2930 C CB  . ALA A 1 385 ? -6.739  -58.015 -24.853 1.00 44.92  ? 384 ALA A CB  1 
ATOM 2931 N N   . HIS A 1 386 ? -4.612  -55.630 -25.427 1.00 50.65  ? 385 HIS A N   1 
ATOM 2932 C CA  . HIS A 1 386 ? -3.217  -55.351 -25.740 1.00 48.96  ? 385 HIS A CA  1 
ATOM 2933 C C   . HIS A 1 386 ? -2.864  -53.873 -25.652 1.00 48.61  ? 385 HIS A C   1 
ATOM 2934 O O   . HIS A 1 386 ? -1.730  -53.502 -25.974 1.00 52.33  ? 385 HIS A O   1 
ATOM 2935 C CB  . HIS A 1 386 ? -2.872  -55.889 -27.134 1.00 49.47  ? 385 HIS A CB  1 
ATOM 2936 C CG  . HIS A 1 386 ? -2.768  -57.382 -27.199 1.00 56.16  ? 385 HIS A CG  1 
ATOM 2937 N ND1 . HIS A 1 386 ? -2.568  -58.064 -28.381 1.00 55.76  ? 385 HIS A ND1 1 
ATOM 2938 C CD2 . HIS A 1 386 ? -2.837  -58.325 -26.229 1.00 55.67  ? 385 HIS A CD2 1 
ATOM 2939 C CE1 . HIS A 1 386 ? -2.517  -59.361 -28.136 1.00 60.41  ? 385 HIS A CE1 1 
ATOM 2940 N NE2 . HIS A 1 386 ? -2.679  -59.547 -26.838 1.00 63.05  ? 385 HIS A NE2 1 
ATOM 2941 N N   . GLY A 1 387 ? -3.798  -53.021 -25.226 1.00 40.23  ? 386 GLY A N   1 
ATOM 2942 C CA  . GLY A 1 387 ? -3.482  -51.622 -25.009 1.00 39.68  ? 386 GLY A CA  1 
ATOM 2943 C C   . GLY A 1 387 ? -3.192  -50.878 -26.301 1.00 55.81  ? 386 GLY A C   1 
ATOM 2944 O O   . GLY A 1 387 ? -3.733  -51.184 -27.369 1.00 57.13  ? 386 GLY A O   1 
ATOM 2945 N N   . ALA A 1 388 ? -2.317  -49.875 -26.193 1.00 53.79  ? 387 ALA A N   1 
ATOM 2946 C CA  . ALA A 1 388 ? -1.930  -49.096 -27.365 1.00 45.94  ? 387 ALA A CA  1 
ATOM 2947 C C   . ALA A 1 388 ? -1.265  -49.969 -28.418 1.00 51.89  ? 387 ALA A C   1 
ATOM 2948 O O   . ALA A 1 388 ? -1.377  -49.692 -29.619 1.00 54.00  ? 387 ALA A O   1 
ATOM 2949 C CB  . ALA A 1 388 ? -0.999  -47.957 -26.954 1.00 37.39  ? 387 ALA A CB  1 
ATOM 2950 N N   . LEU A 1 389 ? -0.569  -51.023 -27.989 1.00 52.48  ? 388 LEU A N   1 
ATOM 2951 C CA  . LEU A 1 389 ? -0.009  -51.973 -28.939 1.00 51.84  ? 388 LEU A CA  1 
ATOM 2952 C C   . LEU A 1 389 ? -1.116  -52.599 -29.778 1.00 54.92  ? 388 LEU A C   1 
ATOM 2953 O O   . LEU A 1 389 ? -1.030  -52.637 -31.010 1.00 53.58  ? 388 LEU A O   1 
ATOM 2954 C CB  . LEU A 1 389 ? 0.797   -53.038 -28.192 1.00 47.52  ? 388 LEU A CB  1 
ATOM 2955 C CG  . LEU A 1 389 ? 1.822   -53.868 -28.971 1.00 44.19  ? 388 LEU A CG  1 
ATOM 2956 C CD1 . LEU A 1 389 ? 2.834   -54.462 -28.015 1.00 51.23  ? 388 LEU A CD1 1 
ATOM 2957 C CD2 . LEU A 1 389 ? 1.171   -54.977 -29.781 1.00 51.78  ? 388 LEU A CD2 1 
ATOM 2958 N N   . GLY A 1 390 ? -2.186  -53.062 -29.125 1.00 60.48  ? 389 GLY A N   1 
ATOM 2959 C CA  . GLY A 1 390 ? -3.303  -53.637 -29.855 1.00 60.52  ? 389 GLY A CA  1 
ATOM 2960 C C   . GLY A 1 390 ? -3.965  -52.663 -30.808 1.00 60.84  ? 389 GLY A C   1 
ATOM 2961 O O   . GLY A 1 390 ? -4.522  -53.071 -31.831 1.00 65.12  ? 389 GLY A O   1 
ATOM 2962 N N   . ALA A 1 391 ? -3.920  -51.367 -30.489 1.00 50.27  ? 390 ALA A N   1 
ATOM 2963 C CA  . ALA A 1 391 ? -4.442  -50.367 -31.412 1.00 51.76  ? 390 ALA A CA  1 
ATOM 2964 C C   . ALA A 1 391 ? -3.612  -50.302 -32.687 1.00 54.23  ? 390 ALA A C   1 
ATOM 2965 O O   . ALA A 1 391 ? -4.140  -49.964 -33.753 1.00 48.95  ? 390 ALA A O   1 
ATOM 2966 C CB  . ALA A 1 391 ? -4.490  -48.998 -30.734 1.00 53.65  ? 390 ALA A CB  1 
ATOM 2967 N N   . ALA A 1 392 ? -2.320  -50.625 -32.599 1.00 52.48  ? 391 ALA A N   1 
ATOM 2968 C CA  . ALA A 1 392 ? -1.484  -50.694 -33.791 1.00 48.89  ? 391 ALA A CA  1 
ATOM 2969 C C   . ALA A 1 392 ? -1.727  -51.981 -34.572 1.00 49.28  ? 391 ALA A C   1 
ATOM 2970 O O   . ALA A 1 392 ? -1.723  -51.967 -35.808 1.00 50.93  ? 391 ALA A O   1 
ATOM 2971 C CB  . ALA A 1 392 ? -0.009  -50.568 -33.410 1.00 49.90  ? 391 ALA A CB  1 
ATOM 2972 N N   . GLN A 1 393 ? -1.935  -53.104 -33.876 1.00 47.68  ? 392 GLN A N   1 
ATOM 2973 C CA  . GLN A 1 393 ? -2.286  -54.338 -34.573 1.00 48.50  ? 392 GLN A CA  1 
ATOM 2974 C C   . GLN A 1 393 ? -3.640  -54.213 -35.254 1.00 47.09  ? 392 GLN A C   1 
ATOM 2975 O O   . GLN A 1 393 ? -3.840  -54.735 -36.357 1.00 48.28  ? 392 GLN A O   1 
ATOM 2976 C CB  . GLN A 1 393 ? -2.284  -55.522 -33.606 1.00 53.70  ? 392 GLN A CB  1 
ATOM 2977 C CG  . GLN A 1 393 ? -1.350  -55.367 -32.423 1.00 57.00  ? 392 GLN A CG  1 
ATOM 2978 C CD  . GLN A 1 393 ? -1.348  -56.582 -31.517 1.00 56.26  ? 392 GLN A CD  1 
ATOM 2979 O OE1 . GLN A 1 393 ? -1.979  -56.581 -30.460 1.00 55.46  ? 392 GLN A OE1 1 
ATOM 2980 N NE2 . GLN A 1 393 ? -0.626  -57.621 -31.919 1.00 63.09  ? 392 GLN A NE2 1 
ATOM 2981 N N   . ALA A 1 394 ? -4.587  -53.524 -34.611 1.00 48.83  ? 393 ALA A N   1 
ATOM 2982 C CA  . ALA A 1 394 ? -5.871  -53.264 -35.250 1.00 51.73  ? 393 ALA A CA  1 
ATOM 2983 C C   . ALA A 1 394 ? -5.698  -52.401 -36.493 1.00 48.32  ? 393 ALA A C   1 
ATOM 2984 O O   . ALA A 1 394 ? -6.371  -52.615 -37.507 1.00 49.31  ? 393 ALA A O   1 
ATOM 2985 C CB  . ALA A 1 394 ? -6.826  -52.597 -34.260 1.00 51.73  ? 393 ALA A CB  1 
ATOM 2986 N N   . TYR A 1 395 ? -4.792  -51.422 -36.433 1.00 49.54  ? 394 TYR A N   1 
ATOM 2987 C CA  . TYR A 1 395 ? -4.512  -50.595 -37.602 1.00 43.39  ? 394 TYR A CA  1 
ATOM 2988 C C   . TYR A 1 395 ? -3.773  -51.387 -38.672 1.00 46.42  ? 394 TYR A C   1 
ATOM 2989 O O   . TYR A 1 395 ? -4.000  -51.185 -39.871 1.00 48.56  ? 394 TYR A O   1 
ATOM 2990 C CB  . TYR A 1 395 ? -3.705  -49.366 -37.183 1.00 44.09  ? 394 TYR A CB  1 
ATOM 2991 C CG  . TYR A 1 395 ? -3.038  -48.625 -38.322 1.00 46.20  ? 394 TYR A CG  1 
ATOM 2992 C CD1 . TYR A 1 395 ? -3.761  -47.760 -39.131 1.00 43.81  ? 394 TYR A CD1 1 
ATOM 2993 C CD2 . TYR A 1 395 ? -1.680  -48.781 -38.578 1.00 48.55  ? 394 TYR A CD2 1 
ATOM 2994 C CE1 . TYR A 1 395 ? -3.152  -47.075 -40.167 1.00 49.67  ? 394 TYR A CE1 1 
ATOM 2995 C CE2 . TYR A 1 395 ? -1.063  -48.101 -39.613 1.00 45.93  ? 394 TYR A CE2 1 
ATOM 2996 C CZ  . TYR A 1 395 ? -1.805  -47.250 -40.404 1.00 48.43  ? 394 TYR A CZ  1 
ATOM 2997 O OH  . TYR A 1 395 ? -1.204  -46.569 -41.437 1.00 48.67  ? 394 TYR A OH  1 
ATOM 2998 N N   . MET A 1 396 ? -2.887  -52.293 -38.261 1.00 45.12  ? 395 MET A N   1 
ATOM 2999 C CA  . MET A 1 396 ? -2.131  -53.082 -39.226 1.00 44.93  ? 395 MET A CA  1 
ATOM 3000 C C   . MET A 1 396 ? -2.996  -54.167 -39.854 1.00 46.35  ? 395 MET A C   1 
ATOM 3001 O O   . MET A 1 396 ? -2.992  -54.344 -41.077 1.00 50.95  ? 395 MET A O   1 
ATOM 3002 C CB  . MET A 1 396 ? -0.903  -53.697 -38.553 1.00 44.53  ? 395 MET A CB  1 
ATOM 3003 C CG  . MET A 1 396 ? -0.008  -54.481 -39.497 1.00 47.01  ? 395 MET A CG  1 
ATOM 3004 S SD  . MET A 1 396 ? 0.966   -55.741 -38.652 1.00 46.83  ? 395 MET A SD  1 
ATOM 3005 C CE  . MET A 1 396 ? -0.325  -56.839 -38.070 1.00 46.08  ? 395 MET A CE  1 
ATOM 3006 N N   . ALA A 1 397 ? -3.750  -54.901 -39.031 1.00 46.73  ? 396 ALA A N   1 
ATOM 3007 C CA  . ALA A 1 397 ? -4.566  -55.989 -39.558 1.00 47.48  ? 396 ALA A CA  1 
ATOM 3008 C C   . ALA A 1 397 ? -5.718  -55.471 -40.408 1.00 49.76  ? 396 ALA A C   1 
ATOM 3009 O O   . ALA A 1 397 ? -6.174  -56.172 -41.319 1.00 50.05  ? 396 ALA A O   1 
ATOM 3010 C CB  . ALA A 1 397 ? -5.096  -56.855 -38.415 1.00 46.46  ? 396 ALA A CB  1 
ATOM 3011 N N   . THR A 1 398 ? -6.198  -54.256 -40.131 1.00 45.90  ? 397 THR A N   1 
ATOM 3012 C CA  . THR A 1 398 ? -7.271  -53.683 -40.939 1.00 49.59  ? 397 THR A CA  1 
ATOM 3013 C C   . THR A 1 398 ? -6.814  -53.459 -42.374 1.00 48.00  ? 397 THR A C   1 
ATOM 3014 O O   . THR A 1 398 ? -7.490  -53.866 -43.325 1.00 48.38  ? 397 THR A O   1 
ATOM 3015 C CB  . THR A 1 398 ? -7.753  -52.369 -40.324 1.00 45.73  ? 397 THR A CB  1 
ATOM 3016 O OG1 . THR A 1 398 ? -8.548  -52.643 -39.164 1.00 48.60  ? 397 THR A OG1 1 
ATOM 3017 C CG2 . THR A 1 398 ? -8.584  -51.584 -41.328 1.00 48.76  ? 397 THR A CG2 1 
ATOM 3018 N N   . TYR A 1 399 ? -5.661  -52.814 -42.548 1.00 46.85  ? 398 TYR A N   1 
ATOM 3019 C CA  . TYR A 1 399 ? -5.154  -52.513 -43.878 1.00 43.48  ? 398 TYR A CA  1 
ATOM 3020 C C   . TYR A 1 399 ? -4.425  -53.686 -44.516 1.00 45.66  ? 398 TYR A C   1 
ATOM 3021 O O   . TYR A 1 399 ? -4.145  -53.640 -45.719 1.00 49.11  ? 398 TYR A O   1 
ATOM 3022 C CB  . TYR A 1 399 ? -4.242  -51.286 -43.818 1.00 42.60  ? 398 TYR A CB  1 
ATOM 3023 C CG  . TYR A 1 399 ? -5.013  -50.007 -43.583 1.00 45.22  ? 398 TYR A CG  1 
ATOM 3024 C CD1 . TYR A 1 399 ? -5.729  -49.409 -44.612 1.00 43.97  ? 398 TYR A CD1 1 
ATOM 3025 C CD2 . TYR A 1 399 ? -5.047  -49.410 -42.329 1.00 41.26  ? 398 TYR A CD2 1 
ATOM 3026 C CE1 . TYR A 1 399 ? -6.445  -48.246 -44.405 1.00 43.12  ? 398 TYR A CE1 1 
ATOM 3027 C CE2 . TYR A 1 399 ? -5.762  -48.246 -42.112 1.00 45.76  ? 398 TYR A CE2 1 
ATOM 3028 C CZ  . TYR A 1 399 ? -6.459  -47.668 -43.153 1.00 46.31  ? 398 TYR A CZ  1 
ATOM 3029 O OH  . TYR A 1 399 ? -7.172  -46.510 -42.944 1.00 46.37  ? 398 TYR A OH  1 
ATOM 3030 N N   . ILE A 1 400 ? -4.115  -54.733 -43.751 1.00 45.05  ? 399 ILE A N   1 
ATOM 3031 C CA  . ILE A 1 400 ? -3.602  -55.958 -44.354 1.00 43.41  ? 399 ILE A CA  1 
ATOM 3032 C C   . ILE A 1 400 ? -4.707  -56.657 -45.136 1.00 45.39  ? 399 ILE A C   1 
ATOM 3033 O O   . ILE A 1 400 ? -4.513  -57.070 -46.285 1.00 53.70  ? 399 ILE A O   1 
ATOM 3034 C CB  . ILE A 1 400 ? -2.993  -56.875 -43.278 1.00 48.38  ? 399 ILE A CB  1 
ATOM 3035 C CG1 . ILE A 1 400 ? -1.532  -56.495 -43.028 1.00 48.72  ? 399 ILE A CG1 1 
ATOM 3036 C CG2 . ILE A 1 400 ? -3.104  -58.340 -43.683 1.00 43.45  ? 399 ILE A CG2 1 
ATOM 3037 C CD1 . ILE A 1 400 ? -0.804  -57.438 -42.097 1.00 40.30  ? 399 ILE A CD1 1 
ATOM 3038 N N   . VAL A 1 401 ? -5.891  -56.780 -44.533 1.00 43.73  ? 400 VAL A N   1 
ATOM 3039 C CA  . VAL A 1 401 ? -7.014  -57.393 -45.232 1.00 47.05  ? 400 VAL A CA  1 
ATOM 3040 C C   . VAL A 1 401 ? -7.708  -56.412 -46.169 1.00 49.14  ? 400 VAL A C   1 
ATOM 3041 O O   . VAL A 1 401 ? -8.398  -56.840 -47.102 1.00 52.45  ? 400 VAL A O   1 
ATOM 3042 C CB  . VAL A 1 401 ? -8.022  -57.983 -44.230 1.00 49.47  ? 400 VAL A CB  1 
ATOM 3043 C CG1 . VAL A 1 401 ? -7.289  -58.721 -43.118 1.00 48.63  ? 400 VAL A CG1 1 
ATOM 3044 C CG2 . VAL A 1 401 ? -8.909  -56.896 -43.655 1.00 49.07  ? 400 VAL A CG2 1 
ATOM 3045 N N   . TYR A 1 402 ? -7.538  -55.106 -45.954 1.00 48.40  ? 401 TYR A N   1 
ATOM 3046 C CA  . TYR A 1 402 ? -8.139  -54.130 -46.856 1.00 47.93  ? 401 TYR A CA  1 
ATOM 3047 C C   . TYR A 1 402 ? -7.408  -54.098 -48.193 1.00 51.93  ? 401 TYR A C   1 
ATOM 3048 O O   . TYR A 1 402 ? -8.044  -54.068 -49.254 1.00 51.11  ? 401 TYR A O   1 
ATOM 3049 C CB  . TYR A 1 402 ? -8.145  -52.749 -46.203 1.00 42.56  ? 401 TYR A CB  1 
ATOM 3050 C CG  . TYR A 1 402 ? -8.720  -51.661 -47.077 1.00 46.42  ? 401 TYR A CG  1 
ATOM 3051 C CD1 . TYR A 1 402 ? -10.036 -51.720 -47.519 1.00 44.30  ? 401 TYR A CD1 1 
ATOM 3052 C CD2 . TYR A 1 402 ? -7.944  -50.578 -47.465 1.00 45.00  ? 401 TYR A CD2 1 
ATOM 3053 C CE1 . TYR A 1 402 ? -10.563 -50.725 -48.320 1.00 46.60  ? 401 TYR A CE1 1 
ATOM 3054 C CE2 . TYR A 1 402 ? -8.461  -49.580 -48.265 1.00 43.13  ? 401 TYR A CE2 1 
ATOM 3055 C CZ  . TYR A 1 402 ? -9.770  -49.658 -48.689 1.00 46.06  ? 401 TYR A CZ  1 
ATOM 3056 O OH  . TYR A 1 402 ? -10.286 -48.665 -49.488 1.00 47.17  ? 401 TYR A OH  1 
ATOM 3057 N N   . PHE A 1 403 ? -6.072  -54.109 -48.163 1.00 48.26  ? 402 PHE A N   1 
ATOM 3058 C CA  . PHE A 1 403 ? -5.307  -54.182 -49.402 1.00 43.21  ? 402 PHE A CA  1 
ATOM 3059 C C   . PHE A 1 403 ? -5.564  -55.488 -50.142 1.00 50.14  ? 402 PHE A C   1 
ATOM 3060 O O   . PHE A 1 403 ? -5.520  -55.518 -51.377 1.00 53.09  ? 402 PHE A O   1 
ATOM 3061 C CB  . PHE A 1 403 ? -3.815  -54.027 -49.112 1.00 42.67  ? 402 PHE A CB  1 
ATOM 3062 C CG  . PHE A 1 403 ? -2.958  -54.022 -50.345 1.00 47.61  ? 402 PHE A CG  1 
ATOM 3063 C CD1 . PHE A 1 403 ? -3.040  -52.982 -51.257 1.00 49.87  ? 402 PHE A CD1 1 
ATOM 3064 C CD2 . PHE A 1 403 ? -2.075  -55.060 -50.595 1.00 49.63  ? 402 PHE A CD2 1 
ATOM 3065 C CE1 . PHE A 1 403 ? -2.252  -52.975 -52.393 1.00 47.90  ? 402 PHE A CE1 1 
ATOM 3066 C CE2 . PHE A 1 403 ? -1.285  -55.058 -51.729 1.00 47.71  ? 402 PHE A CE2 1 
ATOM 3067 C CZ  . PHE A 1 403 ? -1.374  -54.014 -52.629 1.00 49.77  ? 402 PHE A CZ  1 
ATOM 3068 N N   . SER A 1 404 ? -5.828  -56.574 -49.411 1.00 53.15  ? 403 SER A N   1 
ATOM 3069 C CA  . SER A 1 404 ? -6.180  -57.829 -50.065 1.00 51.62  ? 403 SER A CA  1 
ATOM 3070 C C   . SER A 1 404 ? -7.546  -57.735 -50.730 1.00 49.92  ? 403 SER A C   1 
ATOM 3071 O O   . SER A 1 404 ? -7.736  -58.234 -51.846 1.00 52.67  ? 403 SER A O   1 
ATOM 3072 C CB  . SER A 1 404 ? -6.148  -58.977 -49.056 1.00 49.99  ? 403 SER A CB  1 
ATOM 3073 O OG  . SER A 1 404 ? -5.040  -58.857 -48.182 1.00 46.99  ? 403 SER A OG  1 
ATOM 3074 N N   . LEU A 1 405 ? -8.508  -57.091 -50.063 1.00 50.44  ? 404 LEU A N   1 
ATOM 3075 C CA  . LEU A 1 405 ? -9.827  -56.908 -50.659 1.00 51.79  ? 404 LEU A CA  1 
ATOM 3076 C C   . LEU A 1 405 ? -9.778  -55.915 -51.814 1.00 53.22  ? 404 LEU A C   1 
ATOM 3077 O O   . LEU A 1 405 ? -10.493 -56.079 -52.810 1.00 55.85  ? 404 LEU A O   1 
ATOM 3078 C CB  . LEU A 1 405 ? -10.828 -56.453 -49.594 1.00 52.05  ? 404 LEU A CB  1 
ATOM 3079 C CG  . LEU A 1 405 ? -11.248 -57.480 -48.536 1.00 51.82  ? 404 LEU A CG  1 
ATOM 3080 C CD1 . LEU A 1 405 ? -12.595 -57.117 -47.924 1.00 46.34  ? 404 LEU A CD1 1 
ATOM 3081 C CD2 . LEU A 1 405 ? -11.285 -58.886 -49.118 1.00 54.98  ? 404 LEU A CD2 1 
ATOM 3082 N N   . CYS A 1 406 ? -8.942  -54.878 -51.703 1.00 48.12  ? 405 CYS A N   1 
ATOM 3083 C CA  . CYS A 1 406 ? -8.787  -53.934 -52.806 1.00 45.94  ? 405 CYS A CA  1 
ATOM 3084 C C   . CYS A 1 406 ? -8.203  -54.616 -54.037 1.00 50.32  ? 405 CYS A C   1 
ATOM 3085 O O   . CYS A 1 406 ? -8.602  -54.319 -55.169 1.00 51.18  ? 405 CYS A O   1 
ATOM 3086 C CB  . CYS A 1 406 ? -7.907  -52.759 -52.379 1.00 47.38  ? 405 CYS A CB  1 
ATOM 3087 S SG  . CYS A 1 406 ? -8.794  -51.396 -51.591 1.00 50.34  ? 405 CYS A SG  1 
ATOM 3088 N N   . CYS A 1 407 ? -7.251  -55.532 -53.833 1.00 53.97  ? 406 CYS A N   1 
ATOM 3089 C CA  . CYS A 1 407 ? -6.696  -56.294 -54.949 1.00 52.59  ? 406 CYS A CA  1 
ATOM 3090 C C   . CYS A 1 407 ? -7.743  -57.211 -55.566 1.00 52.18  ? 406 CYS A C   1 
ATOM 3091 O O   . CYS A 1 407 ? -7.848  -57.306 -56.795 1.00 50.95  ? 406 CYS A O   1 
ATOM 3092 C CB  . CYS A 1 407 ? -5.491  -57.111 -54.485 1.00 46.40  ? 406 CYS A CB  1 
ATOM 3093 S SG  . CYS A 1 407 ? -3.966  -56.175 -54.265 1.00 59.15  ? 406 CYS A SG  1 
ATOM 3094 N N   . GLY A 1 408 ? -8.519  -57.901 -54.728 1.00 48.46  ? 407 GLY A N   1 
ATOM 3095 C CA  . GLY A 1 408 ? -9.542  -58.793 -55.248 1.00 46.79  ? 407 GLY A CA  1 
ATOM 3096 C C   . GLY A 1 408 ? -10.649 -58.053 -55.973 1.00 49.90  ? 407 GLY A C   1 
ATOM 3097 O O   . GLY A 1 408 ? -11.097 -58.482 -57.040 1.00 56.91  ? 407 GLY A O   1 
ATOM 3098 N N   . VAL A 1 409 ? -11.104 -56.931 -55.410 1.00 49.30  ? 408 VAL A N   1 
ATOM 3099 C CA  . VAL A 1 409 ? -12.149 -56.148 -56.064 1.00 48.55  ? 408 VAL A CA  1 
ATOM 3100 C C   . VAL A 1 409 ? -11.632 -55.555 -57.370 1.00 46.21  ? 408 VAL A C   1 
ATOM 3101 O O   . VAL A 1 409 ? -12.359 -55.491 -58.368 1.00 48.05  ? 408 VAL A O   1 
ATOM 3102 C CB  . VAL A 1 409 ? -12.682 -55.063 -55.109 1.00 44.01  ? 408 VAL A CB  1 
ATOM 3103 C CG1 . VAL A 1 409 ? -13.545 -54.059 -55.859 1.00 39.72  ? 408 VAL A CG1 1 
ATOM 3104 C CG2 . VAL A 1 409 ? -13.474 -55.698 -53.979 1.00 36.75  ? 408 VAL A CG2 1 
ATOM 3105 N N   . PHE A 1 410 ? -10.366 -55.127 -57.392 1.00 43.16  ? 409 PHE A N   1 
ATOM 3106 C CA  . PHE A 1 410 ? -9.788  -54.603 -58.626 1.00 50.46  ? 409 PHE A CA  1 
ATOM 3107 C C   . PHE A 1 410 ? -9.692  -55.685 -59.693 1.00 51.72  ? 409 PHE A C   1 
ATOM 3108 O O   . PHE A 1 410 ? -9.890  -55.414 -60.884 1.00 51.65  ? 409 PHE A O   1 
ATOM 3109 C CB  . PHE A 1 410 ? -8.408  -54.006 -58.355 1.00 48.75  ? 409 PHE A CB  1 
ATOM 3110 C CG  . PHE A 1 410 ? -7.760  -53.397 -59.568 1.00 49.92  ? 409 PHE A CG  1 
ATOM 3111 C CD1 . PHE A 1 410 ? -8.269  -52.241 -60.138 1.00 50.78  ? 409 PHE A CD1 1 
ATOM 3112 C CD2 . PHE A 1 410 ? -6.644  -53.985 -60.141 1.00 54.74  ? 409 PHE A CD2 1 
ATOM 3113 C CE1 . PHE A 1 410 ? -7.674  -51.680 -61.253 1.00 52.97  ? 409 PHE A CE1 1 
ATOM 3114 C CE2 . PHE A 1 410 ? -6.045  -53.429 -61.258 1.00 55.90  ? 409 PHE A CE2 1 
ATOM 3115 C CZ  . PHE A 1 410 ? -6.561  -52.276 -61.814 1.00 54.45  ? 409 PHE A CZ  1 
ATOM 3116 N N   . LEU A 1 411 ? -9.383  -56.917 -59.287 1.00 49.21  ? 410 LEU A N   1 
ATOM 3117 C CA  . LEU A 1 411 ? -9.308  -58.011 -60.248 1.00 48.08  ? 410 LEU A CA  1 
ATOM 3118 C C   . LEU A 1 411 ? -10.685 -58.346 -60.808 1.00 53.49  ? 410 LEU A C   1 
ATOM 3119 O O   . LEU A 1 411 ? -10.829 -58.578 -62.014 1.00 60.91  ? 410 LEU A O   1 
ATOM 3120 C CB  . LEU A 1 411 ? -8.672  -59.237 -59.595 1.00 48.94  ? 410 LEU A CB  1 
ATOM 3121 C CG  . LEU A 1 411 ? -7.166  -59.149 -59.340 1.00 45.37  ? 410 LEU A CG  1 
ATOM 3122 C CD1 . LEU A 1 411 ? -6.693  -60.355 -58.547 1.00 47.21  ? 410 LEU A CD1 1 
ATOM 3123 C CD2 . LEU A 1 411 ? -6.400  -59.030 -60.650 1.00 48.76  ? 410 LEU A CD2 1 
ATOM 3124 N N   . LEU A 1 412 ? -11.711 -58.371 -59.952 1.00 47.67  ? 411 LEU A N   1 
ATOM 3125 C CA  . LEU A 1 412 ? -13.066 -58.603 -60.441 1.00 50.26  ? 411 LEU A CA  1 
ATOM 3126 C C   . LEU A 1 412 ? -13.546 -57.460 -61.325 1.00 55.61  ? 411 LEU A C   1 
ATOM 3127 O O   . LEU A 1 412 ? -14.351 -57.677 -62.237 1.00 60.75  ? 411 LEU A O   1 
ATOM 3128 C CB  . LEU A 1 412 ? -14.026 -58.801 -59.269 1.00 44.40  ? 411 LEU A CB  1 
ATOM 3129 C CG  . LEU A 1 412 ? -13.712 -59.954 -58.317 1.00 45.18  ? 411 LEU A CG  1 
ATOM 3130 C CD1 . LEU A 1 412 ? -14.581 -59.867 -57.073 1.00 43.53  ? 411 LEU A CD1 1 
ATOM 3131 C CD2 . LEU A 1 412 ? -13.903 -61.288 -59.016 1.00 53.03  ? 411 LEU A CD2 1 
ATOM 3132 N N   . TRP A 1 413 ? -13.065 -56.241 -61.069 1.00 56.31  ? 412 TRP A N   1 
ATOM 3133 C CA  . TRP A 1 413 ? -13.433 -55.100 -61.899 1.00 56.11  ? 412 TRP A CA  1 
ATOM 3134 C C   . TRP A 1 413 ? -12.728 -55.141 -63.249 1.00 60.66  ? 412 TRP A C   1 
ATOM 3135 O O   . TRP A 1 413 ? -13.254 -54.621 -64.240 1.00 61.37  ? 412 TRP A O   1 
ATOM 3136 C CB  . TRP A 1 413 ? -13.108 -53.801 -61.160 1.00 53.95  ? 412 TRP A CB  1 
ATOM 3137 C CG  . TRP A 1 413 ? -13.263 -52.555 -61.979 1.00 57.99  ? 412 TRP A CG  1 
ATOM 3138 C CD1 . TRP A 1 413 ? -14.415 -51.859 -62.204 1.00 60.53  ? 412 TRP A CD1 1 
ATOM 3139 C CD2 . TRP A 1 413 ? -12.228 -51.852 -62.678 1.00 60.90  ? 412 TRP A CD2 1 
ATOM 3140 N NE1 . TRP A 1 413 ? -14.162 -50.768 -63.000 1.00 64.93  ? 412 TRP A NE1 1 
ATOM 3141 C CE2 . TRP A 1 413 ? -12.827 -50.742 -63.305 1.00 65.27  ? 412 TRP A CE2 1 
ATOM 3142 C CE3 . TRP A 1 413 ? -10.854 -52.056 -62.836 1.00 59.17  ? 412 TRP A CE3 1 
ATOM 3143 C CZ2 . TRP A 1 413 ? -12.099 -49.838 -64.078 1.00 60.47  ? 412 TRP A CZ2 1 
ATOM 3144 C CZ3 . TRP A 1 413 ? -10.134 -51.158 -63.604 1.00 56.37  ? 412 TRP A CZ3 1 
ATOM 3145 C CH2 . TRP A 1 413 ? -10.757 -50.063 -64.213 1.00 53.30  ? 412 TRP A CH2 1 
ATOM 3146 N N   . ARG A 1 414 ? -11.546 -55.758 -63.309 1.00 58.26  ? 413 ARG A N   1 
ATOM 3147 C CA  . ARG A 1 414 ? -10.795 -55.823 -64.557 1.00 60.42  ? 413 ARG A CA  1 
ATOM 3148 C C   . ARG A 1 414 ? -11.393 -56.849 -65.513 1.00 63.05  ? 413 ARG A C   1 
ATOM 3149 O O   . ARG A 1 414 ? -11.643 -56.543 -66.685 1.00 64.58  ? 413 ARG A O   1 
ATOM 3150 C CB  . ARG A 1 414 ? -9.327  -56.144 -64.263 1.00 58.03  ? 413 ARG A CB  1 
ATOM 3151 C CG  . ARG A 1 414 ? -8.499  -56.509 -65.484 1.00 68.07  ? 413 ARG A CG  1 
ATOM 3152 C CD  . ARG A 1 414 ? -7.198  -57.179 -65.073 1.00 69.23  ? 413 ARG A CD  1 
ATOM 3153 N NE  . ARG A 1 414 ? -6.189  -57.114 -66.124 1.00 77.86  ? 413 ARG A NE  1 
ATOM 3154 C CZ  . ARG A 1 414 ? -4.975  -57.643 -66.032 1.00 75.69  ? 413 ARG A CZ  1 
ATOM 3155 N NH1 . ARG A 1 414 ? -4.586  -58.295 -64.948 1.00 75.16  ? 413 ARG A NH1 1 
ATOM 3156 N NH2 . ARG A 1 414 ? -4.131  -57.512 -67.051 1.00 65.36  ? 413 ARG A NH2 1 
ATOM 3157 N N   . ARG A 1 415 ? -11.634 -58.064 -65.033 1.00 64.61  ? 414 ARG A N   1 
ATOM 3158 C CA  . ARG A 1 415 ? -12.201 -59.119 -65.866 1.00 67.89  ? 414 ARG A CA  1 
ATOM 3159 C C   . ARG A 1 415 ? -13.651 -58.814 -66.232 1.00 69.55  ? 414 ARG A C   1 
ATOM 3160 O O   . ARG A 1 415 ? -14.144 -59.255 -67.270 1.00 69.42  ? 414 ARG A O   1 
ATOM 3161 C CB  . ARG A 1 415 ? -12.117 -60.472 -65.155 1.00 75.78  ? 414 ARG A CB  1 
ATOM 3162 C CG  . ARG A 1 415 ? -10.839 -60.684 -64.360 1.00 72.14  ? 414 ARG A CG  1 
ATOM 3163 C CD  . ARG A 1 415 ? -10.497 -62.162 -64.244 1.00 73.09  ? 414 ARG A CD  1 
ATOM 3164 N NE  . ARG A 1 415 ? -9.322  -62.513 -65.033 1.00 74.88  ? 414 ARG A NE  1 
ATOM 3165 C CZ  . ARG A 1 415 ? -9.001  -63.748 -65.391 1.00 75.70  ? 414 ARG A CZ  1 
ATOM 3166 N NH1 . ARG A 1 415 ? -9.756  -64.783 -65.059 1.00 72.99  ? 414 ARG A NH1 1 
ATOM 3167 N NH2 . ARG A 1 415 ? -7.895  -63.951 -66.101 1.00 73.98  ? 414 ARG A NH2 1 
ATOM 3168 N N   . ALA B 2 2   ? -1.604  -27.282 -12.891 1.00 77.09  ? 0   ALA B N   1 
ATOM 3169 C CA  . ALA B 2 2   ? -0.835  -26.111 -12.484 1.00 77.96  ? 0   ALA B CA  1 
ATOM 3170 C C   . ALA B 2 2   ? -1.545  -24.817 -12.877 1.00 84.58  ? 0   ALA B C   1 
ATOM 3171 O O   . ALA B 2 2   ? -0.977  -23.974 -13.574 1.00 77.63  ? 0   ALA B O   1 
ATOM 3172 C CB  . ALA B 2 2   ? 0.559   -26.158 -13.090 1.00 74.96  ? 0   ALA B CB  1 
ATOM 3173 N N   . GLN B 2 3   ? -2.788  -24.667 -12.426 1.00 95.32  ? 1   GLN B N   1 
ATOM 3174 C CA  . GLN B 2 3   ? -3.592  -23.482 -12.699 1.00 88.45  ? 1   GLN B CA  1 
ATOM 3175 C C   . GLN B 2 3   ? -3.530  -22.539 -11.505 1.00 80.33  ? 1   GLN B C   1 
ATOM 3176 O O   . GLN B 2 3   ? -3.725  -22.964 -10.361 1.00 80.78  ? 1   GLN B O   1 
ATOM 3177 C CB  . GLN B 2 3   ? -5.045  -23.859 -12.994 1.00 87.92  ? 1   GLN B CB  1 
ATOM 3178 C CG  . GLN B 2 3   ? -5.212  -25.083 -13.883 1.00 91.22  ? 1   GLN B CG  1 
ATOM 3179 C CD  . GLN B 2 3   ? -5.313  -24.730 -15.357 1.00 98.47  ? 1   GLN B CD  1 
ATOM 3180 O OE1 . GLN B 2 3   ? -6.277  -24.099 -15.793 1.00 109.40 ? 1   GLN B OE1 1 
ATOM 3181 N NE2 . GLN B 2 3   ? -4.315  -25.137 -16.133 1.00 89.89  ? 1   GLN B NE2 1 
ATOM 3182 N N   . VAL B 2 4   ? -3.261  -21.266 -11.772 1.00 68.07  ? 2   VAL B N   1 
ATOM 3183 C CA  . VAL B 2 4   ? -3.192  -20.273 -10.707 1.00 74.63  ? 2   VAL B CA  1 
ATOM 3184 C C   . VAL B 2 4   ? -4.604  -19.857 -10.320 1.00 72.60  ? 2   VAL B C   1 
ATOM 3185 O O   . VAL B 2 4   ? -5.507  -19.781 -11.164 1.00 63.63  ? 2   VAL B O   1 
ATOM 3186 C CB  . VAL B 2 4   ? -2.330  -19.071 -11.137 1.00 68.81  ? 2   VAL B CB  1 
ATOM 3187 C CG1 . VAL B 2 4   ? -1.083  -19.555 -11.855 1.00 67.81  ? 2   VAL B CG1 1 
ATOM 3188 C CG2 . VAL B 2 4   ? -3.114  -18.111 -12.015 1.00 63.01  ? 2   VAL B CG2 1 
ATOM 3189 N N   . GLN B 2 5   ? -4.807  -19.617 -9.028  1.00 67.75  ? 3   GLN B N   1 
ATOM 3190 C CA  . GLN B 2 5   ? -6.108  -19.265 -8.483  1.00 57.90  ? 3   GLN B CA  1 
ATOM 3191 C C   . GLN B 2 5   ? -6.116  -17.789 -8.125  1.00 58.95  ? 3   GLN B C   1 
ATOM 3192 O O   . GLN B 2 5   ? -5.203  -17.306 -7.448  1.00 57.20  ? 3   GLN B O   1 
ATOM 3193 C CB  . GLN B 2 5   ? -6.429  -20.113 -7.254  1.00 59.87  ? 3   GLN B CB  1 
ATOM 3194 C CG  . GLN B 2 5   ? -7.025  -21.464 -7.581  1.00 65.51  ? 3   GLN B CG  1 
ATOM 3195 C CD  . GLN B 2 5   ? -6.504  -22.553 -6.668  1.00 79.54  ? 3   GLN B CD  1 
ATOM 3196 O OE1 . GLN B 2 5   ? -7.261  -23.160 -5.912  1.00 81.65  ? 3   GLN B OE1 1 
ATOM 3197 N NE2 . GLN B 2 5   ? -5.203  -22.814 -6.740  1.00 82.13  ? 3   GLN B NE2 1 
ATOM 3198 N N   . LEU B 2 6   ? -7.141  -17.078 -8.581  1.00 60.76  ? 4   LEU B N   1 
ATOM 3199 C CA  . LEU B 2 6   ? -7.272  -15.647 -8.349  1.00 55.99  ? 4   LEU B CA  1 
ATOM 3200 C C   . LEU B 2 6   ? -8.498  -15.403 -7.481  1.00 55.88  ? 4   LEU B C   1 
ATOM 3201 O O   . LEU B 2 6   ? -9.617  -15.766 -7.861  1.00 53.77  ? 4   LEU B O   1 
ATOM 3202 C CB  . LEU B 2 6   ? -7.376  -14.889 -9.672  1.00 58.20  ? 4   LEU B CB  1 
ATOM 3203 C CG  . LEU B 2 6   ? -6.232  -15.135 -10.660 1.00 59.61  ? 4   LEU B CG  1 
ATOM 3204 C CD1 . LEU B 2 6   ? -6.631  -14.707 -12.061 1.00 62.59  ? 4   LEU B CD1 1 
ATOM 3205 C CD2 . LEU B 2 6   ? -4.963  -14.419 -10.220 1.00 58.88  ? 4   LEU B CD2 1 
ATOM 3206 N N   . VAL B 2 7   ? -8.283  -14.800 -6.317  1.00 59.10  ? 5   VAL B N   1 
ATOM 3207 C CA  . VAL B 2 7   ? -9.344  -14.504 -5.364  1.00 61.26  ? 5   VAL B CA  1 
ATOM 3208 C C   . VAL B 2 7   ? -9.370  -12.995 -5.172  1.00 59.46  ? 5   VAL B C   1 
ATOM 3209 O O   . VAL B 2 7   ? -8.412  -12.413 -4.649  1.00 61.45  ? 5   VAL B O   1 
ATOM 3210 C CB  . VAL B 2 7   ? -9.135  -15.230 -4.028  1.00 62.24  ? 5   VAL B CB  1 
ATOM 3211 C CG1 . VAL B 2 7   ? -10.121 -14.724 -2.985  1.00 66.54  ? 5   VAL B CG1 1 
ATOM 3212 C CG2 . VAL B 2 7   ? -9.261  -16.735 -4.215  1.00 58.30  ? 5   VAL B CG2 1 
ATOM 3213 N N   . GLU B 2 8   ? -10.458 -12.362 -5.599  1.00 56.68  ? 6   GLU B N   1 
ATOM 3214 C CA  . GLU B 2 8   ? -10.620 -10.924 -5.461  1.00 58.26  ? 6   GLU B CA  1 
ATOM 3215 C C   . GLU B 2 8   ? -11.265 -10.579 -4.122  1.00 59.34  ? 6   GLU B C   1 
ATOM 3216 O O   . GLU B 2 8   ? -11.932 -11.404 -3.492  1.00 62.44  ? 6   GLU B O   1 
ATOM 3217 C CB  . GLU B 2 8   ? -11.463 -10.360 -6.605  1.00 60.27  ? 6   GLU B CB  1 
ATOM 3218 C CG  . GLU B 2 8   ? -10.858 -10.577 -7.980  1.00 57.55  ? 6   GLU B CG  1 
ATOM 3219 C CD  . GLU B 2 8   ? -11.623 -11.594 -8.799  1.00 53.11  ? 6   GLU B CD  1 
ATOM 3220 O OE1 . GLU B 2 8   ? -12.523 -12.255 -8.241  1.00 58.49  ? 6   GLU B OE1 1 
ATOM 3221 O OE2 . GLU B 2 8   ? -11.321 -11.737 -9.999  1.00 51.01  ? 6   GLU B OE2 1 
ATOM 3222 N N   . SER B 2 9   ? -11.059 -9.336  -3.696  1.00 57.39  ? 7   SER B N   1 
ATOM 3223 C CA  . SER B 2 9   ? -11.614 -8.855  -2.439  1.00 56.48  ? 7   SER B CA  1 
ATOM 3224 C C   . SER B 2 9   ? -11.621 -7.335  -2.453  1.00 56.05  ? 7   SER B C   1 
ATOM 3225 O O   . SER B 2 9   ? -10.885 -6.698  -3.213  1.00 49.48  ? 7   SER B O   1 
ATOM 3226 C CB  . SER B 2 9   ? -10.822 -9.378  -1.234  1.00 58.24  ? 7   SER B CB  1 
ATOM 3227 O OG  . SER B 2 9   ? -9.429  -9.374  -1.493  1.00 58.30  ? 7   SER B OG  1 
ATOM 3228 N N   . GLY B 2 10  ? -12.468 -6.762  -1.600  1.00 60.94  ? 8   GLY B N   1 
ATOM 3229 C CA  . GLY B 2 10  ? -12.549 -5.323  -1.469  1.00 49.93  ? 8   GLY B CA  1 
ATOM 3230 C C   . GLY B 2 10  ? -13.626 -4.659  -2.294  1.00 49.48  ? 8   GLY B C   1 
ATOM 3231 O O   . GLY B 2 10  ? -13.516 -3.461  -2.579  1.00 50.17  ? 8   GLY B O   1 
ATOM 3232 N N   . GLY B 2 11  ? -14.664 -5.389  -2.685  1.00 56.81  ? 9   GLY B N   1 
ATOM 3233 C CA  . GLY B 2 11  ? -15.750 -4.833  -3.474  1.00 57.01  ? 9   GLY B CA  1 
ATOM 3234 C C   . GLY B 2 11  ? -16.911 -4.411  -2.589  1.00 66.17  ? 9   GLY B C   1 
ATOM 3235 O O   . GLY B 2 11  ? -17.252 -5.097  -1.626  1.00 80.52  ? 9   GLY B O   1 
ATOM 3236 N N   . GLY B 2 12  ? -17.502 -3.272  -2.921  1.00 57.73  ? 10  GLY B N   1 
ATOM 3237 C CA  . GLY B 2 12  ? -18.608 -2.770  -2.134  1.00 56.82  ? 10  GLY B CA  1 
ATOM 3238 C C   . GLY B 2 12  ? -19.338 -1.656  -2.848  1.00 52.50  ? 10  GLY B C   1 
ATOM 3239 O O   . GLY B 2 12  ? -19.087 -1.369  -4.020  1.00 56.09  ? 10  GLY B O   1 
ATOM 3240 N N   . LEU B 2 13  ? -20.253 -1.028  -2.114  1.00 52.85  ? 11  LEU B N   1 
ATOM 3241 C CA  . LEU B 2 13  ? -21.088 0.048   -2.632  1.00 54.67  ? 11  LEU B CA  1 
ATOM 3242 C C   . LEU B 2 13  ? -20.561 1.383   -2.118  1.00 58.39  ? 11  LEU B C   1 
ATOM 3243 O O   . LEU B 2 13  ? -20.536 1.622   -0.906  1.00 55.27  ? 11  LEU B O   1 
ATOM 3244 C CB  . LEU B 2 13  ? -22.547 -0.157  -2.220  1.00 54.12  ? 11  LEU B CB  1 
ATOM 3245 C CG  . LEU B 2 13  ? -23.616 0.457   -3.128  1.00 59.25  ? 11  LEU B CG  1 
ATOM 3246 C CD1 . LEU B 2 13  ? -24.837 -0.449  -3.220  1.00 59.38  ? 11  LEU B CD1 1 
ATOM 3247 C CD2 . LEU B 2 13  ? -24.014 1.841   -2.637  1.00 58.06  ? 11  LEU B CD2 1 
ATOM 3248 N N   . VAL B 2 14  ? -20.138 2.246   -3.041  1.00 57.23  ? 12  VAL B N   1 
ATOM 3249 C CA  . VAL B 2 14  ? -19.593 3.558   -2.715  1.00 54.28  ? 12  VAL B CA  1 
ATOM 3250 C C   . VAL B 2 14  ? -20.422 4.612   -3.437  1.00 58.86  ? 12  VAL B C   1 
ATOM 3251 O O   . VAL B 2 14  ? -21.021 4.345   -4.484  1.00 58.80  ? 12  VAL B O   1 
ATOM 3252 C CB  . VAL B 2 14  ? -18.098 3.665   -3.102  1.00 51.78  ? 12  VAL B CB  1 
ATOM 3253 C CG1 . VAL B 2 14  ? -17.459 4.912   -2.500  1.00 56.07  ? 12  VAL B CG1 1 
ATOM 3254 C CG2 . VAL B 2 14  ? -17.344 2.416   -2.673  1.00 55.91  ? 12  VAL B CG2 1 
ATOM 3255 N N   . GLN B 2 15  ? -20.468 5.812   -2.864  1.00 66.18  ? 13  GLN B N   1 
ATOM 3256 C CA  . GLN B 2 15  ? -21.173 6.924   -3.480  1.00 59.90  ? 13  GLN B CA  1 
ATOM 3257 C C   . GLN B 2 15  ? -20.342 7.525   -4.613  1.00 57.20  ? 13  GLN B C   1 
ATOM 3258 O O   . GLN B 2 15  ? -19.180 7.170   -4.827  1.00 58.37  ? 13  GLN B O   1 
ATOM 3259 C CB  . GLN B 2 15  ? -21.500 7.992   -2.439  1.00 59.79  ? 13  GLN B CB  1 
ATOM 3260 C CG  . GLN B 2 15  ? -20.322 8.886   -2.093  1.00 62.06  ? 13  GLN B CG  1 
ATOM 3261 C CD  . GLN B 2 15  ? -20.445 9.499   -0.715  1.00 69.17  ? 13  GLN B CD  1 
ATOM 3262 O OE1 . GLN B 2 15  ? -20.470 10.721  -0.567  1.00 74.98  ? 13  GLN B OE1 1 
ATOM 3263 N NE2 . GLN B 2 15  ? -20.522 8.651   0.304   1.00 69.10  ? 13  GLN B NE2 1 
ATOM 3264 N N   . ALA B 2 16  ? -20.955 8.454   -5.343  1.00 58.66  ? 14  ALA B N   1 
ATOM 3265 C CA  . ALA B 2 16  ? -20.283 9.091   -6.469  1.00 61.43  ? 14  ALA B CA  1 
ATOM 3266 C C   . ALA B 2 16  ? -19.158 9.995   -5.979  1.00 58.55  ? 14  ALA B C   1 
ATOM 3267 O O   . ALA B 2 16  ? -19.337 10.779  -5.041  1.00 57.12  ? 14  ALA B O   1 
ATOM 3268 C CB  . ALA B 2 16  ? -21.283 9.893   -7.300  1.00 57.28  ? 14  ALA B CB  1 
ATOM 3269 N N   . GLY B 2 17  ? -17.994 9.888   -6.620  1.00 59.29  ? 15  GLY B N   1 
ATOM 3270 C CA  . GLY B 2 17  ? -16.828 10.652  -6.236  1.00 56.87  ? 15  GLY B CA  1 
ATOM 3271 C C   . GLY B 2 17  ? -15.969 10.019  -5.163  1.00 54.13  ? 15  GLY B C   1 
ATOM 3272 O O   . GLY B 2 17  ? -14.876 10.530  -4.887  1.00 51.41  ? 15  GLY B O   1 
ATOM 3273 N N   . GLY B 2 18  ? -16.420 8.925   -4.554  1.00 55.17  ? 16  GLY B N   1 
ATOM 3274 C CA  . GLY B 2 18  ? -15.668 8.257   -3.513  1.00 53.13  ? 16  GLY B CA  1 
ATOM 3275 C C   . GLY B 2 18  ? -14.496 7.466   -4.057  1.00 56.77  ? 16  GLY B C   1 
ATOM 3276 O O   . GLY B 2 18  ? -14.070 7.630   -5.204  1.00 54.62  ? 16  GLY B O   1 
ATOM 3277 N N   . SER B 2 19  ? -13.964 6.590   -3.206  1.00 64.50  ? 17  SER B N   1 
ATOM 3278 C CA  . SER B 2 19  ? -12.828 5.753   -3.561  1.00 57.28  ? 17  SER B CA  1 
ATOM 3279 C C   . SER B 2 19  ? -12.982 4.382   -2.919  1.00 51.29  ? 17  SER B C   1 
ATOM 3280 O O   . SER B 2 19  ? -13.548 4.246   -1.831  1.00 50.23  ? 17  SER B O   1 
ATOM 3281 C CB  . SER B 2 19  ? -11.496 6.391   -3.133  1.00 58.18  ? 17  SER B CB  1 
ATOM 3282 O OG  . SER B 2 19  ? -11.546 6.847   -1.792  1.00 63.38  ? 17  SER B OG  1 
ATOM 3283 N N   . LEU B 2 20  ? -12.474 3.364   -3.609  1.00 45.75  ? 18  LEU B N   1 
ATOM 3284 C CA  . LEU B 2 20  ? -12.517 1.999   -3.111  1.00 40.91  ? 18  LEU B CA  1 
ATOM 3285 C C   . LEU B 2 20  ? -11.352 1.233   -3.719  1.00 39.83  ? 18  LEU B C   1 
ATOM 3286 O O   . LEU B 2 20  ? -11.034 1.408   -4.899  1.00 48.56  ? 18  LEU B O   1 
ATOM 3287 C CB  . LEU B 2 20  ? -13.855 1.325   -3.443  1.00 39.07  ? 18  LEU B CB  1 
ATOM 3288 C CG  . LEU B 2 20  ? -13.972 -0.177  -3.177  1.00 46.30  ? 18  LEU B CG  1 
ATOM 3289 C CD1 . LEU B 2 20  ? -14.577 -0.408  -1.804  1.00 47.05  ? 18  LEU B CD1 1 
ATOM 3290 C CD2 . LEU B 2 20  ? -14.808 -0.866  -4.243  1.00 47.95  ? 18  LEU B CD2 1 
ATOM 3291 N N   . GLY B 2 21  ? -10.707 0.405   -2.907  1.00 37.89  ? 19  GLY B N   1 
ATOM 3292 C CA  . GLY B 2 21  ? -9.540  -0.358  -3.325  1.00 41.69  ? 19  GLY B CA  1 
ATOM 3293 C C   . GLY B 2 21  ? -9.881  -1.831  -3.477  1.00 40.99  ? 19  GLY B C   1 
ATOM 3294 O O   . GLY B 2 21  ? -10.568 -2.408  -2.631  1.00 41.11  ? 19  GLY B O   1 
ATOM 3295 N N   . LEU B 2 22  ? -9.399  -2.428  -4.561  1.00 44.79  ? 20  LEU B N   1 
ATOM 3296 C CA  . LEU B 2 22  ? -9.579  -3.848  -4.817  1.00 44.31  ? 20  LEU B CA  1 
ATOM 3297 C C   . LEU B 2 22  ? -8.253  -4.580  -4.666  1.00 45.87  ? 20  LEU B C   1 
ATOM 3298 O O   . LEU B 2 22  ? -7.179  -4.005  -4.864  1.00 46.78  ? 20  LEU B O   1 
ATOM 3299 C CB  . LEU B 2 22  ? -10.152 -4.099  -6.216  1.00 46.40  ? 20  LEU B CB  1 
ATOM 3300 C CG  . LEU B 2 22  ? -11.392 -3.304  -6.632  1.00 51.09  ? 20  LEU B CG  1 
ATOM 3301 C CD1 . LEU B 2 22  ? -11.529 -3.278  -8.146  1.00 46.90  ? 20  LEU B CD1 1 
ATOM 3302 C CD2 . LEU B 2 22  ? -12.639 -3.890  -5.991  1.00 45.36  ? 20  LEU B CD2 1 
ATOM 3303 N N   . SER B 2 23  ? -8.340  -5.856  -4.303  1.00 49.41  ? 21  SER B N   1 
ATOM 3304 C CA  . SER B 2 23  ? -7.170  -6.712  -4.197  1.00 51.13  ? 21  SER B CA  1 
ATOM 3305 C C   . SER B 2 23  ? -7.485  -8.050  -4.846  1.00 51.22  ? 21  SER B C   1 
ATOM 3306 O O   . SER B 2 23  ? -8.646  -8.441  -4.980  1.00 51.64  ? 21  SER B O   1 
ATOM 3307 C CB  . SER B 2 23  ? -6.741  -6.916  -2.740  1.00 44.69  ? 21  SER B CB  1 
ATOM 3308 O OG  . SER B 2 23  ? -7.821  -7.404  -1.966  1.00 47.99  ? 21  SER B OG  1 
ATOM 3309 N N   . CYS B 2 24  ? -6.430  -8.750  -5.251  1.00 51.92  ? 22  CYS B N   1 
ATOM 3310 C CA  . CYS B 2 24  ? -6.589  -10.043 -5.908  1.00 51.94  ? 22  CYS B CA  1 
ATOM 3311 C C   . CYS B 2 24  ? -5.351  -10.872 -5.604  1.00 51.65  ? 22  CYS B C   1 
ATOM 3312 O O   . CYS B 2 24  ? -4.248  -10.515 -6.026  1.00 55.51  ? 22  CYS B O   1 
ATOM 3313 C CB  . CYS B 2 24  ? -6.789  -9.869  -7.410  1.00 55.10  ? 22  CYS B CB  1 
ATOM 3314 S SG  . CYS B 2 24  ? -6.452  -11.340 -8.390  1.00 71.36  ? 22  CYS B SG  1 
ATOM 3315 N N   . ALA B 2 25  ? -5.532  -11.966 -4.870  1.00 49.97  ? 23  ALA B N   1 
ATOM 3316 C CA  . ALA B 2 25  ? -4.424  -12.832 -4.492  1.00 49.09  ? 23  ALA B CA  1 
ATOM 3317 C C   . ALA B 2 25  ? -4.297  -13.972 -5.492  1.00 55.93  ? 23  ALA B C   1 
ATOM 3318 O O   . ALA B 2 25  ? -5.280  -14.657 -5.793  1.00 56.42  ? 23  ALA B O   1 
ATOM 3319 C CB  . ALA B 2 25  ? -4.624  -13.381 -3.079  1.00 52.26  ? 23  ALA B CB  1 
ATOM 3320 N N   . ALA B 2 26  ? -3.086  -14.168 -6.006  1.00 56.88  ? 24  ALA B N   1 
ATOM 3321 C CA  . ALA B 2 26  ? -2.799  -15.211 -6.980  1.00 59.15  ? 24  ALA B CA  1 
ATOM 3322 C C   . ALA B 2 26  ? -2.088  -16.368 -6.291  1.00 62.34  ? 24  ALA B C   1 
ATOM 3323 O O   . ALA B 2 26  ? -1.122  -16.156 -5.550  1.00 65.30  ? 24  ALA B O   1 
ATOM 3324 C CB  . ALA B 2 26  ? -1.943  -14.668 -8.125  1.00 58.07  ? 24  ALA B CB  1 
ATOM 3325 N N   . SER B 2 27  ? -2.563  -17.585 -6.538  1.00 65.85  ? 25  SER B N   1 
ATOM 3326 C CA  . SER B 2 27  ? -2.011  -18.771 -5.899  1.00 72.27  ? 25  SER B CA  1 
ATOM 3327 C C   . SER B 2 27  ? -0.885  -19.347 -6.749  1.00 80.92  ? 25  SER B C   1 
ATOM 3328 O O   . SER B 2 27  ? -1.047  -19.539 -7.958  1.00 75.66  ? 25  SER B O   1 
ATOM 3329 C CB  . SER B 2 27  ? -3.101  -19.821 -5.677  1.00 72.13  ? 25  SER B CB  1 
ATOM 3330 O OG  . SER B 2 27  ? -2.660  -20.829 -4.785  1.00 78.24  ? 25  SER B OG  1 
ATOM 3331 N N   . GLY B 2 28  ? 0.249   -19.612 -6.117  1.00 101.97 ? 26  GLY B N   1 
ATOM 3332 C CA  . GLY B 2 28  ? 1.384   -20.225 -6.775  1.00 109.09 ? 26  GLY B CA  1 
ATOM 3333 C C   . GLY B 2 28  ? 2.608   -19.326 -6.766  1.00 113.45 ? 26  GLY B C   1 
ATOM 3334 O O   . GLY B 2 28  ? 2.566   -18.159 -6.383  1.00 110.52 ? 26  GLY B O   1 
ATOM 3335 N N   . ARG B 2 29  ? 3.718   -19.917 -7.199  1.00 105.11 ? 27  ARG B N   1 
ATOM 3336 C CA  . ARG B 2 29  ? 4.986   -19.217 -7.308  1.00 102.08 ? 27  ARG B CA  1 
ATOM 3337 C C   . ARG B 2 29  ? 5.090   -18.605 -8.709  1.00 98.72  ? 27  ARG B C   1 
ATOM 3338 O O   . ARG B 2 29  ? 4.178   -18.728 -9.531  1.00 96.43  ? 27  ARG B O   1 
ATOM 3339 C CB  . ARG B 2 29  ? 6.128   -20.182 -6.970  1.00 99.68  ? 27  ARG B CB  1 
ATOM 3340 C CG  . ARG B 2 29  ? 7.546   -19.613 -6.973  1.00 94.46  ? 27  ARG B CG  1 
ATOM 3341 C CD  . ARG B 2 29  ? 7.737   -18.568 -5.880  1.00 98.79  ? 27  ARG B CD  1 
ATOM 3342 N NE  . ARG B 2 29  ? 7.667   -17.206 -6.403  1.00 103.21 ? 27  ARG B NE  1 
ATOM 3343 C CZ  . ARG B 2 29  ? 6.716   -16.323 -6.117  1.00 95.86  ? 27  ARG B CZ  1 
ATOM 3344 N NH1 . ARG B 2 29  ? 5.731   -16.608 -5.280  1.00 92.02  ? 27  ARG B NH1 1 
ATOM 3345 N NH2 . ARG B 2 29  ? 6.752   -15.123 -6.692  1.00 85.09  ? 27  ARG B NH2 1 
ATOM 3346 N N   . THR B 2 30  ? 6.206   -17.922 -8.982  1.00 97.61  ? 28  THR B N   1 
ATOM 3347 C CA  . THR B 2 30  ? 6.439   -17.203 -10.238 1.00 96.02  ? 28  THR B CA  1 
ATOM 3348 C C   . THR B 2 30  ? 5.412   -16.094 -10.450 1.00 94.41  ? 28  THR B C   1 
ATOM 3349 O O   . THR B 2 30  ? 5.080   -15.747 -11.587 1.00 98.41  ? 28  THR B O   1 
ATOM 3350 C CB  . THR B 2 30  ? 6.464   -18.148 -11.444 1.00 99.14  ? 28  THR B CB  1 
ATOM 3351 O OG1 . THR B 2 30  ? 5.138   -18.615 -11.722 1.00 107.04 ? 28  THR B OG1 1 
ATOM 3352 C CG2 . THR B 2 30  ? 7.375   -19.338 -11.171 1.00 100.37 ? 28  THR B CG2 1 
ATOM 3353 N N   . PHE B 2 31  ? 4.902   -15.533 -9.350  1.00 81.00  ? 29  PHE B N   1 
ATOM 3354 C CA  . PHE B 2 31  ? 4.021   -14.375 -9.447  1.00 74.29  ? 29  PHE B CA  1 
ATOM 3355 C C   . PHE B 2 31  ? 4.760   -13.162 -9.996  1.00 70.22  ? 29  PHE B C   1 
ATOM 3356 O O   . PHE B 2 31  ? 4.169   -12.348 -10.715 1.00 66.21  ? 29  PHE B O   1 
ATOM 3357 C CB  . PHE B 2 31  ? 3.417   -14.066 -8.076  1.00 69.01  ? 29  PHE B CB  1 
ATOM 3358 C CG  . PHE B 2 31  ? 2.572   -12.823 -8.045  1.00 63.15  ? 29  PHE B CG  1 
ATOM 3359 C CD1 . PHE B 2 31  ? 1.231   -12.876 -8.383  1.00 63.98  ? 29  PHE B CD1 1 
ATOM 3360 C CD2 . PHE B 2 31  ? 3.112   -11.606 -7.655  1.00 60.44  ? 29  PHE B CD2 1 
ATOM 3361 C CE1 . PHE B 2 31  ? 0.448   -11.736 -8.351  1.00 60.59  ? 29  PHE B CE1 1 
ATOM 3362 C CE2 . PHE B 2 31  ? 2.334   -10.464 -7.622  1.00 55.68  ? 29  PHE B CE2 1 
ATOM 3363 C CZ  . PHE B 2 31  ? 1.000   -10.530 -7.968  1.00 54.00  ? 29  PHE B CZ  1 
ATOM 3364 N N   . SER B 2 32  ? 6.050   -13.034 -9.679  1.00 71.79  ? 30  SER B N   1 
ATOM 3365 C CA  . SER B 2 32  ? 6.846   -11.927 -10.193 1.00 70.97  ? 30  SER B CA  1 
ATOM 3366 C C   . SER B 2 32  ? 7.091   -12.039 -11.690 1.00 67.42  ? 30  SER B C   1 
ATOM 3367 O O   . SER B 2 32  ? 7.442   -11.039 -12.325 1.00 65.94  ? 30  SER B O   1 
ATOM 3368 C CB  . SER B 2 32  ? 8.186   -11.857 -9.460  1.00 70.21  ? 30  SER B CB  1 
ATOM 3369 O OG  . SER B 2 32  ? 8.797   -13.136 -9.400  1.00 72.08  ? 30  SER B OG  1 
ATOM 3370 N N   . ASN B 2 33  ? 6.924   -13.229 -12.261 1.00 68.81  ? 31  ASN B N   1 
ATOM 3371 C CA  . ASN B 2 33  ? 7.115   -13.456 -13.685 1.00 72.70  ? 31  ASN B CA  1 
ATOM 3372 C C   . ASN B 2 33  ? 5.816   -13.367 -14.475 1.00 71.68  ? 31  ASN B C   1 
ATOM 3373 O O   . ASN B 2 33  ? 5.837   -13.531 -15.699 1.00 68.36  ? 31  ASN B O   1 
ATOM 3374 C CB  . ASN B 2 33  ? 7.768   -14.825 -13.915 1.00 76.76  ? 31  ASN B CB  1 
ATOM 3375 C CG  . ASN B 2 33  ? 9.018   -15.026 -13.074 1.00 74.32  ? 31  ASN B CG  1 
ATOM 3376 O OD1 . ASN B 2 33  ? 9.441   -14.130 -12.343 1.00 75.75  ? 31  ASN B OD1 1 
ATOM 3377 N ND2 . ASN B 2 33  ? 9.617   -16.208 -13.177 1.00 72.66  ? 31  ASN B ND2 1 
ATOM 3378 N N   . TYR B 2 34  ? 4.695   -13.109 -13.809 1.00 68.25  ? 32  TYR B N   1 
ATOM 3379 C CA  . TYR B 2 34  ? 3.386   -13.098 -14.442 1.00 66.69  ? 32  TYR B CA  1 
ATOM 3380 C C   . TYR B 2 34  ? 2.924   -11.668 -14.701 1.00 64.65  ? 32  TYR B C   1 
ATOM 3381 O O   . TYR B 2 34  ? 3.293   -10.733 -13.985 1.00 64.90  ? 32  TYR B O   1 
ATOM 3382 C CB  . TYR B 2 34  ? 2.357   -13.826 -13.572 1.00 63.59  ? 32  TYR B CB  1 
ATOM 3383 C CG  . TYR B 2 34  ? 2.351   -15.335 -13.719 1.00 71.25  ? 32  TYR B CG  1 
ATOM 3384 C CD1 . TYR B 2 34  ? 3.369   -15.997 -14.394 1.00 76.55  ? 32  TYR B CD1 1 
ATOM 3385 C CD2 . TYR B 2 34  ? 1.320   -16.098 -13.184 1.00 72.71  ? 32  TYR B CD2 1 
ATOM 3386 C CE1 . TYR B 2 34  ? 3.363   -17.377 -14.529 1.00 78.70  ? 32  TYR B CE1 1 
ATOM 3387 C CE2 . TYR B 2 34  ? 1.305   -17.475 -13.315 1.00 74.97  ? 32  TYR B CE2 1 
ATOM 3388 C CZ  . TYR B 2 34  ? 2.327   -18.110 -13.987 1.00 78.10  ? 32  TYR B CZ  1 
ATOM 3389 O OH  . TYR B 2 34  ? 2.314   -19.481 -14.119 1.00 76.15  ? 32  TYR B OH  1 
ATOM 3390 N N   . VAL B 2 35  ? 2.108   -11.510 -15.739 1.00 64.83  ? 33  VAL B N   1 
ATOM 3391 C CA  . VAL B 2 35  ? 1.504   -10.229 -16.085 1.00 63.27  ? 33  VAL B CA  1 
ATOM 3392 C C   . VAL B 2 35  ? 0.090   -10.208 -15.522 1.00 61.91  ? 33  VAL B C   1 
ATOM 3393 O O   . VAL B 2 35  ? -0.703  -11.124 -15.777 1.00 60.00  ? 33  VAL B O   1 
ATOM 3394 C CB  . VAL B 2 35  ? 1.507   -10.003 -17.608 1.00 61.77  ? 33  VAL B CB  1 
ATOM 3395 C CG1 . VAL B 2 35  ? 0.583   -8.853  -17.990 1.00 54.23  ? 33  VAL B CG1 1 
ATOM 3396 C CG2 . VAL B 2 35  ? 2.923   -9.741  -18.103 1.00 60.54  ? 33  VAL B CG2 1 
ATOM 3397 N N   . MET B 2 36  ? -0.220  -9.177  -14.742 1.00 65.15  ? 34  MET B N   1 
ATOM 3398 C CA  . MET B 2 36  ? -1.512  -9.039  -14.088 1.00 59.67  ? 34  MET B CA  1 
ATOM 3399 C C   . MET B 2 36  ? -2.320  -7.927  -14.741 1.00 57.81  ? 34  MET B C   1 
ATOM 3400 O O   . MET B 2 36  ? -1.764  -6.953  -15.256 1.00 60.01  ? 34  MET B O   1 
ATOM 3401 C CB  . MET B 2 36  ? -1.347  -8.740  -12.595 1.00 61.98  ? 34  MET B CB  1 
ATOM 3402 C CG  . MET B 2 36  ? -0.504  -9.750  -11.843 1.00 57.54  ? 34  MET B CG  1 
ATOM 3403 S SD  . MET B 2 36  ? -1.476  -11.177 -11.329 1.00 65.55  ? 34  MET B SD  1 
ATOM 3404 C CE  . MET B 2 36  ? -0.453  -12.513 -11.929 1.00 57.64  ? 34  MET B CE  1 
ATOM 3405 N N   . ALA B 2 37  ? -3.642  -8.076  -14.702 1.00 53.82  ? 35  ALA B N   1 
ATOM 3406 C CA  . ALA B 2 37  ? -4.532  -7.098  -15.306 1.00 56.16  ? 35  ALA B CA  1 
ATOM 3407 C C   . ALA B 2 37  ? -5.874  -7.130  -14.592 1.00 53.11  ? 35  ALA B C   1 
ATOM 3408 O O   . ALA B 2 37  ? -6.204  -8.084  -13.883 1.00 52.56  ? 35  ALA B O   1 
ATOM 3409 C CB  . ALA B 2 37  ? -4.719  -7.353  -16.807 1.00 51.24  ? 35  ALA B CB  1 
ATOM 3410 N N   . TRP B 2 38  ? -6.647  -6.067  -14.791 1.00 53.16  ? 36  TRP B N   1 
ATOM 3411 C CA  . TRP B 2 38  ? -7.992  -5.949  -14.249 1.00 51.97  ? 36  TRP B CA  1 
ATOM 3412 C C   . TRP B 2 38  ? -8.985  -5.783  -15.389 1.00 51.75  ? 36  TRP B C   1 
ATOM 3413 O O   . TRP B 2 38  ? -8.689  -5.133  -16.396 1.00 48.62  ? 36  TRP B O   1 
ATOM 3414 C CB  . TRP B 2 38  ? -8.108  -4.759  -13.291 1.00 50.69  ? 36  TRP B CB  1 
ATOM 3415 C CG  . TRP B 2 38  ? -7.709  -5.058  -11.878 1.00 52.61  ? 36  TRP B CG  1 
ATOM 3416 C CD1 . TRP B 2 38  ? -6.547  -4.697  -11.266 1.00 51.08  ? 36  TRP B CD1 1 
ATOM 3417 C CD2 . TRP B 2 38  ? -8.485  -5.750  -10.889 1.00 52.50  ? 36  TRP B CD2 1 
ATOM 3418 N NE1 . TRP B 2 38  ? -6.544  -5.128  -9.961  1.00 56.94  ? 36  TRP B NE1 1 
ATOM 3419 C CE2 . TRP B 2 38  ? -7.721  -5.781  -9.706  1.00 53.08  ? 36  TRP B CE2 1 
ATOM 3420 C CE3 . TRP B 2 38  ? -9.747  -6.351  -10.892 1.00 50.70  ? 36  TRP B CE3 1 
ATOM 3421 C CZ2 . TRP B 2 38  ? -8.178  -6.389  -8.537  1.00 50.38  ? 36  TRP B CZ2 1 
ATOM 3422 C CZ3 . TRP B 2 38  ? -10.198 -6.955  -9.731  1.00 50.96  ? 36  TRP B CZ3 1 
ATOM 3423 C CH2 . TRP B 2 38  ? -9.416  -6.968  -8.570  1.00 50.38  ? 36  TRP B CH2 1 
ATOM 3424 N N   . PHE B 2 39  ? -10.166 -6.369  -15.216 1.00 59.58  ? 37  PHE B N   1 
ATOM 3425 C CA  . PHE B 2 39  ? -11.245 -6.272  -16.184 1.00 60.45  ? 37  PHE B CA  1 
ATOM 3426 C C   . PHE B 2 39  ? -12.548 -6.055  -15.430 1.00 59.38  ? 37  PHE B C   1 
ATOM 3427 O O   . PHE B 2 39  ? -12.674 -6.410  -14.255 1.00 60.20  ? 37  PHE B O   1 
ATOM 3428 C CB  . PHE B 2 39  ? -11.334 -7.533  -17.057 1.00 59.27  ? 37  PHE B CB  1 
ATOM 3429 C CG  . PHE B 2 39  ? -10.316 -7.587  -18.167 1.00 62.59  ? 37  PHE B CG  1 
ATOM 3430 C CD1 . PHE B 2 39  ? -9.077  -8.171  -17.957 1.00 64.89  ? 37  PHE B CD1 1 
ATOM 3431 C CD2 . PHE B 2 39  ? -10.614 -7.095  -19.430 1.00 63.16  ? 37  PHE B CD2 1 
ATOM 3432 C CE1 . PHE B 2 39  ? -8.144  -8.239  -18.976 1.00 67.28  ? 37  PHE B CE1 1 
ATOM 3433 C CE2 . PHE B 2 39  ? -9.684  -7.161  -20.455 1.00 56.12  ? 37  PHE B CE2 1 
ATOM 3434 C CZ  . PHE B 2 39  ? -8.448  -7.734  -20.227 1.00 56.71  ? 37  PHE B CZ  1 
ATOM 3435 N N   . ARG B 2 40  ? -13.520 -5.459  -16.113 1.00 53.26  ? 38  ARG B N   1 
ATOM 3436 C CA  . ARG B 2 40  ? -14.835 -5.242  -15.530 1.00 54.37  ? 38  ARG B CA  1 
ATOM 3437 C C   . ARG B 2 40  ? -15.897 -5.623  -16.548 1.00 60.47  ? 38  ARG B C   1 
ATOM 3438 O O   . ARG B 2 40  ? -15.628 -5.726  -17.747 1.00 68.08  ? 38  ARG B O   1 
ATOM 3439 C CB  . ARG B 2 40  ? -15.022 -3.791  -15.069 1.00 50.99  ? 38  ARG B CB  1 
ATOM 3440 C CG  . ARG B 2 40  ? -15.085 -2.784  -16.196 1.00 57.70  ? 38  ARG B CG  1 
ATOM 3441 C CD  . ARG B 2 40  ? -15.714 -1.480  -15.733 1.00 56.12  ? 38  ARG B CD  1 
ATOM 3442 N NE  . ARG B 2 40  ? -15.644 -0.453  -16.765 1.00 64.53  ? 38  ARG B NE  1 
ATOM 3443 C CZ  . ARG B 2 40  ? -15.190 0.777   -16.570 1.00 63.14  ? 38  ARG B CZ  1 
ATOM 3444 N NH1 . ARG B 2 40  ? -14.770 1.178   -15.381 1.00 55.20  ? 38  ARG B NH1 1 
ATOM 3445 N NH2 . ARG B 2 40  ? -15.156 1.626   -17.593 1.00 64.15  ? 38  ARG B NH2 1 
ATOM 3446 N N   . GLN B 2 41  ? -17.115 -5.837  -16.055 1.00 60.31  ? 39  GLN B N   1 
ATOM 3447 C CA  . GLN B 2 41  ? -18.215 -6.265  -16.914 1.00 61.70  ? 39  GLN B CA  1 
ATOM 3448 C C   . GLN B 2 41  ? -19.510 -5.672  -16.377 1.00 66.08  ? 39  GLN B C   1 
ATOM 3449 O O   . GLN B 2 41  ? -19.983 -6.075  -15.309 1.00 64.39  ? 39  GLN B O   1 
ATOM 3450 C CB  . GLN B 2 41  ? -18.293 -7.787  -16.980 1.00 60.97  ? 39  GLN B CB  1 
ATOM 3451 C CG  . GLN B 2 41  ? -19.082 -8.318  -18.159 1.00 65.43  ? 39  GLN B CG  1 
ATOM 3452 C CD  . GLN B 2 41  ? -18.830 -9.790  -18.405 1.00 69.80  ? 39  GLN B CD  1 
ATOM 3453 O OE1 . GLN B 2 41  ? -18.403 -10.187 -19.490 1.00 77.34  ? 39  GLN B OE1 1 
ATOM 3454 N NE2 . GLN B 2 41  ? -19.087 -10.610 -17.394 1.00 70.82  ? 39  GLN B NE2 1 
ATOM 3455 N N   . ALA B 2 42  ? -20.073 -4.717  -17.114 1.00 67.65  ? 40  ALA B N   1 
ATOM 3456 C CA  . ALA B 2 42  ? -21.343 -4.120  -16.747 1.00 68.36  ? 40  ALA B CA  1 
ATOM 3457 C C   . ALA B 2 42  ? -22.468 -5.143  -16.901 1.00 77.76  ? 40  ALA B C   1 
ATOM 3458 O O   . ALA B 2 42  ? -22.333 -6.117  -17.645 1.00 78.18  ? 40  ALA B O   1 
ATOM 3459 C CB  . ALA B 2 42  ? -21.612 -2.890  -17.613 1.00 76.48  ? 40  ALA B CB  1 
ATOM 3460 N N   . PRO B 2 43  ? -23.596 -4.952  -16.195 1.00 80.74  ? 41  PRO B N   1 
ATOM 3461 C CA  . PRO B 2 43  ? -24.714 -5.896  -16.348 1.00 80.60  ? 41  PRO B CA  1 
ATOM 3462 C C   . PRO B 2 43  ? -25.288 -5.888  -17.757 1.00 82.28  ? 41  PRO B C   1 
ATOM 3463 O O   . PRO B 2 43  ? -25.885 -4.899  -18.194 1.00 85.67  ? 41  PRO B O   1 
ATOM 3464 C CB  . PRO B 2 43  ? -25.746 -5.419  -15.318 1.00 79.94  ? 41  PRO B CB  1 
ATOM 3465 C CG  . PRO B 2 43  ? -25.118 -4.309  -14.556 1.00 82.53  ? 41  PRO B CG  1 
ATOM 3466 C CD  . PRO B 2 43  ? -23.895 -3.854  -15.264 1.00 81.28  ? 41  PRO B CD  1 
ATOM 3467 N N   . GLY B 2 44  ? -25.111 -6.995  -18.474 1.00 85.13  ? 42  GLY B N   1 
ATOM 3468 C CA  . GLY B 2 44  ? -25.557 -7.086  -19.848 1.00 87.79  ? 42  GLY B CA  1 
ATOM 3469 C C   . GLY B 2 44  ? -24.569 -6.581  -20.871 1.00 87.36  ? 42  GLY B C   1 
ATOM 3470 O O   . GLY B 2 44  ? -24.974 -6.247  -21.991 1.00 87.00  ? 42  GLY B O   1 
ATOM 3471 N N   . LYS B 2 45  ? -23.285 -6.512  -20.526 1.00 87.90  ? 43  LYS B N   1 
ATOM 3472 C CA  . LYS B 2 45  ? -22.272 -6.004  -21.441 1.00 86.40  ? 43  LYS B CA  1 
ATOM 3473 C C   . LYS B 2 45  ? -21.196 -7.053  -21.692 1.00 82.97  ? 43  LYS B C   1 
ATOM 3474 O O   . LYS B 2 45  ? -21.441 -8.254  -21.534 1.00 88.93  ? 43  LYS B O   1 
ATOM 3475 C CB  . LYS B 2 45  ? -21.650 -4.719  -20.888 1.00 83.83  ? 43  LYS B CB  1 
ATOM 3476 C CG  . LYS B 2 45  ? -22.140 -3.446  -21.566 1.00 86.55  ? 43  LYS B CG  1 
ATOM 3477 C CD  . LYS B 2 45  ? -23.624 -3.216  -21.320 1.00 84.80  ? 43  LYS B CD  1 
ATOM 3478 C CE  . LYS B 2 45  ? -24.044 -1.812  -21.731 1.00 79.78  ? 43  LYS B CE  1 
ATOM 3479 N NZ  . LYS B 2 45  ? -25.506 -1.595  -21.544 1.00 81.23  ? 43  LYS B NZ  1 
ATOM 3480 N N   . GLU B 2 46  ? -20.005 -6.609  -22.080 1.00 80.05  ? 44  GLU B N   1 
ATOM 3481 C CA  . GLU B 2 46  ? -18.891 -7.490  -22.383 1.00 76.95  ? 44  GLU B CA  1 
ATOM 3482 C C   . GLU B 2 46  ? -17.696 -7.118  -21.513 1.00 71.50  ? 44  GLU B C   1 
ATOM 3483 O O   . GLU B 2 46  ? -17.597 -5.997  -21.005 1.00 71.74  ? 44  GLU B O   1 
ATOM 3484 C CB  . GLU B 2 46  ? -18.515 -7.412  -23.873 1.00 82.89  ? 44  GLU B CB  1 
ATOM 3485 C CG  . GLU B 2 46  ? -17.590 -8.525  -24.360 1.00 84.74  ? 44  GLU B CG  1 
ATOM 3486 C CD  . GLU B 2 46  ? -17.473 -8.581  -25.874 1.00 84.15  ? 44  GLU B CD  1 
ATOM 3487 O OE1 . GLU B 2 46  ? -17.896 -7.617  -26.546 1.00 86.96  ? 44  GLU B OE1 1 
ATOM 3488 O OE2 . GLU B 2 46  ? -16.947 -9.590  -26.392 1.00 82.97  ? 44  GLU B OE2 1 
ATOM 3489 N N   . ARG B 2 47  ? -16.797 -8.084  -21.333 1.00 79.67  ? 45  ARG B N   1 
ATOM 3490 C CA  . ARG B 2 47  ? -15.563 -7.851  -20.593 1.00 81.68  ? 45  ARG B CA  1 
ATOM 3491 C C   . ARG B 2 47  ? -14.761 -6.732  -21.243 1.00 84.74  ? 45  ARG B C   1 
ATOM 3492 O O   . ARG B 2 47  ? -14.401 -6.819  -22.422 1.00 86.73  ? 45  ARG B O   1 
ATOM 3493 C CB  . ARG B 2 47  ? -14.736 -9.134  -20.543 1.00 82.08  ? 45  ARG B CB  1 
ATOM 3494 C CG  . ARG B 2 47  ? -15.010 -10.021 -19.345 1.00 78.33  ? 45  ARG B CG  1 
ATOM 3495 C CD  . ARG B 2 47  ? -14.100 -11.238 -19.361 1.00 76.56  ? 45  ARG B CD  1 
ATOM 3496 N NE  . ARG B 2 47  ? -14.465 -12.208 -18.336 1.00 80.58  ? 45  ARG B NE  1 
ATOM 3497 C CZ  . ARG B 2 47  ? -13.932 -13.417 -18.225 1.00 85.57  ? 45  ARG B CZ  1 
ATOM 3498 N NH1 . ARG B 2 47  ? -13.001 -13.842 -19.064 1.00 85.60  ? 45  ARG B NH1 1 
ATOM 3499 N NH2 . ARG B 2 47  ? -14.342 -14.220 -17.248 1.00 82.64  ? 45  ARG B NH2 1 
ATOM 3500 N N   . GLU B 2 48  ? -14.480 -5.681  -20.476 1.00 66.06  ? 46  GLU B N   1 
ATOM 3501 C CA  . GLU B 2 48  ? -13.741 -4.529  -20.969 1.00 62.15  ? 46  GLU B CA  1 
ATOM 3502 C C   . GLU B 2 48  ? -12.483 -4.317  -20.139 1.00 58.06  ? 46  GLU B C   1 
ATOM 3503 O O   . GLU B 2 48  ? -12.458 -4.587  -18.935 1.00 57.49  ? 46  GLU B O   1 
ATOM 3504 C CB  . GLU B 2 48  ? -14.599 -3.258  -20.945 1.00 63.36  ? 46  GLU B CB  1 
ATOM 3505 C CG  . GLU B 2 48  ? -15.638 -3.226  -19.840 1.00 68.94  ? 46  GLU B CG  1 
ATOM 3506 C CD  . GLU B 2 48  ? -16.281 -1.862  -19.686 1.00 74.99  ? 46  GLU B CD  1 
ATOM 3507 O OE1 . GLU B 2 48  ? -15.599 -0.848  -19.948 1.00 77.74  ? 46  GLU B OE1 1 
ATOM 3508 O OE2 . GLU B 2 48  ? -17.469 -1.802  -19.305 1.00 76.03  ? 46  GLU B OE2 1 
ATOM 3509 N N   . PHE B 2 49  ? -11.441 -3.822  -20.801 1.00 57.11  ? 47  PHE B N   1 
ATOM 3510 C CA  . PHE B 2 49  ? -10.152 -3.627  -20.156 1.00 48.62  ? 47  PHE B CA  1 
ATOM 3511 C C   . PHE B 2 49  ? -10.222 -2.502  -19.131 1.00 51.03  ? 47  PHE B C   1 
ATOM 3512 O O   . PHE B 2 49  ? -10.951 -1.520  -19.295 1.00 54.97  ? 47  PHE B O   1 
ATOM 3513 C CB  . PHE B 2 49  ? -9.084  -3.323  -21.206 1.00 50.32  ? 47  PHE B CB  1 
ATOM 3514 C CG  . PHE B 2 49  ? -7.704  -3.161  -20.644 1.00 49.19  ? 47  PHE B CG  1 
ATOM 3515 C CD1 . PHE B 2 49  ? -7.038  -4.238  -20.085 1.00 48.53  ? 47  PHE B CD1 1 
ATOM 3516 C CD2 . PHE B 2 49  ? -7.064  -1.933  -20.692 1.00 48.50  ? 47  PHE B CD2 1 
ATOM 3517 C CE1 . PHE B 2 49  ? -5.763  -4.090  -19.573 1.00 46.54  ? 47  PHE B CE1 1 
ATOM 3518 C CE2 . PHE B 2 49  ? -5.789  -1.780  -20.183 1.00 48.68  ? 47  PHE B CE2 1 
ATOM 3519 C CZ  . PHE B 2 49  ? -5.138  -2.859  -19.622 1.00 46.52  ? 47  PHE B CZ  1 
ATOM 3520 N N   . VAL B 2 50  ? -9.453  -2.658  -18.055 1.00 50.71  ? 48  VAL B N   1 
ATOM 3521 C CA  . VAL B 2 50  ? -9.385  -1.649  -17.005 1.00 48.78  ? 48  VAL B CA  1 
ATOM 3522 C C   . VAL B 2 50  ? -7.937  -1.217  -16.817 1.00 45.03  ? 48  VAL B C   1 
ATOM 3523 O O   . VAL B 2 50  ? -7.573  -0.079  -17.133 1.00 45.64  ? 48  VAL B O   1 
ATOM 3524 C CB  . VAL B 2 50  ? -9.983  -2.167  -15.684 1.00 48.48  ? 48  VAL B CB  1 
ATOM 3525 C CG1 . VAL B 2 50  ? -9.873  -1.104  -14.607 1.00 43.35  ? 48  VAL B CG1 1 
ATOM 3526 C CG2 . VAL B 2 50  ? -11.433 -2.578  -15.879 1.00 48.65  ? 48  VAL B CG2 1 
ATOM 3527 N N   . ALA B 2 51  ? -7.103  -2.120  -16.305 1.00 43.53  ? 49  ALA B N   1 
ATOM 3528 C CA  . ALA B 2 51  ? -5.703  -1.813  -16.050 1.00 46.03  ? 49  ALA B CA  1 
ATOM 3529 C C   . ALA B 2 51  ? -4.874  -3.079  -16.224 1.00 48.52  ? 49  ALA B C   1 
ATOM 3530 O O   . ALA B 2 51  ? -5.406  -4.190  -16.296 1.00 48.84  ? 49  ALA B O   1 
ATOM 3531 C CB  . ALA B 2 51  ? -5.511  -1.217  -14.651 1.00 40.64  ? 49  ALA B CB  1 
ATOM 3532 N N   . ARG B 2 52  ? -3.555  -2.897  -16.288 1.00 50.79  ? 50  ARG B N   1 
ATOM 3533 C CA  . ARG B 2 52  ? -2.629  -4.008  -16.457 1.00 49.07  ? 50  ARG B CA  1 
ATOM 3534 C C   . ARG B 2 52  ? -1.238  -3.579  -16.010 1.00 53.14  ? 50  ARG B C   1 
ATOM 3535 O O   . ARG B 2 52  ? -0.776  -2.489  -16.361 1.00 52.75  ? 50  ARG B O   1 
ATOM 3536 C CB  . ARG B 2 52  ? -2.584  -4.486  -17.915 1.00 49.08  ? 50  ARG B CB  1 
ATOM 3537 C CG  . ARG B 2 52  ? -1.498  -5.514  -18.208 1.00 49.30  ? 50  ARG B CG  1 
ATOM 3538 C CD  . ARG B 2 52  ? -0.502  -5.001  -19.239 1.00 54.18  ? 50  ARG B CD  1 
ATOM 3539 N NE  . ARG B 2 52  ? -1.165  -4.342  -20.357 1.00 55.52  ? 50  ARG B NE  1 
ATOM 3540 C CZ  . ARG B 2 52  ? -0.535  -3.817  -21.399 1.00 45.74  ? 50  ARG B CZ  1 
ATOM 3541 N NH1 . ARG B 2 52  ? 0.783   -3.871  -21.509 1.00 46.16  ? 50  ARG B NH1 1 
ATOM 3542 N NH2 . ARG B 2 52  ? -1.244  -3.216  -22.349 1.00 45.60  ? 50  ARG B NH2 1 
ATOM 3543 N N   . ILE B 2 53  ? -0.578  -4.447  -15.246 1.00 53.20  ? 51  ILE B N   1 
ATOM 3544 C CA  . ILE B 2 53  ? 0.798   -4.234  -14.815 1.00 53.66  ? 51  ILE B CA  1 
ATOM 3545 C C   . ILE B 2 53  ? 1.675   -5.314  -15.434 1.00 56.47  ? 51  ILE B C   1 
ATOM 3546 O O   . ILE B 2 53  ? 1.234   -6.445  -15.673 1.00 59.05  ? 51  ILE B O   1 
ATOM 3547 C CB  . ILE B 2 53  ? 0.929   -4.215  -13.275 1.00 53.53  ? 51  ILE B CB  1 
ATOM 3548 C CG1 . ILE B 2 53  ? 2.174   -3.430  -12.855 1.00 51.83  ? 51  ILE B CG1 1 
ATOM 3549 C CG2 . ILE B 2 53  ? 0.951   -5.630  -12.704 1.00 49.59  ? 51  ILE B CG2 1 
ATOM 3550 C CD1 . ILE B 2 53  ? 2.319   -3.274  -11.366 1.00 47.95  ? 51  ILE B CD1 1 
ATOM 3551 N N   . SER B 2 54  ? 2.926   -4.954  -15.707 1.00 57.80  ? 52  SER B N   1 
ATOM 3552 C CA  . SER B 2 54  ? 3.844   -5.832  -16.414 1.00 61.72  ? 52  SER B CA  1 
ATOM 3553 C C   . SER B 2 54  ? 4.608   -6.704  -15.418 1.00 64.90  ? 52  SER B C   1 
ATOM 3554 O O   . SER B 2 54  ? 4.279   -6.767  -14.230 1.00 65.09  ? 52  SER B O   1 
ATOM 3555 C CB  . SER B 2 54  ? 4.786   -5.010  -17.291 1.00 67.53  ? 52  SER B CB  1 
ATOM 3556 O OG  . SER B 2 54  ? 5.859   -4.485  -16.529 1.00 75.64  ? 52  SER B OG  1 
ATOM 3557 N N   . GLU B 2 55  ? 5.647   -7.386  -15.899 1.00 68.29  ? 53  GLU B N   1 
ATOM 3558 C CA  . GLU B 2 55  ? 6.440   -8.286  -15.074 1.00 74.59  ? 53  GLU B CA  1 
ATOM 3559 C C   . GLU B 2 55  ? 7.722   -7.652  -14.552 1.00 78.55  ? 53  GLU B C   1 
ATOM 3560 O O   . GLU B 2 55  ? 8.356   -8.224  -13.659 1.00 78.19  ? 53  GLU B O   1 
ATOM 3561 C CB  . GLU B 2 55  ? 6.793   -9.555  -15.861 1.00 79.00  ? 53  GLU B CB  1 
ATOM 3562 C CG  . GLU B 2 55  ? 7.859   -9.352  -16.930 1.00 83.25  ? 53  GLU B CG  1 
ATOM 3563 C CD  . GLU B 2 55  ? 7.286   -8.842  -18.239 1.00 80.05  ? 53  GLU B CD  1 
ATOM 3564 O OE1 . GLU B 2 55  ? 6.048   -8.709  -18.335 1.00 71.92  ? 53  GLU B OE1 1 
ATOM 3565 O OE2 . GLU B 2 55  ? 8.074   -8.571  -19.170 1.00 85.95  ? 53  GLU B OE2 1 
ATOM 3566 N N   . SER B 2 56  ? 8.121   -6.498  -15.081 1.00 86.57  ? 54  SER B N   1 
ATOM 3567 C CA  . SER B 2 56  ? 9.343   -5.846  -14.641 1.00 92.75  ? 54  SER B CA  1 
ATOM 3568 C C   . SER B 2 56  ? 9.214   -4.345  -14.839 1.00 97.26  ? 54  SER B C   1 
ATOM 3569 O O   . SER B 2 56  ? 8.473   -3.879  -15.710 1.00 96.33  ? 54  SER B O   1 
ATOM 3570 C CB  . SER B 2 56  ? 10.569  -6.373  -15.394 1.00 92.29  ? 54  SER B CB  1 
ATOM 3571 O OG  . SER B 2 56  ? 11.763  -5.821  -14.866 1.00 91.41  ? 54  SER B OG  1 
ATOM 3572 N N   . ARG B 2 57  ? 9.937   -3.597  -14.001 1.00 93.50  ? 55  ARG B N   1 
ATOM 3573 C CA  . ARG B 2 57  ? 10.015  -2.140  -14.060 1.00 93.21  ? 55  ARG B CA  1 
ATOM 3574 C C   . ARG B 2 57  ? 8.667   -1.471  -13.803 1.00 95.39  ? 55  ARG B C   1 
ATOM 3575 O O   . ARG B 2 57  ? 8.559   -0.243  -13.883 1.00 97.67  ? 55  ARG B O   1 
ATOM 3576 C CB  . ARG B 2 57  ? 10.584  -1.688  -15.410 1.00 91.54  ? 55  ARG B CB  1 
ATOM 3577 C CG  . ARG B 2 57  ? 12.091  -1.854  -15.540 1.00 95.10  ? 55  ARG B CG  1 
ATOM 3578 C CD  . ARG B 2 57  ? 12.437  -3.030  -16.446 1.00 98.16  ? 55  ARG B CD  1 
ATOM 3579 N NE  . ARG B 2 57  ? 12.012  -2.812  -17.825 1.00 102.55 ? 55  ARG B NE  1 
ATOM 3580 C CZ  . ARG B 2 57  ? 12.356  -3.585  -18.847 1.00 100.42 ? 55  ARG B CZ  1 
ATOM 3581 N NH1 . ARG B 2 57  ? 13.147  -4.632  -18.686 1.00 95.12  ? 55  ARG B NH1 1 
ATOM 3582 N NH2 . ARG B 2 57  ? 11.891  -3.301  -20.061 1.00 92.51  ? 55  ARG B NH2 1 
ATOM 3583 N N   . GLY B 2 58  ? 7.638   -2.254  -13.494 1.00 97.96  ? 56  GLY B N   1 
ATOM 3584 C CA  . GLY B 2 58  ? 6.344   -1.675  -13.169 1.00 93.88  ? 56  GLY B CA  1 
ATOM 3585 C C   . GLY B 2 58  ? 5.683   -0.957  -14.325 1.00 94.21  ? 56  GLY B C   1 
ATOM 3586 O O   . GLY B 2 58  ? 5.065   0.098   -14.129 1.00 95.19  ? 56  GLY B O   1 
ATOM 3587 N N   . THR B 2 59  ? 5.801   -1.503  -15.533 1.00 81.48  ? 57  THR B N   1 
ATOM 3588 C CA  . THR B 2 59  ? 5.147   -0.910  -16.691 1.00 74.24  ? 57  THR B CA  1 
ATOM 3589 C C   . THR B 2 59  ? 3.641   -1.123  -16.589 1.00 65.71  ? 57  THR B C   1 
ATOM 3590 O O   . THR B 2 59  ? 3.176   -2.261  -16.465 1.00 62.93  ? 57  THR B O   1 
ATOM 3591 C CB  . THR B 2 59  ? 5.689   -1.518  -17.982 1.00 74.45  ? 57  THR B CB  1 
ATOM 3592 O OG1 . THR B 2 59  ? 7.082   -1.820  -17.828 1.00 78.29  ? 57  THR B OG1 1 
ATOM 3593 C CG2 . THR B 2 59  ? 5.511   -0.546  -19.136 1.00 70.26  ? 57  THR B CG2 1 
ATOM 3594 N N   . THR B 2 60  ? 2.881   -0.033  -16.641 1.00 60.44  ? 58  THR B N   1 
ATOM 3595 C CA  . THR B 2 60  ? 1.439   -0.078  -16.453 1.00 58.27  ? 58  THR B CA  1 
ATOM 3596 C C   . THR B 2 60  ? 0.721   0.427   -17.697 1.00 62.79  ? 58  THR B C   1 
ATOM 3597 O O   . THR B 2 60  ? 1.267   1.213   -18.478 1.00 65.13  ? 58  THR B O   1 
ATOM 3598 C CB  . THR B 2 60  ? 1.004   0.757   -15.239 1.00 56.17  ? 58  THR B CB  1 
ATOM 3599 O OG1 . THR B 2 60  ? 1.667   2.027   -15.263 1.00 59.72  ? 58  THR B OG1 1 
ATOM 3600 C CG2 . THR B 2 60  ? 1.360   0.037   -13.949 1.00 55.25  ? 58  THR B CG2 1 
ATOM 3601 N N   . ASP B 2 61  ? -0.518  -0.034  -17.868 1.00 50.71  ? 59  ASP B N   1 
ATOM 3602 C CA  . ASP B 2 61  ? -1.375  0.387   -18.969 1.00 48.79  ? 59  ASP B CA  1 
ATOM 3603 C C   . ASP B 2 61  ? -2.809  0.479   -18.475 1.00 44.03  ? 59  ASP B C   1 
ATOM 3604 O O   . ASP B 2 61  ? -3.296  -0.439  -17.809 1.00 45.84  ? 59  ASP B O   1 
ATOM 3605 C CB  . ASP B 2 61  ? -1.285  -0.583  -20.150 1.00 52.96  ? 59  ASP B CB  1 
ATOM 3606 C CG  . ASP B 2 61  ? -1.532  0.099   -21.478 1.00 56.09  ? 59  ASP B CG  1 
ATOM 3607 O OD1 . ASP B 2 61  ? -0.735  0.989   -21.841 1.00 56.91  ? 59  ASP B OD1 1 
ATOM 3608 O OD2 . ASP B 2 61  ? -2.520  -0.254  -22.157 1.00 59.84  ? 59  ASP B OD2 1 
ATOM 3609 N N   . TYR B 2 62  ? -3.483  1.578   -18.807 1.00 43.88  ? 60  TYR B N   1 
ATOM 3610 C CA  . TYR B 2 62  ? -4.831  1.838   -18.325 1.00 47.66  ? 60  TYR B CA  1 
ATOM 3611 C C   . TYR B 2 62  ? -5.773  2.101   -19.491 1.00 48.28  ? 60  TYR B C   1 
ATOM 3612 O O   . TYR B 2 62  ? -5.357  2.557   -20.560 1.00 52.23  ? 60  TYR B O   1 
ATOM 3613 C CB  . TYR B 2 62  ? -4.872  3.043   -17.370 1.00 45.88  ? 60  TYR B CB  1 
ATOM 3614 C CG  . TYR B 2 62  ? -4.091  2.864   -16.087 1.00 42.75  ? 60  TYR B CG  1 
ATOM 3615 C CD1 . TYR B 2 62  ? -2.733  3.148   -16.034 1.00 42.50  ? 60  TYR B CD1 1 
ATOM 3616 C CD2 . TYR B 2 62  ? -4.715  2.425   -14.925 1.00 42.20  ? 60  TYR B CD2 1 
ATOM 3617 C CE1 . TYR B 2 62  ? -2.015  2.992   -14.864 1.00 49.53  ? 60  TYR B CE1 1 
ATOM 3618 C CE2 . TYR B 2 62  ? -4.005  2.268   -13.748 1.00 43.53  ? 60  TYR B CE2 1 
ATOM 3619 C CZ  . TYR B 2 62  ? -2.655  2.553   -13.724 1.00 48.97  ? 60  TYR B CZ  1 
ATOM 3620 O OH  . TYR B 2 62  ? -1.940  2.401   -12.557 1.00 48.22  ? 60  TYR B OH  1 
ATOM 3621 N N   . ALA B 2 63  ? -7.051  1.809   -19.267 1.00 48.48  ? 61  ALA B N   1 
ATOM 3622 C CA  . ALA B 2 63  ? -8.087  2.192   -20.212 1.00 50.90  ? 61  ALA B CA  1 
ATOM 3623 C C   . ALA B 2 63  ? -8.328  3.695   -20.139 1.00 58.05  ? 61  ALA B C   1 
ATOM 3624 O O   . ALA B 2 63  ? -8.160  4.323   -19.090 1.00 62.01  ? 61  ALA B O   1 
ATOM 3625 C CB  . ALA B 2 63  ? -9.383  1.435   -19.924 1.00 46.07  ? 61  ALA B CB  1 
ATOM 3626 N N   . ASP B 2 64  ? -8.725  4.275   -21.274 1.00 58.10  ? 62  ASP B N   1 
ATOM 3627 C CA  . ASP B 2 64  ? -8.907  5.722   -21.329 1.00 63.40  ? 62  ASP B CA  1 
ATOM 3628 C C   . ASP B 2 64  ? -10.018 6.187   -20.396 1.00 59.16  ? 62  ASP B C   1 
ATOM 3629 O O   . ASP B 2 64  ? -9.954  7.301   -19.865 1.00 65.83  ? 62  ASP B O   1 
ATOM 3630 C CB  . ASP B 2 64  ? -9.191  6.160   -22.766 1.00 67.57  ? 62  ASP B CB  1 
ATOM 3631 C CG  . ASP B 2 64  ? -8.076  5.775   -23.722 1.00 78.77  ? 62  ASP B CG  1 
ATOM 3632 O OD1 . ASP B 2 64  ? -7.020  5.305   -23.246 1.00 75.40  ? 62  ASP B OD1 1 
ATOM 3633 O OD2 . ASP B 2 64  ? -8.253  5.943   -24.948 1.00 87.36  ? 62  ASP B OD2 1 
ATOM 3634 N N   . SER B 2 65  ? -11.032 5.349   -20.169 1.00 62.09  ? 63  SER B N   1 
ATOM 3635 C CA  . SER B 2 65  ? -12.131 5.738   -19.294 1.00 62.65  ? 63  SER B CA  1 
ATOM 3636 C C   . SER B 2 65  ? -11.719 5.791   -17.829 1.00 64.55  ? 63  SER B C   1 
ATOM 3637 O O   . SER B 2 65  ? -12.371 6.483   -17.040 1.00 70.90  ? 63  SER B O   1 
ATOM 3638 C CB  . SER B 2 65  ? -13.307 4.775   -19.467 1.00 63.03  ? 63  SER B CB  1 
ATOM 3639 O OG  . SER B 2 65  ? -13.598 4.573   -20.839 1.00 75.28  ? 63  SER B OG  1 
ATOM 3640 N N   . VAL B 2 66  ? -10.657 5.082   -17.447 1.00 55.33  ? 64  VAL B N   1 
ATOM 3641 C CA  . VAL B 2 66  ? -10.206 5.026   -16.065 1.00 50.03  ? 64  VAL B CA  1 
ATOM 3642 C C   . VAL B 2 66  ? -8.799  5.582   -15.899 1.00 51.55  ? 64  VAL B C   1 
ATOM 3643 O O   . VAL B 2 66  ? -8.211  5.456   -14.825 1.00 53.77  ? 64  VAL B O   1 
ATOM 3644 C CB  . VAL B 2 66  ? -10.291 3.592   -15.508 1.00 48.92  ? 64  VAL B CB  1 
ATOM 3645 C CG1 . VAL B 2 66  ? -11.744 3.177   -15.341 1.00 49.72  ? 64  VAL B CG1 1 
ATOM 3646 C CG2 . VAL B 2 66  ? -9.551  2.626   -16.420 1.00 53.69  ? 64  VAL B CG2 1 
ATOM 3647 N N   . LYS B 2 67  ? -8.239  6.186   -16.943 1.00 55.76  ? 65  LYS B N   1 
ATOM 3648 C CA  . LYS B 2 67  ? -6.922  6.797   -16.826 1.00 55.59  ? 65  LYS B CA  1 
ATOM 3649 C C   . LYS B 2 67  ? -6.993  8.006   -15.905 1.00 59.98  ? 65  LYS B C   1 
ATOM 3650 O O   . LYS B 2 67  ? -7.913  8.825   -16.004 1.00 60.20  ? 65  LYS B O   1 
ATOM 3651 C CB  . LYS B 2 67  ? -6.394  7.203   -18.200 1.00 53.42  ? 65  LYS B CB  1 
ATOM 3652 C CG  . LYS B 2 67  ? -4.878  7.296   -18.267 1.00 51.74  ? 65  LYS B CG  1 
ATOM 3653 C CD  . LYS B 2 67  ? -4.318  6.451   -19.399 1.00 57.26  ? 65  LYS B CD  1 
ATOM 3654 C CE  . LYS B 2 67  ? -4.594  7.085   -20.753 1.00 60.28  ? 65  LYS B CE  1 
ATOM 3655 N NZ  . LYS B 2 67  ? -4.563  6.077   -21.851 1.00 65.28  ? 65  LYS B NZ  1 
ATOM 3656 N N   . GLY B 2 68  ? -6.023  8.113   -14.997 1.00 61.34  ? 66  GLY B N   1 
ATOM 3657 C CA  . GLY B 2 68  ? -5.996  9.177   -14.021 1.00 56.77  ? 66  GLY B CA  1 
ATOM 3658 C C   . GLY B 2 68  ? -6.925  8.994   -12.843 1.00 57.84  ? 66  GLY B C   1 
ATOM 3659 O O   . GLY B 2 68  ? -6.765  9.692   -11.835 1.00 61.78  ? 66  GLY B O   1 
ATOM 3660 N N   . ARG B 2 69  ? -7.893  8.083   -12.933 1.00 51.11  ? 67  ARG B N   1 
ATOM 3661 C CA  . ARG B 2 69  ? -8.809  7.798   -11.836 1.00 47.78  ? 67  ARG B CA  1 
ATOM 3662 C C   . ARG B 2 69  ? -8.457  6.518   -11.091 1.00 49.32  ? 67  ARG B C   1 
ATOM 3663 O O   . ARG B 2 69  ? -8.522  6.487   -9.858  1.00 45.54  ? 67  ARG B O   1 
ATOM 3664 C CB  . ARG B 2 69  ? -10.247 7.702   -12.357 1.00 46.12  ? 67  ARG B CB  1 
ATOM 3665 C CG  . ARG B 2 69  ? -10.696 8.896   -13.180 1.00 53.11  ? 67  ARG B CG  1 
ATOM 3666 C CD  . ARG B 2 69  ? -11.987 8.594   -13.925 1.00 52.58  ? 67  ARG B CD  1 
ATOM 3667 N NE  . ARG B 2 69  ? -12.999 8.040   -13.035 1.00 57.75  ? 67  ARG B NE  1 
ATOM 3668 C CZ  . ARG B 2 69  ? -13.578 6.858   -13.201 1.00 57.03  ? 67  ARG B CZ  1 
ATOM 3669 N NH1 . ARG B 2 69  ? -13.287 6.085   -14.235 1.00 54.90  ? 67  ARG B NH1 1 
ATOM 3670 N NH2 . ARG B 2 69  ? -14.471 6.442   -12.308 1.00 57.56  ? 67  ARG B NH2 1 
ATOM 3671 N N   . PHE B 2 70  ? -8.086  5.465   -11.813 1.00 46.13  ? 68  PHE B N   1 
ATOM 3672 C CA  . PHE B 2 70  ? -7.724  4.183   -11.229 1.00 36.34  ? 68  PHE B CA  1 
ATOM 3673 C C   . PHE B 2 70  ? -6.208  4.020   -11.241 1.00 40.83  ? 68  PHE B C   1 
ATOM 3674 O O   . PHE B 2 70  ? -5.512  4.580   -12.091 1.00 40.59  ? 68  PHE B O   1 
ATOM 3675 C CB  . PHE B 2 70  ? -8.369  3.022   -11.993 1.00 41.85  ? 68  PHE B CB  1 
ATOM 3676 C CG  . PHE B 2 70  ? -9.862  2.907   -11.810 1.00 40.38  ? 68  PHE B CG  1 
ATOM 3677 C CD1 . PHE B 2 70  ? -10.598 3.927   -11.229 1.00 39.93  ? 68  PHE B CD1 1 
ATOM 3678 C CD2 . PHE B 2 70  ? -10.532 1.774   -12.245 1.00 38.18  ? 68  PHE B CD2 1 
ATOM 3679 C CE1 . PHE B 2 70  ? -11.967 3.816   -11.075 1.00 42.43  ? 68  PHE B CE1 1 
ATOM 3680 C CE2 . PHE B 2 70  ? -11.900 1.656   -12.092 1.00 40.79  ? 68  PHE B CE2 1 
ATOM 3681 C CZ  . PHE B 2 70  ? -12.618 2.678   -11.505 1.00 45.79  ? 68  PHE B CZ  1 
ATOM 3682 N N   . THR B 2 71  ? -5.702  3.240   -10.290 1.00 43.65  ? 69  THR B N   1 
ATOM 3683 C CA  . THR B 2 71  ? -4.271  2.998   -10.176 1.00 43.59  ? 69  THR B CA  1 
ATOM 3684 C C   . THR B 2 71  ? -4.045  1.532   -9.842  1.00 43.93  ? 69  THR B C   1 
ATOM 3685 O O   . THR B 2 71  ? -4.618  1.017   -8.878  1.00 44.55  ? 69  THR B O   1 
ATOM 3686 C CB  . THR B 2 71  ? -3.635  3.889   -9.101  1.00 45.21  ? 69  THR B CB  1 
ATOM 3687 O OG1 . THR B 2 71  ? -4.305  5.156   -9.071  1.00 46.78  ? 69  THR B OG1 1 
ATOM 3688 C CG2 . THR B 2 71  ? -2.160  4.112   -9.399  1.00 41.73  ? 69  THR B CG2 1 
ATOM 3689 N N   . ILE B 2 72  ? -3.219  0.867   -10.641 1.00 43.43  ? 70  ILE B N   1 
ATOM 3690 C CA  . ILE B 2 72  ? -2.906  -0.543  -10.449 1.00 42.92  ? 70  ILE B CA  1 
ATOM 3691 C C   . ILE B 2 72  ? -1.511  -0.654  -9.851  1.00 43.90  ? 70  ILE B C   1 
ATOM 3692 O O   . ILE B 2 72  ? -0.620  0.150   -10.157 1.00 41.76  ? 70  ILE B O   1 
ATOM 3693 C CB  . ILE B 2 72  ? -3.023  -1.329  -11.773 1.00 47.50  ? 70  ILE B CB  1 
ATOM 3694 C CG1 . ILE B 2 72  ? -2.909  -2.837  -11.527 1.00 47.41  ? 70  ILE B CG1 1 
ATOM 3695 C CG2 . ILE B 2 72  ? -1.989  -0.860  -12.788 1.00 44.90  ? 70  ILE B CG2 1 
ATOM 3696 C CD1 . ILE B 2 72  ? -3.406  -3.686  -12.680 1.00 42.38  ? 70  ILE B CD1 1 
ATOM 3697 N N   . SER B 2 73  ? -1.330  -1.635  -8.970  1.00 46.72  ? 71  SER B N   1 
ATOM 3698 C CA  . SER B 2 73  ? -0.045  -1.871  -8.331  1.00 46.02  ? 71  SER B CA  1 
ATOM 3699 C C   . SER B 2 73  ? 0.065   -3.352  -8.003  1.00 47.56  ? 71  SER B C   1 
ATOM 3700 O O   . SER B 2 73  ? -0.939  -4.062  -7.912  1.00 48.98  ? 71  SER B O   1 
ATOM 3701 C CB  . SER B 2 73  ? 0.126   -1.010  -7.072  1.00 43.59  ? 71  SER B CB  1 
ATOM 3702 O OG  . SER B 2 73  ? -1.062  -0.987  -6.299  1.00 50.29  ? 71  SER B OG  1 
ATOM 3703 N N   . ARG B 2 74  ? 1.302   -3.813  -7.838  1.00 48.75  ? 72  ARG B N   1 
ATOM 3704 C CA  . ARG B 2 74  ? 1.579   -5.221  -7.599  1.00 52.65  ? 72  ARG B CA  1 
ATOM 3705 C C   . ARG B 2 74  ? 2.499   -5.370  -6.397  1.00 59.00  ? 72  ARG B C   1 
ATOM 3706 O O   . ARG B 2 74  ? 3.222   -4.444  -6.018  1.00 59.38  ? 72  ARG B O   1 
ATOM 3707 C CB  . ARG B 2 74  ? 2.210   -5.893  -8.831  1.00 50.69  ? 72  ARG B CB  1 
ATOM 3708 C CG  . ARG B 2 74  ? 3.735   -5.925  -8.830  1.00 51.62  ? 72  ARG B CG  1 
ATOM 3709 C CD  . ARG B 2 74  ? 4.274   -6.587  -10.091 1.00 53.64  ? 72  ARG B CD  1 
ATOM 3710 N NE  . ARG B 2 74  ? 3.930   -8.003  -10.157 1.00 52.92  ? 72  ARG B NE  1 
ATOM 3711 C CZ  . ARG B 2 74  ? 3.521   -8.625  -11.254 1.00 49.96  ? 72  ARG B CZ  1 
ATOM 3712 N NH1 . ARG B 2 74  ? 3.391   -7.985  -12.404 1.00 55.24  ? 72  ARG B NH1 1 
ATOM 3713 N NH2 . ARG B 2 74  ? 3.230   -9.921  -11.194 1.00 52.91  ? 72  ARG B NH2 1 
ATOM 3714 N N   . ASP B 2 75  ? 2.458   -6.559  -5.798  1.00 68.01  ? 73  ASP B N   1 
ATOM 3715 C CA  . ASP B 2 75  ? 3.300   -6.900  -4.652  1.00 68.10  ? 73  ASP B CA  1 
ATOM 3716 C C   . ASP B 2 75  ? 3.722   -8.356  -4.821  1.00 67.96  ? 73  ASP B C   1 
ATOM 3717 O O   . ASP B 2 75  ? 2.933   -9.270  -4.565  1.00 71.54  ? 73  ASP B O   1 
ATOM 3718 C CB  . ASP B 2 75  ? 2.561   -6.679  -3.337  1.00 65.03  ? 73  ASP B CB  1 
ATOM 3719 C CG  . ASP B 2 75  ? 3.500   -6.538  -2.156  1.00 67.59  ? 73  ASP B CG  1 
ATOM 3720 O OD1 . ASP B 2 75  ? 4.666   -6.976  -2.262  1.00 67.94  ? 73  ASP B OD1 1 
ATOM 3721 O OD2 . ASP B 2 75  ? 3.075   -5.979  -1.123  1.00 71.04  ? 73  ASP B OD2 1 
ATOM 3722 N N   . ASN B 2 76  ? 4.966   -8.567  -5.255  1.00 61.20  ? 74  ASN B N   1 
ATOM 3723 C CA  . ASN B 2 76  ? 5.440   -9.921  -5.507  1.00 62.52  ? 74  ASN B CA  1 
ATOM 3724 C C   . ASN B 2 76  ? 5.695   -10.696 -4.223  1.00 65.31  ? 74  ASN B C   1 
ATOM 3725 O O   . ASN B 2 76  ? 5.789   -11.927 -4.266  1.00 69.42  ? 74  ASN B O   1 
ATOM 3726 C CB  . ASN B 2 76  ? 6.709   -9.879  -6.355  1.00 64.47  ? 74  ASN B CB  1 
ATOM 3727 C CG  . ASN B 2 76  ? 6.491   -9.193  -7.685  1.00 61.14  ? 74  ASN B CG  1 
ATOM 3728 O OD1 . ASN B 2 76  ? 5.356   -9.038  -8.136  1.00 56.03  ? 74  ASN B OD1 1 
ATOM 3729 N ND2 . ASN B 2 76  ? 7.578   -8.768  -8.317  1.00 63.98  ? 74  ASN B ND2 1 
ATOM 3730 N N   . ALA B 2 77  ? 5.808   -10.005 -3.087  1.00 76.49  ? 75  ALA B N   1 
ATOM 3731 C CA  . ALA B 2 77  ? 6.043   -10.683 -1.819  1.00 74.42  ? 75  ALA B CA  1 
ATOM 3732 C C   . ALA B 2 77  ? 4.770   -11.295 -1.252  1.00 73.51  ? 75  ALA B C   1 
ATOM 3733 O O   . ALA B 2 77  ? 4.824   -12.358 -0.622  1.00 81.64  ? 75  ALA B O   1 
ATOM 3734 C CB  . ALA B 2 77  ? 6.653   -9.709  -0.810  1.00 73.81  ? 75  ALA B CB  1 
ATOM 3735 N N   . LYS B 2 78  ? 3.625   -10.649 -1.463  1.00 64.32  ? 76  LYS B N   1 
ATOM 3736 C CA  . LYS B 2 78  ? 2.343   -11.144 -0.986  1.00 59.11  ? 76  LYS B CA  1 
ATOM 3737 C C   . LYS B 2 78  ? 1.497   -11.769 -2.086  1.00 61.47  ? 76  LYS B C   1 
ATOM 3738 O O   . LYS B 2 78  ? 0.346   -12.132 -1.826  1.00 61.16  ? 76  LYS B O   1 
ATOM 3739 C CB  . LYS B 2 78  ? 1.563   -10.014 -0.309  1.00 61.85  ? 76  LYS B CB  1 
ATOM 3740 C CG  . LYS B 2 78  ? 2.031   -9.716  1.110   1.00 72.46  ? 76  LYS B CG  1 
ATOM 3741 C CD  . LYS B 2 78  ? 1.816   -8.261  1.480   1.00 68.65  ? 76  LYS B CD  1 
ATOM 3742 C CE  . LYS B 2 78  ? 3.134   -7.499  1.517   1.00 69.39  ? 76  LYS B CE  1 
ATOM 3743 N NZ  . LYS B 2 78  ? 4.207   -8.217  2.268   1.00 70.43  ? 76  LYS B NZ  1 
ATOM 3744 N N   . ASN B 2 79  ? 2.036   -11.902 -3.302  1.00 62.88  ? 77  ASN B N   1 
ATOM 3745 C CA  . ASN B 2 79  ? 1.336   -12.552 -4.412  1.00 53.34  ? 77  ASN B CA  1 
ATOM 3746 C C   . ASN B 2 79  ? -0.036  -11.925 -4.651  1.00 52.38  ? 77  ASN B C   1 
ATOM 3747 O O   . ASN B 2 79  ? -1.030  -12.624 -4.855  1.00 54.57  ? 77  ASN B O   1 
ATOM 3748 C CB  . ASN B 2 79  ? 1.204   -14.057 -4.171  1.00 58.03  ? 77  ASN B CB  1 
ATOM 3749 C CG  . ASN B 2 79  ? 2.301   -14.855 -4.841  1.00 64.54  ? 77  ASN B CG  1 
ATOM 3750 O OD1 . ASN B 2 79  ? 3.487   -14.612 -4.617  1.00 62.84  ? 77  ASN B OD1 1 
ATOM 3751 N ND2 . ASN B 2 79  ? 1.911   -15.826 -5.659  1.00 77.20  ? 77  ASN B ND2 1 
ATOM 3752 N N   . THR B 2 80  ? -0.097  -10.595 -4.615  1.00 54.09  ? 78  THR B N   1 
ATOM 3753 C CA  . THR B 2 80  ? -1.357  -9.882  -4.768  1.00 54.70  ? 78  THR B CA  1 
ATOM 3754 C C   . THR B 2 80  ? -1.145  -8.637  -5.616  1.00 51.10  ? 78  THR B C   1 
ATOM 3755 O O   . THR B 2 80  ? -0.028  -8.132  -5.754  1.00 52.29  ? 78  THR B O   1 
ATOM 3756 C CB  . THR B 2 80  ? -1.966  -9.491  -3.411  1.00 53.99  ? 78  THR B CB  1 
ATOM 3757 O OG1 . THR B 2 80  ? -3.263  -8.910  -3.608  1.00 56.72  ? 78  THR B OG1 1 
ATOM 3758 C CG2 . THR B 2 80  ? -1.070  -8.499  -2.685  1.00 52.40  ? 78  THR B CG2 1 
ATOM 3759 N N   . ILE B 2 81  ? -2.244  -8.150  -6.188  1.00 49.22  ? 79  ILE B N   1 
ATOM 3760 C CA  . ILE B 2 81  ? -2.245  -6.930  -6.984  1.00 52.91  ? 79  ILE B CA  1 
ATOM 3761 C C   . ILE B 2 81  ? -3.446  -6.090  -6.574  1.00 49.24  ? 79  ILE B C   1 
ATOM 3762 O O   . ILE B 2 81  ? -4.507  -6.614  -6.221  1.00 48.75  ? 79  ILE B O   1 
ATOM 3763 C CB  . ILE B 2 81  ? -2.266  -7.218  -8.505  1.00 47.05  ? 79  ILE B CB  1 
ATOM 3764 C CG1 . ILE B 2 81  ? -3.326  -8.261  -8.858  1.00 46.79  ? 79  ILE B CG1 1 
ATOM 3765 C CG2 . ILE B 2 81  ? -0.906  -7.667  -8.986  1.00 49.55  ? 79  ILE B CG2 1 
ATOM 3766 C CD1 . ILE B 2 81  ? -4.619  -7.656  -9.327  1.00 47.96  ? 79  ILE B CD1 1 
ATOM 3767 N N   . TYR B 2 82  ? -3.274  -4.774  -6.627  1.00 47.98  ? 80  TYR B N   1 
ATOM 3768 C CA  . TYR B 2 82  ? -4.282  -3.842  -6.156  1.00 47.11  ? 80  TYR B CA  1 
ATOM 3769 C C   . TYR B 2 82  ? -4.785  -2.971  -7.299  1.00 45.70  ? 80  TYR B C   1 
ATOM 3770 O O   . TYR B 2 82  ? -4.111  -2.786  -8.316  1.00 45.55  ? 80  TYR B O   1 
ATOM 3771 C CB  . TYR B 2 82  ? -3.732  -2.953  -5.034  1.00 45.73  ? 80  TYR B CB  1 
ATOM 3772 C CG  . TYR B 2 82  ? -2.773  -3.662  -4.105  1.00 46.68  ? 80  TYR B CG  1 
ATOM 3773 C CD1 . TYR B 2 82  ? -3.239  -4.404  -3.029  1.00 46.17  ? 80  TYR B CD1 1 
ATOM 3774 C CD2 . TYR B 2 82  ? -1.400  -3.587  -4.305  1.00 47.09  ? 80  TYR B CD2 1 
ATOM 3775 C CE1 . TYR B 2 82  ? -2.367  -5.051  -2.178  1.00 50.62  ? 80  TYR B CE1 1 
ATOM 3776 C CE2 . TYR B 2 82  ? -0.519  -4.232  -3.460  1.00 50.13  ? 80  TYR B CE2 1 
ATOM 3777 C CZ  . TYR B 2 82  ? -1.008  -4.963  -2.396  1.00 55.18  ? 80  TYR B CZ  1 
ATOM 3778 O OH  . TYR B 2 82  ? -0.139  -5.609  -1.545  1.00 60.72  ? 80  TYR B OH  1 
ATOM 3779 N N   . LEU B 2 83  ? -5.991  -2.433  -7.111  1.00 45.25  ? 81  LEU B N   1 
ATOM 3780 C CA  . LEU B 2 83  ? -6.602  -1.486  -8.046  1.00 43.87  ? 81  LEU B CA  1 
ATOM 3781 C C   . LEU B 2 83  ? -7.266  -0.397  -7.203  1.00 45.86  ? 81  LEU B C   1 
ATOM 3782 O O   . LEU B 2 83  ? -8.404  -0.553  -6.753  1.00 43.82  ? 81  LEU B O   1 
ATOM 3783 C CB  . LEU B 2 83  ? -7.597  -2.175  -8.971  1.00 45.01  ? 81  LEU B CB  1 
ATOM 3784 C CG  . LEU B 2 83  ? -8.218  -1.280  -10.043 1.00 45.17  ? 81  LEU B CG  1 
ATOM 3785 C CD1 . LEU B 2 83  ? -7.143  -0.801  -10.999 1.00 43.25  ? 81  LEU B CD1 1 
ATOM 3786 C CD2 . LEU B 2 83  ? -9.322  -2.008  -10.795 1.00 38.24  ? 81  LEU B CD2 1 
ATOM 3787 N N   . GLN B 2 84  ? -6.542  0.698   -6.984  1.00 46.71  ? 82  GLN B N   1 
ATOM 3788 C CA  . GLN B 2 84  ? -7.072  1.835   -6.237  1.00 45.06  ? 82  GLN B CA  1 
ATOM 3789 C C   . GLN B 2 84  ? -7.969  2.651   -7.159  1.00 44.81  ? 82  GLN B C   1 
ATOM 3790 O O   . GLN B 2 84  ? -7.486  3.306   -8.087  1.00 45.79  ? 82  GLN B O   1 
ATOM 3791 C CB  . GLN B 2 84  ? -5.939  2.688   -5.678  1.00 50.62  ? 82  GLN B CB  1 
ATOM 3792 C CG  . GLN B 2 84  ? -6.406  3.986   -5.032  1.00 50.83  ? 82  GLN B CG  1 
ATOM 3793 C CD  . GLN B 2 84  ? -7.280  3.750   -3.814  1.00 50.30  ? 82  GLN B CD  1 
ATOM 3794 O OE1 . GLN B 2 84  ? -7.123  2.756   -3.106  1.00 52.23  ? 82  GLN B OE1 1 
ATOM 3795 N NE2 . GLN B 2 84  ? -8.208  4.668   -3.566  1.00 55.28  ? 82  GLN B NE2 1 
ATOM 3796 N N   . MET B 2 85  ? -9.273  2.621   -6.902  1.00 40.75  ? 83  MET B N   1 
ATOM 3797 C CA  . MET B 2 85  ? -10.258 3.278   -7.756  1.00 39.09  ? 83  MET B CA  1 
ATOM 3798 C C   . MET B 2 85  ? -10.686 4.590   -7.110  1.00 42.84  ? 83  MET B C   1 
ATOM 3799 O O   . MET B 2 85  ? -11.482 4.600   -6.168  1.00 48.23  ? 83  MET B O   1 
ATOM 3800 C CB  . MET B 2 85  ? -11.448 2.359   -7.998  1.00 39.03  ? 83  MET B CB  1 
ATOM 3801 C CG  . MET B 2 85  ? -11.061 1.010   -8.565  1.00 42.36  ? 83  MET B CG  1 
ATOM 3802 S SD  . MET B 2 85  ? -12.499 0.011   -8.973  1.00 56.89  ? 83  MET B SD  1 
ATOM 3803 C CE  . MET B 2 85  ? -13.322 -0.020  -7.388  1.00 45.14  ? 83  MET B CE  1 
ATOM 3804 N N   . ASN B 2 86  ? -10.167 5.699   -7.626  1.00 45.45  ? 84  ASN B N   1 
ATOM 3805 C CA  . ASN B 2 86  ? -10.534 7.029   -7.168  1.00 46.62  ? 84  ASN B CA  1 
ATOM 3806 C C   . ASN B 2 86  ? -11.460 7.698   -8.176  1.00 49.48  ? 84  ASN B C   1 
ATOM 3807 O O   . ASN B 2 86  ? -11.521 7.314   -9.348  1.00 51.49  ? 84  ASN B O   1 
ATOM 3808 C CB  . ASN B 2 86  ? -9.289  7.893   -6.941  1.00 46.30  ? 84  ASN B CB  1 
ATOM 3809 C CG  . ASN B 2 86  ? -8.362  7.314   -5.891  1.00 44.47  ? 84  ASN B CG  1 
ATOM 3810 O OD1 . ASN B 2 86  ? -8.772  7.061   -4.759  1.00 51.96  ? 84  ASN B OD1 1 
ATOM 3811 N ND2 . ASN B 2 86  ? -7.104  7.103   -6.261  1.00 44.67  ? 84  ASN B ND2 1 
ATOM 3812 N N   . SER B 2 87  ? -12.188 8.708   -7.696  1.00 49.04  ? 85  SER B N   1 
ATOM 3813 C CA  . SER B 2 87  ? -13.115 9.494   -8.513  1.00 50.75  ? 85  SER B CA  1 
ATOM 3814 C C   . SER B 2 87  ? -14.144 8.590   -9.197  1.00 55.90  ? 85  SER B C   1 
ATOM 3815 O O   . SER B 2 87  ? -14.264 8.550   -10.423 1.00 56.19  ? 85  SER B O   1 
ATOM 3816 C CB  . SER B 2 87  ? -12.357 10.340  -9.542  1.00 47.77  ? 85  SER B CB  1 
ATOM 3817 O OG  . SER B 2 87  ? -11.196 10.919  -8.976  1.00 48.03  ? 85  SER B OG  1 
ATOM 3818 N N   . LEU B 2 88  ? -14.894 7.864   -8.374  1.00 57.04  ? 86  LEU B N   1 
ATOM 3819 C CA  . LEU B 2 88  ? -15.854 6.894   -8.879  1.00 54.96  ? 86  LEU B CA  1 
ATOM 3820 C C   . LEU B 2 88  ? -17.136 7.583   -9.333  1.00 58.70  ? 86  LEU B C   1 
ATOM 3821 O O   . LEU B 2 88  ? -17.638 8.496   -8.672  1.00 57.90  ? 86  LEU B O   1 
ATOM 3822 C CB  . LEU B 2 88  ? -16.167 5.853   -7.804  1.00 51.55  ? 86  LEU B CB  1 
ATOM 3823 C CG  . LEU B 2 88  ? -15.041 4.859   -7.507  1.00 51.13  ? 86  LEU B CG  1 
ATOM 3824 C CD1 . LEU B 2 88  ? -15.394 3.963   -6.330  1.00 48.54  ? 86  LEU B CD1 1 
ATOM 3825 C CD2 . LEU B 2 88  ? -14.733 4.026   -8.739  1.00 52.06  ? 86  LEU B CD2 1 
ATOM 3826 N N   . ASN B 2 89  ? -17.656 7.143   -10.473 1.00 62.85  ? 87  ASN B N   1 
ATOM 3827 C CA  . ASN B 2 89  ? -18.930 7.586   -11.014 1.00 61.45  ? 87  ASN B CA  1 
ATOM 3828 C C   . ASN B 2 89  ? -19.835 6.380   -11.239 1.00 59.57  ? 87  ASN B C   1 
ATOM 3829 O O   . ASN B 2 89  ? -19.356 5.240   -11.295 1.00 55.59  ? 87  ASN B O   1 
ATOM 3830 C CB  . ASN B 2 89  ? -18.737 8.359   -12.330 1.00 59.04  ? 87  ASN B CB  1 
ATOM 3831 C CG  . ASN B 2 89  ? -17.676 7.746   -13.220 1.00 69.92  ? 87  ASN B CG  1 
ATOM 3832 O OD1 . ASN B 2 89  ? -17.877 6.681   -13.806 1.00 77.68  ? 87  ASN B OD1 1 
ATOM 3833 N ND2 . ASN B 2 89  ? -16.542 8.429   -13.343 1.00 65.98  ? 87  ASN B ND2 1 
ATOM 3834 N N   . PRO B 2 90  ? -21.152 6.588   -11.354 1.00 52.72  ? 88  PRO B N   1 
ATOM 3835 C CA  . PRO B 2 90  ? -22.063 5.442   -11.531 1.00 54.81  ? 88  PRO B CA  1 
ATOM 3836 C C   . PRO B 2 90  ? -21.753 4.577   -12.742 1.00 65.29  ? 88  PRO B C   1 
ATOM 3837 O O   . PRO B 2 90  ? -22.221 3.432   -12.797 1.00 66.68  ? 88  PRO B O   1 
ATOM 3838 C CB  . PRO B 2 90  ? -23.440 6.108   -11.661 1.00 50.47  ? 88  PRO B CB  1 
ATOM 3839 C CG  . PRO B 2 90  ? -23.302 7.387   -10.922 1.00 50.86  ? 88  PRO B CG  1 
ATOM 3840 C CD  . PRO B 2 90  ? -21.892 7.847   -11.155 1.00 51.50  ? 88  PRO B CD  1 
ATOM 3841 N N   . GLY B 2 91  ? -20.986 5.079   -13.711 1.00 67.25  ? 89  GLY B N   1 
ATOM 3842 C CA  . GLY B 2 91  ? -20.595 4.274   -14.855 1.00 61.34  ? 89  GLY B CA  1 
ATOM 3843 C C   . GLY B 2 91  ? -19.628 3.151   -14.537 1.00 62.07  ? 89  GLY B C   1 
ATOM 3844 O O   . GLY B 2 91  ? -19.418 2.281   -15.389 1.00 55.44  ? 89  GLY B O   1 
ATOM 3845 N N   . ASP B 2 92  ? -19.041 3.146   -13.342 1.00 68.66  ? 90  ASP B N   1 
ATOM 3846 C CA  . ASP B 2 92  ? -18.103 2.110   -12.935 1.00 69.83  ? 90  ASP B CA  1 
ATOM 3847 C C   . ASP B 2 92  ? -18.780 0.937   -12.236 1.00 69.31  ? 90  ASP B C   1 
ATOM 3848 O O   . ASP B 2 92  ? -18.085 0.060   -11.714 1.00 64.81  ? 90  ASP B O   1 
ATOM 3849 C CB  . ASP B 2 92  ? -17.027 2.705   -12.022 1.00 68.69  ? 90  ASP B CB  1 
ATOM 3850 C CG  . ASP B 2 92  ? -16.229 3.805   -12.698 1.00 68.27  ? 90  ASP B CG  1 
ATOM 3851 O OD1 . ASP B 2 92  ? -16.461 4.070   -13.898 1.00 69.11  ? 90  ASP B OD1 1 
ATOM 3852 O OD2 . ASP B 2 92  ? -15.369 4.410   -12.024 1.00 62.22  ? 90  ASP B OD2 1 
ATOM 3853 N N   . THR B 2 93  ? -20.112 0.902   -12.212 1.00 65.18  ? 91  THR B N   1 
ATOM 3854 C CA  . THR B 2 93  ? -20.853 -0.188  -11.580 1.00 56.98  ? 91  THR B CA  1 
ATOM 3855 C C   . THR B 2 93  ? -20.737 -1.433  -12.450 1.00 57.79  ? 91  THR B C   1 
ATOM 3856 O O   . THR B 2 93  ? -21.414 -1.559  -13.474 1.00 59.40  ? 91  THR B O   1 
ATOM 3857 C CB  . THR B 2 93  ? -22.312 0.201   -11.372 1.00 53.17  ? 91  THR B CB  1 
ATOM 3858 O OG1 . THR B 2 93  ? -22.386 1.380   -10.561 1.00 52.78  ? 91  THR B OG1 1 
ATOM 3859 C CG2 . THR B 2 93  ? -23.072 -0.928  -10.685 1.00 48.04  ? 91  THR B CG2 1 
ATOM 3860 N N   . ALA B 2 94  ? -19.878 -2.362  -12.040 1.00 57.25  ? 92  ALA B N   1 
ATOM 3861 C CA  . ALA B 2 94  ? -19.633 -3.579  -12.799 1.00 54.12  ? 92  ALA B CA  1 
ATOM 3862 C C   . ALA B 2 94  ? -18.983 -4.603  -11.881 1.00 55.59  ? 92  ALA B C   1 
ATOM 3863 O O   . ALA B 2 94  ? -18.625 -4.308  -10.738 1.00 54.30  ? 92  ALA B O   1 
ATOM 3864 C CB  . ALA B 2 94  ? -18.751 -3.306  -14.020 1.00 55.92  ? 92  ALA B CB  1 
ATOM 3865 N N   . VAL B 2 95  ? -18.833 -5.817  -12.403 1.00 57.15  ? 93  VAL B N   1 
ATOM 3866 C CA  . VAL B 2 95  ? -18.141 -6.890  -11.699 1.00 56.30  ? 93  VAL B CA  1 
ATOM 3867 C C   . VAL B 2 95  ? -16.684 -6.871  -12.150 1.00 56.16  ? 93  VAL B C   1 
ATOM 3868 O O   . VAL B 2 95  ? -16.383 -7.127  -13.318 1.00 58.23  ? 93  VAL B O   1 
ATOM 3869 C CB  . VAL B 2 95  ? -18.794 -8.251  -11.966 1.00 48.47  ? 93  VAL B CB  1 
ATOM 3870 C CG1 . VAL B 2 95  ? -17.939 -9.371  -11.396 1.00 47.87  ? 93  VAL B CG1 1 
ATOM 3871 C CG2 . VAL B 2 95  ? -20.195 -8.289  -11.377 1.00 45.64  ? 93  VAL B CG2 1 
ATOM 3872 N N   . TYR B 2 96  ? -15.781 -6.559  -11.223 1.00 53.62  ? 94  TYR B N   1 
ATOM 3873 C CA  . TYR B 2 96  ? -14.365 -6.417  -11.535 1.00 50.57  ? 94  TYR B CA  1 
ATOM 3874 C C   . TYR B 2 96  ? -13.641 -7.736  -11.295 1.00 52.52  ? 94  TYR B C   1 
ATOM 3875 O O   . TYR B 2 96  ? -13.777 -8.342  -10.227 1.00 54.70  ? 94  TYR B O   1 
ATOM 3876 C CB  . TYR B 2 96  ? -13.738 -5.303  -10.697 1.00 50.10  ? 94  TYR B CB  1 
ATOM 3877 C CG  . TYR B 2 96  ? -14.133 -3.909  -11.135 1.00 51.58  ? 94  TYR B CG  1 
ATOM 3878 C CD1 . TYR B 2 96  ? -15.434 -3.450  -10.970 1.00 49.83  ? 94  TYR B CD1 1 
ATOM 3879 C CD2 . TYR B 2 96  ? -13.206 -3.052  -11.715 1.00 51.56  ? 94  TYR B CD2 1 
ATOM 3880 C CE1 . TYR B 2 96  ? -15.800 -2.180  -11.371 1.00 51.46  ? 94  TYR B CE1 1 
ATOM 3881 C CE2 . TYR B 2 96  ? -13.564 -1.777  -12.116 1.00 47.92  ? 94  TYR B CE2 1 
ATOM 3882 C CZ  . TYR B 2 96  ? -14.862 -1.348  -11.942 1.00 49.54  ? 94  TYR B CZ  1 
ATOM 3883 O OH  . TYR B 2 96  ? -15.229 -0.083  -12.338 1.00 50.39  ? 94  TYR B OH  1 
ATOM 3884 N N   . SER B 2 97  ? -12.872 -8.175  -12.293 1.00 54.05  ? 95  SER B N   1 
ATOM 3885 C CA  . SER B 2 97  ? -12.148 -9.436  -12.242 1.00 51.84  ? 95  SER B CA  1 
ATOM 3886 C C   . SER B 2 97  ? -10.678 -9.202  -12.562 1.00 53.43  ? 95  SER B C   1 
ATOM 3887 O O   . SER B 2 97  ? -10.335 -8.360  -13.396 1.00 56.57  ? 95  SER B O   1 
ATOM 3888 C CB  . SER B 2 97  ? -12.720 -10.466 -13.236 1.00 51.62  ? 95  SER B CB  1 
ATOM 3889 O OG  . SER B 2 97  ? -14.117 -10.634 -13.076 1.00 53.72  ? 95  SER B OG  1 
ATOM 3890 N N   . CYS B 2 98  ? -9.815  -9.962  -11.896 1.00 56.18  ? 96  CYS B N   1 
ATOM 3891 C CA  . CYS B 2 98  ? -8.384  -9.948  -12.159 1.00 57.86  ? 96  CYS B CA  1 
ATOM 3892 C C   . CYS B 2 98  ? -7.994  -11.151 -13.012 1.00 56.07  ? 96  CYS B C   1 
ATOM 3893 O O   . CYS B 2 98  ? -8.613  -12.216 -12.938 1.00 57.07  ? 96  CYS B O   1 
ATOM 3894 C CB  . CYS B 2 98  ? -7.591  -9.945  -10.849 1.00 53.83  ? 96  CYS B CB  1 
ATOM 3895 S SG  . CYS B 2 98  ? -7.938  -11.359 -9.776  1.00 72.73  ? 96  CYS B SG  1 
ATOM 3896 N N   . ALA B 2 99  ? -6.962  -10.966 -13.833 1.00 51.75  ? 97  ALA B N   1 
ATOM 3897 C CA  . ALA B 2 99  ? -6.506  -11.991 -14.759 1.00 55.10  ? 97  ALA B CA  1 
ATOM 3898 C C   . ALA B 2 99  ? -4.990  -12.109 -14.700 1.00 56.13  ? 97  ALA B C   1 
ATOM 3899 O O   . ALA B 2 99  ? -4.284  -11.133 -14.431 1.00 53.56  ? 97  ALA B O   1 
ATOM 3900 C CB  . ALA B 2 99  ? -6.951  -11.687 -16.197 1.00 59.82  ? 97  ALA B CB  1 
ATOM 3901 N N   . ALA B 2 100 ? -4.498  -13.318 -14.959 1.00 54.93  ? 98  ALA B N   1 
ATOM 3902 C CA  . ALA B 2 100 ? -3.076  -13.624 -14.914 1.00 57.06  ? 98  ALA B CA  1 
ATOM 3903 C C   . ALA B 2 100 ? -2.633  -14.211 -16.246 1.00 57.42  ? 98  ALA B C   1 
ATOM 3904 O O   . ALA B 2 100 ? -3.369  -14.985 -16.869 1.00 54.77  ? 98  ALA B O   1 
ATOM 3905 C CB  . ALA B 2 100 ? -2.757  -14.605 -13.780 1.00 57.98  ? 98  ALA B CB  1 
ATOM 3906 N N   . THR B 2 101 ? -1.427  -13.847 -16.676 1.00 58.26  ? 99  THR B N   1 
ATOM 3907 C CA  . THR B 2 101 ? -0.891  -14.331 -17.941 1.00 58.43  ? 99  THR B CA  1 
ATOM 3908 C C   . THR B 2 101 ? 0.622   -14.164 -17.931 1.00 60.52  ? 99  THR B C   1 
ATOM 3909 O O   . THR B 2 101 ? 1.196   -13.552 -17.026 1.00 59.77  ? 99  THR B O   1 
ATOM 3910 C CB  . THR B 2 101 ? -1.511  -13.595 -19.134 1.00 57.22  ? 99  THR B CB  1 
ATOM 3911 O OG1 . THR B 2 101 ? -1.368  -14.391 -20.316 1.00 54.89  ? 99  THR B OG1 1 
ATOM 3912 C CG2 . THR B 2 101 ? -0.827  -12.252 -19.350 1.00 61.08  ? 99  THR B CG2 1 
ATOM 3913 N N   . LEU B 2 102 ? 1.269   -14.727 -18.973 1.00 60.47  ? 100 LEU B N   1 
ATOM 3914 C CA  . LEU B 2 102 ? 2.701   -14.700 -19.218 1.00 61.46  ? 100 LEU B CA  1 
ATOM 3915 C C   . LEU B 2 102 ? 3.054   -13.604 -20.217 1.00 62.29  ? 100 LEU B C   1 
ATOM 3916 O O   . LEU B 2 102 ? 2.241   -13.256 -21.079 1.00 58.45  ? 100 LEU B O   1 
ATOM 3917 C CB  . LEU B 2 102 ? 3.183   -16.052 -19.755 1.00 63.10  ? 100 LEU B CB  1 
ATOM 3918 C CG  . LEU B 2 102 ? 3.535   -17.149 -18.745 1.00 64.71  ? 100 LEU B CG  1 
ATOM 3919 C CD1 . LEU B 2 102 ? 4.611   -16.667 -17.787 1.00 66.23  ? 100 LEU B CD1 1 
ATOM 3920 C CD2 . LEU B 2 102 ? 2.307   -17.640 -17.986 1.00 66.23  ? 100 LEU B CD2 1 
ATOM 3921 N N   . PRO B 2 103 ? 4.259   -13.033 -20.124 1.00 68.66  ? 101 PRO B N   1 
ATOM 3922 C CA  . PRO B 2 103 ? 4.641   -11.984 -21.086 1.00 64.23  ? 101 PRO B CA  1 
ATOM 3923 C C   . PRO B 2 103 ? 4.690   -12.475 -22.522 1.00 64.95  ? 101 PRO B C   1 
ATOM 3924 O O   . PRO B 2 103 ? 4.476   -11.679 -23.446 1.00 61.14  ? 101 PRO B O   1 
ATOM 3925 C CB  . PRO B 2 103 ? 6.025   -11.525 -20.602 1.00 70.95  ? 101 PRO B CB  1 
ATOM 3926 C CG  . PRO B 2 103 ? 6.268   -12.183 -19.297 1.00 78.57  ? 101 PRO B CG  1 
ATOM 3927 C CD  . PRO B 2 103 ? 5.273   -13.268 -19.082 1.00 78.04  ? 101 PRO B CD  1 
ATOM 3928 N N   . ALA B 2 104 ? 4.974   -13.762 -22.740 1.00 65.13  ? 102 ALA B N   1 
ATOM 3929 C CA  . ALA B 2 104 ? 4.890   -14.322 -24.082 1.00 61.90  ? 102 ALA B CA  1 
ATOM 3930 C C   . ALA B 2 104 ? 3.471   -14.279 -24.626 1.00 61.95  ? 102 ALA B C   1 
ATOM 3931 O O   . ALA B 2 104 ? 3.283   -14.302 -25.848 1.00 61.79  ? 102 ALA B O   1 
ATOM 3932 C CB  . ALA B 2 104 ? 5.409   -15.761 -24.090 1.00 67.62  ? 102 ALA B CB  1 
ATOM 3933 N N   . TRP B 2 105 ? 2.469   -14.217 -23.748 1.00 61.04  ? 103 TRP B N   1 
ATOM 3934 C CA  . TRP B 2 105 ? 1.088   -14.079 -24.194 1.00 52.94  ? 103 TRP B CA  1 
ATOM 3935 C C   . TRP B 2 105 ? 0.760   -12.628 -24.529 1.00 54.91  ? 103 TRP B C   1 
ATOM 3936 O O   . TRP B 2 105 ? 0.235   -12.339 -25.605 1.00 57.99  ? 103 TRP B O   1 
ATOM 3937 C CB  . TRP B 2 105 ? 0.129   -14.606 -23.123 1.00 53.12  ? 103 TRP B CB  1 
ATOM 3938 C CG  . TRP B 2 105 ? 0.222   -16.087 -22.861 1.00 52.42  ? 103 TRP B CG  1 
ATOM 3939 C CD1 . TRP B 2 105 ? 1.349   -16.803 -22.569 1.00 56.42  ? 103 TRP B CD1 1 
ATOM 3940 C CD2 . TRP B 2 105 ? -0.862  -17.026 -22.841 1.00 53.00  ? 103 TRP B CD2 1 
ATOM 3941 N NE1 . TRP B 2 105 ? 1.035   -18.128 -22.382 1.00 55.79  ? 103 TRP B NE1 1 
ATOM 3942 C CE2 . TRP B 2 105 ? -0.315  -18.291 -22.542 1.00 55.14  ? 103 TRP B CE2 1 
ATOM 3943 C CE3 . TRP B 2 105 ? -2.240  -16.921 -23.053 1.00 52.37  ? 103 TRP B CE3 1 
ATOM 3944 C CZ2 . TRP B 2 105 ? -1.098  -19.441 -22.451 1.00 56.70  ? 103 TRP B CZ2 1 
ATOM 3945 C CZ3 . TRP B 2 105 ? -3.015  -18.065 -22.961 1.00 53.90  ? 103 TRP B CZ3 1 
ATOM 3946 C CH2 . TRP B 2 105 ? -2.442  -19.308 -22.663 1.00 56.06  ? 103 TRP B CH2 1 
ATOM 3947 N N   . THR B 2 106 ? 1.080   -11.697 -23.628 1.00 67.43  ? 104 THR B N   1 
ATOM 3948 C CA  . THR B 2 106 ? 0.629   -10.318 -23.803 1.00 59.82  ? 104 THR B CA  1 
ATOM 3949 C C   . THR B 2 106 ? 1.191   -9.678  -25.069 1.00 61.18  ? 104 THR B C   1 
ATOM 3950 O O   . THR B 2 106 ? 0.571   -8.761  -25.621 1.00 62.91  ? 104 THR B O   1 
ATOM 3951 C CB  . THR B 2 106 ? 0.995   -9.480  -22.576 1.00 60.64  ? 104 THR B CB  1 
ATOM 3952 O OG1 . THR B 2 106 ? 0.295   -8.230  -22.625 1.00 61.02  ? 104 THR B OG1 1 
ATOM 3953 C CG2 . THR B 2 106 ? 2.495   -9.219  -22.517 1.00 65.66  ? 104 THR B CG2 1 
ATOM 3954 N N   . GLY B 2 107 ? 2.340   -10.146 -25.552 1.00 62.65  ? 105 GLY B N   1 
ATOM 3955 C CA  . GLY B 2 107 ? 2.923   -9.551  -26.743 1.00 60.92  ? 105 GLY B CA  1 
ATOM 3956 C C   . GLY B 2 107 ? 3.278   -8.093  -26.525 1.00 61.43  ? 105 GLY B C   1 
ATOM 3957 O O   . GLY B 2 107 ? 3.773   -7.698  -25.463 1.00 64.96  ? 105 GLY B O   1 
ATOM 3958 N N   . ILE B 2 108 ? 3.016   -7.276  -27.542 1.00 65.47  ? 106 ILE B N   1 
ATOM 3959 C CA  . ILE B 2 108 ? 3.277   -5.846  -27.489 1.00 66.38  ? 106 ILE B CA  1 
ATOM 3960 C C   . ILE B 2 108 ? 1.986   -5.035  -27.500 1.00 69.80  ? 106 ILE B C   1 
ATOM 3961 O O   . ILE B 2 108 ? 1.886   -4.017  -26.810 1.00 72.51  ? 106 ILE B O   1 
ATOM 3962 C CB  . ILE B 2 108 ? 4.207   -5.411  -28.643 1.00 66.63  ? 106 ILE B CB  1 
ATOM 3963 C CG1 . ILE B 2 108 ? 5.366   -6.398  -28.804 1.00 68.44  ? 106 ILE B CG1 1 
ATOM 3964 C CG2 . ILE B 2 108 ? 4.720   -3.997  -28.412 1.00 80.89  ? 106 ILE B CG2 1 
ATOM 3965 C CD1 . ILE B 2 108 ? 6.480   -5.895  -29.702 1.00 67.05  ? 106 ILE B CD1 1 
ATOM 3966 N N   . ILE B 2 109 ? 0.989   -5.466  -28.273 1.00 59.41  ? 107 ILE B N   1 
ATOM 3967 C CA  . ILE B 2 109 ? -0.276  -4.754  -28.385 1.00 57.04  ? 107 ILE B CA  1 
ATOM 3968 C C   . ILE B 2 109 ? -1.462  -5.619  -27.974 1.00 54.58  ? 107 ILE B C   1 
ATOM 3969 O O   . ILE B 2 109 ? -2.609  -5.238  -28.203 1.00 58.77  ? 107 ILE B O   1 
ATOM 3970 C CB  . ILE B 2 109 ? -0.479  -4.193  -29.808 1.00 66.58  ? 107 ILE B CB  1 
ATOM 3971 C CG1 . ILE B 2 109 ? -0.077  -5.225  -30.863 1.00 62.44  ? 107 ILE B CG1 1 
ATOM 3972 C CG2 . ILE B 2 109 ? 0.318   -2.913  -29.996 1.00 65.97  ? 107 ILE B CG2 1 
ATOM 3973 C CD1 . ILE B 2 109 ? -0.702  -4.980  -32.220 1.00 65.82  ? 107 ILE B CD1 1 
ATOM 3974 N N   . GLY B 2 110 ? -1.211  -6.773  -27.360 1.00 53.03  ? 108 GLY B N   1 
ATOM 3975 C CA  . GLY B 2 110 ? -2.288  -7.663  -26.971 1.00 51.57  ? 108 GLY B CA  1 
ATOM 3976 C C   . GLY B 2 110 ? -2.542  -7.710  -25.478 1.00 62.18  ? 108 GLY B C   1 
ATOM 3977 O O   . GLY B 2 110 ? -3.039  -8.715  -24.961 1.00 65.21  ? 108 GLY B O   1 
ATOM 3978 N N   . GLY B 2 111 ? -2.211  -6.624  -24.773 1.00 60.71  ? 109 GLY B N   1 
ATOM 3979 C CA  . GLY B 2 111 ? -2.397  -6.584  -23.333 1.00 54.83  ? 109 GLY B CA  1 
ATOM 3980 C C   . GLY B 2 111 ? -3.804  -6.259  -22.881 1.00 53.91  ? 109 GLY B C   1 
ATOM 3981 O O   . GLY B 2 111 ? -4.120  -6.445  -21.702 1.00 56.35  ? 109 GLY B O   1 
ATOM 3982 N N   . ARG B 2 112 ? -4.654  -5.777  -23.786 1.00 52.78  ? 110 ARG B N   1 
ATOM 3983 C CA  . ARG B 2 112 ? -6.031  -5.438  -23.453 1.00 51.82  ? 110 ARG B CA  1 
ATOM 3984 C C   . ARG B 2 112 ? -7.035  -6.489  -23.906 1.00 51.60  ? 110 ARG B C   1 
ATOM 3985 O O   . ARG B 2 112 ? -8.222  -6.364  -23.586 1.00 55.89  ? 110 ARG B O   1 
ATOM 3986 C CB  . ARG B 2 112 ? -6.409  -4.082  -24.065 1.00 54.01  ? 110 ARG B CB  1 
ATOM 3987 C CG  . ARG B 2 112 ? -5.452  -2.950  -23.719 1.00 50.34  ? 110 ARG B CG  1 
ATOM 3988 C CD  . ARG B 2 112 ? -5.831  -1.672  -24.446 1.00 49.84  ? 110 ARG B CD  1 
ATOM 3989 N NE  . ARG B 2 112 ? -4.996  -0.548  -24.041 1.00 50.15  ? 110 ARG B NE  1 
ATOM 3990 C CZ  . ARG B 2 112 ? -5.458  0.581   -23.523 1.00 50.41  ? 110 ARG B CZ  1 
ATOM 3991 N NH1 . ARG B 2 112 ? -6.753  0.773   -23.328 1.00 54.02  ? 110 ARG B NH1 1 
ATOM 3992 N NH2 . ARG B 2 112 ? -4.601  1.542   -23.190 1.00 52.98  ? 110 ARG B NH2 1 
ATOM 3993 N N   . ARG B 2 113 ? -6.599  -7.515  -24.632 1.00 55.91  ? 111 ARG B N   1 
ATOM 3994 C CA  . ARG B 2 113 ? -7.516  -8.530  -25.136 1.00 63.86  ? 111 ARG B CA  1 
ATOM 3995 C C   . ARG B 2 113 ? -7.737  -9.599  -24.076 1.00 63.93  ? 111 ARG B C   1 
ATOM 3996 O O   . ARG B 2 113 ? -6.761  -10.199 -23.605 1.00 60.60  ? 111 ARG B O   1 
ATOM 3997 C CB  . ARG B 2 113 ? -6.977  -9.158  -26.409 1.00 56.29  ? 111 ARG B CB  1 
ATOM 3998 C CG  . ARG B 2 113 ? -7.288  -8.363  -27.667 1.00 53.03  ? 111 ARG B CG  1 
ATOM 3999 C CD  . ARG B 2 113 ? -6.140  -8.434  -28.657 1.00 62.26  ? 111 ARG B CD  1 
ATOM 4000 N NE  . ARG B 2 113 ? -6.180  -7.341  -29.621 1.00 68.12  ? 111 ARG B NE  1 
ATOM 4001 C CZ  . ARG B 2 113 ? -5.199  -7.053  -30.466 1.00 66.14  ? 111 ARG B CZ  1 
ATOM 4002 N NH1 . ARG B 2 113 ? -4.079  -7.757  -30.490 1.00 62.05  ? 111 ARG B NH1 1 
ATOM 4003 N NH2 . ARG B 2 113 ? -5.342  -6.029  -31.302 1.00 72.52  ? 111 ARG B NH2 1 
ATOM 4004 N N   . PRO B 2 114 ? -8.983  -9.871  -23.676 1.00 57.92  ? 112 PRO B N   1 
ATOM 4005 C CA  . PRO B 2 114 ? -9.210  -10.873 -22.622 1.00 52.32  ? 112 PRO B CA  1 
ATOM 4006 C C   . PRO B 2 114 ? -8.811  -12.279 -23.030 1.00 57.23  ? 112 PRO B C   1 
ATOM 4007 O O   . PRO B 2 114 ? -8.466  -13.087 -22.158 1.00 56.26  ? 112 PRO B O   1 
ATOM 4008 C CB  . PRO B 2 114 ? -10.720 -10.774 -22.357 1.00 58.87  ? 112 PRO B CB  1 
ATOM 4009 C CG  . PRO B 2 114 ? -11.156 -9.481  -22.985 1.00 61.93  ? 112 PRO B CG  1 
ATOM 4010 C CD  . PRO B 2 114 ? -10.238 -9.258  -24.138 1.00 58.89  ? 112 PRO B CD  1 
ATOM 4011 N N   . GLY B 2 115 ? -8.848  -12.599 -24.324 1.00 64.36  ? 113 GLY B N   1 
ATOM 4012 C CA  . GLY B 2 115 ? -8.481  -13.926 -24.786 1.00 57.70  ? 113 GLY B CA  1 
ATOM 4013 C C   . GLY B 2 115 ? -7.029  -14.286 -24.564 1.00 55.35  ? 113 GLY B C   1 
ATOM 4014 O O   . GLY B 2 115 ? -6.663  -15.453 -24.743 1.00 52.38  ? 113 GLY B O   1 
ATOM 4015 N N   . ASN B 2 116 ? -6.200  -13.320 -24.178 1.00 64.19  ? 114 ASN B N   1 
ATOM 4016 C CA  . ASN B 2 116 ? -4.785  -13.558 -23.951 1.00 60.08  ? 114 ASN B CA  1 
ATOM 4017 C C   . ASN B 2 116 ? -4.463  -13.765 -22.481 1.00 57.58  ? 114 ASN B C   1 
ATOM 4018 O O   . ASN B 2 116 ? -3.286  -13.761 -22.108 1.00 55.80  ? 114 ASN B O   1 
ATOM 4019 C CB  . ASN B 2 116 ? -3.962  -12.401 -24.510 1.00 54.30  ? 114 ASN B CB  1 
ATOM 4020 C CG  . ASN B 2 116 ? -3.412  -12.706 -25.877 1.00 60.15  ? 114 ASN B CG  1 
ATOM 4021 O OD1 . ASN B 2 116 ? -2.211  -12.834 -26.064 1.00 62.56  ? 114 ASN B OD1 1 
ATOM 4022 N ND2 . ASN B 2 116 ? -4.301  -12.833 -26.849 1.00 69.82  ? 114 ASN B ND2 1 
ATOM 4023 N N   . TYR B 2 117 ? -5.479  -13.936 -21.640 1.00 50.05  ? 115 TYR B N   1 
ATOM 4024 C CA  . TYR B 2 117 ? -5.287  -14.221 -20.219 1.00 57.62  ? 115 TYR B CA  1 
ATOM 4025 C C   . TYR B 2 117 ? -5.946  -15.557 -19.907 1.00 57.34  ? 115 TYR B C   1 
ATOM 4026 O O   . TYR B 2 117 ? -7.184  -15.637 -19.815 1.00 59.51  ? 115 TYR B O   1 
ATOM 4027 C CB  . TYR B 2 117 ? -5.869  -13.107 -19.350 1.00 57.85  ? 115 TYR B CB  1 
ATOM 4028 C CG  . TYR B 2 117 ? -5.136  -11.785 -19.473 1.00 54.03  ? 115 TYR B CG  1 
ATOM 4029 C CD1 . TYR B 2 117 ? -5.363  -10.942 -20.554 1.00 54.50  ? 115 TYR B CD1 1 
ATOM 4030 C CD2 . TYR B 2 117 ? -4.221  -11.379 -18.510 1.00 52.97  ? 115 TYR B CD2 1 
ATOM 4031 C CE1 . TYR B 2 117 ? -4.698  -9.736  -20.674 1.00 53.37  ? 115 TYR B CE1 1 
ATOM 4032 C CE2 . TYR B 2 117 ? -3.551  -10.172 -18.622 1.00 55.51  ? 115 TYR B CE2 1 
ATOM 4033 C CZ  . TYR B 2 117 ? -3.793  -9.355  -19.708 1.00 57.72  ? 115 TYR B CZ  1 
ATOM 4034 O OH  . TYR B 2 117 ? -3.134  -8.151  -19.833 1.00 55.52  ? 115 TYR B OH  1 
ATOM 4035 N N   . PRO B 2 118 ? -5.171  -16.634 -19.745 1.00 54.61  ? 116 PRO B N   1 
ATOM 4036 C CA  . PRO B 2 118 ? -5.793  -17.955 -19.562 1.00 57.09  ? 116 PRO B CA  1 
ATOM 4037 C C   . PRO B 2 118 ? -6.459  -18.139 -18.209 1.00 60.82  ? 116 PRO B C   1 
ATOM 4038 O O   . PRO B 2 118 ? -7.440  -18.888 -18.116 1.00 60.24  ? 116 PRO B O   1 
ATOM 4039 C CB  . PRO B 2 118 ? -4.615  -18.921 -19.748 1.00 52.90  ? 116 PRO B CB  1 
ATOM 4040 C CG  . PRO B 2 118 ? -3.415  -18.128 -19.348 1.00 50.84  ? 116 PRO B CG  1 
ATOM 4041 C CD  . PRO B 2 118 ? -3.699  -16.700 -19.737 1.00 48.87  ? 116 PRO B CD  1 
ATOM 4042 N N   . TYR B 2 119 ? -5.968  -17.485 -17.161 1.00 60.17  ? 117 TYR B N   1 
ATOM 4043 C CA  . TYR B 2 119 ? -6.471  -17.671 -15.807 1.00 58.09  ? 117 TYR B CA  1 
ATOM 4044 C C   . TYR B 2 119 ? -7.241  -16.433 -15.370 1.00 63.46  ? 117 TYR B C   1 
ATOM 4045 O O   . TYR B 2 119 ? -6.746  -15.308 -15.501 1.00 60.82  ? 117 TYR B O   1 
ATOM 4046 C CB  . TYR B 2 119 ? -5.323  -17.957 -14.837 1.00 57.97  ? 117 TYR B CB  1 
ATOM 4047 C CG  . TYR B 2 119 ? -4.371  -19.027 -15.325 1.00 62.29  ? 117 TYR B CG  1 
ATOM 4048 C CD1 . TYR B 2 119 ? -4.793  -20.341 -15.486 1.00 62.25  ? 117 TYR B CD1 1 
ATOM 4049 C CD2 . TYR B 2 119 ? -3.051  -18.721 -15.633 1.00 59.63  ? 117 TYR B CD2 1 
ATOM 4050 C CE1 . TYR B 2 119 ? -3.927  -21.321 -15.933 1.00 58.36  ? 117 TYR B CE1 1 
ATOM 4051 C CE2 . TYR B 2 119 ? -2.178  -19.695 -16.082 1.00 54.87  ? 117 TYR B CE2 1 
ATOM 4052 C CZ  . TYR B 2 119 ? -2.621  -20.993 -16.229 1.00 56.43  ? 117 TYR B CZ  1 
ATOM 4053 O OH  . TYR B 2 119 ? -1.757  -21.966 -16.675 1.00 59.40  ? 117 TYR B OH  1 
ATOM 4054 N N   . TRP B 2 120 ? -8.444  -16.647 -14.843 1.00 63.79  ? 118 TRP B N   1 
ATOM 4055 C CA  . TRP B 2 120 ? -9.349  -15.569 -14.479 1.00 57.49  ? 118 TRP B CA  1 
ATOM 4056 C C   . TRP B 2 120 ? -9.871  -15.778 -13.067 1.00 60.69  ? 118 TRP B C   1 
ATOM 4057 O O   . TRP B 2 120 ? -9.864  -16.891 -12.535 1.00 69.15  ? 118 TRP B O   1 
ATOM 4058 C CB  . TRP B 2 120 ? -10.531 -15.481 -15.449 1.00 63.32  ? 118 TRP B CB  1 
ATOM 4059 C CG  . TRP B 2 120 ? -10.149 -14.986 -16.796 1.00 65.43  ? 118 TRP B CG  1 
ATOM 4060 C CD1 . TRP B 2 120 ? -9.649  -15.722 -17.828 1.00 57.21  ? 118 TRP B CD1 1 
ATOM 4061 C CD2 . TRP B 2 120 ? -10.230 -13.637 -17.264 1.00 66.83  ? 118 TRP B CD2 1 
ATOM 4062 N NE1 . TRP B 2 120 ? -9.414  -14.913 -18.913 1.00 61.83  ? 118 TRP B NE1 1 
ATOM 4063 C CE2 . TRP B 2 120 ? -9.764  -13.628 -18.592 1.00 61.42  ? 118 TRP B CE2 1 
ATOM 4064 C CE3 . TRP B 2 120 ? -10.654 -12.434 -16.689 1.00 62.66  ? 118 TRP B CE3 1 
ATOM 4065 C CZ2 . TRP B 2 120 ? -9.709  -12.465 -19.355 1.00 60.29  ? 118 TRP B CZ2 1 
ATOM 4066 C CZ3 . TRP B 2 120 ? -10.599 -11.282 -17.447 1.00 63.64  ? 118 TRP B CZ3 1 
ATOM 4067 C CH2 . TRP B 2 120 ? -10.131 -11.305 -18.766 1.00 63.21  ? 118 TRP B CH2 1 
ATOM 4068 N N   . GLY B 2 121 ? -10.333 -14.684 -12.465 1.00 60.72  ? 119 GLY B N   1 
ATOM 4069 C CA  . GLY B 2 121 ? -10.976 -14.732 -11.173 1.00 55.97  ? 119 GLY B CA  1 
ATOM 4070 C C   . GLY B 2 121 ? -12.491 -14.747 -11.299 1.00 55.50  ? 119 GLY B C   1 
ATOM 4071 O O   . GLY B 2 121 ? -13.063 -14.496 -12.356 1.00 61.82  ? 119 GLY B O   1 
ATOM 4072 N N   . GLN B 2 122 ? -13.141 -15.055 -10.176 1.00 63.17  ? 120 GLN B N   1 
ATOM 4073 C CA  . GLN B 2 122 ? -14.596 -15.129 -10.166 1.00 57.09  ? 120 GLN B CA  1 
ATOM 4074 C C   . GLN B 2 122 ? -15.222 -13.752 -10.345 1.00 54.63  ? 120 GLN B C   1 
ATOM 4075 O O   . GLN B 2 122 ? -16.283 -13.630 -10.967 1.00 58.04  ? 120 GLN B O   1 
ATOM 4076 C CB  . GLN B 2 122 ? -15.074 -15.767 -8.864  1.00 59.55  ? 120 GLN B CB  1 
ATOM 4077 C CG  . GLN B 2 122 ? -16.230 -16.736 -9.027  1.00 63.84  ? 120 GLN B CG  1 
ATOM 4078 C CD  . GLN B 2 122 ? -17.149 -16.757 -7.825  1.00 64.66  ? 120 GLN B CD  1 
ATOM 4079 O OE1 . GLN B 2 122 ? -16.855 -16.157 -6.790  1.00 63.94  ? 120 GLN B OE1 1 
ATOM 4080 N NE2 . GLN B 2 122 ? -18.255 -17.481 -7.943  1.00 65.47  ? 120 GLN B NE2 1 
ATOM 4081 N N   . GLY B 2 123 ? -14.583 -12.710 -9.817  1.00 54.22  ? 121 GLY B N   1 
ATOM 4082 C CA  . GLY B 2 123 ? -15.093 -11.360 -9.949  1.00 55.20  ? 121 GLY B CA  1 
ATOM 4083 C C   . GLY B 2 123 ? -15.823 -10.856 -8.721  1.00 58.03  ? 121 GLY B C   1 
ATOM 4084 O O   . GLY B 2 123 ? -16.661 -11.563 -8.152  1.00 63.38  ? 121 GLY B O   1 
ATOM 4085 N N   . THR B 2 124 ? -15.513 -9.633  -8.304  1.00 51.40  ? 122 THR B N   1 
ATOM 4086 C CA  . THR B 2 124 ? -16.188 -8.983  -7.193  1.00 55.43  ? 122 THR B CA  1 
ATOM 4087 C C   . THR B 2 124 ? -17.000 -7.802  -7.711  1.00 57.45  ? 122 THR B C   1 
ATOM 4088 O O   . THR B 2 124 ? -16.684 -7.221  -8.754  1.00 58.59  ? 122 THR B O   1 
ATOM 4089 C CB  . THR B 2 124 ? -15.184 -8.519  -6.129  1.00 58.03  ? 122 THR B CB  1 
ATOM 4090 O OG1 . THR B 2 124 ? -15.882 -8.136  -4.938  1.00 62.25  ? 122 THR B OG1 1 
ATOM 4091 C CG2 . THR B 2 124 ? -14.358 -7.343  -6.636  1.00 51.24  ? 122 THR B CG2 1 
ATOM 4092 N N   . GLN B 2 125 ? -18.058 -7.458  -6.981  1.00 59.35  ? 123 GLN B N   1 
ATOM 4093 C CA  . GLN B 2 125 ? -18.980 -6.412  -7.404  1.00 56.53  ? 123 GLN B CA  1 
ATOM 4094 C C   . GLN B 2 125 ? -18.523 -5.052  -6.893  1.00 53.22  ? 123 GLN B C   1 
ATOM 4095 O O   . GLN B 2 125 ? -18.147 -4.912  -5.725  1.00 53.56  ? 123 GLN B O   1 
ATOM 4096 C CB  . GLN B 2 125 ? -20.396 -6.705  -6.908  1.00 56.02  ? 123 GLN B CB  1 
ATOM 4097 C CG  . GLN B 2 125 ? -21.357 -5.530  -7.018  1.00 59.57  ? 123 GLN B CG  1 
ATOM 4098 C CD  . GLN B 2 125 ? -21.879 -5.317  -8.428  1.00 59.69  ? 123 GLN B CD  1 
ATOM 4099 O OE1 . GLN B 2 125 ? -21.418 -5.948  -9.380  1.00 60.45  ? 123 GLN B OE1 1 
ATOM 4100 N NE2 . GLN B 2 125 ? -22.848 -4.416  -8.567  1.00 55.00  ? 123 GLN B NE2 1 
ATOM 4101 N N   . VAL B 2 126 ? -18.564 -4.055  -7.772  1.00 50.25  ? 124 VAL B N   1 
ATOM 4102 C CA  . VAL B 2 126 ? -18.333 -2.662  -7.412  1.00 52.84  ? 124 VAL B CA  1 
ATOM 4103 C C   . VAL B 2 126 ? -19.544 -1.870  -7.883  1.00 54.75  ? 124 VAL B C   1 
ATOM 4104 O O   . VAL B 2 126 ? -19.864 -1.873  -9.078  1.00 54.62  ? 124 VAL B O   1 
ATOM 4105 C CB  . VAL B 2 126 ? -17.039 -2.114  -8.034  1.00 53.20  ? 124 VAL B CB  1 
ATOM 4106 C CG1 . VAL B 2 126 ? -17.022 -0.589  -7.983  1.00 49.04  ? 124 VAL B CG1 1 
ATOM 4107 C CG2 . VAL B 2 126 ? -15.825 -2.701  -7.333  1.00 54.36  ? 124 VAL B CG2 1 
ATOM 4108 N N   . THR B 2 127 ? -20.223 -1.208  -6.949  1.00 54.66  ? 125 THR B N   1 
ATOM 4109 C CA  . THR B 2 127 ? -21.441 -0.462  -7.237  1.00 55.45  ? 125 THR B CA  1 
ATOM 4110 C C   . THR B 2 127 ? -21.273 0.981   -6.785  1.00 55.03  ? 125 THR B C   1 
ATOM 4111 O O   . THR B 2 127 ? -20.905 1.235   -5.633  1.00 52.46  ? 125 THR B O   1 
ATOM 4112 C CB  . THR B 2 127 ? -22.653 -1.094  -6.543  1.00 52.65  ? 125 THR B CB  1 
ATOM 4113 O OG1 . THR B 2 127 ? -22.786 -2.460  -6.956  1.00 51.40  ? 125 THR B OG1 1 
ATOM 4114 C CG2 . THR B 2 127 ? -23.925 -0.336  -6.889  1.00 49.01  ? 125 THR B CG2 1 
ATOM 4115 N N   . VAL B 2 128 ? -21.541 1.918   -7.691  1.00 55.33  ? 126 VAL B N   1 
ATOM 4116 C CA  . VAL B 2 128 ? -21.453 3.347   -7.414  1.00 55.01  ? 126 VAL B CA  1 
ATOM 4117 C C   . VAL B 2 128 ? -22.856 3.933   -7.483  1.00 60.80  ? 126 VAL B C   1 
ATOM 4118 O O   . VAL B 2 128 ? -23.561 3.756   -8.484  1.00 70.19  ? 126 VAL B O   1 
ATOM 4119 C CB  . VAL B 2 128 ? -20.510 4.059   -8.399  1.00 54.62  ? 126 VAL B CB  1 
ATOM 4120 C CG1 . VAL B 2 128 ? -20.067 5.400   -7.836  1.00 54.79  ? 126 VAL B CG1 1 
ATOM 4121 C CG2 . VAL B 2 128 ? -19.306 3.183   -8.710  1.00 57.43  ? 126 VAL B CG2 1 
ATOM 4122 N N   . SER B 2 129 ? -23.259 4.629   -6.425  1.00 70.55  ? 127 SER B N   1 
ATOM 4123 C CA  . SER B 2 129 ? -24.588 5.232   -6.367  1.00 74.72  ? 127 SER B CA  1 
ATOM 4124 C C   . SER B 2 129 ? -24.717 6.406   -7.333  1.00 75.45  ? 127 SER B C   1 
ATOM 4125 O O   . SER B 2 129 ? -23.732 7.056   -7.684  1.00 73.96  ? 127 SER B O   1 
ATOM 4126 C CB  . SER B 2 129 ? -24.905 5.694   -4.944  1.00 74.33  ? 127 SER B CB  1 
ATOM 4127 O OG  . SER B 2 129 ? -24.427 4.763   -3.991  1.00 77.93  ? 127 SER B OG  1 
ATOM 4128 N N   . ALA C 3 2   ? 13.963  -65.250 -22.480 1.00 84.96  ? 0   ALA C N   1 
ATOM 4129 C CA  . ALA C 3 2   ? 14.608  -65.532 -21.203 1.00 87.46  ? 0   ALA C CA  1 
ATOM 4130 C C   . ALA C 3 2   ? 13.708  -65.148 -20.029 1.00 91.53  ? 0   ALA C C   1 
ATOM 4131 O O   . ALA C 3 2   ? 12.580  -65.630 -19.923 1.00 93.29  ? 0   ALA C O   1 
ATOM 4132 C CB  . ALA C 3 2   ? 15.941  -64.808 -21.112 1.00 84.39  ? 0   ALA C CB  1 
ATOM 4133 N N   . GLN C 3 3   ? 14.205  -64.279 -19.153 1.00 90.07  ? 1   GLN C N   1 
ATOM 4134 C CA  . GLN C 3 3   ? 13.502  -63.952 -17.919 1.00 81.13  ? 1   GLN C CA  1 
ATOM 4135 C C   . GLN C 3 3   ? 14.009  -62.614 -17.392 1.00 78.11  ? 1   GLN C C   1 
ATOM 4136 O O   . GLN C 3 3   ? 14.827  -61.941 -18.026 1.00 78.18  ? 1   GLN C O   1 
ATOM 4137 C CB  . GLN C 3 3   ? 13.691  -65.056 -16.875 1.00 82.11  ? 1   GLN C CB  1 
ATOM 4138 C CG  . GLN C 3 3   ? 15.091  -65.647 -16.854 1.00 81.14  ? 1   GLN C CG  1 
ATOM 4139 C CD  . GLN C 3 3   ? 16.063  -64.816 -16.038 1.00 95.48  ? 1   GLN C CD  1 
ATOM 4140 O OE1 . GLN C 3 3   ? 15.991  -64.780 -14.808 1.00 96.54  ? 1   GLN C OE1 1 
ATOM 4141 N NE2 . GLN C 3 3   ? 16.980  -64.141 -16.722 1.00 95.96  ? 1   GLN C NE2 1 
ATOM 4142 N N   . VAL C 3 4   ? 13.511  -62.238 -16.216 1.00 68.47  ? 2   VAL C N   1 
ATOM 4143 C CA  . VAL C 3 4   ? 13.980  -61.066 -15.485 1.00 65.32  ? 2   VAL C CA  1 
ATOM 4144 C C   . VAL C 3 4   ? 14.112  -61.434 -14.014 1.00 67.35  ? 2   VAL C C   1 
ATOM 4145 O O   . VAL C 3 4   ? 13.293  -62.186 -13.474 1.00 65.68  ? 2   VAL C O   1 
ATOM 4146 C CB  . VAL C 3 4   ? 13.038  -59.855 -15.656 1.00 61.21  ? 2   VAL C CB  1 
ATOM 4147 C CG1 . VAL C 3 4   ? 13.155  -59.283 -17.057 1.00 63.41  ? 2   VAL C CG1 1 
ATOM 4148 C CG2 . VAL C 3 4   ? 11.602  -60.248 -15.350 1.00 59.48  ? 2   VAL C CG2 1 
ATOM 4149 N N   . GLN C 3 5   ? 15.148  -60.906 -13.367 1.00 68.72  ? 3   GLN C N   1 
ATOM 4150 C CA  . GLN C 3 5   ? 15.388  -61.130 -11.948 1.00 59.31  ? 3   GLN C CA  1 
ATOM 4151 C C   . GLN C 3 5   ? 14.998  -59.881 -11.171 1.00 59.38  ? 3   GLN C C   1 
ATOM 4152 O O   . GLN C 3 5   ? 15.429  -58.773 -11.509 1.00 59.00  ? 3   GLN C O   1 
ATOM 4153 C CB  . GLN C 3 5   ? 16.853  -61.479 -11.683 1.00 61.03  ? 3   GLN C CB  1 
ATOM 4154 C CG  . GLN C 3 5   ? 17.205  -62.933 -11.956 1.00 74.38  ? 3   GLN C CG  1 
ATOM 4155 C CD  . GLN C 3 5   ? 17.082  -63.810 -10.723 1.00 79.62  ? 3   GLN C CD  1 
ATOM 4156 O OE1 . GLN C 3 5   ? 16.349  -64.799 -10.724 1.00 79.16  ? 3   GLN C OE1 1 
ATOM 4157 N NE2 . GLN C 3 5   ? 17.801  -63.450 -9.662  1.00 75.18  ? 3   GLN C NE2 1 
ATOM 4158 N N   . LEU C 3 6   ? 14.190  -60.063 -10.132 1.00 59.98  ? 4   LEU C N   1 
ATOM 4159 C CA  . LEU C 3 6   ? 13.664  -58.964 -9.335  1.00 61.81  ? 4   LEU C CA  1 
ATOM 4160 C C   . LEU C 3 6   ? 14.298  -59.004 -7.951  1.00 64.77  ? 4   LEU C C   1 
ATOM 4161 O O   . LEU C 3 6   ? 14.175  -60.006 -7.237  1.00 66.57  ? 4   LEU C O   1 
ATOM 4162 C CB  . LEU C 3 6   ? 12.141  -59.049 -9.240  1.00 61.73  ? 4   LEU C CB  1 
ATOM 4163 C CG  . LEU C 3 6   ? 11.401  -59.051 -10.579 1.00 57.94  ? 4   LEU C CG  1 
ATOM 4164 C CD1 . LEU C 3 6   ? 9.896   -59.061 -10.363 1.00 58.57  ? 4   LEU C CD1 1 
ATOM 4165 C CD2 . LEU C 3 6   ? 11.817  -57.857 -11.425 1.00 56.73  ? 4   LEU C CD2 1 
ATOM 4166 N N   . VAL C 3 7   ? 14.976  -57.920 -7.580  1.00 66.11  ? 5   VAL C N   1 
ATOM 4167 C CA  . VAL C 3 7   ? 15.615  -57.777 -6.277  1.00 67.65  ? 5   VAL C CA  1 
ATOM 4168 C C   . VAL C 3 7   ? 14.947  -56.618 -5.552  1.00 66.17  ? 5   VAL C C   1 
ATOM 4169 O O   . VAL C 3 7   ? 15.003  -55.473 -6.018  1.00 66.88  ? 5   VAL C O   1 
ATOM 4170 C CB  . VAL C 3 7   ? 17.129  -57.543 -6.402  1.00 60.41  ? 5   VAL C CB  1 
ATOM 4171 C CG1 . VAL C 3 7   ? 17.822  -57.822 -5.077  1.00 69.57  ? 5   VAL C CG1 1 
ATOM 4172 C CG2 . VAL C 3 7   ? 17.715  -58.411 -7.505  1.00 56.79  ? 5   VAL C CG2 1 
ATOM 4173 N N   . GLU C 3 8   ? 14.320  -56.910 -4.417  1.00 69.35  ? 6   GLU C N   1 
ATOM 4174 C CA  . GLU C 3 8   ? 13.622  -55.899 -3.638  1.00 79.32  ? 6   GLU C CA  1 
ATOM 4175 C C   . GLU C 3 8   ? 14.568  -55.221 -2.654  1.00 86.71  ? 6   GLU C C   1 
ATOM 4176 O O   . GLU C 3 8   ? 15.573  -55.797 -2.227  1.00 88.51  ? 6   GLU C O   1 
ATOM 4177 C CB  . GLU C 3 8   ? 12.446  -56.516 -2.881  1.00 80.61  ? 6   GLU C CB  1 
ATOM 4178 C CG  . GLU C 3 8   ? 11.194  -56.692 -3.715  1.00 72.77  ? 6   GLU C CG  1 
ATOM 4179 C CD  . GLU C 3 8   ? 11.011  -58.120 -4.182  1.00 78.67  ? 6   GLU C CD  1 
ATOM 4180 O OE1 . GLU C 3 8   ? 11.971  -58.690 -4.742  1.00 83.97  ? 6   GLU C OE1 1 
ATOM 4181 O OE2 . GLU C 3 8   ? 9.912   -58.676 -3.982  1.00 77.81  ? 6   GLU C OE2 1 
ATOM 4182 N N   . SER C 3 9   ? 14.229  -53.985 -2.290  1.00 67.47  ? 7   SER C N   1 
ATOM 4183 C CA  . SER C 3 9   ? 15.041  -53.201 -1.371  1.00 67.35  ? 7   SER C CA  1 
ATOM 4184 C C   . SER C 3 9   ? 14.145  -52.235 -0.609  1.00 65.06  ? 7   SER C C   1 
ATOM 4185 O O   . SER C 3 9   ? 13.201  -51.677 -1.174  1.00 63.40  ? 7   SER C O   1 
ATOM 4186 C CB  . SER C 3 9   ? 16.139  -52.432 -2.116  1.00 64.45  ? 7   SER C CB  1 
ATOM 4187 O OG  . SER C 3 9   ? 17.245  -52.169 -1.271  1.00 62.85  ? 7   SER C OG  1 
ATOM 4188 N N   . GLY C 3 10  ? 14.449  -52.041 0.675   1.00 67.96  ? 8   GLY C N   1 
ATOM 4189 C CA  . GLY C 3 10  ? 13.699  -51.139 1.523   1.00 62.46  ? 8   GLY C CA  1 
ATOM 4190 C C   . GLY C 3 10  ? 13.113  -51.856 2.727   1.00 70.17  ? 8   GLY C C   1 
ATOM 4191 O O   . GLY C 3 10  ? 13.648  -52.876 3.186   1.00 75.87  ? 8   GLY C O   1 
ATOM 4192 N N   . GLY C 3 11  ? 12.009  -51.315 3.233   1.00 69.19  ? 9   GLY C N   1 
ATOM 4193 C CA  . GLY C 3 11  ? 11.351  -51.881 4.391   1.00 69.01  ? 9   GLY C CA  1 
ATOM 4194 C C   . GLY C 3 11  ? 12.074  -51.554 5.683   1.00 74.13  ? 9   GLY C C   1 
ATOM 4195 O O   . GLY C 3 11  ? 13.132  -50.923 5.712   1.00 75.36  ? 9   GLY C O   1 
ATOM 4196 N N   . GLY C 3 12  ? 11.480  -52.005 6.779   1.00 77.02  ? 10  GLY C N   1 
ATOM 4197 C CA  . GLY C 3 12  ? 12.039  -51.817 8.096   1.00 76.62  ? 10  GLY C CA  1 
ATOM 4198 C C   . GLY C 3 12  ? 10.949  -51.520 9.099   1.00 77.39  ? 10  GLY C C   1 
ATOM 4199 O O   . GLY C 3 12  ? 9.759   -51.634 8.810   1.00 78.20  ? 10  GLY C O   1 
ATOM 4200 N N   . LEU C 3 13  ? 11.373  -51.131 10.299  1.00 78.21  ? 11  LEU C N   1 
ATOM 4201 C CA  . LEU C 3 13  ? 10.467  -50.809 11.399  1.00 78.25  ? 11  LEU C CA  1 
ATOM 4202 C C   . LEU C 3 13  ? 10.285  -49.296 11.443  1.00 85.54  ? 11  LEU C C   1 
ATOM 4203 O O   . LEU C 3 13  ? 11.119  -48.574 11.994  1.00 89.97  ? 11  LEU C O   1 
ATOM 4204 C CB  . LEU C 3 13  ? 11.008  -51.343 12.721  1.00 75.93  ? 11  LEU C CB  1 
ATOM 4205 C CG  . LEU C 3 13  ? 10.066  -51.277 13.925  1.00 72.11  ? 11  LEU C CG  1 
ATOM 4206 C CD1 . LEU C 3 13  ? 9.147   -52.489 13.965  1.00 71.15  ? 11  LEU C CD1 1 
ATOM 4207 C CD2 . LEU C 3 13  ? 10.861  -51.158 15.218  1.00 87.81  ? 11  LEU C CD2 1 
ATOM 4208 N N   . VAL C 3 14  ? 9.189   -48.819 10.864  1.00 80.00  ? 12  VAL C N   1 
ATOM 4209 C CA  . VAL C 3 14  ? 8.852   -47.406 10.884  1.00 85.91  ? 12  VAL C CA  1 
ATOM 4210 C C   . VAL C 3 14  ? 7.714   -47.190 11.878  1.00 88.61  ? 12  VAL C C   1 
ATOM 4211 O O   . VAL C 3 14  ? 7.142   -48.134 12.421  1.00 86.12  ? 12  VAL C O   1 
ATOM 4212 C CB  . VAL C 3 14  ? 8.482   -46.880 9.484   1.00 85.50  ? 12  VAL C CB  1 
ATOM 4213 C CG1 . VAL C 3 14  ? 9.710   -46.854 8.590   1.00 78.98  ? 12  VAL C CG1 1 
ATOM 4214 C CG2 . VAL C 3 14  ? 7.388   -47.738 8.868   1.00 80.51  ? 12  VAL C CG2 1 
ATOM 4215 N N   . GLN C 3 15  ? 7.392   -45.926 12.119  1.00 94.15  ? 13  GLN C N   1 
ATOM 4216 C CA  . GLN C 3 15  ? 6.306   -45.569 13.016  1.00 92.11  ? 13  GLN C CA  1 
ATOM 4217 C C   . GLN C 3 15  ? 5.022   -45.332 12.228  1.00 93.62  ? 13  GLN C C   1 
ATOM 4218 O O   . GLN C 3 15  ? 5.034   -45.157 11.007  1.00 90.57  ? 13  GLN C O   1 
ATOM 4219 C CB  . GLN C 3 15  ? 6.665   -44.325 13.835  1.00 96.46  ? 13  GLN C CB  1 
ATOM 4220 C CG  . GLN C 3 15  ? 7.741   -44.559 14.893  1.00 94.65  ? 13  GLN C CG  1 
ATOM 4221 C CD  . GLN C 3 15  ? 7.933   -43.360 15.807  1.00 111.16 ? 13  GLN C CD  1 
ATOM 4222 O OE1 . GLN C 3 15  ? 7.409   -42.277 15.546  1.00 109.76 ? 13  GLN C OE1 1 
ATOM 4223 N NE2 . GLN C 3 15  ? 8.689   -43.550 16.885  1.00 112.61 ? 13  GLN C NE2 1 
ATOM 4224 N N   . ALA C 3 16  ? 3.904   -45.341 12.948  1.00 99.44  ? 14  ALA C N   1 
ATOM 4225 C CA  . ALA C 3 16  ? 2.607   -45.082 12.335  1.00 93.66  ? 14  ALA C CA  1 
ATOM 4226 C C   . ALA C 3 16  ? 2.539   -43.634 11.864  1.00 95.71  ? 14  ALA C C   1 
ATOM 4227 O O   . ALA C 3 16  ? 2.740   -42.706 12.654  1.00 93.24  ? 14  ALA C O   1 
ATOM 4228 C CB  . ALA C 3 16  ? 1.486   -45.382 13.326  1.00 89.69  ? 14  ALA C CB  1 
ATOM 4229 N N   . GLY C 3 17  ? 2.255   -43.441 10.576  1.00 94.36  ? 15  GLY C N   1 
ATOM 4230 C CA  . GLY C 3 17  ? 2.229   -42.122 9.986   1.00 92.37  ? 15  GLY C CA  1 
ATOM 4231 C C   . GLY C 3 17  ? 3.517   -41.700 9.316   1.00 90.57  ? 15  GLY C C   1 
ATOM 4232 O O   . GLY C 3 17  ? 3.525   -40.681 8.614   1.00 85.18  ? 15  GLY C O   1 
ATOM 4233 N N   . ASP C 3 18  ? 4.599   -42.448 9.503   1.00 101.92 ? 16  ASP C N   1 
ATOM 4234 C CA  . ASP C 3 18  ? 5.873   -42.139 8.867   1.00 101.11 ? 16  ASP C CA  1 
ATOM 4235 C C   . ASP C 3 18  ? 5.786   -42.465 7.375   1.00 99.92  ? 16  ASP C C   1 
ATOM 4236 O O   . ASP C 3 18  ? 4.719   -42.767 6.832   1.00 99.49  ? 16  ASP C O   1 
ATOM 4237 C CB  . ASP C 3 18  ? 7.001   -42.903 9.555   1.00 99.74  ? 16  ASP C CB  1 
ATOM 4238 C CG  . ASP C 3 18  ? 7.918   -41.999 10.354  1.00 111.46 ? 16  ASP C CG  1 
ATOM 4239 O OD1 . ASP C 3 18  ? 7.508   -40.863 10.674  1.00 113.41 ? 16  ASP C OD1 1 
ATOM 4240 O OD2 . ASP C 3 18  ? 9.050   -42.427 10.665  1.00 104.87 ? 16  ASP C OD2 1 
ATOM 4241 N N   . SER C 3 19  ? 6.925   -42.407 6.690   1.00 91.55  ? 17  SER C N   1 
ATOM 4242 C CA  . SER C 3 19  ? 6.993   -42.723 5.272   1.00 71.91  ? 17  SER C CA  1 
ATOM 4243 C C   . SER C 3 19  ? 8.104   -43.731 5.021   1.00 72.33  ? 17  SER C C   1 
ATOM 4244 O O   . SER C 3 19  ? 8.996   -43.930 5.850   1.00 68.94  ? 17  SER C O   1 
ATOM 4245 C CB  . SER C 3 19  ? 7.221   -41.469 4.418   1.00 67.10  ? 17  SER C CB  1 
ATOM 4246 O OG  . SER C 3 19  ? 6.010   -40.760 4.222   1.00 75.18  ? 17  SER C OG  1 
ATOM 4247 N N   . LEU C 3 20  ? 8.033   -44.367 3.856   1.00 79.03  ? 18  LEU C N   1 
ATOM 4248 C CA  . LEU C 3 20  ? 9.009   -45.371 3.464   1.00 69.77  ? 18  LEU C CA  1 
ATOM 4249 C C   . LEU C 3 20  ? 8.948   -45.540 1.954   1.00 62.89  ? 18  LEU C C   1 
ATOM 4250 O O   . LEU C 3 20  ? 7.904   -45.318 1.334   1.00 62.31  ? 18  LEU C O   1 
ATOM 4251 C CB  . LEU C 3 20  ? 8.752   -46.704 4.173   1.00 62.82  ? 18  LEU C CB  1 
ATOM 4252 C CG  . LEU C 3 20  ? 9.882   -47.729 4.143   1.00 66.41  ? 18  LEU C CG  1 
ATOM 4253 C CD1 . LEU C 3 20  ? 11.218  -47.065 4.435   1.00 67.63  ? 18  LEU C CD1 1 
ATOM 4254 C CD2 . LEU C 3 20  ? 9.599   -48.828 5.147   1.00 67.29  ? 18  LEU C CD2 1 
ATOM 4255 N N   . THR C 3 21  ? 10.079  -45.926 1.370   1.00 60.41  ? 19  THR C N   1 
ATOM 4256 C CA  . THR C 3 21  ? 10.196  -46.102 -0.072  1.00 59.32  ? 19  THR C CA  1 
ATOM 4257 C C   . THR C 3 21  ? 10.811  -47.464 -0.350  1.00 62.81  ? 19  THR C C   1 
ATOM 4258 O O   . THR C 3 21  ? 11.907  -47.764 0.137   1.00 66.38  ? 19  THR C O   1 
ATOM 4259 C CB  . THR C 3 21  ? 11.044  -44.992 -0.701  1.00 59.58  ? 19  THR C CB  1 
ATOM 4260 O OG1 . THR C 3 21  ? 10.321  -43.755 -0.662  1.00 59.78  ? 19  THR C OG1 1 
ATOM 4261 C CG2 . THR C 3 21  ? 11.378  -45.329 -2.148  1.00 60.99  ? 19  THR C CG2 1 
ATOM 4262 N N   . LEU C 3 22  ? 10.105  -48.284 -1.119  1.00 61.29  ? 20  LEU C N   1 
ATOM 4263 C CA  . LEU C 3 22  ? 10.605  -49.577 -1.558  1.00 59.95  ? 20  LEU C CA  1 
ATOM 4264 C C   . LEU C 3 22  ? 11.080  -49.480 -3.002  1.00 60.86  ? 20  LEU C C   1 
ATOM 4265 O O   . LEU C 3 22  ? 10.631  -48.623 -3.766  1.00 57.91  ? 20  LEU C O   1 
ATOM 4266 C CB  . LEU C 3 22  ? 9.524   -50.652 -1.428  1.00 60.28  ? 20  LEU C CB  1 
ATOM 4267 C CG  . LEU C 3 22  ? 8.683   -50.589 -0.153  1.00 57.38  ? 20  LEU C CG  1 
ATOM 4268 C CD1 . LEU C 3 22  ? 7.292   -51.148 -0.395  1.00 55.10  ? 20  LEU C CD1 1 
ATOM 4269 C CD2 . LEU C 3 22  ? 9.378   -51.333 0.976   1.00 64.96  ? 20  LEU C CD2 1 
ATOM 4270 N N   . SER C 3 23  ? 12.001  -50.369 -3.369  1.00 62.03  ? 21  SER C N   1 
ATOM 4271 C CA  . SER C 3 23  ? 12.600  -50.353 -4.697  1.00 58.21  ? 21  SER C CA  1 
ATOM 4272 C C   . SER C 3 23  ? 12.777  -51.777 -5.197  1.00 57.52  ? 21  SER C C   1 
ATOM 4273 O O   . SER C 3 23  ? 13.347  -52.619 -4.496  1.00 57.72  ? 21  SER C O   1 
ATOM 4274 C CB  . SER C 3 23  ? 13.949  -49.625 -4.688  1.00 59.12  ? 21  SER C CB  1 
ATOM 4275 O OG  . SER C 3 23  ? 13.867  -48.396 -3.987  1.00 62.94  ? 21  SER C OG  1 
ATOM 4276 N N   . CYS C 3 24  ? 12.294  -52.036 -6.409  1.00 54.74  ? 22  CYS C N   1 
ATOM 4277 C CA  . CYS C 3 24  ? 12.411  -53.336 -7.059  1.00 60.90  ? 22  CYS C CA  1 
ATOM 4278 C C   . CYS C 3 24  ? 13.329  -53.178 -8.266  1.00 60.62  ? 22  CYS C C   1 
ATOM 4279 O O   . CYS C 3 24  ? 12.955  -52.545 -9.260  1.00 62.34  ? 22  CYS C O   1 
ATOM 4280 C CB  . CYS C 3 24  ? 11.034  -53.864 -7.464  1.00 63.13  ? 22  CYS C CB  1 
ATOM 4281 S SG  . CYS C 3 24  ? 11.033  -55.416 -8.404  1.00 61.47  ? 22  CYS C SG  1 
ATOM 4282 N N   . ALA C 3 25  ? 14.533  -53.738 -8.172  1.00 60.38  ? 23  ALA C N   1 
ATOM 4283 C CA  . ALA C 3 25  ? 15.496  -53.695 -9.263  1.00 59.60  ? 23  ALA C CA  1 
ATOM 4284 C C   . ALA C 3 25  ? 15.268  -54.879 -10.194 1.00 61.62  ? 23  ALA C C   1 
ATOM 4285 O O   . ALA C 3 25  ? 15.239  -56.030 -9.747  1.00 60.44  ? 23  ALA C O   1 
ATOM 4286 C CB  . ALA C 3 25  ? 16.927  -53.710 -8.725  1.00 55.72  ? 23  ALA C CB  1 
ATOM 4287 N N   . ALA C 3 26  ? 15.102  -54.592 -11.482 1.00 61.08  ? 24  ALA C N   1 
ATOM 4288 C CA  . ALA C 3 26  ? 14.855  -55.610 -12.495 1.00 59.52  ? 24  ALA C CA  1 
ATOM 4289 C C   . ALA C 3 26  ? 16.098  -55.762 -13.360 1.00 59.99  ? 24  ALA C C   1 
ATOM 4290 O O   . ALA C 3 26  ? 16.528  -54.803 -14.009 1.00 62.79  ? 24  ALA C O   1 
ATOM 4291 C CB  . ALA C 3 26  ? 13.645  -55.249 -13.354 1.00 59.11  ? 24  ALA C CB  1 
ATOM 4292 N N   . SER C 3 27  ? 16.670  -56.963 -13.367 1.00 63.25  ? 25  SER C N   1 
ATOM 4293 C CA  . SER C 3 27  ? 17.843  -57.277 -14.172 1.00 67.72  ? 25  SER C CA  1 
ATOM 4294 C C   . SER C 3 27  ? 17.466  -58.354 -15.178 1.00 69.24  ? 25  SER C C   1 
ATOM 4295 O O   . SER C 3 27  ? 17.050  -59.452 -14.791 1.00 67.03  ? 25  SER C O   1 
ATOM 4296 C CB  . SER C 3 27  ? 19.008  -57.737 -13.293 1.00 72.51  ? 25  SER C CB  1 
ATOM 4297 O OG  . SER C 3 27  ? 18.717  -58.969 -12.657 1.00 70.85  ? 25  SER C OG  1 
ATOM 4298 N N   . GLY C 3 28  ? 17.604  -58.040 -16.459 1.00 63.24  ? 26  GLY C N   1 
ATOM 4299 C CA  . GLY C 3 28  ? 17.281  -58.996 -17.497 1.00 66.57  ? 26  GLY C CA  1 
ATOM 4300 C C   . GLY C 3 28  ? 17.211  -58.320 -18.848 1.00 68.75  ? 26  GLY C C   1 
ATOM 4301 O O   . GLY C 3 28  ? 17.420  -57.110 -18.980 1.00 65.99  ? 26  GLY C O   1 
ATOM 4302 N N   . ARG C 3 29  ? 16.912  -59.136 -19.855 1.00 69.34  ? 27  ARG C N   1 
ATOM 4303 C CA  . ARG C 3 29  ? 16.796  -58.644 -21.220 1.00 73.85  ? 27  ARG C CA  1 
ATOM 4304 C C   . ARG C 3 29  ? 15.399  -58.091 -21.471 1.00 78.27  ? 27  ARG C C   1 
ATOM 4305 O O   . ARG C 3 29  ? 14.399  -58.668 -21.031 1.00 75.70  ? 27  ARG C O   1 
ATOM 4306 C CB  . ARG C 3 29  ? 17.103  -59.758 -22.222 1.00 72.00  ? 27  ARG C CB  1 
ATOM 4307 C CG  . ARG C 3 29  ? 16.479  -61.104 -21.877 1.00 75.61  ? 27  ARG C CG  1 
ATOM 4308 C CD  . ARG C 3 29  ? 16.023  -61.837 -23.132 1.00 78.49  ? 27  ARG C CD  1 
ATOM 4309 N NE  . ARG C 3 29  ? 14.594  -61.672 -23.377 1.00 84.82  ? 27  ARG C NE  1 
ATOM 4310 C CZ  . ARG C 3 29  ? 13.868  -62.466 -24.153 1.00 88.26  ? 27  ARG C CZ  1 
ATOM 4311 N NH1 . ARG C 3 29  ? 14.407  -63.492 -24.790 1.00 92.12  ? 27  ARG C NH1 1 
ATOM 4312 N NH2 . ARG C 3 29  ? 12.568  -62.220 -24.297 1.00 84.64  ? 27  ARG C NH2 1 
ATOM 4313 N N   . THR C 3 30  ? 15.341  -56.971 -22.193 1.00 72.14  ? 28  THR C N   1 
ATOM 4314 C CA  . THR C 3 30  ? 14.090  -56.282 -22.515 1.00 65.32  ? 28  THR C CA  1 
ATOM 4315 C C   . THR C 3 30  ? 13.246  -56.063 -21.260 1.00 60.13  ? 28  THR C C   1 
ATOM 4316 O O   . THR C 3 30  ? 12.068  -56.419 -21.198 1.00 57.90  ? 28  THR C O   1 
ATOM 4317 C CB  . THR C 3 30  ? 13.296  -57.041 -23.582 1.00 60.42  ? 28  THR C CB  1 
ATOM 4318 O OG1 . THR C 3 30  ? 12.739  -58.232 -23.014 1.00 66.79  ? 28  THR C OG1 1 
ATOM 4319 C CG2 . THR C 3 30  ? 14.195  -57.415 -24.749 1.00 61.72  ? 28  THR C CG2 1 
ATOM 4320 N N   . ALA C 3 31  ? 13.873  -55.467 -20.242 1.00 61.74  ? 29  ALA C N   1 
ATOM 4321 C CA  . ALA C 3 31  ? 13.187  -55.230 -18.978 1.00 55.18  ? 29  ALA C CA  1 
ATOM 4322 C C   . ALA C 3 31  ? 12.068  -54.205 -19.104 1.00 56.48  ? 29  ALA C C   1 
ATOM 4323 O O   . ALA C 3 31  ? 11.174  -54.179 -18.251 1.00 55.13  ? 29  ALA C O   1 
ATOM 4324 C CB  . ALA C 3 31  ? 14.188  -54.778 -17.914 1.00 54.70  ? 29  ALA C CB  1 
ATOM 4325 N N   . TYR C 3 32  ? 12.092  -53.366 -20.143 1.00 53.61  ? 30  TYR C N   1 
ATOM 4326 C CA  . TYR C 3 32  ? 11.035  -52.381 -20.341 1.00 52.41  ? 30  TYR C CA  1 
ATOM 4327 C C   . TYR C 3 32  ? 9.719   -53.006 -20.779 1.00 50.72  ? 30  TYR C C   1 
ATOM 4328 O O   . TYR C 3 32  ? 8.690   -52.323 -20.746 1.00 53.09  ? 30  TYR C O   1 
ATOM 4329 C CB  . TYR C 3 32  ? 11.471  -51.330 -21.367 1.00 56.41  ? 30  TYR C CB  1 
ATOM 4330 C CG  . TYR C 3 32  ? 11.503  -51.818 -22.803 1.00 55.34  ? 30  TYR C CG  1 
ATOM 4331 C CD1 . TYR C 3 32  ? 12.598  -52.516 -23.297 1.00 57.97  ? 30  TYR C CD1 1 
ATOM 4332 C CD2 . TYR C 3 32  ? 10.441  -51.572 -23.667 1.00 54.71  ? 30  TYR C CD2 1 
ATOM 4333 C CE1 . TYR C 3 32  ? 12.634  -52.959 -24.609 1.00 57.90  ? 30  TYR C CE1 1 
ATOM 4334 C CE2 . TYR C 3 32  ? 10.467  -52.015 -24.980 1.00 53.49  ? 30  TYR C CE2 1 
ATOM 4335 C CZ  . TYR C 3 32  ? 11.565  -52.706 -25.445 1.00 55.18  ? 30  TYR C CZ  1 
ATOM 4336 O OH  . TYR C 3 32  ? 11.598  -53.146 -26.748 1.00 52.91  ? 30  TYR C OH  1 
ATOM 4337 N N   . ARG C 3 33  ? 9.723   -54.273 -21.184 1.00 50.81  ? 31  ARG C N   1 
ATOM 4338 C CA  . ARG C 3 33  ? 8.520   -54.937 -21.664 1.00 51.47  ? 31  ARG C CA  1 
ATOM 4339 C C   . ARG C 3 33  ? 7.718   -55.600 -20.553 1.00 49.56  ? 31  ARG C C   1 
ATOM 4340 O O   . ARG C 3 33  ? 6.620   -56.100 -20.820 1.00 49.90  ? 31  ARG C O   1 
ATOM 4341 C CB  . ARG C 3 33  ? 8.883   -55.996 -22.710 1.00 54.15  ? 31  ARG C CB  1 
ATOM 4342 C CG  . ARG C 3 33  ? 9.976   -55.580 -23.680 1.00 53.23  ? 31  ARG C CG  1 
ATOM 4343 C CD  . ARG C 3 33  ? 9.508   -55.714 -25.114 1.00 52.41  ? 31  ARG C CD  1 
ATOM 4344 N NE  . ARG C 3 33  ? 10.612  -55.936 -26.039 1.00 54.67  ? 31  ARG C NE  1 
ATOM 4345 C CZ  . ARG C 3 33  ? 10.526  -56.661 -27.147 1.00 60.28  ? 31  ARG C CZ  1 
ATOM 4346 N NH1 . ARG C 3 33  ? 9.397   -57.253 -27.500 1.00 55.76  ? 31  ARG C NH1 1 
ATOM 4347 N NH2 . ARG C 3 33  ? 11.602  -56.798 -27.918 1.00 64.20  ? 31  ARG C NH2 1 
ATOM 4348 N N   . TYR C 3 34  ? 8.232   -55.622 -19.328 1.00 51.63  ? 32  TYR C N   1 
ATOM 4349 C CA  . TYR C 3 34  ? 7.591   -56.326 -18.227 1.00 50.25  ? 32  TYR C CA  1 
ATOM 4350 C C   . TYR C 3 34  ? 6.819   -55.330 -17.372 1.00 51.30  ? 32  TYR C C   1 
ATOM 4351 O O   . TYR C 3 34  ? 7.405   -54.394 -16.817 1.00 48.46  ? 32  TYR C O   1 
ATOM 4352 C CB  . TYR C 3 34  ? 8.625   -57.075 -17.385 1.00 49.39  ? 32  TYR C CB  1 
ATOM 4353 C CG  . TYR C 3 34  ? 9.281   -58.232 -18.108 1.00 50.79  ? 32  TYR C CG  1 
ATOM 4354 C CD1 . TYR C 3 34  ? 10.277  -58.010 -19.051 1.00 54.72  ? 32  TYR C CD1 1 
ATOM 4355 C CD2 . TYR C 3 34  ? 8.909   -59.545 -17.847 1.00 50.95  ? 32  TYR C CD2 1 
ATOM 4356 C CE1 . TYR C 3 34  ? 10.881  -59.058 -19.717 1.00 58.75  ? 32  TYR C CE1 1 
ATOM 4357 C CE2 . TYR C 3 34  ? 9.510   -60.603 -18.509 1.00 57.68  ? 32  TYR C CE2 1 
ATOM 4358 C CZ  . TYR C 3 34  ? 10.496  -60.353 -19.442 1.00 59.47  ? 32  TYR C CZ  1 
ATOM 4359 O OH  . TYR C 3 34  ? 11.101  -61.397 -20.105 1.00 59.11  ? 32  TYR C OH  1 
ATOM 4360 N N   . GLY C 3 35  ? 5.505   -55.520 -17.288 1.00 62.13  ? 33  GLY C N   1 
ATOM 4361 C CA  . GLY C 3 35  ? 4.715   -54.756 -16.342 1.00 63.93  ? 33  GLY C CA  1 
ATOM 4362 C C   . GLY C 3 35  ? 4.943   -55.257 -14.927 1.00 67.42  ? 33  GLY C C   1 
ATOM 4363 O O   . GLY C 3 35  ? 5.003   -56.461 -14.671 1.00 68.91  ? 33  GLY C O   1 
ATOM 4364 N N   . MET C 3 36  ? 5.077   -54.317 -13.999 1.00 55.56  ? 34  MET C N   1 
ATOM 4365 C CA  . MET C 3 36  ? 5.475   -54.622 -12.635 1.00 56.25  ? 34  MET C CA  1 
ATOM 4366 C C   . MET C 3 36  ? 4.360   -54.266 -11.664 1.00 52.07  ? 34  MET C C   1 
ATOM 4367 O O   . MET C 3 36  ? 3.660   -53.265 -11.844 1.00 53.31  ? 34  MET C O   1 
ATOM 4368 C CB  . MET C 3 36  ? 6.755   -53.874 -12.270 1.00 52.83  ? 34  MET C CB  1 
ATOM 4369 C CG  . MET C 3 36  ? 7.754   -53.849 -13.406 1.00 54.17  ? 34  MET C CG  1 
ATOM 4370 S SD  . MET C 3 36  ? 8.922   -55.214 -13.313 1.00 68.64  ? 34  MET C SD  1 
ATOM 4371 C CE  . MET C 3 36  ? 10.242  -54.592 -14.351 1.00 64.04  ? 34  MET C CE  1 
ATOM 4372 N N   . GLY C 3 37  ? 4.203   -55.093 -10.642 1.00 53.16  ? 35  GLY C N   1 
ATOM 4373 C CA  . GLY C 3 37  ? 3.210   -54.850 -9.614  1.00 55.46  ? 35  GLY C CA  1 
ATOM 4374 C C   . GLY C 3 37  ? 3.761   -55.193 -8.247  1.00 54.35  ? 35  GLY C C   1 
ATOM 4375 O O   . GLY C 3 37  ? 4.653   -56.032 -8.105  1.00 53.94  ? 35  GLY C O   1 
ATOM 4376 N N   . TRP C 3 38  ? 3.214   -54.527 -7.233  1.00 57.34  ? 36  TRP C N   1 
ATOM 4377 C CA  . TRP C 3 38  ? 3.609   -54.727 -5.845  1.00 57.29  ? 36  TRP C CA  1 
ATOM 4378 C C   . TRP C 3 38  ? 2.531   -55.518 -5.115  1.00 55.19  ? 36  TRP C C   1 
ATOM 4379 O O   . TRP C 3 38  ? 1.346   -55.178 -5.196  1.00 59.28  ? 36  TRP C O   1 
ATOM 4380 C CB  . TRP C 3 38  ? 3.841   -53.386 -5.143  1.00 56.32  ? 36  TRP C CB  1 
ATOM 4381 C CG  . TRP C 3 38  ? 5.092   -52.683 -5.572  1.00 55.48  ? 36  TRP C CG  1 
ATOM 4382 C CD1 . TRP C 3 38  ? 5.199   -51.695 -6.507  1.00 57.58  ? 36  TRP C CD1 1 
ATOM 4383 C CD2 . TRP C 3 38  ? 6.416   -52.917 -5.080  1.00 56.76  ? 36  TRP C CD2 1 
ATOM 4384 N NE1 . TRP C 3 38  ? 6.509   -51.297 -6.627  1.00 56.10  ? 36  TRP C NE1 1 
ATOM 4385 C CE2 . TRP C 3 38  ? 7.277   -52.033 -5.763  1.00 54.62  ? 36  TRP C CE2 1 
ATOM 4386 C CE3 . TRP C 3 38  ? 6.958   -53.787 -4.129  1.00 54.27  ? 36  TRP C CE3 1 
ATOM 4387 C CZ2 . TRP C 3 38  ? 8.649   -51.994 -5.525  1.00 54.55  ? 36  TRP C CZ2 1 
ATOM 4388 C CZ3 . TRP C 3 38  ? 8.319   -53.747 -3.893  1.00 56.40  ? 36  TRP C CZ3 1 
ATOM 4389 C CH2 . TRP C 3 38  ? 9.150   -52.857 -4.589  1.00 59.28  ? 36  TRP C CH2 1 
ATOM 4390 N N   . PHE C 3 39  ? 2.943   -56.566 -4.403  1.00 58.35  ? 37  PHE C N   1 
ATOM 4391 C CA  . PHE C 3 39  ? 2.034   -57.379 -3.608  1.00 61.82  ? 37  PHE C CA  1 
ATOM 4392 C C   . PHE C 3 39  ? 2.542   -57.472 -2.177  1.00 56.28  ? 37  PHE C C   1 
ATOM 4393 O O   . PHE C 3 39  ? 3.749   -57.425 -1.927  1.00 56.84  ? 37  PHE C O   1 
ATOM 4394 C CB  . PHE C 3 39  ? 1.880   -58.791 -4.186  1.00 57.51  ? 37  PHE C CB  1 
ATOM 4395 C CG  . PHE C 3 39  ? 1.159   -58.834 -5.499  1.00 56.53  ? 37  PHE C CG  1 
ATOM 4396 C CD1 . PHE C 3 39  ? 1.817   -58.516 -6.675  1.00 55.18  ? 37  PHE C CD1 1 
ATOM 4397 C CD2 . PHE C 3 39  ? -0.174  -59.201 -5.561  1.00 59.17  ? 37  PHE C CD2 1 
ATOM 4398 C CE1 . PHE C 3 39  ? 1.159   -58.557 -7.887  1.00 55.34  ? 37  PHE C CE1 1 
ATOM 4399 C CE2 . PHE C 3 39  ? -0.839  -59.246 -6.771  1.00 61.44  ? 37  PHE C CE2 1 
ATOM 4400 C CZ  . PHE C 3 39  ? -0.171  -58.923 -7.936  1.00 56.15  ? 37  PHE C CZ  1 
ATOM 4401 N N   . ARG C 3 40  ? 1.608   -57.615 -1.236  1.00 63.89  ? 38  ARG C N   1 
ATOM 4402 C CA  . ARG C 3 40  ? 1.936   -57.766 0.175   1.00 63.46  ? 38  ARG C CA  1 
ATOM 4403 C C   . ARG C 3 40  ? 1.263   -59.015 0.729   1.00 66.72  ? 38  ARG C C   1 
ATOM 4404 O O   . ARG C 3 40  ? 0.186   -59.413 0.275   1.00 72.88  ? 38  ARG C O   1 
ATOM 4405 C CB  . ARG C 3 40  ? 1.524   -56.526 0.993   1.00 57.70  ? 38  ARG C CB  1 
ATOM 4406 C CG  . ARG C 3 40  ? 0.039   -56.418 1.313   1.00 61.40  ? 38  ARG C CG  1 
ATOM 4407 C CD  . ARG C 3 40  ? -0.294  -55.048 1.894   1.00 63.49  ? 38  ARG C CD  1 
ATOM 4408 N NE  . ARG C 3 40  ? -1.730  -54.817 1.999   1.00 70.83  ? 38  ARG C NE  1 
ATOM 4409 C CZ  . ARG C 3 40  ? -2.278  -53.672 2.385   1.00 70.47  ? 38  ARG C CZ  1 
ATOM 4410 N NH1 . ARG C 3 40  ? -1.535  -52.624 2.707   1.00 66.06  ? 38  ARG C NH1 1 
ATOM 4411 N NH2 . ARG C 3 40  ? -3.603  -53.575 2.450   1.00 67.39  ? 38  ARG C NH2 1 
ATOM 4412 N N   . GLN C 3 41  ? 1.913   -59.635 1.715   1.00 69.84  ? 39  GLN C N   1 
ATOM 4413 C CA  . GLN C 3 41  ? 1.446   -60.889 2.298   1.00 68.01  ? 39  GLN C CA  1 
ATOM 4414 C C   . GLN C 3 41  ? 1.433   -60.773 3.814   1.00 67.55  ? 39  GLN C C   1 
ATOM 4415 O O   . GLN C 3 41  ? 2.477   -60.535 4.431   1.00 68.14  ? 39  GLN C O   1 
ATOM 4416 C CB  . GLN C 3 41  ? 2.329   -62.063 1.865   1.00 71.63  ? 39  GLN C CB  1 
ATOM 4417 C CG  . GLN C 3 41  ? 2.154   -63.315 2.710   1.00 76.67  ? 39  GLN C CG  1 
ATOM 4418 C CD  . GLN C 3 41  ? 3.213   -64.361 2.424   1.00 73.54  ? 39  GLN C CD  1 
ATOM 4419 O OE1 . GLN C 3 41  ? 3.362   -64.816 1.289   1.00 68.96  ? 39  GLN C OE1 1 
ATOM 4420 N NE2 . GLN C 3 41  ? 3.958   -64.746 3.455   1.00 75.66  ? 39  GLN C NE2 1 
ATOM 4421 N N   . HIS C 3 42  ? 0.259   -60.953 4.408   1.00 76.20  ? 40  HIS C N   1 
ATOM 4422 C CA  . HIS C 3 42  ? 0.097   -60.951 5.851   1.00 80.30  ? 40  HIS C CA  1 
ATOM 4423 C C   . HIS C 3 42  ? 0.555   -62.295 6.426   1.00 80.89  ? 40  HIS C C   1 
ATOM 4424 O O   . HIS C 3 42  ? 0.723   -63.264 5.682   1.00 81.69  ? 40  HIS C O   1 
ATOM 4425 C CB  . HIS C 3 42  ? -1.361  -60.646 6.191   1.00 80.60  ? 40  HIS C CB  1 
ATOM 4426 C CG  . HIS C 3 42  ? -1.741  -59.214 5.963   1.00 79.68  ? 40  HIS C CG  1 
ATOM 4427 N ND1 . HIS C 3 42  ? -2.765  -58.838 5.120   1.00 80.26  ? 40  HIS C ND1 1 
ATOM 4428 C CD2 . HIS C 3 42  ? -1.225  -58.065 6.462   1.00 76.77  ? 40  HIS C CD2 1 
ATOM 4429 C CE1 . HIS C 3 42  ? -2.868  -57.521 5.115   1.00 75.03  ? 40  HIS C CE1 1 
ATOM 4430 N NE2 . HIS C 3 42  ? -1.945  -57.028 5.920   1.00 76.72  ? 40  HIS C NE2 1 
ATOM 4431 N N   . PRO C 3 43  ? 0.797   -62.379 7.763   1.00 78.35  ? 41  PRO C N   1 
ATOM 4432 C CA  . PRO C 3 43  ? 1.420   -63.595 8.313   1.00 72.56  ? 41  PRO C CA  1 
ATOM 4433 C C   . PRO C 3 43  ? 0.628   -64.859 8.028   1.00 84.68  ? 41  PRO C C   1 
ATOM 4434 O O   . PRO C 3 43  ? -0.366  -65.143 8.702   1.00 87.34  ? 41  PRO C O   1 
ATOM 4435 C CB  . PRO C 3 43  ? 1.478   -63.313 9.821   1.00 75.92  ? 41  PRO C CB  1 
ATOM 4436 C CG  . PRO C 3 43  ? 0.427   -62.292 10.058  1.00 79.86  ? 41  PRO C CG  1 
ATOM 4437 C CD  . PRO C 3 43  ? 0.457   -61.427 8.836   1.00 82.11  ? 41  PRO C CD  1 
ATOM 4438 N N   . GLY C 3 44  ? 1.065   -65.622 7.027   1.00 94.54  ? 42  GLY C N   1 
ATOM 4439 C CA  . GLY C 3 44  ? 0.423   -66.866 6.671   1.00 89.17  ? 42  GLY C CA  1 
ATOM 4440 C C   . GLY C 3 44  ? -0.795  -66.743 5.784   1.00 94.15  ? 42  GLY C C   1 
ATOM 4441 O O   . GLY C 3 44  ? -1.324  -67.772 5.345   1.00 94.19  ? 42  GLY C O   1 
ATOM 4442 N N   . LYS C 3 45  ? -1.261  -65.529 5.502   1.00 98.76  ? 43  LYS C N   1 
ATOM 4443 C CA  . LYS C 3 45  ? -2.443  -65.332 4.680   1.00 97.15  ? 43  LYS C CA  1 
ATOM 4444 C C   . LYS C 3 45  ? -2.054  -65.233 3.206   1.00 95.24  ? 43  LYS C C   1 
ATOM 4445 O O   . LYS C 3 45  ? -0.877  -65.262 2.840   1.00 96.42  ? 43  LYS C O   1 
ATOM 4446 C CB  . LYS C 3 45  ? -3.210  -64.092 5.140   1.00 94.21  ? 43  LYS C CB  1 
ATOM 4447 C CG  . LYS C 3 45  ? -3.676  -64.161 6.588   1.00 101.21 ? 43  LYS C CG  1 
ATOM 4448 C CD  . LYS C 3 45  ? -4.157  -62.808 7.092   1.00 103.92 ? 43  LYS C CD  1 
ATOM 4449 C CE  . LYS C 3 45  ? -5.453  -62.388 6.417   1.00 100.95 ? 43  LYS C CE  1 
ATOM 4450 N NZ  . LYS C 3 45  ? -6.029  -61.164 7.040   1.00 95.87  ? 43  LYS C NZ  1 
ATOM 4451 N N   . GLU C 3 46  ? -3.062  -65.118 2.346   1.00 92.41  ? 44  GLU C N   1 
ATOM 4452 C CA  . GLU C 3 46  ? -2.828  -65.078 0.912   1.00 94.44  ? 44  GLU C CA  1 
ATOM 4453 C C   . GLU C 3 46  ? -2.176  -63.757 0.507   1.00 96.09  ? 44  GLU C C   1 
ATOM 4454 O O   . GLU C 3 46  ? -2.247  -62.749 1.216   1.00 101.42 ? 44  GLU C O   1 
ATOM 4455 C CB  . GLU C 3 46  ? -4.142  -65.275 0.153   1.00 100.87 ? 44  GLU C CB  1 
ATOM 4456 C CG  . GLU C 3 46  ? -3.979  -65.859 -1.242  1.00 101.58 ? 44  GLU C CG  1 
ATOM 4457 C CD  . GLU C 3 46  ? -4.995  -65.312 -2.226  1.00 109.93 ? 44  GLU C CD  1 
ATOM 4458 O OE1 . GLU C 3 46  ? -5.963  -64.660 -1.783  1.00 118.42 ? 44  GLU C OE1 1 
ATOM 4459 O OE2 . GLU C 3 46  ? -4.819  -65.526 -3.445  1.00 105.68 ? 44  GLU C OE2 1 
ATOM 4460 N N   . ARG C 3 47  ? -1.527  -63.777 -0.655  1.00 83.54  ? 45  ARG C N   1 
ATOM 4461 C CA  . ARG C 3 47  ? -0.899  -62.576 -1.188  1.00 77.70  ? 45  ARG C CA  1 
ATOM 4462 C C   . ARG C 3 47  ? -1.958  -61.618 -1.719  1.00 79.42  ? 45  ARG C C   1 
ATOM 4463 O O   . ARG C 3 47  ? -2.834  -62.012 -2.494  1.00 81.55  ? 45  ARG C O   1 
ATOM 4464 C CB  . ARG C 3 47  ? 0.084   -62.942 -2.298  1.00 68.47  ? 45  ARG C CB  1 
ATOM 4465 C CG  . ARG C 3 47  ? 1.380   -62.154 -2.266  1.00 64.88  ? 45  ARG C CG  1 
ATOM 4466 C CD  . ARG C 3 47  ? 2.461   -62.853 -3.068  1.00 59.47  ? 45  ARG C CD  1 
ATOM 4467 N NE  . ARG C 3 47  ? 2.653   -64.231 -2.637  1.00 63.04  ? 45  ARG C NE  1 
ATOM 4468 C CZ  . ARG C 3 47  ? 3.836   -64.806 -2.470  1.00 66.89  ? 45  ARG C CZ  1 
ATOM 4469 N NH1 . ARG C 3 47  ? 4.962   -64.151 -2.701  1.00 63.02  ? 45  ARG C NH1 1 
ATOM 4470 N NH2 . ARG C 3 47  ? 3.891   -66.071 -2.060  1.00 69.47  ? 45  ARG C NH2 1 
ATOM 4471 N N   . GLU C 3 48  ? -1.874  -60.357 -1.305  1.00 78.21  ? 46  GLU C N   1 
ATOM 4472 C CA  . GLU C 3 48  ? -2.838  -59.336 -1.683  1.00 81.27  ? 46  GLU C CA  1 
ATOM 4473 C C   . GLU C 3 48  ? -2.199  -58.310 -2.612  1.00 81.79  ? 46  GLU C C   1 
ATOM 4474 O O   . GLU C 3 48  ? -0.983  -58.098 -2.602  1.00 78.87  ? 46  GLU C O   1 
ATOM 4475 C CB  . GLU C 3 48  ? -3.411  -58.639 -0.443  1.00 82.07  ? 46  GLU C CB  1 
ATOM 4476 C CG  . GLU C 3 48  ? -4.138  -59.574 0.511   1.00 90.12  ? 46  GLU C CG  1 
ATOM 4477 C CD  . GLU C 3 48  ? -3.997  -59.156 1.962   1.00 101.30 ? 46  GLU C CD  1 
ATOM 4478 O OE1 . GLU C 3 48  ? -4.395  -58.020 2.297   1.00 103.50 ? 46  GLU C OE1 1 
ATOM 4479 O OE2 . GLU C 3 48  ? -3.489  -59.966 2.769   1.00 94.42  ? 46  GLU C OE2 1 
ATOM 4480 N N   . PHE C 3 49  ? -3.043  -57.668 -3.417  1.00 71.25  ? 47  PHE C N   1 
ATOM 4481 C CA  . PHE C 3 49  ? -2.593  -56.697 -4.405  1.00 64.12  ? 47  PHE C CA  1 
ATOM 4482 C C   . PHE C 3 49  ? -2.475  -55.309 -3.787  1.00 63.89  ? 47  PHE C C   1 
ATOM 4483 O O   . PHE C 3 49  ? -3.301  -54.910 -2.962  1.00 66.32  ? 47  PHE C O   1 
ATOM 4484 C CB  . PHE C 3 49  ? -3.559  -56.659 -5.590  1.00 60.85  ? 47  PHE C CB  1 
ATOM 4485 C CG  . PHE C 3 49  ? -3.158  -55.691 -6.665  1.00 59.97  ? 47  PHE C CG  1 
ATOM 4486 C CD1 . PHE C 3 49  ? -2.084  -55.966 -7.495  1.00 58.61  ? 47  PHE C CD1 1 
ATOM 4487 C CD2 . PHE C 3 49  ? -3.849  -54.504 -6.840  1.00 59.08  ? 47  PHE C CD2 1 
ATOM 4488 C CE1 . PHE C 3 49  ? -1.710  -55.077 -8.482  1.00 55.58  ? 47  PHE C CE1 1 
ATOM 4489 C CE2 . PHE C 3 49  ? -3.480  -53.611 -7.824  1.00 55.87  ? 47  PHE C CE2 1 
ATOM 4490 C CZ  . PHE C 3 49  ? -2.409  -53.897 -8.645  1.00 58.56  ? 47  PHE C CZ  1 
ATOM 4491 N N   . VAL C 3 50  ? -1.444  -54.570 -4.202  1.00 59.43  ? 48  VAL C N   1 
ATOM 4492 C CA  . VAL C 3 50  ? -1.208  -53.221 -3.696  1.00 60.69  ? 48  VAL C CA  1 
ATOM 4493 C C   . VAL C 3 50  ? -1.245  -52.228 -4.852  1.00 61.97  ? 48  VAL C C   1 
ATOM 4494 O O   . VAL C 3 50  ? -2.151  -51.393 -4.941  1.00 62.31  ? 48  VAL C O   1 
ATOM 4495 C CB  . VAL C 3 50  ? 0.130   -53.131 -2.938  1.00 62.16  ? 48  VAL C CB  1 
ATOM 4496 C CG1 . VAL C 3 50  ? 0.470   -51.677 -2.622  1.00 62.28  ? 48  VAL C CG1 1 
ATOM 4497 C CG2 . VAL C 3 50  ? 0.082   -53.969 -1.669  1.00 62.06  ? 48  VAL C CG2 1 
ATOM 4498 N N   . ALA C 3 51  ? -0.259  -52.312 -5.743  1.00 67.86  ? 49  ALA C N   1 
ATOM 4499 C CA  . ALA C 3 51  ? -0.173  -51.410 -6.882  1.00 59.66  ? 49  ALA C CA  1 
ATOM 4500 C C   . ALA C 3 51  ? 0.497   -52.138 -8.038  1.00 61.27  ? 49  ALA C C   1 
ATOM 4501 O O   . ALA C 3 51  ? 1.127   -53.183 -7.860  1.00 64.83  ? 49  ALA C O   1 
ATOM 4502 C CB  . ALA C 3 51  ? 0.590   -50.129 -6.529  1.00 56.81  ? 49  ALA C CB  1 
ATOM 4503 N N   . SER C 3 52  ? 0.352   -51.572 -9.235  1.00 58.36  ? 50  SER C N   1 
ATOM 4504 C CA  . SER C 3 52  ? 0.973   -52.139 -10.424 1.00 55.60  ? 50  SER C CA  1 
ATOM 4505 C C   . SER C 3 52  ? 1.137   -51.044 -11.466 1.00 54.01  ? 50  SER C C   1 
ATOM 4506 O O   . SER C 3 52  ? 0.554   -49.963 -11.356 1.00 52.76  ? 50  SER C O   1 
ATOM 4507 C CB  . SER C 3 52  ? 0.156   -53.308 -10.989 1.00 55.35  ? 50  SER C CB  1 
ATOM 4508 O OG  . SER C 3 52  ? -1.034  -52.852 -11.608 1.00 58.43  ? 50  SER C OG  1 
ATOM 4509 N N   . ILE C 3 53  ? 1.946   -51.342 -12.480 1.00 56.47  ? 51  ILE C N   1 
ATOM 4510 C CA  . ILE C 3 53  ? 2.197   -50.428 -13.587 1.00 55.58  ? 51  ILE C CA  1 
ATOM 4511 C C   . ILE C 3 53  ? 2.109   -51.205 -14.895 1.00 52.25  ? 51  ILE C C   1 
ATOM 4512 O O   . ILE C 3 53  ? 2.469   -52.386 -14.956 1.00 51.67  ? 51  ILE C O   1 
ATOM 4513 C CB  . ILE C 3 53  ? 3.564   -49.718 -13.439 1.00 54.21  ? 51  ILE C CB  1 
ATOM 4514 C CG1 . ILE C 3 53  ? 3.498   -48.299 -14.010 1.00 54.74  ? 51  ILE C CG1 1 
ATOM 4515 C CG2 . ILE C 3 53  ? 4.691   -50.520 -14.085 1.00 55.06  ? 51  ILE C CG2 1 
ATOM 4516 C CD1 . ILE C 3 53  ? 4.833   -47.586 -14.021 1.00 46.78  ? 51  ILE C CD1 1 
ATOM 4517 N N   . TRP C 3 54  ? 1.594   -50.549 -15.932 1.00 53.98  ? 52  TRP C N   1 
ATOM 4518 C CA  . TRP C 3 54  ? 1.496   -51.153 -17.253 1.00 53.32  ? 52  TRP C CA  1 
ATOM 4519 C C   . TRP C 3 54  ? 2.871   -51.172 -17.910 1.00 51.49  ? 52  TRP C C   1 
ATOM 4520 O O   . TRP C 3 54  ? 3.739   -50.351 -17.601 1.00 52.63  ? 52  TRP C O   1 
ATOM 4521 C CB  . TRP C 3 54  ? 0.489   -50.384 -18.115 1.00 52.61  ? 52  TRP C CB  1 
ATOM 4522 C CG  . TRP C 3 54  ? 0.226   -50.952 -19.494 1.00 52.01  ? 52  TRP C CG  1 
ATOM 4523 C CD1 . TRP C 3 54  ? 0.389   -50.309 -20.688 1.00 46.40  ? 52  TRP C CD1 1 
ATOM 4524 C CD2 . TRP C 3 54  ? -0.267  -52.263 -19.813 1.00 52.29  ? 52  TRP C CD2 1 
ATOM 4525 N NE1 . TRP C 3 54  ? 0.038   -51.136 -21.727 1.00 47.26  ? 52  TRP C NE1 1 
ATOM 4526 C CE2 . TRP C 3 54  ? -0.367  -52.341 -21.217 1.00 51.50  ? 52  TRP C CE2 1 
ATOM 4527 C CE3 . TRP C 3 54  ? -0.628  -53.377 -19.049 1.00 55.02  ? 52  TRP C CE3 1 
ATOM 4528 C CZ2 . TRP C 3 54  ? -0.813  -53.490 -21.871 1.00 46.69  ? 52  TRP C CZ2 1 
ATOM 4529 C CZ3 . TRP C 3 54  ? -1.068  -54.515 -19.702 1.00 50.15  ? 52  TRP C CZ3 1 
ATOM 4530 C CH2 . TRP C 3 54  ? -1.158  -54.562 -21.096 1.00 48.31  ? 52  TRP C CH2 1 
ATOM 4531 N N   . TRP C 3 55  ? 3.067   -52.129 -18.821 1.00 49.48  ? 53  TRP C N   1 
ATOM 4532 C CA  . TRP C 3 55  ? 4.396   -52.348 -19.380 1.00 48.76  ? 53  TRP C CA  1 
ATOM 4533 C C   . TRP C 3 55  ? 4.918   -51.138 -20.148 1.00 53.51  ? 53  TRP C C   1 
ATOM 4534 O O   . TRP C 3 55  ? 6.137   -50.987 -20.282 1.00 53.01  ? 53  TRP C O   1 
ATOM 4535 C CB  . TRP C 3 55  ? 4.399   -53.604 -20.262 1.00 50.36  ? 53  TRP C CB  1 
ATOM 4536 C CG  . TRP C 3 55  ? 3.830   -53.428 -21.638 1.00 48.85  ? 53  TRP C CG  1 
ATOM 4537 C CD1 . TRP C 3 55  ? 2.544   -53.656 -22.025 1.00 46.81  ? 53  TRP C CD1 1 
ATOM 4538 C CD2 . TRP C 3 55  ? 4.536   -53.012 -22.814 1.00 48.51  ? 53  TRP C CD2 1 
ATOM 4539 N NE1 . TRP C 3 55  ? 2.400   -53.396 -23.367 1.00 56.11  ? 53  TRP C NE1 1 
ATOM 4540 C CE2 . TRP C 3 55  ? 3.609   -52.999 -23.874 1.00 54.21  ? 53  TRP C CE2 1 
ATOM 4541 C CE3 . TRP C 3 55  ? 5.860   -52.643 -23.070 1.00 47.60  ? 53  TRP C CE3 1 
ATOM 4542 C CZ2 . TRP C 3 55  ? 3.964   -52.631 -25.171 1.00 50.46  ? 53  TRP C CZ2 1 
ATOM 4543 C CZ3 . TRP C 3 55  ? 6.209   -52.278 -24.356 1.00 49.71  ? 53  TRP C CZ3 1 
ATOM 4544 C CH2 . TRP C 3 55  ? 5.265   -52.275 -25.391 1.00 50.20  ? 53  TRP C CH2 1 
ATOM 4545 N N   . THR C 3 56  ? 4.037   -50.262 -20.638 1.00 53.83  ? 54  THR C N   1 
ATOM 4546 C CA  . THR C 3 56  ? 4.482   -49.020 -21.260 1.00 54.87  ? 54  THR C CA  1 
ATOM 4547 C C   . THR C 3 56  ? 4.721   -47.905 -20.251 1.00 57.35  ? 54  THR C C   1 
ATOM 4548 O O   . THR C 3 56  ? 5.272   -46.863 -20.623 1.00 58.93  ? 54  THR C O   1 
ATOM 4549 C CB  . THR C 3 56  ? 3.470   -48.533 -22.309 1.00 52.88  ? 54  THR C CB  1 
ATOM 4550 O OG1 . THR C 3 56  ? 2.228   -48.210 -21.673 1.00 52.79  ? 54  THR C OG1 1 
ATOM 4551 C CG2 . THR C 3 56  ? 3.233   -49.596 -23.371 1.00 51.45  ? 54  THR C CG2 1 
ATOM 4552 N N   . GLY C 3 57  ? 4.324   -48.096 -18.994 1.00 50.98  ? 55  GLY C N   1 
ATOM 4553 C CA  . GLY C 3 57  ? 4.501   -47.073 -17.983 1.00 50.44  ? 55  GLY C CA  1 
ATOM 4554 C C   . GLY C 3 57  ? 3.539   -45.913 -18.066 1.00 54.80  ? 55  GLY C C   1 
ATOM 4555 O O   . GLY C 3 57  ? 3.866   -44.818 -17.596 1.00 58.21  ? 55  GLY C O   1 
ATOM 4556 N N   . THR C 3 58  ? 2.354   -46.113 -18.650 1.00 55.50  ? 56  THR C N   1 
ATOM 4557 C CA  . THR C 3 58  ? 1.377   -45.044 -18.805 1.00 52.60  ? 56  THR C CA  1 
ATOM 4558 C C   . THR C 3 58  ? 0.165   -45.184 -17.898 1.00 53.73  ? 56  THR C C   1 
ATOM 4559 O O   . THR C 3 58  ? -0.489  -44.175 -17.613 1.00 52.69  ? 56  THR C O   1 
ATOM 4560 C CB  . THR C 3 58  ? 0.882   -44.972 -20.257 1.00 54.84  ? 56  THR C CB  1 
ATOM 4561 O OG1 . THR C 3 58  ? 0.081   -46.124 -20.543 1.00 53.56  ? 56  THR C OG1 1 
ATOM 4562 C CG2 . THR C 3 58  ? 2.056   -44.918 -21.225 1.00 56.45  ? 56  THR C CG2 1 
ATOM 4563 N N   . THR C 3 59  ? -0.157  -46.395 -17.452 1.00 55.20  ? 57  THR C N   1 
ATOM 4564 C CA  . THR C 3 59  ? -1.308  -46.646 -16.596 1.00 55.57  ? 57  THR C CA  1 
ATOM 4565 C C   . THR C 3 59  ? -0.838  -47.289 -15.300 1.00 58.07  ? 57  THR C C   1 
ATOM 4566 O O   . THR C 3 59  ? -0.129  -48.302 -15.327 1.00 52.54  ? 57  THR C O   1 
ATOM 4567 C CB  . THR C 3 59  ? -2.333  -47.547 -17.293 1.00 57.23  ? 57  THR C CB  1 
ATOM 4568 O OG1 . THR C 3 59  ? -2.464  -47.157 -18.666 1.00 62.56  ? 57  THR C OG1 1 
ATOM 4569 C CG2 . THR C 3 59  ? -3.690  -47.439 -16.612 1.00 57.80  ? 57  THR C CG2 1 
ATOM 4570 N N   . THR C 3 60  ? -1.224  -46.695 -14.174 1.00 65.59  ? 58  THR C N   1 
ATOM 4571 C CA  . THR C 3 60  ? -0.934  -47.226 -12.851 1.00 56.46  ? 58  THR C CA  1 
ATOM 4572 C C   . THR C 3 60  ? -2.227  -47.686 -12.193 1.00 58.06  ? 58  THR C C   1 
ATOM 4573 O O   . THR C 3 60  ? -3.259  -47.014 -12.289 1.00 58.04  ? 58  THR C O   1 
ATOM 4574 C CB  . THR C 3 60  ? -0.245  -46.184 -11.964 1.00 55.39  ? 58  THR C CB  1 
ATOM 4575 O OG1 . THR C 3 60  ? -1.003  -44.967 -11.967 1.00 66.29  ? 58  THR C OG1 1 
ATOM 4576 C CG2 . THR C 3 60  ? 1.160   -45.901 -12.466 1.00 50.54  ? 58  THR C CG2 1 
ATOM 4577 N N   . TYR C 3 61  ? -2.163  -48.832 -11.524 1.00 56.91  ? 59  TYR C N   1 
ATOM 4578 C CA  . TYR C 3 61  ? -3.315  -49.448 -10.883 1.00 52.41  ? 59  TYR C CA  1 
ATOM 4579 C C   . TYR C 3 61  ? -3.063  -49.533 -9.385  1.00 59.00  ? 59  TYR C C   1 
ATOM 4580 O O   . TYR C 3 61  ? -1.960  -49.878 -8.953  1.00 59.66  ? 59  TYR C O   1 
ATOM 4581 C CB  . TYR C 3 61  ? -3.596  -50.851 -11.456 1.00 53.17  ? 59  TYR C CB  1 
ATOM 4582 C CG  . TYR C 3 61  ? -3.696  -50.925 -12.973 1.00 57.17  ? 59  TYR C CG  1 
ATOM 4583 C CD1 . TYR C 3 61  ? -2.592  -50.684 -13.787 1.00 57.86  ? 59  TYR C CD1 1 
ATOM 4584 C CD2 . TYR C 3 61  ? -4.904  -51.222 -13.588 1.00 61.82  ? 59  TYR C CD2 1 
ATOM 4585 C CE1 . TYR C 3 61  ? -2.690  -50.745 -15.166 1.00 61.08  ? 59  TYR C CE1 1 
ATOM 4586 C CE2 . TYR C 3 61  ? -5.011  -51.285 -14.967 1.00 64.26  ? 59  TYR C CE2 1 
ATOM 4587 C CZ  . TYR C 3 61  ? -3.903  -51.046 -15.751 1.00 63.87  ? 59  TYR C CZ  1 
ATOM 4588 O OH  . TYR C 3 61  ? -4.010  -51.109 -17.123 1.00 60.35  ? 59  TYR C OH  1 
ATOM 4589 N N   . TYR C 3 62  ? -4.084  -49.210 -8.592  1.00 61.70  ? 60  TYR C N   1 
ATOM 4590 C CA  . TYR C 3 62  ? -3.957  -49.177 -7.143  1.00 59.50  ? 60  TYR C CA  1 
ATOM 4591 C C   . TYR C 3 62  ? -5.133  -49.892 -6.494  1.00 62.37  ? 60  TYR C C   1 
ATOM 4592 O O   . TYR C 3 62  ? -6.240  -49.926 -7.038  1.00 64.38  ? 60  TYR C O   1 
ATOM 4593 C CB  . TYR C 3 62  ? -3.890  -47.739 -6.612  1.00 63.09  ? 60  TYR C CB  1 
ATOM 4594 C CG  . TYR C 3 62  ? -2.641  -46.983 -7.001  1.00 62.13  ? 60  TYR C CG  1 
ATOM 4595 C CD1 . TYR C 3 62  ? -1.450  -47.170 -6.312  1.00 61.70  ? 60  TYR C CD1 1 
ATOM 4596 C CD2 . TYR C 3 62  ? -2.656  -46.070 -8.048  1.00 57.30  ? 60  TYR C CD2 1 
ATOM 4597 C CE1 . TYR C 3 62  ? -0.308  -46.476 -6.660  1.00 59.91  ? 60  TYR C CE1 1 
ATOM 4598 C CE2 . TYR C 3 62  ? -1.519  -45.372 -8.403  1.00 57.41  ? 60  TYR C CE2 1 
ATOM 4599 C CZ  . TYR C 3 62  ? -0.348  -45.579 -7.706  1.00 58.27  ? 60  TYR C CZ  1 
ATOM 4600 O OH  . TYR C 3 62  ? 0.788   -44.887 -8.056  1.00 60.33  ? 60  TYR C OH  1 
ATOM 4601 N N   . ALA C 3 63  ? -4.879  -50.459 -5.318  1.00 64.01  ? 61  ALA C N   1 
ATOM 4602 C CA  . ALA C 3 63  ? -5.940  -51.035 -4.507  1.00 64.76  ? 61  ALA C CA  1 
ATOM 4603 C C   . ALA C 3 63  ? -6.635  -49.941 -3.705  1.00 69.51  ? 61  ALA C C   1 
ATOM 4604 O O   . ALA C 3 63  ? -6.056  -48.890 -3.417  1.00 74.49  ? 61  ALA C O   1 
ATOM 4605 C CB  . ALA C 3 63  ? -5.383  -52.105 -3.569  1.00 62.66  ? 61  ALA C CB  1 
ATOM 4606 N N   . ASP C 3 64  ? -7.893  -50.200 -3.341  1.00 69.16  ? 62  ASP C N   1 
ATOM 4607 C CA  . ASP C 3 64  ? -8.690  -49.175 -2.672  1.00 72.35  ? 62  ASP C CA  1 
ATOM 4608 C C   . ASP C 3 64  ? -8.114  -48.804 -1.311  1.00 68.38  ? 62  ASP C C   1 
ATOM 4609 O O   . ASP C 3 64  ? -8.255  -47.657 -0.871  1.00 69.95  ? 62  ASP C O   1 
ATOM 4610 C CB  . ASP C 3 64  ? -10.139 -49.644 -2.532  1.00 76.31  ? 62  ASP C CB  1 
ATOM 4611 C CG  . ASP C 3 64  ? -10.706 -50.176 -3.836  1.00 80.01  ? 62  ASP C CG  1 
ATOM 4612 O OD1 . ASP C 3 64  ? -10.181 -51.189 -4.345  1.00 81.31  ? 62  ASP C OD1 1 
ATOM 4613 O OD2 . ASP C 3 64  ? -11.674 -49.578 -4.352  1.00 79.49  ? 62  ASP C OD2 1 
ATOM 4614 N N   . SER C 3 65  ? -7.459  -49.748 -0.633  1.00 70.22  ? 63  SER C N   1 
ATOM 4615 C CA  . SER C 3 65  ? -6.864  -49.465 0.667   1.00 71.60  ? 63  SER C CA  1 
ATOM 4616 C C   . SER C 3 65  ? -5.589  -48.636 0.568   1.00 72.84  ? 63  SER C C   1 
ATOM 4617 O O   . SER C 3 65  ? -5.177  -48.037 1.568   1.00 77.95  ? 63  SER C O   1 
ATOM 4618 C CB  . SER C 3 65  ? -6.573  -50.774 1.406   1.00 69.89  ? 63  SER C CB  1 
ATOM 4619 O OG  . SER C 3 65  ? -5.473  -51.458 0.831   1.00 65.56  ? 63  SER C OG  1 
ATOM 4620 N N   . VAL C 3 66  ? -4.964  -48.579 -0.606  1.00 73.57  ? 64  VAL C N   1 
ATOM 4621 C CA  . VAL C 3 66  ? -3.721  -47.847 -0.813  1.00 71.32  ? 64  VAL C CA  1 
ATOM 4622 C C   . VAL C 3 66  ? -3.894  -46.716 -1.827  1.00 74.08  ? 64  VAL C C   1 
ATOM 4623 O O   . VAL C 3 66  ? -2.914  -46.148 -2.294  1.00 75.80  ? 64  VAL C O   1 
ATOM 4624 C CB  . VAL C 3 66  ? -2.585  -48.803 -1.226  1.00 73.70  ? 64  VAL C CB  1 
ATOM 4625 C CG1 . VAL C 3 66  ? -2.579  -50.033 -0.337  1.00 76.70  ? 64  VAL C CG1 1 
ATOM 4626 C CG2 . VAL C 3 66  ? -2.752  -49.224 -2.676  1.00 70.69  ? 64  VAL C CG2 1 
ATOM 4627 N N   . LYS C 3 67  ? -5.144  -46.367 -2.144  1.00 76.61  ? 65  LYS C N   1 
ATOM 4628 C CA  . LYS C 3 67  ? -5.419  -45.438 -3.238  1.00 73.36  ? 65  LYS C CA  1 
ATOM 4629 C C   . LYS C 3 67  ? -4.754  -44.084 -3.013  1.00 72.03  ? 65  LYS C C   1 
ATOM 4630 O O   . LYS C 3 67  ? -4.064  -43.562 -3.897  1.00 72.48  ? 65  LYS C O   1 
ATOM 4631 C CB  . LYS C 3 67  ? -6.930  -45.271 -3.408  1.00 73.88  ? 65  LYS C CB  1 
ATOM 4632 C CG  . LYS C 3 67  ? -7.412  -45.325 -4.852  1.00 78.16  ? 65  LYS C CG  1 
ATOM 4633 C CD  . LYS C 3 67  ? -7.499  -46.758 -5.357  1.00 74.81  ? 65  LYS C CD  1 
ATOM 4634 C CE  . LYS C 3 67  ? -7.987  -46.817 -6.796  1.00 72.53  ? 65  LYS C CE  1 
ATOM 4635 N NZ  . LYS C 3 67  ? -8.599  -48.137 -7.123  1.00 67.46  ? 65  LYS C NZ  1 
ATOM 4636 N N   . GLY C 3 68  ? -4.948  -43.499 -1.835  1.00 65.72  ? 66  GLY C N   1 
ATOM 4637 C CA  . GLY C 3 68  ? -4.491  -42.145 -1.596  1.00 69.82  ? 66  GLY C CA  1 
ATOM 4638 C C   . GLY C 3 68  ? -3.066  -42.023 -1.098  1.00 78.86  ? 66  GLY C C   1 
ATOM 4639 O O   . GLY C 3 68  ? -2.381  -41.044 -1.407  1.00 80.88  ? 66  GLY C O   1 
ATOM 4640 N N   . ARG C 3 69  ? -2.602  -43.009 -0.331  1.00 85.08  ? 67  ARG C N   1 
ATOM 4641 C CA  . ARG C 3 69  ? -1.319  -42.895 0.350   1.00 86.40  ? 67  ARG C CA  1 
ATOM 4642 C C   . ARG C 3 69  ? -0.157  -43.514 -0.414  1.00 85.78  ? 67  ARG C C   1 
ATOM 4643 O O   . ARG C 3 69  ? 0.999   -43.214 -0.097  1.00 88.16  ? 67  ARG C O   1 
ATOM 4644 C CB  . ARG C 3 69  ? -1.402  -43.536 1.739   1.00 83.37  ? 67  ARG C CB  1 
ATOM 4645 C CG  . ARG C 3 69  ? -2.811  -43.681 2.281   1.00 82.04  ? 67  ARG C CG  1 
ATOM 4646 C CD  . ARG C 3 69  ? -2.801  -44.366 3.636   1.00 89.66  ? 67  ARG C CD  1 
ATOM 4647 N NE  . ARG C 3 69  ? -2.065  -45.623 3.608   1.00 82.41  ? 67  ARG C NE  1 
ATOM 4648 C CZ  . ARG C 3 69  ? -2.633  -46.817 3.507   1.00 81.07  ? 67  ARG C CZ  1 
ATOM 4649 N NH1 . ARG C 3 69  ? -3.946  -46.950 3.418   1.00 79.87  ? 67  ARG C NH1 1 
ATOM 4650 N NH2 . ARG C 3 69  ? -1.865  -47.902 3.495   1.00 92.09  ? 67  ARG C NH2 1 
ATOM 4651 N N   . PHE C 3 70  ? -0.426  -44.360 -1.403  1.00 83.22  ? 68  PHE C N   1 
ATOM 4652 C CA  . PHE C 3 70  ? 0.622   -45.067 -2.123  1.00 76.90  ? 68  PHE C CA  1 
ATOM 4653 C C   . PHE C 3 70  ? 0.842   -44.449 -3.498  1.00 79.59  ? 68  PHE C C   1 
ATOM 4654 O O   . PHE C 3 70  ? -0.052  -43.821 -4.070  1.00 86.35  ? 68  PHE C O   1 
ATOM 4655 C CB  . PHE C 3 70  ? 0.273   -46.548 -2.271  1.00 83.31  ? 68  PHE C CB  1 
ATOM 4656 C CG  . PHE C 3 70  ? 0.652   -47.385 -1.082  1.00 88.81  ? 68  PHE C CG  1 
ATOM 4657 C CD1 . PHE C 3 70  ? 0.192   -47.063 0.185   1.00 86.64  ? 68  PHE C CD1 1 
ATOM 4658 C CD2 . PHE C 3 70  ? 1.450   -48.507 -1.234  1.00 88.58  ? 68  PHE C CD2 1 
ATOM 4659 C CE1 . PHE C 3 70  ? 0.532   -47.837 1.279   1.00 83.56  ? 68  PHE C CE1 1 
ATOM 4660 C CE2 . PHE C 3 70  ? 1.792   -49.285 -0.145  1.00 84.81  ? 68  PHE C CE2 1 
ATOM 4661 C CZ  . PHE C 3 70  ? 1.332   -48.949 1.113   1.00 82.43  ? 68  PHE C CZ  1 
ATOM 4662 N N   . THR C 3 71  ? 2.050   -44.640 -4.024  1.00 68.32  ? 69  THR C N   1 
ATOM 4663 C CA  . THR C 3 71  ? 2.411   -44.137 -5.346  1.00 62.09  ? 69  THR C CA  1 
ATOM 4664 C C   . THR C 3 71  ? 3.462   -45.058 -5.942  1.00 59.93  ? 69  THR C C   1 
ATOM 4665 O O   . THR C 3 71  ? 4.537   -45.228 -5.359  1.00 60.79  ? 69  THR C O   1 
ATOM 4666 C CB  . THR C 3 71  ? 2.938   -42.702 -5.273  1.00 63.86  ? 69  THR C CB  1 
ATOM 4667 O OG1 . THR C 3 71  ? 1.932   -41.845 -4.718  1.00 75.47  ? 69  THR C OG1 1 
ATOM 4668 C CG2 . THR C 3 71  ? 3.321   -42.201 -6.660  1.00 59.64  ? 69  THR C CG2 1 
ATOM 4669 N N   . ILE C 3 72  ? 3.155   -45.650 -7.092  1.00 58.71  ? 70  ILE C N   1 
ATOM 4670 C CA  . ILE C 3 72  ? 4.087   -46.523 -7.795  1.00 54.89  ? 70  ILE C CA  1 
ATOM 4671 C C   . ILE C 3 72  ? 4.702   -45.749 -8.952  1.00 56.93  ? 70  ILE C C   1 
ATOM 4672 O O   . ILE C 3 72  ? 4.050   -44.891 -9.563  1.00 60.82  ? 70  ILE C O   1 
ATOM 4673 C CB  . ILE C 3 72  ? 3.390   -47.811 -8.281  1.00 54.27  ? 70  ILE C CB  1 
ATOM 4674 C CG1 . ILE C 3 72  ? 4.418   -48.815 -8.807  1.00 51.43  ? 70  ILE C CG1 1 
ATOM 4675 C CG2 . ILE C 3 72  ? 2.343   -47.503 -9.342  1.00 51.76  ? 70  ILE C CG2 1 
ATOM 4676 C CD1 . ILE C 3 72  ? 3.812   -50.112 -9.275  1.00 52.22  ? 70  ILE C CD1 1 
ATOM 4677 N N   . SER C 3 73  ? 5.971   -46.033 -9.239  1.00 53.82  ? 71  SER C N   1 
ATOM 4678 C CA  . SER C 3 73  ? 6.684   -45.382 -10.326 1.00 51.23  ? 71  SER C CA  1 
ATOM 4679 C C   . SER C 3 73  ? 7.772   -46.322 -10.824 1.00 57.46  ? 71  SER C C   1 
ATOM 4680 O O   . SER C 3 73  ? 8.073   -47.343 -10.201 1.00 60.79  ? 71  SER C O   1 
ATOM 4681 C CB  . SER C 3 73  ? 7.283   -44.042 -9.884  1.00 50.46  ? 71  SER C CB  1 
ATOM 4682 O OG  . SER C 3 73  ? 8.012   -44.184 -8.677  1.00 60.98  ? 71  SER C OG  1 
ATOM 4683 N N   . ARG C 3 74  ? 8.365   -45.964 -11.962 1.00 59.80  ? 72  ARG C N   1 
ATOM 4684 C CA  . ARG C 3 74  ? 9.416   -46.780 -12.557 1.00 61.45  ? 72  ARG C CA  1 
ATOM 4685 C C   . ARG C 3 74  ? 10.367  -45.899 -13.349 1.00 61.66  ? 72  ARG C C   1 
ATOM 4686 O O   . ARG C 3 74  ? 9.926   -45.057 -14.136 1.00 67.69  ? 72  ARG C O   1 
ATOM 4687 C CB  . ARG C 3 74  ? 8.828   -47.864 -13.467 1.00 60.37  ? 72  ARG C CB  1 
ATOM 4688 C CG  . ARG C 3 74  ? 9.870   -48.809 -14.040 1.00 64.64  ? 72  ARG C CG  1 
ATOM 4689 C CD  . ARG C 3 74  ? 9.602   -49.126 -15.499 1.00 68.26  ? 72  ARG C CD  1 
ATOM 4690 N NE  . ARG C 3 74  ? 10.139  -50.432 -15.864 1.00 61.86  ? 72  ARG C NE  1 
ATOM 4691 C CZ  . ARG C 3 74  ? 9.530   -51.296 -16.664 1.00 59.82  ? 72  ARG C CZ  1 
ATOM 4692 N NH1 . ARG C 3 74  ? 8.355   -51.024 -17.209 1.00 57.18  ? 72  ARG C NH1 1 
ATOM 4693 N NH2 . ARG C 3 74  ? 10.112  -52.464 -16.920 1.00 58.96  ? 72  ARG C NH2 1 
ATOM 4694 N N   . ASP C 3 75  ? 11.666  -46.098 -13.139 1.00 66.56  ? 73  ASP C N   1 
ATOM 4695 C CA  . ASP C 3 75  ? 12.705  -45.447 -13.927 1.00 71.51  ? 73  ASP C CA  1 
ATOM 4696 C C   . ASP C 3 75  ? 13.193  -46.448 -14.968 1.00 75.95  ? 73  ASP C C   1 
ATOM 4697 O O   . ASP C 3 75  ? 13.854  -47.434 -14.628 1.00 74.79  ? 73  ASP C O   1 
ATOM 4698 C CB  . ASP C 3 75  ? 13.853  -44.971 -13.040 1.00 67.13  ? 73  ASP C CB  1 
ATOM 4699 C CG  . ASP C 3 75  ? 14.986  -44.345 -13.835 1.00 73.24  ? 73  ASP C CG  1 
ATOM 4700 O OD1 . ASP C 3 75  ? 14.751  -43.918 -14.986 1.00 72.94  ? 73  ASP C OD1 1 
ATOM 4701 O OD2 . ASP C 3 75  ? 16.117  -44.285 -13.309 1.00 77.48  ? 73  ASP C OD2 1 
ATOM 4702 N N   . ASP C 3 76  ? 12.867  -46.193 -16.235 1.00 84.50  ? 74  ASP C N   1 
ATOM 4703 C CA  . ASP C 3 76  ? 13.222  -47.108 -17.311 1.00 79.24  ? 74  ASP C CA  1 
ATOM 4704 C C   . ASP C 3 76  ? 14.698  -47.052 -17.683 1.00 77.81  ? 74  ASP C C   1 
ATOM 4705 O O   . ASP C 3 76  ? 15.168  -47.932 -18.412 1.00 80.27  ? 74  ASP C O   1 
ATOM 4706 C CB  . ASP C 3 76  ? 12.362  -46.820 -18.543 1.00 75.29  ? 74  ASP C CB  1 
ATOM 4707 C CG  . ASP C 3 76  ? 10.896  -46.647 -18.198 1.00 76.81  ? 74  ASP C CG  1 
ATOM 4708 O OD1 . ASP C 3 76  ? 10.563  -45.683 -17.477 1.00 78.00  ? 74  ASP C OD1 1 
ATOM 4709 O OD2 . ASP C 3 76  ? 10.076  -47.482 -18.635 1.00 80.27  ? 74  ASP C OD2 1 
ATOM 4710 N N   . VAL C 3 77  ? 15.438  -46.051 -17.206 1.00 78.38  ? 75  VAL C N   1 
ATOM 4711 C CA  . VAL C 3 77  ? 16.873  -45.996 -17.465 1.00 78.66  ? 75  VAL C CA  1 
ATOM 4712 C C   . VAL C 3 77  ? 17.614  -46.995 -16.585 1.00 75.98  ? 75  VAL C C   1 
ATOM 4713 O O   . VAL C 3 77  ? 18.448  -47.770 -17.066 1.00 74.59  ? 75  VAL C O   1 
ATOM 4714 C CB  . VAL C 3 77  ? 17.402  -44.564 -17.261 1.00 79.73  ? 75  VAL C CB  1 
ATOM 4715 C CG1 . VAL C 3 77  ? 18.844  -44.458 -17.734 1.00 77.34  ? 75  VAL C CG1 1 
ATOM 4716 C CG2 . VAL C 3 77  ? 16.519  -43.562 -17.988 1.00 79.79  ? 75  VAL C CG2 1 
ATOM 4717 N N   . LYS C 3 78  ? 17.325  -46.988 -15.284 1.00 73.84  ? 76  LYS C N   1 
ATOM 4718 C CA  . LYS C 3 78  ? 17.914  -47.937 -14.350 1.00 72.87  ? 76  LYS C CA  1 
ATOM 4719 C C   . LYS C 3 78  ? 17.084  -49.203 -14.185 1.00 72.48  ? 76  LYS C C   1 
ATOM 4720 O O   . LYS C 3 78  ? 17.525  -50.124 -13.489 1.00 75.67  ? 76  LYS C O   1 
ATOM 4721 C CB  . LYS C 3 78  ? 18.114  -47.279 -12.979 1.00 73.31  ? 76  LYS C CB  1 
ATOM 4722 C CG  . LYS C 3 78  ? 19.455  -46.574 -12.811 1.00 76.92  ? 76  LYS C CG  1 
ATOM 4723 C CD  . LYS C 3 78  ? 19.596  -45.955 -11.425 1.00 72.74  ? 76  LYS C CD  1 
ATOM 4724 C CE  . LYS C 3 78  ? 19.044  -44.537 -11.386 1.00 64.64  ? 76  LYS C CE  1 
ATOM 4725 N NZ  . LYS C 3 78  ? 19.262  -43.885 -10.062 1.00 57.46  ? 76  LYS C NZ  1 
ATOM 4726 N N   . ASN C 3 79  ? 15.902  -49.266 -14.803 1.00 71.89  ? 77  ASN C N   1 
ATOM 4727 C CA  . ASN C 3 79  ? 15.019  -50.433 -14.746 1.00 70.54  ? 77  ASN C CA  1 
ATOM 4728 C C   . ASN C 3 79  ? 14.704  -50.817 -13.298 1.00 72.30  ? 77  ASN C C   1 
ATOM 4729 O O   . ASN C 3 79  ? 14.935  -51.944 -12.856 1.00 74.86  ? 77  ASN C O   1 
ATOM 4730 C CB  . ASN C 3 79  ? 15.623  -51.614 -15.514 1.00 66.82  ? 77  ASN C CB  1 
ATOM 4731 C CG  . ASN C 3 79  ? 15.567  -51.422 -17.016 1.00 66.67  ? 77  ASN C CG  1 
ATOM 4732 O OD1 . ASN C 3 79  ? 14.507  -51.148 -17.580 1.00 64.40  ? 77  ASN C OD1 1 
ATOM 4733 N ND2 . ASN C 3 79  ? 16.710  -51.570 -17.675 1.00 63.78  ? 77  ASN C ND2 1 
ATOM 4734 N N   . MET C 3 80  ? 14.159  -49.851 -12.563 1.00 77.21  ? 78  MET C N   1 
ATOM 4735 C CA  . MET C 3 80  ? 13.851  -50.023 -11.149 1.00 73.93  ? 78  MET C CA  1 
ATOM 4736 C C   . MET C 3 80  ? 12.461  -49.474 -10.871 1.00 71.42  ? 78  MET C C   1 
ATOM 4737 O O   . MET C 3 80  ? 12.128  -48.369 -11.310 1.00 77.51  ? 78  MET C O   1 
ATOM 4738 C CB  . MET C 3 80  ? 14.887  -49.312 -10.272 1.00 79.08  ? 78  MET C CB  1 
ATOM 4739 C CG  . MET C 3 80  ? 16.213  -50.042 -10.163 1.00 75.50  ? 78  MET C CG  1 
ATOM 4740 S SD  . MET C 3 80  ? 17.275  -49.342 -8.888  1.00 85.28  ? 78  MET C SD  1 
ATOM 4741 C CE  . MET C 3 80  ? 16.174  -49.364 -7.479  1.00 75.66  ? 78  MET C CE  1 
ATOM 4742 N N   . VAL C 3 81  ? 11.658  -50.241 -10.143 1.00 61.02  ? 79  VAL C N   1 
ATOM 4743 C CA  . VAL C 3 81  ? 10.299  -49.847 -9.792  1.00 58.67  ? 79  VAL C CA  1 
ATOM 4744 C C   . VAL C 3 81  ? 10.282  -49.425 -8.332  1.00 60.00  ? 79  VAL C C   1 
ATOM 4745 O O   . VAL C 3 81  ? 10.885  -50.083 -7.474  1.00 60.53  ? 79  VAL C O   1 
ATOM 4746 C CB  . VAL C 3 81  ? 9.303   -50.991 -10.052 1.00 59.85  ? 79  VAL C CB  1 
ATOM 4747 C CG1 . VAL C 3 81  ? 7.910   -50.615 -9.567  1.00 59.13  ? 79  VAL C CG1 1 
ATOM 4748 C CG2 . VAL C 3 81  ? 9.288   -51.337 -11.523 1.00 62.74  ? 79  VAL C CG2 1 
ATOM 4749 N N   . TYR C 3 82  ? 9.595   -48.326 -8.045  1.00 59.36  ? 80  TYR C N   1 
ATOM 4750 C CA  . TYR C 3 82  ? 9.547   -47.761 -6.709  1.00 57.18  ? 80  TYR C CA  1 
ATOM 4751 C C   . TYR C 3 82  ? 8.114   -47.754 -6.197  1.00 56.46  ? 80  TYR C C   1 
ATOM 4752 O O   . TYR C 3 82  ? 7.157   -47.727 -6.976  1.00 57.80  ? 80  TYR C O   1 
ATOM 4753 C CB  . TYR C 3 82  ? 10.118  -46.339 -6.693  1.00 56.87  ? 80  TYR C CB  1 
ATOM 4754 C CG  . TYR C 3 82  ? 11.535  -46.243 -7.216  1.00 58.55  ? 80  TYR C CG  1 
ATOM 4755 C CD1 . TYR C 3 82  ? 12.607  -46.683 -6.452  1.00 58.03  ? 80  TYR C CD1 1 
ATOM 4756 C CD2 . TYR C 3 82  ? 11.800  -45.716 -8.473  1.00 59.57  ? 80  TYR C CD2 1 
ATOM 4757 C CE1 . TYR C 3 82  ? 13.904  -46.598 -6.924  1.00 62.01  ? 80  TYR C CE1 1 
ATOM 4758 C CE2 . TYR C 3 82  ? 13.094  -45.627 -8.954  1.00 58.99  ? 80  TYR C CE2 1 
ATOM 4759 C CZ  . TYR C 3 82  ? 14.142  -46.070 -8.175  1.00 61.72  ? 80  TYR C CZ  1 
ATOM 4760 O OH  . TYR C 3 82  ? 15.431  -45.985 -8.646  1.00 67.87  ? 80  TYR C OH  1 
ATOM 4761 N N   . LEU C 3 83  ? 7.977   -47.786 -4.872  1.00 59.02  ? 81  LEU C N   1 
ATOM 4762 C CA  . LEU C 3 83  ? 6.672   -47.698 -4.216  1.00 58.13  ? 81  LEU C CA  1 
ATOM 4763 C C   . LEU C 3 83  ? 6.814   -46.729 -3.047  1.00 62.82  ? 81  LEU C C   1 
ATOM 4764 O O   . LEU C 3 83  ? 7.281   -47.112 -1.970  1.00 67.17  ? 81  LEU C O   1 
ATOM 4765 C CB  . LEU C 3 83  ? 6.185   -49.067 -3.754  1.00 58.40  ? 81  LEU C CB  1 
ATOM 4766 C CG  . LEU C 3 83  ? 4.725   -49.139 -3.300  1.00 58.78  ? 81  LEU C CG  1 
ATOM 4767 C CD1 . LEU C 3 83  ? 3.773   -48.895 -4.464  1.00 56.95  ? 81  LEU C CD1 1 
ATOM 4768 C CD2 . LEU C 3 83  ? 4.434   -50.475 -2.634  1.00 57.84  ? 81  LEU C CD2 1 
ATOM 4769 N N   . GLN C 3 84  ? 6.420   -45.477 -3.266  1.00 57.62  ? 82  GLN C N   1 
ATOM 4770 C CA  . GLN C 3 84  ? 6.470   -44.463 -2.222  1.00 59.38  ? 82  GLN C CA  1 
ATOM 4771 C C   . GLN C 3 84  ? 5.291   -44.652 -1.275  1.00 64.05  ? 82  GLN C C   1 
ATOM 4772 O O   . GLN C 3 84  ? 4.132   -44.528 -1.686  1.00 66.99  ? 82  GLN C O   1 
ATOM 4773 C CB  . GLN C 3 84  ? 6.451   -43.065 -2.834  1.00 61.74  ? 82  GLN C CB  1 
ATOM 4774 C CG  . GLN C 3 84  ? 6.608   -41.943 -1.824  1.00 59.44  ? 82  GLN C CG  1 
ATOM 4775 C CD  . GLN C 3 84  ? 5.506   -40.905 -1.929  1.00 64.41  ? 82  GLN C CD  1 
ATOM 4776 O OE1 . GLN C 3 84  ? 4.323   -41.242 -2.011  1.00 67.96  ? 82  GLN C OE1 1 
ATOM 4777 N NE2 . GLN C 3 84  ? 5.889   -39.634 -1.934  1.00 61.22  ? 82  GLN C NE2 1 
ATOM 4778 N N   . MET C 3 85  ? 5.586   -44.948 -0.013  1.00 61.25  ? 83  MET C N   1 
ATOM 4779 C CA  . MET C 3 85  ? 4.575   -45.235 0.995   1.00 66.23  ? 83  MET C CA  1 
ATOM 4780 C C   . MET C 3 85  ? 4.458   -44.051 1.945   1.00 69.36  ? 83  MET C C   1 
ATOM 4781 O O   . MET C 3 85  ? 5.459   -43.614 2.522   1.00 71.54  ? 83  MET C O   1 
ATOM 4782 C CB  . MET C 3 85  ? 4.932   -46.503 1.773   1.00 72.76  ? 83  MET C CB  1 
ATOM 4783 C CG  . MET C 3 85  ? 4.842   -47.783 0.960   1.00 70.19  ? 83  MET C CG  1 
ATOM 4784 S SD  . MET C 3 85  ? 4.691   -49.253 1.991   1.00 71.84  ? 83  MET C SD  1 
ATOM 4785 C CE  . MET C 3 85  ? 6.346   -49.353 2.668   1.00 65.44  ? 83  MET C CE  1 
ATOM 4786 N N   . ASN C 3 86  ? 3.240   -43.540 2.108   1.00 72.27  ? 84  ASN C N   1 
ATOM 4787 C CA  . ASN C 3 86  ? 2.969   -42.408 2.982   1.00 75.15  ? 84  ASN C CA  1 
ATOM 4788 C C   . ASN C 3 86  ? 1.881   -42.777 3.979   1.00 76.08  ? 84  ASN C C   1 
ATOM 4789 O O   . ASN C 3 86  ? 1.013   -43.605 3.693   1.00 78.63  ? 84  ASN C O   1 
ATOM 4790 C CB  . ASN C 3 86  ? 2.536   -41.169 2.182   1.00 71.63  ? 84  ASN C CB  1 
ATOM 4791 C CG  . ASN C 3 86  ? 3.663   -40.583 1.358   1.00 68.66  ? 84  ASN C CG  1 
ATOM 4792 O OD1 . ASN C 3 86  ? 4.834   -40.898 1.574   1.00 71.21  ? 84  ASN C OD1 1 
ATOM 4793 N ND2 . ASN C 3 86  ? 3.314   -39.730 0.402   1.00 67.71  ? 84  ASN C ND2 1 
ATOM 4794 N N   . SER C 3 87  ? 1.938   -42.148 5.153   1.00 75.77  ? 85  SER C N   1 
ATOM 4795 C CA  . SER C 3 87  ? 0.949   -42.336 6.215   1.00 73.88  ? 85  SER C CA  1 
ATOM 4796 C C   . SER C 3 87  ? 0.733   -43.821 6.503   1.00 78.01  ? 85  SER C C   1 
ATOM 4797 O O   . SER C 3 87  ? -0.351  -44.377 6.305   1.00 79.76  ? 85  SER C O   1 
ATOM 4798 C CB  . SER C 3 87  ? -0.369  -41.644 5.863   1.00 75.31  ? 85  SER C CB  1 
ATOM 4799 O OG  . SER C 3 87  ? -0.137  -40.345 5.353   1.00 83.50  ? 85  SER C OG  1 
ATOM 4800 N N   . LEU C 3 88  ? 1.801   -44.459 6.977   1.00 81.22  ? 86  LEU C N   1 
ATOM 4801 C CA  . LEU C 3 88  ? 1.780   -45.896 7.219   1.00 77.88  ? 86  LEU C CA  1 
ATOM 4802 C C   . LEU C 3 88  ? 0.826   -46.219 8.363   1.00 83.78  ? 86  LEU C C   1 
ATOM 4803 O O   . LEU C 3 88  ? 0.986   -45.716 9.478   1.00 82.58  ? 86  LEU C O   1 
ATOM 4804 C CB  . LEU C 3 88  ? 3.189   -46.406 7.524   1.00 77.58  ? 86  LEU C CB  1 
ATOM 4805 C CG  . LEU C 3 88  ? 4.019   -46.851 6.314   1.00 70.90  ? 86  LEU C CG  1 
ATOM 4806 C CD1 . LEU C 3 88  ? 3.233   -47.807 5.433   1.00 66.40  ? 86  LEU C CD1 1 
ATOM 4807 C CD2 . LEU C 3 88  ? 4.505   -45.652 5.506   1.00 77.30  ? 86  LEU C CD2 1 
ATOM 4808 N N   . LYS C 3 89  ? -0.156  -47.053 8.079   1.00 86.60  ? 87  LYS C N   1 
ATOM 4809 C CA  . LYS C 3 89  ? -1.178  -47.489 8.994   1.00 81.73  ? 87  LYS C CA  1 
ATOM 4810 C C   . LYS C 3 89  ? -0.885  -48.918 9.457   1.00 82.08  ? 87  LYS C C   1 
ATOM 4811 O O   . LYS C 3 89  ? -0.090  -49.633 8.838   1.00 80.72  ? 87  LYS C O   1 
ATOM 4812 C CB  . LYS C 3 89  ? -2.536  -47.405 8.286   1.00 83.44  ? 87  LYS C CB  1 
ATOM 4813 C CG  . LYS C 3 89  ? -3.113  -45.994 8.229   1.00 84.46  ? 87  LYS C CG  1 
ATOM 4814 C CD  . LYS C 3 89  ? -4.196  -45.851 7.172   1.00 83.99  ? 87  LYS C CD  1 
ATOM 4815 C CE  . LYS C 3 89  ? -5.334  -46.821 7.419   1.00 85.52  ? 87  LYS C CE  1 
ATOM 4816 N NZ  . LYS C 3 89  ? -6.662  -46.159 7.330   1.00 80.35  ? 87  LYS C NZ  1 
ATOM 4817 N N   . PRO C 3 90  ? -1.507  -49.375 10.555  1.00 84.00  ? 88  PRO C N   1 
ATOM 4818 C CA  . PRO C 3 90  ? -1.142  -50.703 11.110  1.00 82.71  ? 88  PRO C CA  1 
ATOM 4819 C C   . PRO C 3 90  ? -1.450  -51.887 10.200  1.00 80.49  ? 88  PRO C C   1 
ATOM 4820 O O   . PRO C 3 90  ? -0.771  -52.912 10.321  1.00 78.49  ? 88  PRO C O   1 
ATOM 4821 C CB  . PRO C 3 90  ? -1.959  -50.771 12.411  1.00 77.05  ? 88  PRO C CB  1 
ATOM 4822 C CG  . PRO C 3 90  ? -3.163  -49.928 12.155  1.00 79.26  ? 88  PRO C CG  1 
ATOM 4823 C CD  . PRO C 3 90  ? -2.701  -48.811 11.236  1.00 82.99  ? 88  PRO C CD  1 
ATOM 4824 N N   . GLU C 3 91  ? -2.411  -51.774 9.283   1.00 84.19  ? 89  GLU C N   1 
ATOM 4825 C CA  . GLU C 3 91  ? -2.697  -52.857 8.352   1.00 76.77  ? 89  GLU C CA  1 
ATOM 4826 C C   . GLU C 3 91  ? -1.653  -52.987 7.249   1.00 77.26  ? 89  GLU C C   1 
ATOM 4827 O O   . GLU C 3 91  ? -1.762  -53.896 6.416   1.00 82.76  ? 89  GLU C O   1 
ATOM 4828 C CB  . GLU C 3 91  ? -4.085  -52.679 7.724   1.00 77.34  ? 89  GLU C CB  1 
ATOM 4829 C CG  . GLU C 3 91  ? -5.158  -52.209 8.695   1.00 87.21  ? 89  GLU C CG  1 
ATOM 4830 C CD  . GLU C 3 91  ? -5.367  -50.710 8.655   1.00 87.17  ? 89  GLU C CD  1 
ATOM 4831 O OE1 . GLU C 3 91  ? -4.365  -49.975 8.540   1.00 89.82  ? 89  GLU C OE1 1 
ATOM 4832 O OE2 . GLU C 3 91  ? -6.532  -50.269 8.761   1.00 88.84  ? 89  GLU C OE2 1 
ATOM 4833 N N   . ASP C 3 92  ? -0.656  -52.109 7.217   1.00 73.30  ? 90  ASP C N   1 
ATOM 4834 C CA  . ASP C 3 92  ? 0.404   -52.157 6.221   1.00 71.46  ? 90  ASP C CA  1 
ATOM 4835 C C   . ASP C 3 92  ? 1.588   -53.011 6.659   1.00 70.13  ? 90  ASP C C   1 
ATOM 4836 O O   . ASP C 3 92  ? 2.651   -52.938 6.034   1.00 70.06  ? 90  ASP C O   1 
ATOM 4837 C CB  . ASP C 3 92  ? 0.882   -50.742 5.888   1.00 74.92  ? 90  ASP C CB  1 
ATOM 4838 C CG  . ASP C 3 92  ? -0.239  -49.849 5.390   1.00 77.12  ? 90  ASP C CG  1 
ATOM 4839 O OD1 . ASP C 3 92  ? -1.365  -50.356 5.200   1.00 78.18  ? 90  ASP C OD1 1 
ATOM 4840 O OD2 . ASP C 3 92  ? 0.004   -48.638 5.196   1.00 74.29  ? 90  ASP C OD2 1 
ATOM 4841 N N   . THR C 3 93  ? 1.431   -53.814 7.709   1.00 70.32  ? 91  THR C N   1 
ATOM 4842 C CA  . THR C 3 93  ? 2.501   -54.679 8.202   1.00 65.22  ? 91  THR C CA  1 
ATOM 4843 C C   . THR C 3 93  ? 2.438   -55.993 7.434   1.00 68.74  ? 91  THR C C   1 
ATOM 4844 O O   . THR C 3 93  ? 1.597   -56.851 7.715   1.00 72.15  ? 91  THR C O   1 
ATOM 4845 C CB  . THR C 3 93  ? 2.364   -54.908 9.702   1.00 67.37  ? 91  THR C CB  1 
ATOM 4846 O OG1 . THR C 3 93  ? 1.040   -55.369 9.999   1.00 72.12  ? 91  THR C OG1 1 
ATOM 4847 C CG2 . THR C 3 93  ? 2.613   -53.618 10.457  1.00 70.52  ? 91  THR C CG2 1 
ATOM 4848 N N   . ALA C 3 94  ? 3.331   -56.155 6.460   1.00 68.16  ? 92  ALA C N   1 
ATOM 4849 C CA  . ALA C 3 94  ? 3.340   -57.350 5.629   1.00 64.39  ? 92  ALA C CA  1 
ATOM 4850 C C   . ALA C 3 94  ? 4.684   -57.452 4.925   1.00 62.58  ? 92  ALA C C   1 
ATOM 4851 O O   . ALA C 3 94  ? 5.531   -56.561 5.022   1.00 60.35  ? 92  ALA C O   1 
ATOM 4852 C CB  . ALA C 3 94  ? 2.191   -57.336 4.615   1.00 61.19  ? 92  ALA C CB  1 
ATOM 4853 N N   . VAL C 3 95  ? 4.869   -58.562 4.220   1.00 62.84  ? 93  VAL C N   1 
ATOM 4854 C CA  . VAL C 3 95  ? 6.032   -58.759 3.364   1.00 59.46  ? 93  VAL C CA  1 
ATOM 4855 C C   . VAL C 3 95  ? 5.657   -58.282 1.968   1.00 60.87  ? 93  VAL C C   1 
ATOM 4856 O O   . VAL C 3 95  ? 4.724   -58.811 1.353   1.00 62.63  ? 93  VAL C O   1 
ATOM 4857 C CB  . VAL C 3 95  ? 6.476   -60.229 3.355   1.00 59.97  ? 93  VAL C CB  1 
ATOM 4858 C CG1 . VAL C 3 95  ? 7.643   -60.427 2.406   1.00 65.70  ? 93  VAL C CG1 1 
ATOM 4859 C CG2 . VAL C 3 95  ? 6.855   -60.671 4.760   1.00 58.09  ? 93  VAL C CG2 1 
ATOM 4860 N N   . TYR C 3 96  ? 6.372   -57.277 1.472   1.00 58.85  ? 94  TYR C N   1 
ATOM 4861 C CA  . TYR C 3 96  ? 6.032   -56.619 0.216   1.00 62.84  ? 94  TYR C CA  1 
ATOM 4862 C C   . TYR C 3 96  ? 6.867   -57.210 -0.915  1.00 60.72  ? 94  TYR C C   1 
ATOM 4863 O O   . TYR C 3 96  ? 8.100   -57.117 -0.898  1.00 62.13  ? 94  TYR C O   1 
ATOM 4864 C CB  . TYR C 3 96  ? 6.242   -55.107 0.319   1.00 60.09  ? 94  TYR C CB  1 
ATOM 4865 C CG  . TYR C 3 96  ? 5.110   -54.387 1.024   1.00 56.71  ? 94  TYR C CG  1 
ATOM 4866 C CD1 . TYR C 3 96  ? 4.751   -54.722 2.323   1.00 61.67  ? 94  TYR C CD1 1 
ATOM 4867 C CD2 . TYR C 3 96  ? 4.387   -53.390 0.383   1.00 56.20  ? 94  TYR C CD2 1 
ATOM 4868 C CE1 . TYR C 3 96  ? 3.714   -54.075 2.969   1.00 62.77  ? 94  TYR C CE1 1 
ATOM 4869 C CE2 . TYR C 3 96  ? 3.346   -52.738 1.022   1.00 62.75  ? 94  TYR C CE2 1 
ATOM 4870 C CZ  . TYR C 3 96  ? 3.013   -53.086 2.315   1.00 62.63  ? 94  TYR C CZ  1 
ATOM 4871 O OH  . TYR C 3 96  ? 1.979   -52.443 2.956   1.00 59.58  ? 94  TYR C OH  1 
ATOM 4872 N N   . TYR C 3 97  ? 6.193   -57.818 -1.889  1.00 60.99  ? 95  TYR C N   1 
ATOM 4873 C CA  . TYR C 3 97  ? 6.828   -58.426 -3.050  1.00 61.40  ? 95  TYR C CA  1 
ATOM 4874 C C   . TYR C 3 97  ? 6.604   -57.564 -4.285  1.00 58.20  ? 95  TYR C C   1 
ATOM 4875 O O   . TYR C 3 97  ? 5.606   -56.847 -4.390  1.00 55.24  ? 95  TYR C O   1 
ATOM 4876 C CB  . TYR C 3 97  ? 6.272   -59.828 -3.325  1.00 58.18  ? 95  TYR C CB  1 
ATOM 4877 C CG  . TYR C 3 97  ? 6.375   -60.807 -2.178  1.00 64.84  ? 95  TYR C CG  1 
ATOM 4878 C CD1 . TYR C 3 97  ? 7.513   -61.583 -2.003  1.00 67.15  ? 95  TYR C CD1 1 
ATOM 4879 C CD2 . TYR C 3 97  ? 5.325   -60.972 -1.283  1.00 62.96  ? 95  TYR C CD2 1 
ATOM 4880 C CE1 . TYR C 3 97  ? 7.609   -62.485 -0.961  1.00 63.88  ? 95  TYR C CE1 1 
ATOM 4881 C CE2 . TYR C 3 97  ? 5.412   -61.873 -0.239  1.00 63.97  ? 95  TYR C CE2 1 
ATOM 4882 C CZ  . TYR C 3 97  ? 6.556   -62.628 -0.084  1.00 63.68  ? 95  TYR C CZ  1 
ATOM 4883 O OH  . TYR C 3 97  ? 6.648   -63.527 0.954   1.00 64.87  ? 95  TYR C OH  1 
ATOM 4884 N N   . CYS C 3 98  ? 7.536   -57.651 -5.230  1.00 64.95  ? 96  CYS C N   1 
ATOM 4885 C CA  . CYS C 3 98  ? 7.365   -57.054 -6.548  1.00 67.29  ? 96  CYS C CA  1 
ATOM 4886 C C   . CYS C 3 98  ? 7.309   -58.171 -7.579  1.00 66.60  ? 96  CYS C C   1 
ATOM 4887 O O   . CYS C 3 98  ? 8.127   -59.097 -7.546  1.00 70.60  ? 96  CYS C O   1 
ATOM 4888 C CB  . CYS C 3 98  ? 8.485   -56.056 -6.873  1.00 66.59  ? 96  CYS C CB  1 
ATOM 4889 S SG  . CYS C 3 98  ? 10.121  -56.759 -7.180  1.00 87.66  ? 96  CYS C SG  1 
ATOM 4890 N N   . ALA C 3 99  ? 6.328   -58.098 -8.470  1.00 54.58  ? 97  ALA C N   1 
ATOM 4891 C CA  . ALA C 3 99  ? 6.115   -59.115 -9.484  1.00 54.75  ? 97  ALA C CA  1 
ATOM 4892 C C   . ALA C 3 99  ? 6.264   -58.497 -10.867 1.00 58.10  ? 97  ALA C C   1 
ATOM 4893 O O   . ALA C 3 99  ? 6.206   -57.277 -11.035 1.00 57.85  ? 97  ALA C O   1 
ATOM 4894 C CB  . ALA C 3 99  ? 4.734   -59.765 -9.337  1.00 53.87  ? 97  ALA C CB  1 
ATOM 4895 N N   . ALA C 3 100 ? 6.463   -59.358 -11.861 1.00 63.72  ? 98  ALA C N   1 
ATOM 4896 C CA  . ALA C 3 100 ? 6.648   -58.917 -13.234 1.00 56.20  ? 98  ALA C CA  1 
ATOM 4897 C C   . ALA C 3 100 ? 5.938   -59.876 -14.176 1.00 52.35  ? 98  ALA C C   1 
ATOM 4898 O O   . ALA C 3 100 ? 5.824   -61.073 -13.900 1.00 54.62  ? 98  ALA C O   1 
ATOM 4899 C CB  . ALA C 3 100 ? 8.135   -58.824 -13.604 1.00 52.26  ? 98  ALA C CB  1 
ATOM 4900 N N   . LYS C 3 101 ? 5.459   -59.333 -15.292 1.00 52.84  ? 99  LYS C N   1 
ATOM 4901 C CA  . LYS C 3 101 ? 4.844   -60.136 -16.341 1.00 53.87  ? 99  LYS C CA  1 
ATOM 4902 C C   . LYS C 3 101 ? 5.136   -59.480 -17.681 1.00 51.85  ? 99  LYS C C   1 
ATOM 4903 O O   . LYS C 3 101 ? 4.967   -58.266 -17.826 1.00 50.98  ? 99  LYS C O   1 
ATOM 4904 C CB  . LYS C 3 101 ? 3.332   -60.272 -16.127 1.00 50.28  ? 99  LYS C CB  1 
ATOM 4905 C CG  . LYS C 3 101 ? 2.629   -61.150 -17.157 1.00 49.29  ? 99  LYS C CG  1 
ATOM 4906 C CD  . LYS C 3 101 ? 3.285   -62.519 -17.272 1.00 46.25  ? 99  LYS C CD  1 
ATOM 4907 C CE  . LYS C 3 101 ? 2.478   -63.441 -18.171 1.00 40.50  ? 99  LYS C CE  1 
ATOM 4908 N NZ  . LYS C 3 101 ? 1.186   -63.836 -17.544 1.00 38.72  ? 99  LYS C NZ  1 
ATOM 4909 N N   . PHE C 3 102 ? 5.582   -60.281 -18.646 1.00 52.42  ? 100 PHE C N   1 
ATOM 4910 C CA  . PHE C 3 102 ? 5.872   -59.765 -19.979 1.00 51.10  ? 100 PHE C CA  1 
ATOM 4911 C C   . PHE C 3 102 ? 4.607   -59.195 -20.606 1.00 48.91  ? 100 PHE C C   1 
ATOM 4912 O O   . PHE C 3 102 ? 3.608   -59.905 -20.758 1.00 49.99  ? 100 PHE C O   1 
ATOM 4913 C CB  . PHE C 3 102 ? 6.452   -60.873 -20.857 1.00 47.65  ? 100 PHE C CB  1 
ATOM 4914 C CG  . PHE C 3 102 ? 6.965   -60.390 -22.184 1.00 48.95  ? 100 PHE C CG  1 
ATOM 4915 C CD1 . PHE C 3 102 ? 8.259   -59.912 -22.306 1.00 51.22  ? 100 PHE C CD1 1 
ATOM 4916 C CD2 . PHE C 3 102 ? 6.157   -60.416 -23.308 1.00 48.89  ? 100 PHE C CD2 1 
ATOM 4917 C CE1 . PHE C 3 102 ? 8.738   -59.469 -23.523 1.00 49.71  ? 100 PHE C CE1 1 
ATOM 4918 C CE2 . PHE C 3 102 ? 6.630   -59.972 -24.529 1.00 52.42  ? 100 PHE C CE2 1 
ATOM 4919 C CZ  . PHE C 3 102 ? 7.923   -59.497 -24.636 1.00 50.74  ? 100 PHE C CZ  1 
ATOM 4920 N N   . TYR C 3 103 ? 4.655   -57.911 -20.968 1.00 47.22  ? 101 TYR C N   1 
ATOM 4921 C CA  . TYR C 3 103 ? 3.509   -57.211 -21.553 1.00 50.35  ? 101 TYR C CA  1 
ATOM 4922 C C   . TYR C 3 103 ? 2.289   -57.294 -20.639 1.00 50.47  ? 101 TYR C C   1 
ATOM 4923 O O   . TYR C 3 103 ? 1.163   -57.510 -21.091 1.00 53.16  ? 101 TYR C O   1 
ATOM 4924 C CB  . TYR C 3 103 ? 3.179   -57.748 -22.949 1.00 52.05  ? 101 TYR C CB  1 
ATOM 4925 C CG  . TYR C 3 103 ? 4.057   -57.204 -24.056 1.00 49.19  ? 101 TYR C CG  1 
ATOM 4926 C CD1 . TYR C 3 103 ? 5.048   -56.268 -23.790 1.00 48.55  ? 101 TYR C CD1 1 
ATOM 4927 C CD2 . TYR C 3 103 ? 3.893   -57.628 -25.368 1.00 46.42  ? 101 TYR C CD2 1 
ATOM 4928 C CE1 . TYR C 3 103 ? 5.850   -55.769 -24.798 1.00 48.41  ? 101 TYR C CE1 1 
ATOM 4929 C CE2 . TYR C 3 103 ? 4.690   -57.135 -26.384 1.00 45.64  ? 101 TYR C CE2 1 
ATOM 4930 C CZ  . TYR C 3 103 ? 5.667   -56.206 -26.094 1.00 50.86  ? 101 TYR C CZ  1 
ATOM 4931 O OH  . TYR C 3 103 ? 6.465   -55.711 -27.103 1.00 50.06  ? 101 TYR C OH  1 
ATOM 4932 N N   . GLY C 3 104 ? 2.513   -57.125 -19.340 1.00 52.94  ? 102 GLY C N   1 
ATOM 4933 C CA  . GLY C 3 104 ? 1.460   -57.198 -18.354 1.00 53.20  ? 102 GLY C CA  1 
ATOM 4934 C C   . GLY C 3 104 ? 1.479   -55.992 -17.434 1.00 55.57  ? 102 GLY C C   1 
ATOM 4935 O O   . GLY C 3 104 ? 1.872   -54.888 -17.819 1.00 49.00  ? 102 GLY C O   1 
ATOM 4936 N N   . GLY C 3 105 ? 1.048   -56.225 -16.200 1.00 56.59  ? 103 GLY C N   1 
ATOM 4937 C CA  . GLY C 3 105 ? 0.982   -55.184 -15.200 1.00 55.12  ? 103 GLY C CA  1 
ATOM 4938 C C   . GLY C 3 105 ? -0.373  -54.537 -15.027 1.00 59.68  ? 103 GLY C C   1 
ATOM 4939 O O   . GLY C 3 105 ? -0.451  -53.466 -14.414 1.00 56.61  ? 103 GLY C O   1 
ATOM 4940 N N   . ASN C 3 106 ? -1.440  -55.148 -15.545 1.00 69.23  ? 104 ASN C N   1 
ATOM 4941 C CA  . ASN C 3 106 ? -2.787  -54.599 -15.444 1.00 70.96  ? 104 ASN C CA  1 
ATOM 4942 C C   . ASN C 3 106 ? -3.718  -55.514 -14.656 1.00 67.84  ? 104 ASN C C   1 
ATOM 4943 O O   . ASN C 3 106 ? -4.942  -55.372 -14.742 1.00 69.69  ? 104 ASN C O   1 
ATOM 4944 C CB  . ASN C 3 106 ? -3.361  -54.334 -16.837 1.00 69.38  ? 104 ASN C CB  1 
ATOM 4945 C CG  . ASN C 3 106 ? -3.421  -55.587 -17.695 1.00 63.85  ? 104 ASN C CG  1 
ATOM 4946 O OD1 . ASN C 3 106 ? -2.803  -56.603 -17.377 1.00 66.49  ? 104 ASN C OD1 1 
ATOM 4947 N ND2 . ASN C 3 106 ? -4.161  -55.514 -18.796 1.00 64.74  ? 104 ASN C ND2 1 
ATOM 4948 N N   . SER C 3 107 ? -3.164  -56.450 -13.894 1.00 55.87  ? 105 SER C N   1 
ATOM 4949 C CA  . SER C 3 107 ? -3.949  -57.438 -13.175 1.00 57.29  ? 105 SER C CA  1 
ATOM 4950 C C   . SER C 3 107 ? -3.791  -57.252 -11.674 1.00 60.67  ? 105 SER C C   1 
ATOM 4951 O O   . SER C 3 107 ? -2.721  -56.879 -11.185 1.00 60.80  ? 105 SER C O   1 
ATOM 4952 C CB  . SER C 3 107 ? -3.534  -58.858 -13.567 1.00 57.00  ? 105 SER C CB  1 
ATOM 4953 O OG  . SER C 3 107 ? -4.565  -59.786 -13.283 1.00 62.33  ? 105 SER C OG  1 
ATOM 4954 N N   . LYS C 3 108 ? -4.876  -57.516 -10.948 1.00 59.37  ? 106 LYS C N   1 
ATOM 4955 C CA  . LYS C 3 108 ? -4.882  -57.490 -9.493  1.00 57.18  ? 106 LYS C CA  1 
ATOM 4956 C C   . LYS C 3 108 ? -4.725  -58.881 -8.891  1.00 57.39  ? 106 LYS C C   1 
ATOM 4957 O O   . LYS C 3 108 ? -4.945  -59.056 -7.688  1.00 59.77  ? 106 LYS C O   1 
ATOM 4958 C CB  . LYS C 3 108 ? -6.172  -56.841 -8.982  1.00 52.40  ? 106 LYS C CB  1 
ATOM 4959 C CG  . LYS C 3 108 ? -6.521  -55.525 -9.660  1.00 57.74  ? 106 LYS C CG  1 
ATOM 4960 C CD  . LYS C 3 108 ? -7.257  -54.592 -8.712  1.00 56.54  ? 106 LYS C CD  1 
ATOM 4961 C CE  . LYS C 3 108 ? -7.658  -53.298 -9.405  1.00 59.62  ? 106 LYS C CE  1 
ATOM 4962 N NZ  . LYS C 3 108 ? -6.577  -52.276 -9.342  1.00 55.57  ? 106 LYS C NZ  1 
ATOM 4963 N N   . ARG C 3 109 ? -4.345  -59.869 -9.697  1.00 58.81  ? 107 ARG C N   1 
ATOM 4964 C CA  . ARG C 3 109 ? -4.247  -61.245 -9.254  1.00 62.91  ? 107 ARG C CA  1 
ATOM 4965 C C   . ARG C 3 109 ? -2.800  -61.716 -9.322  1.00 63.98  ? 107 ARG C C   1 
ATOM 4966 O O   . ARG C 3 109 ? -2.120  -61.467 -10.328 1.00 62.34  ? 107 ARG C O   1 
ATOM 4967 C CB  . ARG C 3 109 ? -5.140  -62.155 -10.116 1.00 61.34  ? 107 ARG C CB  1 
ATOM 4968 C CG  . ARG C 3 109 ? -6.445  -61.498 -10.544 1.00 61.38  ? 107 ARG C CG  1 
ATOM 4969 C CD  . ARG C 3 109 ? -7.360  -62.471 -11.270 1.00 69.82  ? 107 ARG C CD  1 
ATOM 4970 N NE  . ARG C 3 109 ? -8.746  -62.338 -10.836 1.00 77.40  ? 107 ARG C NE  1 
ATOM 4971 C CZ  . ARG C 3 109 ? -9.734  -63.134 -11.223 1.00 78.64  ? 107 ARG C CZ  1 
ATOM 4972 N NH1 . ARG C 3 109 ? -9.527  -64.130 -12.069 1.00 78.42  ? 107 ARG C NH1 1 
ATOM 4973 N NH2 . ARG C 3 109 ? -10.959 -62.929 -10.746 1.00 76.16  ? 107 ARG C NH2 1 
ATOM 4974 N N   . PRO C 3 110 ? -2.292  -62.387 -8.284  1.00 60.95  ? 108 PRO C N   1 
ATOM 4975 C CA  . PRO C 3 110 ? -0.901  -62.867 -8.332  1.00 58.78  ? 108 PRO C CA  1 
ATOM 4976 C C   . PRO C 3 110 ? -0.661  -63.941 -9.380  1.00 57.96  ? 108 PRO C C   1 
ATOM 4977 O O   . PRO C 3 110 ? 0.494   -64.153 -9.768  1.00 55.30  ? 108 PRO C O   1 
ATOM 4978 C CB  . PRO C 3 110 ? -0.665  -63.413 -6.915  1.00 54.03  ? 108 PRO C CB  1 
ATOM 4979 C CG  . PRO C 3 110 ? -1.738  -62.791 -6.072  1.00 54.99  ? 108 PRO C CG  1 
ATOM 4980 C CD  . PRO C 3 110 ? -2.919  -62.649 -6.979  1.00 54.44  ? 108 PRO C CD  1 
ATOM 4981 N N   . GLY C 3 111 ? -1.707  -64.627 -9.846  1.00 57.26  ? 109 GLY C N   1 
ATOM 4982 C CA  . GLY C 3 111 ? -1.516  -65.652 -10.856 1.00 56.79  ? 109 GLY C CA  1 
ATOM 4983 C C   . GLY C 3 111 ? -1.136  -65.095 -12.213 1.00 54.88  ? 109 GLY C C   1 
ATOM 4984 O O   . GLY C 3 111 ? -0.491  -65.783 -13.011 1.00 50.38  ? 109 GLY C O   1 
ATOM 4985 N N   . ASP C 3 112 ? -1.519  -63.851 -12.494 1.00 55.45  ? 110 ASP C N   1 
ATOM 4986 C CA  . ASP C 3 112 ? -1.223  -63.210 -13.768 1.00 56.03  ? 110 ASP C CA  1 
ATOM 4987 C C   . ASP C 3 112 ? 0.167   -62.586 -13.811 1.00 54.29  ? 110 ASP C C   1 
ATOM 4988 O O   . ASP C 3 112 ? 0.444   -61.781 -14.708 1.00 47.29  ? 110 ASP C O   1 
ATOM 4989 C CB  . ASP C 3 112 ? -2.281  -62.147 -14.075 1.00 53.34  ? 110 ASP C CB  1 
ATOM 4990 C CG  . ASP C 3 112 ? -3.578  -62.745 -14.589 1.00 59.18  ? 110 ASP C CG  1 
ATOM 4991 O OD1 . ASP C 3 112 ? -3.519  -63.748 -15.333 1.00 70.28  ? 110 ASP C OD1 1 
ATOM 4992 O OD2 . ASP C 3 112 ? -4.657  -62.215 -14.245 1.00 55.64  ? 110 ASP C OD2 1 
ATOM 4993 N N   . TYR C 3 113 ? 1.039   -62.928 -12.868 1.00 51.19  ? 111 TYR C N   1 
ATOM 4994 C CA  . TYR C 3 113 ? 2.416   -62.457 -12.852 1.00 48.82  ? 111 TYR C CA  1 
ATOM 4995 C C   . TYR C 3 113 ? 3.340   -63.664 -12.812 1.00 47.72  ? 111 TYR C C   1 
ATOM 4996 O O   . TYR C 3 113 ? 3.096   -64.612 -12.059 1.00 60.62  ? 111 TYR C O   1 
ATOM 4997 C CB  . TYR C 3 113 ? 2.670   -61.536 -11.659 1.00 49.78  ? 111 TYR C CB  1 
ATOM 4998 C CG  . TYR C 3 113 ? 2.001   -60.183 -11.780 1.00 55.44  ? 111 TYR C CG  1 
ATOM 4999 C CD1 . TYR C 3 113 ? 2.638   -59.123 -12.417 1.00 53.39  ? 111 TYR C CD1 1 
ATOM 5000 C CD2 . TYR C 3 113 ? 0.728   -59.968 -11.267 1.00 54.99  ? 111 TYR C CD2 1 
ATOM 5001 C CE1 . TYR C 3 113 ? 2.028   -57.886 -12.530 1.00 48.04  ? 111 TYR C CE1 1 
ATOM 5002 C CE2 . TYR C 3 113 ? 0.110   -58.736 -11.377 1.00 53.34  ? 111 TYR C CE2 1 
ATOM 5003 C CZ  . TYR C 3 113 ? 0.765   -57.700 -12.009 1.00 49.47  ? 111 TYR C CZ  1 
ATOM 5004 O OH  . TYR C 3 113 ? 0.150   -56.474 -12.118 1.00 51.05  ? 111 TYR C OH  1 
ATOM 5005 N N   . ALA C 3 114 ? 4.393   -63.632 -13.624 1.00 45.02  ? 112 ALA C N   1 
ATOM 5006 C CA  . ALA C 3 114 ? 5.239   -64.802 -13.816 1.00 51.62  ? 112 ALA C CA  1 
ATOM 5007 C C   . ALA C 3 114 ? 6.523   -64.762 -13.000 1.00 54.49  ? 112 ALA C C   1 
ATOM 5008 O O   . ALA C 3 114 ? 6.984   -65.810 -12.535 1.00 56.25  ? 112 ALA C O   1 
ATOM 5009 C CB  . ALA C 3 114 ? 5.585   -64.964 -15.300 1.00 50.06  ? 112 ALA C CB  1 
ATOM 5010 N N   . TYR C 3 115 ? 7.112   -63.584 -12.806 1.00 51.80  ? 113 TYR C N   1 
ATOM 5011 C CA  . TYR C 3 115 ? 8.411   -63.453 -12.158 1.00 52.28  ? 113 TYR C CA  1 
ATOM 5012 C C   . TYR C 3 115 ? 8.256   -62.679 -10.858 1.00 51.20  ? 113 TYR C C   1 
ATOM 5013 O O   . TYR C 3 115 ? 7.782   -61.538 -10.863 1.00 50.68  ? 113 TYR C O   1 
ATOM 5014 C CB  . TYR C 3 115 ? 9.412   -62.761 -13.084 1.00 52.41  ? 113 TYR C CB  1 
ATOM 5015 C CG  . TYR C 3 115 ? 9.672   -63.536 -14.351 1.00 57.74  ? 113 TYR C CG  1 
ATOM 5016 C CD1 . TYR C 3 115 ? 10.345  -64.748 -14.316 1.00 55.74  ? 113 TYR C CD1 1 
ATOM 5017 C CD2 . TYR C 3 115 ? 9.228   -63.066 -15.581 1.00 54.06  ? 113 TYR C CD2 1 
ATOM 5018 C CE1 . TYR C 3 115 ? 10.580  -65.467 -15.468 1.00 59.79  ? 113 TYR C CE1 1 
ATOM 5019 C CE2 . TYR C 3 115 ? 9.458   -63.779 -16.741 1.00 52.96  ? 113 TYR C CE2 1 
ATOM 5020 C CZ  . TYR C 3 115 ? 10.136  -64.979 -16.679 1.00 58.38  ? 113 TYR C CZ  1 
ATOM 5021 O OH  . TYR C 3 115 ? 10.372  -65.699 -17.827 1.00 63.45  ? 113 TYR C OH  1 
ATOM 5022 N N   . TRP C 3 116 ? 8.668   -63.296 -9.756  1.00 54.23  ? 114 TRP C N   1 
ATOM 5023 C CA  . TRP C 3 116 ? 8.596   -62.712 -8.427  1.00 55.43  ? 114 TRP C CA  1 
ATOM 5024 C C   . TRP C 3 116 ? 9.996   -62.587 -7.840  1.00 57.41  ? 114 TRP C C   1 
ATOM 5025 O O   . TRP C 3 116 ? 10.962  -63.172 -8.336  1.00 56.75  ? 114 TRP C O   1 
ATOM 5026 C CB  . TRP C 3 116 ? 7.712   -63.557 -7.501  1.00 54.30  ? 114 TRP C CB  1 
ATOM 5027 C CG  . TRP C 3 116 ? 6.288   -63.623 -7.935  1.00 52.32  ? 114 TRP C CG  1 
ATOM 5028 C CD1 . TRP C 3 116 ? 5.777   -64.358 -8.963  1.00 51.39  ? 114 TRP C CD1 1 
ATOM 5029 C CD2 . TRP C 3 116 ? 5.184   -62.923 -7.353  1.00 51.49  ? 114 TRP C CD2 1 
ATOM 5030 N NE1 . TRP C 3 116 ? 4.422   -64.158 -9.060  1.00 54.57  ? 114 TRP C NE1 1 
ATOM 5031 C CE2 . TRP C 3 116 ? 4.033   -63.280 -8.082  1.00 54.43  ? 114 TRP C CE2 1 
ATOM 5032 C CE3 . TRP C 3 116 ? 5.056   -62.030 -6.287  1.00 50.35  ? 114 TRP C CE3 1 
ATOM 5033 C CZ2 . TRP C 3 116 ? 2.770   -62.776 -7.779  1.00 53.17  ? 114 TRP C CZ2 1 
ATOM 5034 C CZ3 . TRP C 3 116 ? 3.803   -61.529 -5.989  1.00 54.54  ? 114 TRP C CZ3 1 
ATOM 5035 C CH2 . TRP C 3 116 ? 2.677   -61.904 -6.730  1.00 52.66  ? 114 TRP C CH2 1 
ATOM 5036 N N   . GLY C 3 117 ? 10.094  -61.811 -6.760  1.00 65.11  ? 115 GLY C N   1 
ATOM 5037 C CA  . GLY C 3 117 ? 11.331  -61.666 -6.023  1.00 76.99  ? 115 GLY C CA  1 
ATOM 5038 C C   . GLY C 3 117 ? 11.123  -61.946 -4.545  1.00 79.35  ? 115 GLY C C   1 
ATOM 5039 O O   . GLY C 3 117 ? 10.008  -62.222 -4.095  1.00 72.15  ? 115 GLY C O   1 
ATOM 5040 N N   . GLN C 3 118 ? 12.226  -61.872 -3.805  1.00 95.69  ? 116 GLN C N   1 
ATOM 5041 C CA  . GLN C 3 118 ? 12.181  -62.051 -2.360  1.00 100.22 ? 116 GLN C CA  1 
ATOM 5042 C C   . GLN C 3 118 ? 11.702  -60.764 -1.699  1.00 103.25 ? 116 GLN C C   1 
ATOM 5043 O O   . GLN C 3 118 ? 12.219  -59.677 -1.978  1.00 109.25 ? 116 GLN C O   1 
ATOM 5044 C CB  . GLN C 3 118 ? 13.551  -62.477 -1.821  1.00 107.63 ? 116 GLN C CB  1 
ATOM 5045 C CG  . GLN C 3 118 ? 14.648  -61.408 -1.824  1.00 112.59 ? 116 GLN C CG  1 
ATOM 5046 C CD  . GLN C 3 118 ? 15.133  -61.048 -3.218  1.00 112.12 ? 116 GLN C CD  1 
ATOM 5047 O OE1 . GLN C 3 118 ? 14.870  -61.763 -4.185  1.00 107.15 ? 116 GLN C OE1 1 
ATOM 5048 N NE2 . GLN C 3 118 ? 15.851  -59.935 -3.324  1.00 109.61 ? 116 GLN C NE2 1 
ATOM 5049 N N   . GLY C 3 119 ? 10.699  -60.886 -0.840  1.00 78.86  ? 117 GLY C N   1 
ATOM 5050 C CA  . GLY C 3 119 ? 10.073  -59.718 -0.263  1.00 73.84  ? 117 GLY C CA  1 
ATOM 5051 C C   . GLY C 3 119 ? 10.958  -58.993 0.731   1.00 81.12  ? 117 GLY C C   1 
ATOM 5052 O O   . GLY C 3 119 ? 12.055  -59.425 1.094   1.00 84.94  ? 117 GLY C O   1 
ATOM 5053 N N   . THR C 3 120 ? 10.453  -57.844 1.165   1.00 78.87  ? 118 THR C N   1 
ATOM 5054 C CA  . THR C 3 120 ? 11.056  -57.049 2.220   1.00 75.06  ? 118 THR C CA  1 
ATOM 5055 C C   . THR C 3 120 ? 10.108  -56.994 3.407   1.00 70.73  ? 118 THR C C   1 
ATOM 5056 O O   . THR C 3 120 ? 8.883   -56.973 3.247   1.00 70.25  ? 118 THR C O   1 
ATOM 5057 C CB  . THR C 3 120 ? 11.374  -55.628 1.744   1.00 71.59  ? 118 THR C CB  1 
ATOM 5058 O OG1 . THR C 3 120 ? 10.168  -54.981 1.315   1.00 71.67  ? 118 THR C OG1 1 
ATOM 5059 C CG2 . THR C 3 120 ? 12.357  -55.669 0.590   1.00 73.40  ? 118 THR C CG2 1 
ATOM 5060 N N   . GLN C 3 121 ? 10.690  -56.979 4.603   1.00 64.39  ? 119 GLN C N   1 
ATOM 5061 C CA  . GLN C 3 121 ? 9.927   -56.917 5.844   1.00 64.34  ? 119 GLN C CA  1 
ATOM 5062 C C   . GLN C 3 121 ? 9.550   -55.470 6.136   1.00 67.78  ? 119 GLN C C   1 
ATOM 5063 O O   . GLN C 3 121 ? 10.393  -54.675 6.560   1.00 68.25  ? 119 GLN C O   1 
ATOM 5064 C CB  . GLN C 3 121 ? 10.721  -57.506 7.007   1.00 71.20  ? 119 GLN C CB  1 
ATOM 5065 C CG  . GLN C 3 121 ? 9.919   -57.727 8.296   1.00 66.94  ? 119 GLN C CG  1 
ATOM 5066 C CD  . GLN C 3 121 ? 8.556   -58.363 8.059   1.00 70.80  ? 119 GLN C CD  1 
ATOM 5067 O OE1 . GLN C 3 121 ? 8.368   -59.103 7.081   1.00 69.45  ? 119 GLN C OE1 1 
ATOM 5068 N NE2 . GLN C 3 121 ? 7.604   -58.080 8.935   1.00 70.98  ? 119 GLN C NE2 1 
ATOM 5069 N N   . VAL C 3 122 ? 8.275   -55.139 5.953   1.00 67.32  ? 120 VAL C N   1 
ATOM 5070 C CA  . VAL C 3 122 ? 7.744   -53.813 6.254   1.00 71.16  ? 120 VAL C CA  1 
ATOM 5071 C C   . VAL C 3 122 ? 6.798   -53.956 7.437   1.00 67.46  ? 120 VAL C C   1 
ATOM 5072 O O   . VAL C 3 122 ? 5.758   -54.617 7.333   1.00 67.85  ? 120 VAL C O   1 
ATOM 5073 C CB  . VAL C 3 122 ? 7.026   -53.200 5.046   1.00 68.87  ? 120 VAL C CB  1 
ATOM 5074 C CG1 . VAL C 3 122 ? 6.507   -51.820 5.386   1.00 70.12  ? 120 VAL C CG1 1 
ATOM 5075 C CG2 . VAL C 3 122 ? 7.958   -53.149 3.846   1.00 61.73  ? 120 VAL C CG2 1 
ATOM 5076 N N   . THR C 3 123 ? 7.151   -53.343 8.563   1.00 69.31  ? 121 THR C N   1 
ATOM 5077 C CA  . THR C 3 123 ? 6.315   -53.375 9.753   1.00 74.39  ? 121 THR C CA  1 
ATOM 5078 C C   . THR C 3 123 ? 6.294   -51.995 10.394  1.00 74.31  ? 121 THR C C   1 
ATOM 5079 O O   . THR C 3 123 ? 7.330   -51.331 10.491  1.00 76.49  ? 121 THR C O   1 
ATOM 5080 C CB  . THR C 3 123 ? 6.809   -54.431 10.753  1.00 72.33  ? 121 THR C CB  1 
ATOM 5081 O OG1 . THR C 3 123 ? 6.197   -54.214 12.030  1.00 65.83  ? 121 THR C OG1 1 
ATOM 5082 C CG2 . THR C 3 123 ? 8.328   -54.385 10.884  1.00 74.64  ? 121 THR C CG2 1 
ATOM 5083 N N   . VAL C 3 124 ? 5.109   -51.563 10.814  1.00 71.29  ? 122 VAL C N   1 
ATOM 5084 C CA  . VAL C 3 124 ? 4.934   -50.269 11.449  1.00 80.62  ? 122 VAL C CA  1 
ATOM 5085 C C   . VAL C 3 124 ? 4.775   -50.477 12.951  1.00 82.80  ? 122 VAL C C   1 
ATOM 5086 O O   . VAL C 3 124 ? 4.357   -51.538 13.421  1.00 80.86  ? 122 VAL C O   1 
ATOM 5087 C CB  . VAL C 3 124 ? 3.733   -49.492 10.854  1.00 78.92  ? 122 VAL C CB  1 
ATOM 5088 C CG1 . VAL C 3 124 ? 3.719   -49.623 9.335   1.00 70.59  ? 122 VAL C CG1 1 
ATOM 5089 C CG2 . VAL C 3 124 ? 2.419   -49.972 11.451  1.00 76.88  ? 122 VAL C CG2 1 
ATOM 5090 N N   . SER C 3 125 ? 5.131   -49.452 13.722  1.00 79.06  ? 123 SER C N   1 
ATOM 5091 C CA  . SER C 3 125 ? 5.103   -49.506 15.182  1.00 84.95  ? 123 SER C CA  1 
ATOM 5092 C C   . SER C 3 125 ? 4.086   -48.476 15.667  1.00 92.07  ? 123 SER C C   1 
ATOM 5093 O O   . SER C 3 125 ? 4.409   -47.296 15.829  1.00 102.07 ? 123 SER C O   1 
ATOM 5094 C CB  . SER C 3 125 ? 6.500   -49.255 15.772  1.00 88.25  ? 123 SER C CB  1 
ATOM 5095 O OG  . SER C 3 125 ? 6.619   -49.775 17.089  1.00 99.01  ? 123 SER C OG  1 
ATOM 5096 N N   . SER C 3 126 ? 2.855   -48.935 15.891  1.00 92.93  ? 124 SER C N   1 
ATOM 5097 C CA  . SER C 3 126 ? 1.783   -48.094 16.415  1.00 95.08  ? 124 SER C CA  1 
ATOM 5098 C C   . SER C 3 126 ? 2.126   -47.614 17.822  1.00 96.74  ? 124 SER C C   1 
ATOM 5099 O O   . SER C 3 126 ? 2.364   -46.424 18.038  1.00 99.47  ? 124 SER C O   1 
ATOM 5100 C CB  . SER C 3 126 ? 0.447   -48.853 16.416  1.00 94.55  ? 124 SER C CB  1 
ATOM 5101 O OG  . SER C 3 126 ? 0.503   -50.025 17.214  1.00 94.79  ? 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   . MET A 1   ? 1.0024 1.0417 1.0061 -0.0702 0.0628  -0.0455 0   MET A N   
2    C CA  . MET A 1   ? 1.0549 1.0834 1.0558 -0.0678 0.0577  -0.0485 0   MET A CA  
3    C C   . MET A 1   ? 1.0184 1.0371 1.0286 -0.0662 0.0533  -0.0458 0   MET A C   
4    O O   . MET A 1   ? 1.0231 1.0437 1.0426 -0.0654 0.0545  -0.0443 0   MET A O   
5    C CB  . MET A 1   ? 1.0683 1.0985 1.0696 -0.0630 0.0595  -0.0585 0   MET A CB  
6    C CG  . MET A 1   ? 1.0151 1.0370 1.0102 -0.0623 0.0545  -0.0619 0   MET A CG  
7    S SD  . MET A 1   ? 1.0228 1.0416 1.0045 -0.0675 0.0501  -0.0544 0   MET A SD  
8    C CE  . MET A 1   ? 0.8366 0.8495 0.8132 -0.0657 0.0449  -0.0612 0   MET A CE  
9    N N   . VAL A 2   ? 1.0300 1.0393 1.0375 -0.0657 0.0483  -0.0451 1   VAL A N   
10   C CA  . VAL A 2   ? 0.9996 1.0000 1.0143 -0.0640 0.0444  -0.0422 1   VAL A CA  
11   C C   . VAL A 2   ? 0.9334 0.9311 0.9571 -0.0592 0.0443  -0.0483 1   VAL A C   
12   O O   . VAL A 2   ? 0.9360 0.9336 0.9578 -0.0578 0.0442  -0.0543 1   VAL A O   
13   C CB  . VAL A 2   ? 0.9757 0.9685 0.9838 -0.0655 0.0394  -0.0375 1   VAL A CB  
14   C CG1 . VAL A 2   ? 0.9207 0.9123 0.9232 -0.0694 0.0387  -0.0298 1   VAL A CG1 
15   C CG2 . VAL A 2   ? 0.9882 0.9823 0.9880 -0.0661 0.0382  -0.0411 1   VAL A CG2 
16   N N   . SER A 3   ? 0.8623 0.8572 0.8955 -0.0568 0.0440  -0.0466 2   SER A N   
17   C CA  . SER A 3   ? 0.8426 0.8338 0.8849 -0.0523 0.0438  -0.0509 2   SER A CA  
18   C C   . SER A 3   ? 0.7638 0.7491 0.8125 -0.0506 0.0414  -0.0459 2   SER A C   
19   O O   . SER A 3   ? 0.7901 0.7746 0.8363 -0.0526 0.0402  -0.0403 2   SER A O   
20   C CB  . SER A 3   ? 0.9044 0.9024 0.9523 -0.0494 0.0482  -0.0566 2   SER A CB  
21   O OG  . SER A 3   ? 0.8088 0.8114 0.8629 -0.0489 0.0498  -0.0534 2   SER A OG  
22   N N   . LEU A 4   ? 0.7706 0.7512 0.8271 -0.0469 0.0407  -0.0479 3   LEU A N   
23   C CA  . LEU A 4   ? 0.7339 0.7093 0.7958 -0.0447 0.0388  -0.0432 3   LEU A CA  
24   C C   . LEU A 4   ? 0.6864 0.6660 0.7524 -0.0435 0.0403  -0.0414 3   LEU A C   
25   O O   . LEU A 4   ? 0.7206 0.6972 0.7871 -0.0431 0.0384  -0.0366 3   LEU A O   
26   C CB  . LEU A 4   ? 0.6734 0.6432 0.7430 -0.0413 0.0380  -0.0452 3   LEU A CB  
27   C CG  . LEU A 4   ? 0.7270 0.6911 0.8008 -0.0391 0.0361  -0.0396 3   LEU A CG  
28   C CD1 . LEU A 4   ? 0.6706 0.6325 0.7375 -0.0412 0.0338  -0.0344 3   LEU A CD1 
29   C CD2 . LEU A 4   ? 0.7081 0.6668 0.7886 -0.0373 0.0353  -0.0410 3   LEU A CD2 
30   N N   . ALA A 5   ? 0.6763 0.6636 0.7454 -0.0429 0.0436  -0.0453 4   ALA A N   
31   C CA  . ALA A 5   ? 0.6860 0.6792 0.7605 -0.0420 0.0447  -0.0436 4   ALA A CA  
32   C C   . ALA A 5   ? 0.6755 0.6717 0.7443 -0.0469 0.0438  -0.0390 4   ALA A C   
33   O O   . ALA A 5   ? 0.6669 0.6625 0.7381 -0.0470 0.0419  -0.0353 4   ALA A O   
34   C CB  . ALA A 5   ? 0.7942 0.7961 0.8744 -0.0395 0.0487  -0.0491 4   ALA A CB  
35   N N   . LYS A 6   ? 0.6851 0.6839 0.7460 -0.0511 0.0449  -0.0391 5   LYS A N   
36   C CA  . LYS A 6   ? 0.7074 0.7076 0.7627 -0.0563 0.0439  -0.0342 5   LYS A CA  
37   C C   . LYS A 6   ? 0.7064 0.6960 0.7575 -0.0568 0.0394  -0.0293 5   LYS A C   
38   O O   . LYS A 6   ? 0.6505 0.6386 0.7007 -0.0591 0.0374  -0.0254 5   LYS A O   
39   C CB  . LYS A 6   ? 0.7069 0.7116 0.7539 -0.0604 0.0461  -0.0346 5   LYS A CB  
40   C CG  . LYS A 6   ? 0.8108 0.8239 0.8595 -0.0584 0.0507  -0.0410 5   LYS A CG  
41   C CD  . LYS A 6   ? 0.7984 0.8243 0.8488 -0.0612 0.0551  -0.0406 5   LYS A CD  
42   C CE  . LYS A 6   ? 0.7246 0.7592 0.7756 -0.0582 0.0601  -0.0474 5   LYS A CE  
43   N NZ  . LYS A 6   ? 0.7808 0.8296 0.8325 -0.0611 0.0652  -0.0465 5   LYS A NZ  
44   N N   . ALA A 7   ? 0.6889 0.6713 0.7375 -0.0545 0.0376  -0.0297 6   ALA A N   
45   C CA  . ALA A 7   ? 0.6049 0.5781 0.6502 -0.0537 0.0339  -0.0255 6   ALA A CA  
46   C C   . ALA A 7   ? 0.6513 0.6220 0.7026 -0.0500 0.0327  -0.0243 6   ALA A C   
47   O O   . ALA A 7   ? 0.7066 0.6717 0.7545 -0.0500 0.0300  -0.0207 6   ALA A O   
48   C CB  . ALA A 7   ? 0.6027 0.5710 0.6458 -0.0520 0.0327  -0.0260 6   ALA A CB  
49   N N   . SER A 8   ? 0.6507 0.6249 0.7102 -0.0466 0.0345  -0.0273 7   SER A N   
50   C CA  . SER A 8   ? 0.6137 0.5863 0.6786 -0.0429 0.0333  -0.0258 7   SER A CA  
51   C C   . SER A 8   ? 0.6133 0.5902 0.6789 -0.0451 0.0322  -0.0244 7   SER A C   
52   O O   . SER A 8   ? 0.6512 0.6245 0.7166 -0.0433 0.0295  -0.0219 7   SER A O   
53   C CB  . SER A 8   ? 0.6520 0.6268 0.7256 -0.0386 0.0353  -0.0290 7   SER A CB  
54   O OG  . SER A 8   ? 0.6833 0.6533 0.7570 -0.0372 0.0356  -0.0302 7   SER A OG  
55   N N   . LEU A 9   ? 0.6362 0.6212 0.7025 -0.0490 0.0343  -0.0258 8   LEU A N   
56   C CA  . LEU A 9   ? 0.5638 0.5540 0.6320 -0.0523 0.0331  -0.0240 8   LEU A CA  
57   C C   . LEU A 9   ? 0.5886 0.5708 0.6485 -0.0560 0.0293  -0.0200 8   LEU A C   
58   O O   . LEU A 9   ? 0.6522 0.6326 0.7126 -0.0566 0.0260  -0.0182 8   LEU A O   
59   C CB  . LEU A 9   ? 0.5932 0.5952 0.6646 -0.0559 0.0369  -0.0258 8   LEU A CB  
60   C CG  . LEU A 9   ? 0.6171 0.6303 0.6997 -0.0529 0.0394  -0.0286 8   LEU A CG  
61   C CD1 . LEU A 9   ? 0.5144 0.5392 0.5988 -0.0554 0.0444  -0.0310 8   LEU A CD1 
62   C CD2 . LEU A 9   ? 0.5875 0.6039 0.6754 -0.0538 0.0360  -0.0261 8   LEU A CD2 
63   N N   . TRP A 10  ? 0.6026 0.5796 0.6544 -0.0584 0.0294  -0.0187 9   TRP A N   
64   C CA  . TRP A 10  ? 0.5974 0.5649 0.6409 -0.0610 0.0257  -0.0150 9   TRP A CA  
65   C C   . TRP A 10  ? 0.6141 0.5721 0.6551 -0.0557 0.0227  -0.0141 9   TRP A C   
66   O O   . TRP A 10  ? 0.6569 0.6078 0.6934 -0.0563 0.0191  -0.0121 9   TRP A O   
67   C CB  . TRP A 10  ? 0.6413 0.6061 0.6771 -0.0640 0.0264  -0.0135 9   TRP A CB  
68   C CG  . TRP A 10  ? 0.6334 0.6048 0.6679 -0.0704 0.0282  -0.0122 9   TRP A CG  
69   C CD1 . TRP A 10  ? 0.6586 0.6380 0.6924 -0.0724 0.0321  -0.0136 9   TRP A CD1 
70   C CD2 . TRP A 10  ? 0.6374 0.6084 0.6712 -0.0761 0.0263  -0.0090 9   TRP A CD2 
71   N NE1 . TRP A 10  ? 0.6452 0.6300 0.6778 -0.0787 0.0333  -0.0108 9   TRP A NE1 
72   C CE2 . TRP A 10  ? 0.6075 0.5872 0.6407 -0.0815 0.0296  -0.0078 9   TRP A CE2 
73   C CE3 . TRP A 10  ? 0.6214 0.5854 0.6547 -0.0772 0.0218  -0.0071 9   TRP A CE3 
74   C CZ2 . TRP A 10  ? 0.5895 0.5715 0.6229 -0.0885 0.0290  -0.0040 9   TRP A CZ2 
75   C CZ3 . TRP A 10  ? 0.6612 0.6264 0.6945 -0.0843 0.0204  -0.0041 9   TRP A CZ3 
76   C CH2 . TRP A 10  ? 0.6153 0.5897 0.6493 -0.0902 0.0241  -0.0022 9   TRP A CH2 
77   N N   . THR A 11  ? 0.6016 0.5591 0.6455 -0.0508 0.0243  -0.0156 10  THR A N   
78   C CA  . THR A 11  ? 0.6306 0.5810 0.6730 -0.0455 0.0225  -0.0142 10  THR A CA  
79   C C   . THR A 11  ? 0.6092 0.5606 0.6550 -0.0432 0.0207  -0.0142 10  THR A C   
80   O O   . THR A 11  ? 0.6584 0.6030 0.6991 -0.0409 0.0178  -0.0126 10  THR A O   
81   C CB  . THR A 11  ? 0.6973 0.6482 0.7435 -0.0417 0.0248  -0.0152 10  THR A CB  
82   O OG1 . THR A 11  ? 0.6706 0.6180 0.7117 -0.0428 0.0246  -0.0142 10  THR A OG1 
83   C CG2 . THR A 11  ? 0.7743 0.7215 0.8224 -0.0361 0.0241  -0.0137 10  THR A CG2 
84   N N   . ALA A 12  ? 0.6256 0.5858 0.6797 -0.0434 0.0223  -0.0162 11  ALA A N   
85   C CA  . ALA A 12  ? 0.6859 0.6485 0.7439 -0.0412 0.0201  -0.0161 11  ALA A CA  
86   C C   . ALA A 12  ? 0.6413 0.6016 0.6947 -0.0452 0.0160  -0.0150 11  ALA A C   
87   O O   . ALA A 12  ? 0.6490 0.6065 0.7009 -0.0428 0.0126  -0.0144 11  ALA A O   
88   C CB  . ALA A 12  ? 0.6068 0.5802 0.6753 -0.0405 0.0226  -0.0184 11  ALA A CB  
89   N N   . ALA A 13  ? 0.6023 0.5632 0.6531 -0.0514 0.0161  -0.0145 12  ALA A N   
90   C CA  . ALA A 13  ? 0.5863 0.5434 0.6330 -0.0561 0.0118  -0.0132 12  ALA A CA  
91   C C   . ALA A 13  ? 0.6159 0.5590 0.6518 -0.0538 0.0083  -0.0120 12  ALA A C   
92   O O   . ALA A 13  ? 0.7005 0.6386 0.7330 -0.0534 0.0038  -0.0121 12  ALA A O   
93   C CB  . ALA A 13  ? 0.5029 0.4642 0.5498 -0.0637 0.0132  -0.0122 12  ALA A CB  
94   N N   . SER A 14  ? 0.6736 0.6108 0.7041 -0.0519 0.0101  -0.0111 13  SER A N   
95   C CA  . SER A 14  ? 0.6551 0.5798 0.6760 -0.0487 0.0074  -0.0099 13  SER A CA  
96   C C   . SER A 14  ? 0.6251 0.5477 0.6452 -0.0414 0.0068  -0.0104 13  SER A C   
97   O O   . SER A 14  ? 0.6137 0.5275 0.6261 -0.0388 0.0034  -0.0104 13  SER A O   
98   C CB  . SER A 14  ? 0.6027 0.5236 0.6195 -0.0481 0.0095  -0.0085 13  SER A CB  
99   O OG  . SER A 14  ? 0.6772 0.6035 0.6991 -0.0441 0.0132  -0.0090 13  SER A OG  
100  N N   . THR A 15  ? 0.7265 0.6566 0.7540 -0.0380 0.0101  -0.0108 14  THR A N   
101  C CA  . THR A 15  ? 0.7022 0.6310 0.7293 -0.0314 0.0098  -0.0102 14  THR A CA  
102  C C   . THR A 15  ? 0.6811 0.6110 0.7079 -0.0312 0.0059  -0.0111 14  THR A C   
103  O O   . THR A 15  ? 0.6898 0.6146 0.7105 -0.0264 0.0038  -0.0107 14  THR A O   
104  C CB  . THR A 15  ? 0.7389 0.6745 0.7747 -0.0284 0.0140  -0.0100 14  THR A CB  
105  O OG1 . THR A 15  ? 0.8193 0.7562 0.8571 -0.0307 0.0170  -0.0102 14  THR A OG1 
106  C CG2 . THR A 15  ? 0.7583 0.6908 0.7921 -0.0216 0.0147  -0.0078 14  THR A CG2 
107  N N   . LEU A 16  ? 0.6620 0.5992 0.6952 -0.0363 0.0048  -0.0124 15  LEU A N   
108  C CA  . LEU A 16  ? 0.6194 0.5587 0.6533 -0.0370 0.0002  -0.0133 15  LEU A CA  
109  C C   . LEU A 16  ? 0.6665 0.5948 0.6895 -0.0384 -0.0051 -0.0138 15  LEU A C   
110  O O   . LEU A 16  ? 0.7315 0.6565 0.7496 -0.0352 -0.0092 -0.0146 15  LEU A O   
111  C CB  . LEU A 16  ? 0.6063 0.5571 0.6506 -0.0428 0.0003  -0.0142 15  LEU A CB  
112  C CG  . LEU A 16  ? 0.5441 0.5005 0.5924 -0.0438 -0.0046 -0.0149 15  LEU A CG  
113  C CD1 . LEU A 16  ? 0.6508 0.6130 0.7043 -0.0369 -0.0038 -0.0146 15  LEU A CD1 
114  C CD2 . LEU A 16  ? 0.5665 0.5336 0.6242 -0.0512 -0.0045 -0.0153 15  LEU A CD2 
115  N N   . VAL A 17  ? 0.6298 0.5516 0.6482 -0.0430 -0.0053 -0.0136 16  VAL A N   
116  C CA  . VAL A 17  ? 0.6690 0.5781 0.6766 -0.0441 -0.0105 -0.0144 16  VAL A CA  
117  C C   . VAL A 17  ? 0.6466 0.5460 0.6441 -0.0361 -0.0101 -0.0143 16  VAL A C   
118  O O   . VAL A 17  ? 0.6132 0.5033 0.6013 -0.0337 -0.0146 -0.0160 16  VAL A O   
119  C CB  . VAL A 17  ? 0.6295 0.5341 0.6356 -0.0514 -0.0109 -0.0134 16  VAL A CB  
120  C CG1 . VAL A 17  ? 0.5665 0.4567 0.5623 -0.0532 -0.0169 -0.0145 16  VAL A CG1 
121  C CG2 . VAL A 17  ? 0.6089 0.5257 0.6258 -0.0590 -0.0098 -0.0128 16  VAL A CG2 
122  N N   . LYS A 18  ? 0.6218 0.5234 0.6210 -0.0319 -0.0048 -0.0126 17  LYS A N   
123  C CA  . LYS A 18  ? 0.6295 0.5239 0.6207 -0.0244 -0.0036 -0.0118 17  LYS A CA  
124  C C   . LYS A 18  ? 0.6523 0.5480 0.6407 -0.0181 -0.0045 -0.0122 17  LYS A C   
125  O O   . LYS A 18  ? 0.6277 0.5149 0.6054 -0.0133 -0.0069 -0.0132 17  LYS A O   
126  C CB  . LYS A 18  ? 0.6600 0.5584 0.6558 -0.0223 0.0020  -0.0095 17  LYS A CB  
127  C CG  . LYS A 18  ? 0.6323 0.5262 0.6223 -0.0146 0.0041  -0.0080 17  LYS A CG  
128  C CD  . LYS A 18  ? 0.6753 0.5737 0.6712 -0.0140 0.0088  -0.0057 17  LYS A CD  
129  C CE  . LYS A 18  ? 0.7050 0.6018 0.6976 -0.0063 0.0115  -0.0034 17  LYS A CE  
130  N NZ  . LYS A 18  ? 0.6819 0.5685 0.6637 -0.0030 0.0094  -0.0040 17  LYS A NZ  
131  N N   . ILE A 19  ? 0.6926 0.5985 0.6900 -0.0176 -0.0027 -0.0113 18  ILE A N   
132  C CA  . ILE A 19  ? 0.6447 0.5523 0.6395 -0.0117 -0.0038 -0.0107 18  ILE A CA  
133  C C   . ILE A 19  ? 0.6597 0.5641 0.6487 -0.0134 -0.0106 -0.0136 18  ILE A C   
134  O O   . ILE A 19  ? 0.6681 0.5687 0.6482 -0.0079 -0.0131 -0.0141 18  ILE A O   
135  C CB  . ILE A 19  ? 0.6971 0.6155 0.7035 -0.0104 -0.0003 -0.0086 18  ILE A CB  
136  C CG1 . ILE A 19  ? 0.6861 0.6127 0.7022 -0.0163 -0.0023 -0.0102 18  ILE A CG1 
137  C CG2 . ILE A 19  ? 0.6805 0.6010 0.6927 -0.0097 0.0056  -0.0064 18  ILE A CG2 
138  C CD1 . ILE A 19  ? 0.7015 0.6365 0.7247 -0.0131 -0.0026 -0.0090 18  ILE A CD1 
139  N N   . GLY A 20  ? 0.6789 0.5851 0.6726 -0.0211 -0.0139 -0.0154 19  GLY A N   
140  C CA  . GLY A 20  ? 0.7075 0.6105 0.6966 -0.0239 -0.0211 -0.0182 19  GLY A CA  
141  C C   . GLY A 20  ? 0.7431 0.6310 0.7175 -0.0222 -0.0250 -0.0207 19  GLY A C   
142  O O   . GLY A 20  ? 0.7111 0.5941 0.6766 -0.0194 -0.0302 -0.0232 19  GLY A O   
143  N N   . ALA A 21  ? 0.6576 0.5379 0.6288 -0.0236 -0.0227 -0.0202 20  ALA A N   
144  C CA  . ALA A 21  ? 0.6409 0.5058 0.5981 -0.0208 -0.0259 -0.0226 20  ALA A CA  
145  C C   . ALA A 21  ? 0.6612 0.5228 0.6088 -0.0103 -0.0235 -0.0225 20  ALA A C   
146  O O   . ALA A 21  ? 0.6715 0.5224 0.6062 -0.0062 -0.0275 -0.0257 20  ALA A O   
147  C CB  . ALA A 21  ? 0.6882 0.5464 0.6452 -0.0240 -0.0238 -0.0213 20  ALA A CB  
148  N N   . GLY A 22  ? 0.6856 0.5564 0.6394 -0.0059 -0.0170 -0.0189 21  GLY A N   
149  C CA  . GLY A 22  ? 0.6607 0.5303 0.6066 0.0037  -0.0140 -0.0177 21  GLY A CA  
150  C C   . GLY A 22  ? 0.6443 0.5163 0.5849 0.0074  -0.0175 -0.0188 21  GLY A C   
151  O O   . GLY A 22  ? 0.6252 0.4917 0.5533 0.0148  -0.0179 -0.0198 21  GLY A O   
152  N N   . LEU A 23  ? 0.6486 0.5294 0.5985 0.0027  -0.0199 -0.0185 22  LEU A N   
153  C CA  . LEU A 23  ? 0.6129 0.4966 0.5581 0.0058  -0.0243 -0.0194 22  LEU A CA  
154  C C   . LEU A 23  ? 0.6555 0.5288 0.5887 0.0043  -0.0325 -0.0249 22  LEU A C   
155  O O   . LEU A 23  ? 0.6633 0.5333 0.5847 0.0101  -0.0358 -0.0267 22  LEU A O   
156  C CB  . LEU A 23  ? 0.6365 0.5331 0.5962 0.0015  -0.0249 -0.0176 22  LEU A CB  
157  C CG  . LEU A 23  ? 0.6391 0.5454 0.6093 0.0046  -0.0179 -0.0125 22  LEU A CG  
158  C CD1 . LEU A 23  ? 0.5488 0.4664 0.5316 0.0016  -0.0196 -0.0115 22  LEU A CD1 
159  C CD2 . LEU A 23  ? 0.6183 0.5233 0.5799 0.0138  -0.0146 -0.0093 22  LEU A CD2 
160  N N   . LEU A 24  ? 0.6578 0.5255 0.5935 -0.0037 -0.0361 -0.0276 23  LEU A N   
161  C CA  . LEU A 24  ? 0.6556 0.5118 0.5806 -0.0062 -0.0446 -0.0331 23  LEU A CA  
162  C C   . LEU A 24  ? 0.7288 0.5705 0.6365 0.0015  -0.0445 -0.0359 23  LEU A C   
163  O O   . LEU A 24  ? 0.7529 0.5878 0.6472 0.0058  -0.0498 -0.0400 23  LEU A O   
164  C CB  . LEU A 24  ? 0.6427 0.4959 0.5754 -0.0169 -0.0477 -0.0341 23  LEU A CB  
165  C CG  . LEU A 24  ? 0.6039 0.4418 0.5259 -0.0207 -0.0563 -0.0395 23  LEU A CG  
166  C CD1 . LEU A 24  ? 0.5572 0.3974 0.4757 -0.0214 -0.0645 -0.0431 23  LEU A CD1 
167  C CD2 . LEU A 24  ? 0.5404 0.3755 0.4709 -0.0315 -0.0577 -0.0388 23  LEU A CD2 
168  N N   . VAL A 25  ? 0.7025 0.5398 0.6099 0.0039  -0.0386 -0.0340 24  VAL A N   
169  C CA  . VAL A 25  ? 0.7295 0.5542 0.6216 0.0122  -0.0377 -0.0365 24  VAL A CA  
170  C C   . VAL A 25  ? 0.7408 0.5703 0.6247 0.0225  -0.0342 -0.0353 24  VAL A C   
171  O O   . VAL A 25  ? 0.7753 0.5956 0.6431 0.0293  -0.0370 -0.0394 24  VAL A O   
172  C CB  . VAL A 25  ? 0.6020 0.4235 0.4980 0.0125  -0.0319 -0.0338 24  VAL A CB  
173  C CG1 . VAL A 25  ? 0.6619 0.4725 0.5435 0.0224  -0.0301 -0.0359 24  VAL A CG1 
174  C CG2 . VAL A 25  ? 0.6414 0.4566 0.5430 0.0026  -0.0358 -0.0347 24  VAL A CG2 
175  N N   . GLY A 26  ? 0.7393 0.5831 0.6337 0.0239  -0.0283 -0.0296 25  GLY A N   
176  C CA  . GLY A 26  ? 0.7666 0.6157 0.6540 0.0333  -0.0245 -0.0270 25  GLY A CA  
177  C C   . GLY A 26  ? 0.7283 0.5758 0.6046 0.0357  -0.0313 -0.0305 25  GLY A C   
178  O O   . GLY A 26  ? 0.6664 0.5106 0.5279 0.0445  -0.0306 -0.0315 25  GLY A O   
179  N N   . LYS A 27  ? 0.6972 0.5480 0.5801 0.0280  -0.0380 -0.0323 26  LYS A N   
180  C CA  . LYS A 27  ? 0.7105 0.5603 0.5834 0.0296  -0.0458 -0.0359 26  LYS A CA  
181  C C   . LYS A 27  ? 0.7898 0.6230 0.6448 0.0315  -0.0522 -0.0436 26  LYS A C   
182  O O   . LYS A 27  ? 0.8508 0.6803 0.6903 0.0378  -0.0561 -0.0469 26  LYS A O   
183  C CB  . LYS A 27  ? 0.7508 0.6091 0.6372 0.0205  -0.0517 -0.0359 26  LYS A CB  
184  C CG  . LYS A 27  ? 0.8041 0.6644 0.6826 0.0218  -0.0601 -0.0388 26  LYS A CG  
185  C CD  . LYS A 27  ? 0.9204 0.7901 0.7957 0.0304  -0.0563 -0.0336 26  LYS A CD  
186  C CE  . LYS A 27  ? 0.8407 0.7062 0.6973 0.0363  -0.0633 -0.0376 26  LYS A CE  
187  N NZ  . LYS A 27  ? 0.7141 0.5901 0.5687 0.0436  -0.0606 -0.0316 26  LYS A NZ  
188  N N   . LEU A 28  ? 0.8041 0.6266 0.6603 0.0265  -0.0535 -0.0466 27  LEU A N   
189  C CA  . LEU A 28  ? 0.7912 0.5957 0.6305 0.0288  -0.0592 -0.0540 27  LEU A CA  
190  C C   . LEU A 28  ? 0.8234 0.6221 0.6476 0.0413  -0.0533 -0.0545 27  LEU A C   
191  O O   . LEU A 28  ? 0.8331 0.6196 0.6391 0.0470  -0.0579 -0.0610 27  LEU A O   
192  C CB  . LEU A 28  ? 0.7573 0.5514 0.6026 0.0204  -0.0617 -0.0559 27  LEU A CB  
193  C CG  . LEU A 28  ? 0.7605 0.5588 0.6194 0.0075  -0.0680 -0.0560 27  LEU A CG  
194  C CD1 . LEU A 28  ? 0.7368 0.5208 0.5964 0.0001  -0.0715 -0.0585 27  LEU A CD1 
195  C CD2 . LEU A 28  ? 0.7250 0.5251 0.5787 0.0057  -0.0772 -0.0601 27  LEU A CD2 
196  N N   . LEU A 29  ? 0.9074 0.7150 0.7392 0.0456  -0.0433 -0.0480 28  LEU A N   
197  C CA  . LEU A 29  ? 0.9004 0.7062 0.7199 0.0576  -0.0367 -0.0473 28  LEU A CA  
198  C C   . LEU A 29  ? 0.9054 0.7159 0.7119 0.0652  -0.0376 -0.0476 28  LEU A C   
199  O O   . LEU A 29  ? 0.9082 0.7111 0.6965 0.0748  -0.0371 -0.0515 28  LEU A O   
200  C CB  . LEU A 29  ? 0.8882 0.7052 0.7210 0.0594  -0.0261 -0.0394 28  LEU A CB  
201  C CG  . LEU A 29  ? 0.8406 0.6517 0.6781 0.0591  -0.0222 -0.0388 28  LEU A CG  
202  C CD1 . LEU A 29  ? 0.8127 0.6163 0.6352 0.0708  -0.0184 -0.0411 28  LEU A CD1 
203  C CD2 . LEU A 29  ? 0.8449 0.6446 0.6856 0.0497  -0.0293 -0.0431 28  LEU A CD2 
204  N N   . ALA A 30  ? 0.8717 0.6947 0.6868 0.0616  -0.0387 -0.0435 29  ALA A N   
205  C CA  . ALA A 30  ? 0.8421 0.6709 0.6455 0.0691  -0.0391 -0.0424 29  ALA A CA  
206  C C   . ALA A 30  ? 0.8937 0.7122 0.6803 0.0694  -0.0501 -0.0510 29  ALA A C   
207  O O   . ALA A 30  ? 0.9542 0.7692 0.7216 0.0787  -0.0505 -0.0537 29  ALA A O   
208  C CB  . ALA A 30  ? 0.7600 0.6048 0.5784 0.0657  -0.0371 -0.0347 29  ALA A CB  
209  N N   . VAL A 31  ? 0.8626 0.6765 0.6559 0.0592  -0.0590 -0.0554 30  VAL A N   
210  C CA  . VAL A 31  ? 0.8712 0.6754 0.6501 0.0582  -0.0706 -0.0638 30  VAL A CA  
211  C C   . VAL A 31  ? 0.8764 0.6617 0.6357 0.0642  -0.0725 -0.0720 30  VAL A C   
212  O O   . VAL A 31  ? 0.9310 0.7082 0.6710 0.0693  -0.0791 -0.0788 30  VAL A O   
213  C CB  . VAL A 31  ? 0.8131 0.6180 0.6064 0.0448  -0.0793 -0.0658 30  VAL A CB  
214  C CG1 . VAL A 31  ? 0.7319 0.5258 0.5111 0.0426  -0.0922 -0.0750 30  VAL A CG1 
215  C CG2 . VAL A 31  ? 0.7796 0.6035 0.5909 0.0406  -0.0775 -0.0583 30  VAL A CG2 
216  N N   . SER A 32  ? 0.9157 0.6936 0.6790 0.0644  -0.0669 -0.0717 31  SER A N   
217  C CA  . SER A 32  ? 0.9331 0.6916 0.6789 0.0699  -0.0696 -0.0799 31  SER A CA  
218  C C   . SER A 32  ? 0.8960 0.6548 0.6257 0.0847  -0.0615 -0.0796 31  SER A C   
219  O O   . SER A 32  ? 0.8982 0.6440 0.6066 0.0923  -0.0654 -0.0876 31  SER A O   
220  C CB  . SER A 32  ? 0.8603 0.6095 0.6168 0.0637  -0.0683 -0.0799 31  SER A CB  
221  O OG  . SER A 32  ? 0.8583 0.6112 0.6319 0.0500  -0.0737 -0.0782 31  SER A OG  
222  N N   . PHE A 33  ? 0.8289 0.6025 0.5684 0.0888  -0.0503 -0.0704 32  PHE A N   
223  C CA  . PHE A 33  ? 0.8350 0.6106 0.5626 0.1022  -0.0411 -0.0687 32  PHE A CA  
224  C C   . PHE A 33  ? 0.8647 0.6572 0.5906 0.1081  -0.0351 -0.0614 32  PHE A C   
225  O O   . PHE A 33  ? 0.8469 0.6403 0.5574 0.1199  -0.0294 -0.0614 32  PHE A O   
226  C CB  . PHE A 33  ? 0.8381 0.6152 0.5780 0.1032  -0.0321 -0.0641 32  PHE A CB  
227  C CG  . PHE A 33  ? 0.8873 0.6488 0.6311 0.0967  -0.0374 -0.0693 32  PHE A CG  
228  C CD1 . PHE A 33  ? 0.8756 0.6172 0.6016 0.1010  -0.0437 -0.0792 32  PHE A CD1 
229  C CD2 . PHE A 33  ? 0.8386 0.6046 0.6032 0.0866  -0.0362 -0.0643 32  PHE A CD2 
230  C CE1 . PHE A 33  ? 0.8622 0.5885 0.5920 0.0949  -0.0486 -0.0833 32  PHE A CE1 
231  C CE2 . PHE A 33  ? 0.8335 0.5854 0.6012 0.0806  -0.0408 -0.0681 32  PHE A CE2 
232  C CZ  . PHE A 33  ? 0.7847 0.5164 0.5353 0.0846  -0.0471 -0.0773 32  PHE A CZ  
233  N N   . GLY A 34  ? 0.8003 0.6058 0.5411 0.1008  -0.0358 -0.0549 33  GLY A N   
234  C CA  . GLY A 34  ? 0.7950 0.6150 0.5343 0.1059  -0.0312 -0.0476 33  GLY A CA  
235  C C   . GLY A 34  ? 0.8404 0.6717 0.5878 0.1114  -0.0181 -0.0383 33  GLY A C   
236  O O   . GLY A 34  ? 0.9033 0.7338 0.6621 0.1096  -0.0128 -0.0366 33  GLY A O   
237  N N   . PRO A 35  ? 0.7954 0.6380 0.5375 0.1180  -0.0129 -0.0316 34  PRO A N   
238  C CA  . PRO A 35  ? 0.7880 0.6427 0.5394 0.1224  -0.0005 -0.0216 34  PRO A CA  
239  C C   . PRO A 35  ? 0.8189 0.6694 0.5608 0.1317  0.0067  -0.0237 34  PRO A C   
240  O O   . PRO A 35  ? 0.8177 0.6763 0.5726 0.1325  0.0159  -0.0170 34  PRO A O   
241  C CB  . PRO A 35  ? 0.8652 0.7308 0.6096 0.1275  0.0019  -0.0146 34  PRO A CB  
242  C CG  . PRO A 35  ? 0.8319 0.6937 0.5711 0.1226  -0.0099 -0.0195 34  PRO A CG  
243  C CD  . PRO A 35  ? 0.7854 0.6312 0.5147 0.1207  -0.0185 -0.0317 34  PRO A CD  
244  N N   . ALA A 36  ? 0.9295 0.7678 0.6494 0.1389  0.0025  -0.0331 35  ALA A N   
245  C CA  . ALA A 36  ? 0.8475 0.6815 0.5578 0.1489  0.0093  -0.0357 35  ALA A CA  
246  C C   . ALA A 36  ? 0.8652 0.6931 0.5903 0.1438  0.0100  -0.0374 35  ALA A C   
247  O O   . ALA A 36  ? 0.9373 0.7724 0.6711 0.1478  0.0193  -0.0321 35  ALA A O   
248  C CB  . ALA A 36  ? 0.8556 0.6758 0.5383 0.1577  0.0035  -0.0467 35  ALA A CB  
249  N N   . GLY A 37  ? 0.8159 0.6311 0.5442 0.1349  0.0002  -0.0443 36  GLY A N   
250  C CA  . GLY A 37  ? 0.8569 0.6663 0.5993 0.1292  0.0003  -0.0451 36  GLY A CA  
251  C C   . GLY A 37  ? 0.7811 0.6049 0.5484 0.1214  0.0060  -0.0352 36  GLY A C   
252  O O   . GLY A 37  ? 0.7950 0.6200 0.5734 0.1209  0.0108  -0.0327 36  GLY A O   
253  N N   . LEU A 38  ? 0.7685 0.6028 0.5444 0.1156  0.0052  -0.0298 37  LEU A N   
254  C CA  . LEU A 38  ? 0.7611 0.6083 0.5599 0.1086  0.0104  -0.0209 37  LEU A CA  
255  C C   . LEU A 38  ? 0.7559 0.6153 0.5596 0.1156  0.0219  -0.0128 37  LEU A C   
256  O O   . LEU A 38  ? 0.7946 0.6611 0.6162 0.1112  0.0267  -0.0074 37  LEU A O   
257  C CB  . LEU A 38  ? 0.7308 0.5856 0.5367 0.1020  0.0067  -0.0173 37  LEU A CB  
258  C CG  . LEU A 38  ? 0.7707 0.6222 0.5897 0.0898  -0.0007 -0.0200 37  LEU A CG  
259  C CD1 . LEU A 38  ? 0.8322 0.6682 0.6387 0.0878  -0.0105 -0.0301 37  LEU A CD1 
260  C CD2 . LEU A 38  ? 0.7468 0.6084 0.5751 0.0849  -0.0026 -0.0152 37  LEU A CD2 
261  N N   . GLY A 39  ? 0.7517 0.6140 0.5398 0.1264  0.0264  -0.0119 38  GLY A N   
262  C CA  . GLY A 39  ? 0.7588 0.6337 0.5516 0.1333  0.0377  -0.0038 38  GLY A CA  
263  C C   . GLY A 39  ? 0.8140 0.6853 0.6068 0.1388  0.0419  -0.0064 38  GLY A C   
264  O O   . GLY A 39  ? 0.8606 0.7432 0.6670 0.1399  0.0501  0.0008  38  GLY A O   
265  N N   . LEU A 40  ? 0.8054 0.6610 0.5835 0.1425  0.0361  -0.0165 39  LEU A N   
266  C CA  . LEU A 40  ? 0.8110 0.6615 0.5891 0.1481  0.0391  -0.0194 39  LEU A CA  
267  C C   . LEU A 40  ? 0.8226 0.6723 0.6208 0.1384  0.0375  -0.0177 39  LEU A C   
268  O O   . LEU A 40  ? 0.8039 0.6584 0.6108 0.1416  0.0432  -0.0146 39  LEU A O   
269  C CB  . LEU A 40  ? 0.7810 0.6125 0.5373 0.1546  0.0326  -0.0311 39  LEU A CB  
270  C CG  . LEU A 40  ? 0.7503 0.5815 0.4846 0.1690  0.0369  -0.0342 39  LEU A CG  
271  C CD1 . LEU A 40  ? 0.7252 0.5349 0.4381 0.1729  0.0278  -0.0471 39  LEU A CD1 
272  C CD2 . LEU A 40  ? 0.7012 0.5426 0.4399 0.1790  0.0480  -0.0295 39  LEU A CD2 
273  N N   . ALA A 41  ? 0.7651 0.6097 0.5706 0.1268  0.0298  -0.0194 40  ALA A N   
274  C CA  . ALA A 41  ? 0.7283 0.5716 0.5509 0.1171  0.0276  -0.0182 40  ALA A CA  
275  C C   . ALA A 41  ? 0.7568 0.6166 0.6002 0.1106  0.0330  -0.0088 40  ALA A C   
276  O O   . ALA A 41  ? 0.8064 0.6664 0.6641 0.1019  0.0311  -0.0076 40  ALA A O   
277  C CB  . ALA A 41  ? 0.7246 0.5549 0.5452 0.1076  0.0171  -0.0246 40  ALA A CB  
278  N N   . ALA A 42  ? 0.8010 0.6738 0.6457 0.1147  0.0396  -0.0021 41  ALA A N   
279  C CA  . ALA A 42  ? 0.7405 0.6275 0.6048 0.1083  0.0443  0.0067  41  ALA A CA  
280  C C   . ALA A 42  ? 0.7670 0.6604 0.6455 0.1080  0.0494  0.0104  41  ALA A C   
281  O O   . ALA A 42  ? 0.8247 0.7213 0.7193 0.0991  0.0483  0.0127  41  ALA A O   
282  C CB  . ALA A 42  ? 0.7502 0.6487 0.6119 0.1132  0.0503  0.0136  41  ALA A CB  
283  N N   . ASN A 43  ? 0.6674 0.5633 0.5402 0.1181  0.0550  0.0110  42  ASN A N   
284  C CA  . ASN A 43  ? 0.6893 0.5925 0.5759 0.1185  0.0595  0.0147  42  ASN A CA  
285  C C   . ASN A 43  ? 0.7566 0.6479 0.6450 0.1142  0.0531  0.0089  42  ASN A C   
286  O O   . ASN A 43  ? 0.7196 0.6164 0.6231 0.1096  0.0541  0.0121  42  ASN A O   
287  C CB  . ASN A 43  ? 0.6861 0.5961 0.5662 0.1312  0.0673  0.0168  42  ASN A CB  
288  C CG  . ASN A 43  ? 0.6578 0.5816 0.5377 0.1351  0.0748  0.0243  42  ASN A CG  
289  O OD1 . ASN A 43  ? 0.7083 0.6367 0.5948 0.1280  0.0742  0.0287  42  ASN A OD1 
290  N ND2 . ASN A 43  ? 0.6183 0.5490 0.4908 0.1467  0.0821  0.0262  42  ASN A ND2 
291  N N   . PHE A 44  ? 0.7808 0.6556 0.6538 0.1155  0.0463  0.0006  43  PHE A N   
292  C CA  . PHE A 44  ? 0.6840 0.5461 0.5580 0.1110  0.0400  -0.0043 43  PHE A CA  
293  C C   . PHE A 44  ? 0.6986 0.5618 0.5859 0.0976  0.0356  -0.0029 43  PHE A C   
294  O O   . PHE A 44  ? 0.7033 0.5670 0.6014 0.0926  0.0347  -0.0015 43  PHE A O   
295  C CB  . PHE A 44  ? 0.6233 0.4667 0.4776 0.1151  0.0336  -0.0134 43  PHE A CB  
296  C CG  . PHE A 44  ? 0.6177 0.4463 0.4719 0.1102  0.0267  -0.0181 43  PHE A CG  
297  C CD1 . PHE A 44  ? 0.5960 0.4204 0.4507 0.1162  0.0282  -0.0184 43  PHE A CD1 
298  C CD2 . PHE A 44  ? 0.6331 0.4524 0.4870 0.0998  0.0189  -0.0216 43  PHE A CD2 
299  C CE1 . PHE A 44  ? 0.6396 0.4495 0.4937 0.1117  0.0218  -0.0219 43  PHE A CE1 
300  C CE2 . PHE A 44  ? 0.6533 0.4590 0.5071 0.0948  0.0128  -0.0249 43  PHE A CE2 
301  C CZ  . PHE A 44  ? 0.6580 0.4584 0.5115 0.1007  0.0142  -0.0250 43  PHE A CZ  
302  N N   . ARG A 45  ? 0.7099 0.5741 0.5964 0.0920  0.0329  -0.0031 44  ARG A N   
303  C CA  . ARG A 45  ? 0.7300 0.5959 0.6289 0.0800  0.0292  -0.0021 44  ARG A CA  
304  C C   . ARG A 45  ? 0.7399 0.6201 0.6572 0.0761  0.0346  0.0050  44  ARG A C   
305  O O   . ARG A 45  ? 0.7241 0.6047 0.6520 0.0677  0.0322  0.0053  44  ARG A O   
306  C CB  . ARG A 45  ? 0.6673 0.5328 0.5620 0.0763  0.0256  -0.0035 44  ARG A CB  
307  C CG  . ARG A 45  ? 0.7191 0.5697 0.5978 0.0770  0.0181  -0.0114 44  ARG A CG  
308  C CD  . ARG A 45  ? 0.7640 0.6164 0.6382 0.0750  0.0148  -0.0122 44  ARG A CD  
309  N NE  . ARG A 45  ? 0.8511 0.7059 0.7371 0.0640  0.0107  -0.0118 44  ARG A NE  
310  C CZ  . ARG A 45  ? 0.8224 0.6809 0.7092 0.0606  0.0076  -0.0118 44  ARG A CZ  
311  N NH1 . ARG A 45  ? 0.7408 0.6006 0.6165 0.0670  0.0075  -0.0118 44  ARG A NH1 
312  N NH2 . ARG A 45  ? 0.9149 0.7765 0.8136 0.0511  0.0045  -0.0115 44  ARG A NH2 
313  N N   . GLN A 46  ? 0.7876 0.6795 0.7086 0.0817  0.0417  0.0107  45  GLN A N   
314  C CA  . GLN A 46  ? 0.7605 0.6654 0.6994 0.0780  0.0464  0.0173  45  GLN A CA  
315  C C   . GLN A 46  ? 0.6995 0.6044 0.6441 0.0788  0.0467  0.0172  45  GLN A C   
316  O O   . GLN A 46  ? 0.6931 0.6044 0.6520 0.0722  0.0469  0.0201  45  GLN A O   
317  C CB  . GLN A 46  ? 0.8312 0.7487 0.7729 0.0838  0.0540  0.0240  45  GLN A CB  
318  C CG  . GLN A 46  ? 0.8115 0.7413 0.7717 0.0772  0.0575  0.0309  45  GLN A CG  
319  C CD  . GLN A 46  ? 0.9454 0.8717 0.9130 0.0668  0.0523  0.0288  45  GLN A CD  
320  O OE1 . GLN A 46  ? 0.8334 0.7595 0.8103 0.0606  0.0500  0.0277  45  GLN A OE1 
321  N NE2 . GLN A 46  ? 1.0894 1.0137 1.0527 0.0652  0.0504  0.0284  45  GLN A NE2 
322  N N   . LEU A 47  ? 0.6852 0.5826 0.6185 0.0870  0.0464  0.0138  46  LEU A N   
323  C CA  . LEU A 47  ? 0.6624 0.5583 0.6002 0.0883  0.0458  0.0136  46  LEU A CA  
324  C C   . LEU A 47  ? 0.6515 0.5378 0.5913 0.0791  0.0388  0.0102  46  LEU A C   
325  O O   . LEU A 47  ? 0.7002 0.5903 0.6504 0.0754  0.0383  0.0124  46  LEU A O   
326  C CB  . LEU A 47  ? 0.6502 0.5384 0.5742 0.1001  0.0467  0.0101  46  LEU A CB  
327  C CG  . LEU A 47  ? 0.6366 0.5176 0.5612 0.1020  0.0439  0.0083  46  LEU A CG  
328  C CD1 . LEU A 47  ? 0.6154 0.5118 0.5539 0.1060  0.0496  0.0145  46  LEU A CD1 
329  C CD2 . LEU A 47  ? 0.6286 0.4933 0.5351 0.1110  0.0412  0.0017  46  LEU A CD2 
330  N N   . ILE A 48  ? 0.6423 0.5169 0.5726 0.0751  0.0333  0.0051  47  ILE A N   
331  C CA  . ILE A 48  ? 0.6305 0.4973 0.5633 0.0656  0.0272  0.0026  47  ILE A CA  
332  C C   . ILE A 48  ? 0.6810 0.5591 0.6291 0.0564  0.0283  0.0064  47  ILE A C   
333  O O   . ILE A 48  ? 0.6991 0.5770 0.6540 0.0501  0.0260  0.0068  47  ILE A O   
334  C CB  . ILE A 48  ? 0.6557 0.5091 0.5760 0.0631  0.0212  -0.0033 47  ILE A CB  
335  C CG1 . ILE A 48  ? 0.7051 0.5456 0.6094 0.0725  0.0196  -0.0079 47  ILE A CG1 
336  C CG2 . ILE A 48  ? 0.6567 0.5034 0.5804 0.0528  0.0155  -0.0051 47  ILE A CG2 
337  C CD1 . ILE A 48  ? 0.7045 0.5400 0.6086 0.0773  0.0199  -0.0076 47  ILE A CD1 
338  N N   . THR A 49  ? 0.6729 0.5608 0.6263 0.0559  0.0319  0.0092  48  THR A N   
339  C CA  . THR A 49  ? 0.6308 0.5283 0.5985 0.0479  0.0330  0.0124  48  THR A CA  
340  C C   . THR A 49  ? 0.6628 0.5696 0.6426 0.0476  0.0361  0.0166  48  THR A C   
341  O O   . THR A 49  ? 0.7182 0.6274 0.7068 0.0403  0.0343  0.0168  48  THR A O   
342  C CB  . THR A 49  ? 0.6931 0.5976 0.6634 0.0484  0.0360  0.0150  48  THR A CB  
343  O OG1 . THR A 49  ? 0.7714 0.6681 0.7319 0.0474  0.0319  0.0110  48  THR A OG1 
344  C CG2 . THR A 49  ? 0.6619 0.5754 0.6475 0.0410  0.0374  0.0182  48  THR A CG2 
345  N N   . VAL A 50  ? 0.6536 0.5666 0.6342 0.0555  0.0408  0.0199  49  VAL A N   
346  C CA  . VAL A 50  ? 0.6486 0.5717 0.6416 0.0553  0.0434  0.0241  49  VAL A CA  
347  C C   . VAL A 50  ? 0.7151 0.6318 0.7058 0.0553  0.0395  0.0219  49  VAL A C   
348  O O   . VAL A 50  ? 0.7395 0.6633 0.7408 0.0522  0.0392  0.0244  49  VAL A O   
349  C CB  . VAL A 50  ? 0.5993 0.5330 0.5955 0.0637  0.0500  0.0291  49  VAL A CB  
350  C CG1 . VAL A 50  ? 0.6513 0.5903 0.6482 0.0639  0.0538  0.0320  49  VAL A CG1 
351  C CG2 . VAL A 50  ? 0.6101 0.5371 0.5934 0.0741  0.0506  0.0267  49  VAL A CG2 
352  N N   . LEU A 51  ? 0.7015 0.6044 0.6784 0.0586  0.0359  0.0174  50  LEU A N   
353  C CA  . LEU A 51  ? 0.6844 0.5792 0.6585 0.0580  0.0316  0.0157  50  LEU A CA  
354  C C   . LEU A 51  ? 0.7411 0.6337 0.7195 0.0470  0.0273  0.0147  50  LEU A C   
355  O O   . LEU A 51  ? 0.7395 0.6307 0.7204 0.0447  0.0246  0.0154  50  LEU A O   
356  C CB  . LEU A 51  ? 0.6464 0.5254 0.6044 0.0642  0.0287  0.0111  50  LEU A CB  
357  C CG  . LEU A 51  ? 0.7130 0.5925 0.6664 0.0765  0.0321  0.0118  50  LEU A CG  
358  C CD1 . LEU A 51  ? 0.7335 0.5964 0.6694 0.0828  0.0294  0.0061  50  LEU A CD1 
359  C CD2 . LEU A 51  ? 0.7679 0.6504 0.7282 0.0784  0.0315  0.0146  50  LEU A CD2 
360  N N   . GLY A 52  ? 0.6893 0.5821 0.6686 0.0405  0.0266  0.0131  51  GLY A N   
361  C CA  . GLY A 52  ? 0.7132 0.6060 0.6973 0.0306  0.0234  0.0121  51  GLY A CA  
362  C C   . GLY A 52  ? 0.7389 0.6438 0.7365 0.0264  0.0251  0.0153  51  GLY A C   
363  O O   . GLY A 52  ? 0.7053 0.6106 0.7061 0.0188  0.0227  0.0143  51  GLY A O   
364  N N   . VAL A 53  ? 0.8018 0.7168 0.8070 0.0310  0.0292  0.0190  52  VAL A N   
365  C CA  . VAL A 53  ? 0.7053 0.6322 0.7242 0.0269  0.0305  0.0219  52  VAL A CA  
366  C C   . VAL A 53  ? 0.6906 0.6230 0.7135 0.0322  0.0311  0.0251  52  VAL A C   
367  O O   . VAL A 53  ? 0.8092 0.7484 0.8408 0.0284  0.0296  0.0267  52  VAL A O   
368  C CB  . VAL A 53  ? 0.6724 0.6080 0.7000 0.0260  0.0346  0.0242  52  VAL A CB  
369  C CG1 . VAL A 53  ? 0.7042 0.6509 0.7464 0.0210  0.0353  0.0268  52  VAL A CG1 
370  C CG2 . VAL A 53  ? 0.5915 0.5219 0.6153 0.0217  0.0337  0.0212  52  VAL A CG2 
371  N N   . LEU A 54  ? 0.7654 0.6951 0.7820 0.0414  0.0331  0.0259  53  LEU A N   
372  C CA  . LEU A 54  ? 0.7816 0.7188 0.8034 0.0481  0.0348  0.0294  53  LEU A CA  
373  C C   . LEU A 54  ? 0.8272 0.7541 0.8397 0.0531  0.0312  0.0279  53  LEU A C   
374  O O   . LEU A 54  ? 0.8939 0.8265 0.9105 0.0595  0.0322  0.0307  53  LEU A O   
375  C CB  . LEU A 54  ? 0.8347 0.7794 0.8581 0.0562  0.0410  0.0324  53  LEU A CB  
376  C CG  . LEU A 54  ? 0.8637 0.8249 0.9029 0.0540  0.0455  0.0376  53  LEU A CG  
377  C CD1 . LEU A 54  ? 0.7885 0.7508 0.8342 0.0435  0.0440  0.0367  53  LEU A CD1 
378  C CD2 . LEU A 54  ? 0.7438 0.7103 0.7812 0.0617  0.0520  0.0405  53  LEU A CD2 
379  N N   . ALA A 55  ? 0.8739 0.7857 0.8745 0.0503  0.0270  0.0238  54  ALA A N   
380  C CA  . ALA A 55  ? 0.9220 0.8221 0.9136 0.0547  0.0233  0.0227  54  ALA A CA  
381  C C   . ALA A 55  ? 0.9658 0.8698 0.9636 0.0510  0.0198  0.0253  54  ALA A C   
382  O O   . ALA A 55  ? 0.9576 0.8602 0.9547 0.0575  0.0185  0.0272  54  ALA A O   
383  C CB  . ALA A 55  ? 0.8152 0.6981 0.7933 0.0517  0.0194  0.0181  54  ALA A CB  
384  N N   . GLY A 56  ? 0.9581 0.8669 0.9618 0.0411  0.0181  0.0254  55  GLY A N   
385  C CA  . GLY A 56  ? 0.9178 0.8311 0.9265 0.0371  0.0146  0.0277  55  GLY A CA  
386  C C   . GLY A 56  ? 0.9180 0.8489 0.9417 0.0354  0.0165  0.0306  55  GLY A C   
387  O O   . GLY A 56  ? 1.0494 0.9858 1.0784 0.0284  0.0138  0.0310  55  GLY A O   
388  N N   . ALA A 57  ? 0.7417 0.6818 0.7724 0.0416  0.0212  0.0327  56  ALA A N   
389  C CA  . ALA A 57  ? 0.6966 0.6539 0.7430 0.0403  0.0235  0.0362  56  ALA A CA  
390  C C   . ALA A 57  ? 0.7070 0.6691 0.7601 0.0304  0.0236  0.0348  56  ALA A C   
391  O O   . ALA A 57  ? 0.6909 0.6654 0.7570 0.0267  0.0236  0.0369  56  ALA A O   
392  C CB  . ALA A 57  ? 0.6734 0.6383 0.7265 0.0417  0.0199  0.0393  56  ALA A CB  
393  N N   . GLY A 58  ? 0.6896 0.6420 0.7347 0.0260  0.0235  0.0310  57  GLY A N   
394  C CA  . GLY A 58  ? 0.6865 0.6425 0.7376 0.0179  0.0240  0.0293  57  GLY A CA  
395  C C   . GLY A 58  ? 0.6515 0.6113 0.7072 0.0101  0.0200  0.0282  57  GLY A C   
396  O O   . GLY A 58  ? 0.6069 0.5728 0.6711 0.0044  0.0206  0.0273  57  GLY A O   
397  N N   . ILE A 59  ? 0.6177 0.5736 0.6674 0.0100  0.0158  0.0281  58  ILE A N   
398  C CA  . ILE A 59  ? 0.6093 0.5692 0.6616 0.0032  0.0117  0.0270  58  ILE A CA  
399  C C   . ILE A 59  ? 0.6323 0.5845 0.6766 -0.0037 0.0104  0.0229  58  ILE A C   
400  O O   . ILE A 59  ? 0.6699 0.6246 0.7140 -0.0093 0.0073  0.0214  58  ILE A O   
401  C CB  . ILE A 59  ? 0.5678 0.5279 0.6172 0.0064  0.0075  0.0298  58  ILE A CB  
402  C CG1 . ILE A 59  ? 0.5273 0.4730 0.5621 0.0087  0.0059  0.0292  58  ILE A CG1 
403  C CG2 . ILE A 59  ? 0.5431 0.5123 0.6013 0.0139  0.0090  0.0340  58  ILE A CG2 
404  C CD1 . ILE A 59  ? 0.5604 0.5042 0.5910 0.0112  0.0013  0.0322  58  ILE A CD1 
405  N N   . PHE A 60  ? 0.6337 0.5777 0.6717 -0.0033 0.0128  0.0208  59  PHE A N   
406  C CA  . PHE A 60  ? 0.5994 0.5368 0.6299 -0.0092 0.0116  0.0174  59  PHE A CA  
407  C C   . PHE A 60  ? 0.5404 0.4843 0.5774 -0.0160 0.0120  0.0144  59  PHE A C   
408  O O   . PHE A 60  ? 0.5742 0.5170 0.6068 -0.0213 0.0100  0.0121  59  PHE A O   
409  C CB  . PHE A 60  ? 0.5802 0.5091 0.6044 -0.0072 0.0137  0.0160  59  PHE A CB  
410  C CG  . PHE A 60  ? 0.7106 0.6332 0.7293 0.0006  0.0140  0.0181  59  PHE A CG  
411  C CD1 . PHE A 60  ? 0.6931 0.6082 0.7038 0.0027  0.0108  0.0194  59  PHE A CD1 
412  C CD2 . PHE A 60  ? 0.7198 0.6438 0.7408 0.0062  0.0175  0.0187  59  PHE A CD2 
413  C CE1 . PHE A 60  ? 0.6392 0.5473 0.6444 0.0106  0.0109  0.0207  59  PHE A CE1 
414  C CE2 . PHE A 60  ? 0.7408 0.6589 0.7556 0.0141  0.0180  0.0200  59  PHE A CE2 
415  C CZ  . PHE A 60  ? 0.7467 0.6566 0.7537 0.0164  0.0146  0.0206  59  PHE A CZ  
416  N N   . ASN A 61  ? 0.5211 0.4716 0.5685 -0.0157 0.0145  0.0144  60  ASN A N   
417  C CA  . ASN A 61  ? 0.5350 0.4904 0.5890 -0.0217 0.0144  0.0112  60  ASN A CA  
418  C C   . ASN A 61  ? 0.5768 0.5384 0.6337 -0.0249 0.0106  0.0109  60  ASN A C   
419  O O   . ASN A 61  ? 0.5982 0.5611 0.6547 -0.0303 0.0092  0.0070  60  ASN A O   
420  C CB  . ASN A 61  ? 0.5098 0.4695 0.5745 -0.0207 0.0177  0.0120  60  ASN A CB  
421  C CG  . ASN A 61  ? 0.5002 0.4546 0.5624 -0.0208 0.0205  0.0099  60  ASN A CG  
422  O OD1 . ASN A 61  ? 0.4710 0.4200 0.5251 -0.0227 0.0199  0.0071  60  ASN A OD1 
423  N ND2 . ASN A 61  ? 0.5049 0.4616 0.5746 -0.0188 0.0236  0.0118  60  ASN A ND2 
424  N N   . GLY A 62  ? 0.5581 0.5238 0.6175 -0.0213 0.0088  0.0148  61  GLY A N   
425  C CA  . GLY A 62  ? 0.5387 0.5101 0.5992 -0.0239 0.0042  0.0149  61  GLY A CA  
426  C C   . GLY A 62  ? 0.5645 0.5301 0.6121 -0.0253 0.0012  0.0144  61  GLY A C   
427  O O   . GLY A 62  ? 0.5475 0.5164 0.5929 -0.0296 -0.0022 0.0126  61  GLY A O   
428  N N   . VAL A 63  ? 0.5512 0.5079 0.5898 -0.0220 0.0023  0.0161  62  VAL A N   
429  C CA  . VAL A 63  ? 0.5525 0.5025 0.5789 -0.0242 -0.0001 0.0163  62  VAL A CA  
430  C C   . VAL A 63  ? 0.5370 0.4867 0.5597 -0.0309 0.0008  0.0117  62  VAL A C   
431  O O   . VAL A 63  ? 0.6207 0.5719 0.6377 -0.0349 -0.0018 0.0110  62  VAL A O   
432  C CB  . VAL A 63  ? 0.5183 0.4574 0.5366 -0.0197 0.0008  0.0186  62  VAL A CB  
433  C CG1 . VAL A 63  ? 0.5400 0.4712 0.5465 -0.0237 -0.0009 0.0187  62  VAL A CG1 
434  C CG2 . VAL A 63  ? 0.4877 0.4268 0.5075 -0.0124 -0.0007 0.0230  62  VAL A CG2 
435  N N   . THR A 64  ? 0.5028 0.4511 0.5288 -0.0319 0.0045  0.0087  63  THR A N   
436  C CA  . THR A 64  ? 0.5246 0.4736 0.5485 -0.0374 0.0059  0.0042  63  THR A CA  
437  C C   . THR A 64  ? 0.5775 0.5341 0.6060 -0.0411 0.0042  0.0008  63  THR A C   
438  O O   . THR A 64  ? 0.6240 0.5818 0.6466 -0.0453 0.0036  -0.0023 63  THR A O   
439  C CB  . THR A 64  ? 0.5100 0.4566 0.5379 -0.0368 0.0098  0.0020  63  THR A CB  
440  O OG1 . THR A 64  ? 0.5279 0.4668 0.5496 -0.0343 0.0105  0.0042  63  THR A OG1 
441  C CG2 . THR A 64  ? 0.5104 0.4591 0.5381 -0.0416 0.0115  -0.0030 63  THR A CG2 
442  N N   . LYS A 65  ? 0.5408 0.5028 0.5796 -0.0396 0.0034  0.0012  64  LYS A N   
443  C CA  . LYS A 65  ? 0.5910 0.5594 0.6350 -0.0435 0.0012  -0.0026 64  LYS A CA  
444  C C   . LYS A 65  ? 0.5771 0.5487 0.6141 -0.0454 -0.0036 -0.0021 64  LYS A C   
445  O O   . LYS A 65  ? 0.5908 0.5648 0.6241 -0.0496 -0.0052 -0.0067 64  LYS A O   
446  C CB  . LYS A 65  ? 0.5549 0.5285 0.6127 -0.0421 0.0011  -0.0013 64  LYS A CB  
447  C CG  . LYS A 65  ? 0.5471 0.5265 0.6114 -0.0466 -0.0021 -0.0054 64  LYS A CG  
448  C CD  . LYS A 65  ? 0.5269 0.5139 0.5982 -0.0459 -0.0064 -0.0019 64  LYS A CD  
449  C CE  . LYS A 65  ? 0.5135 0.5061 0.5921 -0.0510 -0.0104 -0.0063 64  LYS A CE  
450  N NZ  . LYS A 65  ? 0.5578 0.5480 0.6260 -0.0552 -0.0123 -0.0129 64  LYS A NZ  
451  N N   . TYR A 66  ? 0.5894 0.5610 0.6239 -0.0419 -0.0061 0.0034  65  TYR A N   
452  C CA  . TYR A 66  ? 0.5680 0.5432 0.5966 -0.0430 -0.0112 0.0049  65  TYR A CA  
453  C C   . TYR A 66  ? 0.5396 0.5091 0.5534 -0.0447 -0.0115 0.0058  65  TYR A C   
454  O O   . TYR A 66  ? 0.5482 0.5209 0.5549 -0.0473 -0.0151 0.0054  65  TYR A O   
455  C CB  . TYR A 66  ? 0.5263 0.5049 0.5602 -0.0380 -0.0141 0.0107  65  TYR A CB  
456  C CG  . TYR A 66  ? 0.5348 0.5224 0.5839 -0.0379 -0.0151 0.0102  65  TYR A CG  
457  C CD1 . TYR A 66  ? 0.5693 0.5638 0.6226 -0.0429 -0.0187 0.0060  65  TYR A CD1 
458  C CD2 . TYR A 66  ? 0.5365 0.5258 0.5955 -0.0330 -0.0123 0.0137  65  TYR A CD2 
459  C CE1 . TYR A 66  ? 0.5669 0.5693 0.6351 -0.0438 -0.0200 0.0058  65  TYR A CE1 
460  C CE2 . TYR A 66  ? 0.6082 0.6065 0.6820 -0.0336 -0.0127 0.0141  65  TYR A CE2 
461  C CZ  . TYR A 66  ? 0.5872 0.5919 0.6661 -0.0394 -0.0168 0.0103  65  TYR A CZ  
462  O OH  . TYR A 66  ? 0.5738 0.5872 0.6684 -0.0409 -0.0177 0.0110  65  TYR A OH  
463  N N   . VAL A 67  ? 0.5743 0.5358 0.5832 -0.0435 -0.0079 0.0074  66  VAL A N   
464  C CA  . VAL A 67  ? 0.5484 0.5050 0.5446 -0.0464 -0.0076 0.0083  66  VAL A CA  
465  C C   . VAL A 67  ? 0.5985 0.5591 0.5918 -0.0517 -0.0057 0.0025  66  VAL A C   
466  O O   . VAL A 67  ? 0.6862 0.6482 0.6694 -0.0548 -0.0070 0.0026  66  VAL A O   
467  C CB  . VAL A 67  ? 0.4973 0.4445 0.4905 -0.0445 -0.0046 0.0109  66  VAL A CB  
468  C CG1 . VAL A 67  ? 0.5667 0.5107 0.5504 -0.0494 -0.0026 0.0103  66  VAL A CG1 
469  C CG2 . VAL A 67  ? 0.5252 0.4664 0.5158 -0.0395 -0.0073 0.0169  66  VAL A CG2 
470  N N   . ALA A 68  ? 0.5784 0.5409 0.5800 -0.0523 -0.0026 -0.0026 67  ALA A N   
471  C CA  . ALA A 68  ? 0.6054 0.5716 0.6051 -0.0563 -0.0007 -0.0090 67  ALA A CA  
472  C C   . ALA A 68  ? 0.6370 0.6095 0.6354 -0.0583 -0.0049 -0.0122 67  ALA A C   
473  O O   . ALA A 68  ? 0.6348 0.6100 0.6246 -0.0615 -0.0049 -0.0157 67  ALA A O   
474  C CB  . ALA A 68  ? 0.6077 0.5735 0.6175 -0.0557 0.0031  -0.0133 67  ALA A CB  
475  N N   . GLN A 69  ? 0.6052 0.5808 0.6121 -0.0566 -0.0086 -0.0110 68  GLN A N   
476  C CA  . GLN A 69  ? 0.5632 0.5451 0.5699 -0.0588 -0.0137 -0.0141 68  GLN A CA  
477  C C   . GLN A 69  ? 0.6392 0.6227 0.6325 -0.0597 -0.0174 -0.0110 68  GLN A C   
478  O O   . GLN A 69  ? 0.6966 0.6839 0.6823 -0.0628 -0.0197 -0.0153 68  GLN A O   
479  C CB  . GLN A 69  ? 0.5677 0.5536 0.5877 -0.0569 -0.0170 -0.0120 68  GLN A CB  
480  C CG  . GLN A 69  ? 0.5240 0.5163 0.5488 -0.0602 -0.0219 -0.0171 68  GLN A CG  
481  C CD  . GLN A 69  ? 0.5675 0.5650 0.6073 -0.0588 -0.0249 -0.0140 68  GLN A CD  
482  O OE1 . GLN A 69  ? 0.6666 0.6652 0.7181 -0.0604 -0.0242 -0.0172 68  GLN A OE1 
483  N NE2 . GLN A 69  ? 0.5594 0.5603 0.5991 -0.0556 -0.0281 -0.0074 68  GLN A NE2 
484  N N   . TYR A 70  ? 0.6053 0.5852 0.5948 -0.0568 -0.0181 -0.0035 69  TYR A N   
485  C CA  . TYR A 70  ? 0.6181 0.5981 0.5947 -0.0572 -0.0216 0.0010  69  TYR A CA  
486  C C   . TYR A 70  ? 0.7059 0.6796 0.6713 -0.0588 -0.0176 0.0036  69  TYR A C   
487  O O   . TYR A 70  ? 0.7154 0.6850 0.6727 -0.0577 -0.0193 0.0103  69  TYR A O   
488  C CB  . TYR A 70  ? 0.5855 0.5654 0.5656 -0.0527 -0.0260 0.0080  69  TYR A CB  
489  C CG  . TYR A 70  ? 0.5758 0.5641 0.5675 -0.0517 -0.0306 0.0064  69  TYR A CG  
490  C CD1 . TYR A 70  ? 0.6003 0.5960 0.5903 -0.0553 -0.0351 0.0017  69  TYR A CD1 
491  C CD2 . TYR A 70  ? 0.5744 0.5637 0.5790 -0.0473 -0.0305 0.0096  69  TYR A CD2 
492  C CE1 . TYR A 70  ? 0.5725 0.5762 0.5742 -0.0553 -0.0399 0.0004  69  TYR A CE1 
493  C CE2 . TYR A 70  ? 0.5749 0.5733 0.5917 -0.0470 -0.0345 0.0089  69  TYR A CE2 
494  C CZ  . TYR A 70  ? 0.5976 0.6031 0.6135 -0.0514 -0.0395 0.0043  69  TYR A CZ  
495  O OH  . TYR A 70  ? 0.7112 0.7259 0.7402 -0.0518 -0.0440 0.0037  69  TYR A OH  
496  N N   . HIS A 71  ? 0.7561 0.7292 0.7215 -0.0613 -0.0122 -0.0013 70  HIS A N   
497  C CA  . HIS A 71  ? 0.7615 0.7306 0.7178 -0.0636 -0.0082 0.0010  70  HIS A CA  
498  C C   . HIS A 71  ? 0.8786 0.8509 0.8203 -0.0666 -0.0097 0.0029  70  HIS A C   
499  O O   . HIS A 71  ? 0.9064 0.8749 0.8398 -0.0684 -0.0077 0.0080  70  HIS A O   
500  C CB  . HIS A 71  ? 0.7269 0.6970 0.6879 -0.0653 -0.0023 -0.0051 70  HIS A CB  
501  C CG  . HIS A 71  ? 0.8273 0.8043 0.7841 -0.0680 -0.0011 -0.0122 70  HIS A CG  
502  N ND1 . HIS A 71  ? 0.8424 0.8233 0.8053 -0.0676 -0.0035 -0.0187 70  HIS A ND1 
503  C CD2 . HIS A 71  ? 0.9007 0.8813 0.8477 -0.0711 0.0022  -0.0141 70  HIS A CD2 
504  C CE1 . HIS A 71  ? 0.8991 0.8846 0.8554 -0.0699 -0.0019 -0.0250 70  HIS A CE1 
505  N NE2 . HIS A 71  ? 0.9519 0.9381 0.8984 -0.0717 0.0018  -0.0223 70  HIS A NE2 
506  N N   . ASP A 72  ? 0.9997 0.9788 0.9381 -0.0675 -0.0133 -0.0011 71  ASP A N   
507  C CA  . ASP A 72  ? 0.9640 0.9471 0.8873 -0.0700 -0.0150 0.0004  71  ASP A CA  
508  C C   . ASP A 72  ? 0.9465 0.9288 0.8644 -0.0681 -0.0217 0.0078  71  ASP A C   
509  O O   . ASP A 72  ? 0.9809 0.9608 0.8868 -0.0692 -0.0221 0.0145  71  ASP A O   
510  C CB  . ASP A 72  ? 0.9858 0.9765 0.9064 -0.0719 -0.0156 -0.0089 71  ASP A CB  
511  C CG  . ASP A 72  ? 1.0362 1.0290 0.9698 -0.0703 -0.0196 -0.0144 71  ASP A CG  
512  O OD1 . ASP A 72  ? 0.9825 0.9722 0.9272 -0.0676 -0.0213 -0.0106 71  ASP A OD1 
513  O OD2 . ASP A 72  ? 1.1292 1.1267 1.0617 -0.0718 -0.0210 -0.0225 71  ASP A OD2 
514  N N   . ASN A 73  ? 0.7900 0.7746 0.7171 -0.0652 -0.0270 0.0072  72  ASN A N   
515  C CA  . ASN A 73  ? 0.7579 0.7430 0.6818 -0.0625 -0.0338 0.0140  72  ASN A CA  
516  C C   . ASN A 73  ? 0.7708 0.7466 0.6949 -0.0593 -0.0330 0.0228  72  ASN A C   
517  O O   . ASN A 73  ? 0.7686 0.7403 0.7044 -0.0562 -0.0312 0.0230  72  ASN A O   
518  C CB  . ASN A 73  ? 0.6669 0.6583 0.6037 -0.0603 -0.0390 0.0109  72  ASN A CB  
519  C CG  . ASN A 73  ? 0.7567 0.7532 0.6886 -0.0586 -0.0472 0.0155  72  ASN A CG  
520  O OD1 . ASN A 73  ? 0.7584 0.7526 0.6772 -0.0583 -0.0490 0.0219  72  ASN A OD1 
521  N ND2 . ASN A 73  ? 0.7079 0.7119 0.6509 -0.0576 -0.0524 0.0126  72  ASN A ND2 
522  N N   . PRO A 74  ? 0.7864 0.7579 0.6976 -0.0599 -0.0343 0.0302  73  PRO A N   
523  C CA  . PRO A 74  ? 0.7375 0.6978 0.6489 -0.0569 -0.0338 0.0381  73  PRO A CA  
524  C C   . PRO A 74  ? 0.7006 0.6599 0.6194 -0.0505 -0.0393 0.0423  73  PRO A C   
525  O O   . PRO A 74  ? 0.7048 0.6560 0.6301 -0.0465 -0.0380 0.0450  73  PRO A O   
526  C CB  . PRO A 74  ? 0.6648 0.6212 0.5597 -0.0600 -0.0339 0.0450  73  PRO A CB  
527  C CG  . PRO A 74  ? 0.7434 0.7099 0.6295 -0.0646 -0.0330 0.0398  73  PRO A CG  
528  C CD  . PRO A 74  ? 0.7773 0.7530 0.6726 -0.0631 -0.0362 0.0320  73  PRO A CD  
529  N N   . GLN A 75  ? 0.7367 0.7046 0.6548 -0.0491 -0.0456 0.0427  74  GLN A N   
530  C CA  . GLN A 75  ? 0.7229 0.6919 0.6489 -0.0426 -0.0511 0.0472  74  GLN A CA  
531  C C   . GLN A 75  ? 0.6762 0.6480 0.6198 -0.0395 -0.0490 0.0428  74  GLN A C   
532  O O   . GLN A 75  ? 0.6465 0.6130 0.5969 -0.0337 -0.0488 0.0468  74  GLN A O   
533  C CB  . GLN A 75  ? 0.6476 0.6272 0.5700 -0.0425 -0.0587 0.0481  74  GLN A CB  
534  C CG  . GLN A 75  ? 0.6631 0.6466 0.5957 -0.0356 -0.0646 0.0526  74  GLN A CG  
535  C CD  . GLN A 75  ? 0.5923 0.5891 0.5253 -0.0361 -0.0726 0.0517  74  GLN A CD  
536  O OE1 . GLN A 75  ? 0.6023 0.6083 0.5410 -0.0400 -0.0733 0.0439  74  GLN A OE1 
537  N NE2 . GLN A 75  ? 0.6279 0.6252 0.5548 -0.0321 -0.0791 0.0595  74  GLN A NE2 
538  N N   . GLN A 76  ? 0.6471 0.6268 0.5980 -0.0430 -0.0474 0.0348  75  GLN A N   
539  C CA  . GLN A 76  ? 0.6143 0.5967 0.5817 -0.0407 -0.0449 0.0313  75  GLN A CA  
540  C C   . GLN A 76  ? 0.6252 0.5973 0.5944 -0.0396 -0.0380 0.0312  75  GLN A C   
541  O O   . GLN A 76  ? 0.6098 0.5811 0.5902 -0.0352 -0.0362 0.0316  75  GLN A O   
542  C CB  . GLN A 76  ? 0.5640 0.5556 0.5382 -0.0453 -0.0450 0.0230  75  GLN A CB  
543  C CG  . GLN A 76  ? 0.6035 0.6065 0.5813 -0.0456 -0.0527 0.0224  75  GLN A CG  
544  C CD  . GLN A 76  ? 0.6319 0.6409 0.6256 -0.0405 -0.0555 0.0259  75  GLN A CD  
545  O OE1 . GLN A 76  ? 0.6659 0.6711 0.6686 -0.0369 -0.0509 0.0274  75  GLN A OE1 
546  N NE2 . GLN A 76  ? 0.5516 0.5709 0.5487 -0.0401 -0.0631 0.0272  75  GLN A NE2 
547  N N   . LEU A 77  ? 0.6609 0.6258 0.6192 -0.0434 -0.0344 0.0310  76  LEU A N   
548  C CA  . LEU A 77  ? 0.6078 0.5628 0.5672 -0.0427 -0.0288 0.0312  76  LEU A CA  
549  C C   . LEU A 77  ? 0.6407 0.5862 0.5991 -0.0367 -0.0302 0.0381  76  LEU A C   
550  O O   . LEU A 77  ? 0.6009 0.5407 0.5655 -0.0333 -0.0272 0.0376  76  LEU A O   
551  C CB  . LEU A 77  ? 0.6650 0.6160 0.6137 -0.0485 -0.0250 0.0301  76  LEU A CB  
552  C CG  . LEU A 77  ? 0.6747 0.6180 0.6258 -0.0494 -0.0194 0.0286  76  LEU A CG  
553  C CD1 . LEU A 77  ? 0.7185 0.6670 0.6818 -0.0491 -0.0161 0.0218  76  LEU A CD1 
554  C CD2 . LEU A 77  ? 0.6815 0.6223 0.6223 -0.0553 -0.0162 0.0290  76  LEU A CD2 
555  N N   . ARG A 78  ? 0.7399 0.6830 0.6899 -0.0350 -0.0350 0.0444  77  ARG A N   
556  C CA  . ARG A 78  ? 0.7264 0.6599 0.6758 -0.0283 -0.0371 0.0506  77  ARG A CA  
557  C C   . ARG A 78  ? 0.6968 0.6361 0.6602 -0.0213 -0.0378 0.0498  77  ARG A C   
558  O O   . ARG A 78  ? 0.7008 0.6322 0.6674 -0.0156 -0.0361 0.0514  77  ARG A O   
559  C CB  . ARG A 78  ? 0.7225 0.6535 0.6613 -0.0273 -0.0427 0.0579  77  ARG A CB  
560  C CG  . ARG A 78  ? 0.7261 0.6530 0.6506 -0.0343 -0.0419 0.0600  77  ARG A CG  
561  C CD  . ARG A 78  ? 0.7980 0.7240 0.7121 -0.0330 -0.0480 0.0677  77  ARG A CD  
562  N NE  . ARG A 78  ? 0.7437 0.6800 0.6498 -0.0386 -0.0495 0.0662  77  ARG A NE  
563  C CZ  . ARG A 78  ? 0.8646 0.8065 0.7641 -0.0373 -0.0558 0.0706  77  ARG A CZ  
564  N NH1 . ARG A 78  ? 0.9333 0.8717 0.8341 -0.0305 -0.0612 0.0773  77  ARG A NH1 
565  N NH2 . ARG A 78  ? 0.9240 0.8751 0.8150 -0.0425 -0.0567 0.0681  77  ARG A NH2 
566  N N   . ARG A 79  ? 0.6181 0.5714 0.5897 -0.0219 -0.0404 0.0473  78  ARG A N   
567  C CA  . ARG A 79  ? 0.6230 0.5841 0.6091 -0.0159 -0.0411 0.0473  78  ARG A CA  
568  C C   . ARG A 79  ? 0.6491 0.6101 0.6448 -0.0158 -0.0349 0.0425  78  ARG A C   
569  O O   . ARG A 79  ? 0.6229 0.5856 0.6281 -0.0095 -0.0334 0.0438  78  ARG A O   
570  C CB  . ARG A 79  ? 0.5781 0.5545 0.5709 -0.0176 -0.0463 0.0463  78  ARG A CB  
571  C CG  . ARG A 79  ? 0.5669 0.5447 0.5506 -0.0165 -0.0532 0.0517  78  ARG A CG  
572  C CD  . ARG A 79  ? 0.6157 0.6084 0.6037 -0.0200 -0.0589 0.0493  78  ARG A CD  
573  N NE  . ARG A 79  ? 0.5803 0.5748 0.5585 -0.0189 -0.0659 0.0547  78  ARG A NE  
574  C CZ  . ARG A 79  ? 0.5826 0.5889 0.5608 -0.0218 -0.0723 0.0534  78  ARG A CZ  
575  N NH1 . ARG A 79  ? 0.5881 0.6051 0.5761 -0.0262 -0.0728 0.0465  78  ARG A NH1 
576  N NH2 . ARG A 79  ? 0.5953 0.6023 0.5630 -0.0202 -0.0787 0.0591  78  ARG A NH2 
577  N N   . VAL A 80  ? 0.6382 0.5977 0.6313 -0.0223 -0.0311 0.0372  79  VAL A N   
578  C CA  . VAL A 80  ? 0.6003 0.5585 0.6012 -0.0221 -0.0254 0.0332  79  VAL A CA  
579  C C   . VAL A 80  ? 0.6409 0.5861 0.6370 -0.0178 -0.0224 0.0355  79  VAL A C   
580  O O   . VAL A 80  ? 0.6613 0.6059 0.6646 -0.0123 -0.0198 0.0357  79  VAL A O   
581  C CB  . VAL A 80  ? 0.5414 0.5014 0.5408 -0.0297 -0.0225 0.0271  79  VAL A CB  
582  C CG1 . VAL A 80  ? 0.5878 0.5443 0.5929 -0.0292 -0.0167 0.0239  79  VAL A CG1 
583  C CG2 . VAL A 80  ? 0.5271 0.4993 0.5333 -0.0332 -0.0254 0.0236  79  VAL A CG2 
584  N N   . VAL A 81  ? 0.6296 0.5643 0.6132 -0.0203 -0.0228 0.0374  80  VAL A N   
585  C CA  . VAL A 81  ? 0.6112 0.5320 0.5896 -0.0170 -0.0209 0.0391  80  VAL A CA  
586  C C   . VAL A 81  ? 0.6094 0.5257 0.5882 -0.0082 -0.0238 0.0440  80  VAL A C   
587  O O   . VAL A 81  ? 0.5982 0.5069 0.5781 -0.0025 -0.0217 0.0439  80  VAL A O   
588  C CB  . VAL A 81  ? 0.6204 0.5315 0.5864 -0.0229 -0.0209 0.0403  80  VAL A CB  
589  C CG1 . VAL A 81  ? 0.6623 0.5590 0.6242 -0.0210 -0.0190 0.0408  80  VAL A CG1 
590  C CG2 . VAL A 81  ? 0.6408 0.5590 0.6068 -0.0308 -0.0181 0.0356  80  VAL A CG2 
591  N N   . GLY A 82  ? 0.6391 0.5604 0.6171 -0.0064 -0.0287 0.0481  81  GLY A N   
592  C CA  . GLY A 82  ? 0.6080 0.5255 0.5867 0.0026  -0.0316 0.0530  81  GLY A CA  
593  C C   . GLY A 82  ? 0.6337 0.5598 0.6257 0.0098  -0.0294 0.0518  81  GLY A C   
594  O O   . GLY A 82  ? 0.6838 0.6028 0.6760 0.0179  -0.0284 0.0534  81  GLY A O   
595  N N   . THR A 83  ? 0.6377 0.5792 0.6408 0.0068  -0.0285 0.0490  82  THR A N   
596  C CA  . THR A 83  ? 0.6282 0.5794 0.6450 0.0127  -0.0258 0.0486  82  THR A CA  
597  C C   . THR A 83  ? 0.6387 0.5835 0.6561 0.0138  -0.0195 0.0451  82  THR A C   
598  O O   . THR A 83  ? 0.6078 0.5532 0.6304 0.0217  -0.0168 0.0461  82  THR A O   
599  C CB  . THR A 83  ? 0.5965 0.5652 0.6255 0.0081  -0.0270 0.0469  82  THR A CB  
600  O OG1 . THR A 83  ? 0.5483 0.5223 0.5745 0.0057  -0.0335 0.0493  82  THR A OG1 
601  C CG2 . THR A 83  ? 0.5731 0.5536 0.6175 0.0144  -0.0250 0.0484  82  THR A CG2 
602  N N   . SER A 84  ? 0.6159 0.5553 0.6278 0.0065  -0.0172 0.0411  83  SER A N   
603  C CA  . SER A 84  ? 0.6022 0.5353 0.6137 0.0073  -0.0121 0.0379  83  SER A CA  
604  C C   . SER A 84  ? 0.5583 0.4760 0.5603 0.0135  -0.0119 0.0394  83  SER A C   
605  O O   . SER A 84  ? 0.5256 0.4402 0.5290 0.0190  -0.0084 0.0380  83  SER A O   
606  C CB  . SER A 84  ? 0.5914 0.5225 0.5994 -0.0017 -0.0103 0.0337  83  SER A CB  
607  O OG  . SER A 84  ? 0.5304 0.4737 0.5455 -0.0073 -0.0111 0.0317  83  SER A OG  
608  N N   . SER A 85  ? 0.5828 0.4902 0.5745 0.0126  -0.0159 0.0420  84  SER A N   
609  C CA  . SER A 85  ? 0.5870 0.4778 0.5694 0.0182  -0.0166 0.0433  84  SER A CA  
610  C C   . SER A 85  ? 0.6298 0.5219 0.6166 0.0297  -0.0167 0.0456  84  SER A C   
611  O O   . SER A 85  ? 0.6644 0.5463 0.6473 0.0362  -0.0148 0.0443  84  SER A O   
612  C CB  . SER A 85  ? 0.6273 0.5069 0.5984 0.0141  -0.0210 0.0466  84  SER A CB  
613  O OG  . SER A 85  ? 0.7174 0.5807 0.6807 0.0205  -0.0229 0.0487  84  SER A OG  
614  N N   . ALA A 86  ? 0.6276 0.5327 0.6226 0.0325  -0.0189 0.0489  85  ALA A N   
615  C CA  . ALA A 86  ? 0.6036 0.5124 0.6045 0.0439  -0.0188 0.0516  85  ALA A CA  
616  C C   . ALA A 86  ? 0.6111 0.5291 0.6215 0.0483  -0.0129 0.0491  85  ALA A C   
617  O O   . ALA A 86  ? 0.6249 0.5397 0.6354 0.0584  -0.0106 0.0494  85  ALA A O   
618  C CB  . ALA A 86  ? 0.5608 0.4830 0.5692 0.0452  -0.0233 0.0561  85  ALA A CB  
619  N N   . MET A 87  ? 0.6089 0.5383 0.6272 0.0412  -0.0101 0.0467  86  MET A N   
620  C CA  . MET A 87  ? 0.5808 0.5188 0.6078 0.0446  -0.0043 0.0451  86  MET A CA  
621  C C   . MET A 87  ? 0.5624 0.4864 0.5797 0.0470  -0.0007 0.0416  86  MET A C   
622  O O   . MET A 87  ? 0.5506 0.4755 0.5694 0.0552  0.0033  0.0413  86  MET A O   
623  C CB  . MET A 87  ? 0.5740 0.5257 0.6115 0.0359  -0.0028 0.0436  86  MET A CB  
624  C CG  . MET A 87  ? 0.5739 0.5433 0.6252 0.0356  -0.0052 0.0469  86  MET A CG  
625  S SD  . MET A 87  ? 0.5288 0.5079 0.5867 0.0228  -0.0073 0.0442  86  MET A SD  
626  C CE  . MET A 87  ? 0.5274 0.5166 0.5984 0.0223  -0.0007 0.0432  86  MET A CE  
627  N N   . VAL A 88  ? 0.5853 0.4969 0.5923 0.0398  -0.0022 0.0388  87  VAL A N   
628  C CA  . VAL A 88  ? 0.5964 0.4943 0.5939 0.0413  -0.0001 0.0352  87  VAL A CA  
629  C C   . VAL A 88  ? 0.6346 0.5189 0.6234 0.0511  -0.0015 0.0359  87  VAL A C   
630  O O   . VAL A 88  ? 0.6657 0.5441 0.6503 0.0578  0.0014  0.0335  87  VAL A O   
631  C CB  . VAL A 88  ? 0.6088 0.4977 0.5987 0.0311  -0.0019 0.0327  87  VAL A CB  
632  C CG1 . VAL A 88  ? 0.6578 0.5305 0.6367 0.0326  -0.0015 0.0294  87  VAL A CG1 
633  C CG2 . VAL A 88  ? 0.5803 0.4813 0.5783 0.0232  0.0006  0.0308  87  VAL A CG2 
634  N N   . LEU A 89  ? 0.6493 0.5280 0.6345 0.0525  -0.0063 0.0392  88  LEU A N   
635  C CA  . LEU A 89  ? 0.6599 0.5239 0.6367 0.0622  -0.0082 0.0399  88  LEU A CA  
636  C C   . LEU A 89  ? 0.6981 0.5716 0.6822 0.0744  -0.0047 0.0409  88  LEU A C   
637  O O   . LEU A 89  ? 0.7672 0.6308 0.7448 0.0832  -0.0028 0.0384  88  LEU A O   
638  C CB  . LEU A 89  ? 0.6074 0.4641 0.5796 0.0608  -0.0142 0.0442  88  LEU A CB  
639  C CG  . LEU A 89  ? 0.6719 0.5080 0.6329 0.0684  -0.0175 0.0449  88  LEU A CG  
640  C CD1 . LEU A 89  ? 0.6999 0.5166 0.6486 0.0612  -0.0194 0.0420  88  LEU A CD1 
641  C CD2 . LEU A 89  ? 0.6654 0.5011 0.6269 0.0713  -0.0226 0.0509  88  LEU A CD2 
642  N N   . GLY A 90  ? 0.6700 0.5630 0.6676 0.0752  -0.0039 0.0444  89  GLY A N   
643  C CA  . GLY A 90  ? 0.6199 0.5243 0.6262 0.0867  -0.0004 0.0462  89  GLY A CA  
644  C C   . GLY A 90  ? 0.6215 0.5322 0.6308 0.0897  0.0065  0.0434  89  GLY A C   
645  O O   . GLY A 90  ? 0.6928 0.6031 0.7010 0.1010  0.0101  0.0430  89  GLY A O   
646  N N   . PHE A 91  ? 0.6336 0.5500 0.6461 0.0801  0.0087  0.0416  90  PHE A N   
647  C CA  . PHE A 91  ? 0.6381 0.5612 0.6537 0.0824  0.0152  0.0399  90  PHE A CA  
648  C C   . PHE A 91  ? 0.6924 0.5976 0.6927 0.0866  0.0164  0.0351  90  PHE A C   
649  O O   . PHE A 91  ? 0.7042 0.6114 0.7030 0.0953  0.0213  0.0341  90  PHE A O   
650  C CB  . PHE A 91  ? 0.6225 0.5559 0.6461 0.0711  0.0166  0.0396  90  PHE A CB  
651  C CG  . PHE A 91  ? 0.6360 0.5809 0.6668 0.0734  0.0233  0.0400  90  PHE A CG  
652  C CD1 . PHE A 91  ? 0.7056 0.6420 0.7275 0.0736  0.0263  0.0365  90  PHE A CD1 
653  C CD2 . PHE A 91  ? 0.6473 0.6118 0.6941 0.0752  0.0264  0.0444  90  PHE A CD2 
654  C CE1 . PHE A 91  ? 0.6803 0.6270 0.7079 0.0758  0.0325  0.0377  90  PHE A CE1 
655  C CE2 . PHE A 91  ? 0.6910 0.6660 0.7445 0.0769  0.0329  0.0458  90  PHE A CE2 
656  C CZ  . PHE A 91  ? 0.6951 0.6610 0.7385 0.0774  0.0360  0.0426  90  PHE A CZ  
657  N N   . SER A 92  ? 0.6971 0.5852 0.6859 0.0804  0.0119  0.0321  91  SER A N   
658  C CA  . SER A 92  ? 0.7339 0.6045 0.7084 0.0832  0.0119  0.0272  91  SER A CA  
659  C C   . SER A 92  ? 0.7879 0.6464 0.7540 0.0957  0.0111  0.0263  91  SER A C   
660  O O   . SER A 92  ? 0.8348 0.6846 0.7916 0.1025  0.0133  0.0222  91  SER A O   
661  C CB  . SER A 92  ? 0.7638 0.6207 0.7302 0.0723  0.0071  0.0249  91  SER A CB  
662  O OG  . SER A 92  ? 0.8537 0.7009 0.8162 0.0713  0.0017  0.0271  91  SER A OG  
663  N N   . THR A 93  ? 0.7110 0.5685 0.6795 0.0993  0.0077  0.0298  92  THR A N   
664  C CA  . THR A 93  ? 0.7458 0.5928 0.7076 0.1126  0.0071  0.0290  92  THR A CA  
665  C C   . THR A 93  ? 0.7344 0.5971 0.7037 0.1242  0.0139  0.0299  92  THR A C   
666  O O   . THR A 93  ? 0.7605 0.6144 0.7213 0.1357  0.0160  0.0266  92  THR A O   
667  C CB  . THR A 93  ? 0.7421 0.5849 0.7054 0.1138  0.0016  0.0334  92  THR A CB  
668  O OG1 . THR A 93  ? 0.7493 0.6127 0.7273 0.1084  0.0015  0.0386  92  THR A OG1 
669  C CG2 . THR A 93  ? 0.7109 0.5324 0.6624 0.1054  -0.0048 0.0322  92  THR A CG2 
670  N N   . LEU A 94  ? 0.7217 0.6077 0.7069 0.1212  0.0174  0.0341  93  LEU A N   
671  C CA  . LEU A 94  ? 0.7054 0.6086 0.6991 0.1307  0.0247  0.0358  93  LEU A CA  
672  C C   . LEU A 94  ? 0.6953 0.5959 0.6815 0.1316  0.0299  0.0317  93  LEU A C   
673  O O   . LEU A 94  ? 0.6922 0.5960 0.6757 0.1431  0.0353  0.0306  93  LEU A O   
674  C CB  . LEU A 94  ? 0.6098 0.5378 0.6231 0.1253  0.0264  0.0416  93  LEU A CB  
675  C CG  . LEU A 94  ? 0.6625 0.6114 0.6889 0.1354  0.0328  0.0456  93  LEU A CG  
676  C CD1 . LEU A 94  ? 0.5998 0.5643 0.6419 0.1351  0.0297  0.0514  93  LEU A CD1 
677  C CD2 . LEU A 94  ? 0.6165 0.5801 0.6504 0.1316  0.0396  0.0467  93  LEU A CD2 
678  N N   . MET A 95  ? 0.6794 0.5750 0.6619 0.1200  0.0284  0.0294  94  MET A N   
679  C CA  . MET A 95  ? 0.6856 0.5772 0.6595 0.1206  0.0322  0.0254  94  MET A CA  
680  C C   . MET A 95  ? 0.7867 0.6564 0.7421 0.1285  0.0301  0.0193  94  MET A C   
681  O O   . MET A 95  ? 0.7632 0.6320 0.7111 0.1366  0.0346  0.0164  94  MET A O   
682  C CB  . MET A 95  ? 0.7284 0.6192 0.7032 0.1066  0.0302  0.0244  94  MET A CB  
683  C CG  . MET A 95  ? 0.7868 0.6983 0.7765 0.1011  0.0349  0.0286  94  MET A CG  
684  S SD  . MET A 95  ? 1.1058 1.0352 1.1026 0.1127  0.0440  0.0322  94  MET A SD  
685  C CE  . MET A 95  ? 0.6904 0.6388 0.7066 0.1138  0.0440  0.0388  94  MET A CE  
686  N N   . ALA A 96  ? 0.7959 0.6474 0.7434 0.1263  0.0232  0.0174  95  ALA A N   
687  C CA  . ALA A 96  ? 0.7468 0.5754 0.6771 0.1331  0.0203  0.0114  95  ALA A CA  
688  C C   . ALA A 96  ? 0.7946 0.6239 0.7221 0.1498  0.0241  0.0106  95  ALA A C   
689  O O   . ALA A 96  ? 0.8376 0.6550 0.7515 0.1582  0.0253  0.0049  95  ALA A O   
690  C CB  . ALA A 96  ? 0.7003 0.5100 0.6246 0.1268  0.0122  0.0109  95  ALA A CB  
691  N N   . LEU A 97  ? 0.7811 0.6249 0.7214 0.1550  0.0259  0.0162  96  LEU A N   
692  C CA  . LEU A 97  ? 0.7793 0.6270 0.7193 0.1715  0.0303  0.0161  96  LEU A CA  
693  C C   . LEU A 97  ? 0.8087 0.6722 0.7503 0.1777  0.0391  0.0157  96  LEU A C   
694  O O   . LEU A 97  ? 0.7762 0.6348 0.7081 0.1911  0.0428  0.0118  96  LEU A O   
695  C CB  . LEU A 97  ? 0.7454 0.6077 0.7009 0.1748  0.0298  0.0229  96  LEU A CB  
696  C CG  . LEU A 97  ? 0.8351 0.6894 0.7867 0.1905  0.0291  0.0222  96  LEU A CG  
697  C CD1 . LEU A 97  ? 0.8384 0.6656 0.7782 0.1883  0.0202  0.0198  96  LEU A CD1 
698  C CD2 . LEU A 97  ? 0.8650 0.7431 0.8356 0.1959  0.0317  0.0295  96  LEU A CD2 
699  N N   . VAL A 98  ? 0.7673 0.6494 0.7207 0.1684  0.0426  0.0198  97  VAL A N   
700  C CA  . VAL A 98  ? 0.7621 0.6594 0.7174 0.1730  0.0511  0.0206  97  VAL A CA  
701  C C   . VAL A 98  ? 0.8202 0.7009 0.7560 0.1748  0.0511  0.0134  97  VAL A C   
702  O O   . VAL A 98  ? 0.8319 0.7159 0.7603 0.1858  0.0572  0.0114  97  VAL A O   
703  C CB  . VAL A 98  ? 0.6768 0.5950 0.6491 0.1613  0.0537  0.0269  97  VAL A CB  
704  C CG1 . VAL A 98  ? 0.6370 0.5643 0.6071 0.1619  0.0607  0.0271  97  VAL A CG1 
705  C CG2 . VAL A 98  ? 0.6547 0.5944 0.6468 0.1636  0.0561  0.0340  97  VAL A CG2 
706  N N   . PHE A 99  ? 0.8038 0.6672 0.7308 0.1642  0.0443  0.0094  98  PHE A N   
707  C CA  . PHE A 99  ? 0.8191 0.6676 0.7286 0.1645  0.0432  0.0026  98  PHE A CA  
708  C C   . PHE A 99  ? 0.8962 0.7243 0.7883 0.1769  0.0410  -0.0045 98  PHE A C   
709  O O   . PHE A 99  ? 0.9178 0.7400 0.7959 0.1840  0.0435  -0.0098 98  PHE A O   
710  C CB  . PHE A 99  ? 0.8078 0.6454 0.7149 0.1493  0.0364  0.0007  98  PHE A CB  
711  C CG  . PHE A 99  ? 0.8198 0.6735 0.7373 0.1390  0.0393  0.0047  98  PHE A CG  
712  C CD1 . PHE A 99  ? 0.8085 0.6831 0.7446 0.1352  0.0430  0.0119  98  PHE A CD1 
713  C CD2 . PHE A 99  ? 0.8364 0.6842 0.7453 0.1333  0.0379  0.0011  98  PHE A CD2 
714  C CE1 . PHE A 99  ? 0.7893 0.6770 0.7348 0.1260  0.0454  0.0153  98  PHE A CE1 
715  C CE2 . PHE A 99  ? 0.8507 0.7123 0.7691 0.1246  0.0405  0.0049  98  PHE A CE2 
716  C CZ  . PHE A 99  ? 0.7799 0.6607 0.7165 0.1209  0.0443  0.0119  98  PHE A CZ  
717  N N   . VAL A 100 ? 1.0150 0.8315 0.9071 0.1798  0.0362  -0.0047 99  VAL A N   
718  C CA  . VAL A 100 ? 1.0313 0.8256 0.9067 0.1913  0.0333  -0.0118 99  VAL A CA  
719  C C   . VAL A 100 ? 0.9872 0.7916 0.8622 0.2090  0.0410  -0.0119 99  VAL A C   
720  O O   . VAL A 100 ? 1.0797 0.8693 0.9382 0.2205  0.0413  -0.0192 99  VAL A O   
721  C CB  . VAL A 100 ? 0.9591 0.7353 0.8341 0.1879  0.0250  -0.0116 99  VAL A CB  
722  C CG1 . VAL A 100 ? 0.9427 0.7332 0.8329 0.1936  0.0271  -0.0046 99  VAL A CG1 
723  C CG2 . VAL A 100 ? 0.9209 0.6680 0.7763 0.1958  0.0199  -0.0202 99  VAL A CG2 
724  N N   . LEU A 101 ? 0.8997 0.7296 0.7926 0.2117  0.0472  -0.0041 100 LEU A N   
725  C CA  . LEU A 101 ? 0.8860 0.7276 0.7802 0.2288  0.0550  -0.0036 100 LEU A CA  
726  C C   . LEU A 101 ? 0.9290 0.7849 0.8193 0.2331  0.0637  -0.0040 100 LEU A C   
727  O O   . LEU A 101 ? 1.0165 0.8691 0.8944 0.2476  0.0684  -0.0088 100 LEU A O   
728  C CB  . LEU A 101 ? 0.8662 0.7298 0.7823 0.2304  0.0576  0.0052  100 LEU A CB  
729  C CG  . LEU A 101 ? 0.8045 0.6558 0.7237 0.2312  0.0501  0.0063  100 LEU A CG  
730  C CD1 . LEU A 101 ? 0.7250 0.6016 0.6663 0.2338  0.0532  0.0150  100 LEU A CD1 
731  C CD2 . LEU A 101 ? 0.7573 0.5849 0.6594 0.2457  0.0478  -0.0012 100 LEU A CD2 
732  N N   . ALA A 102 ? 0.9528 0.8242 0.8529 0.2211  0.0660  0.0011  101 ALA A N   
733  C CA  . ALA A 102 ? 1.0088 0.8949 0.9066 0.2235  0.0742  0.0024  101 ALA A CA  
734  C C   . ALA A 102 ? 0.9801 0.8502 0.8608 0.2169  0.0703  -0.0038 101 ALA A C   
735  O O   . ALA A 102 ? 0.9858 0.8676 0.8698 0.2098  0.0736  -0.0005 101 ALA A O   
736  C CB  . ALA A 102 ? 1.0177 0.9315 0.9380 0.2152  0.0794  0.0125  101 ALA A CB  
737  N N   . ALA A 103 ? 0.8757 0.7190 0.7384 0.2189  0.0630  -0.0128 102 ALA A N   
738  C CA  . ALA A 103 ? 0.8596 0.6877 0.7068 0.2119  0.0582  -0.0189 102 ALA A CA  
739  C C   . ALA A 103 ? 0.8639 0.6996 0.6994 0.2198  0.0651  -0.0208 102 ALA A C   
740  O O   . ALA A 103 ? 0.8402 0.6741 0.6694 0.2120  0.0633  -0.0221 102 ALA A O   
741  C CB  . ALA A 103 ? 0.9164 0.7141 0.7470 0.2132  0.0488  -0.0282 102 ALA A CB  
742  N N   . ALA A 104 ? 0.8509 0.6961 0.6835 0.2355  0.0732  -0.0206 103 ALA A N   
743  C CA  . ALA A 104 ? 0.8142 0.6672 0.6340 0.2448  0.0806  -0.0222 103 ALA A CA  
744  C C   . ALA A 104 ? 0.8249 0.7050 0.6597 0.2386  0.0884  -0.0120 103 ALA A C   
745  O O   . ALA A 104 ? 0.8358 0.7172 0.6615 0.2353  0.0895  -0.0124 103 ALA A O   
746  C CB  . ALA A 104 ? 0.8350 0.6894 0.6464 0.2644  0.0871  -0.0256 103 ALA A CB  
747  N N   . PRO A 105 ? 0.7837 0.6853 0.6414 0.2367  0.0936  -0.0025 104 PRO A N   
748  C CA  . PRO A 105 ? 0.7346 0.6601 0.6072 0.2292  0.1002  0.0073  104 PRO A CA  
749  C C   . PRO A 105 ? 0.8004 0.7207 0.6758 0.2124  0.0939  0.0083  104 PRO A C   
750  O O   . PRO A 105 ? 0.7478 0.6773 0.6220 0.2090  0.0978  0.0120  104 PRO A O   
751  C CB  . PRO A 105 ? 0.7558 0.7011 0.6528 0.2290  0.1041  0.0158  104 PRO A CB  
752  C CG  . PRO A 105 ? 0.7209 0.6586 0.6118 0.2434  0.1043  0.0108  104 PRO A CG  
753  C CD  . PRO A 105 ? 0.7652 0.6721 0.6357 0.2429  0.0945  0.0000  104 PRO A CD  
754  N N   . ILE A 106 ? 0.8605 0.7666 0.7396 0.2022  0.0845  0.0055  105 ILE A N   
755  C CA  . ILE A 106 ? 0.8374 0.7394 0.7197 0.1868  0.0789  0.0062  105 ILE A CA  
756  C C   . ILE A 106 ? 0.7626 0.6507 0.6240 0.1874  0.0759  -0.0005 105 ILE A C   
757  O O   . ILE A 106 ? 0.7455 0.6395 0.6082 0.1800  0.0765  0.0025  105 ILE A O   
758  C CB  . ILE A 106 ? 0.7655 0.6558 0.6552 0.1764  0.0700  0.0046  105 ILE A CB  
759  C CG1 . ILE A 106 ? 0.7748 0.6753 0.6804 0.1794  0.0719  0.0094  105 ILE A CG1 
760  C CG2 . ILE A 106 ? 0.8192 0.7126 0.7184 0.1606  0.0665  0.0077  105 ILE A CG2 
761  C CD1 . ILE A 106 ? 0.8026 0.6899 0.7122 0.1714  0.0631  0.0075  105 ILE A CD1 
762  N N   . SER A 107 ? 0.7278 0.5969 0.5697 0.1963  0.0722  -0.0097 106 SER A N   
763  C CA  . SER A 107 ? 0.8147 0.6709 0.6357 0.1976  0.0689  -0.0167 106 SER A CA  
764  C C   . SER A 107 ? 0.8465 0.7185 0.6616 0.2053  0.0780  -0.0129 106 SER A C   
765  O O   . SER A 107 ? 0.8006 0.6708 0.6063 0.2015  0.0763  -0.0140 106 SER A O   
766  C CB  . SER A 107 ? 0.8367 0.6691 0.6381 0.2065  0.0633  -0.0276 106 SER A CB  
767  O OG  . SER A 107 ? 0.8579 0.6780 0.6382 0.2084  0.0596  -0.0350 106 SER A OG  
768  N N   . GLN A 108 ? 0.8391 0.7274 0.6600 0.2161  0.0877  -0.0080 107 GLN A N   
769  C CA  . GLN A 108 ? 0.7678 0.6732 0.5844 0.2234  0.0975  -0.0029 107 GLN A CA  
770  C C   . GLN A 108 ? 0.7790 0.7007 0.6109 0.2114  0.1000  0.0070  107 GLN A C   
771  O O   . GLN A 108 ? 0.8377 0.7659 0.6611 0.2130  0.1040  0.0096  107 GLN A O   
772  C CB  . GLN A 108 ? 0.7871 0.7084 0.6097 0.2368  0.1076  0.0011  107 GLN A CB  
773  C CG  . GLN A 108 ? 0.8959 0.8353 0.7126 0.2459  0.1188  0.0065  107 GLN A CG  
774  C CD  . GLN A 108 ? 0.8719 0.7974 0.6590 0.2572  0.1182  -0.0030 107 GLN A CD  
775  O OE1 . GLN A 108 ? 0.8306 0.7454 0.6043 0.2700  0.1182  -0.0111 107 GLN A OE1 
776  N NE2 . GLN A 108 ? 0.8058 0.7309 0.5821 0.2529  0.1173  -0.0023 107 GLN A NE2 
777  N N   . GLY A 109 ? 0.7867 0.7143 0.6402 0.1998  0.0977  0.0124  108 GLY A N   
778  C CA  . GLY A 109 ? 0.7272 0.6691 0.5963 0.1886  0.0999  0.0214  108 GLY A CA  
779  C C   . GLY A 109 ? 0.7043 0.6335 0.5692 0.1767  0.0912  0.0180  108 GLY A C   
780  O O   . GLY A 109 ? 0.7496 0.6867 0.6184 0.1707  0.0930  0.0235  108 GLY A O   
781  N N   . LEU A 110 ? 0.7037 0.6132 0.5611 0.1733  0.0818  0.0095  109 LEU A N   
782  C CA  . LEU A 110 ? 0.7172 0.6155 0.5724 0.1616  0.0733  0.0062  109 LEU A CA  
783  C C   . LEU A 110 ? 0.7670 0.6544 0.6001 0.1656  0.0701  -0.0001 109 LEU A C   
784  O O   . LEU A 110 ? 0.7181 0.6051 0.5508 0.1578  0.0666  0.0009  109 LEU A O   
785  C CB  . LEU A 110 ? 0.6845 0.5677 0.5428 0.1550  0.0647  0.0007  109 LEU A CB  
786  C CG  . LEU A 110 ? 0.6904 0.5827 0.5707 0.1475  0.0653  0.0065  109 LEU A CG  
787  C CD1 . LEU A 110 ? 0.7023 0.5784 0.5825 0.1406  0.0563  0.0010  109 LEU A CD1 
788  C CD2 . LEU A 110 ? 0.6355 0.5423 0.5317 0.1374  0.0676  0.0141  109 LEU A CD2 
789  N N   . PHE A 111 ? 0.7524 0.6310 0.5668 0.1780  0.0709  -0.0067 110 PHE A N   
790  C CA  . PHE A 111 ? 0.7906 0.6571 0.5820 0.1824  0.0667  -0.0141 110 PHE A CA  
791  C C   . PHE A 111 ? 0.8884 0.7632 0.6649 0.1964  0.0751  -0.0132 110 PHE A C   
792  O O   . PHE A 111 ? 0.8242 0.6932 0.5824 0.1993  0.0726  -0.0174 110 PHE A O   
793  C CB  . PHE A 111 ? 0.7498 0.5922 0.5273 0.1838  0.0574  -0.0257 110 PHE A CB  
794  C CG  . PHE A 111 ? 0.7759 0.6082 0.5642 0.1698  0.0484  -0.0273 110 PHE A CG  
795  C CD1 . PHE A 111 ? 0.7945 0.6209 0.5802 0.1598  0.0410  -0.0295 110 PHE A CD1 
796  C CD2 . PHE A 111 ? 0.7737 0.6033 0.5747 0.1670  0.0474  -0.0262 110 PHE A CD2 
797  C CE1 . PHE A 111 ? 0.7379 0.5565 0.5338 0.1471  0.0335  -0.0306 110 PHE A CE1 
798  C CE2 . PHE A 111 ? 0.6770 0.4980 0.4870 0.1544  0.0397  -0.0272 110 PHE A CE2 
799  C CZ  . PHE A 111 ? 0.6885 0.5043 0.4961 0.1444  0.0330  -0.0294 110 PHE A CZ  
800  N N   . GLY A 112 ? 0.8776 0.7666 0.6613 0.2051  0.0849  -0.0078 111 GLY A N   
801  C CA  . GLY A 112 ? 0.8445 0.7427 0.6144 0.2192  0.0938  -0.0067 111 GLY A CA  
802  C C   . GLY A 112 ? 0.9384 0.8234 0.6893 0.2334  0.0936  -0.0169 111 GLY A C   
803  O O   . GLY A 112 ? 1.0288 0.9233 0.7697 0.2468  0.1025  -0.0158 111 GLY A O   
804  N N   . ASN A 113 ? 1.0400 0.9033 0.7853 0.2312  0.0839  -0.0265 112 ASN A N   
805  C CA  . ASN A 113 ? 1.0649 0.9119 0.7922 0.2442  0.0822  -0.0370 112 ASN A CA  
806  C C   . ASN A 113 ? 1.0430 0.8818 0.7835 0.2422  0.0788  -0.0383 112 ASN A C   
807  O O   . ASN A 113 ? 1.0078 0.8552 0.7706 0.2313  0.0782  -0.0310 112 ASN A O   
808  C CB  . ASN A 113 ? 1.0764 0.9001 0.7792 0.2440  0.0720  -0.0489 112 ASN A CB  
809  C CG  . ASN A 113 ? 1.3481 1.1787 1.0424 0.2400  0.0718  -0.0464 112 ASN A CG  
810  O OD1 . ASN A 113 ? 1.5046 1.3531 1.1963 0.2468  0.0814  -0.0400 112 ASN A OD1 
811  N ND2 . ASN A 113 ? 1.3953 1.2125 1.0858 0.2286  0.0608  -0.0510 112 ASN A ND2 
812  N N   . THR A 114 ? 0.9672 0.7886 0.6932 0.2532  0.0762  -0.0479 113 THR A N   
813  C CA  . THR A 114 ? 0.9464 0.7564 0.6815 0.2527  0.0719  -0.0500 113 THR A CA  
814  C C   . THR A 114 ? 1.0170 0.7971 0.7393 0.2471  0.0588  -0.0607 113 THR A C   
815  O O   . THR A 114 ? 0.9938 0.7595 0.7182 0.2488  0.0544  -0.0642 113 THR A O   
816  C CB  . THR A 114 ? 1.0225 0.8367 0.7544 0.2705  0.0797  -0.0514 113 THR A CB  
817  O OG1 . THR A 114 ? 1.0928 0.8991 0.8369 0.2696  0.0760  -0.0513 113 THR A OG1 
818  C CG2 . THR A 114 ? 0.9650 0.7615 0.6681 0.2846  0.0784  -0.0636 113 THR A CG2 
819  N N   . ASP A 115 ? 1.0968 0.8676 0.8066 0.2400  0.0522  -0.0654 114 ASP A N   
820  C CA  . ASP A 115 ? 1.0905 0.8335 0.7876 0.2342  0.0395  -0.0756 114 ASP A CA  
821  C C   . ASP A 115 ? 0.9669 0.7050 0.6812 0.2169  0.0319  -0.0720 114 ASP A C   
822  O O   . ASP A 115 ? 1.0570 0.7742 0.7634 0.2094  0.0212  -0.0790 114 ASP A O   
823  C CB  . ASP A 115 ? 1.0256 0.7622 0.7027 0.2337  0.0352  -0.0821 114 ASP A CB  
824  C CG  . ASP A 115 ? 1.0333 0.7777 0.6927 0.2502  0.0436  -0.0846 114 ASP A CG  
825  O OD1 . ASP A 115 ? 1.0051 0.7588 0.6675 0.2626  0.0528  -0.0821 114 ASP A OD1 
826  O OD2 . ASP A 115 ? 1.0077 0.7499 0.6502 0.2510  0.0412  -0.0889 114 ASP A OD2 
827  N N   . TYR A 116 ? 0.8969 0.6539 0.6343 0.2102  0.0369  -0.0613 115 TYR A N   
828  C CA  . TYR A 116 ? 0.8672 0.6221 0.6209 0.1941  0.0307  -0.0573 115 TYR A CA  
829  C C   . TYR A 116 ? 0.8995 0.6586 0.6698 0.1944  0.0330  -0.0518 115 TYR A C   
830  O O   . TYR A 116 ? 0.8958 0.6650 0.6845 0.1830  0.0326  -0.0446 115 TYR A O   
831  C CB  . TYR A 116 ? 0.7991 0.5727 0.5651 0.1830  0.0329  -0.0497 115 TYR A CB  
832  C CG  . TYR A 116 ? 0.8596 0.6320 0.6104 0.1832  0.0311  -0.0536 115 TYR A CG  
833  C CD1 . TYR A 116 ? 0.8467 0.6046 0.5905 0.1733  0.0209  -0.0594 115 TYR A CD1 
834  C CD2 . TYR A 116 ? 0.9099 0.6965 0.6534 0.1934  0.0395  -0.0513 115 TYR A CD2 
835  C CE1 . TYR A 116 ? 0.8429 0.6005 0.5730 0.1737  0.0185  -0.0628 115 TYR A CE1 
836  C CE2 . TYR A 116 ? 0.9090 0.6946 0.6375 0.1940  0.0376  -0.0545 115 TYR A CE2 
837  C CZ  . TYR A 116 ? 0.9041 0.6752 0.6260 0.1843  0.0267  -0.0604 115 TYR A CZ  
838  O OH  . TYR A 116 ? 0.9607 0.7316 0.6679 0.1850  0.0241  -0.0635 115 TYR A OH  
839  N N   . GLN A 117 ? 0.9250 0.6764 0.6887 0.2078  0.0351  -0.0553 116 GLN A N   
840  C CA  . GLN A 117 ? 0.8494 0.6039 0.6280 0.2089  0.0364  -0.0504 116 GLN A CA  
841  C C   . GLN A 117 ? 0.8479 0.5837 0.6298 0.1971  0.0261  -0.0519 116 GLN A C   
842  O O   . GLN A 117 ? 0.8906 0.6348 0.6900 0.1888  0.0258  -0.0448 116 GLN A O   
843  C CB  . GLN A 117 ? 0.8594 0.6090 0.6293 0.2271  0.0407  -0.0543 116 GLN A CB  
844  C CG  . GLN A 117 ? 0.9031 0.6689 0.6659 0.2403  0.0509  -0.0540 116 GLN A CG  
845  C CD  . GLN A 117 ? 0.9816 0.7486 0.7416 0.2582  0.0569  -0.0556 116 GLN A CD  
846  O OE1 . GLN A 117 ? 0.9967 0.7476 0.7562 0.2619  0.0521  -0.0588 116 GLN A OE1 
847  N NE2 . GLN A 117 ? 0.9871 0.7731 0.7450 0.2698  0.0675  -0.0532 116 GLN A NE2 
848  N N   . GLY A 118 ? 0.8405 0.5509 0.6056 0.1961  0.0176  -0.0611 117 GLY A N   
849  C CA  . GLY A 118 ? 0.8266 0.5188 0.5943 0.1843  0.0079  -0.0622 117 GLY A CA  
850  C C   . GLY A 118 ? 0.8804 0.5836 0.6622 0.1669  0.0057  -0.0562 117 GLY A C   
851  O O   . GLY A 118 ? 0.9815 0.6805 0.7736 0.1571  0.0014  -0.0524 117 GLY A O   
852  N N   . LEU A 119 ? 0.8093 0.5266 0.5915 0.1632  0.0087  -0.0550 118 LEU A N   
853  C CA  . LEU A 119 ? 0.8614 0.5908 0.6578 0.1480  0.0075  -0.0491 118 LEU A CA  
854  C C   . LEU A 119 ? 0.8507 0.6000 0.6675 0.1454  0.0135  -0.0395 118 LEU A C   
855  O O   . LEU A 119 ? 0.8197 0.5714 0.6486 0.1334  0.0104  -0.0353 118 LEU A O   
856  C CB  . LEU A 119 ? 0.8053 0.5452 0.5973 0.1462  0.0094  -0.0498 118 LEU A CB  
857  C CG  . LEU A 119 ? 0.7475 0.5039 0.5551 0.1331  0.0103  -0.0431 118 LEU A CG  
858  C CD1 . LEU A 119 ? 0.7770 0.5211 0.5849 0.1195  0.0010  -0.0459 118 LEU A CD1 
859  C CD2 . LEU A 119 ? 0.7517 0.5229 0.5564 0.1363  0.0156  -0.0414 118 LEU A CD2 
860  N N   . VAL A 120 ? 0.8493 0.6133 0.6700 0.1566  0.0220  -0.0359 119 VAL A N   
861  C CA  . VAL A 120 ? 0.8891 0.6727 0.7296 0.1544  0.0273  -0.0269 119 VAL A CA  
862  C C   . VAL A 120 ? 0.8919 0.6656 0.7379 0.1529  0.0229  -0.0257 119 VAL A C   
863  O O   . VAL A 120 ? 0.9111 0.6941 0.7722 0.1439  0.0223  -0.0196 119 VAL A O   
864  C CB  . VAL A 120 ? 0.8574 0.6594 0.7011 0.1670  0.0373  -0.0232 119 VAL A CB  
865  C CG1 . VAL A 120 ? 0.8919 0.7138 0.7569 0.1644  0.0419  -0.0141 119 VAL A CG1 
866  C CG2 . VAL A 120 ? 0.7559 0.5683 0.5946 0.1674  0.0417  -0.0230 119 VAL A CG2 
867  N N   . ARG A 121 ? 0.8749 0.6292 0.7081 0.1621  0.0195  -0.0315 120 ARG A N   
868  C CA  . ARG A 121 ? 0.8993 0.6418 0.7362 0.1609  0.0146  -0.0302 120 ARG A CA  
869  C C   . ARG A 121 ? 0.8491 0.5799 0.6876 0.1451  0.0064  -0.0302 120 ARG A C   
870  O O   . ARG A 121 ? 0.8850 0.6142 0.7322 0.1396  0.0035  -0.0257 120 ARG A O   
871  C CB  . ARG A 121 ? 0.8861 0.6079 0.7079 0.1744  0.0123  -0.0370 120 ARG A CB  
872  C CG  . ARG A 121 ? 0.8650 0.5992 0.6868 0.1913  0.0208  -0.0363 120 ARG A CG  
873  C CD  . ARG A 121 ? 0.9482 0.6602 0.7548 0.2051  0.0182  -0.0437 120 ARG A CD  
874  N NE  . ARG A 121 ? 0.8858 0.6081 0.6871 0.2220  0.0267  -0.0457 120 ARG A NE  
875  C CZ  . ARG A 121 ? 0.8704 0.5830 0.6532 0.2307  0.0276  -0.0541 120 ARG A CZ  
876  N NH1 . ARG A 121 ? 0.9106 0.6028 0.6784 0.2240  0.0201  -0.0616 120 ARG A NH1 
877  N NH2 . ARG A 121 ? 0.8937 0.6181 0.6726 0.2465  0.0364  -0.0549 120 ARG A NH2 
878  N N   . LEU A 122 ? 0.8727 0.5962 0.7030 0.1378  0.0027  -0.0348 121 LEU A N   
879  C CA  . LEU A 122 ? 0.8901 0.6064 0.7238 0.1223  -0.0040 -0.0341 121 LEU A CA  
880  C C   . LEU A 122 ? 0.9159 0.6543 0.7667 0.1118  -0.0005 -0.0268 121 LEU A C   
881  O O   . LEU A 122 ? 0.9427 0.6794 0.8005 0.1003  -0.0045 -0.0238 121 LEU A O   
882  C CB  . LEU A 122 ? 0.7953 0.4976 0.6156 0.1181  -0.0095 -0.0415 121 LEU A CB  
883  C CG  . LEU A 122 ? 0.8329 0.5064 0.6387 0.1194  -0.0178 -0.0486 121 LEU A CG  
884  C CD1 . LEU A 122 ? 0.9557 0.6193 0.7672 0.1050  -0.0248 -0.0460 121 LEU A CD1 
885  C CD2 . LEU A 122 ? 0.8278 0.4908 0.6270 0.1340  -0.0163 -0.0504 121 LEU A CD2 
886  N N   . VAL A 123 ? 0.8605 0.6192 0.7178 0.1158  0.0068  -0.0238 122 VAL A N   
887  C CA  . VAL A 123 ? 0.8263 0.6052 0.7001 0.1068  0.0102  -0.0171 122 VAL A CA  
888  C C   . VAL A 123 ? 0.8178 0.6032 0.7038 0.1058  0.0109  -0.0113 122 VAL A C   
889  O O   . VAL A 123 ? 0.8381 0.6322 0.7355 0.0954  0.0101  -0.0070 122 VAL A O   
890  C CB  . VAL A 123 ? 0.7798 0.5774 0.6574 0.1118  0.0179  -0.0149 122 VAL A CB  
891  C CG1 . VAL A 123 ? 0.7288 0.5471 0.6249 0.1046  0.0219  -0.0076 122 VAL A CG1 
892  C CG2 . VAL A 123 ? 0.7908 0.5838 0.6580 0.1097  0.0162  -0.0196 122 VAL A CG2 
893  N N   . ALA A 124 ? 0.8200 0.6011 0.7034 0.1170  0.0120  -0.0112 123 ALA A N   
894  C CA  . ALA A 124 ? 0.8263 0.6133 0.7206 0.1170  0.0119  -0.0055 123 ALA A CA  
895  C C   . ALA A 124 ? 0.8303 0.6060 0.7253 0.1053  0.0049  -0.0044 123 ALA A C   
896  O O   . ALA A 124 ? 0.8650 0.6517 0.7719 0.0986  0.0048  0.0010  123 ALA A O   
897  C CB  . ALA A 124 ? 0.7701 0.5507 0.6594 0.1316  0.0131  -0.0065 123 ALA A CB  
898  N N   . LEU A 125 ? 0.8224 0.5763 0.7047 0.1027  -0.0011 -0.0095 124 LEU A N   
899  C CA  . LEU A 125 ? 0.8532 0.5972 0.7362 0.0905  -0.0073 -0.0079 124 LEU A CA  
900  C C   . LEU A 125 ? 0.8185 0.5727 0.7077 0.0775  -0.0071 -0.0072 124 LEU A C   
901  O O   . LEU A 125 ? 0.8672 0.6241 0.7629 0.0672  -0.0094 -0.0036 124 LEU A O   
902  C CB  . LEU A 125 ? 0.8629 0.5800 0.7314 0.0913  -0.0141 -0.0131 124 LEU A CB  
903  C CG  . LEU A 125 ? 0.9189 0.6236 0.7868 0.0782  -0.0206 -0.0115 124 LEU A CG  
904  C CD1 . LEU A 125 ? 0.8895 0.5982 0.7655 0.0759  -0.0213 -0.0042 124 LEU A CD1 
905  C CD2 . LEU A 125 ? 0.9364 0.6140 0.7900 0.0791  -0.0273 -0.0172 124 LEU A CD2 
906  N N   . VAL A 126 ? 0.7810 0.5416 0.6682 0.0785  -0.0043 -0.0105 125 VAL A N   
907  C CA  . VAL A 126 ? 0.7990 0.5690 0.6921 0.0672  -0.0042 -0.0100 125 VAL A CA  
908  C C   . VAL A 126 ? 0.7673 0.5581 0.6758 0.0629  0.0003  -0.0041 125 VAL A C   
909  O O   . VAL A 126 ? 0.8085 0.6038 0.7237 0.0521  -0.0013 -0.0020 125 VAL A O   
910  C CB  . VAL A 126 ? 0.8171 0.5887 0.7037 0.0704  -0.0025 -0.0146 125 VAL A CB  
911  C CG1 . VAL A 126 ? 0.7737 0.5626 0.6708 0.0628  0.0006  -0.0121 125 VAL A CG1 
912  C CG2 . VAL A 126 ? 0.7539 0.5054 0.6271 0.0682  -0.0092 -0.0209 125 VAL A CG2 
913  N N   . GLN A 127 ? 0.8050 0.6090 0.7196 0.0712  0.0059  -0.0013 126 GLN A N   
914  C CA  . GLN A 127 ? 0.8340 0.6572 0.7636 0.0670  0.0096  0.0040  126 GLN A CA  
915  C C   . GLN A 127 ? 0.8535 0.6762 0.7884 0.0623  0.0065  0.0077  126 GLN A C   
916  O O   . GLN A 127 ? 0.8930 0.7289 0.8389 0.0556  0.0076  0.0110  126 GLN A O   
917  C CB  . GLN A 127 ? 0.8238 0.6614 0.7593 0.0768  0.0160  0.0065  126 GLN A CB  
918  C CG  . GLN A 127 ? 0.8156 0.6486 0.7476 0.0885  0.0165  0.0070  126 GLN A CG  
919  C CD  . GLN A 127 ? 0.8306 0.6735 0.7743 0.0881  0.0165  0.0125  126 GLN A CD  
920  O OE1 . GLN A 127 ? 0.8222 0.6821 0.7790 0.0832  0.0191  0.0164  126 GLN A OE1 
921  N NE2 . GLN A 127 ? 0.8064 0.6383 0.7453 0.0934  0.0130  0.0126  126 GLN A NE2 
922  N N   . MET A 128 ? 0.8181 0.6254 0.7451 0.0659  0.0023  0.0071  127 MET A N   
923  C CA  . MET A 128 ? 0.7830 0.5879 0.7130 0.0608  -0.0013 0.0109  127 MET A CA  
924  C C   . MET A 128 ? 0.7797 0.5820 0.7099 0.0474  -0.0045 0.0109  127 MET A C   
925  O O   . MET A 128 ? 0.8299 0.6412 0.7674 0.0406  -0.0048 0.0145  127 MET A O   
926  C CB  . MET A 128 ? 0.7822 0.5691 0.7027 0.0680  -0.0053 0.0105  127 MET A CB  
927  C CG  . MET A 128 ? 0.8273 0.6199 0.7506 0.0812  -0.0023 0.0122  127 MET A CG  
928  S SD  . MET A 128 ? 1.0829 0.8636 1.0037 0.0861  -0.0073 0.0161  127 MET A SD  
929  C CE  . MET A 128 ? 0.8118 0.6086 0.7448 0.0752  -0.0083 0.0227  127 MET A CE  
930  N N   . GLY A 129 ? 0.7366 0.5275 0.6588 0.0436  -0.0068 0.0066  128 GLY A N   
931  C CA  . GLY A 129 ? 0.7204 0.5110 0.6440 0.0312  -0.0091 0.0065  128 GLY A CA  
932  C C   . GLY A 129 ? 0.7466 0.5552 0.6803 0.0259  -0.0050 0.0069  128 GLY A C   
933  O O   . GLY A 129 ? 0.7638 0.5780 0.7023 0.0164  -0.0056 0.0083  128 GLY A O   
934  N N   . ILE A 130 ? 0.7773 0.5952 0.7140 0.0322  -0.0007 0.0057  129 ILE A N   
935  C CA  . ILE A 130 ? 0.7429 0.5771 0.6896 0.0279  0.0032  0.0064  129 ILE A CA  
936  C C   . ILE A 130 ? 0.7037 0.5508 0.6611 0.0253  0.0048  0.0106  129 ILE A C   
937  O O   . ILE A 130 ? 0.7247 0.5802 0.6888 0.0173  0.0054  0.0111  129 ILE A O   
938  C CB  . ILE A 130 ? 0.7387 0.5788 0.6855 0.0356  0.0074  0.0051  129 ILE A CB  
939  C CG1 . ILE A 130 ? 0.7757 0.6060 0.7129 0.0355  0.0053  0.0004  129 ILE A CG1 
940  C CG2 . ILE A 130 ? 0.7595 0.6173 0.7188 0.0329  0.0119  0.0075  129 ILE A CG2 
941  C CD1 . ILE A 130 ? 0.6451 0.4807 0.5803 0.0433  0.0093  -0.0007 129 ILE A CD1 
942  N N   . ALA A 131 ? 0.7242 0.5729 0.6830 0.0321  0.0053  0.0133  130 ALA A N   
943  C CA  . ALA A 131 ? 0.7868 0.6481 0.7556 0.0299  0.0060  0.0172  130 ALA A CA  
944  C C   . ALA A 131 ? 0.7535 0.6108 0.7206 0.0214  0.0020  0.0185  130 ALA A C   
945  O O   . ALA A 131 ? 0.6521 0.5201 0.6265 0.0150  0.0026  0.0196  130 ALA A O   
946  C CB  . ALA A 131 ? 0.7643 0.6285 0.7353 0.0397  0.0069  0.0200  130 ALA A CB  
947  N N   . TRP A 132 ? 0.7570 0.5986 0.7142 0.0212  -0.0020 0.0184  131 TRP A N   
948  C CA  . TRP A 132 ? 0.7602 0.5979 0.7149 0.0132  -0.0054 0.0206  131 TRP A CA  
949  C C   . TRP A 132 ? 0.7021 0.5424 0.6579 0.0031  -0.0050 0.0185  131 TRP A C   
950  O O   . TRP A 132 ? 0.7256 0.5728 0.6845 -0.0040 -0.0052 0.0202  131 TRP A O   
951  C CB  . TRP A 132 ? 0.8017 0.6209 0.7459 0.0157  -0.0099 0.0217  131 TRP A CB  
952  C CG  . TRP A 132 ? 0.8954 0.7139 0.8399 0.0231  -0.0113 0.0256  131 TRP A CG  
953  C CD1 . TRP A 132 ? 0.9753 0.7877 0.9170 0.0343  -0.0113 0.0252  131 TRP A CD1 
954  C CD2 . TRP A 132 ? 0.7900 0.6151 0.7377 0.0205  -0.0132 0.0303  131 TRP A CD2 
955  N NE1 . TRP A 132 ? 0.9789 0.7940 0.9231 0.0389  -0.0130 0.0297  131 TRP A NE1 
956  C CE2 . TRP A 132 ? 0.8644 0.6873 0.8120 0.0304  -0.0145 0.0330  131 TRP A CE2 
957  C CE3 . TRP A 132 ? 0.7571 0.5902 0.7074 0.0112  -0.0139 0.0324  131 TRP A CE3 
958  C CZ2 . TRP A 132 ? 0.8703 0.6988 0.8207 0.0309  -0.0171 0.0381  131 TRP A CZ2 
959  C CZ3 . TRP A 132 ? 0.8232 0.6614 0.7749 0.0116  -0.0163 0.0370  131 TRP A CZ3 
960  C CH2 . TRP A 132 ? 0.8246 0.6606 0.7766 0.0213  -0.0181 0.0400  131 TRP A CH2 
961  N N   . GLY A 133 ? 0.7003 0.5359 0.6533 0.0027  -0.0043 0.0148  132 GLY A N   
962  C CA  . GLY A 133 ? 0.6782 0.5182 0.6338 -0.0061 -0.0037 0.0128  132 GLY A CA  
963  C C   . GLY A 133 ? 0.7073 0.5641 0.6733 -0.0086 0.0001  0.0126  132 GLY A C   
964  O O   . GLY A 133 ? 0.6926 0.5555 0.6617 -0.0161 0.0005  0.0126  132 GLY A O   
965  N N   . ASN A 134 ? 0.7842 0.6487 0.7557 -0.0021 0.0031  0.0125  133 ASN A N   
966  C CA  . ASN A 134 ? 0.7305 0.6097 0.7124 -0.0044 0.0064  0.0125  133 ASN A CA  
967  C C   . ASN A 134 ? 0.7310 0.6169 0.7167 -0.0079 0.0054  0.0148  133 ASN A C   
968  O O   . ASN A 134 ? 0.7645 0.6596 0.7563 -0.0132 0.0068  0.0138  133 ASN A O   
969  C CB  . ASN A 134 ? 0.7835 0.6689 0.7705 0.0030  0.0097  0.0129  133 ASN A CB  
970  C CG  . ASN A 134 ? 0.8170 0.6993 0.8013 0.0055  0.0113  0.0104  133 ASN A CG  
971  O OD1 . ASN A 134 ? 0.8187 0.6953 0.7987 0.0011  0.0096  0.0080  133 ASN A OD1 
972  N ND2 . ASN A 134 ? 0.7197 0.6066 0.7067 0.0125  0.0145  0.0113  133 ASN A ND2 
973  N N   . LEU A 135 ? 0.6816 0.5627 0.6632 -0.0048 0.0028  0.0177  134 LEU A N   
974  C CA  . LEU A 135 ? 0.6894 0.5765 0.6731 -0.0081 0.0010  0.0202  134 LEU A CA  
975  C C   . LEU A 135 ? 0.6406 0.5256 0.6198 -0.0169 -0.0003 0.0198  134 LEU A C   
976  O O   . LEU A 135 ? 0.6376 0.5318 0.6205 -0.0218 0.0001  0.0193  134 LEU A O   
977  C CB  . LEU A 135 ? 0.7091 0.5909 0.6890 -0.0020 -0.0019 0.0239  134 LEU A CB  
978  C CG  . LEU A 135 ? 0.5694 0.4563 0.5497 -0.0049 -0.0047 0.0271  134 LEU A CG  
979  C CD1 . LEU A 135 ? 0.4529 0.3557 0.4440 -0.0063 -0.0032 0.0264  134 LEU A CD1 
980  C CD2 . LEU A 135 ? 0.5851 0.4654 0.5614 0.0021  -0.0079 0.0311  134 LEU A CD2 
981  N N   . LEU A 136 ? 0.6419 0.5148 0.6129 -0.0190 -0.0021 0.0199  135 LEU A N   
982  C CA  . LEU A 136 ? 0.6297 0.5014 0.5969 -0.0276 -0.0028 0.0203  135 LEU A CA  
983  C C   . LEU A 136 ? 0.6336 0.5152 0.6070 -0.0327 0.0004  0.0166  135 LEU A C   
984  O O   . LEU A 136 ? 0.6038 0.4916 0.5775 -0.0389 0.0012  0.0165  135 LEU A O   
985  C CB  . LEU A 136 ? 0.6350 0.4918 0.5939 -0.0292 -0.0055 0.0214  135 LEU A CB  
986  C CG  . LEU A 136 ? 0.6395 0.4838 0.5915 -0.0236 -0.0091 0.0249  135 LEU A CG  
987  C CD1 . LEU A 136 ? 0.6577 0.4859 0.6016 -0.0266 -0.0121 0.0254  135 LEU A CD1 
988  C CD2 . LEU A 136 ? 0.5665 0.4145 0.5172 -0.0244 -0.0108 0.0294  135 LEU A CD2 
989  N N   . LEU A 137 ? 0.6317 0.5147 0.6095 -0.0296 0.0025  0.0135  136 LEU A N   
990  C CA  . LEU A 137 ? 0.5937 0.4859 0.5781 -0.0333 0.0055  0.0102  136 LEU A CA  
991  C C   . LEU A 137 ? 0.5929 0.4966 0.5846 -0.0335 0.0074  0.0094  136 LEU A C   
992  O O   . LEU A 137 ? 0.6149 0.5261 0.6109 -0.0378 0.0093  0.0068  136 LEU A O   
993  C CB  . LEU A 137 ? 0.6013 0.4917 0.5880 -0.0296 0.0068  0.0078  136 LEU A CB  
994  C CG  . LEU A 137 ? 0.5588 0.4378 0.5385 -0.0296 0.0044  0.0074  136 LEU A CG  
995  C CD1 . LEU A 137 ? 0.5855 0.4630 0.5661 -0.0238 0.0054  0.0053  136 LEU A CD1 
996  C CD2 . LEU A 137 ? 0.5256 0.4052 0.5050 -0.0376 0.0039  0.0064  136 LEU A CD2 
997  N N   . ALA A 138 ? 0.5824 0.4880 0.5761 -0.0288 0.0065  0.0114  137 ALA A N   
998  C CA  . ALA A 138 ? 0.5474 0.4636 0.5484 -0.0295 0.0073  0.0107  137 ALA A CA  
999  C C   . ALA A 138 ? 0.5530 0.4723 0.5500 -0.0349 0.0056  0.0111  137 ALA A C   
1000 O O   . ALA A 138 ? 0.5535 0.4809 0.5548 -0.0383 0.0066  0.0083  137 ALA A O   
1001 C CB  . ALA A 138 ? 0.5546 0.4732 0.5599 -0.0232 0.0068  0.0131  137 ALA A CB  
1002 N N   . LEU A 139 ? 0.5509 0.4633 0.5393 -0.0356 0.0028  0.0145  138 LEU A N   
1003 C CA  . LEU A 139 ? 0.5526 0.4678 0.5356 -0.0406 0.0013  0.0156  138 LEU A CA  
1004 C C   . LEU A 139 ? 0.6027 0.5208 0.5844 -0.0471 0.0039  0.0128  138 LEU A C   
1005 O O   . LEU A 139 ? 0.6761 0.6019 0.6574 -0.0508 0.0045  0.0110  138 LEU A O   
1006 C CB  . LEU A 139 ? 0.5362 0.4422 0.5101 -0.0398 -0.0021 0.0209  138 LEU A CB  
1007 C CG  . LEU A 139 ? 0.5896 0.4896 0.5637 -0.0322 -0.0045 0.0239  138 LEU A CG  
1008 C CD1 . LEU A 139 ? 0.6661 0.5522 0.6306 -0.0317 -0.0072 0.0279  138 LEU A CD1 
1009 C CD2 . LEU A 139 ? 0.5809 0.4889 0.5584 -0.0295 -0.0068 0.0256  138 LEU A CD2 
1010 N N   . MET A 140 ? 0.5816 0.4943 0.5626 -0.0483 0.0053  0.0122  139 MET A N   
1011 C CA  . MET A 140 ? 0.5639 0.4812 0.5456 -0.0539 0.0080  0.0096  139 MET A CA  
1012 C C   . MET A 140 ? 0.5972 0.5240 0.5875 -0.0536 0.0110  0.0044  139 MET A C   
1013 O O   . MET A 140 ? 0.6758 0.6093 0.6666 -0.0576 0.0133  0.0018  139 MET A O   
1014 C CB  . MET A 140 ? 0.5640 0.4740 0.5444 -0.0552 0.0081  0.0102  139 MET A CB  
1015 C CG  . MET A 140 ? 0.7242 0.6260 0.6959 -0.0593 0.0058  0.0148  139 MET A CG  
1016 S SD  . MET A 140 ? 0.7438 0.6343 0.7141 -0.0602 0.0042  0.0153  139 MET A SD  
1017 C CE  . MET A 140 ? 0.6401 0.5289 0.6156 -0.0518 0.0043  0.0118  139 MET A CE  
1018 N N   . LYS A 141 ? 0.5674 0.4946 0.5644 -0.0486 0.0113  0.0031  140 LYS A N   
1019 C CA  . LYS A 141 ? 0.5472 0.4821 0.5526 -0.0483 0.0136  -0.0012 140 LYS A CA  
1020 C C   . LYS A 141 ? 0.5725 0.5139 0.5782 -0.0501 0.0128  -0.0028 140 LYS A C   
1021 O O   . LYS A 141 ? 0.5390 0.4862 0.5482 -0.0522 0.0147  -0.0073 140 LYS A O   
1022 C CB  . LYS A 141 ? 0.5408 0.4744 0.5531 -0.0429 0.0141  -0.0010 140 LYS A CB  
1023 C CG  . LYS A 141 ? 0.6057 0.5355 0.6193 -0.0413 0.0156  -0.0014 140 LYS A CG  
1024 C CD  . LYS A 141 ? 0.5499 0.4790 0.5689 -0.0357 0.0164  -0.0006 140 LYS A CD  
1025 C CE  . LYS A 141 ? 0.5220 0.4459 0.5392 -0.0334 0.0168  -0.0004 140 LYS A CE  
1026 N NZ  . LYS A 141 ? 0.5782 0.5005 0.5976 -0.0272 0.0175  0.0014  140 LYS A NZ  
1027 N N   . GLY A 142 ? 0.5783 0.5185 0.5799 -0.0490 0.0096  0.0005  141 GLY A N   
1028 C CA  . GLY A 142 ? 0.5426 0.4892 0.5439 -0.0507 0.0078  -0.0011 141 GLY A CA  
1029 C C   . GLY A 142 ? 0.5790 0.5291 0.5732 -0.0558 0.0088  -0.0033 141 GLY A C   
1030 O O   . GLY A 142 ? 0.5759 0.5322 0.5706 -0.0575 0.0084  -0.0072 141 GLY A O   
1031 N N   . PHE A 143 ? 0.5649 0.5115 0.5524 -0.0582 0.0100  -0.0008 142 PHE A N   
1032 C CA  . PHE A 143 ? 0.5597 0.5109 0.5408 -0.0631 0.0120  -0.0021 142 PHE A CA  
1033 C C   . PHE A 143 ? 0.5687 0.5237 0.5549 -0.0646 0.0165  -0.0066 142 PHE A C   
1034 O O   . PHE A 143 ? 0.5257 0.4850 0.5074 -0.0684 0.0191  -0.0072 142 PHE A O   
1035 C CB  . PHE A 143 ? 0.5575 0.5034 0.5288 -0.0657 0.0108  0.0041  142 PHE A CB  
1036 C CG  . PHE A 143 ? 0.6039 0.5471 0.5687 -0.0644 0.0063  0.0086  142 PHE A CG  
1037 C CD1 . PHE A 143 ? 0.5689 0.5189 0.5287 -0.0658 0.0049  0.0074  142 PHE A CD1 
1038 C CD2 . PHE A 143 ? 0.6372 0.5713 0.6007 -0.0612 0.0033  0.0138  142 PHE A CD2 
1039 C CE1 . PHE A 143 ? 0.6203 0.5686 0.5744 -0.0643 0.0002  0.0118  142 PHE A CE1 
1040 C CE2 . PHE A 143 ? 0.6690 0.6011 0.6272 -0.0593 -0.0010 0.0182  142 PHE A CE2 
1041 C CZ  . PHE A 143 ? 0.6606 0.6002 0.6144 -0.0609 -0.0026 0.0175  142 PHE A CZ  
1042 N N   . ARG A 144 ? 0.5441 0.4982 0.5397 -0.0615 0.0176  -0.0092 143 ARG A N   
1043 C CA  . ARG A 144 ? 0.5601 0.5180 0.5619 -0.0619 0.0214  -0.0134 143 ARG A CA  
1044 C C   . ARG A 144 ? 0.5417 0.4990 0.5406 -0.0650 0.0231  -0.0108 143 ARG A C   
1045 O O   . ARG A 144 ? 0.5057 0.4695 0.5064 -0.0672 0.0265  -0.0136 143 ARG A O   
1046 C CB  . ARG A 144 ? 0.6220 0.5874 0.6247 -0.0630 0.0235  -0.0194 143 ARG A CB  
1047 C CG  . ARG A 144 ? 0.6022 0.5679 0.6083 -0.0609 0.0210  -0.0223 143 ARG A CG  
1048 C CD  . ARG A 144 ? 0.6023 0.5732 0.6112 -0.0613 0.0232  -0.0297 143 ARG A CD  
1049 N NE  . ARG A 144 ? 0.6653 0.6415 0.6646 -0.0642 0.0240  -0.0318 143 ARG A NE  
1050 C CZ  . ARG A 144 ? 0.7125 0.6934 0.7110 -0.0644 0.0259  -0.0388 143 ARG A CZ  
1051 N NH1 . ARG A 144 ? 0.7166 0.6968 0.7242 -0.0620 0.0269  -0.0443 143 ARG A NH1 
1052 N NH2 . ARG A 144 ? 0.7342 0.7202 0.7222 -0.0668 0.0268  -0.0401 143 ARG A NH2 
1053 N N   . ASP A 145 ? 0.5851 0.5348 0.5801 -0.0652 0.0207  -0.0056 144 ASP A N   
1054 C CA  . ASP A 145 ? 0.5768 0.5244 0.5695 -0.0689 0.0213  -0.0027 144 ASP A CA  
1055 C C   . ASP A 145 ? 0.6764 0.6214 0.6763 -0.0664 0.0214  -0.0041 144 ASP A C   
1056 O O   . ASP A 145 ? 0.6725 0.6089 0.6714 -0.0639 0.0187  -0.0018 144 ASP A O   
1057 C CB  . ASP A 145 ? 0.5091 0.4479 0.4932 -0.0704 0.0179  0.0034  144 ASP A CB  
1058 C CG  . ASP A 145 ? 0.6359 0.5728 0.6170 -0.0760 0.0184  0.0068  144 ASP A CG  
1059 O OD1 . ASP A 145 ? 0.6665 0.6113 0.6523 -0.0789 0.0217  0.0046  144 ASP A OD1 
1060 O OD2 . ASP A 145 ? 0.6869 0.6143 0.6615 -0.0774 0.0153  0.0119  144 ASP A OD2 
1061 N N   . ALA A 146 ? 0.6196 0.5724 0.6266 -0.0667 0.0246  -0.0081 145 ALA A N   
1062 C CA  . ALA A 146 ? 0.5860 0.5377 0.5999 -0.0642 0.0245  -0.0093 145 ALA A CA  
1063 C C   . ALA A 146 ? 0.6173 0.5651 0.6292 -0.0676 0.0229  -0.0062 145 ALA A C   
1064 O O   . ALA A 146 ? 0.6941 0.6358 0.7072 -0.0652 0.0205  -0.0057 145 ALA A O   
1065 C CB  . ALA A 146 ? 0.5684 0.5294 0.5906 -0.0632 0.0281  -0.0142 145 ALA A CB  
1066 N N   . ALA A 147 ? 0.6318 0.5832 0.6405 -0.0735 0.0239  -0.0041 146 ALA A N   
1067 C CA  . ALA A 147 ? 0.6234 0.5711 0.6312 -0.0780 0.0220  -0.0010 146 ALA A CA  
1068 C C   . ALA A 147 ? 0.6173 0.5508 0.6173 -0.0775 0.0173  0.0029  146 ALA A C   
1069 O O   . ALA A 147 ? 0.6262 0.5525 0.6263 -0.0778 0.0142  0.0036  146 ALA A O   
1070 C CB  . ALA A 147 ? 0.6307 0.5867 0.6377 -0.0849 0.0248  0.0012  146 ALA A CB  
1071 N N   . GLY A 148 ? 0.6572 0.5862 0.6503 -0.0764 0.0165  0.0051  147 GLY A N   
1072 C CA  . GLY A 148 ? 0.6736 0.5889 0.6595 -0.0749 0.0122  0.0086  147 GLY A CA  
1073 C C   . GLY A 148 ? 0.6479 0.5566 0.6355 -0.0679 0.0102  0.0065  147 GLY A C   
1074 O O   . GLY A 148 ? 0.6604 0.5579 0.6440 -0.0668 0.0068  0.0079  147 GLY A O   
1075 N N   . ASN A 149 ? 0.6420 0.5572 0.6353 -0.0633 0.0124  0.0031  148 ASN A N   
1076 C CA  . ASN A 149 ? 0.6086 0.5192 0.6037 -0.0566 0.0113  0.0017  148 ASN A CA  
1077 C C   . ASN A 149 ? 0.5672 0.4769 0.5654 -0.0567 0.0106  -0.0001 148 ASN A C   
1078 O O   . ASN A 149 ? 0.5365 0.4376 0.5314 -0.0531 0.0080  0.0000  148 ASN A O   
1079 C CB  . ASN A 149 ? 0.5705 0.4885 0.5716 -0.0526 0.0139  -0.0006 148 ASN A CB  
1080 C CG  . ASN A 149 ? 0.5877 0.5019 0.5907 -0.0458 0.0134  -0.0009 148 ASN A CG  
1081 O OD1 . ASN A 149 ? 0.5821 0.4891 0.5803 -0.0422 0.0115  0.0013  148 ASN A OD1 
1082 N ND2 . ASN A 149 ? 0.6406 0.5600 0.6505 -0.0436 0.0154  -0.0033 148 ASN A ND2 
1083 N N   . ALA A 150 ? 0.5414 0.4605 0.5458 -0.0605 0.0127  -0.0020 149 ALA A N   
1084 C CA  . ALA A 150 ? 0.5590 0.4790 0.5674 -0.0607 0.0116  -0.0036 149 ALA A CA  
1085 C C   . ALA A 150 ? 0.6219 0.5329 0.6249 -0.0649 0.0075  -0.0017 149 ALA A C   
1086 O O   . ALA A 150 ? 0.6639 0.5685 0.6652 -0.0625 0.0043  -0.0028 149 ALA A O   
1087 C CB  . ALA A 150 ? 0.6101 0.5433 0.6273 -0.0636 0.0149  -0.0058 149 ALA A CB  
1088 N N   . LEU A 151 ? 0.5973 0.5073 0.5971 -0.0712 0.0072  0.0012  150 LEU A N   
1089 C CA  . LEU A 151 ? 0.6054 0.5059 0.6008 -0.0762 0.0030  0.0034  150 LEU A CA  
1090 C C   . LEU A 151 ? 0.6367 0.5210 0.6231 -0.0715 -0.0011 0.0041  150 LEU A C   
1091 O O   . LEU A 151 ? 0.6239 0.4985 0.6070 -0.0727 -0.0055 0.0036  150 LEU A O   
1092 C CB  . LEU A 151 ? 0.6215 0.5242 0.6151 -0.0840 0.0041  0.0075  150 LEU A CB  
1093 C CG  . LEU A 151 ? 0.5939 0.5081 0.5950 -0.0915 0.0058  0.0080  150 LEU A CG  
1094 C CD1 . LEU A 151 ? 0.6480 0.5549 0.6497 -0.0959 0.0008  0.0085  150 LEU A CD1 
1095 C CD2 . LEU A 151 ? 0.6236 0.5528 0.6342 -0.0885 0.0099  0.0039  150 LEU A CD2 
1096 N N   . SER A 152 ? 0.6534 0.5348 0.6360 -0.0660 0.0000  0.0049  151 SER A N   
1097 C CA  . SER A 152 ? 0.6425 0.5099 0.6173 -0.0602 -0.0032 0.0053  151 SER A CA  
1098 C C   . SER A 152 ? 0.6365 0.5017 0.6117 -0.0538 -0.0041 0.0017  151 SER A C   
1099 O O   . SER A 152 ? 0.6991 0.5518 0.6674 -0.0509 -0.0079 0.0009  151 SER A O   
1100 C CB  . SER A 152 ? 0.6139 0.4814 0.5863 -0.0557 -0.0016 0.0073  151 SER A CB  
1101 O OG  . SER A 152 ? 0.6651 0.5348 0.6358 -0.0613 -0.0010 0.0109  151 SER A OG  
1102 N N   . LEU A 153 ? 0.6250 0.5018 0.6076 -0.0513 -0.0008 -0.0005 152 LEU A N   
1103 C CA  . LEU A 153 ? 0.5873 0.4630 0.5699 -0.0452 -0.0014 -0.0031 152 LEU A CA  
1104 C C   . LEU A 153 ? 0.6568 0.5301 0.6391 -0.0487 -0.0050 -0.0051 152 LEU A C   
1105 O O   . LEU A 153 ? 0.6826 0.5483 0.6595 -0.0443 -0.0080 -0.0071 152 LEU A O   
1106 C CB  . LEU A 153 ? 0.5733 0.4612 0.5640 -0.0418 0.0030  -0.0040 152 LEU A CB  
1107 C CG  . LEU A 153 ? 0.5640 0.4548 0.5561 -0.0379 0.0061  -0.0025 152 LEU A CG  
1108 C CD1 . LEU A 153 ? 0.5123 0.4140 0.5133 -0.0358 0.0098  -0.0036 152 LEU A CD1 
1109 C CD2 . LEU A 153 ? 0.5194 0.4009 0.5046 -0.0310 0.0048  -0.0015 152 LEU A CD2 
1110 N N   . ILE A 154 ? 0.6497 0.5302 0.6379 -0.0564 -0.0050 -0.0047 153 ILE A N   
1111 C CA  . ILE A 154 ? 0.6854 0.5658 0.6753 -0.0605 -0.0088 -0.0064 153 ILE A CA  
1112 C C   . ILE A 154 ? 0.6729 0.5374 0.6538 -0.0631 -0.0145 -0.0062 153 ILE A C   
1113 O O   . ILE A 154 ? 0.7280 0.5852 0.7046 -0.0613 -0.0190 -0.0089 153 ILE A O   
1114 C CB  . ILE A 154 ? 0.6113 0.5053 0.6112 -0.0681 -0.0067 -0.0056 153 ILE A CB  
1115 C CG1 . ILE A 154 ? 0.6035 0.5116 0.6121 -0.0644 -0.0019 -0.0070 153 ILE A CG1 
1116 C CG2 . ILE A 154 ? 0.4902 0.3840 0.4925 -0.0738 -0.0115 -0.0065 153 ILE A CG2 
1117 C CD1 . ILE A 154 ? 0.6674 0.5893 0.6850 -0.0702 0.0016  -0.0064 153 ILE A CD1 
1118 N N   . VAL A 155 ? 0.6726 0.5308 0.6500 -0.0674 -0.0148 -0.0030 154 VAL A N   
1119 C CA  . VAL A 155 ? 0.6481 0.4890 0.6168 -0.0698 -0.0204 -0.0024 154 VAL A CA  
1120 C C   . VAL A 155 ? 0.6613 0.4892 0.6204 -0.0603 -0.0224 -0.0049 154 VAL A C   
1121 O O   . VAL A 155 ? 0.6806 0.4956 0.6328 -0.0596 -0.0278 -0.0076 154 VAL A O   
1122 C CB  . VAL A 155 ? 0.6338 0.4707 0.6006 -0.0756 -0.0197 0.0025  154 VAL A CB  
1123 C CG1 . VAL A 155 ? 0.6542 0.4708 0.6116 -0.0773 -0.0257 0.0034  154 VAL A CG1 
1124 C CG2 . VAL A 155 ? 0.6219 0.4721 0.5976 -0.0852 -0.0175 0.0051  154 VAL A CG2 
1125 N N   . GLY A 156 ? 0.6419 0.4735 0.6004 -0.0527 -0.0182 -0.0044 155 GLY A N   
1126 C CA  . GLY A 156 ? 0.6915 0.5130 0.6416 -0.0429 -0.0191 -0.0063 155 GLY A CA  
1127 C C   . GLY A 156 ? 0.7180 0.5407 0.6667 -0.0381 -0.0203 -0.0105 155 GLY A C   
1128 O O   . GLY A 156 ? 0.6923 0.5036 0.6316 -0.0315 -0.0228 -0.0131 155 GLY A O   
1129 N N   . SER A 157 ? 0.6907 0.5271 0.6479 -0.0408 -0.0186 -0.0112 156 SER A N   
1130 C CA  . SER A 157 ? 0.6718 0.5101 0.6277 -0.0368 -0.0202 -0.0145 156 SER A CA  
1131 C C   . SER A 157 ? 0.7274 0.5565 0.6785 -0.0414 -0.0273 -0.0175 156 SER A C   
1132 O O   . SER A 157 ? 0.7245 0.5482 0.6685 -0.0364 -0.0305 -0.0210 156 SER A O   
1133 C CB  . SER A 157 ? 0.6215 0.4771 0.5887 -0.0379 -0.0165 -0.0139 156 SER A CB  
1134 O OG  . SER A 157 ? 0.6357 0.4990 0.6076 -0.0340 -0.0105 -0.0116 156 SER A OG  
1135 N N   . LEU A 158 ? 0.7373 0.5648 0.6920 -0.0511 -0.0300 -0.0161 157 LEU A N   
1136 C CA  . LEU A 158 ? 0.8160 0.6346 0.7674 -0.0568 -0.0373 -0.0187 157 LEU A CA  
1137 C C   . LEU A 158 ? 0.8275 0.6247 0.7653 -0.0533 -0.0420 -0.0210 157 LEU A C   
1138 O O   . LEU A 158 ? 0.8279 0.6157 0.7578 -0.0509 -0.0475 -0.0257 157 LEU A O   
1139 C CB  . LEU A 158 ? 0.8062 0.6305 0.7667 -0.0687 -0.0381 -0.0157 157 LEU A CB  
1140 C CG  . LEU A 158 ? 0.7005 0.5460 0.6747 -0.0722 -0.0337 -0.0140 157 LEU A CG  
1141 C CD1 . LEU A 158 ? 0.7094 0.5608 0.6918 -0.0836 -0.0337 -0.0105 157 LEU A CD1 
1142 C CD2 . LEU A 158 ? 0.7109 0.5640 0.6883 -0.0698 -0.0363 -0.0175 157 LEU A CD2 
1143 N N   . ILE A 159 ? 0.7299 0.5188 0.6642 -0.0525 -0.0402 -0.0180 158 ILE A N   
1144 C CA  . ILE A 159 ? 0.7008 0.4689 0.6223 -0.0479 -0.0442 -0.0201 158 ILE A CA  
1145 C C   . ILE A 159 ? 0.7160 0.4814 0.6293 -0.0350 -0.0422 -0.0235 158 ILE A C   
1146 O O   . ILE A 159 ? 0.7250 0.4736 0.6264 -0.0295 -0.0461 -0.0272 158 ILE A O   
1147 C CB  . ILE A 159 ? 0.7487 0.5094 0.6694 -0.0500 -0.0429 -0.0153 158 ILE A CB  
1148 C CG1 . ILE A 159 ? 0.7091 0.4836 0.6353 -0.0454 -0.0353 -0.0116 158 ILE A CG1 
1149 C CG2 . ILE A 159 ? 0.7493 0.5098 0.6759 -0.0630 -0.0455 -0.0117 158 ILE A CG2 
1150 C CD1 . ILE A 159 ? 0.7316 0.5051 0.6599 -0.0501 -0.0337 -0.0059 158 ILE A CD1 
1151 N N   . GLY A 160 ? 0.7241 0.5054 0.6432 -0.0299 -0.0361 -0.0222 159 GLY A N   
1152 C CA  . GLY A 160 ? 0.7284 0.5092 0.6405 -0.0182 -0.0337 -0.0246 159 GLY A CA  
1153 C C   . GLY A 160 ? 0.7573 0.5354 0.6629 -0.0160 -0.0380 -0.0297 159 GLY A C   
1154 O O   . GLY A 160 ? 0.8370 0.6060 0.7309 -0.0071 -0.0390 -0.0333 159 GLY A O   
1155 N N   . VAL A 161 ? 0.6967 0.4833 0.6095 -0.0237 -0.0407 -0.0302 160 VAL A N   
1156 C CA  . VAL A 161 ? 0.6803 0.4644 0.5870 -0.0226 -0.0462 -0.0350 160 VAL A CA  
1157 C C   . VAL A 161 ? 0.7608 0.5248 0.6566 -0.0251 -0.0544 -0.0397 160 VAL A C   
1158 O O   . VAL A 161 ? 0.7663 0.5204 0.6495 -0.0189 -0.0584 -0.0451 160 VAL A O   
1159 C CB  . VAL A 161 ? 0.6433 0.4434 0.5624 -0.0302 -0.0471 -0.0339 160 VAL A CB  
1160 C CG1 . VAL A 161 ? 0.6730 0.4692 0.5862 -0.0311 -0.0548 -0.0389 160 VAL A CG1 
1161 C CG2 . VAL A 161 ? 0.6723 0.4897 0.5998 -0.0256 -0.0397 -0.0305 160 VAL A CG2 
1162 N N   . LEU A 162 ? 0.7019 0.4588 0.6017 -0.0343 -0.0571 -0.0377 161 LEU A N   
1163 C CA  . LEU A 162 ? 0.6572 0.3928 0.5471 -0.0374 -0.0651 -0.0417 161 LEU A CA  
1164 C C   . LEU A 162 ? 0.6772 0.3960 0.5525 -0.0261 -0.0646 -0.0446 161 LEU A C   
1165 O O   . LEU A 162 ? 0.7922 0.4941 0.6549 -0.0231 -0.0710 -0.0508 161 LEU A O   
1166 C CB  . LEU A 162 ? 0.7448 0.4767 0.6425 -0.0493 -0.0669 -0.0374 161 LEU A CB  
1167 C CG  . LEU A 162 ? 0.7619 0.4693 0.6501 -0.0528 -0.0745 -0.0399 161 LEU A CG  
1168 C CD1 . LEU A 162 ? 0.7142 0.4153 0.6005 -0.0598 -0.0838 -0.0451 161 LEU A CD1 
1169 C CD2 . LEU A 162 ? 0.7001 0.4043 0.5949 -0.0614 -0.0732 -0.0333 161 LEU A CD2 
1170 N N   . ALA A 163 ? 0.6752 0.3989 0.5524 -0.0196 -0.0572 -0.0406 162 ALA A N   
1171 C CA  . ALA A 163 ? 0.7244 0.4345 0.5895 -0.0081 -0.0560 -0.0428 162 ALA A CA  
1172 C C   . ALA A 163 ? 0.7632 0.4750 0.6184 0.0030  -0.0549 -0.0478 162 ALA A C   
1173 O O   . ALA A 163 ? 0.8026 0.4984 0.6436 0.0110  -0.0578 -0.0531 162 ALA A O   
1174 C CB  . ALA A 163 ? 0.6785 0.3958 0.5498 -0.0044 -0.0487 -0.0368 162 ALA A CB  
1175 N N   . TYR A 164 ? 0.7464 0.4772 0.6084 0.0039  -0.0507 -0.0460 163 TYR A N   
1176 C CA  . TYR A 164 ? 0.7397 0.4731 0.5920 0.0138  -0.0496 -0.0499 163 TYR A CA  
1177 C C   . TYR A 164 ? 0.7457 0.4658 0.5862 0.0124  -0.0588 -0.0573 163 TYR A C   
1178 O O   . TYR A 164 ? 0.7768 0.4856 0.6019 0.0218  -0.0605 -0.0629 163 TYR A O   
1179 C CB  . TYR A 164 ? 0.6960 0.4515 0.5589 0.0137  -0.0442 -0.0458 163 TYR A CB  
1180 C CG  . TYR A 164 ? 0.7038 0.4622 0.5574 0.0201  -0.0456 -0.0495 163 TYR A CG  
1181 C CD1 . TYR A 164 ? 0.7077 0.4646 0.5501 0.0327  -0.0414 -0.0508 163 TYR A CD1 
1182 C CD2 . TYR A 164 ? 0.7299 0.4930 0.5855 0.0138  -0.0513 -0.0515 163 TYR A CD2 
1183 C CE1 . TYR A 164 ? 0.7305 0.4902 0.5629 0.0389  -0.0425 -0.0538 163 TYR A CE1 
1184 C CE2 . TYR A 164 ? 0.7743 0.5400 0.6205 0.0199  -0.0532 -0.0547 163 TYR A CE2 
1185 C CZ  . TYR A 164 ? 0.8031 0.5668 0.6370 0.0324  -0.0487 -0.0558 163 TYR A CZ  
1186 O OH  . TYR A 164 ? 0.8966 0.6632 0.7198 0.0387  -0.0504 -0.0585 163 TYR A OH  
1187 N N   . TYR A 165 ? 0.7348 0.4563 0.5824 0.0005  -0.0649 -0.0577 164 TYR A N   
1188 C CA  . TYR A 165 ? 0.7319 0.4418 0.5698 -0.0024 -0.0747 -0.0648 164 TYR A CA  
1189 C C   . TYR A 165 ? 0.7893 0.4735 0.6137 -0.0004 -0.0805 -0.0703 164 TYR A C   
1190 O O   . TYR A 165 ? 0.7626 0.4338 0.5720 0.0044  -0.0866 -0.0779 164 TYR A O   
1191 C CB  . TYR A 165 ? 0.7151 0.4334 0.5662 -0.0164 -0.0798 -0.0631 164 TYR A CB  
1192 C CG  . TYR A 165 ? 0.8033 0.5164 0.6474 -0.0195 -0.0896 -0.0697 164 TYR A CG  
1193 C CD1 . TYR A 165 ? 0.8235 0.5437 0.6597 -0.0116 -0.0900 -0.0728 164 TYR A CD1 
1194 C CD2 . TYR A 165 ? 0.8436 0.5449 0.6891 -0.0306 -0.0988 -0.0724 164 TYR A CD2 
1195 C CE1 . TYR A 165 ? 0.8417 0.5576 0.6709 -0.0144 -0.0997 -0.0790 164 TYR A CE1 
1196 C CE2 . TYR A 165 ? 0.8221 0.5190 0.6618 -0.0340 -0.1086 -0.0787 164 TYR A CE2 
1197 C CZ  . TYR A 165 ? 0.8810 0.5854 0.7124 -0.0257 -0.1092 -0.0822 164 TYR A CZ  
1198 O OH  . TYR A 165 ? 1.0190 0.7195 0.8441 -0.0291 -0.1197 -0.0887 164 TYR A OH  
1199 N N   . VAL A 166 ? 0.7672 0.4432 0.5961 -0.0039 -0.0791 -0.0666 165 VAL A N   
1200 C CA  . VAL A 166 ? 0.7646 0.4149 0.5812 -0.0014 -0.0844 -0.0712 165 VAL A CA  
1201 C C   . VAL A 166 ? 0.8351 0.4782 0.6370 0.0148  -0.0804 -0.0752 165 VAL A C   
1202 O O   . VAL A 166 ? 0.8751 0.4992 0.6610 0.0207  -0.0861 -0.0832 165 VAL A O   
1203 C CB  . VAL A 166 ? 0.8070 0.4516 0.6326 -0.0088 -0.0834 -0.0650 165 VAL A CB  
1204 C CG1 . VAL A 166 ? 0.7330 0.3545 0.5463 -0.0007 -0.0847 -0.0676 165 VAL A CG1 
1205 C CG2 . VAL A 166 ? 0.7017 0.3433 0.5358 -0.0248 -0.0906 -0.0637 165 VAL A CG2 
1206 N N   . SER A 167 ? 0.8862 0.5446 0.6934 0.0225  -0.0705 -0.0699 166 SER A N   
1207 C CA  . SER A 167 ? 0.9177 0.5720 0.7130 0.0380  -0.0656 -0.0725 166 SER A CA  
1208 C C   . SER A 167 ? 0.9252 0.5830 0.7084 0.0459  -0.0663 -0.0784 166 SER A C   
1209 O O   . SER A 167 ? 0.9411 0.5866 0.7081 0.0574  -0.0666 -0.0845 166 SER A O   
1210 C CB  . SER A 167 ? 0.9210 0.5928 0.7274 0.0428  -0.0552 -0.0646 166 SER A CB  
1211 O OG  . SER A 167 ? 0.8603 0.5548 0.6774 0.0397  -0.0505 -0.0602 166 SER A OG  
1212 N N   . TYR A 168 ? 0.8508 0.5253 0.6410 0.0403  -0.0663 -0.0765 167 TYR A N   
1213 C CA  . TYR A 168 ? 0.8346 0.5133 0.6130 0.0475  -0.0672 -0.0812 167 TYR A CA  
1214 C C   . TYR A 168 ? 0.8381 0.4971 0.6013 0.0459  -0.0784 -0.0910 167 TYR A C   
1215 O O   . TYR A 168 ? 0.9227 0.5737 0.6681 0.0564  -0.0796 -0.0977 167 TYR A O   
1216 C CB  . TYR A 168 ? 0.8167 0.5183 0.6075 0.0421  -0.0647 -0.0760 167 TYR A CB  
1217 C CG  . TYR A 168 ? 0.8557 0.5580 0.6379 0.0410  -0.0718 -0.0813 167 TYR A CG  
1218 C CD1 . TYR A 168 ? 0.9123 0.6150 0.6784 0.0528  -0.0704 -0.0852 167 TYR A CD1 
1219 C CD2 . TYR A 168 ? 0.8646 0.5682 0.6548 0.0284  -0.0798 -0.0822 167 TYR A CD2 
1220 C CE1 . TYR A 168 ? 0.9217 0.6253 0.6790 0.0520  -0.0775 -0.0900 167 TYR A CE1 
1221 C CE2 . TYR A 168 ? 0.8945 0.5997 0.6774 0.0274  -0.0871 -0.0869 167 TYR A CE2 
1222 C CZ  . TYR A 168 ? 0.9230 0.6279 0.6890 0.0393  -0.0861 -0.0909 167 TYR A CZ  
1223 O OH  . TYR A 168 ? 0.9484 0.6552 0.7063 0.0385  -0.0938 -0.0956 167 TYR A OH  
1224 N N   . ARG A 169 ? 0.8449 0.4961 0.6147 0.0326  -0.0867 -0.0920 168 ARG A N   
1225 C CA  . ARG A 169 ? 0.9067 0.5385 0.6631 0.0297  -0.0983 -0.1014 168 ARG A CA  
1226 C C   . ARG A 169 ? 1.0002 0.6056 0.7413 0.0370  -0.1012 -0.1079 168 ARG A C   
1227 O O   . ARG A 169 ? 1.0201 0.6073 0.7459 0.0382  -0.1103 -0.1174 168 ARG A O   
1228 C CB  . ARG A 169 ? 0.8574 0.4892 0.6270 0.0126  -0.1063 -0.0999 168 ARG A CB  
1229 C CG  . ARG A 169 ? 0.8729 0.5225 0.6486 0.0069  -0.1095 -0.0995 168 ARG A CG  
1230 C CD  . ARG A 169 ? 0.8977 0.5343 0.6573 0.0078  -0.1206 -0.1096 168 ARG A CD  
1231 N NE  . ARG A 169 ? 0.9919 0.6174 0.7570 -0.0066 -0.1317 -0.1124 168 ARG A NE  
1232 C CZ  . ARG A 169 ? 1.0284 0.6684 0.8085 -0.0188 -0.1359 -0.1092 168 ARG A CZ  
1233 N NH1 . ARG A 169 ? 0.9238 0.5888 0.7144 -0.0182 -0.1305 -0.1037 168 ARG A NH1 
1234 N NH2 . ARG A 169 ? 1.1016 0.7309 0.8869 -0.0320 -0.1459 -0.1115 168 ARG A NH2 
1235 N N   . LEU A 170 ? 0.9458 0.5485 0.6905 0.0422  -0.0942 -0.1034 169 LEU A N   
1236 C CA  . LEU A 170 ? 0.9445 0.5229 0.6759 0.0505  -0.0960 -0.1088 169 LEU A CA  
1237 C C   . LEU A 170 ? 0.9455 0.5259 0.6638 0.0687  -0.0883 -0.1114 169 LEU A C   
1238 O O   . LEU A 170 ? 0.9150 0.4782 0.6141 0.0779  -0.0923 -0.1209 169 LEU A O   
1239 C CB  . LEU A 170 ? 0.9371 0.5101 0.6808 0.0446  -0.0941 -0.1018 169 LEU A CB  
1240 C CG  . LEU A 170 ? 0.9036 0.4554 0.6488 0.0320  -0.1043 -0.1036 169 LEU A CG  
1241 C CD1 . LEU A 170 ? 0.8245 0.3864 0.5802 0.0164  -0.1103 -0.1023 169 LEU A CD1 
1242 C CD2 . LEU A 170 ? 0.8375 0.3853 0.5930 0.0288  -0.1008 -0.0957 169 LEU A CD2 
1243 N N   . GLY A 171 ? 0.9160 0.5175 0.6445 0.0739  -0.0772 -0.1033 170 GLY A N   
1244 C CA  . GLY A 171 ? 0.8550 0.4612 0.5738 0.0906  -0.0688 -0.1043 170 GLY A CA  
1245 C C   . GLY A 171 ? 0.8644 0.4880 0.5775 0.0966  -0.0647 -0.1047 170 GLY A C   
1246 O O   . GLY A 171 ? 0.9308 0.5571 0.6325 0.1108  -0.0585 -0.1068 170 GLY A O   
1247 N N   . GLY A 172 ? 0.8374 0.4737 0.5587 0.0861  -0.0677 -0.1022 171 GLY A N   
1248 C CA  . GLY A 172 ? 0.8079 0.4598 0.5235 0.0911  -0.0648 -0.1022 171 GLY A CA  
1249 C C   . GLY A 172 ? 0.8746 0.5511 0.6035 0.0946  -0.0530 -0.0921 171 GLY A C   
1250 O O   . GLY A 172 ? 0.9194 0.6076 0.6676 0.0855  -0.0502 -0.0843 171 GLY A O   
1251 N N   . TYR A 173 ? 0.8421 0.5265 0.5605 0.1077  -0.0461 -0.0922 172 TYR A N   
1252 C CA  . TYR A 173 ? 0.7848 0.4927 0.5155 0.1109  -0.0350 -0.0824 172 TYR A CA  
1253 C C   . TYR A 173 ? 0.7991 0.5104 0.5433 0.1119  -0.0281 -0.0764 172 TYR A C   
1254 O O   . TYR A 173 ? 0.8248 0.5513 0.5877 0.1049  -0.0237 -0.0681 172 TYR A O   
1255 C CB  . TYR A 173 ? 0.7811 0.4961 0.4966 0.1248  -0.0290 -0.0835 172 TYR A CB  
1256 C CG  . TYR A 173 ? 0.7480 0.4874 0.4758 0.1268  -0.0185 -0.0731 172 TYR A CG  
1257 C CD1 . TYR A 173 ? 0.7566 0.5102 0.4968 0.1174  -0.0192 -0.0673 172 TYR A CD1 
1258 C CD2 . TYR A 173 ? 0.7402 0.4886 0.4681 0.1380  -0.0079 -0.0688 172 TYR A CD2 
1259 C CE1 . TYR A 173 ? 0.7464 0.5204 0.4979 0.1189  -0.0101 -0.0578 172 TYR A CE1 
1260 C CE2 . TYR A 173 ? 0.7243 0.4945 0.4643 0.1389  0.0014  -0.0589 172 TYR A CE2 
1261 C CZ  . TYR A 173 ? 0.7180 0.5000 0.4695 0.1292  0.0001  -0.0535 172 TYR A CZ  
1262 O OH  . TYR A 173 ? 0.7309 0.5328 0.4945 0.1299  0.0088  -0.0437 172 TYR A OH  
1263 N N   . GLU A 174 ? 0.8084 0.5054 0.5431 0.1209  -0.0275 -0.0808 173 GLU A N   
1264 C CA  . GLU A 174 ? 0.8040 0.5031 0.5513 0.1218  -0.0223 -0.0753 173 GLU A CA  
1265 C C   . GLU A 174 ? 0.7784 0.4722 0.5396 0.1073  -0.0280 -0.0727 173 GLU A C   
1266 O O   . GLU A 174 ? 0.7712 0.4747 0.5482 0.1039  -0.0234 -0.0654 173 GLU A O   
1267 C CB  . GLU A 174 ? 0.7585 0.4419 0.4923 0.1349  -0.0214 -0.0811 173 GLU A CB  
1268 C CG  . GLU A 174 ? 0.8130 0.5092 0.5411 0.1501  -0.0111 -0.0793 173 GLU A CG  
1269 C CD  . GLU A 174 ? 0.9155 0.5967 0.6310 0.1639  -0.0099 -0.0852 173 GLU A CD  
1270 O OE1 . GLU A 174 ? 0.9038 0.5776 0.6273 0.1632  -0.0105 -0.0834 173 GLU A OE1 
1271 O OE2 . GLU A 174 ? 0.9924 0.6694 0.6896 0.1761  -0.0082 -0.0915 173 GLU A OE2 
1272 N N   . GLY A 175 ? 0.8140 0.4929 0.5697 0.0987  -0.0381 -0.0785 174 GLY A N   
1273 C CA  . GLY A 175 ? 0.7786 0.4548 0.5479 0.0841  -0.0430 -0.0752 174 GLY A CA  
1274 C C   . GLY A 175 ? 0.7989 0.4969 0.5851 0.0746  -0.0399 -0.0679 174 GLY A C   
1275 O O   . GLY A 175 ? 0.8472 0.5517 0.6487 0.0664  -0.0383 -0.0618 174 GLY A O   
1276 N N   . ALA A 176 ? 0.7805 0.4899 0.5637 0.0761  -0.0390 -0.0684 175 ALA A N   
1277 C CA  . ALA A 176 ? 0.7134 0.4434 0.5124 0.0686  -0.0356 -0.0615 175 ALA A CA  
1278 C C   . ALA A 176 ? 0.7024 0.4485 0.5135 0.0726  -0.0253 -0.0534 175 ALA A C   
1279 O O   . ALA A 176 ? 0.7364 0.4955 0.5638 0.0645  -0.0228 -0.0473 175 ALA A O   
1280 C CB  . ALA A 176 ? 0.7394 0.4768 0.5312 0.0706  -0.0372 -0.0635 175 ALA A CB  
1281 N N   . LEU A 177 ? 0.6980 0.4439 0.5018 0.0849  -0.0194 -0.0535 176 LEU A N   
1282 C CA  . LEU A 177 ? 0.6813 0.4422 0.4977 0.0883  -0.0102 -0.0458 176 LEU A CA  
1283 C C   . LEU A 177 ? 0.7314 0.4879 0.5584 0.0824  -0.0111 -0.0431 176 LEU A C   
1284 O O   . LEU A 177 ? 0.7806 0.5506 0.6234 0.0770  -0.0071 -0.0365 176 LEU A O   
1285 C CB  . LEU A 177 ? 0.6691 0.4317 0.4754 0.1032  -0.0037 -0.0465 176 LEU A CB  
1286 C CG  . LEU A 177 ? 0.6304 0.3982 0.4243 0.1104  -0.0019 -0.0485 176 LEU A CG  
1287 C CD1 . LEU A 177 ? 0.6587 0.4322 0.4456 0.1248  0.0066  -0.0473 176 LEU A CD1 
1288 C CD2 . LEU A 177 ? 0.6248 0.4094 0.4295 0.1033  0.0000  -0.0427 176 LEU A CD2 
1289 N N   . LEU A 178 ? 0.7146 0.4514 0.5326 0.0835  -0.0167 -0.0482 177 LEU A N   
1290 C CA  . LEU A 178 ? 0.7091 0.4403 0.5359 0.0776  -0.0184 -0.0453 177 LEU A CA  
1291 C C   . LEU A 178 ? 0.7250 0.4614 0.5640 0.0627  -0.0218 -0.0422 177 LEU A C   
1292 O O   . LEU A 178 ? 0.7408 0.4843 0.5924 0.0572  -0.0196 -0.0366 177 LEU A O   
1293 C CB  . LEU A 178 ? 0.7330 0.4400 0.5468 0.0811  -0.0246 -0.0514 177 LEU A CB  
1294 C CG  . LEU A 178 ? 0.7211 0.4190 0.5417 0.0752  -0.0273 -0.0482 177 LEU A CG  
1295 C CD1 . LEU A 178 ? 0.7680 0.4739 0.5949 0.0836  -0.0205 -0.0431 177 LEU A CD1 
1296 C CD2 . LEU A 178 ? 0.6616 0.3330 0.4693 0.0749  -0.0358 -0.0547 177 LEU A CD2 
1297 N N   . GLY A 179 ? 0.6928 0.4267 0.5283 0.0563  -0.0272 -0.0459 178 GLY A N   
1298 C CA  . GLY A 179 ? 0.7090 0.4499 0.5567 0.0429  -0.0299 -0.0430 178 GLY A CA  
1299 C C   . GLY A 179 ? 0.7422 0.5052 0.6043 0.0408  -0.0230 -0.0366 178 GLY A C   
1300 O O   . GLY A 179 ? 0.7340 0.5044 0.6087 0.0319  -0.0223 -0.0324 178 GLY A O   
1301 N N   . LEU A 180 ? 0.7117 0.4850 0.5716 0.0489  -0.0179 -0.0358 179 LEU A N   
1302 C CA  . LEU A 180 ? 0.6916 0.4845 0.5652 0.0474  -0.0113 -0.0295 179 LEU A CA  
1303 C C   . LEU A 180 ? 0.7175 0.5162 0.6011 0.0479  -0.0062 -0.0244 179 LEU A C   
1304 O O   . LEU A 180 ? 0.6653 0.4764 0.5626 0.0417  -0.0033 -0.0199 179 LEU A O   
1305 C CB  . LEU A 180 ? 0.5845 0.3859 0.4528 0.0564  -0.0068 -0.0290 179 LEU A CB  
1306 C CG  . LEU A 180 ? 0.6546 0.4590 0.5194 0.0537  -0.0104 -0.0311 179 LEU A CG  
1307 C CD1 . LEU A 180 ? 0.7745 0.5931 0.6410 0.0598  -0.0040 -0.0268 179 LEU A CD1 
1308 C CD2 . LEU A 180 ? 0.6203 0.4287 0.4969 0.0413  -0.0143 -0.0301 179 LEU A CD2 
1309 N N   . ALA A 181 ? 0.6792 0.4692 0.5563 0.0554  -0.0053 -0.0253 180 ALA A N   
1310 C CA  . ALA A 181 ? 0.7121 0.5071 0.5985 0.0559  -0.0017 -0.0206 180 ALA A CA  
1311 C C   . ALA A 181 ? 0.7097 0.4974 0.6005 0.0461  -0.0064 -0.0199 180 ALA A C   
1312 O O   . ALA A 181 ? 0.6957 0.4917 0.5973 0.0426  -0.0039 -0.0152 180 ALA A O   
1313 C CB  . ALA A 181 ? 0.6470 0.4358 0.5253 0.0681  0.0008  -0.0216 180 ALA A CB  
1314 N N   . LEU A 182 ? 0.6996 0.4723 0.5824 0.0414  -0.0133 -0.0243 181 LEU A N   
1315 C CA  . LEU A 182 ? 0.7134 0.4784 0.5996 0.0320  -0.0176 -0.0230 181 LEU A CA  
1316 C C   . LEU A 182 ? 0.6785 0.4557 0.5767 0.0205  -0.0175 -0.0202 181 LEU A C   
1317 O O   . LEU A 182 ? 0.7529 0.5293 0.6565 0.0129  -0.0188 -0.0173 181 LEU A O   
1318 C CB  . LEU A 182 ? 0.6552 0.3991 0.5293 0.0304  -0.0252 -0.0283 181 LEU A CB  
1319 C CG  . LEU A 182 ? 0.6243 0.3511 0.4887 0.0384  -0.0270 -0.0300 181 LEU A CG  
1320 C CD1 . LEU A 182 ? 0.6560 0.3609 0.5081 0.0362  -0.0352 -0.0361 181 LEU A CD1 
1321 C CD2 . LEU A 182 ? 0.6785 0.4060 0.5503 0.0355  -0.0259 -0.0242 181 LEU A CD2 
1322 N N   . ILE A 183 ? 0.6862 0.4746 0.5880 0.0194  -0.0158 -0.0209 182 ILE A N   
1323 C CA  . ILE A 183 ? 0.7300 0.5304 0.6434 0.0095  -0.0153 -0.0186 182 ILE A CA  
1324 C C   . ILE A 183 ? 0.7348 0.5472 0.6596 0.0074  -0.0103 -0.0135 182 ILE A C   
1325 O O   . ILE A 183 ? 0.7213 0.5360 0.6524 -0.0013 -0.0114 -0.0117 182 ILE A O   
1326 C CB  . ILE A 183 ? 0.7287 0.5382 0.6434 0.0104  -0.0147 -0.0202 182 ILE A CB  
1327 C CG1 . ILE A 183 ? 0.6754 0.4735 0.5802 0.0088  -0.0216 -0.0255 182 ILE A CG1 
1328 C CG2 . ILE A 183 ? 0.6907 0.5153 0.6192 0.0029  -0.0123 -0.0172 182 ILE A CG2 
1329 C CD1 . ILE A 183 ? 0.6159 0.4194 0.5165 0.0138  -0.0215 -0.0276 182 ILE A CD1 
1330 N N   . PRO A 184 ? 0.6998 0.5204 0.6278 0.0146  -0.0049 -0.0110 183 PRO A N   
1331 C CA  . PRO A 184 ? 0.6885 0.5190 0.6268 0.0121  -0.0014 -0.0066 183 PRO A CA  
1332 C C   . PRO A 184 ? 0.6891 0.5106 0.6243 0.0121  -0.0034 -0.0051 183 PRO A C   
1333 O O   . PRO A 184 ? 0.6948 0.5230 0.6372 0.0081  -0.0021 -0.0018 183 PRO A O   
1334 C CB  . PRO A 184 ? 0.6456 0.4867 0.5880 0.0200  0.0043  -0.0045 183 PRO A CB  
1335 C CG  . PRO A 184 ? 0.7255 0.5651 0.6612 0.0250  0.0044  -0.0072 183 PRO A CG  
1336 C CD  . PRO A 184 ? 0.6772 0.5006 0.6008 0.0246  -0.0016 -0.0116 183 PRO A CD  
1337 N N   . ALA A 185 ? 0.6684 0.4745 0.5926 0.0168  -0.0069 -0.0075 184 ALA A N   
1338 C CA  . ALA A 185 ? 0.7124 0.5088 0.6331 0.0183  -0.0089 -0.0056 184 ALA A CA  
1339 C C   . ALA A 185 ? 0.7328 0.5199 0.6521 0.0085  -0.0138 -0.0050 184 ALA A C   
1340 O O   . ALA A 185 ? 0.7412 0.5268 0.6623 0.0061  -0.0144 -0.0012 184 ALA A O   
1341 C CB  . ALA A 185 ? 0.7104 0.4933 0.6198 0.0289  -0.0102 -0.0085 184 ALA A CB  
1342 N N   . LEU A 186 ? 0.7376 0.5192 0.6539 0.0024  -0.0174 -0.0081 185 LEU A N   
1343 C CA  . LEU A 186 ? 0.7579 0.5306 0.6731 -0.0074 -0.0220 -0.0071 185 LEU A CA  
1344 C C   . LEU A 186 ? 0.7825 0.5691 0.7082 -0.0169 -0.0198 -0.0034 185 LEU A C   
1345 O O   . LEU A 186 ? 0.8031 0.5850 0.7290 -0.0258 -0.0227 -0.0018 185 LEU A O   
1346 C CB  . LEU A 186 ? 0.6906 0.4532 0.5998 -0.0109 -0.0272 -0.0118 185 LEU A CB  
1347 C CG  . LEU A 186 ? 0.6437 0.3880 0.5400 -0.0026 -0.0309 -0.0163 185 LEU A CG  
1348 C CD1 . LEU A 186 ? 0.6921 0.4271 0.5829 -0.0073 -0.0369 -0.0213 185 LEU A CD1 
1349 C CD2 . LEU A 186 ? 0.6658 0.3947 0.5567 -0.0009 -0.0334 -0.0140 185 LEU A CD2 
1350 N N   . VAL A 187 ? 0.8535 0.6568 0.7876 -0.0153 -0.0145 -0.0021 186 VAL A N   
1351 C CA  . VAL A 187 ? 0.7854 0.6013 0.7284 -0.0231 -0.0121 0.0008  186 VAL A CA  
1352 C C   . VAL A 187 ? 0.8172 0.6307 0.7594 -0.0247 -0.0124 0.0052  186 VAL A C   
1353 O O   . VAL A 187 ? 0.7755 0.5970 0.7224 -0.0318 -0.0112 0.0077  186 VAL A O   
1354 C CB  . VAL A 187 ? 0.7539 0.5865 0.7058 -0.0205 -0.0070 0.0005  186 VAL A CB  
1355 C CG1 . VAL A 187 ? 0.8105 0.6476 0.7644 -0.0139 -0.0041 0.0029  186 VAL A CG1 
1356 C CG2 . VAL A 187 ? 0.7581 0.6028 0.7185 -0.0290 -0.0052 0.0011  186 VAL A CG2 
1357 N N   . VAL A 188 ? 0.7833 0.5861 0.7190 -0.0177 -0.0140 0.0063  187 VAL A N   
1358 C CA  . VAL A 188 ? 0.7303 0.5302 0.6647 -0.0183 -0.0149 0.0109  187 VAL A CA  
1359 C C   . VAL A 188 ? 0.7980 0.5877 0.7282 -0.0271 -0.0188 0.0135  187 VAL A C   
1360 O O   . VAL A 188 ? 0.8004 0.5916 0.7307 -0.0306 -0.0189 0.0182  187 VAL A O   
1361 C CB  . VAL A 188 ? 0.6859 0.4769 0.6150 -0.0075 -0.0158 0.0114  187 VAL A CB  
1362 C CG1 . VAL A 188 ? 0.6450 0.4155 0.5637 -0.0054 -0.0206 0.0091  187 VAL A CG1 
1363 C CG2 . VAL A 188 ? 0.7463 0.5400 0.6768 -0.0066 -0.0159 0.0165  187 VAL A CG2 
1364 N N   . ILE A 189 ? 0.8274 0.6073 0.7540 -0.0312 -0.0220 0.0109  188 ILE A N   
1365 C CA  . ILE A 189 ? 0.8488 0.6188 0.7723 -0.0406 -0.0257 0.0138  188 ILE A CA  
1366 C C   . ILE A 189 ? 0.8886 0.6740 0.8199 -0.0506 -0.0229 0.0158  188 ILE A C   
1367 O O   . ILE A 189 ? 0.8511 0.6370 0.7821 -0.0565 -0.0229 0.0210  188 ILE A O   
1368 C CB  . ILE A 189 ? 0.7244 0.4782 0.6419 -0.0419 -0.0309 0.0100  188 ILE A CB  
1369 C CG1 . ILE A 189 ? 0.7374 0.4730 0.6452 -0.0323 -0.0341 0.0085  188 ILE A CG1 
1370 C CG2 . ILE A 189 ? 0.7508 0.4984 0.6684 -0.0540 -0.0342 0.0132  188 ILE A CG2 
1371 C CD1 . ILE A 189 ? 0.8774 0.5959 0.7791 -0.0351 -0.0383 0.0132  188 ILE A CD1 
1372 N N   . PRO A 190 ? 0.7782 0.5766 0.7165 -0.0523 -0.0202 0.0123  189 PRO A N   
1373 C CA  . PRO A 190 ? 0.7440 0.5578 0.6900 -0.0606 -0.0170 0.0140  189 PRO A CA  
1374 C C   . PRO A 190 ? 0.7505 0.5765 0.6997 -0.0588 -0.0127 0.0163  189 PRO A C   
1375 O O   . PRO A 190 ? 0.7325 0.5666 0.6841 -0.0656 -0.0108 0.0193  189 PRO A O   
1376 C CB  . PRO A 190 ? 0.7230 0.5462 0.6754 -0.0607 -0.0156 0.0092  189 PRO A CB  
1377 C CG  . PRO A 190 ? 0.7437 0.5537 0.6899 -0.0552 -0.0196 0.0055  189 PRO A CG  
1378 C CD  . PRO A 190 ? 0.7401 0.5399 0.6793 -0.0471 -0.0202 0.0068  189 PRO A CD  
1379 N N   . ALA A 191 ? 0.7597 0.5878 0.7091 -0.0500 -0.0113 0.0151  190 ALA A N   
1380 C CA  . ALA A 191 ? 0.7160 0.5555 0.6688 -0.0486 -0.0081 0.0169  190 ALA A CA  
1381 C C   . ALA A 191 ? 0.7141 0.5478 0.6611 -0.0506 -0.0101 0.0223  190 ALA A C   
1382 O O   . ALA A 191 ? 0.7186 0.5619 0.6672 -0.0547 -0.0081 0.0246  190 ALA A O   
1383 C CB  . ALA A 191 ? 0.6633 0.5064 0.6187 -0.0391 -0.0065 0.0149  190 ALA A CB  
1384 N N   . ALA A 192 ? 0.7275 0.5451 0.6672 -0.0475 -0.0141 0.0244  191 ALA A N   
1385 C CA  . ALA A 192 ? 0.7307 0.5411 0.6643 -0.0492 -0.0164 0.0303  191 ALA A CA  
1386 C C   . ALA A 192 ? 0.7941 0.6036 0.7260 -0.0600 -0.0169 0.0339  191 ALA A C   
1387 O O   . ALA A 192 ? 0.8388 0.6528 0.7686 -0.0638 -0.0163 0.0387  191 ALA A O   
1388 C CB  . ALA A 192 ? 0.6805 0.4725 0.6070 -0.0424 -0.0207 0.0314  191 ALA A CB  
1389 N N   . ILE A 193 ? 0.7937 0.5983 0.7266 -0.0653 -0.0180 0.0319  192 ILE A N   
1390 C CA  . ILE A 193 ? 0.7384 0.5437 0.6713 -0.0762 -0.0180 0.0357  192 ILE A CA  
1391 C C   . ILE A 193 ? 0.7826 0.6081 0.7216 -0.0808 -0.0127 0.0357  192 ILE A C   
1392 O O   . ILE A 193 ? 0.8785 0.7081 0.8154 -0.0874 -0.0115 0.0408  192 ILE A O   
1393 C CB  . ILE A 193 ? 0.7412 0.5383 0.6755 -0.0807 -0.0208 0.0330  192 ILE A CB  
1394 C CG1 . ILE A 193 ? 0.7718 0.5466 0.6980 -0.0822 -0.0266 0.0364  192 ILE A CG1 
1395 C CG2 . ILE A 193 ? 0.7800 0.5902 0.7211 -0.0909 -0.0181 0.0338  192 ILE A CG2 
1396 C CD1 . ILE A 193 ? 0.7505 0.5116 0.6699 -0.0712 -0.0294 0.0352  192 ILE A CD1 
1397 N N   . MET A 194 ? 0.8358 0.6739 0.7817 -0.0772 -0.0095 0.0301  193 MET A N   
1398 C CA  . MET A 194 ? 0.7721 0.6284 0.7237 -0.0802 -0.0046 0.0291  193 MET A CA  
1399 C C   . MET A 194 ? 0.8790 0.7408 0.8274 -0.0775 -0.0033 0.0314  193 MET A C   
1400 O O   . MET A 194 ? 0.9773 0.8516 0.9270 -0.0813 0.0001  0.0317  193 MET A O   
1401 C CB  . MET A 194 ? 0.7571 0.6233 0.7169 -0.0765 -0.0020 0.0226  193 MET A CB  
1402 C CG  . MET A 194 ? 0.8455 0.7273 0.8126 -0.0820 0.0023  0.0207  193 MET A CG  
1403 S SD  . MET A 194 ? 1.0389 0.9198 1.0104 -0.0891 0.0011  0.0203  193 MET A SD  
1404 C CE  . MET A 194 ? 1.0083 0.8892 0.9757 -0.0992 0.0016  0.0275  193 MET A CE  
1405 N N   . LEU A 195 ? 0.8284 0.6816 0.7725 -0.0706 -0.0062 0.0327  194 LEU A N   
1406 C CA  . LEU A 195 ? 0.8417 0.7006 0.7833 -0.0678 -0.0060 0.0348  194 LEU A CA  
1407 C C   . LEU A 195 ? 0.8856 0.7405 0.8191 -0.0730 -0.0074 0.0418  194 LEU A C   
1408 O O   . LEU A 195 ? 0.8982 0.7630 0.8297 -0.0745 -0.0060 0.0434  194 LEU A O   
1409 C CB  . LEU A 195 ? 0.7777 0.6306 0.7191 -0.0583 -0.0085 0.0343  194 LEU A CB  
1410 C CG  . LEU A 195 ? 0.7907 0.6536 0.7338 -0.0541 -0.0080 0.0343  194 LEU A CG  
1411 C CD1 . LEU A 195 ? 0.7104 0.5864 0.6627 -0.0524 -0.0045 0.0283  194 LEU A CD1 
1412 C CD2 . LEU A 195 ? 0.7054 0.5598 0.6460 -0.0460 -0.0115 0.0368  194 LEU A CD2 
1413 N N   . ILE A 196 ? 0.8742 0.7144 0.8025 -0.0759 -0.0106 0.0462  195 ILE A N   
1414 C CA  . ILE A 196 ? 0.9223 0.7572 0.8426 -0.0810 -0.0121 0.0540  195 ILE A CA  
1415 C C   . ILE A 196 ? 0.9209 0.7620 0.8417 -0.0915 -0.0091 0.0566  195 ILE A C   
1416 O O   . ILE A 196 ? 0.9385 0.7815 0.8532 -0.0963 -0.0085 0.0629  195 ILE A O   
1417 C CB  . ILE A 196 ? 0.9582 0.7719 0.8721 -0.0784 -0.0176 0.0584  195 ILE A CB  
1418 C CG1 . ILE A 196 ? 0.8766 0.6792 0.7908 -0.0852 -0.0190 0.0592  195 ILE A CG1 
1419 C CG2 . ILE A 196 ? 0.9845 0.7924 0.9000 -0.0675 -0.0198 0.0543  195 ILE A CG2 
1420 C CD1 . ILE A 196 ? 0.8598 0.6394 0.7672 -0.0830 -0.0247 0.0630  195 ILE A CD1 
1421 N N   . LYS A 197 ? 0.9263 0.7715 0.8543 -0.0950 -0.0071 0.0521  196 LYS A N   
1422 C CA  . LYS A 197 ? 0.9581 0.8118 0.8885 -0.1047 -0.0038 0.0546  196 LYS A CA  
1423 C C   . LYS A 197 ? 0.9336 0.8071 0.8659 -0.1058 0.0018  0.0527  196 LYS A C   
1424 O O   . LYS A 197 ? 1.0288 0.9088 0.9569 -0.1118 0.0044  0.0578  196 LYS A O   
1425 C CB  . LYS A 197 ? 0.9902 0.8433 0.9286 -0.1078 -0.0039 0.0504  196 LYS A CB  
1426 C CG  . LYS A 197 ? 0.9834 0.8459 0.9261 -0.1181 -0.0007 0.0534  196 LYS A CG  
1427 C CD  . LYS A 197 ? 0.9728 0.8390 0.9253 -0.1201 -0.0007 0.0481  196 LYS A CD  
1428 C CE  . LYS A 197 ? 0.9170 0.7640 0.8678 -0.1210 -0.0071 0.0484  196 LYS A CE  
1429 N NZ  . LYS A 197 ? 0.8742 0.7256 0.8342 -0.1245 -0.0078 0.0441  196 LYS A NZ  
1430 N N   . ARG A 198 ? 0.9185 0.8014 0.8567 -0.0999 0.0038  0.0453  197 ARG A N   
1431 C CA  . ARG A 198 ? 0.9586 0.8584 0.8981 -0.0999 0.0085  0.0423  197 ARG A CA  
1432 C C   . ARG A 198 ? 0.9989 0.8995 0.9300 -0.0971 0.0072  0.0452  197 ARG A C   
1433 O O   . ARG A 198 ? 1.0715 0.9849 1.0007 -0.0983 0.0106  0.0437  197 ARG A O   
1434 C CB  . ARG A 198 ? 0.9995 0.9070 0.9482 -0.0946 0.0103  0.0339  197 ARG A CB  
1435 C CG  . ARG A 198 ? 0.8911 0.7973 0.8480 -0.0961 0.0105  0.0309  197 ARG A CG  
1436 C CD  . ARG A 198 ? 0.7860 0.6995 0.7514 -0.0905 0.0124  0.0234  197 ARG A CD  
1437 N NE  . ARG A 198 ? 0.7629 0.6920 0.7339 -0.0929 0.0175  0.0200  197 ARG A NE  
1438 C CZ  . ARG A 198 ? 0.7915 0.7274 0.7685 -0.0977 0.0199  0.0195  197 ARG A CZ  
1439 N NH1 . ARG A 198 ? 0.8181 0.7465 0.7965 -0.1014 0.0172  0.0222  197 ARG A NH1 
1440 N NH2 . ARG A 198 ? 0.7898 0.7404 0.7718 -0.0985 0.0249  0.0160  197 ARG A NH2 
1441 N N   . GLY A 199 ? 0.9761 0.8635 0.9018 -0.0931 0.0023  0.0490  198 GLY A N   
1442 C CA  . GLY A 199 ? 0.9948 0.8828 0.9125 -0.0905 0.0002  0.0527  198 GLY A CA  
1443 C C   . GLY A 199 ? 1.0054 0.9052 0.9261 -0.0854 0.0011  0.0466  198 GLY A C   
1444 O O   . GLY A 199 ? 1.0946 1.0025 1.0094 -0.0863 0.0016  0.0478  198 GLY A O   
1445 N N   . VAL A 200 ? 1.0180 0.9187 0.9476 -0.0803 0.0013  0.0402  199 VAL A N   
1446 C CA  . VAL A 200 ? 1.0424 0.9535 0.9762 -0.0762 0.0020  0.0345  199 VAL A CA  
1447 C C   . VAL A 200 ? 0.9124 0.8209 0.8422 -0.0712 -0.0026 0.0375  199 VAL A C   
1448 O O   . VAL A 200 ? 0.9511 0.8688 0.8792 -0.0706 -0.0031 0.0357  199 VAL A O   
1449 C CB  . VAL A 200 ? 1.0562 0.9689 1.0010 -0.0725 0.0036  0.0280  199 VAL A CB  
1450 C CG1 . VAL A 200 ? 1.1221 1.0405 1.0715 -0.0771 0.0081  0.0247  199 VAL A CG1 
1451 C CG2 . VAL A 200 ? 0.9712 0.8713 0.9177 -0.0678 0.0005  0.0297  199 VAL A CG2 
1452 N N   . ILE A 201 ? 0.8281 0.7241 0.7560 -0.0675 -0.0064 0.0418  200 ILE A N   
1453 C CA  . ILE A 201 ? 0.8157 0.7089 0.7401 -0.0623 -0.0111 0.0456  200 ILE A CA  
1454 C C   . ILE A 201 ? 0.8321 0.7102 0.7488 -0.0622 -0.0145 0.0533  200 ILE A C   
1455 O O   . ILE A 201 ? 0.8734 0.7410 0.7907 -0.0635 -0.0140 0.0538  200 ILE A O   
1456 C CB  . ILE A 201 ? 0.7781 0.6728 0.7116 -0.0546 -0.0123 0.0417  200 ILE A CB  
1457 C CG1 . ILE A 201 ? 0.8044 0.6895 0.7426 -0.0519 -0.0113 0.0399  200 ILE A CG1 
1458 C CG2 . ILE A 201 ? 0.8404 0.7494 0.7812 -0.0549 -0.0100 0.0351  200 ILE A CG2 
1459 C CD1 . ILE A 201 ? 0.7910 0.6738 0.7348 -0.0433 -0.0131 0.0391  200 ILE A CD1 
1460 N N   . PRO A 202 ? 0.8224 0.6984 0.7316 -0.0607 -0.0183 0.0594  201 PRO A N   
1461 C CA  . PRO A 202 ? 0.7742 0.6338 0.6767 -0.0592 -0.0222 0.0668  201 PRO A CA  
1462 C C   . PRO A 202 ? 0.7169 0.5669 0.6248 -0.0507 -0.0245 0.0651  201 PRO A C   
1463 O O   . PRO A 202 ? 0.7366 0.5944 0.6523 -0.0449 -0.0243 0.0604  201 PRO A O   
1464 C CB  . PRO A 202 ? 0.7315 0.5939 0.6255 -0.0585 -0.0259 0.0732  201 PRO A CB  
1465 C CG  . PRO A 202 ? 0.7884 0.6682 0.6821 -0.0627 -0.0230 0.0693  201 PRO A CG  
1466 C CD  . PRO A 202 ? 0.7644 0.6523 0.6697 -0.0611 -0.0196 0.0600  201 PRO A CD  
1467 N N   . LEU A 203 ? 0.6972 0.5298 0.6007 -0.0500 -0.0268 0.0691  202 LEU A N   
1468 C CA  . LEU A 203 ? 0.7242 0.5461 0.6311 -0.0414 -0.0289 0.0672  202 LEU A CA  
1469 C C   . LEU A 203 ? 0.7384 0.5621 0.6458 -0.0324 -0.0325 0.0699  202 LEU A C   
1470 O O   . LEU A 203 ? 0.7951 0.6181 0.7086 -0.0241 -0.0328 0.0666  202 LEU A O   
1471 C CB  . LEU A 203 ? 0.7724 0.5737 0.6734 -0.0430 -0.0311 0.0704  202 LEU A CB  
1472 C CG  . LEU A 203 ? 0.7825 0.5701 0.6849 -0.0340 -0.0332 0.0678  202 LEU A CG  
1473 C CD1 . LEU A 203 ? 0.8088 0.5875 0.7121 -0.0378 -0.0318 0.0633  202 LEU A CD1 
1474 C CD2 . LEU A 203 ? 0.8234 0.5944 0.7184 -0.0289 -0.0385 0.0747  202 LEU A CD2 
1475 N N   . SER A 204 ? 0.7300 0.5569 0.6314 -0.0338 -0.0354 0.0760  203 SER A N   
1476 C CA  . SER A 204 ? 0.7303 0.5609 0.6331 -0.0254 -0.0395 0.0789  203 SER A CA  
1477 C C   . SER A 204 ? 0.7071 0.5559 0.6207 -0.0220 -0.0378 0.0728  203 SER A C   
1478 O O   . SER A 204 ? 0.7270 0.5797 0.6455 -0.0139 -0.0405 0.0738  203 SER A O   
1479 C CB  . SER A 204 ? 0.6797 0.5112 0.5730 -0.0282 -0.0432 0.0868  203 SER A CB  
1480 O OG  . SER A 204 ? 0.6592 0.5054 0.5508 -0.0360 -0.0407 0.0851  203 SER A OG  
1481 N N   . TYR A 205 ? 0.7088 0.5686 0.6267 -0.0280 -0.0334 0.0668  204 TYR A N   
1482 C CA  . TYR A 205 ? 0.7177 0.5932 0.6464 -0.0255 -0.0318 0.0610  204 TYR A CA  
1483 C C   . TYR A 205 ? 0.7097 0.5822 0.6471 -0.0178 -0.0304 0.0578  204 TYR A C   
1484 O O   . TYR A 205 ? 0.6828 0.5665 0.6296 -0.0130 -0.0305 0.0557  204 TYR A O   
1485 C CB  . TYR A 205 ? 0.6745 0.5600 0.6054 -0.0333 -0.0273 0.0553  204 TYR A CB  
1486 C CG  . TYR A 205 ? 0.7369 0.6317 0.6614 -0.0392 -0.0283 0.0566  204 TYR A CG  
1487 C CD1 . TYR A 205 ? 0.7501 0.6394 0.6634 -0.0411 -0.0316 0.0638  204 TYR A CD1 
1488 C CD2 . TYR A 205 ? 0.7243 0.6331 0.6536 -0.0428 -0.0261 0.0505  204 TYR A CD2 
1489 C CE1 . TYR A 205 ? 0.7108 0.6091 0.6168 -0.0461 -0.0324 0.0650  204 TYR A CE1 
1490 C CE2 . TYR A 205 ? 0.7203 0.6373 0.6424 -0.0476 -0.0270 0.0508  204 TYR A CE2 
1491 C CZ  . TYR A 205 ? 0.6781 0.5904 0.5882 -0.0492 -0.0300 0.0581  204 TYR A CZ  
1492 O OH  . TYR A 205 ? 0.6999 0.6209 0.6015 -0.0537 -0.0308 0.0584  204 TYR A OH  
1493 N N   . LEU A 206 ? 0.7035 0.5616 0.6380 -0.0165 -0.0292 0.0574  205 LEU A N   
1494 C CA  . LEU A 206 ? 0.7449 0.5991 0.6854 -0.0087 -0.0276 0.0543  205 LEU A CA  
1495 C C   . LEU A 206 ? 0.7368 0.5862 0.6776 0.0015  -0.0312 0.0583  205 LEU A C   
1496 O O   . LEU A 206 ? 0.7147 0.5621 0.6603 0.0093  -0.0296 0.0558  205 LEU A O   
1497 C CB  . LEU A 206 ? 0.6768 0.5166 0.6127 -0.0109 -0.0259 0.0520  205 LEU A CB  
1498 C CG  . LEU A 206 ? 0.6418 0.4872 0.5798 -0.0194 -0.0219 0.0473  205 LEU A CG  
1499 C CD1 . LEU A 206 ? 0.6255 0.4560 0.5579 -0.0227 -0.0217 0.0465  205 LEU A CD1 
1500 C CD2 . LEU A 206 ? 0.5942 0.4522 0.5426 -0.0167 -0.0181 0.0417  205 LEU A CD2 
1501 N N   . LYS A 207 ? 0.7585 0.6063 0.6941 0.0022  -0.0357 0.0644  206 LYS A N   
1502 C CA  . LYS A 207 ? 0.7601 0.6043 0.6968 0.0126  -0.0394 0.0685  206 LYS A CA  
1503 C C   . LYS A 207 ? 0.7726 0.6345 0.7223 0.0186  -0.0382 0.0661  206 LYS A C   
1504 O O   . LYS A 207 ? 0.8274 0.7053 0.7829 0.0136  -0.0377 0.0644  206 LYS A O   
1505 C CB  . LYS A 207 ? 0.8199 0.6608 0.7487 0.0115  -0.0448 0.0761  206 LYS A CB  
1506 C CG  . LYS A 207 ? 0.8872 0.7158 0.8131 0.0217  -0.0491 0.0813  206 LYS A CG  
1507 C CD  . LYS A 207 ? 0.8909 0.7290 0.8175 0.0250  -0.0544 0.0875  206 LYS A CD  
1508 C CE  . LYS A 207 ? 0.9354 0.7908 0.8757 0.0331  -0.0542 0.0855  206 LYS A CE  
1509 N NZ  . LYS A 207 ? 1.0533 0.9005 0.9978 0.0448  -0.0530 0.0844  206 LYS A NZ  
1510 N N   . PRO A 208 ? 0.7909 0.6508 0.7457 0.0291  -0.0376 0.0658  207 PRO A N   
1511 C CA  . PRO A 208 ? 0.7793 0.6573 0.7480 0.0342  -0.0356 0.0639  207 PRO A CA  
1512 C C   . PRO A 208 ? 0.7738 0.6664 0.7481 0.0350  -0.0401 0.0681  207 PRO A C   
1513 O O   . PRO A 208 ? 0.7824 0.6702 0.7527 0.0401  -0.0450 0.0737  207 PRO A O   
1514 C CB  . PRO A 208 ? 0.7427 0.6129 0.7131 0.0461  -0.0339 0.0635  207 PRO A CB  
1515 C CG  . PRO A 208 ? 0.7106 0.5583 0.6683 0.0449  -0.0339 0.0622  207 PRO A CG  
1516 C CD  . PRO A 208 ? 0.8100 0.6506 0.7583 0.0364  -0.0380 0.0663  207 PRO A CD  
1517 N N   . SER A 209 ? 0.8068 0.7169 0.7902 0.0296  -0.0390 0.0654  208 SER A N   
1518 C CA  . SER A 209 ? 0.7676 0.6944 0.7585 0.0296  -0.0434 0.0680  208 SER A CA  
1519 C C   . SER A 209 ? 0.7325 0.6767 0.7398 0.0310  -0.0402 0.0648  208 SER A C   
1520 O O   . SER A 209 ? 0.7505 0.6934 0.7618 0.0315  -0.0345 0.0608  208 SER A O   
1521 C CB  . SER A 209 ? 0.7109 0.6406 0.6943 0.0193  -0.0464 0.0679  208 SER A CB  
1522 O OG  . SER A 209 ? 0.7264 0.6744 0.7187 0.0177  -0.0500 0.0680  208 SER A OG  
1523 N N   . TRP A 210 ? 0.6809 0.6417 0.6978 0.0312  -0.0443 0.0667  209 TRP A N   
1524 C CA  . TRP A 210 ? 0.6487 0.6270 0.6826 0.0319  -0.0419 0.0647  209 TRP A CA  
1525 C C   . TRP A 210 ? 0.5910 0.5847 0.6310 0.0246  -0.0467 0.0639  209 TRP A C   
1526 O O   . TRP A 210 ? 0.6201 0.6202 0.6605 0.0266  -0.0533 0.0680  209 TRP A O   
1527 C CB  . TRP A 210 ? 0.6201 0.6049 0.6645 0.0437  -0.0415 0.0686  209 TRP A CB  
1528 C CG  . TRP A 210 ? 0.6181 0.6175 0.6789 0.0450  -0.0365 0.0667  209 TRP A CG  
1529 C CD1 . TRP A 210 ? 0.6404 0.6604 0.7179 0.0449  -0.0384 0.0684  209 TRP A CD1 
1530 C CD2 . TRP A 210 ? 0.6599 0.6549 0.7221 0.0461  -0.0289 0.0633  209 TRP A CD2 
1531 N NE1 . TRP A 210 ? 0.6841 0.7126 0.7737 0.0457  -0.0320 0.0667  209 TRP A NE1 
1532 C CE2 . TRP A 210 ? 0.6898 0.7032 0.7697 0.0468  -0.0260 0.0636  209 TRP A CE2 
1533 C CE3 . TRP A 210 ? 0.6784 0.6562 0.7288 0.0465  -0.0244 0.0602  209 TRP A CE3 
1534 C CZ2 . TRP A 210 ? 0.6317 0.6464 0.7168 0.0481  -0.0186 0.0615  209 TRP A CZ2 
1535 C CZ3 . TRP A 210 ? 0.6255 0.6048 0.6809 0.0480  -0.0176 0.0575  209 TRP A CZ3 
1536 C CH2 . TRP A 210 ? 0.5594 0.5568 0.6315 0.0490  -0.0146 0.0584  209 TRP A CH2 
1537 N N   . ASP A 211 ? 0.5650 0.5641 0.6096 0.0165  -0.0439 0.0585  210 ASP A N   
1538 C CA  . ASP A 211 ? 0.5242 0.5379 0.5763 0.0094  -0.0480 0.0563  210 ASP A CA  
1539 C C   . ASP A 211 ? 0.5571 0.5847 0.6281 0.0100  -0.0449 0.0550  210 ASP A C   
1540 O O   . ASP A 211 ? 0.5704 0.5946 0.6443 0.0082  -0.0386 0.0517  210 ASP A O   
1541 C CB  . ASP A 211 ? 0.5568 0.5648 0.5986 -0.0006 -0.0475 0.0508  210 ASP A CB  
1542 C CG  . ASP A 211 ? 0.6066 0.6267 0.6513 -0.0073 -0.0535 0.0484  210 ASP A CG  
1543 O OD1 . ASP A 211 ? 0.5806 0.6133 0.6402 -0.0095 -0.0539 0.0462  210 ASP A OD1 
1544 O OD2 . ASP A 211 ? 0.6501 0.6670 0.6819 -0.0105 -0.0580 0.0489  210 ASP A OD2 
1545 N N   . ASN A 212 ? 0.5338 0.5775 0.6180 0.0122  -0.0496 0.0581  211 ASN A N   
1546 C CA  . ASN A 212 ? 0.5080 0.5664 0.6119 0.0132  -0.0467 0.0585  211 ASN A CA  
1547 C C   . ASN A 212 ? 0.5614 0.6222 0.6705 0.0033  -0.0444 0.0526  211 ASN A C   
1548 O O   . ASN A 212 ? 0.5903 0.6515 0.7070 0.0035  -0.0378 0.0516  211 ASN A O   
1549 C CB  . ASN A 212 ? 0.5723 0.6488 0.6898 0.0159  -0.0533 0.0629  211 ASN A CB  
1550 C CG  . ASN A 212 ? 0.6354 0.7107 0.7510 0.0275  -0.0546 0.0692  211 ASN A CG  
1551 O OD1 . ASN A 212 ? 0.6234 0.6845 0.7293 0.0340  -0.0499 0.0700  211 ASN A OD1 
1552 N ND2 . ASN A 212 ? 0.7477 0.8378 0.8728 0.0305  -0.0615 0.0734  211 ASN A ND2 
1553 N N   . GLY A 213 ? 0.5388 0.6008 0.6431 -0.0051 -0.0499 0.0487  212 GLY A N   
1554 C CA  . GLY A 213 ? 0.5383 0.6014 0.6471 -0.0141 -0.0482 0.0426  212 GLY A CA  
1555 C C   . GLY A 213 ? 0.5461 0.5945 0.6452 -0.0157 -0.0410 0.0388  212 GLY A C   
1556 O O   . GLY A 213 ? 0.5655 0.6144 0.6719 -0.0201 -0.0372 0.0353  212 GLY A O   
1557 N N   . LEU A 214 ? 0.5469 0.5819 0.6301 -0.0123 -0.0394 0.0397  213 LEU A N   
1558 C CA  . LEU A 214 ? 0.5788 0.6005 0.6532 -0.0137 -0.0330 0.0364  213 LEU A CA  
1559 C C   . LEU A 214 ? 0.5549 0.5736 0.6345 -0.0069 -0.0265 0.0389  213 LEU A C   
1560 O O   . LEU A 214 ? 0.5677 0.5802 0.6464 -0.0087 -0.0210 0.0360  213 LEU A O   
1561 C CB  . LEU A 214 ? 0.5989 0.6078 0.6545 -0.0142 -0.0343 0.0363  213 LEU A CB  
1562 C CG  . LEU A 214 ? 0.5719 0.5790 0.6180 -0.0225 -0.0368 0.0314  213 LEU A CG  
1563 C CD1 . LEU A 214 ? 0.6178 0.6366 0.6672 -0.0254 -0.0444 0.0313  213 LEU A CD1 
1564 C CD2 . LEU A 214 ? 0.5666 0.5610 0.5951 -0.0227 -0.0363 0.0325  213 LEU A CD2 
1565 N N   . ALA A 215 ? 0.5559 0.5793 0.6406 0.0013  -0.0270 0.0443  214 ALA A N   
1566 C CA  . ALA A 215 ? 0.5405 0.5619 0.6294 0.0087  -0.0207 0.0465  214 ALA A CA  
1567 C C   . ALA A 215 ? 0.5442 0.5773 0.6495 0.0068  -0.0167 0.0462  214 ALA A C   
1568 O O   . ALA A 215 ? 0.5255 0.5546 0.6315 0.0092  -0.0103 0.0458  214 ALA A O   
1569 C CB  . ALA A 215 ? 0.4785 0.5023 0.5686 0.0189  -0.0222 0.0520  214 ALA A CB  
1570 N N   . GLY A 216 ? 0.5305 0.5778 0.6489 0.0021  -0.0207 0.0466  215 GLY A N   
1571 C CA  . GLY A 216 ? 0.4833 0.5412 0.6181 -0.0012 -0.0174 0.0468  215 GLY A CA  
1572 C C   . GLY A 216 ? 0.5257 0.5757 0.6574 -0.0088 -0.0146 0.0414  215 GLY A C   
1573 O O   . GLY A 216 ? 0.5685 0.6205 0.7085 -0.0092 -0.0092 0.0421  215 GLY A O   
1574 N N   . GLN A 217 ? 0.5841 0.6255 0.7039 -0.0145 -0.0181 0.0364  216 GLN A N   
1575 C CA  . GLN A 217 ? 0.5797 0.6133 0.6962 -0.0209 -0.0154 0.0309  216 GLN A CA  
1576 C C   . GLN A 217 ? 0.5881 0.6101 0.6960 -0.0169 -0.0088 0.0308  216 GLN A C   
1577 O O   . GLN A 217 ? 0.6123 0.6322 0.7244 -0.0189 -0.0043 0.0292  216 GLN A O   
1578 C CB  . GLN A 217 ? 0.6368 0.6653 0.7422 -0.0272 -0.0204 0.0256  216 GLN A CB  
1579 C CG  . GLN A 217 ? 0.6294 0.6672 0.7441 -0.0343 -0.0259 0.0225  216 GLN A CG  
1580 C CD  . GLN A 217 ? 0.7195 0.7561 0.8225 -0.0377 -0.0324 0.0193  216 GLN A CD  
1581 O OE1 . GLN A 217 ? 0.7411 0.7693 0.8289 -0.0355 -0.0322 0.0195  216 GLN A OE1 
1582 N NE2 . GLN A 217 ? 0.7758 0.8209 0.8856 -0.0432 -0.0385 0.0165  216 GLN A NE2 
1583 N N   . LEU A 218 ? 0.5462 0.5601 0.6418 -0.0112 -0.0086 0.0324  217 LEU A N   
1584 C CA  . LEU A 218 ? 0.5633 0.5666 0.6512 -0.0069 -0.0031 0.0324  217 LEU A CA  
1585 C C   . LEU A 218 ? 0.5504 0.5597 0.6483 -0.0007 0.0020  0.0363  217 LEU A C   
1586 O O   . LEU A 218 ? 0.5522 0.5554 0.6471 0.0012  0.0071  0.0356  217 LEU A O   
1587 C CB  . LEU A 218 ? 0.5590 0.5516 0.6323 -0.0025 -0.0047 0.0334  217 LEU A CB  
1588 C CG  . LEU A 218 ? 0.5138 0.4988 0.5748 -0.0083 -0.0084 0.0303  217 LEU A CG  
1589 C CD1 . LEU A 218 ? 0.5280 0.5048 0.5775 -0.0039 -0.0112 0.0333  217 LEU A CD1 
1590 C CD2 . LEU A 218 ? 0.5279 0.5044 0.5828 -0.0127 -0.0048 0.0258  217 LEU A CD2 
1591 N N   . SER A 219 ? 0.4821 0.5043 0.5919 0.0025  0.0008  0.0406  218 SER A N   
1592 C CA  . SER A 219 ? 0.5273 0.5580 0.6482 0.0079  0.0062  0.0448  218 SER A CA  
1593 C C   . SER A 219 ? 0.5481 0.5831 0.6793 0.0019  0.0095  0.0441  218 SER A C   
1594 O O   . SER A 219 ? 0.5868 0.6232 0.7216 0.0056  0.0156  0.0466  218 SER A O   
1595 C CB  . SER A 219 ? 0.4664 0.5120 0.5994 0.0123  0.0040  0.0499  218 SER A CB  
1596 O OG  . SER A 219 ? 0.5540 0.5948 0.6777 0.0198  0.0017  0.0514  218 SER A OG  
1597 N N   . LYS A 220 ? 0.5409 0.5776 0.6765 -0.0071 0.0055  0.0407  219 LYS A N   
1598 C CA  . LYS A 220 ? 0.5359 0.5737 0.6802 -0.0130 0.0082  0.0395  219 LYS A CA  
1599 C C   . LYS A 220 ? 0.5175 0.5421 0.6508 -0.0128 0.0125  0.0364  219 LYS A C   
1600 O O   . LYS A 220 ? 0.5226 0.5475 0.6618 -0.0133 0.0171  0.0378  219 LYS A O   
1601 C CB  . LYS A 220 ? 0.5585 0.5994 0.7087 -0.0223 0.0024  0.0355  219 LYS A CB  
1602 C CG  . LYS A 220 ? 0.6259 0.6818 0.7897 -0.0237 -0.0025 0.0386  219 LYS A CG  
1603 C CD  . LYS A 220 ? 0.5928 0.6612 0.7743 -0.0220 0.0017  0.0450  219 LYS A CD  
1604 C CE  . LYS A 220 ? 0.5700 0.6547 0.7641 -0.0204 -0.0022 0.0495  219 LYS A CE  
1605 N NZ  . LYS A 220 ? 0.4513 0.5380 0.6396 -0.0098 -0.0003 0.0535  219 LYS A NZ  
1606 N N   . PHE A 221 ? 0.5212 0.5346 0.6390 -0.0121 0.0109  0.0326  220 PHE A N   
1607 C CA  . PHE A 221 ? 0.5497 0.5515 0.6571 -0.0112 0.0145  0.0301  220 PHE A CA  
1608 C C   . PHE A 221 ? 0.5591 0.5590 0.6632 -0.0027 0.0195  0.0338  220 PHE A C   
1609 O O   . PHE A 221 ? 0.5567 0.5508 0.6570 -0.0016 0.0234  0.0331  220 PHE A O   
1610 C CB  . PHE A 221 ? 0.5577 0.5493 0.6506 -0.0133 0.0114  0.0256  220 PHE A CB  
1611 C CG  . PHE A 221 ? 0.5920 0.5830 0.6853 -0.0214 0.0083  0.0206  220 PHE A CG  
1612 C CD1 . PHE A 221 ? 0.5588 0.5559 0.6548 -0.0250 0.0030  0.0197  220 PHE A CD1 
1613 C CD2 . PHE A 221 ? 0.5908 0.5756 0.6815 -0.0248 0.0105  0.0166  220 PHE A CD2 
1614 C CE1 . PHE A 221 ? 0.5725 0.5687 0.6674 -0.0319 0.0002  0.0143  220 PHE A CE1 
1615 C CE2 . PHE A 221 ? 0.5993 0.5834 0.6898 -0.0313 0.0080  0.0113  220 PHE A CE2 
1616 C CZ  . PHE A 221 ? 0.5860 0.5756 0.6782 -0.0349 0.0029  0.0100  220 PHE A CZ  
1617 N N   . THR A 222 ? 0.5700 0.5749 0.6750 0.0037  0.0191  0.0376  221 THR A N   
1618 C CA  . THR A 222 ? 0.5606 0.5652 0.6631 0.0126  0.0241  0.0409  221 THR A CA  
1619 C C   . THR A 222 ? 0.5827 0.5970 0.6977 0.0130  0.0294  0.0448  221 THR A C   
1620 O O   . THR A 222 ? 0.6128 0.6233 0.7232 0.0172  0.0344  0.0458  221 THR A O   
1621 C CB  . THR A 222 ? 0.5597 0.5684 0.6617 0.0200  0.0226  0.0439  221 THR A CB  
1622 O OG1 . THR A 222 ? 0.5860 0.5826 0.6739 0.0207  0.0185  0.0410  221 THR A OG1 
1623 C CG2 . THR A 222 ? 0.5157 0.5270 0.6176 0.0298  0.0284  0.0474  221 THR A CG2 
1624 N N   . LEU A 223 ? 0.6049 0.6316 0.7355 0.0084  0.0282  0.0474  222 LEU A N   
1625 C CA  . LEU A 223 ? 0.6041 0.6402 0.7480 0.0074  0.0331  0.0520  222 LEU A CA  
1626 C C   . LEU A 223 ? 0.5948 0.6223 0.7358 0.0028  0.0353  0.0496  222 LEU A C   
1627 O O   . LEU A 223 ? 0.5934 0.6224 0.7366 0.0055  0.0408  0.0532  222 LEU A O   
1628 C CB  . LEU A 223 ? 0.6137 0.6638 0.7756 0.0017  0.0302  0.0546  222 LEU A CB  
1629 C CG  . LEU A 223 ? 0.6149 0.6767 0.7830 0.0064  0.0279  0.0580  222 LEU A CG  
1630 C CD1 . LEU A 223 ? 0.6364 0.7129 0.8238 -0.0005 0.0245  0.0606  222 LEU A CD1 
1631 C CD2 . LEU A 223 ? 0.6681 0.7354 0.8358 0.0171  0.0343  0.0631  222 LEU A CD2 
1632 N N   . MET A 224 ? 0.5589 0.5778 0.6947 -0.0038 0.0310  0.0437  223 MET A N   
1633 C CA  . MET A 224 ? 0.5567 0.5674 0.6899 -0.0075 0.0327  0.0411  223 MET A CA  
1634 C C   . MET A 224 ? 0.5558 0.5573 0.6752 -0.0014 0.0362  0.0405  223 MET A C   
1635 O O   . MET A 224 ? 0.5524 0.5515 0.6722 -0.0008 0.0399  0.0420  223 MET A O   
1636 C CB  . MET A 224 ? 0.5683 0.5726 0.6985 -0.0149 0.0276  0.0345  223 MET A CB  
1637 C CG  . MET A 224 ? 0.5918 0.6034 0.7357 -0.0222 0.0241  0.0339  223 MET A CG  
1638 S SD  . MET A 224 ? 0.6408 0.6461 0.7782 -0.0293 0.0176  0.0255  223 MET A SD  
1639 C CE  . MET A 224 ? 0.5449 0.5382 0.6632 -0.0254 0.0189  0.0220  223 MET A CE  
1640 N N   . ALA A 225 ? 0.5730 0.5687 0.6801 0.0031  0.0345  0.0384  224 ALA A N   
1641 C CA  . ALA A 225 ? 0.5641 0.5507 0.6579 0.0088  0.0369  0.0374  224 ALA A CA  
1642 C C   . ALA A 225 ? 0.6216 0.6135 0.7169 0.0165  0.0425  0.0427  224 ALA A C   
1643 O O   . ALA A 225 ? 0.6126 0.5991 0.7002 0.0199  0.0455  0.0426  224 ALA A O   
1644 C CB  . ALA A 225 ? 0.5357 0.5141 0.6168 0.0113  0.0333  0.0342  224 ALA A CB  
1645 N N   . LEU A 226 ? 0.6010 0.6046 0.7062 0.0194  0.0440  0.0473  225 LEU A N   
1646 C CA  . LEU A 226 ? 0.5735 0.5844 0.6812 0.0268  0.0502  0.0528  225 LEU A CA  
1647 C C   . LEU A 226 ? 0.5873 0.6036 0.7047 0.0233  0.0543  0.0570  225 LEU A C   
1648 O O   . LEU A 226 ? 0.6196 0.6382 0.7345 0.0289  0.0599  0.0608  225 LEU A O   
1649 C CB  . LEU A 226 ? 0.5109 0.5345 0.6280 0.0310  0.0507  0.0569  225 LEU A CB  
1650 C CG  . LEU A 226 ? 0.5290 0.5580 0.6430 0.0419  0.0568  0.0610  225 LEU A CG  
1651 C CD1 . LEU A 226 ? 0.6058 0.6218 0.7016 0.0494  0.0553  0.0563  225 LEU A CD1 
1652 C CD2 . LEU A 226 ? 0.5039 0.5500 0.6331 0.0446  0.0583  0.0665  225 LEU A CD2 
1653 N N   . ILE A 227 ? 0.6020 0.6197 0.7298 0.0142  0.0516  0.0562  226 ILE A N   
1654 C CA  . ILE A 227 ? 0.5391 0.5607 0.6773 0.0103  0.0550  0.0605  226 ILE A CA  
1655 C C   . ILE A 227 ? 0.5391 0.5496 0.6667 0.0109  0.0564  0.0584  226 ILE A C   
1656 O O   . ILE A 227 ? 0.6088 0.6214 0.7373 0.0136  0.0614  0.0635  226 ILE A O   
1657 C CB  . ILE A 227 ? 0.5322 0.5573 0.6847 0.0005  0.0510  0.0596  226 ILE A CB  
1658 C CG1 . ILE A 227 ? 0.5040 0.5441 0.6713 -0.0001 0.0509  0.0644  226 ILE A CG1 
1659 C CG2 . ILE A 227 ? 0.5566 0.5789 0.7159 -0.0046 0.0529  0.0616  226 ILE A CG2 
1660 C CD1 . ILE A 227 ? 0.5181 0.5610 0.6969 -0.0094 0.0449  0.0617  226 ILE A CD1 
1661 N N   . THR A 228 ? 0.5488 0.5481 0.6662 0.0086  0.0521  0.0515  227 THR A N   
1662 C CA  . THR A 228 ? 0.6105 0.6002 0.7188 0.0090  0.0528  0.0493  227 THR A CA  
1663 C C   . THR A 228 ? 0.6343 0.6214 0.7298 0.0177  0.0561  0.0507  227 THR A C   
1664 O O   . THR A 228 ? 0.6490 0.6320 0.7393 0.0194  0.0581  0.0517  227 THR A O   
1665 C CB  . THR A 228 ? 0.6077 0.5880 0.7092 0.0045  0.0476  0.0417  227 THR A CB  
1666 O OG1 . THR A 228 ? 0.6716 0.6469 0.7605 0.0085  0.0456  0.0384  227 THR A OG1 
1667 C CG2 . THR A 228 ? 0.5649 0.5482 0.6766 -0.0030 0.0439  0.0394  227 THR A CG2 
1668 N N   . SER A 229 ? 0.6251 0.6140 0.7148 0.0236  0.0564  0.0507  228 SER A N   
1669 C CA  . SER A 229 ? 0.6255 0.6107 0.7017 0.0324  0.0592  0.0509  228 SER A CA  
1670 C C   . SER A 229 ? 0.6081 0.6023 0.6879 0.0377  0.0660  0.0582  228 SER A C   
1671 O O   . SER A 229 ? 0.6947 0.6865 0.7625 0.0456  0.0687  0.0585  228 SER A O   
1672 C CB  . SER A 229 ? 0.6060 0.5891 0.6747 0.0377  0.0573  0.0483  228 SER A CB  
1673 O OG  . SER A 229 ? 0.7579 0.7364 0.8272 0.0320  0.0516  0.0437  228 SER A OG  
1674 N N   . VAL A 230 ? 0.6602 0.6646 0.7559 0.0335  0.0686  0.0641  229 VAL A N   
1675 C CA  . VAL A 230 ? 0.6818 0.6963 0.7822 0.0380  0.0757  0.0722  229 VAL A CA  
1676 C C   . VAL A 230 ? 0.7242 0.7406 0.8356 0.0315  0.0773  0.0771  229 VAL A C   
1677 O O   . VAL A 230 ? 0.8185 0.8362 0.9268 0.0347  0.0820  0.0823  229 VAL A O   
1678 C CB  . VAL A 230 ? 0.6348 0.6632 0.7455 0.0412  0.0787  0.0767  229 VAL A CB  
1679 C CG1 . VAL A 230 ? 0.6968 0.7229 0.7943 0.0509  0.0790  0.0733  229 VAL A CG1 
1680 C CG2 . VAL A 230 ? 0.6447 0.6777 0.7704 0.0330  0.0741  0.0756  229 VAL A CG2 
1681 N N   . THR A 231 ? 0.6541 0.6701 0.7778 0.0224  0.0733  0.0754  230 THR A N   
1682 C CA  . THR A 231 ? 0.5772 0.5953 0.7141 0.0158  0.0746  0.0804  230 THR A CA  
1683 C C   . THR A 231 ? 0.6132 0.6221 0.7418 0.0167  0.0755  0.0808  230 THR A C   
1684 O O   . THR A 231 ? 0.6081 0.6209 0.7363 0.0203  0.0809  0.0881  230 THR A O   
1685 C CB  . THR A 231 ? 0.5657 0.5817 0.7140 0.0063  0.0688  0.0761  230 THR A CB  
1686 O OG1 . THR A 231 ? 0.5822 0.6073 0.7378 0.0056  0.0672  0.0758  230 THR A OG1 
1687 C CG2 . THR A 231 ? 0.5113 0.5288 0.6743 -0.0005 0.0700  0.0813  230 THR A CG2 
1688 N N   . LEU A 232 ? 0.5901 0.5879 0.7124 0.0137  0.0704  0.0735  231 LEU A N   
1689 C CA  . LEU A 232 ? 0.6069 0.5965 0.7228 0.0144  0.0705  0.0736  231 LEU A CA  
1690 C C   . LEU A 232 ? 0.6731 0.6608 0.7725 0.0231  0.0730  0.0745  231 LEU A C   
1691 O O   . LEU A 232 ? 0.7241 0.7104 0.8205 0.0255  0.0756  0.0792  231 LEU A O   
1692 C CB  . LEU A 232 ? 0.6902 0.6699 0.8041 0.0094  0.0645  0.0653  231 LEU A CB  
1693 C CG  . LEU A 232 ? 0.6214 0.5997 0.7500 0.0013  0.0624  0.0649  231 LEU A CG  
1694 C CD1 . LEU A 232 ? 0.6268 0.5952 0.7513 -0.0014 0.0581  0.0577  231 LEU A CD1 
1695 C CD2 . LEU A 232 ? 0.5889 0.5704 0.7279 0.0002  0.0666  0.0741  231 LEU A CD2 
1696 N N   . PRO A 233 ? 0.6719 0.6585 0.7597 0.0282  0.0719  0.0699  232 PRO A N   
1697 C CA  . PRO A 233 ? 0.6872 0.6716 0.7588 0.0368  0.0741  0.0704  232 PRO A CA  
1698 C C   . PRO A 233 ? 0.6026 0.5963 0.6755 0.0421  0.0814  0.0796  232 PRO A C   
1699 O O   . PRO A 233 ? 0.6153 0.6068 0.6777 0.0470  0.0834  0.0822  232 PRO A O   
1700 C CB  . PRO A 233 ? 0.6423 0.6242 0.7045 0.0406  0.0717  0.0642  232 PRO A CB  
1701 C CG  . PRO A 233 ? 0.5663 0.5444 0.6351 0.0331  0.0663  0.0585  232 PRO A CG  
1702 C CD  . PRO A 233 ? 0.5813 0.5657 0.6678 0.0263  0.0675  0.0630  232 PRO A CD  
1703 N N   . VAL A 234 ? 0.5601 0.5649 0.6455 0.0414  0.0853  0.0851  233 VAL A N   
1704 C CA  . VAL A 234 ? 0.5695 0.5850 0.6579 0.0458  0.0929  0.0949  233 VAL A CA  
1705 C C   . VAL A 234 ? 0.5946 0.6091 0.6899 0.0414  0.0946  0.1016  233 VAL A C   
1706 O O   . VAL A 234 ? 0.6326 0.6501 0.7217 0.0464  0.0996  0.1084  233 VAL A O   
1707 C CB  . VAL A 234 ? 0.5343 0.5634 0.6371 0.0452  0.0964  0.0993  233 VAL A CB  
1708 C CG1 . VAL A 234 ? 0.5774 0.6186 0.6920 0.0445  0.1036  0.1111  233 VAL A CG1 
1709 C CG2 . VAL A 234 ? 0.5284 0.5606 0.6208 0.0541  0.0978  0.0959  233 VAL A CG2 
1710 N N   . ALA A 235 ? 0.5267 0.5365 0.6342 0.0324  0.0904  0.1000  234 ALA A N   
1711 C CA  . ALA A 235 ? 0.5731 0.5795 0.6871 0.0283  0.0911  0.1056  234 ALA A CA  
1712 C C   . ALA A 235 ? 0.6461 0.6441 0.7439 0.0335  0.0902  0.1044  234 ALA A C   
1713 O O   . ALA A 235 ? 0.6519 0.6514 0.7480 0.0360  0.0941  0.1125  234 ALA A O   
1714 C CB  . ALA A 235 ? 0.5427 0.5430 0.6699 0.0188  0.0856  0.1013  234 ALA A CB  
1715 N N   . TYR A 236 ? 0.6385 0.6281 0.7243 0.0352  0.0848  0.0947  235 TYR A N   
1716 C CA  . TYR A 236 ? 0.6430 0.6256 0.7136 0.0400  0.0830  0.0930  235 TYR A CA  
1717 C C   . TYR A 236 ? 0.6272 0.6147 0.6837 0.0493  0.0880  0.0973  235 TYR A C   
1718 O O   . TYR A 236 ? 0.6582 0.6442 0.7063 0.0531  0.0893  0.1017  235 TYR A O   
1719 C CB  . TYR A 236 ? 0.5857 0.5595 0.6480 0.0390  0.0762  0.0818  235 TYR A CB  
1720 C CG  . TYR A 236 ? 0.6371 0.6047 0.7091 0.0316  0.0715  0.0779  235 TYR A CG  
1721 C CD1 . TYR A 236 ? 0.6789 0.6419 0.7514 0.0312  0.0703  0.0804  235 TYR A CD1 
1722 C CD2 . TYR A 236 ? 0.6477 0.6143 0.7280 0.0256  0.0682  0.0719  235 TYR A CD2 
1723 C CE1 . TYR A 236 ? 0.6786 0.6360 0.7600 0.0254  0.0664  0.0764  235 TYR A CE1 
1724 C CE2 . TYR A 236 ? 0.6449 0.6060 0.7330 0.0195  0.0644  0.0679  235 TYR A CE2 
1725 C CZ  . TYR A 236 ? 0.6273 0.5838 0.7162 0.0196  0.0636  0.0700  235 TYR A CZ  
1726 O OH  . TYR A 236 ? 0.6455 0.5967 0.7422 0.0145  0.0601  0.0656  235 TYR A OH  
1727 N N   . ILE A 237 ? 0.6723 0.6660 0.7258 0.0534  0.0908  0.0963  236 ILE A N   
1728 C CA  . ILE A 237 ? 0.6266 0.6258 0.6666 0.0630  0.0962  0.1000  236 ILE A CA  
1729 C C   . ILE A 237 ? 0.6225 0.6302 0.6680 0.0640  0.1033  0.1124  236 ILE A C   
1730 O O   . ILE A 237 ? 0.6751 0.6832 0.7072 0.0706  0.1061  0.1163  236 ILE A O   
1731 C CB  . ILE A 237 ? 0.5931 0.5983 0.6322 0.0672  0.0985  0.0972  236 ILE A CB  
1732 C CG1 . ILE A 237 ? 0.6600 0.6548 0.6856 0.0696  0.0921  0.0858  236 ILE A CG1 
1733 C CG2 . ILE A 237 ? 0.5769 0.5924 0.6089 0.0763  0.1067  0.1042  236 ILE A CG2 
1734 C CD1 . ILE A 237 ? 0.6027 0.6012 0.6225 0.0765  0.0944  0.0830  236 ILE A CD1 
1735 N N   . MET A 238 ? 0.5740 0.5886 0.6393 0.0573  0.1060  0.1189  237 MET A N   
1736 C CA  . MET A 238 ? 0.6108 0.6328 0.6837 0.0567  0.1124  0.1315  237 MET A CA  
1737 C C   . MET A 238 ? 0.6137 0.6266 0.6821 0.0554  0.1099  0.1342  237 MET A C   
1738 O O   . MET A 238 ? 0.6568 0.6735 0.7214 0.0587  0.1150  0.1440  237 MET A O   
1739 C CB  . MET A 238 ? 0.6309 0.6603 0.7274 0.0481  0.1142  0.1370  237 MET A CB  
1740 C CG  . MET A 238 ? 0.6339 0.6761 0.7372 0.0500  0.1181  0.1374  237 MET A CG  
1741 S SD  . MET A 238 ? 0.6990 0.7526 0.8310 0.0398  0.1207  0.1461  237 MET A SD  
1742 C CE  . MET A 238 ? 0.4172 0.4835 0.5538 0.0432  0.1221  0.1424  237 MET A CE  
1743 N N   . MET A 239 ? 0.6642 0.6656 0.7326 0.0511  0.1022  0.1260  238 MET A N   
1744 C CA  . MET A 239 ? 0.6505 0.6435 0.7158 0.0503  0.0993  0.1281  238 MET A CA  
1745 C C   . MET A 239 ? 0.6913 0.6822 0.7348 0.0593  0.0990  0.1274  238 MET A C   
1746 O O   . MET A 239 ? 0.7255 0.7159 0.7644 0.0619  0.1009  0.1353  238 MET A O   
1747 C CB  . MET A 239 ? 0.6804 0.6632 0.7521 0.0439  0.0915  0.1190  238 MET A CB  
1748 C CG  . MET A 239 ? 0.6790 0.6611 0.7718 0.0347  0.0911  0.1214  238 MET A CG  
1749 S SD  . MET A 239 ? 0.6834 0.6556 0.7822 0.0281  0.0828  0.1088  238 MET A SD  
1750 C CE  . MET A 239 ? 0.6291 0.5916 0.7304 0.0271  0.0800  0.1118  238 MET A CE  
1751 N N   . ARG A 240 ? 0.6464 0.6355 0.6760 0.0640  0.0964  0.1182  239 ARG A N   
1752 C CA  . ARG A 240 ? 0.6633 0.6499 0.6713 0.0725  0.0954  0.1165  239 ARG A CA  
1753 C C   . ARG A 240 ? 0.6462 0.6423 0.6460 0.0798  0.1037  0.1261  239 ARG A C   
1754 O O   . ARG A 240 ? 0.6321 0.6271 0.6172 0.0856  0.1040  0.1295  239 ARG A O   
1755 C CB  . ARG A 240 ? 0.6556 0.6371 0.6513 0.0754  0.0905  0.1042  239 ARG A CB  
1756 C CG  . ARG A 240 ? 0.6577 0.6335 0.6642 0.0678  0.0847  0.0955  239 ARG A CG  
1757 C CD  . ARG A 240 ? 0.7473 0.7169 0.7405 0.0705  0.0796  0.0844  239 ARG A CD  
1758 N NE  . ARG A 240 ? 0.8825 0.8567 0.8700 0.0760  0.0837  0.0835  239 ARG A NE  
1759 C CZ  . ARG A 240 ? 0.9287 0.9010 0.8977 0.0843  0.0839  0.0800  239 ARG A CZ  
1760 N NH1 . ARG A 240 ? 0.8666 0.8325 0.8202 0.0877  0.0798  0.0770  239 ARG A NH1 
1761 N NH2 . ARG A 240 ? 0.7819 0.7588 0.7477 0.0896  0.0882  0.0794  239 ARG A NH2 
1762 N N   . LYS A 241 ? 0.6686 0.6750 0.6774 0.0799  0.1105  0.1308  240 LYS A N   
1763 C CA  . LYS A 241 ? 0.6786 0.6959 0.6808 0.0869  0.1194  0.1408  240 LYS A CA  
1764 C C   . LYS A 241 ? 0.7658 0.7859 0.7754 0.0841  0.1232  0.1539  240 LYS A C   
1765 O O   . LYS A 241 ? 0.8248 0.8484 0.8209 0.0908  0.1275  0.1610  240 LYS A O   
1766 C CB  . LYS A 241 ? 0.6988 0.7280 0.7114 0.0874  0.1258  0.1429  240 LYS A CB  
1767 C CG  . LYS A 241 ? 0.7486 0.7751 0.7540 0.0909  0.1225  0.1309  240 LYS A CG  
1768 C CD  . LYS A 241 ? 0.7333 0.7624 0.7167 0.1030  0.1262  0.1288  240 LYS A CD  
1769 C CE  . LYS A 241 ? 0.7397 0.7626 0.7150 0.1064  0.1217  0.1162  240 LYS A CE  
1770 N NZ  . LYS A 241 ? 0.6823 0.6904 0.6554 0.1007  0.1113  0.1062  240 LYS A NZ  
1771 N N   . LEU A 242 ? 0.6698 0.6875 0.6999 0.0744  0.1215  0.1572  241 LEU A N   
1772 C CA  . LEU A 242 ? 0.6420 0.6593 0.6796 0.0712  0.1239  0.1693  241 LEU A CA  
1773 C C   . LEU A 242 ? 0.6760 0.6833 0.6992 0.0747  0.1186  0.1681  241 LEU A C   
1774 O O   . LEU A 242 ? 0.6670 0.6762 0.6844 0.0779  0.1221  0.1788  241 LEU A O   
1775 C CB  . LEU A 242 ? 0.5837 0.5981 0.6458 0.0601  0.1219  0.1712  241 LEU A CB  
1776 C CG  . LEU A 242 ? 0.5951 0.6093 0.6683 0.0558  0.1254  0.1850  241 LEU A CG  
1777 C CD1 . LEU A 242 ? 0.6078 0.6350 0.6761 0.0610  0.1353  0.1983  241 LEU A CD1 
1778 C CD2 . LEU A 242 ? 0.7250 0.7374 0.8230 0.0448  0.1239  0.1863  241 LEU A CD2 
1779 N N   . LEU A 243 ? 0.6700 0.6675 0.6877 0.0740  0.1100  0.1558  242 LEU A N   
1780 C CA  . LEU A 243 ? 0.6749 0.6644 0.6791 0.0777  0.1044  0.1541  242 LEU A CA  
1781 C C   . LEU A 243 ? 0.6954 0.6889 0.6758 0.0881  0.1067  0.1551  242 LEU A C   
1782 O O   . LEU A 243 ? 0.6846 0.6780 0.6552 0.0923  0.1074  0.1627  242 LEU A O   
1783 C CB  . LEU A 243 ? 0.5880 0.5679 0.5930 0.0743  0.0950  0.1407  242 LEU A CB  
1784 C CG  . LEU A 243 ? 0.5370 0.5080 0.5399 0.0736  0.0875  0.1382  242 LEU A CG  
1785 C CD1 . LEU A 243 ? 0.6304 0.5949 0.6374 0.0692  0.0801  0.1248  242 LEU A CD1 
1786 C CD2 . LEU A 243 ? 0.7149 0.6858 0.6968 0.0820  0.0858  0.1399  242 LEU A CD2 
1787 N N   . ALA A 244 ? 0.7057 0.7029 0.6761 0.0926  0.1082  0.1478  243 ALA A N   
1788 C CA  . ALA A 244 ? 0.7130 0.7130 0.6594 0.1030  0.1101  0.1473  243 ALA A CA  
1789 C C   . ALA A 244 ? 0.7162 0.7267 0.6590 0.1077  0.1198  0.1616  243 ALA A C   
1790 O O   . ALA A 244 ? 0.7296 0.7423 0.6515 0.1164  0.1214  0.1634  243 ALA A O   
1791 C CB  . ALA A 244 ? 0.6248 0.6256 0.5623 0.1072  0.1100  0.1366  243 ALA A CB  
1792 N N   . ALA A 245 ? 0.7249 0.7423 0.6874 0.1020  0.1262  0.1718  244 ALA A N   
1793 C CA  . ALA A 245 ? 0.6346 0.6628 0.5963 0.1051  0.1359  0.1870  244 ALA A CA  
1794 C C   . ALA A 245 ? 0.6771 0.7005 0.6386 0.1036  0.1344  0.1972  244 ALA A C   
1795 O O   . ALA A 245 ? 0.8092 0.8362 0.7538 0.1109  0.1377  0.2047  244 ALA A O   
1796 C CB  . ALA A 245 ? 0.5455 0.5840 0.5298 0.0990  0.1432  0.1940  244 ALA A CB  
1797 N N   . GLN A 246 ? 0.6876 0.7027 0.6671 0.0947  0.1292  0.1976  245 GLN A N   
1798 C CA  . GLN A 246 ? 0.6776 0.6866 0.6583 0.0934  0.1272  0.2071  245 GLN A CA  
1799 C C   . GLN A 246 ? 0.7094 0.7105 0.6708 0.0994  0.1190  0.2006  245 GLN A C   
1800 O O   . GLN A 246 ? 0.7381 0.7368 0.6935 0.1019  0.1183  0.2097  245 GLN A O   
1801 C CB  . GLN A 246 ? 0.6761 0.6775 0.6817 0.0828  0.1237  0.2080  245 GLN A CB  
1802 C CG  . GLN A 246 ? 0.6754 0.6838 0.7018 0.0755  0.1297  0.2119  245 GLN A CG  
1803 C CD  . GLN A 246 ? 0.7094 0.7265 0.7421 0.0747  0.1390  0.2296  245 GLN A CD  
1804 O OE1 . GLN A 246 ? 0.6989 0.7103 0.7371 0.0720  0.1387  0.2398  245 GLN A OE1 
1805 N NE2 . GLN A 246 ? 0.6913 0.7226 0.7238 0.0770  0.1475  0.2337  245 GLN A NE2 
1806 N N   . TYR A 247 ? 0.7077 0.7048 0.6597 0.1015  0.1127  0.1856  246 TYR A N   
1807 C CA  . TYR A 247 ? 0.7367 0.7269 0.6715 0.1064  0.1041  0.1784  246 TYR A CA  
1808 C C   . TYR A 247 ? 0.7747 0.7666 0.6899 0.1130  0.1026  0.1671  246 TYR A C   
1809 O O   . TYR A 247 ? 0.8322 0.8321 0.7406 0.1174  0.1100  0.1690  246 TYR A O   
1810 C CB  . TYR A 247 ? 0.7222 0.7024 0.6703 0.0996  0.0950  0.1707  246 TYR A CB  
1811 C CG  . TYR A 247 ? 0.6221 0.5985 0.5881 0.0941  0.0956  0.1811  246 TYR A CG  
1812 C CD1 . TYR A 247 ? 0.6247 0.6014 0.6128 0.0860  0.0995  0.1841  246 TYR A CD1 
1813 C CD2 . TYR A 247 ? 0.6665 0.6388 0.6275 0.0970  0.0920  0.1878  246 TYR A CD2 
1814 C CE1 . TYR A 247 ? 0.6053 0.5769 0.6095 0.0808  0.0998  0.1930  246 TYR A CE1 
1815 C CE2 . TYR A 247 ? 0.6878 0.6551 0.6651 0.0924  0.0925  0.1973  246 TYR A CE2 
1816 C CZ  . TYR A 247 ? 0.5871 0.5535 0.5859 0.0842  0.0964  0.1996  246 TYR A CZ  
1817 O OH  . TYR A 247 ? 0.5555 0.5153 0.5705 0.0794  0.0964  0.2085  246 TYR A OH  
1818 N N   . SER A 248 ? 0.8909 0.8751 0.7973 0.1137  0.0930  0.1552  247 SER A N   
1819 C CA  . SER A 248 ? 0.9353 0.9186 0.8223 0.1197  0.0901  0.1439  247 SER A CA  
1820 C C   . SER A 248 ? 0.9232 0.9023 0.8199 0.1144  0.0869  0.1314  247 SER A C   
1821 O O   . SER A 248 ? 0.8863 0.8623 0.8028 0.1061  0.0847  0.1299  247 SER A O   
1822 C CB  . SER A 248 ? 0.9433 0.9212 0.8125 0.1241  0.0810  0.1389  247 SER A CB  
1823 O OG  . SER A 248 ? 0.9595 0.9358 0.8083 0.1302  0.0784  0.1285  247 SER A OG  
1824 N N   . TRP A 249 ? 0.8284 0.8070 0.7100 0.1196  0.0865  0.1225  248 TRP A N   
1825 C CA  . TRP A 249 ? 0.7238 0.6971 0.6115 0.1153  0.0823  0.1103  248 TRP A CA  
1826 C C   . TRP A 249 ? 0.7533 0.7175 0.6419 0.1107  0.0714  0.1014  248 TRP A C   
1827 O O   . TRP A 249 ? 0.7722 0.7323 0.6733 0.1040  0.0678  0.0942  248 TRP A O   
1828 C CB  . TRP A 249 ? 0.6315 0.6050 0.5019 0.1228  0.0843  0.1032  248 TRP A CB  
1829 C CG  . TRP A 249 ? 0.6855 0.6666 0.5653 0.1234  0.0934  0.1066  248 TRP A CG  
1830 C CD1 . TRP A 249 ? 0.5988 0.5894 0.4706 0.1311  0.1027  0.1133  248 TRP A CD1 
1831 C CD2 . TRP A 249 ? 0.7535 0.7346 0.6527 0.1163  0.0939  0.1035  248 TRP A CD2 
1832 N NE1 . TRP A 249 ? 0.6309 0.6279 0.5172 0.1291  0.1089  0.1148  248 TRP A NE1 
1833 C CE2 . TRP A 249 ? 0.7191 0.7102 0.6220 0.1200  0.1033  0.1088  248 TRP A CE2 
1834 C CE3 . TRP A 249 ? 0.5987 0.5732 0.5123 0.1073  0.0874  0.0970  248 TRP A CE3 
1835 C CZ2 . TRP A 249 ? 0.6084 0.6029 0.5291 0.1150  0.1056  0.1077  248 TRP A CZ2 
1836 C CZ3 . TRP A 249 ? 0.6258 0.6029 0.5555 0.1025  0.0899  0.0959  248 TRP A CZ3 
1837 C CH2 . TRP A 249 ? 0.6551 0.6421 0.5884 0.1062  0.0986  0.1012  248 TRP A CH2 
1838 N N   . ASP A 250 ? 0.7852 0.7472 0.6609 0.1142  0.0659  0.1019  249 ASP A N   
1839 C CA  . ASP A 250 ? 0.7646 0.7202 0.6435 0.1097  0.0557  0.0948  249 ASP A CA  
1840 C C   . ASP A 250 ? 0.7121 0.6678 0.6137 0.1021  0.0554  0.0998  249 ASP A C   
1841 O O   . ASP A 250 ? 0.7205 0.6719 0.6317 0.0963  0.0490  0.0927  249 ASP A O   
1842 C CB  . ASP A 250 ? 0.7756 0.7302 0.6355 0.1157  0.0498  0.0948  249 ASP A CB  
1843 C CG  . ASP A 250 ? 0.8097 0.7612 0.6466 0.1221  0.0470  0.0858  249 ASP A CG  
1844 O OD1 . ASP A 250 ? 0.8662 0.8125 0.7040 0.1193  0.0443  0.0755  249 ASP A OD1 
1845 O OD2 . ASP A 250 ? 0.8299 0.7836 0.6475 0.1300  0.0475  0.0890  249 ASP A OD2 
1846 N N   . GLU A 251 ? 0.7195 0.6798 0.6299 0.1022  0.0623  0.1120  250 GLU A N   
1847 C CA  . GLU A 251 ? 0.7030 0.6620 0.6356 0.0949  0.0625  0.1162  250 GLU A CA  
1848 C C   . GLU A 251 ? 0.6636 0.6216 0.6118 0.0879  0.0642  0.1102  250 GLU A C   
1849 O O   . GLU A 251 ? 0.6445 0.5991 0.6084 0.0814  0.0611  0.1076  250 GLU A O   
1850 C CB  . GLU A 251 ? 0.6986 0.6618 0.6367 0.0962  0.0696  0.1309  250 GLU A CB  
1851 C CG  . GLU A 251 ? 0.6153 0.5754 0.5755 0.0893  0.0695  0.1358  250 GLU A CG  
1852 C CD  . GLU A 251 ? 0.6457 0.6012 0.6065 0.0901  0.0625  0.1368  250 GLU A CD  
1853 O OE1 . GLU A 251 ? 0.7231 0.6787 0.6678 0.0954  0.0571  0.1334  250 GLU A OE1 
1854 O OE2 . GLU A 251 ? 0.6663 0.6184 0.6440 0.0856  0.0623  0.1409  250 GLU A OE2 
1855 N N   . VAL A 252 ? 0.6902 0.6513 0.6337 0.0897  0.0689  0.1080  251 VAL A N   
1856 C CA  . VAL A 252 ? 0.6474 0.6072 0.6024 0.0839  0.0689  0.1008  251 VAL A CA  
1857 C C   . VAL A 252 ? 0.6742 0.6274 0.6244 0.0817  0.0604  0.0883  251 VAL A C   
1858 O O   . VAL A 252 ? 0.6795 0.6301 0.6420 0.0751  0.0580  0.0825  251 VAL A O   
1859 C CB  . VAL A 252 ? 0.6452 0.6106 0.5960 0.0874  0.0759  0.1019  251 VAL A CB  
1860 C CG1 . VAL A 252 ? 0.7209 0.6851 0.6834 0.0817  0.0754  0.0949  251 VAL A CG1 
1861 C CG2 . VAL A 252 ? 0.6035 0.5771 0.5599 0.0892  0.0848  0.1151  251 VAL A CG2 
1862 N N   . GLY A 253 ? 0.6200 0.5707 0.5523 0.0870  0.0555  0.0842  252 GLY A N   
1863 C CA  . GLY A 253 ? 0.6000 0.5446 0.5276 0.0846  0.0473  0.0728  252 GLY A CA  
1864 C C   . GLY A 253 ? 0.6695 0.6121 0.6102 0.0783  0.0415  0.0708  252 GLY A C   
1865 O O   . GLY A 253 ? 0.7452 0.6846 0.6918 0.0730  0.0371  0.0626  252 GLY A O   
1866 N N   . ILE A 254 ? 0.6003 0.5451 0.5459 0.0793  0.0417  0.0784  253 ILE A N   
1867 C CA  . ILE A 254 ? 0.6614 0.6048 0.6201 0.0744  0.0366  0.0766  253 ILE A CA  
1868 C C   . ILE A 254 ? 0.6475 0.5904 0.6258 0.0675  0.0400  0.0765  253 ILE A C   
1869 O O   . ILE A 254 ? 0.6476 0.5889 0.6365 0.0625  0.0361  0.0712  253 ILE A O   
1870 C CB  . ILE A 254 ? 0.6308 0.5758 0.5887 0.0783  0.0353  0.0849  253 ILE A CB  
1871 C CG1 . ILE A 254 ? 0.6356 0.5826 0.6008 0.0792  0.0432  0.0966  253 ILE A CG1 
1872 C CG2 . ILE A 254 ? 0.6901 0.6359 0.6273 0.0852  0.0313  0.0845  253 ILE A CG2 
1873 C CD1 . ILE A 254 ? 0.6412 0.5882 0.6093 0.0819  0.0419  0.1054  253 ILE A CD1 
1874 N N   . TRP A 255 ? 0.6429 0.5879 0.6264 0.0671  0.0473  0.0822  254 TRP A N   
1875 C CA  . TRP A 255 ? 0.6350 0.5795 0.6358 0.0603  0.0498  0.0811  254 TRP A CA  
1876 C C   . TRP A 255 ? 0.6636 0.6068 0.6636 0.0568  0.0481  0.0715  254 TRP A C   
1877 O O   . TRP A 255 ? 0.6809 0.6226 0.6929 0.0507  0.0466  0.0668  254 TRP A O   
1878 C CB  . TRP A 255 ? 0.6187 0.5668 0.6267 0.0603  0.0576  0.0907  254 TRP A CB  
1879 C CG  . TRP A 255 ? 0.6790 0.6267 0.7046 0.0531  0.0596  0.0895  254 TRP A CG  
1880 C CD1 . TRP A 255 ? 0.6619 0.6058 0.7006 0.0475  0.0564  0.0855  254 TRP A CD1 
1881 C CD2 . TRP A 255 ? 0.6744 0.6262 0.7062 0.0511  0.0652  0.0921  254 TRP A CD2 
1882 N NE1 . TRP A 255 ? 0.6178 0.5625 0.6694 0.0419  0.0592  0.0851  254 TRP A NE1 
1883 C CE2 . TRP A 255 ? 0.6256 0.5754 0.6739 0.0437  0.0643  0.0893  254 TRP A CE2 
1884 C CE3 . TRP A 255 ? 0.6391 0.5968 0.6644 0.0551  0.0707  0.0965  254 TRP A CE3 
1885 C CZ2 . TRP A 255 ? 0.5936 0.5471 0.6521 0.0398  0.0682  0.0909  254 TRP A CZ2 
1886 C CZ3 . TRP A 255 ? 0.6029 0.5651 0.6394 0.0514  0.0750  0.0983  254 TRP A CZ3 
1887 C CH2 . TRP A 255 ? 0.5993 0.5594 0.6524 0.0436  0.0734  0.0956  254 TRP A CH2 
1888 N N   . GLN A 256 ? 0.6711 0.6143 0.6564 0.0610  0.0482  0.0685  255 GLN A N   
1889 C CA  . GLN A 256 ? 0.7150 0.6555 0.6981 0.0583  0.0459  0.0596  255 GLN A CA  
1890 C C   . GLN A 256 ? 0.6814 0.6180 0.6636 0.0548  0.0383  0.0515  255 GLN A C   
1891 O O   . GLN A 256 ? 0.7051 0.6396 0.6929 0.0496  0.0363  0.0453  255 GLN A O   
1892 C CB  . GLN A 256 ? 0.7522 0.6925 0.7192 0.0646  0.0478  0.0584  255 GLN A CB  
1893 C CG  . GLN A 256 ? 0.7908 0.7365 0.7613 0.0669  0.0559  0.0648  255 GLN A CG  
1894 C CD  . GLN A 256 ? 0.8021 0.7481 0.7559 0.0746  0.0582  0.0634  255 GLN A CD  
1895 O OE1 . GLN A 256 ? 0.7895 0.7410 0.7451 0.0775  0.0648  0.0679  255 GLN A OE1 
1896 N NE2 . GLN A 256 ? 0.7862 0.7265 0.7240 0.0781  0.0526  0.0571  255 GLN A NE2 
1897 N N   . GLY A 257 ? 0.6266 0.5628 0.6020 0.0576  0.0339  0.0518  256 GLY A N   
1898 C CA  . GLY A 257 ? 0.6316 0.5658 0.6075 0.0541  0.0266  0.0447  256 GLY A CA  
1899 C C   . GLY A 257 ? 0.7428 0.6785 0.7363 0.0481  0.0261  0.0438  256 GLY A C   
1900 O O   . GLY A 257 ? 0.8061 0.7409 0.8040 0.0430  0.0226  0.0370  256 GLY A O   
1901 N N   . VAL A 258 ? 0.7123 0.6500 0.7159 0.0486  0.0295  0.0506  257 VAL A N   
1902 C CA  . VAL A 258 ? 0.6746 0.6127 0.6945 0.0436  0.0293  0.0494  257 VAL A CA  
1903 C C   . VAL A 258 ? 0.7048 0.6420 0.7323 0.0380  0.0320  0.0454  257 VAL A C   
1904 O O   . VAL A 258 ? 0.7094 0.6466 0.7447 0.0331  0.0299  0.0397  257 VAL A O   
1905 C CB  . VAL A 258 ? 0.6622 0.6007 0.6904 0.0458  0.0323  0.0578  257 VAL A CB  
1906 C CG1 . VAL A 258 ? 0.6480 0.5856 0.6927 0.0412  0.0322  0.0557  257 VAL A CG1 
1907 C CG2 . VAL A 258 ? 0.6224 0.5621 0.6426 0.0516  0.0289  0.0619  257 VAL A CG2 
1908 N N   . SER A 259 ? 0.7122 0.6494 0.7372 0.0389  0.0367  0.0485  258 SER A N   
1909 C CA  . SER A 259 ? 0.6903 0.6273 0.7221 0.0340  0.0387  0.0452  258 SER A CA  
1910 C C   . SER A 259 ? 0.7272 0.6622 0.7515 0.0319  0.0351  0.0374  258 SER A C   
1911 O O   . SER A 259 ? 0.8284 0.7630 0.8590 0.0268  0.0349  0.0331  258 SER A O   
1912 C CB  . SER A 259 ? 0.6922 0.6313 0.7243 0.0359  0.0445  0.0512  258 SER A CB  
1913 O OG  . SER A 259 ? 0.6955 0.6362 0.7300 0.0391  0.0478  0.0598  258 SER A OG  
1914 N N   . SER A 260 ? 0.7235 0.6568 0.7340 0.0358  0.0321  0.0355  259 SER A N   
1915 C CA  . SER A 260 ? 0.8083 0.7380 0.8114 0.0336  0.0282  0.0284  259 SER A CA  
1916 C C   . SER A 260 ? 0.7873 0.7175 0.7976 0.0278  0.0239  0.0231  259 SER A C   
1917 O O   . SER A 260 ? 0.7996 0.7286 0.8133 0.0228  0.0233  0.0188  259 SER A O   
1918 C CB  . SER A 260 ? 0.7830 0.7097 0.7696 0.0390  0.0253  0.0271  259 SER A CB  
1919 O OG  . SER A 260 ? 0.7656 0.6935 0.7499 0.0402  0.0209  0.0271  259 SER A OG  
1920 N N   . ILE A 261 ? 0.7463 0.6789 0.7591 0.0285  0.0210  0.0237  260 ILE A N   
1921 C CA  . ILE A 261 ? 0.7548 0.6898 0.7758 0.0236  0.0176  0.0192  260 ILE A CA  
1922 C C   . ILE A 261 ? 0.8439 0.7810 0.8790 0.0197  0.0211  0.0193  260 ILE A C   
1923 O O   . ILE A 261 ? 0.8401 0.7793 0.8817 0.0150  0.0196  0.0148  260 ILE A O   
1924 C CB  . ILE A 261 ? 0.7005 0.6387 0.7213 0.0262  0.0135  0.0202  260 ILE A CB  
1925 C CG1 . ILE A 261 ? 0.6702 0.6107 0.6998 0.0293  0.0165  0.0262  260 ILE A CG1 
1926 C CG2 . ILE A 261 ? 0.7730 0.7087 0.7784 0.0308  0.0100  0.0204  260 ILE A CG2 
1927 C CD1 . ILE A 261 ? 0.7250 0.6694 0.7565 0.0321  0.0123  0.0273  260 ILE A CD1 
1928 N N   . SER A 262 ? 0.8532 0.7900 0.8932 0.0215  0.0257  0.0243  261 SER A N   
1929 C CA  . SER A 262 ? 0.7676 0.7050 0.8199 0.0175  0.0286  0.0237  261 SER A CA  
1930 C C   . SER A 262 ? 0.8050 0.7415 0.8565 0.0130  0.0293  0.0196  261 SER A C   
1931 O O   . SER A 262 ? 0.7967 0.7343 0.8554 0.0084  0.0292  0.0156  261 SER A O   
1932 C CB  . SER A 262 ? 0.7783 0.7151 0.8364 0.0198  0.0328  0.0304  261 SER A CB  
1933 O OG  . SER A 262 ? 0.8235 0.7607 0.8820 0.0242  0.0321  0.0350  261 SER A OG  
1934 N N   . ASP A 263 ? 0.9251 0.8595 0.9673 0.0148  0.0299  0.0205  262 ASP A N   
1935 C CA  . ASP A 263 ? 0.9755 0.9086 1.0162 0.0112  0.0301  0.0172  262 ASP A CA  
1936 C C   . ASP A 263 ? 0.9053 0.8374 0.9429 0.0072  0.0261  0.0114  262 ASP A C   
1937 O O   . ASP A 263 ? 0.9512 0.8832 0.9913 0.0026  0.0261  0.0084  262 ASP A O   
1938 C CB  . ASP A 263 ? 0.9688 0.8996 0.9999 0.0153  0.0315  0.0196  262 ASP A CB  
1939 C CG  . ASP A 263 ? 1.1299 1.0635 1.1662 0.0179  0.0364  0.0257  262 ASP A CG  
1940 O OD1 . ASP A 263 ? 1.1075 1.0433 1.1554 0.0149  0.0383  0.0272  262 ASP A OD1 
1941 O OD2 . ASP A 263 ? 1.2477 1.1812 1.2764 0.0230  0.0384  0.0290  262 ASP A OD2 
1942 N N   . ALA A 264 ? 0.8136 0.7454 0.8460 0.0084  0.0224  0.0100  263 ALA A N   
1943 C CA  . ALA A 264 ? 0.8299 0.7612 0.8600 0.0040  0.0184  0.0050  263 ALA A CA  
1944 C C   . ALA A 264 ? 0.7909 0.7275 0.8322 -0.0007 0.0188  0.0025  263 ALA A C   
1945 O O   . ALA A 264 ? 0.8039 0.7409 0.8466 -0.0057 0.0186  -0.0006 263 ALA A O   
1946 C CB  . ALA A 264 ? 0.7958 0.7259 0.8178 0.0063  0.0138  0.0042  263 ALA A CB  
1947 N N   . TYR A 265 ? 0.7555 0.6961 0.8044 0.0014  0.0194  0.0040  264 TYR A N   
1948 C CA  . TYR A 265 ? 0.7471 0.6930 0.8064 -0.0018 0.0199  0.0011  264 TYR A CA  
1949 C C   . TYR A 265 ? 0.7859 0.7316 0.8519 -0.0042 0.0237  0.0003  264 TYR A C   
1950 O O   . TYR A 265 ? 0.7927 0.7420 0.8645 -0.0077 0.0243  -0.0034 264 TYR A O   
1951 C CB  . TYR A 265 ? 0.7013 0.6509 0.7667 0.0020  0.0190  0.0029  264 TYR A CB  
1952 C CG  . TYR A 265 ? 0.7257 0.6743 0.7991 0.0050  0.0225  0.0059  264 TYR A CG  
1953 C CD1 . TYR A 265 ? 0.7230 0.6678 0.7931 0.0091  0.0241  0.0115  264 TYR A CD1 
1954 C CD2 . TYR A 265 ? 0.7573 0.7086 0.8413 0.0036  0.0243  0.0033  264 TYR A CD2 
1955 C CE1 . TYR A 265 ? 0.7085 0.6516 0.7865 0.0110  0.0270  0.0149  264 TYR A CE1 
1956 C CE2 . TYR A 265 ? 0.7036 0.6522 0.7949 0.0060  0.0269  0.0058  264 TYR A CE2 
1957 C CZ  . TYR A 265 ? 0.7304 0.6747 0.8191 0.0093  0.0281  0.0119  264 TYR A CZ  
1958 O OH  . TYR A 265 ? 0.7283 0.6692 0.8249 0.0109  0.0305  0.0150  264 TYR A OH  
1959 N N   . LEU A 266 ? 0.7697 0.7118 0.8349 -0.0023 0.0262  0.0035  265 LEU A N   
1960 C CA  . LEU A 266 ? 0.7639 0.7058 0.8350 -0.0053 0.0289  0.0023  265 LEU A CA  
1961 C C   . LEU A 266 ? 0.8221 0.7634 0.8881 -0.0095 0.0283  -0.0005 265 LEU A C   
1962 O O   . LEU A 266 ? 0.8422 0.7846 0.9124 -0.0129 0.0296  -0.0029 265 LEU A O   
1963 C CB  . LEU A 266 ? 0.8031 0.7426 0.8768 -0.0026 0.0315  0.0072  265 LEU A CB  
1964 C CG  . LEU A 266 ? 0.7170 0.6560 0.7982 0.0005  0.0329  0.0106  265 LEU A CG  
1965 C CD1 . LEU A 266 ? 0.5719 0.5090 0.6576 0.0008  0.0358  0.0152  265 LEU A CD1 
1966 C CD2 . LEU A 266 ? 0.7250 0.6657 0.8148 -0.0012 0.0326  0.0064  265 LEU A CD2 
1967 N N   . GLN A 267 ? 0.7837 0.7226 0.8403 -0.0094 0.0261  -0.0003 266 GLN A N   
1968 C CA  . GLN A 267 ? 0.7654 0.7025 0.8167 -0.0131 0.0252  -0.0023 266 GLN A CA  
1969 C C   . GLN A 267 ? 0.8482 0.7889 0.9019 -0.0184 0.0244  -0.0063 266 GLN A C   
1970 O O   . GLN A 267 ? 0.8164 0.7563 0.8671 -0.0220 0.0242  -0.0076 266 GLN A O   
1971 C CB  . GLN A 267 ? 0.7680 0.7001 0.8085 -0.0111 0.0227  -0.0013 266 GLN A CB  
1972 C CG  . GLN A 267 ? 0.8113 0.7393 0.8460 -0.0116 0.0228  -0.0007 266 GLN A CG  
1973 C CD  . GLN A 267 ? 0.8024 0.7240 0.8260 -0.0086 0.0204  -0.0002 266 GLN A CD  
1974 O OE1 . GLN A 267 ? 0.7529 0.6731 0.7725 -0.0067 0.0182  -0.0007 266 GLN A OE1 
1975 N NE2 . GLN A 267 ? 0.7998 0.7173 0.8183 -0.0079 0.0203  0.0004  266 GLN A NE2 
1976 N N   . PHE A 268 ? 0.8809 0.8263 0.9402 -0.0186 0.0241  -0.0080 267 PHE A N   
1977 C CA  . PHE A 268 ? 0.8670 0.8177 0.9299 -0.0231 0.0244  -0.0116 267 PHE A CA  
1978 C C   . PHE A 268 ? 0.8938 0.8465 0.9615 -0.0250 0.0273  -0.0139 267 PHE A C   
1979 O O   . PHE A 268 ? 0.8978 0.8541 0.9653 -0.0291 0.0279  -0.0167 267 PHE A O   
1980 C CB  . PHE A 268 ? 0.8457 0.8023 0.9149 -0.0219 0.0237  -0.0127 267 PHE A CB  
1981 C CG  . PHE A 268 ? 0.8169 0.7731 0.8815 -0.0215 0.0198  -0.0115 267 PHE A CG  
1982 C CD1 . PHE A 268 ? 0.8006 0.7575 0.8611 -0.0265 0.0175  -0.0128 267 PHE A CD1 
1983 C CD2 . PHE A 268 ? 0.7552 0.7099 0.8191 -0.0164 0.0182  -0.0091 267 PHE A CD2 
1984 C CE1 . PHE A 268 ? 0.7331 0.6888 0.7894 -0.0267 0.0131  -0.0122 267 PHE A CE1 
1985 C CE2 . PHE A 268 ? 0.7779 0.7320 0.8365 -0.0160 0.0140  -0.0086 267 PHE A CE2 
1986 C CZ  . PHE A 268 ? 0.7554 0.7098 0.8105 -0.0213 0.0112  -0.0105 267 PHE A CZ  
1987 N N   . ILE A 269 ? 1.0193 0.9697 1.0910 -0.0222 0.0289  -0.0126 268 ILE A N   
1988 C CA  . ILE A 269 ? 1.0387 0.9899 1.1150 -0.0240 0.0309  -0.0153 268 ILE A CA  
1989 C C   . ILE A 269 ? 1.0118 0.9594 1.0850 -0.0249 0.0308  -0.0133 268 ILE A C   
1990 O O   . ILE A 269 ? 1.0307 0.9794 1.1027 -0.0282 0.0309  -0.0158 268 ILE A O   
1991 C CB  . ILE A 269 ? 0.9873 0.9385 1.0728 -0.0208 0.0324  -0.0158 268 ILE A CB  
1992 C CG1 . ILE A 269 ? 1.0096 0.9663 1.0999 -0.0205 0.0330  -0.0195 268 ILE A CG1 
1993 C CG2 . ILE A 269 ? 0.9865 0.9356 1.0763 -0.0221 0.0337  -0.0175 268 ILE A CG2 
1994 C CD1 . ILE A 269 ? 0.9915 0.9481 1.0880 -0.0156 0.0329  -0.0176 268 ILE A CD1 
1995 N N   . THR A 270 ? 0.8473 0.7916 0.9188 -0.0216 0.0306  -0.0089 269 THR A N   
1996 C CA  . THR A 270 ? 0.8092 0.7517 0.8797 -0.0218 0.0308  -0.0066 269 THR A CA  
1997 C C   . THR A 270 ? 0.7811 0.7228 0.8434 -0.0242 0.0291  -0.0070 269 THR A C   
1998 O O   . THR A 270 ? 0.7310 0.6730 0.7933 -0.0257 0.0289  -0.0067 269 THR A O   
1999 C CB  . THR A 270 ? 0.8465 0.7869 0.9170 -0.0172 0.0316  -0.0013 269 THR A CB  
2000 O OG1 . THR A 270 ? 0.8892 0.8278 0.9522 -0.0146 0.0303  -0.0001 269 THR A OG1 
2001 C CG2 . THR A 270 ? 0.7949 0.7355 0.8742 -0.0153 0.0333  0.0003  269 THR A CG2 
2002 N N   . ALA A 271 ? 0.7945 0.7349 0.8501 -0.0248 0.0276  -0.0075 270 ALA A N   
2003 C CA  . ALA A 271 ? 0.7465 0.6844 0.7941 -0.0271 0.0258  -0.0073 270 ALA A CA  
2004 C C   . ALA A 271 ? 0.7458 0.6869 0.7934 -0.0322 0.0258  -0.0103 270 ALA A C   
2005 O O   . ALA A 271 ? 0.7573 0.6966 0.7991 -0.0342 0.0244  -0.0095 270 ALA A O   
2006 C CB  . ALA A 271 ? 0.7541 0.6885 0.7949 -0.0268 0.0237  -0.0068 270 ALA A CB  
2007 N N   . SER A 272 ? 0.7472 0.6930 0.8006 -0.0338 0.0274  -0.0137 271 SER A N   
2008 C CA  . SER A 272 ? 0.6832 0.6328 0.7358 -0.0380 0.0280  -0.0170 271 SER A CA  
2009 C C   . SER A 272 ? 0.6622 0.6125 0.7176 -0.0385 0.0282  -0.0183 271 SER A C   
2010 O O   . SER A 272 ? 0.6809 0.6338 0.7334 -0.0418 0.0281  -0.0208 271 SER A O   
2011 C CB  . SER A 272 ? 0.6701 0.6250 0.7273 -0.0390 0.0299  -0.0206 271 SER A CB  
2012 O OG  . SER A 272 ? 0.7636 0.7185 0.8282 -0.0351 0.0307  -0.0207 271 SER A OG  
2013 N N   . PHE A 273 ? 0.6302 0.5786 0.6911 -0.0356 0.0283  -0.0165 272 PHE A N   
2014 C CA  . PHE A 273 ? 0.6367 0.5860 0.7014 -0.0367 0.0278  -0.0175 272 PHE A CA  
2015 C C   . PHE A 273 ? 0.6093 0.5585 0.6682 -0.0380 0.0257  -0.0153 272 PHE A C   
2016 O O   . PHE A 273 ? 0.6516 0.6030 0.7107 -0.0406 0.0244  -0.0174 272 PHE A O   
2017 C CB  . PHE A 273 ? 0.6868 0.6346 0.7600 -0.0338 0.0286  -0.0150 272 PHE A CB  
2018 C CG  . PHE A 273 ? 0.6710 0.6183 0.7511 -0.0325 0.0304  -0.0173 272 PHE A CG  
2019 C CD1 . PHE A 273 ? 0.6829 0.6321 0.7623 -0.0336 0.0312  -0.0220 272 PHE A CD1 
2020 C CD2 . PHE A 273 ? 0.6431 0.5883 0.7308 -0.0300 0.0313  -0.0143 272 PHE A CD2 
2021 C CE1 . PHE A 273 ? 0.6932 0.6418 0.7794 -0.0316 0.0327  -0.0241 272 PHE A CE1 
2022 C CE2 . PHE A 273 ? 0.5841 0.5277 0.6781 -0.0285 0.0326  -0.0159 272 PHE A CE2 
2023 C CZ  . PHE A 273 ? 0.6524 0.5976 0.7459 -0.0289 0.0331  -0.0211 272 PHE A CZ  
2024 N N   . SER A 274 ? 0.5827 0.5289 0.6359 -0.0361 0.0249  -0.0113 273 SER A N   
2025 C CA  . SER A 274 ? 0.6169 0.5623 0.6644 -0.0365 0.0226  -0.0089 273 SER A CA  
2026 C C   . SER A 274 ? 0.5992 0.5446 0.6385 -0.0404 0.0215  -0.0103 273 SER A C   
2027 O O   . SER A 274 ? 0.5900 0.5346 0.6241 -0.0411 0.0193  -0.0083 273 SER A O   
2028 C CB  . SER A 274 ? 0.6288 0.5698 0.6729 -0.0321 0.0223  -0.0045 273 SER A CB  
2029 O OG  . SER A 274 ? 0.7609 0.7026 0.8117 -0.0284 0.0241  -0.0025 273 SER A OG  
2030 N N   . VAL A 275 ? 0.6268 0.5736 0.6652 -0.0427 0.0230  -0.0132 274 VAL A N   
2031 C CA  . VAL A 275 ? 0.6126 0.5604 0.6436 -0.0467 0.0226  -0.0137 274 VAL A CA  
2032 C C   . VAL A 275 ? 0.6632 0.6168 0.6947 -0.0497 0.0236  -0.0181 274 VAL A C   
2033 O O   . VAL A 275 ? 0.6728 0.6280 0.6973 -0.0528 0.0228  -0.0179 274 VAL A O   
2034 C CB  . VAL A 275 ? 0.5915 0.5386 0.6212 -0.0478 0.0236  -0.0136 274 VAL A CB  
2035 C CG1 . VAL A 275 ? 0.5878 0.5353 0.6098 -0.0524 0.0231  -0.0125 274 VAL A CG1 
2036 C CG2 . VAL A 275 ? 0.6290 0.5701 0.6583 -0.0442 0.0224  -0.0106 274 VAL A CG2 
2037 N N   . TYR A 276 ? 0.7313 0.6874 0.7704 -0.0486 0.0252  -0.0221 275 TYR A N   
2038 C CA  . TYR A 276 ? 0.7536 0.7142 0.7931 -0.0507 0.0262  -0.0275 275 TYR A CA  
2039 C C   . TYR A 276 ? 0.7680 0.7280 0.8135 -0.0498 0.0248  -0.0298 275 TYR A C   
2040 O O   . TYR A 276 ? 0.8048 0.7668 0.8469 -0.0519 0.0229  -0.0320 275 TYR A O   
2041 C CB  . TYR A 276 ? 0.7796 0.7436 0.8225 -0.0505 0.0296  -0.0314 275 TYR A CB  
2042 C CG  . TYR A 276 ? 0.8039 0.7720 0.8469 -0.0515 0.0310  -0.0379 275 TYR A CG  
2043 C CD1 . TYR A 276 ? 0.8196 0.7921 0.8539 -0.0547 0.0314  -0.0396 275 TYR A CD1 
2044 C CD2 . TYR A 276 ? 0.8217 0.7887 0.8728 -0.0492 0.0319  -0.0424 275 TYR A CD2 
2045 C CE1 . TYR A 276 ? 0.8437 0.8199 0.8767 -0.0551 0.0328  -0.0462 275 TYR A CE1 
2046 C CE2 . TYR A 276 ? 0.8604 0.8299 0.9108 -0.0496 0.0329  -0.0493 275 TYR A CE2 
2047 C CZ  . TYR A 276 ? 0.8635 0.8378 0.9044 -0.0524 0.0335  -0.0515 275 TYR A CZ  
2048 O OH  . TYR A 276 ? 0.8739 0.8507 0.9127 -0.0523 0.0346  -0.0590 275 TYR A OH  
2049 N N   . LEU A 277 ? 0.6302 0.5878 0.6846 -0.0470 0.0254  -0.0292 276 LEU A N   
2050 C CA  . LEU A 277 ? 0.5493 0.5061 0.6110 -0.0470 0.0243  -0.0316 276 LEU A CA  
2051 C C   . LEU A 277 ? 0.6102 0.5676 0.6713 -0.0480 0.0209  -0.0285 276 LEU A C   
2052 O O   . LEU A 277 ? 0.6154 0.5743 0.6781 -0.0502 0.0187  -0.0318 276 LEU A O   
2053 C CB  . LEU A 277 ? 0.5913 0.5452 0.6626 -0.0439 0.0259  -0.0300 276 LEU A CB  
2054 C CG  . LEU A 277 ? 0.5461 0.4980 0.6266 -0.0443 0.0248  -0.0316 276 LEU A CG  
2055 C CD1 . LEU A 277 ? 0.5521 0.5037 0.6336 -0.0458 0.0250  -0.0394 276 LEU A CD1 
2056 C CD2 . LEU A 277 ? 0.5995 0.5483 0.6882 -0.0410 0.0265  -0.0274 276 LEU A CD2 
2057 N N   . LEU A 278 ? 0.4897 0.4461 0.5486 -0.0461 0.0203  -0.0225 277 LEU A N   
2058 C CA  . LEU A 278 ? 0.5223 0.4803 0.5816 -0.0462 0.0173  -0.0193 277 LEU A CA  
2059 C C   . LEU A 278 ? 0.5687 0.5294 0.6197 -0.0493 0.0144  -0.0210 277 LEU A C   
2060 O O   . LEU A 278 ? 0.5757 0.5394 0.6295 -0.0510 0.0113  -0.0222 277 LEU A O   
2061 C CB  . LEU A 278 ? 0.5503 0.5063 0.6087 -0.0424 0.0177  -0.0129 277 LEU A CB  
2062 C CG  . LEU A 278 ? 0.5346 0.4928 0.5924 -0.0413 0.0149  -0.0088 277 LEU A CG  
2063 C CD1 . LEU A 278 ? 0.5210 0.4837 0.5896 -0.0420 0.0135  -0.0085 277 LEU A CD1 
2064 C CD2 . LEU A 278 ? 0.5210 0.4760 0.5759 -0.0366 0.0159  -0.0035 277 LEU A CD2 
2065 N N   . PRO A 279 ? 0.5492 0.5093 0.5903 -0.0503 0.0150  -0.0208 278 PRO A N   
2066 C CA  . PRO A 279 ? 0.5756 0.5384 0.6080 -0.0532 0.0123  -0.0217 278 PRO A CA  
2067 C C   . PRO A 279 ? 0.6156 0.5817 0.6471 -0.0561 0.0121  -0.0286 278 PRO A C   
2068 O O   . PRO A 279 ? 0.5662 0.5353 0.5940 -0.0580 0.0085  -0.0301 278 PRO A O   
2069 C CB  . PRO A 279 ? 0.5748 0.5355 0.5976 -0.0538 0.0137  -0.0188 278 PRO A CB  
2070 C CG  . PRO A 279 ? 0.5810 0.5395 0.6079 -0.0525 0.0173  -0.0196 278 PRO A CG  
2071 C CD  . PRO A 279 ? 0.5853 0.5423 0.6223 -0.0493 0.0175  -0.0187 278 PRO A CD  
2072 N N   . THR A 280 ? 0.6424 0.6082 0.6770 -0.0560 0.0155  -0.0333 279 THR A N   
2073 C CA  . THR A 280 ? 0.5840 0.5521 0.6171 -0.0579 0.0156  -0.0409 279 THR A CA  
2074 C C   . THR A 280 ? 0.6049 0.5725 0.6454 -0.0587 0.0120  -0.0439 279 THR A C   
2075 O O   . THR A 280 ? 0.6379 0.6077 0.6738 -0.0610 0.0090  -0.0483 279 THR A O   
2076 C CB  . THR A 280 ? 0.5766 0.5443 0.6129 -0.0566 0.0202  -0.0450 279 THR A CB  
2077 O OG1 . THR A 280 ? 0.6129 0.5818 0.6443 -0.0564 0.0231  -0.0415 279 THR A OG1 
2078 C CG2 . THR A 280 ? 0.5639 0.5339 0.5966 -0.0578 0.0208  -0.0534 279 THR A CG2 
2079 N N   . LEU A 281 ? 0.5563 0.5211 0.6081 -0.0570 0.0122  -0.0413 280 LEU A N   
2080 C CA  . LEU A 281 ? 0.5536 0.5181 0.6143 -0.0585 0.0088  -0.0432 280 LEU A CA  
2081 C C   . LEU A 281 ? 0.5896 0.5582 0.6489 -0.0601 0.0039  -0.0399 280 LEU A C   
2082 O O   . LEU A 281 ? 0.6273 0.5974 0.6912 -0.0627 -0.0002 -0.0430 280 LEU A O   
2083 C CB  . LEU A 281 ? 0.4728 0.4340 0.5459 -0.0564 0.0107  -0.0398 280 LEU A CB  
2084 C CG  . LEU A 281 ? 0.4380 0.3948 0.5152 -0.0548 0.0144  -0.0437 280 LEU A CG  
2085 C CD1 . LEU A 281 ? 0.4593 0.4128 0.5485 -0.0530 0.0156  -0.0394 280 LEU A CD1 
2086 C CD2 . LEU A 281 ? 0.4934 0.4487 0.5693 -0.0569 0.0131  -0.0528 280 LEU A CD2 
2087 N N   . SER A 282 ? 0.5556 0.5259 0.6090 -0.0585 0.0038  -0.0337 281 SER A N   
2088 C CA  . SER A 282 ? 0.6029 0.5775 0.6547 -0.0592 -0.0011 -0.0303 281 SER A CA  
2089 C C   . SER A 282 ? 0.6074 0.5849 0.6484 -0.0622 -0.0045 -0.0347 281 SER A C   
2090 O O   . SER A 282 ? 0.6157 0.5974 0.6577 -0.0639 -0.0099 -0.0348 281 SER A O   
2091 C CB  . SER A 282 ? 0.5436 0.5176 0.5919 -0.0559 -0.0002 -0.0225 281 SER A CB  
2092 O OG  . SER A 282 ? 0.6087 0.5804 0.6448 -0.0560 0.0017  -0.0223 281 SER A OG  
2093 N N   . ARG A 283 ? 0.6141 0.5903 0.6449 -0.0629 -0.0017 -0.0383 282 ARG A N   
2094 C CA  . ARG A 283 ? 0.6228 0.6023 0.6419 -0.0654 -0.0043 -0.0426 282 ARG A CA  
2095 C C   . ARG A 283 ? 0.7034 0.6831 0.7254 -0.0677 -0.0065 -0.0515 282 ARG A C   
2096 O O   . ARG A 283 ? 0.7237 0.7068 0.7386 -0.0699 -0.0111 -0.0551 282 ARG A O   
2097 C CB  . ARG A 283 ? 0.7029 0.6822 0.7105 -0.0654 0.0003  -0.0430 282 ARG A CB  
2098 C CG  . ARG A 283 ? 0.6670 0.6443 0.6718 -0.0638 0.0025  -0.0348 282 ARG A CG  
2099 C CD  . ARG A 283 ? 0.7756 0.7549 0.7658 -0.0655 0.0023  -0.0322 282 ARG A CD  
2100 N NE  . ARG A 283 ? 0.8285 0.8105 0.8116 -0.0671 0.0063  -0.0375 282 ARG A NE  
2101 C CZ  . ARG A 283 ? 0.8033 0.7854 0.7816 -0.0677 0.0109  -0.0351 282 ARG A CZ  
2102 N NH1 . ARG A 283 ? 0.8129 0.7911 0.7922 -0.0671 0.0117  -0.0280 282 ARG A NH1 
2103 N NH2 . ARG A 283 ? 0.8012 0.7876 0.7737 -0.0689 0.0148  -0.0402 282 ARG A NH2 
2104 N N   . LEU A 284 ? 0.6655 0.6412 0.6973 -0.0670 -0.0038 -0.0552 283 LEU A N   
2105 C CA  . LEU A 284 ? 0.6122 0.5858 0.6474 -0.0689 -0.0059 -0.0641 283 LEU A CA  
2106 C C   . LEU A 284 ? 0.6566 0.6315 0.7016 -0.0715 -0.0122 -0.0634 283 LEU A C   
2107 O O   . LEU A 284 ? 0.7143 0.6891 0.7710 -0.0707 -0.0121 -0.0571 283 LEU A O   
2108 C CB  . LEU A 284 ? 0.5912 0.5591 0.6345 -0.0670 -0.0011 -0.0674 283 LEU A CB  
2109 C CG  . LEU A 284 ? 0.5898 0.5578 0.6253 -0.0646 0.0050  -0.0693 283 LEU A CG  
2110 C CD1 . LEU A 284 ? 0.6105 0.5732 0.6551 -0.0622 0.0089  -0.0730 283 LEU A CD1 
2111 C CD2 . LEU A 284 ? 0.6040 0.5757 0.6253 -0.0658 0.0046  -0.0757 283 LEU A CD2 
2112 N N   . THR A 285 ? 0.7079 0.6846 0.7481 -0.0746 -0.0178 -0.0697 284 THR A N   
2113 C CA  . THR A 285 ? 0.7607 0.7398 0.8103 -0.0779 -0.0248 -0.0697 284 THR A CA  
2114 C C   . THR A 285 ? 0.8184 0.7921 0.8739 -0.0809 -0.0277 -0.0791 284 THR A C   
2115 O O   . THR A 285 ? 0.8473 0.8224 0.9128 -0.0846 -0.0337 -0.0795 284 THR A O   
2116 C CB  . THR A 285 ? 0.7670 0.7533 0.8067 -0.0794 -0.0309 -0.0684 284 THR A CB  
2117 O OG1 . THR A 285 ? 0.6732 0.6593 0.6968 -0.0800 -0.0314 -0.0762 284 THR A OG1 
2118 C CG2 . THR A 285 ? 0.7279 0.7183 0.7639 -0.0764 -0.0288 -0.0582 284 THR A CG2 
2119 N N   . GLU A 286 ? 0.8397 0.8072 0.8900 -0.0795 -0.0238 -0.0868 285 GLU A N   
2120 C CA  . GLU A 286 ? 0.8602 0.8204 0.9152 -0.0816 -0.0263 -0.0965 285 GLU A CA  
2121 C C   . GLU A 286 ? 0.8441 0.7966 0.9119 -0.0796 -0.0213 -0.0952 285 GLU A C   
2122 O O   . GLU A 286 ? 0.8413 0.7934 0.9076 -0.0755 -0.0145 -0.0916 285 GLU A O   
2123 C CB  . GLU A 286 ? 0.9231 0.8816 0.9623 -0.0806 -0.0259 -0.1073 285 GLU A CB  
2124 C CG  . GLU A 286 ? 0.9868 0.9493 1.0159 -0.0841 -0.0337 -0.1130 285 GLU A CG  
2125 C CD  . GLU A 286 ? 1.0851 1.0441 1.1263 -0.0891 -0.0418 -0.1167 285 GLU A CD  
2126 O OE1 . GLU A 286 ? 1.0867 1.0368 1.1396 -0.0897 -0.0410 -0.1202 285 GLU A OE1 
2127 O OE2 . GLU A 286 ? 1.0708 1.0362 1.1102 -0.0927 -0.0493 -0.1159 285 GLU A OE2 
2128 N N   . LYS A 287 ? 0.8130 0.7595 0.8938 -0.0828 -0.0250 -0.0979 286 LYS A N   
2129 C CA  . LYS A 287 ? 0.7489 0.6873 0.8422 -0.0811 -0.0208 -0.0960 286 LYS A CA  
2130 C C   . LYS A 287 ? 0.7248 0.6559 0.8117 -0.0770 -0.0160 -0.1039 286 LYS A C   
2131 O O   . LYS A 287 ? 0.7457 0.6720 0.8397 -0.0736 -0.0109 -0.1008 286 LYS A O   
2132 C CB  . LYS A 287 ? 0.6959 0.6289 0.8044 -0.0862 -0.0263 -0.0970 286 LYS A CB  
2133 C CG  . LYS A 287 ? 0.6699 0.6106 0.7904 -0.0892 -0.0286 -0.0864 286 LYS A CG  
2134 C CD  . LYS A 287 ? 0.7054 0.6401 0.8442 -0.0935 -0.0310 -0.0844 286 LYS A CD  
2135 C CE  . LYS A 287 ? 0.7059 0.6442 0.8513 -0.1006 -0.0400 -0.0869 286 LYS A CE  
2136 N NZ  . LYS A 287 ? 0.7090 0.6364 0.8667 -0.1057 -0.0439 -0.0920 286 LYS A NZ  
2137 N N   . ARG A 288 ? 0.7508 0.6815 0.8243 -0.0766 -0.0174 -0.1140 287 ARG A N   
2138 C CA  . ARG A 288 ? 0.7561 0.6817 0.8233 -0.0718 -0.0123 -0.1217 287 ARG A CA  
2139 C C   . ARG A 288 ? 0.7500 0.6820 0.8119 -0.0671 -0.0047 -0.1156 287 ARG A C   
2140 O O   . ARG A 288 ? 0.7033 0.6314 0.7696 -0.0629 0.0007  -0.1157 287 ARG A O   
2141 C CB  . ARG A 288 ? 0.7962 0.7214 0.8489 -0.0723 -0.0154 -0.1338 287 ARG A CB  
2142 C CG  . ARG A 288 ? 0.7437 0.6645 0.7991 -0.0780 -0.0245 -0.1398 287 ARG A CG  
2143 C CD  . ARG A 288 ? 0.7761 0.6976 0.8141 -0.0778 -0.0275 -0.1518 287 ARG A CD  
2144 N NE  . ARG A 288 ? 0.8479 0.7605 0.8884 -0.0820 -0.0357 -0.1619 287 ARG A NE  
2145 C CZ  . ARG A 288 ? 0.8603 0.7597 0.9121 -0.0824 -0.0370 -0.1672 287 ARG A CZ  
2146 N NH1 . ARG A 288 ? 0.8052 0.6985 0.8661 -0.0781 -0.0304 -0.1639 287 ARG A NH1 
2147 N NH2 . ARG A 288 ? 0.8511 0.7425 0.9047 -0.0873 -0.0455 -0.1760 287 ARG A NH2 
2148 N N   . ASP A 289 ? 0.8880 0.8296 0.9406 -0.0679 -0.0045 -0.1102 288 ASP A N   
2149 C CA  . ASP A 289 ? 0.8622 0.8096 0.9102 -0.0645 0.0019  -0.1039 288 ASP A CA  
2150 C C   . ASP A 289 ? 0.8362 0.7827 0.8963 -0.0635 0.0041  -0.0936 288 ASP A C   
2151 O O   . ASP A 289 ? 0.8588 0.8066 0.9194 -0.0600 0.0096  -0.0900 288 ASP A O   
2152 C CB  . ASP A 289 ? 0.8597 0.8160 0.8940 -0.0659 0.0010  -0.1009 288 ASP A CB  
2153 C CG  . ASP A 289 ? 0.9787 0.9367 1.0001 -0.0674 -0.0024 -0.1103 288 ASP A CG  
2154 O OD1 . ASP A 289 ? 0.9655 0.9224 0.9799 -0.0647 0.0012  -0.1184 288 ASP A OD1 
2155 O OD2 . ASP A 289 ? 1.0001 0.9609 1.0179 -0.0710 -0.0087 -0.1096 288 ASP A OD2 
2156 N N   . ILE A 290 ? 0.7368 0.6822 0.8068 -0.0664 -0.0002 -0.0887 289 ILE A N   
2157 C CA  . ILE A 290 ? 0.6708 0.6154 0.7519 -0.0651 0.0022  -0.0793 289 ILE A CA  
2158 C C   . ILE A 290 ? 0.6444 0.5810 0.7346 -0.0623 0.0055  -0.0811 289 ILE A C   
2159 O O   . ILE A 290 ? 0.6181 0.5547 0.7115 -0.0589 0.0100  -0.0754 289 ILE A O   
2160 C CB  . ILE A 290 ? 0.6843 0.6310 0.7744 -0.0687 -0.0028 -0.0737 289 ILE A CB  
2161 C CG1 . ILE A 290 ? 0.6624 0.6176 0.7451 -0.0691 -0.0042 -0.0676 289 ILE A CG1 
2162 C CG2 . ILE A 290 ? 0.6644 0.6077 0.7685 -0.0676 -0.0005 -0.0665 289 ILE A CG2 
2163 C CD1 . ILE A 290 ? 0.6224 0.5819 0.7129 -0.0726 -0.0097 -0.0635 289 ILE A CD1 
2164 N N   . THR A 291 ? 0.6233 0.5525 0.7174 -0.0636 0.0030  -0.0892 290 THR A N   
2165 C CA  . THR A 291 ? 0.6438 0.5642 0.7464 -0.0606 0.0058  -0.0912 290 THR A CA  
2166 C C   . THR A 291 ? 0.6299 0.5517 0.7254 -0.0551 0.0115  -0.0944 290 THR A C   
2167 O O   . THR A 291 ? 0.6100 0.5290 0.7120 -0.0513 0.0153  -0.0910 290 THR A O   
2168 C CB  . THR A 291 ? 0.6912 0.6018 0.7984 -0.0632 0.0013  -0.1001 290 THR A CB  
2169 O OG1 . THR A 291 ? 0.7308 0.6429 0.8424 -0.0692 -0.0049 -0.0983 290 THR A OG1 
2170 C CG2 . THR A 291 ? 0.6871 0.5872 0.8066 -0.0609 0.0031  -0.0990 290 THR A CG2 
2171 N N   . ARG A 292 ? 0.6289 0.5561 0.7116 -0.0548 0.0122  -0.1005 291 ARG A N   
2172 C CA  . ARG A 292 ? 0.6294 0.5602 0.7061 -0.0500 0.0180  -0.1032 291 ARG A CA  
2173 C C   . ARG A 292 ? 0.5792 0.5167 0.6562 -0.0484 0.0218  -0.0934 291 ARG A C   
2174 O O   . ARG A 292 ? 0.5547 0.4928 0.6349 -0.0443 0.0261  -0.0924 291 ARG A O   
2175 C CB  . ARG A 292 ? 0.6366 0.5728 0.6988 -0.0504 0.0181  -0.1111 291 ARG A CB  
2176 C CG  . ARG A 292 ? 0.6335 0.5705 0.6918 -0.0452 0.0233  -0.1188 291 ARG A CG  
2177 C CD  . ARG A 292 ? 0.6883 0.6151 0.7488 -0.0436 0.0211  -0.1299 291 ARG A CD  
2178 N NE  . ARG A 292 ? 0.6869 0.6131 0.7480 -0.0371 0.0266  -0.1359 291 ARG A NE  
2179 C CZ  . ARG A 292 ? 0.6374 0.5535 0.7019 -0.0338 0.0260  -0.1453 291 ARG A CZ  
2180 N NH1 . ARG A 292 ? 0.6164 0.5214 0.6840 -0.0370 0.0198  -0.1500 291 ARG A NH1 
2181 N NH2 . ARG A 292 ? 0.6716 0.5887 0.7370 -0.0269 0.0314  -0.1499 291 ARG A NH2 
2182 N N   . GLU A 293 ? 0.5443 0.4867 0.6184 -0.0515 0.0198  -0.0863 292 GLU A N   
2183 C CA  . GLU A 293 ? 0.5889 0.5364 0.6622 -0.0502 0.0227  -0.0777 292 GLU A CA  
2184 C C   . GLU A 293 ? 0.5907 0.5336 0.6755 -0.0481 0.0237  -0.0713 292 GLU A C   
2185 O O   . GLU A 293 ? 0.5251 0.4700 0.6110 -0.0451 0.0271  -0.0674 292 GLU A O   
2186 C CB  . GLU A 293 ? 0.5938 0.5464 0.6601 -0.0535 0.0200  -0.0724 292 GLU A CB  
2187 C CG  . GLU A 293 ? 0.6418 0.5994 0.7030 -0.0524 0.0229  -0.0656 292 GLU A CG  
2188 C CD  . GLU A 293 ? 0.7238 0.6869 0.7755 -0.0520 0.0263  -0.0693 292 GLU A CD  
2189 O OE1 . GLU A 293 ? 0.8143 0.7805 0.8566 -0.0541 0.0250  -0.0735 292 GLU A OE1 
2190 O OE2 . GLU A 293 ? 0.6590 0.6240 0.7125 -0.0496 0.0303  -0.0678 292 GLU A OE2 
2191 N N   . VAL A 294 ? 0.5822 0.5197 0.6759 -0.0498 0.0206  -0.0699 293 VAL A N   
2192 C CA  . VAL A 294 ? 0.4988 0.4323 0.6030 -0.0479 0.0217  -0.0631 293 VAL A CA  
2193 C C   . VAL A 294 ? 0.5498 0.4779 0.6591 -0.0437 0.0246  -0.0664 293 VAL A C   
2194 O O   . VAL A 294 ? 0.6269 0.5551 0.7398 -0.0403 0.0273  -0.0611 293 VAL A O   
2195 C CB  . VAL A 294 ? 0.5383 0.4682 0.6514 -0.0514 0.0179  -0.0604 293 VAL A CB  
2196 C CG1 . VAL A 294 ? 0.5633 0.4874 0.6879 -0.0493 0.0195  -0.0549 293 VAL A CG1 
2197 C CG2 . VAL A 294 ? 0.5002 0.4368 0.6104 -0.0538 0.0160  -0.0542 293 VAL A CG2 
2198 N N   . VAL A 295 ? 0.5712 0.4944 0.6807 -0.0435 0.0238  -0.0754 294 VAL A N   
2199 C CA  . VAL A 295 ? 0.5469 0.4649 0.6615 -0.0387 0.0264  -0.0791 294 VAL A CA  
2200 C C   . VAL A 295 ? 0.5667 0.4924 0.6758 -0.0347 0.0308  -0.0793 294 VAL A C   
2201 O O   . VAL A 295 ? 0.5392 0.4641 0.6538 -0.0304 0.0333  -0.0765 294 VAL A O   
2202 C CB  . VAL A 295 ? 0.4907 0.4011 0.6057 -0.0390 0.0244  -0.0898 294 VAL A CB  
2203 C CG1 . VAL A 295 ? 0.4317 0.3386 0.5491 -0.0328 0.0278  -0.0952 294 VAL A CG1 
2204 C CG2 . VAL A 295 ? 0.4683 0.3692 0.5927 -0.0428 0.0200  -0.0886 294 VAL A CG2 
2205 N N   . LYS A 296 ? 0.5397 0.4736 0.6382 -0.0364 0.0316  -0.0818 295 LYS A N   
2206 C CA  . LYS A 296 ? 0.5514 0.4937 0.6454 -0.0337 0.0358  -0.0814 295 LYS A CA  
2207 C C   . LYS A 296 ? 0.5440 0.4893 0.6407 -0.0331 0.0366  -0.0718 295 LYS A C   
2208 O O   . LYS A 296 ? 0.5253 0.4743 0.6246 -0.0295 0.0394  -0.0704 295 LYS A O   
2209 C CB  . LYS A 296 ? 0.5068 0.4569 0.5887 -0.0365 0.0363  -0.0848 295 LYS A CB  
2210 C CG  . LYS A 296 ? 0.5798 0.5398 0.6572 -0.0358 0.0401  -0.0814 295 LYS A CG  
2211 C CD  . LYS A 296 ? 0.6326 0.6001 0.6988 -0.0374 0.0420  -0.0865 295 LYS A CD  
2212 C CE  . LYS A 296 ? 0.6522 0.6216 0.7092 -0.0425 0.0390  -0.0829 295 LYS A CE  
2213 N NZ  . LYS A 296 ? 0.6681 0.6469 0.7162 -0.0443 0.0419  -0.0802 295 LYS A NZ  
2214 N N   . SER A 297 ? 0.5619 0.5062 0.6581 -0.0361 0.0340  -0.0653 296 SER A N   
2215 C CA  . SER A 297 ? 0.5414 0.4874 0.6389 -0.0351 0.0346  -0.0568 296 SER A CA  
2216 C C   . SER A 297 ? 0.5392 0.4800 0.6464 -0.0311 0.0353  -0.0537 296 SER A C   
2217 O O   . SER A 297 ? 0.5525 0.4959 0.6607 -0.0283 0.0368  -0.0497 296 SER A O   
2218 C CB  . SER A 297 ? 0.5246 0.4704 0.6193 -0.0383 0.0319  -0.0511 296 SER A CB  
2219 O OG  . SER A 297 ? 0.5682 0.5184 0.6538 -0.0417 0.0308  -0.0535 296 SER A OG  
2220 N N   . LEU A 298 ? 0.5322 0.4654 0.6465 -0.0310 0.0340  -0.0554 297 LEU A N   
2221 C CA  . LEU A 298 ? 0.5365 0.4639 0.6600 -0.0272 0.0346  -0.0520 297 LEU A CA  
2222 C C   . LEU A 298 ? 0.5646 0.4930 0.6904 -0.0222 0.0370  -0.0563 297 LEU A C   
2223 O O   . LEU A 298 ? 0.5572 0.4845 0.6881 -0.0182 0.0379  -0.0519 297 LEU A O   
2224 C CB  . LEU A 298 ? 0.5100 0.4281 0.6410 -0.0290 0.0324  -0.0529 297 LEU A CB  
2225 C CG  . LEU A 298 ? 0.5639 0.4816 0.6969 -0.0329 0.0304  -0.0461 297 LEU A CG  
2226 C CD1 . LEU A 298 ? 0.5386 0.4479 0.6802 -0.0357 0.0279  -0.0476 297 LEU A CD1 
2227 C CD2 . LEU A 298 ? 0.5351 0.4545 0.6698 -0.0302 0.0319  -0.0365 297 LEU A CD2 
2228 N N   . LYS A 299 ? 0.5475 0.4788 0.6694 -0.0221 0.0382  -0.0647 298 LYS A N   
2229 C CA  . LYS A 299 ? 0.5431 0.4774 0.6676 -0.0169 0.0410  -0.0691 298 LYS A CA  
2230 C C   . LYS A 299 ? 0.5378 0.4821 0.6606 -0.0153 0.0429  -0.0645 298 LYS A C   
2231 O O   . LYS A 299 ? 0.5545 0.5017 0.6823 -0.0104 0.0447  -0.0654 298 LYS A O   
2232 C CB  . LYS A 299 ? 0.6355 0.5721 0.7549 -0.0170 0.0423  -0.0792 298 LYS A CB  
2233 C CG  . LYS A 299 ? 0.6071 0.5335 0.7318 -0.0141 0.0417  -0.0867 298 LYS A CG  
2234 C CD  . LYS A 299 ? 0.5934 0.5226 0.7106 -0.0142 0.0430  -0.0972 298 LYS A CD  
2235 C CE  . LYS A 299 ? 0.6366 0.5551 0.7526 -0.0175 0.0391  -0.1030 298 LYS A CE  
2236 N NZ  . LYS A 299 ? 0.6716 0.5934 0.7776 -0.0181 0.0399  -0.1131 298 LYS A NZ  
2237 N N   . PHE A 300 ? 0.5766 0.5258 0.6926 -0.0193 0.0421  -0.0598 299 PHE A N   
2238 C CA  . PHE A 300 ? 0.6100 0.5677 0.7237 -0.0190 0.0432  -0.0558 299 PHE A CA  
2239 C C   . PHE A 300 ? 0.5932 0.5483 0.7089 -0.0179 0.0414  -0.0475 299 PHE A C   
2240 O O   . PHE A 300 ? 0.5445 0.5033 0.6634 -0.0148 0.0417  -0.0448 299 PHE A O   
2241 C CB  . PHE A 300 ? 0.6462 0.6104 0.7501 -0.0240 0.0434  -0.0562 299 PHE A CB  
2242 C CG  . PHE A 300 ? 0.6842 0.6543 0.7851 -0.0253 0.0432  -0.0507 299 PHE A CG  
2243 C CD1 . PHE A 300 ? 0.6623 0.6408 0.7662 -0.0235 0.0451  -0.0513 299 PHE A CD1 
2244 C CD2 . PHE A 300 ? 0.6671 0.6345 0.7627 -0.0282 0.0409  -0.0450 299 PHE A CD2 
2245 C CE1 . PHE A 300 ? 0.6369 0.6202 0.7384 -0.0254 0.0442  -0.0465 299 PHE A CE1 
2246 C CE2 . PHE A 300 ? 0.6739 0.6450 0.7662 -0.0294 0.0401  -0.0406 299 PHE A CE2 
2247 C CZ  . PHE A 300 ? 0.6512 0.6300 0.7464 -0.0284 0.0415  -0.0414 299 PHE A CZ  
2248 N N   . VAL A 301 ? 0.6244 0.5739 0.7382 -0.0203 0.0395  -0.0434 300 VAL A N   
2249 C CA  . VAL A 301 ? 0.6292 0.5771 0.7428 -0.0192 0.0382  -0.0356 300 VAL A CA  
2250 C C   . VAL A 301 ? 0.6431 0.5860 0.7649 -0.0145 0.0383  -0.0326 300 VAL A C   
2251 O O   . VAL A 301 ? 0.6789 0.6228 0.8006 -0.0118 0.0377  -0.0272 300 VAL A O   
2252 C CB  . VAL A 301 ? 0.6302 0.5752 0.7396 -0.0226 0.0367  -0.0320 300 VAL A CB  
2253 C CG1 . VAL A 301 ? 0.6640 0.6134 0.7651 -0.0268 0.0364  -0.0346 300 VAL A CG1 
2254 C CG2 . VAL A 301 ? 0.6424 0.5807 0.7579 -0.0233 0.0361  -0.0325 300 VAL A CG2 
2255 N N   . LEU A 302 ? 0.6088 0.5456 0.7371 -0.0133 0.0386  -0.0359 301 LEU A N   
2256 C CA  . LEU A 302 ? 0.5739 0.5046 0.7101 -0.0090 0.0385  -0.0321 301 LEU A CA  
2257 C C   . LEU A 302 ? 0.5803 0.5155 0.7195 -0.0037 0.0391  -0.0323 301 LEU A C   
2258 O O   . LEU A 302 ? 0.6108 0.5453 0.7515 -0.0005 0.0383  -0.0258 301 LEU A O   
2259 C CB  . LEU A 302 ? 0.5380 0.4597 0.6808 -0.0094 0.0382  -0.0358 301 LEU A CB  
2260 C CG  . LEU A 302 ? 0.5328 0.4492 0.6761 -0.0141 0.0368  -0.0327 301 LEU A CG  
2261 C CD1 . LEU A 302 ? 0.5099 0.4164 0.6608 -0.0148 0.0358  -0.0366 301 LEU A CD1 
2262 C CD2 . LEU A 302 ? 0.5102 0.4262 0.6540 -0.0132 0.0368  -0.0227 301 LEU A CD2 
2263 N N   . PRO A 303 ? 0.6036 0.5442 0.7439 -0.0024 0.0405  -0.0390 302 PRO A N   
2264 C CA  . PRO A 303 ? 0.5904 0.5377 0.7344 0.0025  0.0409  -0.0384 302 PRO A CA  
2265 C C   . PRO A 303 ? 0.5832 0.5387 0.7216 0.0008  0.0398  -0.0340 302 PRO A C   
2266 O O   . PRO A 303 ? 0.5642 0.5237 0.7056 0.0046  0.0387  -0.0306 302 PRO A O   
2267 C CB  . PRO A 303 ? 0.5356 0.4881 0.6818 0.0038  0.0433  -0.0470 302 PRO A CB  
2268 C CG  . PRO A 303 ? 0.5722 0.5169 0.7168 0.0010  0.0437  -0.0524 302 PRO A CG  
2269 C CD  . PRO A 303 ? 0.5708 0.5123 0.7093 -0.0046 0.0419  -0.0476 302 PRO A CD  
2270 N N   . ALA A 304 ? 0.6044 0.5621 0.7347 -0.0047 0.0396  -0.0340 303 ALA A N   
2271 C CA  . ALA A 304 ? 0.6007 0.5644 0.7251 -0.0066 0.0381  -0.0304 303 ALA A CA  
2272 C C   . ALA A 304 ? 0.6654 0.6245 0.7881 -0.0045 0.0359  -0.0232 303 ALA A C   
2273 O O   . ALA A 304 ? 0.6247 0.5879 0.7470 -0.0023 0.0342  -0.0202 303 ALA A O   
2274 C CB  . ALA A 304 ? 0.5853 0.5506 0.7012 -0.0126 0.0383  -0.0319 303 ALA A CB  
2275 N N   . VAL A 305 ? 0.6938 0.6451 0.8153 -0.0051 0.0360  -0.0202 304 VAL A N   
2276 C CA  . VAL A 305 ? 0.6887 0.6363 0.8079 -0.0027 0.0347  -0.0130 304 VAL A CA  
2277 C C   . VAL A 305 ? 0.6886 0.6345 0.8147 0.0030  0.0343  -0.0100 304 VAL A C   
2278 O O   . VAL A 305 ? 0.6732 0.6197 0.7965 0.0060  0.0327  -0.0047 304 VAL A O   
2279 C CB  . VAL A 305 ? 0.7086 0.6500 0.8263 -0.0049 0.0354  -0.0100 304 VAL A CB  
2280 C CG1 . VAL A 305 ? 0.6706 0.6059 0.7968 -0.0047 0.0366  -0.0115 304 VAL A CG1 
2281 C CG2 . VAL A 305 ? 0.6766 0.6160 0.7900 -0.0025 0.0348  -0.0025 304 VAL A CG2 
2282 N N   . ALA A 306 ? 0.6283 0.5718 0.7627 0.0049  0.0355  -0.0135 305 ALA A N   
2283 C CA  . ALA A 306 ? 0.6236 0.5647 0.7649 0.0109  0.0349  -0.0105 305 ALA A CA  
2284 C C   . ALA A 306 ? 0.6387 0.5889 0.7808 0.0141  0.0333  -0.0110 305 ALA A C   
2285 O O   . ALA A 306 ? 0.6709 0.6214 0.8140 0.0185  0.0314  -0.0057 305 ALA A O   
2286 C CB  . ALA A 306 ? 0.5441 0.4790 0.6940 0.0124  0.0363  -0.0149 305 ALA A CB  
2287 N N   . ALA A 307 ? 0.5993 0.5578 0.7411 0.0116  0.0340  -0.0170 306 ALA A N   
2288 C CA  . ALA A 307 ? 0.6031 0.5720 0.7467 0.0136  0.0323  -0.0172 306 ALA A CA  
2289 C C   . ALA A 307 ? 0.6362 0.6072 0.7715 0.0118  0.0292  -0.0125 306 ALA A C   
2290 O O   . ALA A 307 ? 0.6701 0.6454 0.8067 0.0153  0.0263  -0.0093 306 ALA A O   
2291 C CB  . ALA A 307 ? 0.5385 0.5165 0.6841 0.0107  0.0343  -0.0241 306 ALA A CB  
2292 N N   . ALA A 308 ? 0.6535 0.6215 0.7801 0.0068  0.0294  -0.0122 307 ALA A N   
2293 C CA  . ALA A 308 ? 0.6565 0.6249 0.7741 0.0056  0.0265  -0.0084 307 ALA A CA  
2294 C C   . ALA A 308 ? 0.7005 0.6634 0.8158 0.0103  0.0251  -0.0018 307 ALA A C   
2295 O O   . ALA A 308 ? 0.6695 0.6348 0.7803 0.0123  0.0218  0.0011  307 ALA A O   
2296 C CB  . ALA A 308 ? 0.5843 0.5496 0.6935 0.0001  0.0273  -0.0095 307 ALA A CB  
2297 N N   . SER A 309 ? 0.7837 0.7391 0.9017 0.0120  0.0274  0.0007  308 SER A N   
2298 C CA  . SER A 309 ? 0.7365 0.6870 0.8525 0.0164  0.0268  0.0079  308 SER A CA  
2299 C C   . SER A 309 ? 0.6962 0.6497 0.8176 0.0221  0.0246  0.0102  308 SER A C   
2300 O O   . SER A 309 ? 0.7209 0.6751 0.8370 0.0256  0.0220  0.0153  308 SER A O   
2301 C CB  . SER A 309 ? 0.7197 0.6621 0.8396 0.0161  0.0299  0.0106  308 SER A CB  
2302 O OG  . SER A 309 ? 0.7447 0.6856 0.8607 0.0110  0.0316  0.0084  308 SER A OG  
2303 N N   . PHE A 310 ? 0.6217 0.5774 0.7534 0.0237  0.0253  0.0064  309 PHE A N   
2304 C CA  . PHE A 310 ? 0.6146 0.5736 0.7525 0.0299  0.0230  0.0087  309 PHE A CA  
2305 C C   . PHE A 310 ? 0.6387 0.6073 0.7725 0.0303  0.0188  0.0088  309 PHE A C   
2306 O O   . PHE A 310 ? 0.6680 0.6376 0.7998 0.0349  0.0156  0.0140  309 PHE A O   
2307 C CB  . PHE A 310 ? 0.5833 0.5437 0.7328 0.0319  0.0248  0.0034  309 PHE A CB  
2308 C CG  . PHE A 310 ? 0.6140 0.5760 0.7716 0.0394  0.0228  0.0063  309 PHE A CG  
2309 C CD1 . PHE A 310 ? 0.6053 0.5589 0.7627 0.0439  0.0220  0.0140  309 PHE A CD1 
2310 C CD2 . PHE A 310 ? 0.6259 0.5982 0.7915 0.0420  0.0219  0.0021  309 PHE A CD2 
2311 C CE1 . PHE A 310 ? 0.6313 0.5858 0.7958 0.0511  0.0198  0.0173  309 PHE A CE1 
2312 C CE2 . PHE A 310 ? 0.6134 0.5876 0.7870 0.0496  0.0198  0.0050  309 PHE A CE2 
2313 C CZ  . PHE A 310 ? 0.6277 0.5924 0.8004 0.0543  0.0185  0.0127  309 PHE A CZ  
2314 N N   . THR A 311 ? 0.5928 0.5684 0.7250 0.0252  0.0185  0.0034  310 THR A N   
2315 C CA  . THR A 311 ? 0.5975 0.5820 0.7267 0.0244  0.0140  0.0031  310 THR A CA  
2316 C C   . THR A 311 ? 0.6434 0.6236 0.7599 0.0245  0.0110  0.0076  310 THR A C   
2317 O O   . THR A 311 ? 0.5964 0.5815 0.7102 0.0266  0.0062  0.0095  310 THR A O   
2318 C CB  . THR A 311 ? 0.5922 0.5838 0.7221 0.0179  0.0148  -0.0029 310 THR A CB  
2319 O OG1 . THR A 311 ? 0.7171 0.7019 0.8387 0.0128  0.0171  -0.0041 310 THR A OG1 
2320 C CG2 . THR A 311 ? 0.5530 0.5508 0.6950 0.0188  0.0180  -0.0076 310 THR A CG2 
2321 N N   . VAL A 312 ? 0.6293 0.6010 0.7380 0.0225  0.0136  0.0092  311 VAL A N   
2322 C CA  . VAL A 312 ? 0.6114 0.5787 0.7078 0.0240  0.0116  0.0137  311 VAL A CA  
2323 C C   . VAL A 312 ? 0.6719 0.6372 0.7686 0.0309  0.0105  0.0204  311 VAL A C   
2324 O O   . VAL A 312 ? 0.6781 0.6442 0.7661 0.0338  0.0068  0.0236  311 VAL A O   
2325 C CB  . VAL A 312 ? 0.6030 0.5629 0.6926 0.0209  0.0153  0.0141  311 VAL A CB  
2326 C CG1 . VAL A 312 ? 0.6295 0.5847 0.7075 0.0242  0.0146  0.0196  311 VAL A CG1 
2327 C CG2 . VAL A 312 ? 0.6335 0.5951 0.7199 0.0146  0.0151  0.0084  311 VAL A CG2 
2328 N N   . TRP A 313 ? 0.6339 0.5959 0.7400 0.0336  0.0134  0.0226  312 TRP A N   
2329 C CA  . TRP A 313 ? 0.5775 0.5371 0.6849 0.0402  0.0124  0.0297  312 TRP A CA  
2330 C C   . TRP A 313 ? 0.6042 0.5722 0.7150 0.0442  0.0071  0.0297  312 TRP A C   
2331 O O   . TRP A 313 ? 0.6297 0.5979 0.7348 0.0491  0.0038  0.0355  312 TRP A O   
2332 C CB  . TRP A 313 ? 0.5557 0.5085 0.6732 0.0417  0.0163  0.0317  312 TRP A CB  
2333 C CG  . TRP A 313 ? 0.5838 0.5325 0.7027 0.0482  0.0155  0.0400  312 TRP A CG  
2334 C CD1 . TRP A 313 ? 0.6065 0.5500 0.7174 0.0503  0.0166  0.0482  312 TRP A CD1 
2335 C CD2 . TRP A 313 ? 0.5815 0.5312 0.7104 0.0538  0.0136  0.0417  312 TRP A CD2 
2336 N NE1 . TRP A 313 ? 0.6063 0.5470 0.7210 0.0565  0.0154  0.0552  312 TRP A NE1 
2337 C CE2 . TRP A 313 ? 0.5638 0.5078 0.6897 0.0589  0.0133  0.0513  312 TRP A CE2 
2338 C CE3 . TRP A 313 ? 0.5903 0.5456 0.7303 0.0555  0.0124  0.0361  312 TRP A CE3 
2339 C CZ2 . TRP A 313 ? 0.5699 0.5126 0.7035 0.0655  0.0113  0.0557  312 TRP A CZ2 
2340 C CZ3 . TRP A 313 ? 0.5690 0.5236 0.7173 0.0625  0.0106  0.0399  312 TRP A CZ3 
2341 C CH2 . TRP A 313 ? 0.5669 0.5146 0.7119 0.0674  0.0098  0.0497  312 TRP A CH2 
2342 N N   . LEU A 314 ? 0.6025 0.5783 0.7225 0.0424  0.0061  0.0236  313 LEU A N   
2343 C CA  . LEU A 314 ? 0.5787 0.5646 0.7033 0.0457  0.0008  0.0235  313 LEU A CA  
2344 C C   . LEU A 314 ? 0.6313 0.6217 0.7446 0.0437  -0.0046 0.0233  313 LEU A C   
2345 O O   . LEU A 314 ? 0.6251 0.6220 0.7385 0.0475  -0.0102 0.0255  313 LEU A O   
2346 C CB  . LEU A 314 ? 0.5908 0.5857 0.7285 0.0440  0.0018  0.0170  313 LEU A CB  
2347 C CG  . LEU A 314 ? 0.5840 0.5744 0.7316 0.0445  0.0074  0.0141  313 LEU A CG  
2348 C CD1 . LEU A 314 ? 0.5598 0.5596 0.7152 0.0405  0.0093  0.0064  313 LEU A CD1 
2349 C CD2 . LEU A 314 ? 0.5539 0.5415 0.7102 0.0526  0.0071  0.0183  313 LEU A CD2 
2350 N N   . LEU A 315 ? 0.6443 0.6311 0.7481 0.0380  -0.0035 0.0204  314 LEU A N   
2351 C CA  . LEU A 315 ? 0.6279 0.6166 0.7201 0.0357  -0.0087 0.0193  314 LEU A CA  
2352 C C   . LEU A 315 ? 0.6756 0.6551 0.7524 0.0377  -0.0080 0.0234  314 LEU A C   
2353 O O   . LEU A 315 ? 0.6813 0.6586 0.7467 0.0348  -0.0102 0.0211  314 LEU A O   
2354 C CB  . LEU A 315 ? 0.6666 0.6584 0.7593 0.0278  -0.0086 0.0126  314 LEU A CB  
2355 C CG  . LEU A 315 ? 0.7236 0.7274 0.8232 0.0249  -0.0139 0.0090  314 LEU A CG  
2356 C CD1 . LEU A 315 ? 0.6149 0.6278 0.7314 0.0270  -0.0120 0.0080  314 LEU A CD1 
2357 C CD2 . LEU A 315 ? 0.7309 0.7349 0.8268 0.0166  -0.0144 0.0038  314 LEU A CD2 
2358 N N   . ARG A 316 ? 0.6718 0.6458 0.7484 0.0428  -0.0047 0.0298  315 ARG A N   
2359 C CA  . ARG A 316 ? 0.6479 0.6146 0.7107 0.0450  -0.0029 0.0345  315 ARG A CA  
2360 C C   . ARG A 316 ? 0.7112 0.6800 0.7610 0.0487  -0.0090 0.0364  315 ARG A C   
2361 O O   . ARG A 316 ? 0.7762 0.7405 0.8117 0.0489  -0.0089 0.0366  315 ARG A O   
2362 C CB  . ARG A 316 ? 0.5943 0.5553 0.6613 0.0489  0.0021  0.0417  315 ARG A CB  
2363 C CG  . ARG A 316 ? 0.5979 0.5611 0.6706 0.0553  -0.0004 0.0475  315 ARG A CG  
2364 C CD  . ARG A 316 ? 0.5763 0.5326 0.6575 0.0572  0.0050  0.0531  315 ARG A CD  
2365 N NE  . ARG A 316 ? 0.5778 0.5345 0.6644 0.0637  0.0028  0.0594  315 ARG A NE  
2366 C CZ  . ARG A 316 ? 0.6298 0.5915 0.7281 0.0659  -0.0002 0.0570  315 ARG A CZ  
2367 N NH1 . ARG A 316 ? 0.6138 0.5815 0.7198 0.0618  -0.0009 0.0484  315 ARG A NH1 
2368 N NH2 . ARG A 316 ? 0.7074 0.6683 0.8099 0.0726  -0.0022 0.0637  315 ARG A NH2 
2369 N N   . ASP A 317 ? 0.6935 0.6691 0.7475 0.0520  -0.0146 0.0376  316 ASP A N   
2370 C CA  . ASP A 317 ? 0.6895 0.6679 0.7310 0.0550  -0.0216 0.0383  316 ASP A CA  
2371 C C   . ASP A 317 ? 0.7641 0.7443 0.7997 0.0490  -0.0261 0.0305  316 ASP A C   
2372 O O   . ASP A 317 ? 0.8249 0.8027 0.8452 0.0501  -0.0302 0.0296  316 ASP A O   
2373 C CB  . ASP A 317 ? 0.7123 0.6988 0.7614 0.0598  -0.0271 0.0415  316 ASP A CB  
2374 C CG  . ASP A 317 ? 0.6895 0.6727 0.7445 0.0660  -0.0231 0.0497  316 ASP A CG  
2375 O OD1 . ASP A 317 ? 0.6977 0.6733 0.7544 0.0651  -0.0159 0.0520  316 ASP A OD1 
2376 O OD2 . ASP A 317 ? 0.6769 0.6651 0.7354 0.0715  -0.0276 0.0540  316 ASP A OD2 
2377 N N   . PHE A 318 ? 0.8728 0.8569 0.9200 0.0427  -0.0253 0.0248  317 PHE A N   
2378 C CA  . PHE A 318 ? 0.8660 0.8509 0.9089 0.0361  -0.0291 0.0180  317 PHE A CA  
2379 C C   . PHE A 318 ? 0.9311 0.9055 0.9605 0.0341  -0.0257 0.0164  317 PHE A C   
2380 O O   . PHE A 318 ? 0.9902 0.9613 1.0081 0.0319  -0.0302 0.0126  317 PHE A O   
2381 C CB  . PHE A 318 ? 0.8891 0.8813 0.9482 0.0301  -0.0279 0.0136  317 PHE A CB  
2382 C CG  . PHE A 318 ? 0.9683 0.9605 1.0246 0.0221  -0.0306 0.0074  317 PHE A CG  
2383 C CD1 . PHE A 318 ? 1.0208 1.0054 1.0734 0.0176  -0.0256 0.0049  317 PHE A CD1 
2384 C CD2 . PHE A 318 ? 1.0114 1.0114 1.0698 0.0188  -0.0383 0.0044  317 PHE A CD2 
2385 C CE1 . PHE A 318 ? 1.1043 1.0879 1.1545 0.0103  -0.0282 0.0000  317 PHE A CE1 
2386 C CE2 . PHE A 318 ? 1.0763 1.0754 1.1328 0.0109  -0.0409 -0.0007 317 PHE A CE2 
2387 C CZ  . PHE A 318 ? 1.1840 1.1744 1.2361 0.0067  -0.0357 -0.0027 317 PHE A CZ  
2388 N N   . ALA A 319 ? 0.8470 0.8158 0.8780 0.0352  -0.0180 0.0193  318 ALA A N   
2389 C CA  . ALA A 319 ? 0.8296 0.7897 0.8496 0.0339  -0.0143 0.0183  318 ALA A CA  
2390 C C   . ALA A 319 ? 0.8748 0.8303 0.8777 0.0399  -0.0157 0.0215  318 ALA A C   
2391 O O   . ALA A 319 ? 0.8595 0.8090 0.8497 0.0392  -0.0166 0.0183  318 ALA A O   
2392 C CB  . ALA A 319 ? 0.7720 0.7292 0.8000 0.0332  -0.0063 0.0207  318 ALA A CB  
2393 N N   . ILE A 320 ? 0.8597 0.8173 0.8615 0.0462  -0.0158 0.0279  319 ILE A N   
2394 C CA  . ILE A 320 ? 0.8802 0.8343 0.8648 0.0525  -0.0166 0.0315  319 ILE A CA  
2395 C C   . ILE A 320 ? 0.9491 0.9040 0.9217 0.0526  -0.0255 0.0265  319 ILE A C   
2396 O O   . ILE A 320 ? 0.9799 0.9295 0.9352 0.0556  -0.0266 0.0253  319 ILE A O   
2397 C CB  . ILE A 320 ? 0.8625 0.8189 0.8492 0.0590  -0.0145 0.0406  319 ILE A CB  
2398 C CG1 . ILE A 320 ? 0.7583 0.7119 0.7552 0.0585  -0.0058 0.0455  319 ILE A CG1 
2399 C CG2 . ILE A 320 ? 0.8653 0.8198 0.8332 0.0658  -0.0159 0.0447  319 ILE A CG2 
2400 C CD1 . ILE A 320 ? 0.6268 0.5829 0.6352 0.0618  -0.0046 0.0525  319 ILE A CD1 
2401 N N   . TRP A 321 ? 0.9295 0.8911 0.9112 0.0492  -0.0320 0.0231  320 TRP A N   
2402 C CA  . TRP A 321 ? 0.9643 0.9273 0.9363 0.0483  -0.0415 0.0182  320 TRP A CA  
2403 C C   . TRP A 321 ? 0.9875 0.9433 0.9520 0.0426  -0.0430 0.0106  320 TRP A C   
2404 O O   . TRP A 321 ? 1.0109 0.9617 0.9593 0.0440  -0.0484 0.0070  320 TRP A O   
2405 C CB  . TRP A 321 ? 0.9267 0.9005 0.9131 0.0457  -0.0478 0.0171  320 TRP A CB  
2406 C CG  . TRP A 321 ? 0.9436 0.9208 0.9212 0.0459  -0.0585 0.0138  320 TRP A CG  
2407 C CD1 . TRP A 321 ? 0.8863 0.8593 0.8549 0.0409  -0.0646 0.0066  320 TRP A CD1 
2408 C CD2 . TRP A 321 ? 1.0405 1.0254 1.0175 0.0512  -0.0650 0.0175  320 TRP A CD2 
2409 N NE1 . TRP A 321 ? 0.9403 0.9183 0.9029 0.0424  -0.0748 0.0051  320 TRP A NE1 
2410 C CE2 . TRP A 321 ? 1.0637 1.0496 1.0312 0.0488  -0.0752 0.0119  320 TRP A CE2 
2411 C CE3 . TRP A 321 ? 1.0079 0.9986 0.9915 0.0577  -0.0635 0.0253  320 TRP A CE3 
2412 C CZ2 . TRP A 321 ? 1.0235 1.0171 0.9878 0.0528  -0.0842 0.0136  320 TRP A CZ2 
2413 C CZ3 . TRP A 321 ? 0.8867 0.8846 0.8670 0.0621  -0.0721 0.0275  320 TRP A CZ3 
2414 C CH2 . TRP A 321 ? 0.8806 0.8806 0.8513 0.0596  -0.0824 0.0216  320 TRP A CH2 
2415 N N   . LEU A 322 ? 0.9684 0.9230 0.9436 0.0364  -0.0384 0.0081  321 LEU A N   
2416 C CA  . LEU A 322 ? 0.9595 0.9071 0.9291 0.0306  -0.0402 0.0015  321 LEU A CA  
2417 C C   . LEU A 322 ? 0.9297 0.8680 0.8913 0.0323  -0.0329 0.0021  321 LEU A C   
2418 O O   . LEU A 322 ? 0.9213 0.8516 0.8665 0.0354  -0.0343 -0.0001 321 LEU A O   
2419 C CB  . LEU A 322 ? 0.9812 0.9343 0.9670 0.0219  -0.0410 -0.0019 321 LEU A CB  
2420 C CG  . LEU A 322 ? 1.0080 0.9735 1.0082 0.0193  -0.0460 -0.0019 321 LEU A CG  
2421 C CD1 . LEU A 322 ? 1.0056 0.9741 1.0158 0.0098  -0.0478 -0.0067 321 LEU A CD1 
2422 C CD2 . LEU A 322 ? 0.9814 0.9499 0.9733 0.0226  -0.0550 -0.0022 321 LEU A CD2 
2423 N N   . LEU A 323 ? 0.9540 0.8937 0.9274 0.0305  -0.0254 0.0047  322 LEU A N   
2424 C CA  . LEU A 323 ? 0.9262 0.8585 0.8945 0.0313  -0.0189 0.0051  322 LEU A CA  
2425 C C   . LEU A 323 ? 0.9035 0.8324 0.8584 0.0396  -0.0157 0.0095  322 LEU A C   
2426 O O   . LEU A 323 ? 0.9127 0.8350 0.8582 0.0416  -0.0124 0.0085  322 LEU A O   
2427 C CB  . LEU A 323 ? 0.8674 0.8031 0.8512 0.0282  -0.0121 0.0076  322 LEU A CB  
2428 C CG  . LEU A 323 ? 0.7417 0.6802 0.7373 0.0201  -0.0133 0.0032  322 LEU A CG  
2429 C CD1 . LEU A 323 ? 0.6716 0.6191 0.6835 0.0190  -0.0117 0.0054  322 LEU A CD1 
2430 C CD2 . LEU A 323 ? 0.7658 0.6987 0.7614 0.0167  -0.0086 0.0017  322 LEU A CD2 
2431 N N   . LEU A 324 ? 0.9450 0.8787 0.8990 0.0448  -0.0163 0.0146  323 LEU A N   
2432 C CA  . LEU A 324 ? 0.9550 0.8867 0.8949 0.0529  -0.0138 0.0193  323 LEU A CA  
2433 C C   . LEU A 324 ? 0.9990 0.9304 0.9245 0.0565  -0.0219 0.0168  323 LEU A C   
2434 O O   . LEU A 324 ? 1.0194 0.9536 0.9485 0.0525  -0.0296 0.0126  323 LEU A O   
2435 C CB  . LEU A 324 ? 0.9076 0.8442 0.8561 0.0565  -0.0078 0.0283  323 LEU A CB  
2436 C CG  . LEU A 324 ? 0.8025 0.7388 0.7638 0.0537  0.0004  0.0312  323 LEU A CG  
2437 C CD1 . LEU A 324 ? 0.7745 0.7052 0.7300 0.0520  0.0033  0.0271  323 LEU A CD1 
2438 C CD2 . LEU A 324 ? 0.8064 0.7466 0.7863 0.0478  -0.0002 0.0298  323 LEU A CD2 
2439 N N   . SER A 325 ? 1.0151 0.9438 0.9240 0.0639  -0.0202 0.0196  324 SER A N   
2440 C CA  . SER A 325 ? 1.0930 1.0206 0.9851 0.0681  -0.0280 0.0169  324 SER A CA  
2441 C C   . SER A 325 ? 1.0532 0.9888 0.9484 0.0713  -0.0316 0.0227  324 SER A C   
2442 O O   . SER A 325 ? 1.0653 1.0013 0.9466 0.0751  -0.0386 0.0211  324 SER A O   
2443 C CB  . SER A 325 ? 1.1423 1.0642 1.0137 0.0758  -0.0245 0.0172  324 SER A CB  
2444 O OG  . SER A 325 ? 1.1312 1.0503 0.9844 0.0793  -0.0328 0.0124  324 SER A OG  
2445 N N   . ASN A 326 ? 1.0369 0.9784 0.9495 0.0700  -0.0274 0.0290  325 ASN A N   
2446 C CA  . ASN A 326 ? 1.0590 1.0076 0.9762 0.0736  -0.0303 0.0354  325 ASN A CA  
2447 C C   . ASN A 326 ? 1.1231 1.0713 1.0225 0.0825  -0.0291 0.0419  325 ASN A C   
2448 O O   . ASN A 326 ? 1.2131 1.1654 1.1064 0.0865  -0.0354 0.0444  325 ASN A O   
2449 C CB  . ASN A 326 ? 1.0795 1.0333 1.0012 0.0702  -0.0409 0.0302  325 ASN A CB  
2450 C CG  . ASN A 326 ? 1.0324 0.9946 0.9678 0.0720  -0.0427 0.0363  325 ASN A CG  
2451 O OD1 . ASN A 326 ? 1.0357 1.0002 0.9887 0.0696  -0.0377 0.0391  325 ASN A OD1 
2452 N ND2 . ASN A 326 ? 0.9825 0.9492 0.9096 0.0765  -0.0504 0.0380  325 ASN A ND2 
2453 N N   . LYS A 327 ? 1.0906 1.0346 0.9818 0.0857  -0.0209 0.0450  326 LYS A N   
2454 C CA  . LYS A 327 ? 1.1413 1.0854 1.0143 0.0943  -0.0183 0.0512  326 LYS A CA  
2455 C C   . LYS A 327 ? 1.1350 1.0835 1.0161 0.0978  -0.0127 0.0636  326 LYS A C   
2456 O O   . LYS A 327 ? 1.1235 1.0750 0.9945 0.1038  -0.0152 0.0697  326 LYS A O   
2457 C CB  . LYS A 327 ? 1.0865 1.0253 0.9470 0.0968  -0.0117 0.0491  326 LYS A CB  
2458 C CG  . LYS A 327 ? 1.1479 1.0804 0.9926 0.0966  -0.0182 0.0379  326 LYS A CG  
2459 C CD  . LYS A 327 ? 1.1670 1.0947 0.9973 0.1015  -0.0114 0.0367  326 LYS A CD  
2460 C CE  . LYS A 327 ? 1.0764 0.9953 0.8962 0.0996  -0.0170 0.0246  326 LYS A CE  
2461 N NZ  . LYS A 327 ? 1.0591 0.9759 0.8647 0.1008  -0.0285 0.0183  326 LYS A NZ  
2462 N N   . PHE A 328 ? 1.0089 0.9572 0.9075 0.0939  -0.0053 0.0674  327 PHE A N   
2463 C CA  . PHE A 328 ? 0.8942 0.8450 0.8032 0.0959  0.0001  0.0789  327 PHE A CA  
2464 C C   . PHE A 328 ? 0.8058 0.7577 0.7372 0.0901  -0.0019 0.0775  327 PHE A C   
2465 O O   . PHE A 328 ? 0.7891 0.7392 0.7349 0.0853  0.0036  0.0772  327 PHE A O   
2466 C CB  . PHE A 328 ? 0.8622 0.8115 0.7719 0.0966  0.0109  0.0850  327 PHE A CB  
2467 C CG  . PHE A 328 ? 0.9115 0.8601 0.8000 0.1021  0.0138  0.0845  327 PHE A CG  
2468 C CD1 . PHE A 328 ? 0.8914 0.8423 0.7617 0.1098  0.0124  0.0900  327 PHE A CD1 
2469 C CD2 . PHE A 328 ? 0.8626 0.8086 0.7490 0.1001  0.0179  0.0786  327 PHE A CD2 
2470 C CE1 . PHE A 328 ? 0.8930 0.8435 0.7429 0.1156  0.0155  0.0889  327 PHE A CE1 
2471 C CE2 . PHE A 328 ? 0.8822 0.8276 0.7492 0.1061  0.0209  0.0776  327 PHE A CE2 
2472 C CZ  . PHE A 328 ? 0.8861 0.8338 0.7345 0.1140  0.0199  0.0825  327 PHE A CZ  
2473 N N   . THR A 329 ? 0.7820 0.7376 0.7164 0.0910  -0.0099 0.0765  328 THR A N   
2474 C CA  . THR A 329 ? 0.8034 0.7612 0.7585 0.0865  -0.0120 0.0746  328 THR A CA  
2475 C C   . THR A 329 ? 0.7859 0.7422 0.7557 0.0871  -0.0057 0.0835  328 THR A C   
2476 O O   . THR A 329 ? 0.7545 0.7121 0.7412 0.0844  -0.0070 0.0819  328 THR A O   
2477 C CB  . THR A 329 ? 0.8612 0.8249 0.8163 0.0883  -0.0219 0.0725  328 THR A CB  
2478 O OG1 . THR A 329 ? 0.8478 0.8133 0.8009 0.0951  -0.0227 0.0827  328 THR A OG1 
2479 C CG2 . THR A 329 ? 0.9079 0.8722 0.8448 0.0890  -0.0291 0.0654  328 THR A CG2 
2480 N N   . ALA A 330 ? 0.7664 0.7199 0.7306 0.0905  0.0012  0.0927  329 ALA A N   
2481 C CA  . ALA A 330 ? 0.6774 0.6280 0.6561 0.0902  0.0069  0.1012  329 ALA A CA  
2482 C C   . ALA A 330 ? 0.6507 0.5979 0.6428 0.0836  0.0132  0.0978  329 ALA A C   
2483 O O   . ALA A 330 ? 0.6596 0.6035 0.6653 0.0822  0.0173  0.1033  329 ALA A O   
2484 C CB  . ALA A 330 ? 0.6794 0.6290 0.6479 0.0959  0.0117  0.1137  329 ALA A CB  
2485 N N   . MET A 331 ? 0.6481 0.5954 0.6365 0.0794  0.0137  0.0890  330 MET A N   
2486 C CA  . MET A 331 ? 0.6701 0.6146 0.6706 0.0732  0.0191  0.0858  330 MET A CA  
2487 C C   . MET A 331 ? 0.5936 0.5378 0.6116 0.0686  0.0168  0.0803  330 MET A C   
2488 O O   . MET A 331 ? 0.5779 0.5198 0.6064 0.0634  0.0207  0.0773  330 MET A O   
2489 C CB  . MET A 331 ? 0.6685 0.6129 0.6597 0.0707  0.0200  0.0783  330 MET A CB  
2490 C CG  . MET A 331 ? 0.6844 0.6305 0.6633 0.0717  0.0126  0.0706  330 MET A CG  
2491 S SD  . MET A 331 ? 0.7202 0.6638 0.6919 0.0675  0.0130  0.0607  330 MET A SD  
2492 C CE  . MET A 331 ? 0.7894 0.7332 0.7398 0.0723  0.0054  0.0565  330 MET A CE  
2493 N N   . ARG A 332 ? 0.6035 0.5507 0.6247 0.0706  0.0106  0.0789  331 ARG A N   
2494 C CA  . ARG A 332 ? 0.6206 0.5687 0.6587 0.0673  0.0089  0.0739  331 ARG A CA  
2495 C C   . ARG A 332 ? 0.6367 0.5795 0.6887 0.0667  0.0140  0.0793  331 ARG A C   
2496 O O   . ARG A 332 ? 0.6467 0.5887 0.7123 0.0632  0.0144  0.0741  331 ARG A O   
2497 C CB  . ARG A 332 ? 0.5988 0.5525 0.6382 0.0709  0.0015  0.0730  331 ARG A CB  
2498 C CG  . ARG A 332 ? 0.6515 0.6050 0.6861 0.0782  -0.0001 0.0831  331 ARG A CG  
2499 C CD  . ARG A 332 ? 0.6657 0.6263 0.6982 0.0819  -0.0087 0.0815  331 ARG A CD  
2500 N NE  . ARG A 332 ? 0.6296 0.5948 0.6782 0.0794  -0.0116 0.0750  331 ARG A NE  
2501 C CZ  . ARG A 332 ? 0.6398 0.6055 0.7018 0.0828  -0.0123 0.0783  331 ARG A CZ  
2502 N NH1 . ARG A 332 ? 0.6737 0.6345 0.7358 0.0883  -0.0107 0.0884  331 ARG A NH1 
2503 N NH2 . ARG A 332 ? 0.5692 0.5407 0.6450 0.0809  -0.0146 0.0715  331 ARG A NH2 
2504 N N   . ASP A 333 ? 0.6409 0.5799 0.6895 0.0698  0.0180  0.0894  332 ASP A N   
2505 C CA  . ASP A 333 ? 0.6113 0.5438 0.6729 0.0684  0.0228  0.0949  332 ASP A CA  
2506 C C   . ASP A 333 ? 0.6044 0.5343 0.6700 0.0622  0.0285  0.0925  332 ASP A C   
2507 O O   . ASP A 333 ? 0.7576 0.6822 0.8364 0.0590  0.0314  0.0934  332 ASP A O   
2508 C CB  . ASP A 333 ? 0.5754 0.5051 0.6327 0.0737  0.0246  0.1079  332 ASP A CB  
2509 C CG  . ASP A 333 ? 0.6311 0.5633 0.6848 0.0803  0.0186  0.1114  332 ASP A CG  
2510 O OD1 . ASP A 333 ? 0.6587 0.5951 0.7164 0.0806  0.0131  0.1038  332 ASP A OD1 
2511 O OD2 . ASP A 333 ? 0.6895 0.6202 0.7366 0.0852  0.0193  0.1223  332 ASP A OD2 
2512 N N   . LEU A 334 ? 0.5885 0.5216 0.6430 0.0607  0.0299  0.0894  333 LEU A N   
2513 C CA  . LEU A 334 ? 0.6079 0.5399 0.6660 0.0553  0.0347  0.0868  333 LEU A CA  
2514 C C   . LEU A 334 ? 0.6295 0.5614 0.6963 0.0496  0.0331  0.0761  333 LEU A C   
2515 O O   . LEU A 334 ? 0.6652 0.5960 0.7368 0.0448  0.0365  0.0736  333 LEU A O   
2516 C CB  . LEU A 334 ? 0.5533 0.4887 0.5961 0.0568  0.0366  0.0872  333 LEU A CB  
2517 C CG  . LEU A 334 ? 0.6398 0.5756 0.6762 0.0603  0.0420  0.0982  333 LEU A CG  
2518 C CD1 . LEU A 334 ? 0.6139 0.5511 0.6388 0.0674  0.0394  0.1048  333 LEU A CD1 
2519 C CD2 . LEU A 334 ? 0.6108 0.5498 0.6380 0.0599  0.0457  0.0963  333 LEU A CD2 
2520 N N   . PHE A 335 ? 0.5771 0.5112 0.6464 0.0502  0.0280  0.0701  334 PHE A N   
2521 C CA  . PHE A 335 ? 0.6589 0.5945 0.7346 0.0450  0.0267  0.0600  334 PHE A CA  
2522 C C   . PHE A 335 ? 0.6987 0.6300 0.7895 0.0417  0.0293  0.0587  334 PHE A C   
2523 O O   . PHE A 335 ? 0.6327 0.5630 0.7272 0.0364  0.0315  0.0538  334 PHE A O   
2524 C CB  . PHE A 335 ? 0.6565 0.5973 0.7313 0.0465  0.0209  0.0547  334 PHE A CB  
2525 C CG  . PHE A 335 ? 0.6010 0.5455 0.6623 0.0463  0.0176  0.0511  334 PHE A CG  
2526 C CD1 . PHE A 335 ? 0.6100 0.5549 0.6579 0.0511  0.0162  0.0562  334 PHE A CD1 
2527 C CD2 . PHE A 335 ? 0.6103 0.5575 0.6718 0.0414  0.0157  0.0425  334 PHE A CD2 
2528 C CE1 . PHE A 335 ? 0.6158 0.5627 0.6507 0.0511  0.0127  0.0520  334 PHE A CE1 
2529 C CE2 . PHE A 335 ? 0.6070 0.5559 0.6564 0.0409  0.0122  0.0391  334 PHE A CE2 
2530 C CZ  . PHE A 335 ? 0.6349 0.5833 0.6709 0.0458  0.0105  0.0434  334 PHE A CZ  
2531 N N   . ALA A 336 ? 0.6648 0.5929 0.7640 0.0450  0.0286  0.0626  335 ALA A N   
2532 C CA  . ALA A 336 ? 0.6064 0.5294 0.7196 0.0425  0.0301  0.0598  335 ALA A CA  
2533 C C   . ALA A 336 ? 0.6843 0.6020 0.8014 0.0377  0.0346  0.0619  335 ALA A C   
2534 O O   . ALA A 336 ? 0.7489 0.6643 0.8738 0.0331  0.0356  0.0556  335 ALA A O   
2535 C CB  . ALA A 336 ? 0.5606 0.4795 0.6812 0.0478  0.0286  0.0650  335 ALA A CB  
2536 N N   . TRP A 337 ? 0.7554 0.6719 0.8673 0.0387  0.0374  0.0708  336 TRP A N   
2537 C CA  . TRP A 337 ? 0.7569 0.6702 0.8737 0.0340  0.0416  0.0737  336 TRP A CA  
2538 C C   . TRP A 337 ? 0.7065 0.6242 0.8196 0.0292  0.0424  0.0666  336 TRP A C   
2539 O O   . TRP A 337 ? 0.6898 0.6052 0.8108 0.0240  0.0437  0.0627  336 TRP A O   
2540 C CB  . TRP A 337 ? 0.7355 0.6487 0.8475 0.0366  0.0449  0.0856  336 TRP A CB  
2541 C CG  . TRP A 337 ? 0.7803 0.6887 0.8948 0.0415  0.0440  0.0939  336 TRP A CG  
2542 C CD1 . TRP A 337 ? 0.7835 0.6947 0.8888 0.0479  0.0414  0.0978  336 TRP A CD1 
2543 C CD2 . TRP A 337 ? 0.8283 0.7278 0.9553 0.0403  0.0452  0.0994  336 TRP A CD2 
2544 N NE1 . TRP A 337 ? 0.8092 0.7142 0.9204 0.0513  0.0410  0.1060  336 TRP A NE1 
2545 C CE2 . TRP A 337 ? 0.8151 0.7122 0.9396 0.0467  0.0435  0.1072  336 TRP A CE2 
2546 C CE3 . TRP A 337 ? 0.7892 0.6820 0.9290 0.0344  0.0471  0.0985  336 TRP A CE3 
2547 C CZ2 . TRP A 337 ? 0.8157 0.7031 0.9504 0.0475  0.0439  0.1144  336 TRP A CZ2 
2548 C CZ3 . TRP A 337 ? 0.8968 0.7797 1.0467 0.0348  0.0473  0.1051  336 TRP A CZ3 
2549 C CH2 . TRP A 337 ? 0.8528 0.7327 1.0002 0.0414  0.0458  0.1132  336 TRP A CH2 
2550 N N   . GLN A 338 ? 0.6308 0.5543 0.7315 0.0311  0.0413  0.0646  337 GLN A N   
2551 C CA  . GLN A 338 ? 0.6403 0.5672 0.7368 0.0271  0.0417  0.0583  337 GLN A CA  
2552 C C   . GLN A 338 ? 0.6762 0.6030 0.7783 0.0232  0.0393  0.0484  337 GLN A C   
2553 O O   . GLN A 338 ? 0.6437 0.5708 0.7486 0.0184  0.0404  0.0440  337 GLN A O   
2554 C CB  . GLN A 338 ? 0.6136 0.5448 0.6952 0.0305  0.0404  0.0581  337 GLN A CB  
2555 C CG  . GLN A 338 ? 0.6576 0.5910 0.7340 0.0271  0.0399  0.0510  337 GLN A CG  
2556 C CD  . GLN A 338 ? 0.6814 0.6164 0.7532 0.0271  0.0437  0.0547  337 GLN A CD  
2557 O OE1 . GLN A 338 ? 0.6598 0.5955 0.7292 0.0305  0.0468  0.0628  337 GLN A OE1 
2558 N NE2 . GLN A 338 ? 0.6098 0.5458 0.6805 0.0236  0.0437  0.0493  337 GLN A NE2 
2559 N N   . LEU A 339 ? 0.7247 0.6522 0.8289 0.0254  0.0362  0.0451  338 LEU A N   
2560 C CA  . LEU A 339 ? 0.6922 0.6213 0.8009 0.0221  0.0345  0.0359  338 LEU A CA  
2561 C C   . LEU A 339 ? 0.6113 0.5355 0.7319 0.0191  0.0361  0.0333  338 LEU A C   
2562 O O   . LEU A 339 ? 0.6248 0.5503 0.7480 0.0151  0.0360  0.0258  338 LEU A O   
2563 C CB  . LEU A 339 ? 0.6754 0.6085 0.7837 0.0257  0.0308  0.0336  338 LEU A CB  
2564 C CG  . LEU A 339 ? 0.6659 0.6038 0.7621 0.0274  0.0280  0.0338  338 LEU A CG  
2565 C CD1 . LEU A 339 ? 0.6687 0.6124 0.7666 0.0288  0.0239  0.0295  338 LEU A CD1 
2566 C CD2 . LEU A 339 ? 0.6915 0.6304 0.7801 0.0232  0.0288  0.0303  338 LEU A CD2 
2567 N N   . VAL A 340 ? 0.5871 0.5054 0.7147 0.0208  0.0375  0.0393  339 VAL A N   
2568 C CA  . VAL A 340 ? 0.5699 0.4818 0.7082 0.0173  0.0387  0.0368  339 VAL A CA  
2569 C C   . VAL A 340 ? 0.5752 0.4874 0.7132 0.0117  0.0407  0.0365  339 VAL A C   
2570 O O   . VAL A 340 ? 0.5247 0.4356 0.6671 0.0073  0.0405  0.0298  339 VAL A O   
2571 C CB  . VAL A 340 ? 0.5910 0.4951 0.7372 0.0203  0.0392  0.0439  339 VAL A CB  
2572 C CG1 . VAL A 340 ? 0.5398 0.4360 0.6962 0.0156  0.0405  0.0426  339 VAL A CG1 
2573 C CG2 . VAL A 340 ? 0.4873 0.3905 0.6367 0.0257  0.0368  0.0418  339 VAL A CG2 
2574 N N   . GLY A 341 ? 0.5091 0.4237 0.6415 0.0121  0.0426  0.0437  340 GLY A N   
2575 C CA  . GLY A 341 ? 0.5454 0.4621 0.6779 0.0075  0.0444  0.0438  340 GLY A CA  
2576 C C   . GLY A 341 ? 0.5090 0.4307 0.6351 0.0050  0.0431  0.0360  340 GLY A C   
2577 O O   . GLY A 341 ? 0.5881 0.5108 0.7163 0.0005  0.0436  0.0335  340 GLY A O   
2578 N N   . ASP A 342 ? 0.5974 0.5223 0.7156 0.0077  0.0411  0.0324  341 ASP A N   
2579 C CA  . ASP A 342 ? 0.6087 0.5375 0.7212 0.0049  0.0396  0.0252  341 ASP A CA  
2580 C C   . ASP A 342 ? 0.5215 0.4490 0.6407 0.0010  0.0388  0.0175  341 ASP A C   
2581 O O   . ASP A 342 ? 0.5275 0.4571 0.6444 -0.0030 0.0385  0.0128  341 ASP A O   
2582 C CB  . ASP A 342 ? 0.5508 0.4830 0.6547 0.0080  0.0373  0.0235  341 ASP A CB  
2583 C CG  . ASP A 342 ? 0.5984 0.5318 0.6922 0.0116  0.0376  0.0292  341 ASP A CG  
2584 O OD1 . ASP A 342 ? 0.6186 0.5517 0.7114 0.0115  0.0401  0.0337  341 ASP A OD1 
2585 O OD2 . ASP A 342 ? 0.6151 0.5503 0.7021 0.0147  0.0351  0.0289  341 ASP A OD2 
2586 N N   . VAL A 343 ? 0.5347 0.4587 0.6615 0.0025  0.0385  0.0161  342 VAL A N   
2587 C CA  . VAL A 343 ? 0.5370 0.4597 0.6694 -0.0002 0.0380  0.0082  342 VAL A CA  
2588 C C   . VAL A 343 ? 0.5737 0.4927 0.7112 -0.0050 0.0387  0.0072  342 VAL A C   
2589 O O   . VAL A 343 ? 0.6202 0.5409 0.7564 -0.0089 0.0381  0.0008  342 VAL A O   
2590 C CB  . VAL A 343 ? 0.5075 0.4268 0.6470 0.0038  0.0375  0.0070  342 VAL A CB  
2591 C CG1 . VAL A 343 ? 0.4535 0.3695 0.5993 0.0015  0.0376  -0.0010 342 VAL A CG1 
2592 C CG2 . VAL A 343 ? 0.5075 0.4330 0.6429 0.0076  0.0362  0.0062  342 VAL A CG2 
2593 N N   . LEU A 344 ? 0.5345 0.4486 0.6778 -0.0050 0.0397  0.0137  343 LEU A N   
2594 C CA  . LEU A 344 ? 0.4869 0.3978 0.6366 -0.0101 0.0398  0.0133  343 LEU A CA  
2595 C C   . LEU A 344 ? 0.5188 0.4358 0.6637 -0.0132 0.0402  0.0149  343 LEU A C   
2596 O O   . LEU A 344 ? 0.5292 0.4460 0.6781 -0.0180 0.0394  0.0123  343 LEU A O   
2597 C CB  . LEU A 344 ? 0.5013 0.4055 0.6601 -0.0098 0.0408  0.0206  343 LEU A CB  
2598 C CG  . LEU A 344 ? 0.5322 0.4279 0.6981 -0.0075 0.0398  0.0181  343 LEU A CG  
2599 C CD1 . LEU A 344 ? 0.5259 0.4207 0.6905 -0.0012 0.0406  0.0250  343 LEU A CD1 
2600 C CD2 . LEU A 344 ? 0.6023 0.4892 0.7791 -0.0118 0.0393  0.0189  343 LEU A CD2 
2601 N N   . LYS A 345 ? 0.5025 0.4246 0.6388 -0.0103 0.0412  0.0189  344 LYS A N   
2602 C CA  . LYS A 345 ? 0.5452 0.4726 0.6764 -0.0122 0.0415  0.0198  344 LYS A CA  
2603 C C   . LYS A 345 ? 0.5729 0.5029 0.6985 -0.0149 0.0395  0.0117  344 LYS A C   
2604 O O   . LYS A 345 ? 0.5652 0.4979 0.6902 -0.0182 0.0388  0.0103  344 LYS A O   
2605 C CB  . LYS A 345 ? 0.4452 0.3761 0.5680 -0.0076 0.0430  0.0259  344 LYS A CB  
2606 C CG  . LYS A 345 ? 0.5050 0.4407 0.6232 -0.0084 0.0438  0.0276  344 LYS A CG  
2607 C CD  . LYS A 345 ? 0.5201 0.4581 0.6286 -0.0031 0.0453  0.0327  344 LYS A CD  
2608 C CE  . LYS A 345 ? 0.5051 0.4430 0.6029 -0.0012 0.0429  0.0276  344 LYS A CE  
2609 N NZ  . LYS A 345 ? 0.5417 0.4805 0.6293 0.0042  0.0437  0.0316  344 LYS A NZ  
2610 N N   . VAL A 346 ? 0.5472 0.4772 0.6692 -0.0134 0.0385  0.0068  345 VAL A N   
2611 C CA  . VAL A 346 ? 0.5663 0.4990 0.6832 -0.0161 0.0371  -0.0004 345 VAL A CA  
2612 C C   . VAL A 346 ? 0.5736 0.5044 0.6963 -0.0203 0.0363  -0.0060 345 VAL A C   
2613 O O   . VAL A 346 ? 0.5382 0.4716 0.6573 -0.0238 0.0351  -0.0096 345 VAL A O   
2614 C CB  . VAL A 346 ? 0.5634 0.4979 0.6767 -0.0137 0.0366  -0.0036 345 VAL A CB  
2615 C CG1 . VAL A 346 ? 0.5793 0.5162 0.6911 -0.0168 0.0359  -0.0114 345 VAL A CG1 
2616 C CG2 . VAL A 346 ? 0.5337 0.4708 0.6381 -0.0113 0.0361  -0.0002 345 VAL A CG2 
2617 N N   . GLY A 347 ? 0.5895 0.5151 0.7207 -0.0198 0.0365  -0.0068 346 GLY A N   
2618 C CA  . GLY A 347 ? 0.6098 0.5321 0.7461 -0.0236 0.0352  -0.0128 346 GLY A CA  
2619 C C   . GLY A 347 ? 0.5922 0.5153 0.7313 -0.0281 0.0341  -0.0106 346 GLY A C   
2620 O O   . GLY A 347 ? 0.6530 0.5768 0.7915 -0.0320 0.0322  -0.0162 346 GLY A O   
2621 N N   . ALA A 348 ? 0.5426 0.4665 0.6849 -0.0273 0.0353  -0.0022 347 ALA A N   
2622 C CA  . ALA A 348 ? 0.5278 0.4545 0.6741 -0.0312 0.0345  0.0008  347 ALA A CA  
2623 C C   . ALA A 348 ? 0.5719 0.5055 0.7097 -0.0319 0.0337  -0.0001 347 ALA A C   
2624 O O   . ALA A 348 ? 0.5621 0.4990 0.7026 -0.0354 0.0321  0.0001  347 ALA A O   
2625 C CB  . ALA A 348 ? 0.5160 0.4430 0.6685 -0.0297 0.0369  0.0106  347 ALA A CB  
2626 N N   . TYR A 349 ? 0.6019 0.5374 0.7297 -0.0287 0.0345  -0.0009 348 TYR A N   
2627 C CA  . TYR A 349 ? 0.5615 0.5019 0.6808 -0.0292 0.0335  -0.0017 348 TYR A CA  
2628 C C   . TYR A 349 ? 0.6020 0.5434 0.7193 -0.0335 0.0309  -0.0088 348 TYR A C   
2629 O O   . TYR A 349 ? 0.6289 0.5740 0.7423 -0.0352 0.0293  -0.0085 348 TYR A O   
2630 C CB  . TYR A 349 ? 0.5617 0.5024 0.6713 -0.0256 0.0343  -0.0015 348 TYR A CB  
2631 C CG  . TYR A 349 ? 0.6232 0.5649 0.7296 -0.0213 0.0360  0.0054  348 TYR A CG  
2632 C CD1 . TYR A 349 ? 0.6796 0.6229 0.7919 -0.0206 0.0375  0.0116  348 TYR A CD1 
2633 C CD2 . TYR A 349 ? 0.6043 0.5458 0.7017 -0.0182 0.0360  0.0057  348 TYR A CD2 
2634 C CE1 . TYR A 349 ? 0.6598 0.6047 0.7681 -0.0160 0.0396  0.0177  348 TYR A CE1 
2635 C CE2 . TYR A 349 ? 0.6358 0.5775 0.7286 -0.0138 0.0373  0.0111  348 TYR A CE2 
2636 C CZ  . TYR A 349 ? 0.6804 0.6240 0.7782 -0.0124 0.0394  0.0170  348 TYR A CZ  
2637 O OH  . TYR A 349 ? 0.6516 0.5961 0.7439 -0.0074 0.0413  0.0222  348 TYR A OH  
2638 N N   . VAL A 350 ? 0.5754 0.5135 0.6948 -0.0348 0.0304  -0.0150 349 VAL A N   
2639 C CA  . VAL A 350 ? 0.5093 0.4483 0.6258 -0.0386 0.0281  -0.0222 349 VAL A CA  
2640 C C   . VAL A 350 ? 0.5143 0.4543 0.6366 -0.0426 0.0254  -0.0217 349 VAL A C   
2641 O O   . VAL A 350 ? 0.5490 0.4930 0.6665 -0.0451 0.0230  -0.0237 349 VAL A O   
2642 C CB  . VAL A 350 ? 0.4789 0.4140 0.5971 -0.0382 0.0286  -0.0292 349 VAL A CB  
2643 C CG1 . VAL A 350 ? 0.5005 0.4366 0.6148 -0.0418 0.0264  -0.0370 349 VAL A CG1 
2644 C CG2 . VAL A 350 ? 0.5134 0.4498 0.6268 -0.0344 0.0310  -0.0294 349 VAL A CG2 
2645 N N   . PHE A 351 ? 0.4922 0.4291 0.6253 -0.0434 0.0255  -0.0186 350 PHE A N   
2646 C CA  . PHE A 351 ? 0.4663 0.4052 0.6068 -0.0477 0.0227  -0.0173 350 PHE A CA  
2647 C C   . PHE A 351 ? 0.5883 0.5347 0.7277 -0.0469 0.0230  -0.0104 350 PHE A C   
2648 O O   . PHE A 351 ? 0.4781 0.4291 0.6199 -0.0502 0.0200  -0.0105 350 PHE A O   
2649 C CB  . PHE A 351 ? 0.4645 0.3979 0.6177 -0.0492 0.0230  -0.0147 350 PHE A CB  
2650 C CG  . PHE A 351 ? 0.5661 0.4908 0.7212 -0.0495 0.0223  -0.0218 350 PHE A CG  
2651 C CD1 . PHE A 351 ? 0.5188 0.4413 0.6721 -0.0530 0.0188  -0.0309 350 PHE A CD1 
2652 C CD2 . PHE A 351 ? 0.5729 0.4917 0.7310 -0.0457 0.0251  -0.0195 350 PHE A CD2 
2653 C CE1 . PHE A 351 ? 0.5379 0.4520 0.6924 -0.0524 0.0185  -0.0381 350 PHE A CE1 
2654 C CE2 . PHE A 351 ? 0.6189 0.5295 0.7791 -0.0451 0.0246  -0.0261 350 PHE A CE2 
2655 C CZ  . PHE A 351 ? 0.5236 0.4316 0.6820 -0.0482 0.0215  -0.0357 350 PHE A CZ  
2656 N N   . GLY A 352 ? 0.4198 0.3673 0.5551 -0.0422 0.0263  -0.0047 351 GLY A N   
2657 C CA  . GLY A 352 ? 0.4294 0.3834 0.5628 -0.0402 0.0270  0.0012  351 GLY A CA  
2658 C C   . GLY A 352 ? 0.4994 0.4563 0.6226 -0.0405 0.0247  -0.0019 351 GLY A C   
2659 O O   . GLY A 352 ? 0.5387 0.5012 0.6629 -0.0410 0.0230  0.0006  351 GLY A O   
2660 N N   . TYR A 353 ? 0.5955 0.5493 0.7094 -0.0400 0.0246  -0.0070 352 TYR A N   
2661 C CA  . TYR A 353 ? 0.5897 0.5456 0.6935 -0.0408 0.0225  -0.0095 352 TYR A CA  
2662 C C   . TYR A 353 ? 0.5164 0.4747 0.6215 -0.0455 0.0187  -0.0142 352 TYR A C   
2663 O O   . TYR A 353 ? 0.4918 0.4535 0.5909 -0.0463 0.0162  -0.0142 352 TYR A O   
2664 C CB  . TYR A 353 ? 0.5512 0.5041 0.6457 -0.0396 0.0238  -0.0130 352 TYR A CB  
2665 C CG  . TYR A 353 ? 0.5856 0.5375 0.6736 -0.0355 0.0256  -0.0087 352 TYR A CG  
2666 C CD1 . TYR A 353 ? 0.6074 0.5602 0.6869 -0.0350 0.0242  -0.0072 352 TYR A CD1 
2667 C CD2 . TYR A 353 ? 0.6242 0.5736 0.7143 -0.0321 0.0282  -0.0061 352 TYR A CD2 
2668 C CE1 . TYR A 353 ? 0.6220 0.5723 0.6951 -0.0313 0.0253  -0.0040 352 TYR A CE1 
2669 C CE2 . TYR A 353 ? 0.6477 0.5958 0.7310 -0.0284 0.0292  -0.0030 352 TYR A CE2 
2670 C CZ  . TYR A 353 ? 0.6626 0.6106 0.7374 -0.0282 0.0277  -0.0022 352 TYR A CZ  
2671 O OH  . TYR A 353 ? 0.6846 0.6298 0.7523 -0.0246 0.0281  0.0002  352 TYR A OH  
2672 N N   . LEU A 354 ? 0.4618 0.4177 0.5743 -0.0485 0.0177  -0.0183 353 LEU A N   
2673 C CA  . LEU A 354 ? 0.4937 0.4516 0.6079 -0.0531 0.0133  -0.0230 353 LEU A CA  
2674 C C   . LEU A 354 ? 0.4906 0.4546 0.6124 -0.0545 0.0108  -0.0177 353 LEU A C   
2675 O O   . LEU A 354 ? 0.5325 0.5010 0.6518 -0.0570 0.0067  -0.0195 353 LEU A O   
2676 C CB  . LEU A 354 ? 0.5127 0.4651 0.6332 -0.0557 0.0126  -0.0290 353 LEU A CB  
2677 C CG  . LEU A 354 ? 0.4119 0.3650 0.5382 -0.0610 0.0075  -0.0332 353 LEU A CG  
2678 C CD1 . LEU A 354 ? 0.4626 0.4188 0.5778 -0.0629 0.0040  -0.0391 353 LEU A CD1 
2679 C CD2 . LEU A 354 ? 0.4950 0.4401 0.6289 -0.0628 0.0072  -0.0382 353 LEU A CD2 
2680 N N   . VAL A 355 ? 0.4850 0.4502 0.6160 -0.0527 0.0134  -0.0110 354 VAL A N   
2681 C CA  . VAL A 355 ? 0.4625 0.4354 0.6018 -0.0533 0.0120  -0.0050 354 VAL A CA  
2682 C C   . VAL A 355 ? 0.5242 0.5021 0.6548 -0.0497 0.0117  -0.0019 354 VAL A C   
2683 O O   . VAL A 355 ? 0.4737 0.4586 0.6072 -0.0508 0.0083  -0.0002 354 VAL A O   
2684 C CB  . VAL A 355 ? 0.4059 0.3795 0.5562 -0.0516 0.0159  0.0021  354 VAL A CB  
2685 C CG1 . VAL A 355 ? 0.4919 0.4754 0.6496 -0.0505 0.0160  0.0095  354 VAL A CG1 
2686 C CG2 . VAL A 355 ? 0.3938 0.3624 0.5548 -0.0562 0.0150  -0.0002 354 VAL A CG2 
2687 N N   . ILE A 356 ? 0.5103 0.4842 0.6305 -0.0453 0.0147  -0.0012 355 ILE A N   
2688 C CA  . ILE A 356 ? 0.5125 0.4886 0.6235 -0.0419 0.0141  0.0013  355 ILE A CA  
2689 C C   . ILE A 356 ? 0.5170 0.4937 0.6198 -0.0450 0.0098  -0.0035 355 ILE A C   
2690 O O   . ILE A 356 ? 0.4915 0.4728 0.5922 -0.0443 0.0069  -0.0012 355 ILE A O   
2691 C CB  . ILE A 356 ? 0.4855 0.4560 0.5874 -0.0372 0.0179  0.0027  355 ILE A CB  
2692 C CG1 . ILE A 356 ? 0.5171 0.4875 0.6258 -0.0338 0.0221  0.0076  355 ILE A CG1 
2693 C CG2 . ILE A 356 ? 0.4792 0.4500 0.5715 -0.0337 0.0170  0.0051  355 ILE A CG2 
2694 C CD1 . ILE A 356 ? 0.5321 0.4964 0.6329 -0.0301 0.0251  0.0076  355 ILE A CD1 
2695 N N   . ALA A 357 ? 0.5118 0.4842 0.6098 -0.0481 0.0093  -0.0100 356 ALA A N   
2696 C CA  . ALA A 357 ? 0.4640 0.4372 0.5529 -0.0509 0.0058  -0.0147 356 ALA A CA  
2697 C C   . ALA A 357 ? 0.5261 0.5052 0.6203 -0.0545 0.0005  -0.0158 356 ALA A C   
2698 O O   . ALA A 357 ? 0.5870 0.5686 0.6731 -0.0558 -0.0031 -0.0174 356 ALA A O   
2699 C CB  . ALA A 357 ? 0.4496 0.4182 0.5334 -0.0530 0.0072  -0.0217 356 ALA A CB  
2700 N N   . LYS A 358 ? 0.5183 0.4999 0.6261 -0.0563 -0.0003 -0.0148 357 LYS A N   
2701 C CA  . LYS A 358 ? 0.4500 0.4381 0.5650 -0.0603 -0.0059 -0.0156 357 LYS A CA  
2702 C C   . LYS A 358 ? 0.5004 0.4969 0.6242 -0.0581 -0.0067 -0.0078 357 LYS A C   
2703 O O   . LYS A 358 ? 0.5250 0.5287 0.6567 -0.0613 -0.0116 -0.0075 357 LYS A O   
2704 C CB  . LYS A 358 ? 0.4708 0.4561 0.5961 -0.0650 -0.0072 -0.0202 357 LYS A CB  
2705 C CG  . LYS A 358 ? 0.5165 0.4942 0.6337 -0.0669 -0.0070 -0.0291 357 LYS A CG  
2706 C CD  . LYS A 358 ? 0.6100 0.5899 0.7158 -0.0692 -0.0118 -0.0348 357 LYS A CD  
2707 C CE  . LYS A 358 ? 0.5339 0.5111 0.6242 -0.0663 -0.0087 -0.0365 357 LYS A CE  
2708 N NZ  . LYS A 358 ? 0.5538 0.5340 0.6320 -0.0684 -0.0130 -0.0406 357 LYS A NZ  
2709 N N   . ALA A 359 ? 0.5652 0.5614 0.6879 -0.0525 -0.0020 -0.0017 358 ALA A N   
2710 C CA  . ALA A 359 ? 0.5740 0.5784 0.7038 -0.0488 -0.0018 0.0057  358 ALA A CA  
2711 C C   . ALA A 359 ? 0.6127 0.6248 0.7603 -0.0521 -0.0027 0.0085  358 ALA A C   
2712 O O   . ALA A 359 ? 0.6203 0.6424 0.7759 -0.0528 -0.0064 0.0115  358 ALA A O   
2713 C CB  . ALA A 359 ? 0.6085 0.6174 0.7311 -0.0473 -0.0063 0.0067  358 ALA A CB  
2714 N N   . SER A 360 ? 0.5335 0.5412 0.6882 -0.0542 0.0004  0.0080  359 SER A N   
2715 C CA  . SER A 360 ? 0.5142 0.5275 0.6864 -0.0584 -0.0002 0.0109  359 SER A CA  
2716 C C   . SER A 360 ? 0.5235 0.5408 0.7030 -0.0536 0.0061  0.0195  359 SER A C   
2717 O O   . SER A 360 ? 0.5954 0.6059 0.7742 -0.0522 0.0109  0.0205  359 SER A O   
2718 C CB  . SER A 360 ? 0.4748 0.4796 0.6503 -0.0641 -0.0013 0.0049  359 SER A CB  
2719 O OG  . SER A 360 ? 0.5008 0.5102 0.6937 -0.0692 -0.0028 0.0077  359 SER A OG  
2720 N N   . LEU A 361 ? 0.5229 0.5517 0.7091 -0.0508 0.0062  0.0257  360 LEU A N   
2721 C CA  . LEU A 361 ? 0.5223 0.5569 0.7160 -0.0460 0.0125  0.0340  360 LEU A CA  
2722 C C   . LEU A 361 ? 0.5274 0.5639 0.7370 -0.0514 0.0143  0.0373  360 LEU A C   
2723 O O   . LEU A 361 ? 0.5201 0.5563 0.7326 -0.0482 0.0205  0.0430  360 LEU A O   
2724 C CB  . LEU A 361 ? 0.4488 0.4966 0.6475 -0.0416 0.0121  0.0397  360 LEU A CB  
2725 C CG  . LEU A 361 ? 0.5755 0.6304 0.7789 -0.0346 0.0192  0.0480  360 LEU A CG  
2726 C CD1 . LEU A 361 ? 0.5917 0.6365 0.7782 -0.0269 0.0238  0.0472  360 LEU A CD1 
2727 C CD2 . LEU A 361 ? 0.5916 0.6618 0.8039 -0.0311 0.0180  0.0531  360 LEU A CD2 
2728 N N   . ARG A 362 ? 0.5430 0.5806 0.7625 -0.0596 0.0086  0.0338  361 ARG A N   
2729 C CA  . ARG A 362 ? 0.4945 0.5321 0.7296 -0.0657 0.0094  0.0368  361 ARG A CA  
2730 C C   . ARG A 362 ? 0.4980 0.5214 0.7272 -0.0654 0.0132  0.0346  361 ARG A C   
2731 O O   . ARG A 362 ? 0.4853 0.5086 0.7213 -0.0643 0.0186  0.0413  361 ARG A O   
2732 C CB  . ARG A 362 ? 0.4522 0.4919 0.6971 -0.0748 0.0013  0.0318  361 ARG A CB  
2733 C CG  . ARG A 362 ? 0.4705 0.5252 0.7222 -0.0754 -0.0035 0.0338  361 ARG A CG  
2734 C CD  . ARG A 362 ? 0.4423 0.4944 0.6886 -0.0806 -0.0125 0.0245  361 ARG A CD  
2735 N NE  . ARG A 362 ? 0.5059 0.5495 0.7313 -0.0758 -0.0128 0.0184  361 ARG A NE  
2736 C CZ  . ARG A 362 ? 0.4229 0.4716 0.6388 -0.0696 -0.0127 0.0202  361 ARG A CZ  
2737 N NH1 . ARG A 362 ? 0.3601 0.4226 0.5849 -0.0664 -0.0124 0.0275  361 ARG A NH1 
2738 N NH2 . ARG A 362 ? 0.4508 0.4906 0.6482 -0.0665 -0.0130 0.0148  361 ARG A NH2 
2739 N N   . PHE A 363 ? 0.5151 0.5271 0.7315 -0.0659 0.0106  0.0257  362 PHE A N   
2740 C CA  . PHE A 363 ? 0.5111 0.5102 0.7217 -0.0648 0.0139  0.0233  362 PHE A CA  
2741 C C   . PHE A 363 ? 0.5154 0.5130 0.7157 -0.0566 0.0203  0.0276  362 PHE A C   
2742 O O   . PHE A 363 ? 0.4621 0.4514 0.6599 -0.0549 0.0238  0.0281  362 PHE A O   
2743 C CB  . PHE A 363 ? 0.5110 0.5001 0.7111 -0.0671 0.0096  0.0124  362 PHE A CB  
2744 C CG  . PHE A 363 ? 0.4796 0.4639 0.6892 -0.0749 0.0046  0.0072  362 PHE A CG  
2745 C CD1 . PHE A 363 ? 0.4607 0.4365 0.6785 -0.0772 0.0065  0.0082  362 PHE A CD1 
2746 C CD2 . PHE A 363 ? 0.4805 0.4682 0.6904 -0.0797 -0.0023 0.0012  362 PHE A CD2 
2747 C CE1 . PHE A 363 ? 0.4802 0.4497 0.7065 -0.0843 0.0014  0.0029  362 PHE A CE1 
2748 C CE2 . PHE A 363 ? 0.4495 0.4318 0.6673 -0.0869 -0.0076 -0.0046 362 PHE A CE2 
2749 C CZ  . PHE A 363 ? 0.5465 0.5192 0.7727 -0.0893 -0.0057 -0.0039 362 PHE A CZ  
2750 N N   . TYR A 364 ? 0.5596 0.5645 0.7537 -0.0513 0.0215  0.0305  363 TYR A N   
2751 C CA  . TYR A 364 ? 0.5918 0.5949 0.7757 -0.0434 0.0270  0.0340  363 TYR A CA  
2752 C C   . TYR A 364 ? 0.6211 0.6300 0.8143 -0.0409 0.0328  0.0435  363 TYR A C   
2753 O O   . TYR A 364 ? 0.5786 0.5819 0.7671 -0.0373 0.0372  0.0459  363 TYR A O   
2754 C CB  . TYR A 364 ? 0.6001 0.6071 0.7735 -0.0384 0.0260  0.0334  363 TYR A CB  
2755 C CG  . TYR A 364 ? 0.5602 0.5596 0.7179 -0.0321 0.0290  0.0321  363 TYR A CG  
2756 C CD1 . TYR A 364 ? 0.5553 0.5564 0.7103 -0.0255 0.0344  0.0379  363 TYR A CD1 
2757 C CD2 . TYR A 364 ? 0.6175 0.6084 0.7633 -0.0331 0.0265  0.0250  363 TYR A CD2 
2758 C CE1 . TYR A 364 ? 0.5485 0.5422 0.6891 -0.0202 0.0362  0.0362  363 TYR A CE1 
2759 C CE2 . TYR A 364 ? 0.5873 0.5718 0.7201 -0.0282 0.0287  0.0239  363 TYR A CE2 
2760 C CZ  . TYR A 364 ? 0.5754 0.5608 0.7056 -0.0220 0.0331  0.0293  363 TYR A CZ  
2761 O OH  . TYR A 364 ? 0.6538 0.6323 0.7710 -0.0176 0.0345  0.0277  363 TYR A OH  
2762 N N   . ILE A 365 ? 0.5538 0.5749 0.7601 -0.0425 0.0328  0.0492  364 ILE A N   
2763 C CA  . ILE A 365 ? 0.4962 0.5247 0.7128 -0.0407 0.0387  0.0589  364 ILE A CA  
2764 C C   . ILE A 365 ? 0.5054 0.5266 0.7300 -0.0459 0.0399  0.0606  364 ILE A C   
2765 O O   . ILE A 365 ? 0.5338 0.5542 0.7588 -0.0427 0.0456  0.0672  364 ILE A O   
2766 C CB  . ILE A 365 ? 0.4218 0.4665 0.6531 -0.0423 0.0381  0.0645  364 ILE A CB  
2767 C CG1 . ILE A 365 ? 0.4426 0.4938 0.6652 -0.0354 0.0376  0.0636  364 ILE A CG1 
2768 C CG2 . ILE A 365 ? 0.3506 0.4043 0.5943 -0.0415 0.0447  0.0752  364 ILE A CG2 
2769 C CD1 . ILE A 365 ? 0.4632 0.5288 0.6988 -0.0381 0.0338  0.0657  364 ILE A CD1 
2770 N N   . LEU A 366 ? 0.4770 0.4920 0.7072 -0.0536 0.0342  0.0545  365 LEU A N   
2771 C CA  . LEU A 366 ? 0.4756 0.4813 0.7131 -0.0584 0.0346  0.0553  365 LEU A CA  
2772 C C   . LEU A 366 ? 0.4863 0.4802 0.7106 -0.0531 0.0378  0.0535  365 LEU A C   
2773 O O   . LEU A 366 ? 0.4876 0.4772 0.7160 -0.0528 0.0415  0.0591  365 LEU A O   
2774 C CB  . LEU A 366 ? 0.4588 0.4587 0.7024 -0.0667 0.0273  0.0473  365 LEU A CB  
2775 C CG  . LEU A 366 ? 0.4444 0.4334 0.6973 -0.0724 0.0265  0.0472  365 LEU A CG  
2776 C CD1 . LEU A 366 ? 0.4205 0.4175 0.6931 -0.0783 0.0274  0.0564  365 LEU A CD1 
2777 C CD2 . LEU A 366 ? 0.4637 0.4425 0.7140 -0.0776 0.0196  0.0356  365 LEU A CD2 
2778 N N   . ALA A 367 ? 0.4970 0.4861 0.7059 -0.0491 0.0363  0.0462  366 ALA A N   
2779 C CA  . ALA A 367 ? 0.5027 0.4817 0.6998 -0.0445 0.0386  0.0440  366 ALA A CA  
2780 C C   . ALA A 367 ? 0.5870 0.5697 0.7785 -0.0372 0.0446  0.0518  366 ALA A C   
2781 O O   . ALA A 367 ? 0.5780 0.5546 0.7672 -0.0348 0.0476  0.0547  366 ALA A O   
2782 C CB  . ALA A 367 ? 0.4007 0.3750 0.5840 -0.0430 0.0353  0.0346  366 ALA A CB  
2783 N N   . GLU A 368 ? 0.5455 0.5379 0.7342 -0.0332 0.0464  0.0551  367 GLU A N   
2784 C CA  . GLU A 368 ? 0.4948 0.4906 0.6764 -0.0255 0.0522  0.0615  367 GLU A CA  
2785 C C   . GLU A 368 ? 0.5115 0.5125 0.7047 -0.0262 0.0571  0.0717  367 GLU A C   
2786 O O   . GLU A 368 ? 0.4735 0.4723 0.6609 -0.0214 0.0615  0.0765  367 GLU A O   
2787 C CB  . GLU A 368 ? 0.5105 0.5146 0.6862 -0.0205 0.0527  0.0617  367 GLU A CB  
2788 C CG  . GLU A 368 ? 0.5908 0.5889 0.7532 -0.0192 0.0484  0.0531  367 GLU A CG  
2789 C CD  . GLU A 368 ? 0.6564 0.6470 0.8029 -0.0129 0.0502  0.0512  367 GLU A CD  
2790 O OE1 . GLU A 368 ? 0.6411 0.6350 0.7819 -0.0062 0.0543  0.0558  367 GLU A OE1 
2791 O OE2 . GLU A 368 ? 0.6875 0.6691 0.8271 -0.0147 0.0475  0.0450  367 GLU A OE2 
2792 N N   . VAL A 369 ? 0.5332 0.5416 0.7428 -0.0324 0.0562  0.0753  368 VAL A N   
2793 C CA  . VAL A 369 ? 0.4908 0.5050 0.7131 -0.0341 0.0610  0.0859  368 VAL A CA  
2794 C C   . VAL A 369 ? 0.4709 0.4729 0.6952 -0.0370 0.0611  0.0869  368 VAL A C   
2795 O O   . VAL A 369 ? 0.5685 0.5709 0.7939 -0.0346 0.0663  0.0956  368 VAL A O   
2796 C CB  . VAL A 369 ? 0.4345 0.4601 0.6755 -0.0411 0.0592  0.0893  368 VAL A CB  
2797 C CG1 . VAL A 369 ? 0.4377 0.4656 0.6945 -0.0463 0.0625  0.0991  368 VAL A CG1 
2798 C CG2 . VAL A 369 ? 0.3962 0.4367 0.6369 -0.0360 0.0615  0.0922  368 VAL A CG2 
2799 N N   . SER A 370 ? 0.4757 0.4665 0.6996 -0.0417 0.0554  0.0782  369 SER A N   
2800 C CA  . SER A 370 ? 0.4977 0.4760 0.7237 -0.0438 0.0550  0.0784  369 SER A CA  
2801 C C   . SER A 370 ? 0.5567 0.5296 0.7684 -0.0358 0.0585  0.0800  369 SER A C   
2802 O O   . SER A 370 ? 0.5427 0.5118 0.7569 -0.0347 0.0618  0.0873  369 SER A O   
2803 C CB  . SER A 370 ? 0.4758 0.4438 0.7026 -0.0490 0.0484  0.0674  369 SER A CB  
2804 O OG  . SER A 370 ? 0.5566 0.5306 0.7925 -0.0553 0.0442  0.0641  369 SER A OG  
2805 N N   . GLN A 371 ? 0.5503 0.5227 0.7471 -0.0305 0.0575  0.0735  370 GLN A N   
2806 C CA  . GLN A 371 ? 0.5328 0.5008 0.7158 -0.0232 0.0600  0.0743  370 GLN A CA  
2807 C C   . GLN A 371 ? 0.5469 0.5230 0.7274 -0.0177 0.0662  0.0846  370 GLN A C   
2808 O O   . GLN A 371 ? 0.5225 0.4948 0.6976 -0.0136 0.0689  0.0894  370 GLN A O   
2809 C CB  . GLN A 371 ? 0.5217 0.4880 0.6904 -0.0197 0.0572  0.0652  370 GLN A CB  
2810 C CG  . GLN A 371 ? 0.5429 0.5021 0.7122 -0.0243 0.0518  0.0552  370 GLN A CG  
2811 C CD  . GLN A 371 ? 0.5760 0.5351 0.7323 -0.0217 0.0494  0.0476  370 GLN A CD  
2812 O OE1 . GLN A 371 ? 0.5639 0.5200 0.7089 -0.0167 0.0501  0.0464  370 GLN A OE1 
2813 N NE2 . GLN A 371 ? 0.5882 0.5506 0.7461 -0.0253 0.0463  0.0427  370 GLN A NE2 
2814 N N   . PHE A 372 ? 0.5851 0.5728 0.7691 -0.0171 0.0685  0.0880  371 PHE A N   
2815 C CA  . PHE A 372 ? 0.5003 0.4972 0.6826 -0.0116 0.0751  0.0979  371 PHE A CA  
2816 C C   . PHE A 372 ? 0.5249 0.5221 0.7191 -0.0149 0.0787  0.1083  371 PHE A C   
2817 O O   . PHE A 372 ? 0.5543 0.5517 0.7422 -0.0099 0.0834  0.1155  371 PHE A O   
2818 C CB  . PHE A 372 ? 0.4487 0.4589 0.6352 -0.0105 0.0768  0.0995  371 PHE A CB  
2819 C CG  . PHE A 372 ? 0.4620 0.4825 0.6439 -0.0031 0.0840  0.1080  371 PHE A CG  
2820 C CD1 . PHE A 372 ? 0.5082 0.5373 0.7019 -0.0047 0.0896  0.1194  371 PHE A CD1 
2821 C CD2 . PHE A 372 ? 0.4820 0.5035 0.6476 0.0056  0.0853  0.1046  371 PHE A CD2 
2822 C CE1 . PHE A 372 ? 0.5154 0.5550 0.7042 0.0027  0.0969  0.1273  371 PHE A CE1 
2823 C CE2 . PHE A 372 ? 0.4523 0.4830 0.6123 0.0132  0.0920  0.1116  371 PHE A CE2 
2824 C CZ  . PHE A 372 ? 0.5214 0.5617 0.6928 0.0121  0.0982  0.1230  371 PHE A CZ  
2825 N N   . THR A 373 ? 0.5133 0.5103 0.7245 -0.0237 0.0763  0.1092  372 THR A N   
2826 C CA  . THR A 373 ? 0.5404 0.5371 0.7647 -0.0280 0.0794  0.1197  372 THR A CA  
2827 C C   . THR A 373 ? 0.5816 0.5642 0.8002 -0.0266 0.0787  0.1202  372 THR A C   
2828 O O   . THR A 373 ? 0.6431 0.6261 0.8612 -0.0240 0.0835  0.1303  372 THR A O   
2829 C CB  . THR A 373 ? 0.4706 0.4684 0.7143 -0.0384 0.0757  0.1192  372 THR A CB  
2830 O OG1 . THR A 373 ? 0.4315 0.4414 0.6789 -0.0394 0.0744  0.1161  372 THR A OG1 
2831 C CG2 . THR A 373 ? 0.4409 0.4425 0.6999 -0.0432 0.0800  0.1323  372 THR A CG2 
2832 N N   . LEU A 374 ? 0.5937 0.5645 0.8081 -0.0279 0.0728  0.1097  373 LEU A N   
2833 C CA  . LEU A 374 ? 0.6430 0.6009 0.8532 -0.0262 0.0717  0.1097  373 LEU A CA  
2834 C C   . LEU A 374 ? 0.6548 0.6136 0.8485 -0.0168 0.0751  0.1128  373 LEU A C   
2835 O O   . LEU A 374 ? 0.6748 0.6284 0.8670 -0.0143 0.0770  0.1197  373 LEU A O   
2836 C CB  . LEU A 374 ? 0.6941 0.6410 0.9029 -0.0287 0.0652  0.0971  373 LEU A CB  
2837 C CG  . LEU A 374 ? 0.6693 0.6122 0.8933 -0.0379 0.0610  0.0930  373 LEU A CG  
2838 C CD1 . LEU A 374 ? 0.5859 0.5226 0.8046 -0.0390 0.0552  0.0791  373 LEU A CD1 
2839 C CD2 . LEU A 374 ? 0.5445 0.4774 0.7804 -0.0421 0.0610  0.0993  373 LEU A CD2 
2840 N N   . LEU A 375 ? 0.6258 0.5909 0.8068 -0.0115 0.0754  0.1078  374 LEU A N   
2841 C CA  . LEU A 375 ? 0.5800 0.5459 0.7446 -0.0028 0.0779  0.1100  374 LEU A CA  
2842 C C   . LEU A 375 ? 0.6154 0.5891 0.7802 0.0005  0.0847  0.1230  374 LEU A C   
2843 O O   . LEU A 375 ? 0.6170 0.5883 0.7720 0.0061  0.0868  0.1279  374 LEU A O   
2844 C CB  . LEU A 375 ? 0.5300 0.5002 0.6817 0.0015  0.0766  0.1020  374 LEU A CB  
2845 C CG  . LEU A 375 ? 0.5061 0.4679 0.6483 0.0025  0.0710  0.0909  374 LEU A CG  
2846 C CD1 . LEU A 375 ? 0.5576 0.5235 0.6889 0.0057  0.0699  0.0843  374 LEU A CD1 
2847 C CD2 . LEU A 375 ? 0.5618 0.5172 0.6948 0.0074  0.0706  0.0925  374 LEU A CD2 
2848 N N   . MET A 376 ? 0.5968 0.5808 0.7729 -0.0029 0.0884  0.1289  375 MET A N   
2849 C CA  . MET A 376 ? 0.6318 0.6255 0.8086 0.0003  0.0958  0.1417  375 MET A CA  
2850 C C   . MET A 376 ? 0.6877 0.6763 0.8750 -0.0038 0.0977  0.1521  375 MET A C   
2851 O O   . MET A 376 ? 0.7135 0.7055 0.8952 0.0008  0.1031  0.1624  375 MET A O   
2852 C CB  . MET A 376 ? 0.6147 0.6231 0.8015 -0.0018 0.0993  0.1448  375 MET A CB  
2853 C CG  . MET A 376 ? 0.6420 0.6588 0.8151 0.0063  0.1013  0.1404  375 MET A CG  
2854 S SD  . MET A 376 ? 0.8896 0.9040 1.0381 0.0181  0.1044  0.1414  375 MET A SD  
2855 C CE  . MET A 376 ? 0.5651 0.5656 0.7005 0.0192  0.0958  0.1264  375 MET A CE  
2856 N N   . VAL A 377 ? 0.6333 0.6134 0.8352 -0.0123 0.0933  0.1498  376 VAL A N   
2857 C CA  . VAL A 377 ? 0.6571 0.6297 0.8690 -0.0164 0.0944  0.1593  376 VAL A CA  
2858 C C   . VAL A 377 ? 0.7155 0.6765 0.9149 -0.0105 0.0927  0.1591  376 VAL A C   
2859 O O   . VAL A 377 ? 0.7314 0.6910 0.9296 -0.0082 0.0964  0.1704  376 VAL A O   
2860 C CB  . VAL A 377 ? 0.6403 0.6053 0.8707 -0.0268 0.0893  0.1556  376 VAL A CB  
2861 C CG1 . VAL A 377 ? 0.6947 0.6497 0.9356 -0.0311 0.0900  0.1653  376 VAL A CG1 
2862 C CG2 . VAL A 377 ? 0.5778 0.5558 0.8214 -0.0328 0.0906  0.1568  376 VAL A CG2 
2863 N N   . PHE A 378 ? 0.7641 0.7177 0.9541 -0.0078 0.0872  0.1467  377 PHE A N   
2864 C CA  . PHE A 378 ? 0.8298 0.7735 1.0093 -0.0023 0.0848  0.1457  377 PHE A CA  
2865 C C   . PHE A 378 ? 0.8091 0.7594 0.9706 0.0070  0.0884  0.1500  377 PHE A C   
2866 O O   . PHE A 378 ? 0.7683 0.7130 0.9224 0.0118  0.0881  0.1545  377 PHE A O   
2867 C CB  . PHE A 378 ? 0.7187 0.6542 0.8953 -0.0027 0.0781  0.1313  377 PHE A CB  
2868 C CG  . PHE A 378 ? 0.6908 0.6161 0.8824 -0.0103 0.0740  0.1270  377 PHE A CG  
2869 C CD1 . PHE A 378 ? 0.7163 0.6323 0.9180 -0.0129 0.0742  0.1348  377 PHE A CD1 
2870 C CD2 . PHE A 378 ? 0.7062 0.6306 0.9013 -0.0146 0.0697  0.1150  377 PHE A CD2 
2871 C CE1 . PHE A 378 ? 0.7524 0.6575 0.9674 -0.0196 0.0701  0.1300  377 PHE A CE1 
2872 C CE2 . PHE A 378 ? 0.7043 0.6189 0.9118 -0.0211 0.0658  0.1102  377 PHE A CE2 
2873 C CZ  . PHE A 378 ? 0.6649 0.5695 0.8824 -0.0235 0.0659  0.1173  377 PHE A CZ  
2874 N N   . ALA A 379 ? 0.7658 0.7275 0.9197 0.0102  0.0914  0.1485  378 ALA A N   
2875 C CA  . ALA A 379 ? 0.7278 0.6952 0.8635 0.0193  0.0947  0.1519  378 ALA A CA  
2876 C C   . ALA A 379 ? 0.7648 0.7378 0.9013 0.0213  0.1017  0.1672  378 ALA A C   
2877 O O   . ALA A 379 ? 0.7019 0.6731 0.8261 0.0276  0.1028  0.1726  378 ALA A O   
2878 C CB  . ALA A 379 ? 0.6441 0.6207 0.7714 0.0225  0.0958  0.1453  378 ALA A CB  
2879 N N   . HIS A 380 ? 0.8881 0.8688 1.0394 0.0158  0.1064  0.1749  379 HIS A N   
2880 C CA  . HIS A 380 ? 0.8384 0.8255 0.9929 0.0164  0.1136  0.1907  379 HIS A CA  
2881 C C   . HIS A 380 ? 0.7762 0.7515 0.9358 0.0141  0.1121  0.1986  379 HIS A C   
2882 O O   . HIS A 380 ? 0.8427 0.8216 1.0007 0.0161  0.1178  0.2123  379 HIS A O   
2883 C CB  . HIS A 380 ? 0.9029 0.9012 1.0754 0.0095  0.1182  0.1967  379 HIS A CB  
2884 C CG  . HIS A 380 ? 1.0226 1.0356 1.1897 0.0138  0.1220  0.1935  379 HIS A CG  
2885 N ND1 . HIS A 380 ? 1.0795 1.0953 1.2531 0.0103  0.1184  0.1831  379 HIS A ND1 
2886 C CD2 . HIS A 380 ? 0.9508 0.9762 1.1061 0.0218  0.1291  0.1993  379 HIS A CD2 
2887 C CE1 . HIS A 380 ? 0.9741 1.0031 1.1409 0.0161  0.1230  0.1828  379 HIS A CE1 
2888 N NE2 . HIS A 380 ? 0.9682 1.0031 1.1238 0.0233  0.1297  0.1922  379 HIS A NE2 
2889 N N   . TRP A 381 ? 0.7293 0.6908 0.8945 0.0104  0.1049  0.1905  380 TRP A N   
2890 C CA  . TRP A 381 ? 0.7009 0.6496 0.8718 0.0087  0.1028  0.1970  380 TRP A CA  
2891 C C   . TRP A 381 ? 0.7379 0.6792 0.8926 0.0168  0.0991  0.1939  380 TRP A C   
2892 O O   . TRP A 381 ? 0.7374 0.6717 0.8916 0.0187  0.0993  0.2033  380 TRP A O   
2893 C CB  . TRP A 381 ? 0.7329 0.6703 0.9215 -0.0003 0.0973  0.1904  380 TRP A CB  
2894 C CG  . TRP A 381 ? 0.8107 0.7327 1.0060 -0.0018 0.0945  0.1956  380 TRP A CG  
2895 C CD1 . TRP A 381 ? 0.7765 0.6956 0.9767 -0.0027 0.0984  0.2110  380 TRP A CD1 
2896 C CD2 . TRP A 381 ? 0.8442 0.7517 1.0421 -0.0022 0.0874  0.1856  380 TRP A CD2 
2897 N NE1 . TRP A 381 ? 0.7955 0.6979 1.0012 -0.0035 0.0936  0.2112  380 TRP A NE1 
2898 C CE2 . TRP A 381 ? 0.8142 0.7095 1.0186 -0.0029 0.0870  0.1954  380 TRP A CE2 
2899 C CE3 . TRP A 381 ? 0.8318 0.7355 1.0270 -0.0019 0.0816  0.1697  380 TRP A CE3 
2900 C CZ2 . TRP A 381 ? 0.8450 0.7246 1.0535 -0.0025 0.0809  0.1892  380 TRP A CZ2 
2901 C CZ3 . TRP A 381 ? 0.7639 0.6533 0.9632 -0.0017 0.0761  0.1637  380 TRP A CZ3 
2902 C CH2 . TRP A 381 ? 0.7926 0.6701 0.9986 -0.0017 0.0757  0.1731  380 TRP A CH2 
2903 N N   . LEU A 382 ? 0.7386 0.6815 0.8803 0.0216  0.0954  0.1816  381 LEU A N   
2904 C CA  . LEU A 382 ? 0.6659 0.6023 0.7943 0.0284  0.0906  0.1772  381 LEU A CA  
2905 C C   . LEU A 382 ? 0.6731 0.6178 0.7805 0.0372  0.0921  0.1768  381 LEU A C   
2906 O O   . LEU A 382 ? 0.7075 0.6489 0.8035 0.0433  0.0900  0.1797  381 LEU A O   
2907 C CB  . LEU A 382 ? 0.6615 0.5908 0.7933 0.0260  0.0834  0.1620  381 LEU A CB  
2908 C CG  . LEU A 382 ? 0.7094 0.6274 0.8591 0.0190  0.0803  0.1601  381 LEU A CG  
2909 C CD1 . LEU A 382 ? 0.6897 0.6061 0.8438 0.0149  0.0758  0.1452  381 LEU A CD1 
2910 C CD2 . LEU A 382 ? 0.6811 0.5880 0.8305 0.0226  0.0768  0.1633  381 LEU A CD2 
2911 N N   . ILE A 383 ? 0.6342 0.5891 0.7357 0.0383  0.0953  0.1733  382 ILE A N   
2912 C CA  . ILE A 383 ? 0.6247 0.5861 0.7053 0.0468  0.0963  0.1711  382 ILE A CA  
2913 C C   . ILE A 383 ? 0.6589 0.6253 0.7294 0.0527  0.1019  0.1849  382 ILE A C   
2914 O O   . ILE A 383 ? 0.6468 0.6116 0.7007 0.0598  0.0994  0.1848  382 ILE A O   
2915 C CB  . ILE A 383 ? 0.6800 0.6502 0.7577 0.0470  0.0986  0.1641  382 ILE A CB  
2916 C CG1 . ILE A 383 ? 0.7071 0.6720 0.7871 0.0437  0.0918  0.1492  382 ILE A CG1 
2917 C CG2 . ILE A 383 ? 0.6089 0.5865 0.6658 0.0562  0.1017  0.1653  382 ILE A CG2 
2918 C CD1 . ILE A 383 ? 0.5782 0.5501 0.6533 0.0448  0.0930  0.1418  382 ILE A CD1 
2919 N N   . PRO A 384 ? 0.6368 0.6097 0.7161 0.0501  0.1093  0.1973  383 PRO A N   
2920 C CA  . PRO A 384 ? 0.6738 0.6525 0.7416 0.0562  0.1153  0.2109  383 PRO A CA  
2921 C C   . PRO A 384 ? 0.6446 0.6139 0.7097 0.0582  0.1122  0.2184  383 PRO A C   
2922 O O   . PRO A 384 ? 0.6492 0.6224 0.7006 0.0646  0.1158  0.2284  383 PRO A O   
2923 C CB  . PRO A 384 ? 0.6378 0.6255 0.7207 0.0509  0.1237  0.2225  383 PRO A CB  
2924 C CG  . PRO A 384 ? 0.6296 0.6194 0.7264 0.0443  0.1222  0.2125  383 PRO A CG  
2925 C CD  . PRO A 384 ? 0.6293 0.6061 0.7289 0.0416  0.1128  0.1999  383 PRO A CD  
2926 N N   . ALA A 385 ? 0.6040 0.5611 0.6809 0.0535  0.1057  0.2139  384 ALA A N   
2927 C CA  . ALA A 385 ? 0.5437 0.4911 0.6200 0.0556  0.1024  0.2210  384 ALA A CA  
2928 C C   . ALA A 385 ? 0.5823 0.5226 0.6500 0.0600  0.0936  0.2100  384 ALA A C   
2929 O O   . ALA A 385 ? 0.5609 0.4976 0.6195 0.0656  0.0910  0.2157  384 ALA A O   
2930 C CB  . ALA A 385 ? 0.5568 0.4946 0.6555 0.0471  0.1022  0.2269  384 ALA A CB  
2931 N N   . HIS A 386 ? 0.6383 0.5773 0.7089 0.0574  0.0889  0.1949  385 HIS A N   
2932 C CA  . HIS A 386 ? 0.6205 0.5538 0.6859 0.0604  0.0807  0.1843  385 HIS A CA  
2933 C C   . HIS A 386 ? 0.6193 0.5590 0.6686 0.0647  0.0782  0.1732  385 HIS A C   
2934 O O   . HIS A 386 ? 0.6687 0.6052 0.7143 0.0663  0.0713  0.1636  385 HIS A O   
2935 C CB  . HIS A 386 ? 0.6239 0.5485 0.7073 0.0536  0.0765  0.1758  385 HIS A CB  
2936 C CG  . HIS A 386 ? 0.7073 0.6218 0.8049 0.0509  0.0763  0.1844  385 HIS A CG  
2937 N ND1 . HIS A 386 ? 0.6997 0.6050 0.8139 0.0450  0.0731  0.1781  385 HIS A ND1 
2938 C CD2 . HIS A 386 ? 0.7023 0.6136 0.7994 0.0534  0.0786  0.1988  385 HIS A CD2 
2939 C CE1 . HIS A 386 ? 0.7585 0.6545 0.8822 0.0440  0.0734  0.1879  385 HIS A CE1 
2940 N NE2 . HIS A 386 ? 0.7941 0.6935 0.9080 0.0489  0.0767  0.2010  385 HIS A NE2 
2941 N N   . GLY A 387 ? 0.5133 0.4619 0.5533 0.0665  0.0835  0.1743  386 GLY A N   
2942 C CA  . GLY A 387 ? 0.5105 0.4636 0.5335 0.0713  0.0810  0.1645  386 GLY A CA  
2943 C C   . GLY A 387 ? 0.7136 0.6643 0.7428 0.0666  0.0765  0.1500  386 GLY A C   
2944 O O   . GLY A 387 ? 0.7255 0.6747 0.7707 0.0597  0.0777  0.1476  386 GLY A O   
2945 N N   . ALA A 388 ? 0.6925 0.6430 0.7084 0.0703  0.0709  0.1403  387 ALA A N   
2946 C CA  . ALA A 388 ? 0.5923 0.5406 0.6126 0.0661  0.0664  0.1269  387 ALA A CA  
2947 C C   . ALA A 388 ? 0.6642 0.6061 0.7013 0.0604  0.0626  0.1237  387 ALA A C   
2948 O O   . ALA A 388 ? 0.6882 0.6288 0.7347 0.0548  0.0614  0.1155  387 ALA A O   
2949 C CB  . ALA A 388 ? 0.4896 0.4381 0.4929 0.0707  0.0605  0.1184  387 ALA A CB  
2950 N N   . LEU A 389 ? 0.6717 0.6097 0.7125 0.0622  0.0607  0.1299  388 LEU A N   
2951 C CA  . LEU A 389 ? 0.6604 0.5916 0.7176 0.0577  0.0578  0.1275  388 LEU A CA  
2952 C C   . LEU A 389 ? 0.6948 0.6241 0.7678 0.0509  0.0624  0.1299  388 LEU A C   
2953 O O   . LEU A 389 ? 0.6752 0.6015 0.7590 0.0455  0.0605  0.1216  388 LEU A O   
2954 C CB  . LEU A 389 ? 0.6069 0.5339 0.6648 0.0619  0.0555  0.1355  388 LEU A CB  
2955 C CG  . LEU A 389 ? 0.5626 0.4828 0.6336 0.0603  0.0507  0.1312  388 LEU A CG  
2956 C CD1 . LEU A 389 ? 0.6540 0.5725 0.7199 0.0670  0.0469  0.1374  388 LEU A CD1 
2957 C CD2 . LEU A 389 ? 0.6552 0.5683 0.7439 0.0545  0.0537  0.1341  388 LEU A CD2 
2958 N N   . GLY A 390 ? 0.7640 0.6957 0.8382 0.0509  0.0685  0.1412  389 GLY A N   
2959 C CA  . GLY A 390 ? 0.7595 0.6905 0.8494 0.0438  0.0726  0.1441  389 GLY A CA  
2960 C C   . GLY A 390 ? 0.7614 0.6971 0.8532 0.0397  0.0732  0.1348  389 GLY A C   
2961 O O   . GLY A 390 ? 0.8115 0.7450 0.9177 0.0329  0.0735  0.1323  389 GLY A O   
2962 N N   . ALA A 391 ? 0.6304 0.5720 0.7076 0.0439  0.0729  0.1296  390 ALA A N   
2963 C CA  . ALA A 391 ? 0.6478 0.5929 0.7260 0.0406  0.0727  0.1205  390 ALA A CA  
2964 C C   . ALA A 391 ? 0.6786 0.6182 0.7635 0.0362  0.0669  0.1091  390 ALA A C   
2965 O O   . ALA A 391 ? 0.6091 0.5496 0.7010 0.0312  0.0668  0.1032  390 ALA A O   
2966 C CB  . ALA A 391 ? 0.6759 0.6266 0.7361 0.0466  0.0732  0.1174  390 ALA A CB  
2967 N N   . ALA A 392 ? 0.6590 0.5935 0.7418 0.0384  0.0622  0.1063  391 ALA A N   
2968 C CA  . ALA A 392 ? 0.6125 0.5426 0.7026 0.0346  0.0575  0.0963  391 ALA A CA  
2969 C C   . ALA A 392 ? 0.6137 0.5377 0.7208 0.0293  0.0580  0.0979  391 ALA A C   
2970 O O   . ALA A 392 ? 0.6328 0.5548 0.7478 0.0243  0.0562  0.0898  391 ALA A O   
2971 C CB  . ALA A 392 ? 0.6282 0.5567 0.7112 0.0390  0.0524  0.0927  391 ALA A CB  
2972 N N   . GLN A 393 ? 0.5929 0.5133 0.7053 0.0304  0.0602  0.1082  392 GLN A N   
2973 C CA  . GLN A 393 ? 0.6004 0.5135 0.7291 0.0250  0.0606  0.1101  392 GLN A CA  
2974 C C   . GLN A 393 ? 0.5787 0.4951 0.7156 0.0185  0.0636  0.1100  392 GLN A C   
2975 O O   . GLN A 393 ? 0.5914 0.5030 0.7401 0.0126  0.0620  0.1049  392 GLN A O   
2976 C CB  . GLN A 393 ? 0.6667 0.5747 0.7990 0.0274  0.0623  0.1224  392 GLN A CB  
2977 C CG  . GLN A 393 ? 0.7123 0.6216 0.8318 0.0354  0.0609  0.1267  392 GLN A CG  
2978 C CD  . GLN A 393 ? 0.7037 0.6072 0.8268 0.0378  0.0624  0.1396  392 GLN A CD  
2979 O OE1 . GLN A 393 ? 0.6942 0.6021 0.8109 0.0402  0.0667  0.1504  392 GLN A OE1 
2980 N NE2 . GLN A 393 ? 0.7902 0.6838 0.9232 0.0376  0.0592  0.1388  392 GLN A NE2 
2981 N N   . ALA A 394 ? 0.5998 0.5249 0.7306 0.0197  0.0679  0.1154  393 ALA A N   
2982 C CA  . ALA A 394 ? 0.6321 0.5625 0.7706 0.0142  0.0706  0.1151  393 ALA A CA  
2983 C C   . ALA A 394 ? 0.5890 0.5204 0.7267 0.0113  0.0670  0.1022  393 ALA A C   
2984 O O   . ALA A 394 ? 0.5980 0.5292 0.7465 0.0050  0.0664  0.0989  393 ALA A O   
2985 C CB  . ALA A 394 ? 0.6313 0.5720 0.7622 0.0176  0.0762  0.1230  393 ALA A CB  
2986 N N   . TYR A 395 ? 0.6083 0.5407 0.7333 0.0156  0.0643  0.0952  394 TYR A N   
2987 C CA  . TYR A 395 ? 0.5307 0.4636 0.6543 0.0129  0.0608  0.0837  394 TYR A CA  
2988 C C   . TYR A 395 ? 0.5684 0.4939 0.7013 0.0090  0.0571  0.0769  394 TYR A C   
2989 O O   . TYR A 395 ? 0.5940 0.5194 0.7317 0.0042  0.0553  0.0695  394 TYR A O   
2990 C CB  . TYR A 395 ? 0.5440 0.4794 0.6519 0.0181  0.0588  0.0788  394 TYR A CB  
2991 C CG  . TYR A 395 ? 0.5717 0.5060 0.6777 0.0156  0.0547  0.0674  394 TYR A CG  
2992 C CD1 . TYR A 395 ? 0.5403 0.4782 0.6459 0.0125  0.0548  0.0628  394 TYR A CD1 
2993 C CD2 . TYR A 395 ? 0.6031 0.5337 0.7080 0.0165  0.0508  0.0619  394 TYR A CD2 
2994 C CE1 . TYR A 395 ? 0.6157 0.5526 0.7189 0.0100  0.0512  0.0533  394 TYR A CE1 
2995 C CE2 . TYR A 395 ? 0.5703 0.5011 0.6736 0.0139  0.0477  0.0523  394 TYR A CE2 
2996 C CZ  . TYR A 395 ? 0.6015 0.5351 0.7035 0.0105  0.0479  0.0482  394 TYR A CZ  
2997 O OH  . TYR A 395 ? 0.6052 0.5390 0.7052 0.0078  0.0450  0.0396  394 TYR A OH  
2998 N N   . MET A 396 ? 0.5533 0.4726 0.6883 0.0115  0.0558  0.0792  395 MET A N   
2999 C CA  . MET A 396 ? 0.5506 0.4625 0.6941 0.0090  0.0525  0.0725  395 MET A CA  
3000 C C   . MET A 396 ? 0.5656 0.4721 0.7234 0.0030  0.0533  0.0744  395 MET A C   
3001 O O   . MET A 396 ? 0.6228 0.5264 0.7867 -0.0015 0.0510  0.0661  395 MET A O   
3002 C CB  . MET A 396 ? 0.5476 0.4549 0.6894 0.0144  0.0507  0.0746  395 MET A CB  
3003 C CG  . MET A 396 ? 0.5786 0.4790 0.7287 0.0134  0.0476  0.0672  395 MET A CG  
3004 S SD  . MET A 396 ? 0.5776 0.4701 0.7317 0.0193  0.0463  0.0736  395 MET A SD  
3005 C CE  . MET A 396 ? 0.5672 0.4534 0.7302 0.0162  0.0498  0.0859  395 MET A CE  
3006 N N   . ALA A 397 ? 0.5690 0.4742 0.7322 0.0025  0.0563  0.0854  396 ALA A N   
3007 C CA  . ALA A 397 ? 0.5757 0.4749 0.7535 -0.0039 0.0566  0.0879  396 ALA A CA  
3008 C C   . ALA A 397 ? 0.6010 0.5063 0.7833 -0.0101 0.0570  0.0844  396 ALA A C   
3009 O O   . ALA A 397 ? 0.6025 0.5028 0.7962 -0.0164 0.0551  0.0811  396 ALA A O   
3010 C CB  . ALA A 397 ? 0.5619 0.4588 0.7445 -0.0032 0.0601  0.1018  396 ALA A CB  
3011 N N   . THR A 398 ? 0.5515 0.4674 0.7252 -0.0083 0.0591  0.0850  397 THR A N   
3012 C CA  . THR A 398 ? 0.5946 0.5174 0.7724 -0.0133 0.0591  0.0818  397 THR A CA  
3013 C C   . THR A 398 ? 0.5753 0.4949 0.7535 -0.0167 0.0545  0.0691  397 THR A C   
3014 O O   . THR A 398 ? 0.5773 0.4957 0.7651 -0.0230 0.0526  0.0658  397 THR A O   
3015 C CB  . THR A 398 ? 0.5456 0.4793 0.7127 -0.0092 0.0621  0.0843  397 THR A CB  
3016 O OG1 . THR A 398 ? 0.5796 0.5183 0.7487 -0.0075 0.0672  0.0965  397 THR A OG1 
3017 C CG2 . THR A 398 ? 0.5810 0.5213 0.7502 -0.0132 0.0609  0.0786  397 THR A CG2 
3018 N N   . TYR A 399 ? 0.5647 0.4833 0.7323 -0.0126 0.0526  0.0620  398 TYR A N   
3019 C CA  . TYR A 399 ? 0.5229 0.4398 0.6894 -0.0152 0.0489  0.0505  398 TYR A CA  
3020 C C   . TYR A 399 ? 0.5515 0.4583 0.7253 -0.0168 0.0464  0.0454  398 TYR A C   
3021 O O   . TYR A 399 ? 0.5956 0.5007 0.7698 -0.0196 0.0436  0.0359  398 TYR A O   
3022 C CB  . TYR A 399 ? 0.5149 0.4358 0.6678 -0.0107 0.0481  0.0455  398 TYR A CB  
3023 C CG  . TYR A 399 ? 0.5478 0.4771 0.6933 -0.0099 0.0496  0.0473  398 TYR A CG  
3024 C CD1 . TYR A 399 ? 0.5303 0.4635 0.6769 -0.0140 0.0483  0.0426  398 TYR A CD1 
3025 C CD2 . TYR A 399 ? 0.4992 0.4323 0.6363 -0.0045 0.0522  0.0537  398 TYR A CD2 
3026 C CE1 . TYR A 399 ? 0.5193 0.4596 0.6595 -0.0125 0.0495  0.0443  398 TYR A CE1 
3027 C CE2 . TYR A 399 ? 0.5562 0.4962 0.6864 -0.0029 0.0536  0.0548  398 TYR A CE2 
3028 C CZ  . TYR A 399 ? 0.5614 0.5047 0.6935 -0.0068 0.0523  0.0502  398 TYR A CZ  
3029 O OH  . TYR A 399 ? 0.5623 0.5118 0.6878 -0.0045 0.0536  0.0514  398 TYR A OH  
3030 N N   . ILE A 400 ? 0.5443 0.4443 0.7233 -0.0147 0.0472  0.0516  399 ILE A N   
3031 C CA  . ILE A 400 ? 0.5243 0.4132 0.7117 -0.0161 0.0449  0.0472  399 ILE A CA  
3032 C C   . ILE A 400 ? 0.5469 0.4319 0.7458 -0.0238 0.0436  0.0462  399 ILE A C   
3033 O O   . ILE A 400 ? 0.6529 0.5323 0.8552 -0.0269 0.0405  0.0368  399 ILE A O   
3034 C CB  . ILE A 400 ? 0.5889 0.4707 0.7787 -0.0114 0.0459  0.0549  399 ILE A CB  
3035 C CG1 . ILE A 400 ? 0.5957 0.4785 0.7769 -0.0045 0.0448  0.0510  399 ILE A CG1 
3036 C CG2 . ILE A 400 ? 0.5265 0.3954 0.7289 -0.0146 0.0442  0.0547  399 ILE A CG2 
3037 C CD1 . ILE A 400 ? 0.4906 0.3663 0.6744 0.0008  0.0449  0.0575  399 ILE A CD1 
3038 N N   . VAL A 401 ? 0.5226 0.4113 0.7274 -0.0270 0.0458  0.0557  400 VAL A N   
3039 C CA  . VAL A 401 ? 0.5614 0.4480 0.7783 -0.0350 0.0442  0.0554  400 VAL A CA  
3040 C C   . VAL A 401 ? 0.5855 0.4816 0.7998 -0.0387 0.0427  0.0492  400 VAL A C   
3041 O O   . VAL A 401 ? 0.6254 0.5194 0.8480 -0.0454 0.0396  0.0449  400 VAL A O   
3042 C CB  . VAL A 401 ? 0.5886 0.4763 0.8149 -0.0376 0.0474  0.0689  400 VAL A CB  
3043 C CG1 . VAL A 401 ? 0.5807 0.4607 0.8063 -0.0324 0.0494  0.0768  400 VAL A CG1 
3044 C CG2 . VAL A 401 ? 0.5799 0.4825 0.8020 -0.0368 0.0511  0.0753  400 VAL A CG2 
3045 N N   . TYR A 402 ? 0.5768 0.4826 0.7795 -0.0346 0.0443  0.0485  401 TYR A N   
3046 C CA  . TYR A 402 ? 0.5691 0.4832 0.7686 -0.0374 0.0426  0.0429  401 TYR A CA  
3047 C C   . TYR A 402 ? 0.6227 0.5322 0.8183 -0.0389 0.0386  0.0302  401 TYR A C   
3048 O O   . TYR A 402 ? 0.6106 0.5217 0.8097 -0.0442 0.0355  0.0248  401 TYR A O   
3049 C CB  . TYR A 402 ? 0.5017 0.4258 0.6898 -0.0322 0.0455  0.0459  401 TYR A CB  
3050 C CG  . TYR A 402 ? 0.5492 0.4813 0.7331 -0.0342 0.0437  0.0408  401 TYR A CG  
3051 C CD1 . TYR A 402 ? 0.5174 0.4553 0.7106 -0.0395 0.0428  0.0429  401 TYR A CD1 
3052 C CD2 . TYR A 402 ? 0.5348 0.4686 0.7062 -0.0309 0.0427  0.0344  401 TYR A CD2 
3053 C CE1 . TYR A 402 ? 0.5453 0.4906 0.7346 -0.0408 0.0408  0.0387  401 TYR A CE1 
3054 C CE2 . TYR A 402 ? 0.5104 0.4506 0.6776 -0.0326 0.0409  0.0304  401 TYR A CE2 
3055 C CZ  . TYR A 402 ? 0.5428 0.4886 0.7187 -0.0371 0.0400  0.0326  401 TYR A CZ  
3056 O OH  . TYR A 402 ? 0.5561 0.5083 0.7278 -0.0382 0.0378  0.0291  401 TYR A OH  
3057 N N   . PHE A 403 ? 0.5801 0.4848 0.7687 -0.0341 0.0385  0.0256  402 PHE A N   
3058 C CA  . PHE A 403 ? 0.5186 0.4194 0.7038 -0.0349 0.0355  0.0139  402 PHE A CA  
3059 C C   . PHE A 403 ? 0.6063 0.4971 0.8018 -0.0396 0.0325  0.0095  402 PHE A C   
3060 O O   . PHE A 403 ? 0.6445 0.5340 0.8386 -0.0426 0.0295  -0.0001 402 PHE A O   
3061 C CB  . PHE A 403 ? 0.5149 0.4137 0.6926 -0.0286 0.0364  0.0110  402 PHE A CB  
3062 C CG  . PHE A 403 ? 0.5795 0.4763 0.7532 -0.0288 0.0343  -0.0006 402 PHE A CG  
3063 C CD1 . PHE A 403 ? 0.6083 0.5122 0.7743 -0.0307 0.0333  -0.0063 402 PHE A CD1 
3064 C CD2 . PHE A 403 ? 0.6067 0.4947 0.7843 -0.0266 0.0336  -0.0054 402 PHE A CD2 
3065 C CE1 . PHE A 403 ? 0.5851 0.4881 0.7468 -0.0308 0.0319  -0.0164 402 PHE A CE1 
3066 C CE2 . PHE A 403 ? 0.5839 0.4712 0.7576 -0.0261 0.0324  -0.0161 402 PHE A CE2 
3067 C CZ  . PHE A 403 ? 0.6101 0.5053 0.7756 -0.0284 0.0317  -0.0215 402 PHE A CZ  
3068 N N   . SER A 404 ? 0.6436 0.5270 0.8490 -0.0404 0.0333  0.0163  403 SER A N   
3069 C CA  . SER A 404 ? 0.6244 0.4968 0.8403 -0.0455 0.0300  0.0124  403 SER A CA  
3070 C C   . SER A 404 ? 0.5992 0.4762 0.8215 -0.0534 0.0273  0.0120  403 SER A C   
3071 O O   . SER A 404 ? 0.6348 0.5064 0.8601 -0.0580 0.0231  0.0032  403 SER A O   
3072 C CB  . SER A 404 ? 0.6039 0.4665 0.8290 -0.0446 0.0314  0.0212  403 SER A CB  
3073 O OG  . SER A 404 ? 0.5683 0.4301 0.7870 -0.0367 0.0342  0.0245  403 SER A OG  
3074 N N   . LEU A 405 ? 0.6015 0.4892 0.8258 -0.0548 0.0297  0.0212  404 LEU A N   
3075 C CA  . LEU A 405 ? 0.6139 0.5086 0.8452 -0.0618 0.0271  0.0214  404 LEU A CA  
3076 C C   . LEU A 405 ? 0.6329 0.5344 0.8546 -0.0622 0.0244  0.0119  404 LEU A C   
3077 O O   . LEU A 405 ? 0.6645 0.5669 0.8906 -0.0682 0.0199  0.0066  404 LEU A O   
3078 C CB  . LEU A 405 ? 0.6120 0.5177 0.8481 -0.0620 0.0311  0.0341  404 LEU A CB  
3079 C CG  . LEU A 405 ? 0.6066 0.5077 0.8546 -0.0638 0.0338  0.0453  404 LEU A CG  
3080 C CD1 . LEU A 405 ? 0.5302 0.4444 0.7863 -0.0667 0.0366  0.0560  404 LEU A CD1 
3081 C CD2 . LEU A 405 ? 0.6476 0.5345 0.9068 -0.0699 0.0295  0.0414  404 LEU A CD2 
3082 N N   . CYS A 406 ? 0.5712 0.4774 0.7797 -0.0561 0.0266  0.0098  405 CYS A N   
3083 C CA  . CYS A 406 ? 0.5451 0.4568 0.7437 -0.0563 0.0242  0.0014  405 CYS A CA  
3084 C C   . CYS A 406 ? 0.6040 0.5071 0.8010 -0.0585 0.0203  -0.0104 405 CYS A C   
3085 O O   . CYS A 406 ? 0.6147 0.5209 0.8089 -0.0622 0.0166  -0.0172 405 CYS A O   
3086 C CB  . CYS A 406 ? 0.5660 0.4828 0.7515 -0.0497 0.0274  0.0019  405 CYS A CB  
3087 S SG  . CYS A 406 ? 0.6004 0.5300 0.7824 -0.0476 0.0302  0.0109  405 CYS A SG  
3088 N N   . CYS A 407 ? 0.6532 0.5456 0.8516 -0.0557 0.0211  -0.0130 406 CYS A N   
3089 C CA  . CYS A 407 ? 0.6392 0.5226 0.8366 -0.0569 0.0178  -0.0245 406 CYS A CA  
3090 C C   . CYS A 407 ? 0.6324 0.5100 0.8401 -0.0645 0.0130  -0.0271 406 CYS A C   
3091 O O   . CYS A 407 ? 0.6185 0.4946 0.8227 -0.0676 0.0088  -0.0370 406 CYS A O   
3092 C CB  . CYS A 407 ? 0.5640 0.4371 0.7619 -0.0515 0.0199  -0.0259 406 CYS A CB  
3093 S SG  . CYS A 407 ? 0.7277 0.6068 0.9128 -0.0432 0.0238  -0.0280 406 CYS A SG  
3094 N N   . GLY A 408 ? 0.5821 0.4566 0.8025 -0.0677 0.0133  -0.0182 407 GLY A N   
3095 C CA  . GLY A 408 ? 0.5588 0.4279 0.7909 -0.0759 0.0083  -0.0198 407 GLY A CA  
3096 C C   . GLY A 408 ? 0.5943 0.4752 0.8264 -0.0813 0.0048  -0.0209 407 GLY A C   
3097 O O   . GLY A 408 ? 0.6835 0.5611 0.9178 -0.0869 -0.0010 -0.0291 407 GLY A O   
3098 N N   . VAL A 409 ? 0.5830 0.4778 0.8126 -0.0795 0.0080  -0.0130 408 VAL A N   
3099 C CA  . VAL A 409 ? 0.5693 0.4763 0.7991 -0.0836 0.0048  -0.0134 408 VAL A CA  
3100 C C   . VAL A 409 ? 0.5439 0.4520 0.7601 -0.0826 0.0015  -0.0250 408 VAL A C   
3101 O O   . VAL A 409 ? 0.5657 0.4775 0.7827 -0.0878 -0.0040 -0.0301 408 VAL A O   
3102 C CB  . VAL A 409 ? 0.5074 0.4280 0.7368 -0.0804 0.0094  -0.0024 408 VAL A CB  
3103 C CG1 . VAL A 409 ? 0.4497 0.3831 0.6764 -0.0826 0.0063  -0.0037 408 VAL A CG1 
3104 C CG2 . VAL A 409 ? 0.4100 0.3319 0.6543 -0.0829 0.0121  0.0094  408 VAL A CG2 
3105 N N   . PHE A 410 ? 0.5103 0.4158 0.7138 -0.0761 0.0048  -0.0291 409 PHE A N   
3106 C CA  . PHE A 410 ? 0.6067 0.5135 0.7970 -0.0750 0.0025  -0.0396 409 PHE A CA  
3107 C C   . PHE A 410 ? 0.6257 0.5221 0.8173 -0.0789 -0.0026 -0.0507 409 PHE A C   
3108 O O   . PHE A 410 ? 0.6263 0.5255 0.8107 -0.0814 -0.0068 -0.0586 409 PHE A O   
3109 C CB  . PHE A 410 ? 0.5890 0.4956 0.7676 -0.0677 0.0075  -0.0409 409 PHE A CB  
3110 C CG  . PHE A 410 ? 0.6076 0.5168 0.7725 -0.0665 0.0062  -0.0504 409 PHE A CG  
3111 C CD1 . PHE A 410 ? 0.6175 0.5369 0.7749 -0.0678 0.0046  -0.0497 409 PHE A CD1 
3112 C CD2 . PHE A 410 ? 0.6729 0.5745 0.8323 -0.0639 0.0068  -0.0595 409 PHE A CD2 
3113 C CE1 . PHE A 410 ? 0.6488 0.5708 0.7931 -0.0669 0.0037  -0.0575 409 PHE A CE1 
3114 C CE2 . PHE A 410 ? 0.6907 0.5959 0.8372 -0.0628 0.0063  -0.0676 409 PHE A CE2 
3115 C CZ  . PHE A 410 ? 0.6716 0.5870 0.8104 -0.0646 0.0047  -0.0663 409 PHE A CZ  
3116 N N   . LEU A 411 ? 0.5954 0.4792 0.7953 -0.0791 -0.0024 -0.0514 410 LEU A N   
3117 C CA  . LEU A 411 ? 0.5846 0.4565 0.7859 -0.0824 -0.0075 -0.0625 410 LEU A CA  
3118 C C   . LEU A 411 ? 0.6495 0.5231 0.8597 -0.0913 -0.0143 -0.0633 410 LEU A C   
3119 O O   . LEU A 411 ? 0.7460 0.6170 0.9511 -0.0945 -0.0199 -0.0740 410 LEU A O   
3120 C CB  . LEU A 411 ? 0.5979 0.4548 0.8067 -0.0801 -0.0057 -0.0622 410 LEU A CB  
3121 C CG  . LEU A 411 ? 0.5569 0.4103 0.7568 -0.0712 -0.0005 -0.0650 410 LEU A CG  
3122 C CD1 . LEU A 411 ? 0.5818 0.4209 0.7911 -0.0688 0.0009  -0.0625 410 LEU A CD1 
3123 C CD2 . LEU A 411 ? 0.6044 0.4569 0.7914 -0.0688 -0.0019 -0.0787 410 LEU A CD2 
3124 N N   . LEU A 412 ? 0.5696 0.4484 0.7932 -0.0954 -0.0140 -0.0521 411 LEU A N   
3125 C CA  . LEU A 412 ? 0.5975 0.4808 0.8313 -0.1042 -0.0206 -0.0518 411 LEU A CA  
3126 C C   . LEU A 412 ? 0.6637 0.5610 0.8884 -0.1049 -0.0236 -0.0547 411 LEU A C   
3127 O O   . LEU A 412 ? 0.7272 0.6263 0.9547 -0.1113 -0.0308 -0.0601 411 LEU A O   
3128 C CB  . LEU A 412 ? 0.5161 0.4044 0.7667 -0.1078 -0.0185 -0.0379 411 LEU A CB  
3129 C CG  . LEU A 412 ? 0.5269 0.4017 0.7880 -0.1079 -0.0157 -0.0328 411 LEU A CG  
3130 C CD1 . LEU A 412 ? 0.4986 0.3821 0.7733 -0.1100 -0.0118 -0.0173 411 LEU A CD1 
3131 C CD2 . LEU A 412 ? 0.6289 0.4882 0.8978 -0.1146 -0.0226 -0.0412 411 LEU A CD2 
3132 N N   . TRP A 413 ? 0.6731 0.5799 0.8867 -0.0985 -0.0185 -0.0511 412 TRP A N   
3133 C CA  . TRP A 413 ? 0.6697 0.5887 0.8735 -0.0985 -0.0211 -0.0532 412 TRP A CA  
3134 C C   . TRP A 413 ? 0.7339 0.6480 0.9230 -0.0977 -0.0245 -0.0666 412 TRP A C   
3135 O O   . TRP A 413 ? 0.7426 0.6639 0.9255 -0.1003 -0.0296 -0.0707 412 TRP A O   
3136 C CB  . TRP A 413 ? 0.6415 0.5702 0.8381 -0.0919 -0.0147 -0.0450 412 TRP A CB  
3137 C CG  . TRP A 413 ? 0.6933 0.6323 0.8777 -0.0906 -0.0166 -0.0470 412 TRP A CG  
3138 C CD1 . TRP A 413 ? 0.7202 0.6713 0.9083 -0.0932 -0.0200 -0.0425 412 TRP A CD1 
3139 C CD2 . TRP A 413 ? 0.7361 0.6747 0.9032 -0.0862 -0.0150 -0.0534 412 TRP A CD2 
3140 N NE1 . TRP A 413 ? 0.7789 0.7358 0.9524 -0.0905 -0.0210 -0.0455 412 TRP A NE1 
3141 C CE2 . TRP A 413 ? 0.7900 0.7395 0.9504 -0.0866 -0.0178 -0.0520 412 TRP A CE2 
3142 C CE3 . TRP A 413 ? 0.7201 0.6508 0.8773 -0.0819 -0.0115 -0.0596 412 TRP A CE3 
3143 C CZ2 . TRP A 413 ? 0.7340 0.6858 0.8777 -0.0833 -0.0171 -0.0563 412 TRP A CZ2 
3144 C CZ3 . TRP A 413 ? 0.6886 0.6230 0.8300 -0.0788 -0.0105 -0.0640 412 TRP A CZ3 
3145 C CH2 . TRP A 413 ? 0.6487 0.5931 0.7833 -0.0798 -0.0133 -0.0621 412 TRP A CH2 
3146 N N   . ARG A 414 ? 0.7094 0.6118 0.8926 -0.0938 -0.0218 -0.0733 413 ARG A N   
3147 C CA  . ARG A 414 ? 0.7429 0.6413 0.9116 -0.0922 -0.0239 -0.0860 413 ARG A CA  
3148 C C   . ARG A 414 ? 0.7776 0.6681 0.9498 -0.0986 -0.0320 -0.0959 413 ARG A C   
3149 O O   . ARG A 414 ? 0.7989 0.6935 0.9612 -0.1007 -0.0370 -0.1034 413 ARG A O   
3150 C CB  . ARG A 414 ? 0.7175 0.6073 0.8799 -0.0852 -0.0179 -0.0897 413 ARG A CB  
3151 C CG  . ARG A 414 ? 0.8510 0.7349 1.0006 -0.0832 -0.0193 -0.1036 413 ARG A CG  
3152 C CD  . ARG A 414 ? 0.8693 0.7431 1.0182 -0.0768 -0.0141 -0.1070 413 ARG A CD  
3153 N NE  . ARG A 414 ? 0.9837 0.8570 1.1178 -0.0725 -0.0127 -0.1183 413 ARG A NE  
3154 C CZ  . ARG A 414 ? 0.9593 0.8257 1.0909 -0.0661 -0.0083 -0.1233 413 ARG A CZ  
3155 N NH1 . ARG A 414 ? 0.9516 0.8101 1.0940 -0.0632 -0.0053 -0.1183 413 ARG A NH1 
3156 N NH2 . ARG A 414 ? 0.8324 0.7005 0.9503 -0.0623 -0.0068 -0.1333 413 ARG A NH2 
3157 N N   . ARG A 415 ? 0.7969 0.6755 0.9826 -0.1020 -0.0337 -0.0958 414 ARG A N   
3158 C CA  . ARG A 415 ? 0.8401 0.7091 1.0302 -0.1086 -0.0420 -0.1053 414 ARG A CA  
3159 C C   . ARG A 415 ? 0.8550 0.7348 1.0527 -0.1167 -0.0491 -0.1021 414 ARG A C   
3160 O O   . ARG A 415 ? 0.8550 0.7318 1.0508 -0.1220 -0.0573 -0.1116 414 ARG A O   
3161 C CB  . ARG A 415 ? 0.9408 0.7935 1.1449 -0.1105 -0.0420 -0.1045 414 ARG A CB  
3162 C CG  . ARG A 415 ? 0.8982 0.7432 1.0997 -0.1021 -0.0339 -0.1025 414 ARG A CG  
3163 C CD  . ARG A 415 ? 0.9144 0.7392 1.1235 -0.1028 -0.0358 -0.1081 414 ARG A CD  
3164 N NE  . ARG A 415 ? 0.9446 0.7600 1.1403 -0.0963 -0.0348 -0.1215 414 ARG A NE  
3165 C CZ  . ARG A 415 ? 0.9604 0.7575 1.1582 -0.0963 -0.0381 -0.1312 414 ARG A CZ  
3166 N NH1 . ARG A 415 ? 0.9252 0.7100 1.1382 -0.1032 -0.0431 -0.1293 414 ARG A NH1 
3167 N NH2 . ARG A 415 ? 0.9451 0.7361 1.1298 -0.0892 -0.0362 -0.1431 414 ARG A NH2 
3168 N N   . ALA B 2   ? 1.5216 0.4933 0.9142 0.2923  0.1964  0.0086  0   ALA B N   
3169 C CA  . ALA B 2   ? 1.5035 0.5498 0.9089 0.3240  0.1620  0.0177  0   ALA B CA  
3170 C C   . ALA B 2   ? 1.5653 0.6532 0.9951 0.2849  0.1426  0.0026  0   ALA B C   
3171 O O   . ALA B 2   ? 1.4413 0.6048 0.9035 0.2824  0.1201  -0.0134 0   ALA B O   
3172 C CB  . ALA B 2   ? 1.4475 0.5337 0.8667 0.3657  0.1513  0.0066  0   ALA B CB  
3173 N N   . GLN B 3   ? 1.7103 0.7750 1.1365 0.2459  0.1500  0.0079  1   GLN B N   
3174 C CA  . GLN B 3   ? 1.5926 0.7169 1.0511 0.2019  0.1292  -0.0038 1   GLN B CA  
3175 C C   . GLN B 3   ? 1.4718 0.6459 0.9343 0.2173  0.1073  0.0205  1   GLN B C   
3176 O O   . GLN B 3   ? 1.5060 0.6296 0.9336 0.2382  0.1203  0.0453  1   GLN B O   
3177 C CB  . GLN B 3   ? 1.6012 0.6785 1.0609 0.1482  0.1503  -0.0196 1   GLN B CB  
3178 C CG  . GLN B 3   ? 1.6642 0.6844 1.1173 0.1318  0.1787  -0.0429 1   GLN B CG  
3179 C CD  . GLN B 3   ? 1.7364 0.7936 1.2116 0.1026  0.1671  -0.0802 1   GLN B CD  
3180 O OE1 . GLN B 3   ? 1.8511 0.9531 1.3523 0.0597  0.1541  -0.0976 1   GLN B OE1 
3181 N NE2 . GLN B 3   ? 1.6306 0.6853 1.0994 0.1270  0.1697  -0.0916 1   GLN B NE2 
3182 N N   . VAL B 4   ? 1.2723 0.5407 0.7735 0.2070  0.0768  0.0129  2   VAL B N   
3183 C CA  . VAL B 4   ? 1.3346 0.6564 0.8447 0.2172  0.0555  0.0296  2   VAL B CA  
3184 C C   . VAL B 4   ? 1.3106 0.6226 0.8251 0.1757  0.0594  0.0324  2   VAL B C   
3185 O O   . VAL B 4   ? 1.1916 0.5017 0.7243 0.1333  0.0641  0.0139  2   VAL B O   
3186 C CB  . VAL B 4   ? 1.2145 0.6342 0.7660 0.2199  0.0273  0.0178  2   VAL B CB  
3187 C CG1 . VAL B 4   ? 1.1965 0.6275 0.7526 0.2498  0.0291  0.0064  2   VAL B CG1 
3188 C CG2 . VAL B 4   ? 1.1172 0.5766 0.7003 0.1714  0.0182  0.0019  2   VAL B CG2 
3189 N N   . GLN B 5   ? 1.2564 0.5647 0.7533 0.1900  0.0576  0.0537  3   GLN B N   
3190 C CA  . GLN B 5   ? 1.1341 0.4320 0.6338 0.1555  0.0648  0.0577  3   GLN B CA  
3191 C C   . GLN B 5   ? 1.1083 0.4910 0.6406 0.1477  0.0359  0.0569  3   GLN B C   
3192 O O   . GLN B 5   ? 1.0736 0.4969 0.6030 0.1806  0.0185  0.0657  3   GLN B O   
3193 C CB  . GLN B 5   ? 1.2018 0.4225 0.6506 0.1753  0.0909  0.0831  3   GLN B CB  
3194 C CG  . GLN B 5   ? 1.3151 0.4369 0.7372 0.1605  0.1305  0.0805  3   GLN B CG  
3195 C CD  . GLN B 5   ? 1.5216 0.6000 0.9005 0.1991  0.1513  0.1033  3   GLN B CD  
3196 O OE1 . GLN B 5   ? 1.5696 0.6052 0.9276 0.1868  0.1796  0.1137  3   GLN B OE1 
3197 N NE2 . GLN B 5   ? 1.5535 0.6469 0.9200 0.2464  0.1382  0.1092  3   GLN B NE2 
3198 N N   . LEU B 6   ? 1.1113 0.5219 0.6753 0.1057  0.0311  0.0438  4   LEU B N   
3199 C CA  . LEU B 6   ? 1.0167 0.4985 0.6122 0.0952  0.0079  0.0416  4   LEU B CA  
3200 C C   . LEU B 6   ? 1.0196 0.4894 0.6140 0.0744  0.0171  0.0484  4   LEU B C   
3201 O O   . LEU B 6   ? 0.9983 0.4432 0.6016 0.0425  0.0317  0.0387  4   LEU B O   
3202 C CB  . LEU B 6   ? 1.0172 0.5454 0.6487 0.0705  -0.0064 0.0223  4   LEU B CB  
3203 C CG  . LEU B 6   ? 1.0308 0.5702 0.6638 0.0861  -0.0106 0.0129  4   LEU B CG  
3204 C CD1 . LEU B 6   ? 1.0543 0.6168 0.7071 0.0587  -0.0165 -0.0049 4   LEU B CD1 
3205 C CD2 . LEU B 6   ? 1.0009 0.5912 0.6450 0.1139  -0.0260 0.0167  4   LEU B CD2 
3206 N N   . VAL B 7   ? 1.0560 0.5479 0.6415 0.0920  0.0090  0.0615  5   VAL B N   
3207 C CA  . VAL B 7   ? 1.0874 0.5712 0.6691 0.0763  0.0190  0.0686  5   VAL B CA  
3208 C C   . VAL B 7   ? 1.0294 0.5845 0.6454 0.0690  -0.0044 0.0617  5   VAL B C   
3209 O O   . VAL B 7   ? 1.0430 0.6350 0.6566 0.0935  -0.0208 0.0643  5   VAL B O   
3210 C CB  . VAL B 7   ? 1.1343 0.5683 0.6621 0.1065  0.0359  0.0918  5   VAL B CB  
3211 C CG1 . VAL B 7   ? 1.1893 0.6257 0.7133 0.0917  0.0452  0.0981  5   VAL B CG1 
3212 C CG2 . VAL B 7   ? 1.1257 0.4729 0.6165 0.1108  0.0669  0.1001  5   VAL B CG2 
3213 N N   . GLU B 8   ? 0.9761 0.5521 0.6255 0.0362  -0.0054 0.0505  6   GLU B N   
3214 C CA  . GLU B 8   ? 0.9666 0.5995 0.6474 0.0287  -0.0230 0.0445  6   GLU B CA  
3215 C C   . GLU B 8   ? 0.9837 0.6158 0.6550 0.0282  -0.0148 0.0521  6   GLU B C   
3216 O O   . GLU B 8   ? 1.0459 0.6338 0.6929 0.0240  0.0076  0.0605  6   GLU B O   
3217 C CB  . GLU B 8   ? 0.9716 0.6291 0.6894 0.0013  -0.0298 0.0301  6   GLU B CB  
3218 C CG  . GLU B 8   ? 0.9342 0.5958 0.6568 0.0014  -0.0379 0.0216  6   GLU B CG  
3219 C CD  . GLU B 8   ? 0.8881 0.5202 0.6096 -0.0174 -0.0266 0.0110  6   GLU B CD  
3220 O OE1 . GLU B 8   ? 0.9674 0.5702 0.6848 -0.0310 -0.0088 0.0104  6   GLU B OE1 
3221 O OE2 . GLU B 8   ? 0.8585 0.4967 0.5831 -0.0203 -0.0334 0.0009  6   GLU B OE2 
3222 N N   . SER B 9   ? 0.9375 0.6158 0.6272 0.0313  -0.0297 0.0478  7   SER B N   
3223 C CA  . SER B 9   ? 0.9266 0.6110 0.6083 0.0315  -0.0234 0.0516  7   SER B CA  
3224 C C   . SER B 9   ? 0.8921 0.6278 0.6096 0.0243  -0.0388 0.0394  7   SER B C   
3225 O O   . SER B 9   ? 0.7927 0.5558 0.5316 0.0256  -0.0534 0.0314  7   SER B O   
3226 C CB  . SER B 9   ? 0.9707 0.6384 0.6039 0.0628  -0.0204 0.0646  7   SER B CB  
3227 O OG  . SER B 9   ? 0.9649 0.6557 0.5946 0.0873  -0.0384 0.0616  7   SER B OG  
3228 N N   . GLY B 10  ? 0.9495 0.6934 0.6724 0.0162  -0.0315 0.0379  8   GLY B N   
3229 C CA  . GLY B 10  ? 0.7867 0.5703 0.5402 0.0106  -0.0415 0.0261  8   GLY B CA  
3230 C C   . GLY B 10  ? 0.7638 0.5594 0.5566 -0.0093 -0.0416 0.0194  8   GLY B C   
3231 O O   . GLY B 10  ? 0.7560 0.5764 0.5740 -0.0111 -0.0503 0.0116  8   GLY B O   
3232 N N   . GLY B 11  ? 0.8601 0.6393 0.6593 -0.0232 -0.0312 0.0206  9   GLY B N   
3233 C CA  . GLY B 11  ? 0.8428 0.6431 0.6804 -0.0376 -0.0346 0.0117  9   GLY B CA  
3234 C C   . GLY B 11  ? 0.9489 0.7617 0.8037 -0.0459 -0.0220 0.0064  9   GLY B C   
3235 O O   . GLY B 11  ? 1.1438 0.9365 0.9790 -0.0500 -0.0030 0.0101  9   GLY B O   
3236 N N   . GLY B 12  ? 0.8208 0.6634 0.7092 -0.0463 -0.0302 -0.0012 10  GLY B N   
3237 C CA  . GLY B 12  ? 0.7962 0.6560 0.7066 -0.0518 -0.0184 -0.0087 10  GLY B CA  
3238 C C   . GLY B 12  ? 0.7178 0.6095 0.6677 -0.0476 -0.0300 -0.0166 10  GLY B C   
3239 O O   . GLY B 12  ? 0.7594 0.6567 0.7152 -0.0411 -0.0463 -0.0146 10  GLY B O   
3240 N N   . LEU B 13  ? 0.7082 0.6188 0.6812 -0.0483 -0.0199 -0.0247 11  LEU B N   
3241 C CA  . LEU B 13  ? 0.7085 0.6494 0.7194 -0.0386 -0.0286 -0.0320 11  LEU B CA  
3242 C C   . LEU B 13  ? 0.7600 0.6923 0.7663 -0.0252 -0.0280 -0.0304 11  LEU B C   
3243 O O   . LEU B 13  ? 0.7244 0.6526 0.7230 -0.0277 -0.0136 -0.0353 11  LEU B O   
3244 C CB  . LEU B 13  ? 0.6783 0.6513 0.7266 -0.0480 -0.0158 -0.0465 11  LEU B CB  
3245 C CG  . LEU B 13  ? 0.7135 0.7307 0.8070 -0.0366 -0.0302 -0.0571 11  LEU B CG  
3246 C CD1 . LEU B 13  ? 0.6897 0.7453 0.8212 -0.0549 -0.0223 -0.0762 11  LEU B CD1 
3247 C CD2 . LEU B 13  ? 0.6884 0.7168 0.8009 -0.0180 -0.0273 -0.0596 11  LEU B CD2 
3248 N N   . VAL B 14  ? 0.7466 0.6731 0.7545 -0.0117 -0.0409 -0.0248 12  VAL B N   
3249 C CA  . VAL B 14  ? 0.7154 0.6261 0.7208 -0.0019 -0.0365 -0.0253 12  VAL B CA  
3250 C C   . VAL B 14  ? 0.7629 0.6810 0.7927 0.0171  -0.0410 -0.0238 12  VAL B C   
3251 O O   . VAL B 14  ? 0.7533 0.6882 0.7927 0.0260  -0.0546 -0.0193 12  VAL B O   
3252 C CB  . VAL B 14  ? 0.7011 0.5864 0.6799 -0.0036 -0.0406 -0.0190 12  VAL B CB  
3253 C CG1 . VAL B 14  ? 0.7604 0.6303 0.7397 -0.0018 -0.0301 -0.0271 12  VAL B CG1 
3254 C CG2 . VAL B 14  ? 0.7625 0.6454 0.7165 -0.0146 -0.0416 -0.0178 12  VAL B CG2 
3255 N N   . GLN B 15  ? 0.8569 0.7626 0.8949 0.0258  -0.0295 -0.0290 13  GLN B N   
3256 C CA  . GLN B 15  ? 0.7728 0.6751 0.8281 0.0500  -0.0307 -0.0250 13  GLN B CA  
3257 C C   . GLN B 15  ? 0.7590 0.6240 0.7903 0.0610  -0.0348 -0.0091 13  GLN B C   
3258 O O   . GLN B 15  ? 0.7880 0.6339 0.7959 0.0469  -0.0347 -0.0052 13  GLN B O   
3259 C CB  . GLN B 15  ? 0.7692 0.6629 0.8397 0.0553  -0.0124 -0.0372 13  GLN B CB  
3260 C CG  . GLN B 15  ? 0.8186 0.6692 0.8703 0.0488  0.0016  -0.0406 13  GLN B CG  
3261 C CD  . GLN B 15  ? 0.9055 0.7556 0.9669 0.0424  0.0200  -0.0610 13  GLN B CD  
3262 O OE1 . GLN B 15  ? 0.9863 0.8079 1.0548 0.0521  0.0349  -0.0673 13  GLN B OE1 
3263 N NE2 . GLN B 15  ? 0.8970 0.7741 0.9545 0.0268  0.0215  -0.0716 13  GLN B NE2 
3264 N N   . ALA B 16  ? 0.7796 0.6336 0.8154 0.0890  -0.0364 0.0005  14  ALA B N   
3265 C CA  . ALA B 16  ? 0.8391 0.6497 0.8452 0.1030  -0.0354 0.0192  14  ALA B CA  
3266 C C   . ALA B 16  ? 0.8238 0.5835 0.8176 0.0897  -0.0106 0.0156  14  ALA B C   
3267 O O   . ALA B 16  ? 0.8041 0.5523 0.8139 0.0886  0.0060  0.0026  14  ALA B O   
3268 C CB  . ALA B 16  ? 0.7873 0.5948 0.7944 0.1428  -0.0420 0.0326  14  ALA B CB  
3269 N N   . GLY B 17  ? 0.8509 0.5829 0.8191 0.0779  -0.0066 0.0236  15  GLY B N   
3270 C CA  . GLY B 17  ? 0.8354 0.5273 0.7981 0.0597  0.0178  0.0146  15  GLY B CA  
3271 C C   . GLY B 17  ? 0.7880 0.5073 0.7612 0.0295  0.0180  -0.0081 15  GLY B C   
3272 O O   . GLY B 17  ? 0.7603 0.4596 0.7336 0.0113  0.0349  -0.0213 15  GLY B O   
3273 N N   . GLY B 18  ? 0.7835 0.5481 0.7646 0.0246  0.0009  -0.0141 16  GLY B N   
3274 C CA  . GLY B 18  ? 0.7492 0.5386 0.7309 0.0039  -0.0006 -0.0318 16  GLY B CA  
3275 C C   . GLY B 18  ? 0.7993 0.5927 0.7650 -0.0071 -0.0081 -0.0285 16  GLY B C   
3276 O O   . GLY B 18  ? 0.7831 0.5543 0.7378 -0.0040 -0.0063 -0.0156 16  GLY B O   
3277 N N   . SER B 19  ? 0.8894 0.7108 0.8507 -0.0174 -0.0154 -0.0397 17  SER B N   
3278 C CA  . SER B 19  ? 0.7989 0.6302 0.7475 -0.0242 -0.0231 -0.0393 17  SER B CA  
3279 C C   . SER B 19  ? 0.7195 0.5749 0.6543 -0.0225 -0.0360 -0.0374 17  SER B C   
3280 O O   . SER B 19  ? 0.7024 0.5699 0.6362 -0.0217 -0.0345 -0.0440 17  SER B O   
3281 C CB  . SER B 19  ? 0.8057 0.6419 0.7628 -0.0375 -0.0131 -0.0612 17  SER B CB  
3282 O OG  . SER B 19  ? 0.8632 0.7161 0.8288 -0.0420 -0.0086 -0.0831 17  SER B OG  
3283 N N   . LEU B 20  ? 0.6535 0.5106 0.5743 -0.0214 -0.0453 -0.0279 18  LEU B N   
3284 C CA  . LEU B 20  ? 0.5949 0.4624 0.4972 -0.0183 -0.0533 -0.0236 18  LEU B CA  
3285 C C   . LEU B 20  ? 0.5848 0.4541 0.4745 -0.0165 -0.0599 -0.0212 18  LEU B C   
3286 O O   . LEU B 20  ? 0.6976 0.5567 0.5906 -0.0183 -0.0598 -0.0158 18  LEU B O   
3287 C CB  . LEU B 20  ? 0.5735 0.4351 0.4758 -0.0173 -0.0551 -0.0118 18  LEU B CB  
3288 C CG  . LEU B 20  ? 0.6732 0.5312 0.5547 -0.0174 -0.0569 -0.0054 18  LEU B CG  
3289 C CD1 . LEU B 20  ? 0.6844 0.5456 0.5577 -0.0179 -0.0474 -0.0086 18  LEU B CD1 
3290 C CD2 . LEU B 20  ? 0.6942 0.5466 0.5811 -0.0213 -0.0605 0.0016  18  LEU B CD2 
3291 N N   . GLY B 21  ? 0.5618 0.4436 0.4342 -0.0099 -0.0646 -0.0250 19  GLY B N   
3292 C CA  . GLY B 21  ? 0.6112 0.4997 0.4732 -0.0033 -0.0711 -0.0251 19  GLY B CA  
3293 C C   . GLY B 21  ? 0.6173 0.4866 0.4535 0.0049  -0.0737 -0.0099 19  GLY B C   
3294 O O   . GLY B 21  ? 0.6282 0.4873 0.4466 0.0086  -0.0701 -0.0038 19  GLY B O   
3295 N N   . LEU B 22  ? 0.6696 0.5299 0.5024 0.0062  -0.0762 -0.0048 20  LEU B N   
3296 C CA  . LEU B 22  ? 0.6792 0.5160 0.4883 0.0127  -0.0759 0.0062  20  LEU B CA  
3297 C C   . LEU B 22  ? 0.7016 0.5460 0.4955 0.0305  -0.0805 0.0040  20  LEU B C   
3298 O O   . LEU B 22  ? 0.6981 0.5710 0.5085 0.0331  -0.0848 -0.0080 20  LEU B O   
3299 C CB  . LEU B 22  ? 0.7093 0.5299 0.5237 0.0025  -0.0754 0.0109  20  LEU B CB  
3300 C CG  . LEU B 22  ? 0.7620 0.5844 0.5947 -0.0093 -0.0751 0.0115  20  LEU B CG  
3301 C CD1 . LEU B 22  ? 0.7100 0.5279 0.5441 -0.0127 -0.0794 0.0133  20  LEU B CD1 
3302 C CD2 . LEU B 22  ? 0.6927 0.5066 0.5242 -0.0152 -0.0696 0.0135  20  LEU B CD2 
3303 N N   . SER B 23  ? 0.7653 0.5833 0.5288 0.0434  -0.0772 0.0146  21  SER B N   
3304 C CA  . SER B 23  ? 0.7929 0.6124 0.5374 0.0673  -0.0814 0.0154  21  SER B CA  
3305 C C   . SER B 23  ? 0.8171 0.5900 0.5389 0.0696  -0.0721 0.0269  21  SER B C   
3306 O O   . SER B 23  ? 0.8351 0.5759 0.5511 0.0538  -0.0615 0.0333  21  SER B O   
3307 C CB  . SER B 23  ? 0.7160 0.5474 0.4345 0.0917  -0.0859 0.0170  21  SER B CB  
3308 O OG  . SER B 23  ? 0.7801 0.5740 0.4694 0.0902  -0.0738 0.0314  21  SER B OG  
3309 N N   . CYS B 24  ? 0.8293 0.6013 0.5419 0.0887  -0.0747 0.0260  22  CYS B N   
3310 C CA  . CYS B 24  ? 0.8530 0.5770 0.5436 0.0922  -0.0637 0.0337  22  CYS B CA  
3311 C C   . CYS B 24  ? 0.8573 0.5795 0.5258 0.1284  -0.0664 0.0366  22  CYS B C   
3312 O O   . CYS B 24  ? 0.8851 0.6491 0.5749 0.1385  -0.0765 0.0243  22  CYS B O   
3313 C CB  . CYS B 24  ? 0.8854 0.6104 0.5976 0.0704  -0.0631 0.0247  22  CYS B CB  
3314 S SG  . CYS B 24  ? 1.1131 0.7941 0.8040 0.0784  -0.0523 0.0245  22  CYS B SG  
3315 N N   . ALA B 25  ? 0.8665 0.5398 0.4923 0.1493  -0.0553 0.0527  23  ALA B N   
3316 C CA  . ALA B 25  ? 0.8676 0.5329 0.4645 0.1923  -0.0577 0.0592  23  ALA B CA  
3317 C C   . ALA B 25  ? 0.9749 0.5900 0.5601 0.1952  -0.0433 0.0611  23  ALA B C   
3318 O O   . ALA B 25  ? 1.0064 0.5614 0.5759 0.1749  -0.0233 0.0674  23  ALA B O   
3319 C CB  . ALA B 25  ? 0.9361 0.5679 0.4816 0.2207  -0.0514 0.0793  23  ALA B CB  
3320 N N   . ALA B 26  ? 0.9740 0.6169 0.5702 0.2190  -0.0518 0.0519  24  ALA B N   
3321 C CA  . ALA B 26  ? 1.0202 0.6205 0.6067 0.2255  -0.0384 0.0502  24  ALA B CA  
3322 C C   . ALA B 26  ? 1.0885 0.6498 0.6306 0.2769  -0.0323 0.0656  24  ALA B C   
3323 O O   . ALA B 26  ? 1.1106 0.7195 0.6509 0.3153  -0.0497 0.0659  24  ALA B O   
3324 C CB  . ALA B 26  ? 0.9744 0.6292 0.6027 0.2177  -0.0477 0.0288  24  ALA B CB  
3325 N N   . SER B 27  ? 1.1734 0.6488 0.6797 0.2790  -0.0070 0.0768  25  SER B N   
3326 C CA  . SER B 27  ? 1.2914 0.7092 0.7455 0.3303  0.0051  0.0963  25  SER B CA  
3327 C C   . SER B 27  ? 1.3946 0.8209 0.8592 0.3584  0.0037  0.0847  25  SER B C   
3328 O O   . SER B 27  ? 1.3250 0.7383 0.8114 0.3298  0.0139  0.0682  25  SER B O   
3329 C CB  . SER B 27  ? 1.3413 0.6503 0.7491 0.3170  0.0406  0.1140  25  SER B CB  
3330 O OG  . SER B 27  ? 1.4451 0.7191 0.8086 0.3569  0.0547  0.1325  25  SER B OG  
3331 N N   . GLY B 28  ? 1.6574 1.1104 1.1065 0.4163  -0.0096 0.0913  26  GLY B N   
3332 C CA  . GLY B 28  ? 1.7410 1.2047 1.1993 0.4522  -0.0102 0.0809  26  GLY B CA  
3333 C C   . GLY B 28  ? 1.7395 1.3222 1.2489 0.4716  -0.0414 0.0588  26  GLY B C   
3334 O O   . GLY B 28  ? 1.6673 1.3228 1.2092 0.4504  -0.0613 0.0483  26  GLY B O   
3335 N N   . ARG B 29  ? 1.6249 1.2254 1.1434 0.5122  -0.0425 0.0491  27  ARG B N   
3336 C CA  . ARG B 29  ? 1.5294 1.2454 1.1038 0.5314  -0.0671 0.0223  27  ARG B CA  
3337 C C   . ARG B 29  ? 1.4563 1.2082 1.0862 0.4811  -0.0596 -0.0053 27  ARG B C   
3338 O O   . ARG B 29  ? 1.4506 1.1422 1.0711 0.4371  -0.0403 -0.0027 27  ARG B O   
3339 C CB  . ARG B 29  ? 1.5002 1.2279 1.0592 0.5948  -0.0704 0.0242  27  ARG B CB  
3340 C CG  . ARG B 29  ? 1.3719 1.2261 0.9910 0.6225  -0.0957 -0.0069 27  ARG B CG  
3341 C CD  . ARG B 29  ? 1.3903 1.3339 1.0293 0.6226  -0.1250 -0.0166 27  ARG B CD  
3342 N NE  . ARG B 29  ? 1.4008 1.4160 1.1046 0.5752  -0.1333 -0.0439 27  ARG B NE  
3343 C CZ  . ARG B 29  ? 1.3110 1.3171 1.0140 0.5264  -0.1339 -0.0390 27  ARG B CZ  
3344 N NH1 . ARG B 29  ? 1.3055 1.2417 0.9493 0.5297  -0.1314 -0.0088 27  ARG B NH1 
3345 N NH2 . ARG B 29  ? 1.1353 1.2005 0.8972 0.4736  -0.1339 -0.0648 27  ARG B NH2 
3346 N N   . THR B 30  ? 1.3891 1.2428 1.0767 0.4874  -0.0740 -0.0335 28  THR B N   
3347 C CA  . THR B 30  ? 1.3383 1.2332 1.0769 0.4420  -0.0648 -0.0593 28  THR B CA  
3348 C C   . THR B 30  ? 1.3155 1.2074 1.0644 0.3801  -0.0636 -0.0580 28  THR B C   
3349 O O   . THR B 30  ? 1.3659 1.2454 1.1278 0.3390  -0.0492 -0.0664 28  THR B O   
3350 C CB  . THR B 30  ? 1.4029 1.2372 1.1269 0.4410  -0.0402 -0.0617 28  THR B CB  
3351 O OG1 . THR B 30  ? 1.5508 1.2867 1.2295 0.4107  -0.0241 -0.0426 28  THR B OG1 
3352 C CG2 . THR B 30  ? 1.4283 1.2503 1.1350 0.5077  -0.0388 -0.0591 28  THR B CG2 
3353 N N   . PHE B 31  ? 1.1451 1.0480 0.8846 0.3768  -0.0786 -0.0472 29  PHE B N   
3354 C CA  . PHE B 31  ? 1.0528 0.9626 0.8075 0.3239  -0.0790 -0.0480 29  PHE B CA  
3355 C C   . PHE B 31  ? 0.9535 0.9458 0.7687 0.2972  -0.0807 -0.0764 29  PHE B C   
3356 O O   . PHE B 31  ? 0.9019 0.8850 0.7290 0.2519  -0.0710 -0.0786 29  PHE B O   
3357 C CB  . PHE B 31  ? 0.9943 0.9016 0.7263 0.3307  -0.0932 -0.0331 29  PHE B CB  
3358 C CG  . PHE B 31  ? 0.9096 0.8294 0.6604 0.2822  -0.0945 -0.0356 29  PHE B CG  
3359 C CD1 . PHE B 31  ? 0.9505 0.8038 0.6767 0.2494  -0.0825 -0.0191 29  PHE B CD1 
3360 C CD2 . PHE B 31  ? 0.8339 0.8335 0.6291 0.2703  -0.1069 -0.0569 29  PHE B CD2 
3361 C CE1 . PHE B 31  ? 0.8978 0.7633 0.6411 0.2108  -0.0843 -0.0208 29  PHE B CE1 
3362 C CE2 . PHE B 31  ? 0.7677 0.7704 0.5775 0.2288  -0.1053 -0.0584 29  PHE B CE2 
3363 C CZ  . PHE B 31  ? 0.7779 0.7133 0.5604 0.2018  -0.0948 -0.0386 29  PHE B CZ  
3364 N N   . SER B 32  ? 0.9337 1.0065 0.7874 0.3257  -0.0912 -0.0992 30  SER B N   
3365 C CA  . SER B 32  ? 0.8762 1.0279 0.7925 0.2979  -0.0866 -0.1305 30  SER B CA  
3366 C C   . SER B 32  ? 0.8332 0.9674 0.7609 0.2761  -0.0619 -0.1385 30  SER B C   
3367 O O   . SER B 32  ? 0.7884 0.9614 0.7557 0.2410  -0.0487 -0.1574 30  SER B O   
3368 C CB  . SER B 32  ? 0.8184 1.0702 0.7790 0.3348  -0.1040 -0.1588 30  SER B CB  
3369 O OG  . SER B 32  ? 0.8511 1.0954 0.7923 0.3899  -0.1087 -0.1540 30  SER B OG  
3370 N N   . ASN B 33  ? 0.8835 0.9565 0.7742 0.2961  -0.0527 -0.1252 31  ASN B N   
3371 C CA  . ASN B 33  ? 0.9394 0.9912 0.8319 0.2788  -0.0294 -0.1333 31  ASN B CA  
3372 C C   . ASN B 33  ? 0.9651 0.9405 0.8178 0.2401  -0.0180 -0.1153 31  ASN B C   
3373 O O   . ASN B 33  ? 0.9331 0.8866 0.7778 0.2242  0.0003  -0.1211 31  ASN B O   
3374 C CB  . ASN B 33  ? 1.0017 1.0351 0.8799 0.3245  -0.0244 -0.1355 31  ASN B CB  
3375 C CG  . ASN B 33  ? 0.9322 1.0452 0.8466 0.3732  -0.0401 -0.1525 31  ASN B CG  
3376 O OD1 . ASN B 33  ? 0.9115 1.1007 0.8657 0.3693  -0.0552 -0.1674 31  ASN B OD1 
3377 N ND2 . ASN B 33  ? 0.9206 1.0183 0.8220 0.4210  -0.0369 -0.1530 31  ASN B ND2 
3378 N N   . TYR B 34  ? 0.9416 0.8817 0.7699 0.2262  -0.0289 -0.0958 32  TYR B N   
3379 C CA  . TYR B 34  ? 0.9548 0.8306 0.7485 0.1942  -0.0222 -0.0811 32  TYR B CA  
3380 C C   . TYR B 34  ? 0.9160 0.8135 0.7268 0.1552  -0.0216 -0.0816 32  TYR B C   
3381 O O   . TYR B 34  ? 0.8923 0.8391 0.7347 0.1509  -0.0288 -0.0881 32  TYR B O   
3382 C CB  . TYR B 34  ? 0.9473 0.7655 0.7034 0.2040  -0.0303 -0.0601 32  TYR B CB  
3383 C CG  . TYR B 34  ? 1.0758 0.8338 0.7975 0.2307  -0.0206 -0.0547 32  TYR B CG  
3384 C CD1 . TYR B 34  ? 1.1381 0.9043 0.8663 0.2538  -0.0102 -0.0686 32  TYR B CD1 
3385 C CD2 . TYR B 34  ? 1.1299 0.8193 0.8133 0.2315  -0.0177 -0.0372 32  TYR B CD2 
3386 C CE1 . TYR B 34  ? 1.1972 0.9005 0.8925 0.2794  0.0018  -0.0644 32  TYR B CE1 
3387 C CE2 . TYR B 34  ? 1.1913 0.8152 0.8418 0.2535  -0.0030 -0.0330 32  TYR B CE2 
3388 C CZ  . TYR B 34  ? 1.2279 0.8566 0.8832 0.2785  0.0062  -0.0463 32  TYR B CZ  
3389 O OH  . TYR B 34  ? 1.2388 0.7948 0.8599 0.3016  0.0238  -0.0429 32  TYR B OH  
3390 N N   . VAL B 35  ? 0.9387 0.7982 0.7263 0.1285  -0.0127 -0.0761 33  VAL B N   
3391 C CA  . VAL B 35  ? 0.9157 0.7808 0.7076 0.0966  -0.0108 -0.0714 33  VAL B CA  
3392 C C   . VAL B 35  ? 0.9175 0.7469 0.6878 0.0868  -0.0239 -0.0546 33  VAL B C   
3393 O O   . VAL B 35  ? 0.9177 0.7031 0.6591 0.0875  -0.0251 -0.0490 33  VAL B O   
3394 C CB  . VAL B 35  ? 0.9073 0.7579 0.6819 0.0791  0.0061  -0.0753 33  VAL B CB  
3395 C CG1 . VAL B 35  ? 0.8201 0.6582 0.5824 0.0532  0.0061  -0.0634 33  VAL B CG1 
3396 C CG2 . VAL B 35  ? 0.8681 0.7609 0.6712 0.0826  0.0244  -0.0933 33  VAL B CG2 
3397 N N   . MET B 36  ? 0.9458 0.7958 0.7337 0.0763  -0.0313 -0.0498 34  MET B N   
3398 C CA  . MET B 36  ? 0.8891 0.7143 0.6637 0.0675  -0.0422 -0.0360 34  MET B CA  
3399 C C   . MET B 36  ? 0.8684 0.6879 0.6402 0.0430  -0.0401 -0.0301 34  MET B C   
3400 O O   . MET B 36  ? 0.8856 0.7240 0.6706 0.0330  -0.0298 -0.0345 34  MET B O   
3401 C CB  . MET B 36  ? 0.9044 0.7547 0.6958 0.0785  -0.0528 -0.0348 34  MET B CB  
3402 C CG  . MET B 36  ? 0.8458 0.7056 0.6347 0.1112  -0.0575 -0.0381 34  MET B CG  
3403 S SD  . MET B 36  ? 0.9836 0.7778 0.7291 0.1254  -0.0579 -0.0205 34  MET B SD  
3404 C CE  . MET B 36  ? 0.8931 0.6709 0.6260 0.1548  -0.0489 -0.0269 34  MET B CE  
3405 N N   . ALA B 37  ? 0.8325 0.6251 0.5873 0.0346  -0.0480 -0.0207 35  ALA B N   
3406 C CA  . ALA B 37  ? 0.8657 0.6538 0.6145 0.0187  -0.0495 -0.0139 35  ALA B CA  
3407 C C   . ALA B 37  ? 0.8307 0.6082 0.5792 0.0133  -0.0609 -0.0069 35  ALA B C   
3408 O O   . ALA B 37  ? 0.8295 0.5931 0.5745 0.0180  -0.0637 -0.0071 35  ALA B O   
3409 C CB  . ALA B 37  ? 0.8175 0.5901 0.5390 0.0146  -0.0451 -0.0160 35  ALA B CB  
3410 N N   . TRP B 38  ? 0.8291 0.6105 0.5800 0.0045  -0.0643 -0.0003 36  TRP B N   
3411 C CA  . TRP B 38  ? 0.8133 0.5922 0.5690 -0.0009 -0.0741 0.0039  36  TRP B CA  
3412 C C   . TRP B 38  ? 0.8165 0.5930 0.5567 -0.0049 -0.0814 0.0043  36  TRP B C   
3413 O O   . TRP B 38  ? 0.7826 0.5583 0.5067 -0.0020 -0.0782 0.0085  36  TRP B O   
3414 C CB  . TRP B 38  ? 0.7858 0.5780 0.5622 -0.0026 -0.0739 0.0092  36  TRP B CB  
3415 C CG  . TRP B 38  ? 0.8031 0.6032 0.5925 0.0020  -0.0737 0.0066  36  TRP B CG  
3416 C CD1 . TRP B 38  ? 0.7728 0.5921 0.5757 0.0075  -0.0696 0.0007  36  TRP B CD1 
3417 C CD2 . TRP B 38  ? 0.8052 0.5967 0.5928 0.0027  -0.0771 0.0085  36  TRP B CD2 
3418 N NE1 . TRP B 38  ? 0.8446 0.6697 0.6492 0.0158  -0.0740 -0.0001 36  TRP B NE1 
3419 C CE2 . TRP B 38  ? 0.8074 0.6102 0.5994 0.0129  -0.0762 0.0070  36  TRP B CE2 
3420 C CE3 . TRP B 38  ? 0.7885 0.5660 0.5719 -0.0051 -0.0789 0.0094  36  TRP B CE3 
3421 C CZ2 . TRP B 38  ? 0.7797 0.5721 0.5623 0.0185  -0.0758 0.0113  36  TRP B CZ2 
3422 C CZ3 . TRP B 38  ? 0.7964 0.5626 0.5772 -0.0045 -0.0746 0.0117  36  TRP B CZ3 
3423 C CH2 . TRP B 38  ? 0.7896 0.5592 0.5653 0.0085  -0.0725 0.0151  36  TRP B CH2 
3424 N N   . PHE B 39  ? 0.9143 0.6913 0.6583 -0.0110 -0.0902 -0.0011 37  PHE B N   
3425 C CA  . PHE B 39  ? 0.9245 0.7127 0.6597 -0.0131 -0.1021 -0.0063 37  PHE B CA  
3426 C C   . PHE B 39  ? 0.8973 0.7017 0.6573 -0.0188 -0.1100 -0.0086 37  PHE B C   
3427 O O   . PHE B 39  ? 0.9039 0.7023 0.6810 -0.0250 -0.1034 -0.0088 37  PHE B O   
3428 C CB  . PHE B 39  ? 0.9175 0.6984 0.6360 -0.0187 -0.1034 -0.0229 37  PHE B CB  
3429 C CG  . PHE B 39  ? 0.9722 0.7440 0.6618 -0.0114 -0.0976 -0.0228 37  PHE B CG  
3430 C CD1 . PHE B 39  ? 1.0081 0.7626 0.6949 -0.0083 -0.0836 -0.0234 37  PHE B CD1 
3431 C CD2 . PHE B 39  ? 0.9850 0.7672 0.6477 -0.0049 -0.1058 -0.0229 37  PHE B CD2 
3432 C CE1 . PHE B 39  ? 1.0478 0.7969 0.7115 -0.0026 -0.0752 -0.0257 37  PHE B CE1 
3433 C CE2 . PHE B 39  ? 0.9099 0.6811 0.5414 0.0011  -0.0966 -0.0228 37  PHE B CE2 
3434 C CZ  . PHE B 39  ? 0.9214 0.6768 0.5563 0.0004  -0.0800 -0.0252 37  PHE B CZ  
3435 N N   . ARG B 40  ? 0.8123 0.6392 0.5721 -0.0139 -0.1236 -0.0104 38  ARG B N   
3436 C CA  . ARG B 40  ? 0.8083 0.6603 0.5970 -0.0179 -0.1318 -0.0165 38  ARG B CA  
3437 C C   . ARG B 40  ? 0.8749 0.7588 0.6638 -0.0186 -0.1491 -0.0350 38  ARG B C   
3438 O O   . ARG B 40  ? 0.9805 0.8664 0.7399 -0.0107 -0.1569 -0.0380 38  ARG B O   
3439 C CB  . ARG B 40  ? 0.7606 0.6182 0.5587 -0.0048 -0.1326 -0.0006 38  ARG B CB  
3440 C CG  . ARG B 40  ? 0.8527 0.7136 0.6259 0.0154  -0.1414 0.0107  38  ARG B CG  
3441 C CD  . ARG B 40  ? 0.8259 0.6931 0.6134 0.0295  -0.1429 0.0223  38  ARG B CD  
3442 N NE  . ARG B 40  ? 0.9475 0.8028 0.7015 0.0533  -0.1458 0.0389  38  ARG B NE  
3443 C CZ  . ARG B 40  ? 0.9431 0.7680 0.6880 0.0636  -0.1311 0.0574  38  ARG B CZ  
3444 N NH1 . ARG B 40  ? 0.8383 0.6501 0.6090 0.0516  -0.1159 0.0579  38  ARG B NH1 
3445 N NH2 . ARG B 40  ? 0.9756 0.7802 0.6814 0.0869  -0.1299 0.0751  38  ARG B NH2 
3446 N N   . GLN B 41  ? 0.8514 0.7651 0.6749 -0.0284 -0.1544 -0.0503 39  GLN B N   
3447 C CA  . GLN B 41  ? 0.8504 0.8083 0.6854 -0.0320 -0.1722 -0.0762 39  GLN B CA  
3448 C C   . GLN B 41  ? 0.8773 0.8799 0.7537 -0.0293 -0.1814 -0.0838 39  GLN B C   
3449 O O   . GLN B 41  ? 0.8444 0.8475 0.7547 -0.0484 -0.1673 -0.0921 39  GLN B O   
3450 C CB  . GLN B 41  ? 0.8418 0.7904 0.6843 -0.0592 -0.1622 -0.1026 39  GLN B CB  
3451 C CG  . GLN B 41  ? 0.8828 0.8752 0.7281 -0.0644 -0.1808 -0.1349 39  GLN B CG  
3452 C CD  . GLN B 41  ? 0.9480 0.9149 0.7893 -0.0906 -0.1661 -0.1597 39  GLN B CD  
3453 O OE1 . GLN B 41  ? 1.0546 1.0189 0.8651 -0.0871 -0.1732 -0.1705 39  GLN B OE1 
3454 N NE2 . GLN B 41  ? 0.9601 0.9023 0.8285 -0.1161 -0.1426 -0.1685 39  GLN B NE2 
3455 N N   . ALA B 42  ? 0.8871 0.9255 0.7577 -0.0028 -0.2032 -0.0802 40  ALA B N   
3456 C CA  . ALA B 42  ? 0.8654 0.9549 0.7771 0.0062  -0.2150 -0.0897 40  ALA B CA  
3457 C C   . ALA B 42  ? 0.9515 1.0970 0.9062 -0.0169 -0.2229 -0.1314 40  ALA B C   
3458 O O   . ALA B 42  ? 0.9594 1.1085 0.9025 -0.0321 -0.2263 -0.1526 40  ALA B O   
3459 C CB  . ALA B 42  ? 0.9698 1.0796 0.8566 0.0473  -0.2371 -0.0738 40  ALA B CB  
3460 N N   . PRO B 43  ? 0.9562 1.1471 0.9642 -0.0225 -0.2231 -0.1472 41  PRO B N   
3461 C CA  . PRO B 43  ? 0.9177 1.1692 0.9755 -0.0487 -0.2275 -0.1927 41  PRO B CA  
3462 C C   . PRO B 43  ? 0.9185 1.2363 0.9716 -0.0301 -0.2629 -0.2177 41  PRO B C   
3463 O O   . PRO B 43  ? 0.9442 1.3111 0.9999 0.0071  -0.2892 -0.2131 41  PRO B O   
3464 C CB  . PRO B 43  ? 0.8775 1.1677 0.9924 -0.0516 -0.2202 -0.2006 41  PRO B CB  
3465 C CG  . PRO B 43  ? 0.9340 1.1764 1.0254 -0.0289 -0.2105 -0.1593 41  PRO B CG  
3466 C CD  . PRO B 43  ? 0.9567 1.1476 0.9839 -0.0061 -0.2174 -0.1279 41  PRO B CD  
3467 N N   . GLY B 44  ? 0.9574 1.2765 1.0006 -0.0531 -0.2636 -0.2449 42  GLY B N   
3468 C CA  . GLY B 44  ? 0.9743 1.3562 1.0053 -0.0365 -0.2978 -0.2721 42  GLY B CA  
3469 C C   . GLY B 44  ? 1.0069 1.3521 0.9604 -0.0025 -0.3118 -0.2414 42  GLY B C   
3470 O O   . GLY B 44  ? 0.9922 1.3904 0.9228 0.0274  -0.3445 -0.2525 42  GLY B O   
3471 N N   . LYS B 45  ? 1.0565 1.3155 0.9679 -0.0049 -0.2873 -0.2045 43  LYS B N   
3472 C CA  . LYS B 45  ? 1.0746 1.2939 0.9145 0.0237  -0.2931 -0.1748 43  LYS B CA  
3473 C C   . LYS B 45  ? 1.0589 1.2238 0.8696 -0.0015 -0.2730 -0.1788 43  LYS B C   
3474 O O   . LYS B 45  ? 1.1230 1.2934 0.9626 -0.0363 -0.2630 -0.2127 43  LYS B O   
3475 C CB  . LYS B 45  ? 1.0657 1.2366 0.8828 0.0496  -0.2818 -0.1265 43  LYS B CB  
3476 C CG  . LYS B 45  ? 1.0999 1.2987 0.8900 0.0977  -0.3061 -0.1079 43  LYS B CG  
3477 C CD  . LYS B 45  ? 1.0322 1.3118 0.8779 0.1078  -0.3288 -0.1329 43  LYS B CD  
3478 C CE  . LYS B 45  ? 0.9729 1.2665 0.7920 0.1622  -0.3478 -0.1061 43  LYS B CE  
3479 N NZ  . LYS B 45  ? 0.9423 1.3248 0.8194 0.1773  -0.3726 -0.1334 43  LYS B NZ  
3480 N N   . GLU B 46  ? 1.0587 1.1692 0.8137 0.0157  -0.2638 -0.1458 44  GLU B N   
3481 C CA  . GLU B 46  ? 1.0459 1.1068 0.7710 -0.0012 -0.2449 -0.1473 44  GLU B CA  
3482 C C   . GLU B 46  ? 1.0016 0.9975 0.7177 -0.0020 -0.2176 -0.1115 44  GLU B C   
3483 O O   . GLU B 46  ? 1.0076 0.9936 0.7245 0.0151  -0.2153 -0.0831 44  GLU B O   
3484 C CB  . GLU B 46  ? 1.1394 1.2065 0.8037 0.0202  -0.2594 -0.1490 44  GLU B CB  
3485 C CG  . GLU B 46  ? 1.1835 1.2139 0.8225 0.0010  -0.2428 -0.1635 44  GLU B CG  
3486 C CD  . GLU B 46  ? 1.1889 1.2381 0.7704 0.0192  -0.2593 -0.1751 44  GLU B CD  
3487 O OE1 . GLU B 46  ? 1.2254 1.3043 0.7744 0.0526  -0.2812 -0.1616 44  GLU B OE1 
3488 O OE2 . GLU B 46  ? 1.1856 1.2168 0.7501 0.0027  -0.2492 -0.1971 44  GLU B OE2 
3489 N N   . ARG B 47  ? 1.1213 1.0752 0.8308 -0.0213 -0.1968 -0.1161 45  ARG B N   
3490 C CA  . ARG B 47  ? 1.1666 1.0688 0.8680 -0.0203 -0.1737 -0.0880 45  ARG B CA  
3491 C C   . ARG B 47  ? 1.2241 1.1113 0.8842 0.0047  -0.1730 -0.0601 45  ARG B C   
3492 O O   . ARG B 47  ? 1.2637 1.1495 0.8823 0.0145  -0.1768 -0.0631 45  ARG B O   
3493 C CB  . ARG B 47  ? 1.1862 1.0516 0.8810 -0.0373 -0.1549 -0.1001 45  ARG B CB  
3494 C CG  . ARG B 47  ? 1.1331 0.9798 0.8633 -0.0592 -0.1393 -0.1093 45  ARG B CG  
3495 C CD  . ARG B 47  ? 1.1309 0.9320 0.8459 -0.0679 -0.1192 -0.1168 45  ARG B CD  
3496 N NE  . ARG B 47  ? 1.1828 0.9568 0.9219 -0.0873 -0.1012 -0.1257 45  ARG B NE  
3497 C CZ  . ARG B 47  ? 1.2652 0.9927 0.9934 -0.0953 -0.0807 -0.1344 45  ARG B CZ  
3498 N NH1 . ARG B 47  ? 1.2816 0.9900 0.9807 -0.0864 -0.0769 -0.1383 45  ARG B NH1 
3499 N NH2 . ARG B 47  ? 1.2333 0.9287 0.9777 -0.1112 -0.0607 -0.1385 45  ARG B NH2 
3500 N N   . GLU B 48  ? 0.9890 0.8621 0.6589 0.0135  -0.1649 -0.0345 46  GLU B N   
3501 C CA  . GLU B 48  ? 0.9584 0.8092 0.5937 0.0330  -0.1570 -0.0081 46  GLU B CA  
3502 C C   . GLU B 48  ? 0.9144 0.7312 0.5605 0.0245  -0.1325 0.0056  46  GLU B C   
3503 O O   . GLU B 48  ? 0.8956 0.7112 0.5775 0.0123  -0.1271 0.0027  46  GLU B O   
3504 C CB  . GLU B 48  ? 0.9690 0.8342 0.6042 0.0543  -0.1685 0.0077  46  GLU B CB  
3505 C CG  . GLU B 48  ? 1.0135 0.9062 0.6997 0.0470  -0.1772 -0.0012 46  GLU B CG  
3506 C CD  . GLU B 48  ? 1.0876 0.9862 0.7755 0.0709  -0.1831 0.0172  46  GLU B CD  
3507 O OE1 . GLU B 48  ? 1.1449 1.0067 0.8021 0.0859  -0.1693 0.0421  46  GLU B OE1 
3508 O OE2 . GLU B 48  ? 1.0765 1.0147 0.7976 0.0745  -0.1988 0.0055  46  GLU B OE2 
3509 N N   . PHE B 49  ? 0.9212 0.7136 0.5352 0.0317  -0.1170 0.0189  47  PHE B N   
3510 C CA  . PHE B 49  ? 0.8161 0.5871 0.4440 0.0232  -0.0940 0.0256  47  PHE B CA  
3511 C C   . PHE B 49  ? 0.8394 0.6058 0.4938 0.0235  -0.0875 0.0386  47  PHE B C   
3512 O O   . PHE B 49  ? 0.8929 0.6570 0.5385 0.0358  -0.0924 0.0512  47  PHE B O   
3513 C CB  . PHE B 49  ? 0.8571 0.6072 0.4475 0.0282  -0.0752 0.0332  47  PHE B CB  
3514 C CG  . PHE B 49  ? 0.8393 0.5789 0.4509 0.0181  -0.0512 0.0335  47  PHE B CG  
3515 C CD1 . PHE B 49  ? 0.8198 0.5687 0.4555 0.0100  -0.0494 0.0180  47  PHE B CD1 
3516 C CD2 . PHE B 49  ? 0.8380 0.5590 0.4456 0.0178  -0.0290 0.0474  47  PHE B CD2 
3517 C CE1 . PHE B 49  ? 0.7859 0.5376 0.4449 0.0048  -0.0310 0.0145  47  PHE B CE1 
3518 C CE2 . PHE B 49  ? 0.8306 0.5533 0.4658 0.0059  -0.0072 0.0406  47  PHE B CE2 
3519 C CZ  . PHE B 49  ? 0.7871 0.5310 0.4495 0.0009  -0.0108 0.0233  47  PHE B CZ  
3520 N N   . VAL B 50  ? 0.8251 0.5910 0.5105 0.0122  -0.0768 0.0341  48  VAL B N   
3521 C CA  . VAL B 50  ? 0.7925 0.5564 0.5044 0.0095  -0.0692 0.0406  48  VAL B CA  
3522 C C   . VAL B 50  ? 0.7447 0.5006 0.4655 0.0020  -0.0466 0.0389  48  VAL B C   
3523 O O   . VAL B 50  ? 0.7613 0.4985 0.4744 0.0017  -0.0290 0.0481  48  VAL B O   
3524 C CB  . VAL B 50  ? 0.7722 0.5532 0.5167 0.0034  -0.0798 0.0321  48  VAL B CB  
3525 C CG1 . VAL B 50  ? 0.6992 0.4800 0.4681 0.0008  -0.0717 0.0355  48  VAL B CG1 
3526 C CG2 . VAL B 50  ? 0.7696 0.5646 0.5141 0.0065  -0.0983 0.0286  48  VAL B CG2 
3527 N N   . ALA B 51  ? 0.7153 0.4854 0.4531 -0.0034 -0.0453 0.0259  49  ALA B N   
3528 C CA  . ALA B 51  ? 0.7383 0.5163 0.4943 -0.0099 -0.0269 0.0177  49  ALA B CA  
3529 C C   . ALA B 51  ? 0.7658 0.5560 0.5217 -0.0064 -0.0277 0.0059  49  ALA B C   
3530 O O   . ALA B 51  ? 0.7751 0.5616 0.5191 -0.0008 -0.0411 0.0042  49  ALA B O   
3531 C CB  . ALA B 51  ? 0.6525 0.4475 0.4443 -0.0157 -0.0262 0.0105  49  ALA B CB  
3532 N N   . ARG B 52  ? 0.7842 0.5891 0.5566 -0.0101 -0.0108 -0.0046 50  ARG B N   
3533 C CA  . ARG B 52  ? 0.7562 0.5761 0.5323 -0.0026 -0.0093 -0.0171 50  ARG B CA  
3534 C C   . ARG B 52  ? 0.7836 0.6382 0.5974 -0.0068 0.0055  -0.0340 50  ARG B C   
3535 O O   . ARG B 52  ? 0.7752 0.6299 0.5991 -0.0212 0.0266  -0.0365 50  ARG B O   
3536 C CB  . ARG B 52  ? 0.7748 0.5747 0.5153 -0.0006 -0.0013 -0.0146 50  ARG B CB  
3537 C CG  . ARG B 52  ? 0.7711 0.5850 0.5171 0.0076  0.0059  -0.0294 50  ARG B CG  
3538 C CD  . ARG B 52  ? 0.8332 0.6503 0.5749 0.0006  0.0329  -0.0348 50  ARG B CD  
3539 N NE  . ARG B 52  ? 0.8756 0.6599 0.5739 -0.0052 0.0412  -0.0193 50  ARG B NE  
3540 C CZ  . ARG B 52  ? 0.7623 0.5352 0.4404 -0.0112 0.0682  -0.0177 50  ARG B CZ  
3541 N NH1 . ARG B 52  ? 0.7510 0.5470 0.4557 -0.0165 0.0914  -0.0340 50  ARG B NH1 
3542 N NH2 . ARG B 52  ? 0.7882 0.5273 0.4172 -0.0102 0.0731  0.0003  50  ARG B NH2 
3543 N N   . ILE B 53  ? 0.7678 0.6518 0.6019 0.0067  -0.0041 -0.0468 51  ILE B N   
3544 C CA  . ILE B 53  ? 0.7437 0.6761 0.6189 0.0075  0.0051  -0.0690 51  ILE B CA  
3545 C C   . ILE B 53  ? 0.7760 0.7203 0.6493 0.0228  0.0099  -0.0787 51  ILE B C   
3546 O O   . ILE B 53  ? 0.8272 0.7451 0.6714 0.0381  -0.0002 -0.0700 51  ILE B O   
3547 C CB  . ILE B 53  ? 0.7212 0.6893 0.6233 0.0172  -0.0127 -0.0786 51  ILE B CB  
3548 C CG1 . ILE B 53  ? 0.6636 0.6896 0.6161 0.0081  -0.0017 -0.1068 51  ILE B CG1 
3549 C CG2 . ILE B 53  ? 0.6757 0.6452 0.5631 0.0464  -0.0314 -0.0755 51  ILE B CG2 
3550 C CD1 . ILE B 53  ? 0.5923 0.6606 0.5689 0.0175  -0.0205 -0.1204 51  ILE B CD1 
3551 N N   . SER B 54  ? 0.7680 0.7524 0.6756 0.0172  0.0283  -0.0995 52  SER B N   
3552 C CA  . SER B 54  ? 0.8116 0.8114 0.7222 0.0307  0.0380  -0.1115 52  SER B CA  
3553 C C   . SER B 54  ? 0.8268 0.8739 0.7654 0.0606  0.0201  -0.1270 52  SER B C   
3554 O O   . SER B 54  ? 0.8239 0.8822 0.7669 0.0725  -0.0014 -0.1239 52  SER B O   
3555 C CB  . SER B 54  ? 0.8710 0.8905 0.8045 0.0091  0.0714  -0.1270 52  SER B CB  
3556 O OG  . SER B 54  ? 0.9309 1.0176 0.9256 0.0042  0.0766  -0.1556 52  SER B OG  
3557 N N   . GLU B 55  ? 0.8549 0.9303 0.8095 0.0763  0.0296  -0.1435 53  GLU B N   
3558 C CA  . GLU B 55  ? 0.9121 1.0325 0.8893 0.1131  0.0128  -0.1573 53  GLU B CA  
3559 C C   . GLU B 55  ? 0.9103 1.1205 0.9538 0.1130  0.0161  -0.1912 53  GLU B C   
3560 O O   . GLU B 55  ? 0.8817 1.1422 0.9468 0.1473  -0.0039 -0.2043 53  GLU B O   
3561 C CB  . GLU B 55  ? 0.9823 1.0810 0.9382 0.1375  0.0195  -0.1570 53  GLU B CB  
3562 C CG  . GLU B 55  ? 1.0153 1.1479 1.0000 0.1274  0.0477  -0.1795 53  GLU B CG  
3563 C CD  . GLU B 55  ? 1.0036 1.0845 0.9534 0.0943  0.0718  -0.1676 53  GLU B CD  
3564 O OE1 . GLU B 55  ? 0.9343 0.9580 0.8402 0.0825  0.0629  -0.1434 53  GLU B OE1 
3565 O OE2 . GLU B 55  ? 1.0668 1.1668 1.0319 0.0819  0.1002  -0.1830 53  GLU B OE2 
3566 N N   . SER B 56  ? 0.9940 1.2257 1.0696 0.0763  0.0419  -0.2070 54  SER B N   
3567 C CA  . SER B 56  ? 1.0184 1.3401 1.1656 0.0685  0.0497  -0.2463 54  SER B CA  
3568 C C   . SER B 56  ? 1.0707 1.3864 1.2384 0.0205  0.0758  -0.2538 54  SER B C   
3569 O O   . SER B 56  ? 1.0963 1.3409 1.2229 -0.0032 0.0961  -0.2295 54  SER B O   
3570 C CB  . SER B 56  ? 0.9852 1.3545 1.1668 0.0796  0.0687  -0.2716 54  SER B CB  
3571 O OG  . SER B 56  ? 0.9143 1.3847 1.1742 0.0740  0.0731  -0.3156 54  SER B OG  
3572 N N   . ARG B 57  ? 0.9774 1.3680 1.2072 0.0085  0.0748  -0.2890 55  ARG B N   
3573 C CA  . ARG B 57  ? 0.9630 1.3548 1.2239 -0.0386 0.1043  -0.3050 55  ARG B CA  
3574 C C   . ARG B 57  ? 1.0318 1.3471 1.2452 -0.0534 0.0990  -0.2727 55  ARG B C   
3575 O O   . ARG B 57  ? 1.0622 1.3588 1.2900 -0.0902 0.1254  -0.2794 55  ARG B O   
3576 C CB  . ARG B 57  ? 0.9448 1.3183 1.2149 -0.0694 0.1534  -0.3115 55  ARG B CB  
3577 C CG  . ARG B 57  ? 0.9334 1.4023 1.2776 -0.0706 0.1701  -0.3585 55  ARG B CG  
3578 C CD  . ARG B 57  ? 0.9821 1.4440 1.3034 -0.0421 0.1730  -0.3490 55  ARG B CD  
3579 N NE  . ARG B 57  ? 1.0838 1.4613 1.3513 -0.0638 0.2098  -0.3213 55  ARG B NE  
3580 C CZ  . ARG B 57  ? 1.0683 1.4327 1.3146 -0.0508 0.2254  -0.3168 55  ARG B CZ  
3581 N NH1 . ARG B 57  ? 0.9700 1.3966 1.2475 -0.0162 0.2100  -0.3378 55  ARG B NH1 
3582 N NH2 . ARG B 57  ? 1.0133 1.2996 1.2021 -0.0699 0.2571  -0.2908 55  ARG B NH2 
3583 N N   . GLY B 58  ? 1.0979 1.3674 1.2566 -0.0255 0.0682  -0.2392 56  GLY B N   
3584 C CA  . GLY B 58  ? 1.0797 1.2875 1.1998 -0.0362 0.0608  -0.2118 56  GLY B CA  
3585 C C   . GLY B 58  ? 1.1214 1.2535 1.2046 -0.0619 0.0908  -0.1871 56  GLY B C   
3586 O O   . GLY B 58  ? 1.1468 1.2458 1.2244 -0.0829 0.1007  -0.1796 56  GLY B O   
3587 N N   . THR B 59  ? 0.9797 1.0826 1.0337 -0.0576 0.1056  -0.1743 57  THR B N   
3588 C CA  . THR B 59  ? 0.9279 0.9584 0.9346 -0.0745 0.1311  -0.1479 57  THR B CA  
3589 C C   . THR B 59  ? 0.8562 0.8310 0.8093 -0.0613 0.1053  -0.1140 57  THR B C   
3590 O O   . THR B 59  ? 0.8301 0.8008 0.7600 -0.0373 0.0784  -0.1038 57  THR B O   
3591 C CB  . THR B 59  ? 0.9410 0.9611 0.9267 -0.0707 0.1518  -0.1462 57  THR B CB  
3592 O OG1 . THR B 59  ? 0.9465 1.0381 0.9902 -0.0706 0.1627  -0.1819 57  THR B OG1 
3593 C CG2 . THR B 59  ? 0.9191 0.8810 0.8694 -0.0941 0.1912  -0.1297 57  THR B CG2 
3594 N N   . THR B 60  ? 0.8099 0.7413 0.7453 -0.0768 0.1160  -0.0982 58  THR B N   
3595 C CA  . THR B 60  ? 0.8098 0.6990 0.7050 -0.0654 0.0923  -0.0708 58  THR B CA  
3596 C C   . THR B 60  ? 0.9060 0.7329 0.7468 -0.0678 0.1088  -0.0434 58  THR B C   
3597 O O   . THR B 60  ? 0.9455 0.7502 0.7792 -0.0831 0.1444  -0.0427 58  THR B O   
3598 C CB  . THR B 60  ? 0.7722 0.6691 0.6930 -0.0733 0.0839  -0.0760 58  THR B CB  
3599 O OG1 . THR B 60  ? 0.8078 0.7038 0.7576 -0.0998 0.1179  -0.0912 58  THR B OG1 
3600 C CG2 . THR B 60  ? 0.7302 0.6839 0.6850 -0.0605 0.0566  -0.0958 58  THR B CG2 
3601 N N   . ASP B 61  ? 0.7751 0.5752 0.5764 -0.0515 0.0835  -0.0218 59  ASP B N   
3602 C CA  . ASP B 61  ? 0.7861 0.5355 0.5319 -0.0459 0.0897  0.0040  59  ASP B CA  
3603 C C   . ASP B 61  ? 0.7347 0.4710 0.4673 -0.0345 0.0618  0.0193  59  ASP B C   
3604 O O   . ASP B 61  ? 0.7462 0.5049 0.4905 -0.0264 0.0340  0.0140  59  ASP B O   
3605 C CB  . ASP B 61  ? 0.8546 0.5970 0.5608 -0.0351 0.0881  0.0077  59  ASP B CB  
3606 C CG  . ASP B 61  ? 0.9289 0.6246 0.5778 -0.0324 0.1098  0.0285  59  ASP B CG  
3607 O OD1 . ASP B 61  ? 0.9452 0.6224 0.5947 -0.0465 0.1474  0.0291  59  ASP B OD1 
3608 O OD2 . ASP B 61  ? 0.9977 0.6760 0.5998 -0.0160 0.0905  0.0432  59  ASP B OD2 
3609 N N   . TYR B 62  ? 0.7541 0.4518 0.4615 -0.0326 0.0720  0.0383  60  TYR B N   
3610 C CA  . TYR B 62  ? 0.8066 0.4964 0.5080 -0.0208 0.0486  0.0507  60  TYR B CA  
3611 C C   . TYR B 62  ? 0.8446 0.5010 0.4890 -0.0016 0.0440  0.0746  60  TYR B C   
3612 O O   . TYR B 62  ? 0.9187 0.5425 0.5234 0.0012  0.0677  0.0869  60  TYR B O   
3613 C CB  . TYR B 62  ? 0.7774 0.4572 0.5086 -0.0308 0.0616  0.0487  60  TYR B CB  
3614 C CG  . TYR B 62  ? 0.7055 0.4269 0.4919 -0.0465 0.0602  0.0223  60  TYR B CG  
3615 C CD1 . TYR B 62  ? 0.6876 0.4243 0.5028 -0.0651 0.0861  0.0026  60  TYR B CD1 
3616 C CD2 . TYR B 62  ? 0.6819 0.4306 0.4910 -0.0416 0.0337  0.0154  60  TYR B CD2 
3617 C CE1 . TYR B 62  ? 0.7439 0.5289 0.6093 -0.0753 0.0807  -0.0249 60  TYR B CE1 
3618 C CE2 . TYR B 62  ? 0.6718 0.4598 0.5224 -0.0507 0.0304  -0.0078 60  TYR B CE2 
3619 C CZ  . TYR B 62  ? 0.7242 0.5336 0.6031 -0.0659 0.0514  -0.0287 60  TYR B CZ  
3620 O OH  . TYR B 62  ? 0.6843 0.5431 0.6046 -0.0711 0.0441  -0.0551 60  TYR B OH  
3621 N N   . ALA B 63  ? 0.8448 0.5125 0.4847 0.0127  0.0138  0.0797  61  ALA B N   
3622 C CA  . ALA B 63  ? 0.8982 0.5456 0.4902 0.0359  0.0037  0.0997  61  ALA B CA  
3623 C C   . ALA B 63  ? 1.0067 0.6122 0.5868 0.0441  0.0238  0.1192  61  ALA B C   
3624 O O   . ALA B 63  ? 1.0446 0.6473 0.6642 0.0315  0.0343  0.1129  61  ALA B O   
3625 C CB  . ALA B 63  ? 0.8218 0.5043 0.4244 0.0463  -0.0336 0.0930  61  ALA B CB  
3626 N N   . ASP B 64  ? 1.0389 0.6088 0.5598 0.0677  0.0300  0.1428  62  ASP B N   
3627 C CA  . ASP B 64  ? 1.1315 0.6469 0.6304 0.0800  0.0550  0.1655  62  ASP B CA  
3628 C C   . ASP B 64  ? 1.0635 0.5912 0.5931 0.0918  0.0351  0.1660  62  ASP B C   
3629 O O   . ASP B 64  ? 1.1571 0.6467 0.6975 0.0898  0.0589  0.1732  62  ASP B O   
3630 C CB  . ASP B 64  ? 1.2256 0.6984 0.6435 0.1111  0.0630  0.1945  62  ASP B CB  
3631 C CG  . ASP B 64  ? 1.3847 0.8407 0.7675 0.0990  0.0884  0.1945  62  ASP B CG  
3632 O OD1 . ASP B 64  ? 1.3208 0.7962 0.7480 0.0665  0.1032  0.1721  62  ASP B OD1 
3633 O OD2 . ASP B 64  ? 1.5280 0.9538 0.8374 0.1246  0.0935  0.2163  62  ASP B OD2 
3634 N N   . SER B 65  ? 1.0775 0.6575 0.6242 0.1021  -0.0049 0.1555  63  SER B N   
3635 C CA  . SER B 65  ? 1.0678 0.6658 0.6468 0.1131  -0.0226 0.1536  63  SER B CA  
3636 C C   . SER B 65  ? 1.0676 0.6782 0.7069 0.0845  -0.0134 0.1343  63  SER B C   
3637 O O   . SER B 65  ? 1.1411 0.7487 0.8039 0.0908  -0.0140 0.1347  63  SER B O   
3638 C CB  . SER B 65  ? 1.0509 0.7067 0.6372 0.1270  -0.0640 0.1427  63  SER B CB  
3639 O OG  . SER B 65  ? 1.2248 0.8806 0.7551 0.1519  -0.0765 0.1538  63  SER B OG  
3640 N N   . VAL B 66  ? 0.9377 0.5643 0.6004 0.0565  -0.0057 0.1166  64  VAL B N   
3641 C CA  . VAL B 66  ? 0.8466 0.4932 0.5609 0.0332  -0.0011 0.0963  64  VAL B CA  
3642 C C   . VAL B 66  ? 0.8693 0.4943 0.5951 0.0107  0.0324  0.0881  64  VAL B C   
3643 O O   . VAL B 66  ? 0.8753 0.5253 0.6422 -0.0086 0.0349  0.0669  64  VAL B O   
3644 C CB  . VAL B 66  ? 0.8080 0.5038 0.5469 0.0235  -0.0260 0.0783  64  VAL B CB  
3645 C CG1 . VAL B 66  ? 0.8077 0.5291 0.5521 0.0376  -0.0535 0.0789  64  VAL B CG1 
3646 C CG2 . VAL B 66  ? 0.8739 0.5753 0.5909 0.0197  -0.0267 0.0756  64  VAL B CG2 
3647 N N   . LYS B 67  ? 0.9491 0.5307 0.6388 0.0128  0.0592  0.1026  65  LYS B N   
3648 C CA  . LYS B 67  ? 0.9480 0.5098 0.6543 -0.0127 0.0969  0.0911  65  LYS B CA  
3649 C C   . LYS B 67  ? 1.0024 0.5399 0.7365 -0.0227 0.1171  0.0844  65  LYS B C   
3650 O O   . LYS B 67  ? 1.0253 0.5240 0.7379 -0.0031 0.1198  0.1034  65  LYS B O   
3651 C CB  . LYS B 67  ? 0.9538 0.4664 0.6094 -0.0087 0.1272  0.1103  65  LYS B CB  
3652 C CG  . LYS B 67  ? 0.9245 0.4381 0.6031 -0.0395 0.1625  0.0911  65  LYS B CG  
3653 C CD  . LYS B 67  ? 1.0030 0.5237 0.6489 -0.0364 0.1647  0.0955  65  LYS B CD  
3654 C CE  . LYS B 67  ? 1.0880 0.5425 0.6598 -0.0173 0.1881  0.1286  65  LYS B CE  
3655 N NZ  . LYS B 67  ? 1.1612 0.6299 0.6894 -0.0032 0.1737  0.1353  65  LYS B NZ  
3656 N N   . GLY B 68  ? 0.9949 0.5583 0.7776 -0.0514 0.1304  0.0548  66  GLY B N   
3657 C CA  . GLY B 68  ? 0.9312 0.4796 0.7461 -0.0658 0.1490  0.0395  66  GLY B CA  
3658 C C   . GLY B 68  ? 0.9258 0.5070 0.7648 -0.0569 0.1190  0.0313  66  GLY B C   
3659 O O   . GLY B 68  ? 0.9637 0.5475 0.8360 -0.0722 0.1306  0.0100  66  GLY B O   
3660 N N   . ARG B 69  ? 0.8371 0.4437 0.6610 -0.0347 0.0832  0.0447  67  ARG B N   
3661 C CA  . ARG B 69  ? 0.7769 0.4158 0.6227 -0.0276 0.0576  0.0370  67  ARG B CA  
3662 C C   . ARG B 69  ? 0.7697 0.4670 0.6372 -0.0355 0.0333  0.0190  67  ARG B C   
3663 O O   . ARG B 69  ? 0.7038 0.4286 0.5978 -0.0421 0.0260  0.0012  67  ARG B O   
3664 C CB  . ARG B 69  ? 0.7678 0.3971 0.5874 0.0017  0.0375  0.0609  67  ARG B CB  
3665 C CG  . ARG B 69  ? 0.8870 0.4563 0.6745 0.0209  0.0578  0.0845  67  ARG B CG  
3666 C CD  . ARG B 69  ? 0.8878 0.4633 0.6467 0.0546  0.0316  0.1061  67  ARG B CD  
3667 N NE  . ARG B 69  ? 0.9267 0.5507 0.7167 0.0591  0.0040  0.0945  67  ARG B NE  
3668 C CZ  . ARG B 69  ? 0.9015 0.5713 0.6942 0.0633  -0.0254 0.0910  67  ARG B CZ  
3669 N NH1 . ARG B 69  ? 0.8816 0.5576 0.6468 0.0658  -0.0347 0.0971  67  ARG B NH1 
3670 N NH2 . ARG B 69  ? 0.8851 0.5934 0.7087 0.0632  -0.0425 0.0790  67  ARG B NH2 
3671 N N   . PHE B 70  ? 0.7295 0.4421 0.5813 -0.0326 0.0222  0.0239  68  PHE B N   
3672 C CA  . PHE B 70  ? 0.5865 0.3434 0.4510 -0.0352 0.0021  0.0108  68  PHE B CA  
3673 C C   . PHE B 70  ? 0.6313 0.4078 0.5124 -0.0497 0.0152  -0.0076 68  PHE B C   
3674 O O   . PHE B 70  ? 0.6373 0.3922 0.5127 -0.0583 0.0387  -0.0062 68  PHE B O   
3675 C CB  . PHE B 70  ? 0.6633 0.4243 0.5023 -0.0217 -0.0182 0.0247  68  PHE B CB  
3676 C CG  . PHE B 70  ? 0.6459 0.4078 0.4804 -0.0093 -0.0355 0.0343  68  PHE B CG  
3677 C CD1 . PHE B 70  ? 0.6396 0.3914 0.4860 -0.0057 -0.0309 0.0361  68  PHE B CD1 
3678 C CD2 . PHE B 70  ? 0.6180 0.3927 0.4398 -0.0024 -0.0543 0.0381  68  PHE B CD2 
3679 C CE1 . PHE B 70  ? 0.6676 0.4284 0.5160 0.0064  -0.0460 0.0419  68  PHE B CE1 
3680 C CE2 . PHE B 70  ? 0.6465 0.4310 0.4724 0.0058  -0.0686 0.0414  68  PHE B CE2 
3681 C CZ  . PHE B 70  ? 0.7063 0.4869 0.5468 0.0112  -0.0650 0.0435  68  PHE B CZ  
3682 N N   . THR B 71  ? 0.6463 0.4652 0.5469 -0.0505 0.0010  -0.0250 69  THR B N   
3683 C CA  . THR B 71  ? 0.6268 0.4795 0.5499 -0.0594 0.0081  -0.0469 69  THR B CA  
3684 C C   . THR B 71  ? 0.6230 0.5064 0.5399 -0.0442 -0.0146 -0.0484 69  THR B C   
3685 O O   . THR B 71  ? 0.6284 0.5231 0.5413 -0.0342 -0.0323 -0.0472 69  THR B O   
3686 C CB  . THR B 71  ? 0.6257 0.5059 0.5863 -0.0747 0.0178  -0.0755 69  THR B CB  
3687 O OG1 . THR B 71  ? 0.6586 0.4997 0.6193 -0.0839 0.0351  -0.0707 69  THR B OG1 
3688 C CG2 . THR B 71  ? 0.5618 0.4711 0.5524 -0.0906 0.0364  -0.1007 69  THR B CG2 
3689 N N   . ILE B 72  ? 0.6151 0.5069 0.5283 -0.0415 -0.0109 -0.0503 70  ILE B N   
3690 C CA  . ILE B 72  ? 0.6046 0.5169 0.5092 -0.0242 -0.0282 -0.0510 70  ILE B CA  
3691 C C   . ILE B 72  ? 0.5885 0.5538 0.5256 -0.0220 -0.0279 -0.0779 70  ILE B C   
3692 O O   . ILE B 72  ? 0.5455 0.5297 0.5116 -0.0385 -0.0090 -0.0963 70  ILE B O   
3693 C CB  . ILE B 72  ? 0.6808 0.5669 0.5572 -0.0186 -0.0259 -0.0366 70  ILE B CB  
3694 C CG1 . ILE B 72  ? 0.6817 0.5750 0.5448 0.0002  -0.0415 -0.0355 70  ILE B CG1 
3695 C CG2 . ILE B 72  ? 0.6440 0.5329 0.5290 -0.0295 -0.0031 -0.0449 70  ILE B CG2 
3696 C CD1 . ILE B 72  ? 0.6390 0.5005 0.4707 0.0041  -0.0421 -0.0228 70  ILE B CD1 
3697 N N   . SER B 73  ? 0.6173 0.6078 0.5499 -0.0008 -0.0475 -0.0812 71  SER B N   
3698 C CA  . SER B 73  ? 0.5791 0.6294 0.5400 0.0104  -0.0539 -0.1072 71  SER B CA  
3699 C C   . SER B 73  ? 0.6069 0.6586 0.5416 0.0428  -0.0715 -0.0972 71  SER B C   
3700 O O   . SER B 73  ? 0.6517 0.6593 0.5498 0.0519  -0.0780 -0.0736 71  SER B O   
3701 C CB  . SER B 73  ? 0.5265 0.6167 0.5129 0.0043  -0.0596 -0.1296 71  SER B CB  
3702 O OG  . SER B 73  ? 0.6300 0.6911 0.5896 0.0085  -0.0695 -0.1130 71  SER B OG  
3703 N N   . ARG B 74  ? 0.5982 0.7006 0.5536 0.0608  -0.0770 -0.1167 72  ARG B N   
3704 C CA  . ARG B 74  ? 0.6568 0.7572 0.5863 0.0971  -0.0905 -0.1073 72  ARG B CA  
3705 C C   . ARG B 74  ? 0.7097 0.8771 0.6550 0.1253  -0.1094 -0.1285 72  ARG B C   
3706 O O   . ARG B 74  ? 0.6790 0.9090 0.6682 0.1131  -0.1103 -0.1594 72  ARG B O   
3707 C CB  . ARG B 74  ? 0.6338 0.7264 0.5657 0.1018  -0.0790 -0.1076 72  ARG B CB  
3708 C CG  . ARG B 74  ? 0.6070 0.7726 0.5817 0.1155  -0.0796 -0.1379 72  ARG B CG  
3709 C CD  . ARG B 74  ? 0.6369 0.7898 0.6116 0.1193  -0.0647 -0.1377 72  ARG B CD  
3710 N NE  . ARG B 74  ? 0.6579 0.7644 0.5882 0.1504  -0.0722 -0.1161 72  ARG B NE  
3711 C CZ  . ARG B 74  ? 0.6477 0.6998 0.5509 0.1449  -0.0593 -0.1020 72  ARG B CZ  
3712 N NH1 . ARG B 74  ? 0.7171 0.7551 0.6265 0.1139  -0.0406 -0.1039 72  ARG B NH1 
3713 N NH2 . ARG B 74  ? 0.7124 0.7201 0.5777 0.1719  -0.0636 -0.0862 72  ARG B NH2 
3714 N N   . ASP B 75  ? 0.8415 0.9942 0.7484 0.1643  -0.1235 -0.1126 73  ASP B N   
3715 C CA  . ASP B 75  ? 0.8223 1.0352 0.7300 0.2034  -0.1453 -0.1275 73  ASP B CA  
3716 C C   . ASP B 75  ? 0.8383 1.0297 0.7141 0.2474  -0.1497 -0.1117 73  ASP B C   
3717 O O   . ASP B 75  ? 0.9252 1.0471 0.7459 0.2650  -0.1478 -0.0806 73  ASP B O   
3718 C CB  . ASP B 75  ? 0.7967 1.0018 0.6725 0.2108  -0.1576 -0.1186 73  ASP B CB  
3719 C CG  . ASP B 75  ? 0.7974 1.0861 0.6845 0.2425  -0.1817 -0.1452 73  ASP B CG  
3720 O OD1 . ASP B 75  ? 0.7753 1.1213 0.6848 0.2712  -0.1923 -0.1636 73  ASP B OD1 
3721 O OD2 . ASP B 75  ? 0.8407 1.1428 0.7155 0.2398  -0.1907 -0.1501 73  ASP B OD2 
3722 N N   . ASN B 76  ? 0.7214 0.9705 0.6336 0.2646  -0.1522 -0.1348 74  ASN B N   
3723 C CA  . ASN B 76  ? 0.7541 0.9819 0.6396 0.3087  -0.1539 -0.1219 74  ASN B CA  
3724 C C   . ASN B 76  ? 0.7990 1.0390 0.6434 0.3663  -0.1765 -0.1119 74  ASN B C   
3725 O O   . ASN B 76  ? 0.8805 1.0741 0.6831 0.4071  -0.1748 -0.0903 74  ASN B O   
3726 C CB  . ASN B 76  ? 0.7391 1.0309 0.6797 0.3114  -0.1485 -0.1520 74  ASN B CB  
3727 C CG  . ASN B 76  ? 0.6945 0.9650 0.6636 0.2590  -0.1222 -0.1578 74  ASN B CG  
3728 O OD1 . ASN B 76  ? 0.6641 0.8616 0.6032 0.2293  -0.1098 -0.1344 74  ASN B OD1 
3729 N ND2 . ASN B 76  ? 0.6895 1.0259 0.7156 0.2487  -0.1126 -0.1898 74  ASN B ND2 
3730 N N   . ALA B 77  ? 0.9193 1.2166 0.7702 0.3721  -0.1960 -0.1269 75  ALA B N   
3731 C CA  . ALA B 77  ? 0.9046 1.2157 0.7073 0.4309  -0.2189 -0.1163 75  ALA B CA  
3732 C C   . ALA B 77  ? 0.9539 1.1615 0.6777 0.4373  -0.2093 -0.0724 75  ALA B C   
3733 O O   . ALA B 77  ? 1.0897 1.2566 0.7557 0.4841  -0.2099 -0.0482 75  ALA B O   
3734 C CB  . ALA B 77  ? 0.8498 1.2674 0.6871 0.4347  -0.2442 -0.1536 75  ALA B CB  
3735 N N   . LYS B 78  ? 0.8534 1.0133 0.5771 0.3856  -0.1932 -0.0630 76  LYS B N   
3736 C CA  . LYS B 78  ? 0.8395 0.9069 0.4994 0.3828  -0.1796 -0.0264 76  LYS B CA  
3737 C C   . LYS B 78  ? 0.9036 0.8808 0.5513 0.3555  -0.1528 -0.0041 76  LYS B C   
3738 O O   . LYS B 78  ? 0.9385 0.8411 0.5444 0.3434  -0.1372 0.0213  76  LYS B O   
3739 C CB  . LYS B 78  ? 0.8666 0.9492 0.5341 0.3483  -0.1816 -0.0338 76  LYS B CB  
3740 C CG  . LYS B 78  ? 0.9871 1.1313 0.6349 0.3826  -0.2056 -0.0462 76  LYS B CG  
3741 C CD  . LYS B 78  ? 0.9063 1.1053 0.5968 0.3425  -0.2110 -0.0757 76  LYS B CD  
3742 C CE  . LYS B 78  ? 0.8568 1.1689 0.6108 0.3452  -0.2316 -0.1231 76  LYS B CE  
3743 N NZ  . LYS B 78  ? 0.8589 1.2164 0.6007 0.3967  -0.2453 -0.1301 76  LYS B NZ  
3744 N N   . ASN B 79  ? 0.9063 0.8924 0.5904 0.3446  -0.1460 -0.0162 77  ASN B N   
3745 C CA  . ASN B 79  ? 0.8154 0.7238 0.4874 0.3216  -0.1229 -0.0006 77  ASN B CA  
3746 C C   . ASN B 79  ? 0.8157 0.6852 0.4892 0.2714  -0.1108 0.0072  77  ASN B C   
3747 O O   . ASN B 79  ? 0.8795 0.6739 0.5202 0.2604  -0.0940 0.0269  77  ASN B O   
3748 C CB  . ASN B 79  ? 0.9209 0.7515 0.5323 0.3610  -0.1115 0.0264  77  ASN B CB  
3749 C CG  . ASN B 79  ? 0.9976 0.8375 0.6170 0.3947  -0.1110 0.0189  77  ASN B CG  
3750 O OD1 . ASN B 79  ? 0.9400 0.8593 0.5883 0.4247  -0.1298 -0.0008 77  ASN B OD1 
3751 N ND2 . ASN B 79  ? 1.1915 0.9537 0.7881 0.3900  -0.0888 0.0310  77  ASN B ND2 
3752 N N   . THR B 80  ? 0.8064 0.7284 0.5205 0.2412  -0.1181 -0.0107 78  THR B N   
3753 C CA  . THR B 80  ? 0.8218 0.7160 0.5404 0.1997  -0.1092 -0.0047 78  THR B CA  
3754 C C   . THR B 80  ? 0.7455 0.6811 0.5151 0.1651  -0.1082 -0.0251 78  THR B C   
3755 O O   . THR B 80  ? 0.7290 0.7239 0.5339 0.1693  -0.1143 -0.0473 78  THR B O   
3756 C CB  . THR B 80  ? 0.8191 0.7157 0.5165 0.2034  -0.1149 0.0019  78  THR B CB  
3757 O OG1 . THR B 80  ? 0.8617 0.7285 0.5648 0.1659  -0.1043 0.0081  78  THR B OG1 
3758 C CG2 . THR B 80  ? 0.7619 0.7396 0.4894 0.2111  -0.1328 -0.0233 78  THR B CG2 
3759 N N   . ILE B 81  ? 0.7315 0.6345 0.5042 0.1315  -0.0985 -0.0178 79  ILE B N   
3760 C CA  . ILE B 81  ? 0.7585 0.6840 0.5677 0.1006  -0.0937 -0.0305 79  ILE B CA  
3761 C C   . ILE B 81  ? 0.7169 0.6275 0.5264 0.0786  -0.0920 -0.0241 79  ILE B C   
3762 O O   . ILE B 81  ? 0.7321 0.6044 0.5159 0.0782  -0.0900 -0.0085 79  ILE B O   
3763 C CB  . ILE B 81  ? 0.6924 0.5928 0.5024 0.0878  -0.0828 -0.0280 79  ILE B CB  
3764 C CG1 . ILE B 81  ? 0.7200 0.5617 0.4961 0.0868  -0.0781 -0.0107 79  ILE B CG1 
3765 C CG2 . ILE B 81  ? 0.7099 0.6393 0.5333 0.1049  -0.0813 -0.0414 79  ILE B CG2 
3766 C CD1 . ILE B 81  ? 0.7415 0.5623 0.5185 0.0597  -0.0750 -0.0043 79  ILE B CD1 
3767 N N   . TYR B 82  ? 0.6809 0.6206 0.5216 0.0597  -0.0897 -0.0380 80  TYR B N   
3768 C CA  . TYR B 82  ? 0.6714 0.6021 0.5166 0.0427  -0.0876 -0.0352 80  TYR B CA  
3769 C C   . TYR B 82  ? 0.6554 0.5673 0.5137 0.0197  -0.0768 -0.0319 80  TYR B C   
3770 O O   . TYR B 82  ? 0.6490 0.5643 0.5173 0.0137  -0.0690 -0.0366 80  TYR B O   
3771 C CB  . TYR B 82  ? 0.6321 0.6075 0.4979 0.0431  -0.0926 -0.0555 80  TYR B CB  
3772 C CG  . TYR B 82  ? 0.6347 0.6474 0.4916 0.0715  -0.1062 -0.0653 80  TYR B CG  
3773 C CD1 . TYR B 82  ? 0.6454 0.6442 0.4646 0.0933  -0.1141 -0.0524 80  TYR B CD1 
3774 C CD2 . TYR B 82  ? 0.6137 0.6769 0.4985 0.0788  -0.1101 -0.0877 80  TYR B CD2 
3775 C CE1 . TYR B 82  ? 0.6967 0.7275 0.4989 0.1268  -0.1278 -0.0583 80  TYR B CE1 
3776 C CE2 . TYR B 82  ? 0.6406 0.7462 0.5178 0.1113  -0.1262 -0.0980 80  TYR B CE2 
3777 C CZ  . TYR B 82  ? 0.7257 0.8132 0.5577 0.1378  -0.1363 -0.0815 80  TYR B CZ  
3778 O OH  . TYR B 82  ? 0.7881 0.9154 0.6035 0.1773  -0.1537 -0.0886 80  TYR B OH  
3779 N N   . LEU B 83  ? 0.6574 0.5492 0.5128 0.0096  -0.0753 -0.0232 81  LEU B N   
3780 C CA  . LEU B 83  ? 0.6437 0.5169 0.5063 -0.0053 -0.0668 -0.0176 81  LEU B CA  
3781 C C   . LEU B 83  ? 0.6636 0.5393 0.5397 -0.0124 -0.0641 -0.0214 81  LEU B C   
3782 O O   . LEU B 83  ? 0.6439 0.5085 0.5126 -0.0109 -0.0681 -0.0132 81  LEU B O   
3783 C CB  . LEU B 83  ? 0.6743 0.5191 0.5169 -0.0048 -0.0700 -0.0023 81  LEU B CB  
3784 C CG  . LEU B 83  ? 0.6821 0.5105 0.5236 -0.0116 -0.0650 0.0055  81  LEU B CG  
3785 C CD1 . LEU B 83  ? 0.6584 0.4848 0.4999 -0.0153 -0.0529 0.0026  81  LEU B CD1 
3786 C CD2 . LEU B 83  ? 0.6046 0.4190 0.4295 -0.0096 -0.0734 0.0145  81  LEU B CD2 
3787 N N   . GLN B 84  ? 0.6619 0.5527 0.5604 -0.0218 -0.0546 -0.0371 82  GLN B N   
3788 C CA  . GLN B 84  ? 0.6367 0.5260 0.5493 -0.0297 -0.0483 -0.0444 82  GLN B CA  
3789 C C   . GLN B 84  ? 0.6469 0.4995 0.5561 -0.0339 -0.0382 -0.0293 82  GLN B C   
3790 O O   . GLN B 84  ? 0.6645 0.4997 0.5757 -0.0407 -0.0238 -0.0277 82  GLN B O   
3791 C CB  . GLN B 84  ? 0.6883 0.6066 0.6286 -0.0409 -0.0392 -0.0719 82  GLN B CB  
3792 C CG  . GLN B 84  ? 0.6885 0.5981 0.6447 -0.0522 -0.0276 -0.0834 82  GLN B CG  
3793 C CD  . GLN B 84  ? 0.6823 0.6007 0.6284 -0.0431 -0.0391 -0.0832 82  GLN B CD  
3794 O OE1 . GLN B 84  ? 0.7039 0.6458 0.6347 -0.0303 -0.0541 -0.0834 82  GLN B OE1 
3795 N NE2 . GLN B 84  ? 0.7510 0.6470 0.7025 -0.0475 -0.0296 -0.0816 82  GLN B NE2 
3796 N N   . MET B 85  ? 0.6014 0.4428 0.5041 -0.0278 -0.0444 -0.0183 83  MET B N   
3797 C CA  . MET B 85  ? 0.5913 0.4053 0.4887 -0.0236 -0.0404 -0.0032 83  MET B CA  
3798 C C   . MET B 85  ? 0.6370 0.4402 0.5504 -0.0259 -0.0283 -0.0097 83  MET B C   
3799 O O   . MET B 85  ? 0.6991 0.5132 0.6203 -0.0232 -0.0328 -0.0139 83  MET B O   
3800 C CB  . MET B 85  ? 0.5928 0.4101 0.4799 -0.0148 -0.0552 0.0085  83  MET B CB  
3801 C CG  . MET B 85  ? 0.6388 0.4611 0.5098 -0.0140 -0.0643 0.0117  83  MET B CG  
3802 S SD  . MET B 85  ? 0.8236 0.6492 0.6886 -0.0104 -0.0772 0.0183  83  MET B SD  
3803 C CE  . MET B 85  ? 0.6654 0.5034 0.5463 -0.0136 -0.0748 0.0118  83  MET B CE  
3804 N N   . ASN B 86  ? 0.6777 0.4547 0.5943 -0.0315 -0.0091 -0.0108 84  ASN B N   
3805 C CA  . ASN B 86  ? 0.6960 0.4501 0.6253 -0.0334 0.0077  -0.0167 84  ASN B CA  
3806 C C   . ASN B 86  ? 0.7513 0.4655 0.6632 -0.0159 0.0134  0.0070  84  ASN B C   
3807 O O   . ASN B 86  ? 0.7885 0.4913 0.6766 -0.0059 0.0080  0.0253  84  ASN B O   
3808 C CB  . ASN B 86  ? 0.6887 0.4351 0.6353 -0.0538 0.0313  -0.0383 84  ASN B CB  
3809 C CG  . ASN B 86  ? 0.6424 0.4393 0.6078 -0.0660 0.0220  -0.0657 84  ASN B CG  
3810 O OD1 . ASN B 86  ? 0.7270 0.5499 0.6973 -0.0626 0.0098  -0.0761 84  ASN B OD1 
3811 N ND2 . ASN B 86  ? 0.6366 0.4500 0.6108 -0.0779 0.0281  -0.0780 84  ASN B ND2 
3812 N N   . SER B 87  ? 0.7493 0.4434 0.6707 -0.0089 0.0238  0.0057  85  SER B N   
3813 C CA  . SER B 87  ? 0.7894 0.4449 0.6940 0.0152  0.0294  0.0280  85  SER B CA  
3814 C C   . SER B 87  ? 0.8503 0.5319 0.7418 0.0362  0.0016  0.0447  85  SER B C   
3815 O O   . SER B 87  ? 0.8692 0.5337 0.7323 0.0521  -0.0023 0.0642  85  SER B O   
3816 C CB  . SER B 87  ? 0.7783 0.3779 0.6590 0.0146  0.0562  0.0407  85  SER B CB  
3817 O OG  . SER B 87  ? 0.7792 0.3666 0.6791 -0.0139 0.0822  0.0177  85  SER B OG  
3818 N N   . LEU B 88  ? 0.8436 0.5679 0.7557 0.0350  -0.0159 0.0344  86  LEU B N   
3819 C CA  . LEU B 88  ? 0.8070 0.5645 0.7168 0.0471  -0.0401 0.0414  86  LEU B CA  
3820 C C   . LEU B 88  ? 0.8540 0.6103 0.7659 0.0763  -0.0461 0.0521  86  LEU B C   
3821 O O   . LEU B 88  ? 0.8419 0.5878 0.7703 0.0849  -0.0352 0.0483  86  LEU B O   
3822 C CB  . LEU B 88  ? 0.7434 0.5412 0.6739 0.0324  -0.0499 0.0258  86  LEU B CB  
3823 C CG  . LEU B 88  ? 0.7384 0.5440 0.6604 0.0128  -0.0510 0.0186  86  LEU B CG  
3824 C CD1 . LEU B 88  ? 0.6928 0.5255 0.6260 0.0031  -0.0553 0.0072  86  LEU B CD1 
3825 C CD2 . LEU B 88  ? 0.7573 0.5624 0.6583 0.0149  -0.0618 0.0284  86  LEU B CD2 
3826 N N   . ASN B 89  ? 0.9076 0.6777 0.8025 0.0940  -0.0644 0.0637  87  ASN B N   
3827 C CA  . ASN B 89  ? 0.8839 0.6698 0.7812 0.1271  -0.0780 0.0715  87  ASN B CA  
3828 C C   . ASN B 89  ? 0.8329 0.6815 0.7491 0.1256  -0.1047 0.0590  87  ASN B C   
3829 O O   . ASN B 89  ? 0.7785 0.6416 0.6921 0.1021  -0.1102 0.0508  87  ASN B O   
3830 C CB  . ASN B 89  ? 0.8826 0.6262 0.7345 0.1564  -0.0750 0.0965  87  ASN B CB  
3831 C CG  . ASN B 89  ? 1.0379 0.7646 0.8543 0.1430  -0.0738 0.1038  87  ASN B CG  
3832 O OD1 . ASN B 89  ? 1.1253 0.8896 0.9366 0.1404  -0.0954 0.0984  87  ASN B OD1 
3833 N ND2 . ASN B 89  ? 1.0143 0.6845 0.8083 0.1331  -0.0459 0.1133  87  ASN B ND2 
3834 N N   . PRO B 90  ? 0.7254 0.6135 0.6642 0.1498  -0.1198 0.0544  88  PRO B N   
3835 C CA  . PRO B 90  ? 0.7207 0.6750 0.6869 0.1428  -0.1421 0.0352  88  PRO B CA  
3836 C C   . PRO B 90  ? 0.8596 0.8245 0.7967 0.1411  -0.1594 0.0365  88  PRO B C   
3837 O O   . PRO B 90  ? 0.8547 0.8651 0.8137 0.1232  -0.1719 0.0161  88  PRO B O   
3838 C CB  . PRO B 90  ? 0.6428 0.6387 0.6363 0.1776  -0.1556 0.0309  88  PRO B CB  
3839 C CG  . PRO B 90  ? 0.6622 0.6135 0.6566 0.1906  -0.1336 0.0418  88  PRO B CG  
3840 C CD  . PRO B 90  ? 0.7100 0.5879 0.6587 0.1818  -0.1142 0.0614  88  PRO B CD  
3841 N N   . GLY B 91  ? 0.9153 0.8370 0.8030 0.1576  -0.1573 0.0582  89  GLY B N   
3842 C CA  . GLY B 91  ? 0.8493 0.7774 0.7041 0.1555  -0.1709 0.0588  89  GLY B CA  
3843 C C   . GLY B 91  ? 0.8620 0.7795 0.7168 0.1169  -0.1614 0.0488  89  GLY B C   
3844 O O   . GLY B 91  ? 0.7806 0.7101 0.6159 0.1113  -0.1727 0.0429  89  GLY B O   
3845 N N   . ASP B 92  ? 0.9461 0.8427 0.8200 0.0934  -0.1417 0.0459  90  ASP B N   
3846 C CA  . ASP B 92  ? 0.9649 0.8512 0.8371 0.0635  -0.1331 0.0381  90  ASP B CA  
3847 C C   . ASP B 92  ? 0.9356 0.8574 0.8403 0.0427  -0.1377 0.0173  90  ASP B C   
3848 O O   . ASP B 92  ? 0.8840 0.7924 0.7860 0.0215  -0.1284 0.0125  90  ASP B O   
3849 C CB  . ASP B 92  ? 0.9632 0.8123 0.8345 0.0522  -0.1107 0.0442  90  ASP B CB  
3850 C CG  . ASP B 92  ? 0.9820 0.7885 0.8232 0.0650  -0.0977 0.0617  90  ASP B CG  
3851 O OD1 . ASP B 92  ? 1.0049 0.8042 0.8168 0.0855  -0.1054 0.0740  90  ASP B OD1 
3852 O OD2 . ASP B 92  ? 0.9129 0.6929 0.7583 0.0541  -0.0781 0.0619  90  ASP B OD2 
3853 N N   . THR B 93  ? 0.8587 0.8242 0.7937 0.0492  -0.1497 0.0045  91  THR B N   
3854 C CA  . THR B 93  ? 0.7328 0.7304 0.7017 0.0258  -0.1482 -0.0175 91  THR B CA  
3855 C C   . THR B 93  ? 0.7438 0.7507 0.7012 0.0120  -0.1570 -0.0302 91  THR B C   
3856 O O   . THR B 93  ? 0.7508 0.7950 0.7111 0.0225  -0.1767 -0.0417 91  THR B O   
3857 C CB  . THR B 93  ? 0.6529 0.7024 0.6648 0.0360  -0.1566 -0.0320 91  THR B CB  
3858 O OG1 . THR B 93  ? 0.6497 0.6851 0.6704 0.0501  -0.1460 -0.0210 91  THR B OG1 
3859 C CG2 . THR B 93  ? 0.5654 0.6450 0.6151 0.0063  -0.1477 -0.0569 91  THR B CG2 
3860 N N   . ALA B 94  ? 0.7528 0.7268 0.6956 -0.0092 -0.1426 -0.0299 92  ALA B N   
3861 C CA  . ALA B 94  ? 0.7187 0.6899 0.6476 -0.0231 -0.1459 -0.0421 92  ALA B CA  
3862 C C   . ALA B 94  ? 0.7517 0.6861 0.6745 -0.0447 -0.1246 -0.0421 92  ALA B C   
3863 O O   . ALA B 94  ? 0.7419 0.6562 0.6652 -0.0457 -0.1107 -0.0311 92  ALA B O   
3864 C CB  . ALA B 94  ? 0.7609 0.7150 0.6488 -0.0071 -0.1559 -0.0301 92  ALA B CB  
3865 N N   . VAL B 95  ? 0.7779 0.7023 0.6911 -0.0594 -0.1220 -0.0551 93  VAL B N   
3866 C CA  . VAL B 95  ? 0.7869 0.6673 0.6848 -0.0737 -0.1012 -0.0525 93  VAL B CA  
3867 C C   . VAL B 95  ? 0.8079 0.6571 0.6690 -0.0606 -0.1024 -0.0372 93  VAL B C   
3868 O O   . VAL B 95  ? 0.8388 0.6900 0.6836 -0.0574 -0.1116 -0.0429 93  VAL B O   
3869 C CB  . VAL B 95  ? 0.6846 0.5630 0.5939 -0.0982 -0.0917 -0.0770 93  VAL B CB  
3870 C CG1 . VAL B 95  ? 0.7056 0.5255 0.5876 -0.1058 -0.0687 -0.0696 93  VAL B CG1 
3871 C CG2 . VAL B 95  ? 0.6230 0.5352 0.5759 -0.1155 -0.0847 -0.0952 93  VAL B CG2 
3872 N N   . TYR B 96  ? 0.7874 0.6132 0.6367 -0.0527 -0.0928 -0.0206 94  TYR B N   
3873 C CA  . TYR B 96  ? 0.7635 0.5704 0.5876 -0.0403 -0.0929 -0.0095 94  TYR B CA  
3874 C C   . TYR B 96  ? 0.8059 0.5792 0.6105 -0.0428 -0.0806 -0.0106 94  TYR B C   
3875 O O   . TYR B 96  ? 0.8408 0.5943 0.6431 -0.0464 -0.0676 -0.0080 94  TYR B O   
3876 C CB  . TYR B 96  ? 0.7557 0.5650 0.5829 -0.0300 -0.0908 0.0030  94  TYR B CB  
3877 C CG  . TYR B 96  ? 0.7643 0.5930 0.6024 -0.0226 -0.0991 0.0073  94  TYR B CG  
3878 C CD1 . TYR B 96  ? 0.7275 0.5781 0.5877 -0.0237 -0.1044 0.0030  94  TYR B CD1 
3879 C CD2 . TYR B 96  ? 0.7701 0.5926 0.5962 -0.0136 -0.0987 0.0154  94  TYR B CD2 
3880 C CE1 . TYR B 96  ? 0.7423 0.6046 0.6082 -0.0109 -0.1111 0.0092  94  TYR B CE1 
3881 C CE2 . TYR B 96  ? 0.7215 0.5486 0.5506 -0.0046 -0.1013 0.0225  94  TYR B CE2 
3882 C CZ  . TYR B 96  ? 0.7301 0.5753 0.5770 -0.0007 -0.1086 0.0206  94  TYR B CZ  
3883 O OH  . TYR B 96  ? 0.7414 0.5858 0.5874 0.0141  -0.1104 0.0298  94  TYR B OH  
3884 N N   . SER B 97  ? 0.8347 0.5981 0.6211 -0.0384 -0.0828 -0.0135 95  SER B N   
3885 C CA  . SER B 97  ? 0.8247 0.5537 0.5913 -0.0364 -0.0709 -0.0154 95  SER B CA  
3886 C C   . SER B 97  ? 0.8499 0.5778 0.6024 -0.0196 -0.0719 -0.0085 95  SER B C   
3887 O O   . SER B 97  ? 0.8830 0.6304 0.6359 -0.0164 -0.0793 -0.0077 95  SER B O   
3888 C CB  . SER B 97  ? 0.8270 0.5452 0.5890 -0.0505 -0.0687 -0.0340 95  SER B CB  
3889 O OG  . SER B 97  ? 0.8419 0.5731 0.6260 -0.0697 -0.0680 -0.0473 95  SER B OG  
3890 N N   . CYS B 98  ? 0.8968 0.6016 0.6362 -0.0072 -0.0625 -0.0037 96  CYS B N   
3891 C CA  . CYS B 98  ? 0.9190 0.6286 0.6509 0.0099  -0.0622 -0.0021 96  CYS B CA  
3892 C C   . CYS B 98  ? 0.9118 0.5935 0.6252 0.0131  -0.0542 -0.0106 96  CYS B C   
3893 O O   . CYS B 98  ? 0.9397 0.5866 0.6420 0.0062  -0.0448 -0.0152 96  CYS B O   
3894 C CB  . CYS B 98  ? 0.8673 0.5803 0.5978 0.0287  -0.0606 0.0064  96  CYS B CB  
3895 S SG  . CYS B 98  ? 1.1320 0.7956 0.8356 0.0388  -0.0472 0.0148  96  CYS B SG  
3896 N N   . ALA B 99  ? 0.8534 0.5485 0.5643 0.0217  -0.0546 -0.0148 97  ALA B N   
3897 C CA  . ALA B 99  ? 0.9092 0.5815 0.6029 0.0258  -0.0463 -0.0253 97  ALA B CA  
3898 C C   . ALA B 99  ? 0.9181 0.6014 0.6132 0.0487  -0.0416 -0.0251 97  ALA B C   
3899 O O   . ALA B 99  ? 0.8672 0.5873 0.5805 0.0539  -0.0458 -0.0223 97  ALA B O   
3900 C CB  . ALA B 99  ? 0.9680 0.6506 0.6545 0.0111  -0.0506 -0.0361 97  ALA B CB  
3901 N N   . ALA B 100 ? 0.9185 0.5710 0.5974 0.0619  -0.0311 -0.0312 98  ALA B N   
3902 C CA  . ALA B 100 ? 0.9404 0.6052 0.6226 0.0884  -0.0262 -0.0338 98  ALA B CA  
3903 C C   . ALA B 100 ? 0.9527 0.6057 0.6232 0.0879  -0.0158 -0.0487 98  ALA B C   
3904 O O   . ALA B 100 ? 0.9383 0.5535 0.5892 0.0753  -0.0096 -0.0570 98  ALA B O   
3905 C CB  . ALA B 100 ? 0.9664 0.6014 0.6354 0.1164  -0.0219 -0.0246 98  ALA B CB  
3906 N N   . THR B 101 ? 0.9471 0.6350 0.6315 0.0999  -0.0122 -0.0555 99  THR B N   
3907 C CA  . THR B 101 ? 0.9555 0.6364 0.6283 0.1009  0.0003  -0.0705 99  THR B CA  
3908 C C   . THR B 101 ? 0.9604 0.6821 0.6570 0.1229  0.0069  -0.0779 99  THR B C   
3909 O O   . THR B 101 ? 0.9283 0.6900 0.6526 0.1334  -0.0004 -0.0740 99  THR B O   
3910 C CB  . THR B 101 ? 0.9418 0.6302 0.6021 0.0742  -0.0003 -0.0750 99  THR B CB  
3911 O OG1 . THR B 101 ? 0.9277 0.5942 0.5638 0.0735  0.0112  -0.0911 99  THR B OG1 
3912 C CG2 . THR B 101 ? 0.9693 0.7028 0.6488 0.0691  0.0019  -0.0717 99  THR B CG2 
3913 N N   . LEU B 102 ? 0.9646 0.6806 0.6523 0.1290  0.0216  -0.0927 100 LEU B N   
3914 C CA  . LEU B 102 ? 0.9554 0.7119 0.6678 0.1483  0.0326  -0.1056 100 LEU B CA  
3915 C C   . LEU B 102 ? 0.9519 0.7423 0.6725 0.1253  0.0439  -0.1126 100 LEU B C   
3916 O O   . LEU B 102 ? 0.9204 0.6885 0.6118 0.1020  0.0457  -0.1092 100 LEU B O   
3917 C CB  . LEU B 102 ? 0.9929 0.7164 0.6882 0.1708  0.0465  -0.1183 100 LEU B CB  
3918 C CG  . LEU B 102 ? 1.0216 0.7212 0.7157 0.2095  0.0438  -0.1132 100 LEU B CG  
3919 C CD1 . LEU B 102 ? 1.0059 0.7706 0.7401 0.2367  0.0339  -0.1131 100 LEU B CD1 
3920 C CD2 . LEU B 102 ? 1.0696 0.7109 0.7359 0.2034  0.0363  -0.0963 100 LEU B CD2 
3921 N N   . PRO B 103 ? 1.0016 0.8466 0.7606 0.1320  0.0531  -0.1232 101 PRO B N   
3922 C CA  . PRO B 103 ? 0.9360 0.8045 0.7000 0.1081  0.0721  -0.1290 101 PRO B CA  
3923 C C   . PRO B 103 ? 0.9665 0.8076 0.6938 0.1035  0.0910  -0.1377 101 PRO B C   
3924 O O   . PRO B 103 ? 0.9279 0.7629 0.6323 0.0817  0.1041  -0.1339 101 PRO B O   
3925 C CB  . PRO B 103 ? 0.9796 0.9157 0.8006 0.1174  0.0813  -0.1459 101 PRO B CB  
3926 C CG  . PRO B 103 ? 1.0624 1.0170 0.9060 0.1486  0.0601  -0.1465 101 PRO B CG  
3927 C CD  . PRO B 103 ? 1.0918 0.9819 0.8915 0.1615  0.0467  -0.1311 101 PRO B CD  
3928 N N   . ALA B 104 ? 0.9789 0.8000 0.6956 0.1255  0.0943  -0.1492 102 ALA B N   
3929 C CA  . ALA B 104 ? 0.9616 0.7523 0.6382 0.1206  0.1108  -0.1604 102 ALA B CA  
3930 C C   . ALA B 104 ? 0.9932 0.7400 0.6205 0.0997  0.0990  -0.1509 102 ALA B C   
3931 O O   . ALA B 104 ? 1.0092 0.7410 0.5976 0.0893  0.1103  -0.1586 102 ALA B O   
3932 C CB  . ALA B 104 ? 1.0408 0.8118 0.7168 0.1497  0.1170  -0.1760 102 ALA B CB  
3933 N N   . TRP B 105 ? 0.9867 0.7176 0.6152 0.0946  0.0765  -0.1364 103 TRP B N   
3934 C CA  . TRP B 105 ? 0.9055 0.6086 0.4974 0.0748  0.0631  -0.1305 103 TRP B CA  
3935 C C   . TRP B 105 ? 0.9265 0.6495 0.5105 0.0577  0.0611  -0.1156 103 TRP B C   
3936 O O   . TRP B 105 ? 0.9826 0.6954 0.5254 0.0477  0.0625  -0.1161 103 TRP B O   
3937 C CB  . TRP B 105 ? 0.9134 0.5922 0.5128 0.0750  0.0442  -0.1229 103 TRP B CB  
3938 C CG  . TRP B 105 ? 0.9190 0.5589 0.5137 0.0905  0.0501  -0.1348 103 TRP B CG  
3939 C CD1 . TRP B 105 ? 0.9650 0.6040 0.5749 0.1178  0.0627  -0.1413 103 TRP B CD1 
3940 C CD2 . TRP B 105 ? 0.9486 0.5422 0.5230 0.0804  0.0461  -0.1425 103 TRP B CD2 
3941 N NE1 . TRP B 105 ? 0.9802 0.5657 0.5741 0.1279  0.0684  -0.1489 103 TRP B NE1 
3942 C CE2 . TRP B 105 ? 0.9889 0.5442 0.5622 0.1020  0.0604  -0.1510 103 TRP B CE2 
3943 C CE3 . TRP B 105 ? 0.9490 0.5319 0.5089 0.0554  0.0333  -0.1454 103 TRP B CE3 
3944 C CZ2 . TRP B 105 ? 1.0338 0.5312 0.5895 0.0954  0.0669  -0.1615 103 TRP B CZ2 
3945 C CZ3 . TRP B 105 ? 0.9872 0.5243 0.5366 0.0466  0.0376  -0.1600 103 TRP B CZ3 
3946 C CH2 . TRP B 105 ? 1.0312 0.5214 0.5774 0.0646  0.0564  -0.1676 103 TRP B CH2 
3947 N N   . THR B 106 ? 1.0643 0.8139 0.6838 0.0562  0.0587  -0.1028 104 THR B N   
3948 C CA  . THR B 106 ? 0.9684 0.7249 0.5795 0.0406  0.0580  -0.0865 104 THR B CA  
3949 C C   . THR B 106 ? 0.9951 0.7520 0.5775 0.0341  0.0831  -0.0872 104 THR B C   
3950 O O   . THR B 106 ? 1.0322 0.7763 0.5819 0.0254  0.0837  -0.0722 104 THR B O   
3951 C CB  . THR B 106 ? 0.9540 0.7382 0.6121 0.0388  0.0550  -0.0784 104 THR B CB  
3952 O OG1 . THR B 106 ? 0.9642 0.7427 0.6114 0.0247  0.0524  -0.0614 104 THR B OG1 
3953 C CG2 . THR B 106 ? 0.9928 0.8137 0.6881 0.0422  0.0776  -0.0915 104 THR B CG2 
3954 N N   . GLY B 107 ? 1.0069 0.7761 0.5974 0.0405  0.1058  -0.1035 105 GLY B N   
3955 C CA  . GLY B 107 ? 0.9956 0.7627 0.5565 0.0331  0.1356  -0.1042 105 GLY B CA  
3956 C C   . GLY B 107 ? 0.9924 0.7707 0.5710 0.0184  0.1534  -0.0904 105 GLY B C   
3957 O O   . GLY B 107 ? 1.0083 0.8163 0.6433 0.0151  0.1525  -0.0935 105 GLY B O   
3958 N N   . ILE B 108 ? 1.0699 0.8215 0.5964 0.0103  0.1711  -0.0758 106 ILE B N   
3959 C CA  . ILE B 108 ? 1.0817 0.8270 0.6134 -0.0047 0.1954  -0.0603 106 ILE B CA  
3960 C C   . ILE B 108 ? 1.1496 0.8617 0.6409 -0.0039 0.1769  -0.0331 106 ILE B C   
3961 O O   . ILE B 108 ? 1.1766 0.8859 0.6927 -0.0134 0.1809  -0.0213 106 ILE B O   
3962 C CB  . ILE B 108 ? 1.0983 0.8324 0.6009 -0.0132 0.2423  -0.0625 106 ILE B CB  
3963 C CG1 . ILE B 108 ? 1.0979 0.8676 0.6351 -0.0090 0.2579  -0.0924 106 ILE B CG1 
3964 C CG2 . ILE B 108 ? 1.2738 1.0016 0.7979 -0.0337 0.2764  -0.0527 106 ILE B CG2 
3965 C CD1 . ILE B 108 ? 1.0823 0.8531 0.6121 -0.0221 0.3105  -0.0998 106 ILE B CD1 
3966 N N   . ILE B 109 ? 1.0453 0.7357 0.4764 0.0085  0.1564  -0.0259 107 ILE B N   
3967 C CA  . ILE B 109 ? 1.0364 0.7033 0.4277 0.0153  0.1360  -0.0024 107 ILE B CA  
3968 C C   . ILE B 109 ? 0.9994 0.6791 0.3953 0.0236  0.0918  -0.0099 107 ILE B C   
3969 O O   . ILE B 109 ? 1.0667 0.7371 0.4291 0.0325  0.0701  0.0036  107 ILE B O   
3970 C CB  . ILE B 109 ? 1.1971 0.8291 0.5035 0.0249  0.1541  0.0151  107 ILE B CB  
3971 C CG1 . ILE B 109 ? 1.1560 0.7919 0.4244 0.0304  0.1612  -0.0042 107 ILE B CG1 
3972 C CG2 . ILE B 109 ? 1.2013 0.8050 0.5003 0.0143  0.1998  0.0331  107 ILE B CG2 
3973 C CD1 . ILE B 109 ? 1.2393 0.8488 0.4130 0.0472  0.1608  0.0095  107 ILE B CD1 
3974 N N   . GLY B 110 ? 0.9591 0.6594 0.3965 0.0218  0.0800  -0.0317 108 GLY B N   
3975 C CA  . GLY B 110 ? 0.9368 0.6427 0.3798 0.0251  0.0459  -0.0413 108 GLY B CA  
3976 C C   . GLY B 110 ? 1.0478 0.7665 0.5483 0.0209  0.0302  -0.0397 108 GLY B C   
3977 O O   . GLY B 110 ? 1.0799 0.8008 0.5971 0.0212  0.0124  -0.0521 108 GLY B O   
3978 N N   . GLY B 111 ? 1.0182 0.7420 0.5466 0.0160  0.0396  -0.0253 109 GLY B N   
3979 C CA  . GLY B 111 ? 0.9223 0.6604 0.5008 0.0131  0.0258  -0.0244 109 GLY B CA  
3980 C C   . GLY B 111 ? 0.9129 0.6472 0.4884 0.0131  0.0008  -0.0136 109 GLY B C   
3981 O O   . GLY B 111 ? 0.9288 0.6727 0.5397 0.0111  -0.0119 -0.0147 109 GLY B O   
3982 N N   . ARG B 112 ? 0.9165 0.6398 0.4491 0.0178  -0.0064 -0.0037 110 ARG B N   
3983 C CA  . ARG B 112 ? 0.9029 0.6308 0.4353 0.0209  -0.0310 0.0040  110 ARG B CA  
3984 C C   . ARG B 112 ? 0.9018 0.6398 0.4190 0.0222  -0.0542 -0.0128 110 ARG B C   
3985 O O   . ARG B 112 ? 0.9486 0.7001 0.4748 0.0231  -0.0755 -0.0127 110 ARG B O   
3986 C CB  . ARG B 112 ? 0.9472 0.6604 0.4445 0.0307  -0.0260 0.0265  110 ARG B CB  
3987 C CG  . ARG B 112 ? 0.9020 0.5981 0.4128 0.0249  0.0034  0.0405  110 ARG B CG  
3988 C CD  . ARG B 112 ? 0.9209 0.5871 0.3856 0.0372  0.0142  0.0654  110 ARG B CD  
3989 N NE  . ARG B 112 ? 0.9266 0.5701 0.4086 0.0267  0.0469  0.0760  110 ARG B NE  
3990 C CZ  . ARG B 112 ? 0.9338 0.5584 0.4231 0.0293  0.0509  0.0918  110 ARG B CZ  
3991 N NH1 . ARG B 112 ? 0.9803 0.6097 0.4624 0.0453  0.0231  0.1007  110 ARG B NH1 
3992 N NH2 . ARG B 112 ? 0.9677 0.5699 0.4754 0.0148  0.0853  0.0955  110 ARG B NH2 
3993 N N   . ARG B 113 ? 0.9640 0.6982 0.4621 0.0209  -0.0490 -0.0308 111 ARG B N   
3994 C CA  . ARG B 113 ? 1.0661 0.8095 0.5507 0.0180  -0.0679 -0.0531 111 ARG B CA  
3995 C C   . ARG B 113 ? 1.0536 0.7942 0.5811 0.0061  -0.0716 -0.0680 111 ARG B C   
3996 O O   . ARG B 113 ? 1.0111 0.7364 0.5551 0.0056  -0.0555 -0.0711 111 ARG B O   
3997 C CB  . ARG B 113 ? 0.9871 0.7230 0.4285 0.0214  -0.0582 -0.0685 111 ARG B CB  
3998 C CG  . ARG B 113 ? 0.9642 0.7044 0.3463 0.0354  -0.0624 -0.0589 111 ARG B CG  
3999 C CD  . ARG B 113 ? 1.1006 0.8231 0.4419 0.0401  -0.0360 -0.0595 111 ARG B CD  
4000 N NE  . ARG B 113 ? 1.1976 0.9111 0.4795 0.0560  -0.0296 -0.0375 111 ARG B NE  
4001 C CZ  . ARG B 113 ? 1.1932 0.8861 0.4337 0.0606  -0.0003 -0.0299 111 ARG B CZ  
4002 N NH1 . ARG B 113 ? 1.1375 0.8247 0.3953 0.0510  0.0237  -0.0451 111 ARG B NH1 
4003 N NH2 . ARG B 113 ? 1.3002 0.9763 0.4790 0.0772  0.0076  -0.0059 111 ARG B NH2 
4004 N N   . PRO B 114 ? 0.9671 0.7212 0.5122 -0.0020 -0.0902 -0.0776 112 PRO B N   
4005 C CA  . PRO B 114 ? 0.8887 0.6301 0.4693 -0.0144 -0.0871 -0.0888 112 PRO B CA  
4006 C C   . PRO B 114 ? 0.9623 0.6795 0.5329 -0.0204 -0.0754 -0.1126 112 PRO B C   
4007 O O   . PRO B 114 ? 0.9523 0.6427 0.5425 -0.0230 -0.0628 -0.1140 112 PRO B O   
4008 C CB  . PRO B 114 ? 0.9572 0.7233 0.5565 -0.0244 -0.1067 -0.0977 112 PRO B CB  
4009 C CG  . PRO B 114 ? 0.9932 0.7867 0.5731 -0.0105 -0.1220 -0.0834 112 PRO B CG  
4010 C CD  . PRO B 114 ? 0.9733 0.7564 0.5077 0.0016  -0.1132 -0.0786 112 PRO B CD  
4011 N N   . GLY B 115 ? 1.0621 0.7848 0.5986 -0.0204 -0.0779 -0.1312 113 GLY B N   
4012 C CA  . GLY B 115 ? 0.9899 0.6868 0.5154 -0.0265 -0.0647 -0.1574 113 GLY B CA  
4013 C C   . GLY B 115 ? 0.9698 0.6385 0.4948 -0.0138 -0.0416 -0.1488 113 GLY B C   
4014 O O   . GLY B 115 ? 0.9437 0.5829 0.4637 -0.0152 -0.0274 -0.1683 113 GLY B O   
4015 N N   . ASN B 116 ? 1.0758 0.7545 0.6087 -0.0012 -0.0365 -0.1231 114 ASN B N   
4016 C CA  . ASN B 116 ? 1.0250 0.6921 0.5657 0.0124  -0.0165 -0.1182 114 ASN B CA  
4017 C C   . ASN B 116 ? 0.9843 0.6423 0.5611 0.0193  -0.0139 -0.1058 114 ASN B C   
4018 O O   . ASN B 116 ? 0.9558 0.6178 0.5467 0.0344  -0.0021 -0.1003 114 ASN B O   
4019 C CB  . ASN B 116 ? 0.9486 0.6367 0.4779 0.0195  -0.0081 -0.1038 114 ASN B CB  
4020 C CG  . ASN B 116 ? 1.0368 0.7208 0.5278 0.0228  0.0054  -0.1184 114 ASN B CG  
4021 O OD1 . ASN B 116 ? 1.0659 0.7500 0.5612 0.0315  0.0259  -0.1210 114 ASN B OD1 
4022 N ND2 . ASN B 116 ? 1.1713 0.8565 0.6249 0.0168  -0.0063 -0.1308 114 ASN B ND2 
4023 N N   . TYR B 117 ? 0.8868 0.5367 0.4783 0.0098  -0.0244 -0.1028 115 TYR B N   
4024 C CA  . TYR B 117 ? 0.9793 0.6151 0.5948 0.0181  -0.0212 -0.0903 115 TYR B CA  
4025 C C   . TYR B 117 ? 0.9919 0.5840 0.6026 0.0107  -0.0135 -0.1033 115 TYR B C   
4026 O O   . TYR B 117 ? 1.0186 0.6088 0.6339 -0.0094 -0.0204 -0.1105 115 TYR B O   
4027 C CB  . TYR B 117 ? 0.9672 0.6277 0.6031 0.0129  -0.0344 -0.0723 115 TYR B CB  
4028 C CG  . TYR B 117 ? 0.9051 0.5988 0.5488 0.0189  -0.0358 -0.0595 115 TYR B CG  
4029 C CD1 . TYR B 117 ? 0.9118 0.6211 0.5377 0.0127  -0.0390 -0.0588 115 TYR B CD1 
4030 C CD2 . TYR B 117 ? 0.8791 0.5875 0.5461 0.0310  -0.0320 -0.0496 115 TYR B CD2 
4031 C CE1 . TYR B 117 ? 0.8898 0.6179 0.5201 0.0156  -0.0330 -0.0467 115 TYR B CE1 
4032 C CE2 . TYR B 117 ? 0.8975 0.6348 0.5767 0.0310  -0.0286 -0.0432 115 TYR B CE2 
4033 C CZ  . TYR B 117 ? 0.9302 0.6722 0.5907 0.0218  -0.0263 -0.0408 115 TYR B CZ  
4034 O OH  . TYR B 117 ? 0.8933 0.6530 0.5632 0.0193  -0.0160 -0.0338 115 TYR B OH  
4035 N N   . PRO B 118 ? 0.9724 0.5273 0.5752 0.0264  0.0034  -0.1080 116 PRO B N   
4036 C CA  . PRO B 118 ? 1.0254 0.5252 0.6184 0.0174  0.0179  -0.1217 116 PRO B CA  
4037 C C   . PRO B 118 ? 1.0777 0.5526 0.6805 0.0143  0.0211  -0.1064 116 PRO B C   
4038 O O   . PRO B 118 ? 1.0828 0.5222 0.6837 -0.0072 0.0319  -0.1197 116 PRO B O   
4039 C CB  . PRO B 118 ? 0.9889 0.4534 0.5676 0.0429  0.0367  -0.1266 116 PRO B CB  
4040 C CG  . PRO B 118 ? 0.9449 0.4496 0.5372 0.0697  0.0300  -0.1082 116 PRO B CG  
4041 C CD  . PRO B 118 ? 0.8971 0.4585 0.5012 0.0539  0.0122  -0.1030 116 PRO B CD  
4042 N N   . TYR B 119 ? 1.0598 0.5532 0.6730 0.0332  0.0143  -0.0817 117 TYR B N   
4043 C CA  . TYR B 119 ? 1.0417 0.5094 0.6562 0.0355  0.0194  -0.0649 117 TYR B CA  
4044 C C   . TYR B 119 ? 1.0868 0.6012 0.7231 0.0197  0.0015  -0.0562 117 TYR B C   
4045 O O   . TYR B 119 ? 1.0328 0.5962 0.6820 0.0263  -0.0139 -0.0493 117 TYR B O   
4046 C CB  . TYR B 119 ? 1.0484 0.5015 0.6527 0.0745  0.0246  -0.0452 117 TYR B CB  
4047 C CG  . TYR B 119 ? 1.1216 0.5376 0.7073 0.0986  0.0402  -0.0528 117 TYR B CG  
4048 C CD1 . TYR B 119 ? 1.1534 0.4955 0.7161 0.0934  0.0646  -0.0621 117 TYR B CD1 
4049 C CD2 . TYR B 119 ? 1.0724 0.5267 0.6665 0.1257  0.0335  -0.0534 117 TYR B CD2 
4050 C CE1 . TYR B 119 ? 1.1232 0.4262 0.6680 0.1179  0.0809  -0.0696 117 TYR B CE1 
4051 C CE2 . TYR B 119 ? 1.0270 0.4507 0.6070 0.1507  0.0483  -0.0618 117 TYR B CE2 
4052 C CZ  . TYR B 119 ? 1.0816 0.4274 0.6351 0.1484  0.0715  -0.0688 117 TYR B CZ  
4053 O OH  . TYR B 119 ? 1.1361 0.4463 0.6746 0.1757  0.0883  -0.0777 117 TYR B OH  
4054 N N   . TRP B 120 ? 1.0951 0.5917 0.7367 -0.0016 0.0070  -0.0578 118 TRP B N   
4055 C CA  . TRP B 120 ? 0.9938 0.5325 0.6581 -0.0175 -0.0079 -0.0533 118 TRP B CA  
4056 C C   . TRP B 120 ? 1.0434 0.5556 0.7068 -0.0178 0.0038  -0.0385 118 TRP B C   
4057 O O   . TRP B 120 ? 1.1771 0.6303 0.8199 -0.0136 0.0267  -0.0350 118 TRP B O   
4058 C CB  . TRP B 120 ? 1.0554 0.6166 0.7338 -0.0473 -0.0153 -0.0773 118 TRP B CB  
4059 C CG  . TRP B 120 ? 1.0725 0.6678 0.7455 -0.0449 -0.0303 -0.0880 118 TRP B CG  
4060 C CD1 . TRP B 120 ? 0.9804 0.5587 0.6347 -0.0436 -0.0239 -0.1050 118 TRP B CD1 
4061 C CD2 . TRP B 120 ? 1.0708 0.7172 0.7513 -0.0418 -0.0508 -0.0812 118 TRP B CD2 
4062 N NE1 . TRP B 120 ? 1.0280 0.6461 0.6751 -0.0401 -0.0394 -0.1086 118 TRP B NE1 
4063 C CE2 . TRP B 120 ? 1.0052 0.6620 0.6664 -0.0383 -0.0552 -0.0927 118 TRP B CE2 
4064 C CE3 . TRP B 120 ? 1.0013 0.6802 0.6995 -0.0406 -0.0632 -0.0663 118 TRP B CE3 
4065 C CZ2 . TRP B 120 ? 0.9809 0.6748 0.6353 -0.0326 -0.0698 -0.0864 118 TRP B CZ2 
4066 C CZ3 . TRP B 120 ? 1.0030 0.7169 0.6980 -0.0349 -0.0777 -0.0613 118 TRP B CZ3 
4067 C CH2 . TRP B 120 ? 1.0040 0.7229 0.6750 -0.0304 -0.0802 -0.0697 118 TRP B CH2 
4068 N N   . GLY B 121 ? 1.0243 0.5761 0.7066 -0.0218 -0.0092 -0.0292 119 GLY B N   
4069 C CA  . GLY B 121 ? 0.9702 0.5045 0.6521 -0.0253 0.0017  -0.0173 119 GLY B CA  
4070 C C   . GLY B 121 ? 0.9532 0.4964 0.6593 -0.0589 0.0068  -0.0338 119 GLY B C   
4071 O O   . GLY B 121 ? 1.0154 0.5919 0.7415 -0.0762 -0.0055 -0.0540 119 GLY B O   
4072 N N   . GLN B 122 ? 1.0604 0.5764 0.7636 -0.0664 0.0257  -0.0259 120 GLN B N   
4073 C CA  . GLN B 122 ? 0.9695 0.4974 0.7023 -0.1001 0.0351  -0.0445 120 GLN B CA  
4074 C C   . GLN B 122 ? 0.9024 0.5026 0.6706 -0.1050 0.0092  -0.0491 120 GLN B C   
4075 O O   . GLN B 122 ? 0.9228 0.5590 0.7234 -0.1279 0.0032  -0.0727 120 GLN B O   
4076 C CB  . GLN B 122 ? 1.0230 0.4995 0.7402 -0.1064 0.0673  -0.0327 120 GLN B CB  
4077 C CG  . GLN B 122 ? 1.0813 0.5286 0.8157 -0.1446 0.0968  -0.0574 120 GLN B CG  
4078 C CD  . GLN B 122 ? 1.0950 0.5266 0.8350 -0.1605 0.1232  -0.0513 120 GLN B CD  
4079 O OE1 . GLN B 122 ? 1.0915 0.5249 0.8129 -0.1391 0.1207  -0.0257 120 GLN B OE1 
4080 N NE2 . GLN B 122 ? 1.1018 0.5181 0.8675 -0.1996 0.1515  -0.0776 120 GLN B NE2 
4081 N N   . GLY B 123 ? 0.8910 0.5145 0.6545 -0.0824 -0.0059 -0.0291 121 GLY B N   
4082 C CA  . GLY B 123 ? 0.8746 0.5556 0.6669 -0.0831 -0.0268 -0.0308 121 GLY B CA  
4083 C C   . GLY B 123 ? 0.9029 0.5931 0.7089 -0.0875 -0.0184 -0.0241 121 GLY B C   
4084 O O   . GLY B 123 ? 0.9759 0.6450 0.7874 -0.1059 0.0038  -0.0307 121 GLY B O   
4085 N N   . THR B 124 ? 0.8075 0.5266 0.6190 -0.0726 -0.0323 -0.0128 122 THR B N   
4086 C CA  . THR B 124 ? 0.8492 0.5826 0.6745 -0.0750 -0.0261 -0.0086 122 THR B CA  
4087 C C   . THR B 124 ? 0.8453 0.6302 0.7074 -0.0780 -0.0435 -0.0181 122 THR B C   
4088 O O   . THR B 124 ? 0.8520 0.6571 0.7173 -0.0696 -0.0622 -0.0195 122 THR B O   
4089 C CB  . THR B 124 ? 0.8937 0.6171 0.6942 -0.0537 -0.0261 0.0090  122 THR B CB  
4090 O OG1 . THR B 124 ? 0.9437 0.6721 0.7494 -0.0575 -0.0145 0.0115  122 THR B OG1 
4091 C CG2 . THR B 124 ? 0.7949 0.5488 0.6031 -0.0398 -0.0471 0.0111  122 THR B CG2 
4092 N N   . GLN B 125 ? 0.8549 0.6585 0.7416 -0.0874 -0.0351 -0.0237 123 GLN B N   
4093 C CA  . GLN B 125 ? 0.7903 0.6434 0.7141 -0.0865 -0.0499 -0.0337 123 GLN B CA  
4094 C C   . GLN B 125 ? 0.7460 0.6084 0.6678 -0.0678 -0.0578 -0.0207 123 GLN B C   
4095 O O   . GLN B 125 ? 0.7606 0.6061 0.6683 -0.0644 -0.0458 -0.0121 123 GLN B O   
4096 C CB  . GLN B 125 ? 0.7645 0.6401 0.7240 -0.1063 -0.0353 -0.0509 123 GLN B CB  
4097 C CG  . GLN B 125 ? 0.7781 0.7075 0.7777 -0.0987 -0.0487 -0.0596 123 GLN B CG  
4098 C CD  . GLN B 125 ? 0.7579 0.7308 0.7793 -0.0934 -0.0736 -0.0745 123 GLN B CD  
4099 O OE1 . GLN B 125 ? 0.7768 0.7395 0.7804 -0.0958 -0.0823 -0.0780 123 GLN B OE1 
4100 N NE2 . GLN B 125 ? 0.6696 0.6928 0.7272 -0.0829 -0.0857 -0.0837 123 GLN B NE2 
4101 N N   . VAL B 126 ? 0.6967 0.5833 0.6293 -0.0550 -0.0762 -0.0202 124 VAL B N   
4102 C CA  . VAL B 126 ? 0.7262 0.6190 0.6626 -0.0398 -0.0800 -0.0116 124 VAL B CA  
4103 C C   . VAL B 126 ? 0.7273 0.6573 0.6956 -0.0320 -0.0903 -0.0193 124 VAL B C   
4104 O O   . VAL B 126 ? 0.7187 0.6670 0.6894 -0.0251 -0.1061 -0.0230 124 VAL B O   
4105 C CB  . VAL B 126 ? 0.7449 0.6194 0.6569 -0.0276 -0.0871 -0.0001 124 VAL B CB  
4106 C CG1 . VAL B 126 ? 0.6881 0.5664 0.6086 -0.0142 -0.0887 0.0054  124 VAL B CG1 
4107 C CG2 . VAL B 126 ? 0.7761 0.6255 0.6640 -0.0300 -0.0783 0.0049  124 VAL B CG2 
4108 N N   . THR B 127 ? 0.7141 0.6580 0.7049 -0.0301 -0.0819 -0.0227 125 THR B N   
4109 C CA  . THR B 127 ? 0.6991 0.6827 0.7250 -0.0187 -0.0903 -0.0315 125 THR B CA  
4110 C C   . THR B 127 ? 0.6969 0.6704 0.7234 -0.0002 -0.0872 -0.0223 125 THR B C   
4111 O O   . THR B 127 ? 0.6719 0.6278 0.6935 -0.0061 -0.0718 -0.0213 125 THR B O   
4112 C CB  . THR B 127 ? 0.6410 0.6562 0.7033 -0.0360 -0.0783 -0.0504 125 THR B CB  
4113 O OG1 . THR B 127 ? 0.6248 0.6414 0.6868 -0.0574 -0.0758 -0.0616 125 THR B OG1 
4114 C CG2 . THR B 127 ? 0.5628 0.6310 0.6684 -0.0207 -0.0895 -0.0632 125 THR B CG2 
4115 N N   . VAL B 128 ? 0.6972 0.6790 0.7260 0.0236  -0.1008 -0.0163 126 VAL B N   
4116 C CA  . VAL B 128 ? 0.6993 0.6630 0.7279 0.0433  -0.0948 -0.0075 126 VAL B CA  
4117 C C   . VAL B 128 ? 0.7470 0.7512 0.8119 0.0634  -0.1015 -0.0160 126 VAL B C   
4118 O O   . VAL B 128 ? 0.8512 0.8902 0.9255 0.0782  -0.1208 -0.0195 126 VAL B O   
4119 C CB  . VAL B 128 ? 0.7185 0.6445 0.7123 0.0588  -0.0986 0.0107  126 VAL B CB  
4120 C CG1 . VAL B 128 ? 0.7342 0.6239 0.7237 0.0677  -0.0817 0.0172  126 VAL B CG1 
4121 C CG2 . VAL B 128 ? 0.7708 0.6754 0.7359 0.0408  -0.0980 0.0146  126 VAL B CG2 
4122 N N   . SER B 129 ? 0.8634 0.8681 0.9491 0.0659  -0.0865 -0.0219 127 SER B N   
4123 C CA  . SER B 129 ? 0.8892 0.9353 1.0145 0.0873  -0.0904 -0.0320 127 SER B CA  
4124 C C   . SER B 129 ? 0.9072 0.9396 1.0200 0.1274  -0.1019 -0.0165 127 SER B C   
4125 O O   . SER B 129 ? 0.9195 0.8966 0.9941 0.1347  -0.0960 0.0021  127 SER B O   
4126 C CB  . SER B 129 ? 0.8778 0.9223 1.0242 0.0799  -0.0677 -0.0426 127 SER B CB  
4127 O OG  . SER B 129 ? 0.9300 0.9648 1.0663 0.0470  -0.0529 -0.0488 127 SER B OG  
4128 N N   . ALA C 2   ? 1.1174 1.0814 1.0292 0.1812  -0.1011 -0.1007 0   ALA C N   
4129 C CA  . ALA C 2   ? 1.1502 1.1104 1.0625 0.2032  -0.1098 -0.1053 0   ALA C CA  
4130 C C   . ALA C 2   ? 1.2139 1.1351 1.1288 0.1806  -0.1128 -0.0882 0   ALA C C   
4131 O O   . ALA C 2   ? 1.2652 1.1252 1.1542 0.1670  -0.1167 -0.0788 0   ALA C O   
4132 C CB  . ALA C 2   ? 1.0692 1.1159 1.0213 0.2133  -0.1039 -0.1132 0   ALA C CB  
4133 N N   . GLN C 3   ? 1.1729 1.1318 1.1176 0.1751  -0.1107 -0.0846 1   GLN C N   
4134 C CA  . GLN C 3   ? 1.0721 0.9959 1.0145 0.1599  -0.1130 -0.0718 1   GLN C CA  
4135 C C   . GLN C 3   ? 1.0040 0.9796 0.9841 0.1445  -0.1069 -0.0683 1   GLN C C   
4136 O O   . GLN C 3   ? 0.9751 1.0120 0.9834 0.1404  -0.1011 -0.0735 1   GLN C O   
4137 C CB  . GLN C 3   ? 1.1133 0.9874 1.0190 0.1856  -0.1276 -0.0763 1   GLN C CB  
4138 C CG  . GLN C 3   ? 1.0918 0.9970 0.9942 0.2246  -0.1374 -0.0940 1   GLN C CG  
4139 C CD  . GLN C 3   ? 1.2425 1.2077 1.1775 0.2268  -0.1391 -0.0967 1   GLN C CD  
4140 O OE1 . GLN C 3   ? 1.2675 1.2087 1.1917 0.2268  -0.1470 -0.0915 1   GLN C OE1 
4141 N NE2 . GLN C 3   ? 1.2093 1.2542 1.1824 0.2259  -0.1321 -0.1045 1   GLN C NE2 
4142 N N   . VAL C 4   ? 0.8924 0.8405 0.8686 0.1339  -0.1082 -0.0596 2   VAL C N   
4143 C CA  . VAL C 4   ? 0.8334 0.8145 0.8337 0.1207  -0.1058 -0.0582 2   VAL C CA  
4144 C C   . VAL C 4   ? 0.8765 0.8279 0.8547 0.1330  -0.1163 -0.0594 2   VAL C C   
4145 O O   . VAL C 4   ? 0.8845 0.7794 0.8318 0.1372  -0.1191 -0.0531 2   VAL C O   
4146 C CB  . VAL C 4   ? 0.7780 0.7532 0.7945 0.0898  -0.0933 -0.0447 2   VAL C CB  
4147 C CG1 . VAL C 4   ? 0.7861 0.7984 0.8247 0.0762  -0.0848 -0.0428 2   VAL C CG1 
4148 C CG2 . VAL C 4   ? 0.7812 0.7009 0.7778 0.0837  -0.0899 -0.0328 2   VAL C CG2 
4149 N N   . GLN C 5   ? 0.8758 0.8667 0.8683 0.1362  -0.1228 -0.0667 3   GLN C N   
4150 C CA  . GLN C 5   ? 0.7713 0.7399 0.7421 0.1467  -0.1344 -0.0682 3   GLN C CA  
4151 C C   . GLN C 5   ? 0.7723 0.7347 0.7490 0.1203  -0.1280 -0.0623 3   GLN C C   
4152 O O   . GLN C 5   ? 0.7451 0.7473 0.7494 0.1008  -0.1234 -0.0641 3   GLN C O   
4153 C CB  . GLN C 5   ? 0.7737 0.7923 0.7530 0.1713  -0.1499 -0.0816 3   GLN C CB  
4154 C CG  . GLN C 5   ? 0.9558 0.9583 0.9119 0.2093  -0.1609 -0.0887 3   GLN C CG  
4155 C CD  . GLN C 5   ? 1.0560 1.0011 0.9682 0.2298  -0.1762 -0.0862 3   GLN C CD  
4156 O OE1 . GLN C 5   ? 1.0851 0.9636 0.9589 0.2394  -0.1782 -0.0807 3   GLN C OE1 
4157 N NE2 . GLN C 5   ? 0.9913 0.9598 0.9053 0.2339  -0.1883 -0.0894 3   GLN C NE2 
4158 N N   . LEU C 6   ? 0.8076 0.7172 0.7542 0.1193  -0.1276 -0.0554 4   LEU C N   
4159 C CA  . LEU C 6   ? 0.8372 0.7306 0.7807 0.0991  -0.1197 -0.0511 4   LEU C CA  
4160 C C   . LEU C 6   ? 0.8851 0.7712 0.8047 0.1074  -0.1333 -0.0572 4   LEU C C   
4161 O O   . LEU C 6   ? 0.9300 0.7826 0.8166 0.1247  -0.1416 -0.0551 4   LEU C O   
4162 C CB  . LEU C 6   ? 0.8569 0.7031 0.7855 0.0905  -0.1053 -0.0381 4   LEU C CB  
4163 C CG  . LEU C 6   ? 0.7999 0.6521 0.7496 0.0817  -0.0943 -0.0307 4   LEU C CG  
4164 C CD1 . LEU C 6   ? 0.8229 0.6399 0.7627 0.0723  -0.0812 -0.0174 4   LEU C CD1 
4165 C CD2 . LEU C 6   ? 0.7605 0.6517 0.7434 0.0665  -0.0891 -0.0329 4   LEU C CD2 
4166 N N   . VAL C 7   ? 0.8886 0.8025 0.8208 0.0930  -0.1370 -0.0642 5   VAL C N   
4167 C CA  . VAL C 7   ? 0.9166 0.8277 0.8262 0.0963  -0.1516 -0.0710 5   VAL C CA  
4168 C C   . VAL C 7   ? 0.9144 0.7918 0.8080 0.0751  -0.1414 -0.0699 5   VAL C C   
4169 O O   . VAL C 7   ? 0.9122 0.8030 0.8259 0.0536  -0.1348 -0.0717 5   VAL C O   
4170 C CB  . VAL C 7   ? 0.7941 0.7718 0.7295 0.0968  -0.1688 -0.0825 5   VAL C CB  
4171 C CG1 . VAL C 7   ? 0.9195 0.8960 0.8279 0.1087  -0.1894 -0.0888 5   VAL C CG1 
4172 C CG2 . VAL C 7   ? 0.7249 0.7464 0.6864 0.1166  -0.1719 -0.0849 5   VAL C CG2 
4173 N N   . GLU C 8   ? 0.9836 0.8143 0.8370 0.0818  -0.1400 -0.0668 6   GLU C N   
4174 C CA  . GLU C 8   ? 1.1292 0.9240 0.9604 0.0677  -0.1286 -0.0675 6   GLU C CA  
4175 C C   . GLU C 8   ? 1.2270 1.0279 1.0397 0.0595  -0.1450 -0.0800 6   GLU C C   
4176 O O   . GLU C 8   ? 1.2431 1.0691 1.0506 0.0696  -0.1659 -0.0854 6   GLU C O   
4177 C CB  . GLU C 8   ? 1.1736 0.9205 0.9686 0.0770  -0.1163 -0.0580 6   GLU C CB  
4178 C CG  . GLU C 8   ? 1.0720 0.8088 0.8841 0.0749  -0.0958 -0.0456 6   GLU C CG  
4179 C CD  . GLU C 8   ? 1.1481 0.8820 0.9589 0.0868  -0.0998 -0.0366 6   GLU C CD  
4180 O OE1 . GLU C 8   ? 1.2022 0.9615 1.0268 0.0963  -0.1153 -0.0414 6   GLU C OE1 
4181 O OE2 . GLU C 8   ? 1.1521 0.8583 0.9462 0.0863  -0.0875 -0.0250 6   GLU C OE2 
4182 N N   . SER C 9   ? 0.9957 0.7716 0.7961 0.0421  -0.1366 -0.0850 7   SER C N   
4183 C CA  . SER C 9   ? 1.0028 0.7760 0.7801 0.0288  -0.1522 -0.0981 7   SER C CA  
4184 C C   . SER C 9   ? 1.0058 0.7210 0.7450 0.0218  -0.1375 -0.1020 7   SER C C   
4185 O O   . SER C 9   ? 0.9888 0.6824 0.7377 0.0196  -0.1172 -0.0968 7   SER C O   
4186 C CB  . SER C 9   ? 0.9385 0.7590 0.7515 0.0061  -0.1644 -0.1049 7   SER C CB  
4187 O OG  . SER C 9   ? 0.9167 0.7567 0.7145 -0.0043 -0.1881 -0.1166 7   SER C OG  
4188 N N   . GLY C 10  ? 1.0658 0.7565 0.7597 0.0208  -0.1485 -0.1119 8   GLY C N   
4189 C CA  . GLY C 10  ? 1.0301 0.6638 0.6793 0.0174  -0.1355 -0.1192 8   GLY C CA  
4190 C C   . GLY C 10  ? 1.1541 0.7572 0.7546 0.0354  -0.1300 -0.1171 8   GLY C C   
4191 O O   . GLY C 10  ? 1.2243 0.8443 0.8140 0.0451  -0.1459 -0.1136 8   GLY C O   
4192 N N   . GLY C 11  ? 1.1671 0.7254 0.7364 0.0410  -0.1070 -0.1186 9   GLY C N   
4193 C CA  . GLY C 11  ? 1.1909 0.7208 0.7104 0.0552  -0.0970 -0.1161 9   GLY C CA  
4194 C C   . GLY C 11  ? 1.2830 0.7882 0.7455 0.0498  -0.1155 -0.1312 9   GLY C C   
4195 O O   . GLY C 11  ? 1.2958 0.8088 0.7588 0.0334  -0.1385 -0.1440 9   GLY C O   
4196 N N   . GLY C 12  ? 1.3464 0.8232 0.7568 0.0615  -0.1055 -0.1290 10  GLY C N   
4197 C CA  . GLY C 12  ? 1.3714 0.8212 0.7185 0.0584  -0.1218 -0.1419 10  GLY C CA  
4198 C C   . GLY C 12  ? 1.4157 0.8201 0.7046 0.0687  -0.0951 -0.1457 10  GLY C C   
4199 O O   . GLY C 12  ? 1.4223 0.8250 0.7241 0.0795  -0.0642 -0.1357 10  GLY C O   
4200 N N   . LEU C 13  ? 1.4588 0.8304 0.6825 0.0650  -0.1075 -0.1608 11  LEU C N   
4201 C CA  . LEU C 13  ? 1.4961 0.8236 0.6533 0.0754  -0.0833 -0.1679 11  LEU C CA  
4202 C C   . LEU C 13  ? 1.6083 0.8955 0.7462 0.0719  -0.0744 -0.1906 11  LEU C C   
4203 O O   . LEU C 13  ? 1.6868 0.9461 0.7856 0.0579  -0.0975 -0.2100 11  LEU C O   
4204 C CB  . LEU C 13  ? 1.4959 0.8055 0.5835 0.0749  -0.1024 -0.1706 11  LEU C CB  
4205 C CG  . LEU C 13  ? 1.4855 0.7556 0.4986 0.0864  -0.0759 -0.1742 11  LEU C CG  
4206 C CD1 . LEU C 13  ? 1.4660 0.7538 0.4834 0.0969  -0.0527 -0.1484 11  LEU C CD1 
4207 C CD2 . LEU C 13  ? 1.7210 0.9598 0.6557 0.0800  -0.1016 -0.1884 11  LEU C CD2 
4208 N N   . VAL C 14  ? 1.5316 0.8137 0.6945 0.0847  -0.0425 -0.1882 12  VAL C N   
4209 C CA  . VAL C 14  ? 1.6298 0.8646 0.7698 0.0883  -0.0309 -0.2086 12  VAL C CA  
4210 C C   . VAL C 14  ? 1.6940 0.8970 0.7758 0.1120  0.0024  -0.2159 12  VAL C C   
4211 O O   . VAL C 14  ? 1.6600 0.8846 0.7278 0.1217  0.0184  -0.2022 12  VAL C O   
4212 C CB  . VAL C 14  ? 1.5972 0.8467 0.8048 0.0895  -0.0210 -0.2020 12  VAL C CB  
4213 C CG1 . VAL C 14  ? 1.4905 0.7659 0.7443 0.0633  -0.0536 -0.1996 12  VAL C CG1 
4214 C CG2 . VAL C 14  ? 1.5022 0.7973 0.7595 0.1063  0.0063  -0.1787 12  VAL C CG2 
4215 N N   . GLN C 15  ? 1.7945 0.9439 0.8389 0.1214  0.0131  -0.2378 13  GLN C N   
4216 C CA  . GLN C 15  ? 1.7861 0.9209 0.7926 0.1461  0.0462  -0.2431 13  GLN C CA  
4217 C C   . GLN C 15  ? 1.7864 0.9373 0.8336 0.1730  0.0818  -0.2359 13  GLN C C   
4218 O O   . GLN C 15  ? 1.7246 0.8879 0.8285 0.1705  0.0779  -0.2288 13  GLN C O   
4219 C CB  . GLN C 15  ? 1.8715 0.9590 0.8346 0.1417  0.0362  -0.2640 13  GLN C CB  
4220 C CG  . GLN C 15  ? 1.8686 0.9444 0.7831 0.1195  0.0064  -0.2714 13  GLN C CG  
4221 C CD  . GLN C 15  ? 2.1110 1.1373 0.9751 0.1173  0.0013  -0.2927 13  GLN C CD  
4222 O OE1 . GLN C 15  ? 2.1028 1.0981 0.9696 0.1299  0.0150  -0.3024 13  GLN C OE1 
4223 N NE2 . GLN C 15  ? 2.1487 1.1655 0.9647 0.1020  -0.0199 -0.2996 13  GLN C NE2 
4224 N N   . ALA C 16  ? 1.8652 1.0247 0.8883 0.1982  0.1163  -0.2359 14  ALA C N   
4225 C CA  . ALA C 16  ? 1.7702 0.9556 0.8329 0.2272  0.1515  -0.2292 14  ALA C CA  
4226 C C   . ALA C 16  ? 1.8025 0.9531 0.8809 0.2373  0.1468  -0.2420 14  ALA C C   
4227 O O   . ALA C 16  ? 1.8005 0.9077 0.8344 0.2395  0.1408  -0.2597 14  ALA C O   
4228 C CB  . ALA C 16  ? 1.7217 0.9324 0.7539 0.2500  0.1887  -0.2271 14  ALA C CB  
4229 N N   . GLY C 17  ? 1.7603 0.9264 0.8984 0.2429  0.1487  -0.2322 15  GLY C N   
4230 C CA  . GLY C 17  ? 1.7417 0.8727 0.8951 0.2497  0.1412  -0.2400 15  GLY C CA  
4231 C C   . GLY C 17  ? 1.7265 0.8252 0.8896 0.2154  0.1034  -0.2426 15  GLY C C   
4232 O O   . GLY C 17  ? 1.6618 0.7328 0.8420 0.2165  0.0962  -0.2444 15  GLY C O   
4233 N N   . ASP C 18  ? 1.8718 0.9764 1.0244 0.1850  0.0789  -0.2419 16  ASP C N   
4234 C CA  . ASP C 18  ? 1.8622 0.9504 1.0292 0.1498  0.0434  -0.2436 16  ASP C CA  
4235 C C   . ASP C 18  ? 1.8145 0.9334 1.0485 0.1464  0.0425  -0.2269 16  ASP C C   
4236 O O   . ASP C 18  ? 1.7882 0.9351 1.0568 0.1722  0.0682  -0.2149 16  ASP C O   
4237 C CB  . ASP C 18  ? 1.8513 0.9480 0.9903 0.1226  0.0173  -0.2475 16  ASP C CB  
4238 C CG  . ASP C 18  ? 2.0298 1.0833 1.1219 0.1007  -0.0070 -0.2650 16  ASP C CG  
4239 O OD1 . ASP C 18  ? 2.0781 1.0875 1.1435 0.1119  0.0019  -0.2762 16  ASP C OD1 
4240 O OD2 . ASP C 18  ? 1.9461 1.0109 1.0274 0.0730  -0.0361 -0.2675 16  ASP C OD2 
4241 N N   . SER C 19  ? 1.7019 0.8202 0.9562 0.1134  0.0126  -0.2255 17  SER C N   
4242 C CA  . SER C 19  ? 1.4144 0.5765 0.7414 0.1040  0.0084  -0.2057 17  SER C CA  
4243 C C   . SER C 19  ? 1.3890 0.6081 0.7509 0.0745  -0.0165 -0.1952 17  SER C C   
4244 O O   . SER C 19  ? 1.3600 0.5728 0.6864 0.0576  -0.0366 -0.2059 17  SER C O   
4245 C CB  . SER C 19  ? 1.3678 0.4831 0.6986 0.0933  -0.0013 -0.2097 17  SER C CB  
4246 O OG  . SER C 19  ? 1.4735 0.5733 0.8098 0.1262  0.0233  -0.2064 17  SER C OG  
4247 N N   . LEU C 20  ? 1.4321 0.7078 0.8628 0.0709  -0.0157 -0.1745 18  LEU C N   
4248 C CA  . LEU C 20  ? 1.2826 0.6163 0.7519 0.0498  -0.0367 -0.1639 18  LEU C CA  
4249 C C   . LEU C 20  ? 1.1595 0.5339 0.6962 0.0440  -0.0359 -0.1464 18  LEU C C   
4250 O O   . LEU C 20  ? 1.1452 0.5182 0.7041 0.0619  -0.0154 -0.1371 18  LEU C O   
4251 C CB  . LEU C 20  ? 1.1846 0.5533 0.6491 0.0623  -0.0307 -0.1556 18  LEU C CB  
4252 C CG  . LEU C 20  ? 1.2087 0.6226 0.6919 0.0463  -0.0564 -0.1498 18  LEU C CG  
4253 C CD1 . LEU C 20  ? 1.2356 0.6363 0.6976 0.0205  -0.0861 -0.1657 18  LEU C CD1 
4254 C CD2 . LEU C 20  ? 1.2271 0.6491 0.6804 0.0596  -0.0517 -0.1447 18  LEU C CD2 
4255 N N   . THR C 21  ? 1.1042 0.5185 0.6726 0.0201  -0.0586 -0.1423 19  THR C N   
4256 C CA  . THR C 21  ? 1.0570 0.5122 0.6848 0.0116  -0.0599 -0.1272 19  THR C CA  
4257 C C   . THR C 21  ? 1.0679 0.5874 0.7311 0.0091  -0.0709 -0.1175 19  THR C C   
4258 O O   . THR C 21  ? 1.1102 0.6481 0.7638 -0.0039 -0.0923 -0.1250 19  THR C O   
4259 C CB  . THR C 21  ? 1.0657 0.5025 0.6957 -0.0176 -0.0758 -0.1327 19  THR C CB  
4260 O OG1 . THR C 21  ? 1.1017 0.4702 0.6996 -0.0106 -0.0643 -0.1388 19  THR C OG1 
4261 C CG2 . THR C 21  ? 1.0461 0.5359 0.7354 -0.0296 -0.0792 -0.1171 19  THR C CG2 
4262 N N   . LEU C 22  ? 1.0250 0.5771 0.7266 0.0227  -0.0578 -0.1015 20  LEU C N   
4263 C CA  . LEU C 22  ? 0.9800 0.5844 0.7133 0.0233  -0.0674 -0.0922 20  LEU C CA  
4264 C C   . LEU C 22  ? 0.9632 0.6044 0.7449 0.0101  -0.0730 -0.0849 20  LEU C C   
4265 O O   . LEU C 22  ? 0.9263 0.5529 0.7211 0.0048  -0.0640 -0.0808 20  LEU C O   
4266 C CB  . LEU C 22  ? 0.9809 0.5923 0.7172 0.0436  -0.0506 -0.0796 20  LEU C CB  
4267 C CG  . LEU C 22  ? 0.9715 0.5470 0.6618 0.0573  -0.0356 -0.0834 20  LEU C CG  
4268 C CD1 . LEU C 22  ? 0.9345 0.5194 0.6397 0.0716  -0.0118 -0.0685 20  LEU C CD1 
4269 C CD2 . LEU C 22  ? 1.0810 0.6533 0.7339 0.0579  -0.0505 -0.0889 20  LEU C CD2 
4270 N N   . SER C 23  ? 0.9543 0.6429 0.7597 0.0068  -0.0881 -0.0831 21  SER C N   
4271 C CA  . SER C 23  ? 0.8772 0.6084 0.7260 -0.0057 -0.0934 -0.0778 21  SER C CA  
4272 C C   . SER C 23  ? 0.8465 0.6195 0.7195 0.0089  -0.0969 -0.0707 21  SER C C   
4273 O O   . SER C 23  ? 0.8493 0.6347 0.7092 0.0191  -0.1095 -0.0752 21  SER C O   
4274 C CB  . SER C 23  ? 0.8809 0.6330 0.7323 -0.0312 -0.1123 -0.0881 21  SER C CB  
4275 O OG  . SER C 23  ? 0.9584 0.6593 0.7738 -0.0455 -0.1131 -0.0974 21  SER C OG  
4276 N N   . CYS C 24  ? 0.7953 0.5853 0.6991 0.0108  -0.0872 -0.0601 22  CYS C N   
4277 C CA  . CYS C 24  ? 0.8563 0.6782 0.7795 0.0240  -0.0901 -0.0544 22  CYS C CA  
4278 C C   . CYS C 24  ? 0.8248 0.6956 0.7830 0.0125  -0.0964 -0.0553 22  CYS C C   
4279 O O   . CYS C 24  ? 0.8398 0.7126 0.8162 0.0009  -0.0871 -0.0484 22  CYS C O   
4280 C CB  . CYS C 24  ? 0.8902 0.6924 0.8160 0.0343  -0.0740 -0.0417 22  CYS C CB  
4281 S SG  . CYS C 24  ? 0.8556 0.6823 0.7977 0.0469  -0.0778 -0.0351 22  CYS C SG  
4282 N N   . ALA C 25  ? 0.8050 0.7178 0.7715 0.0167  -0.1120 -0.0633 23  ALA C N   
4283 C CA  . ALA C 25  ? 0.7643 0.7355 0.7647 0.0079  -0.1166 -0.0653 23  ALA C CA  
4284 C C   . ALA C 25  ? 0.7798 0.7679 0.7936 0.0280  -0.1127 -0.0607 23  ALA C C   
4285 O O   . ALA C 25  ? 0.7731 0.7516 0.7718 0.0518  -0.1191 -0.0626 23  ALA C O   
4286 C CB  . ALA C 25  ? 0.6968 0.7163 0.7038 0.0048  -0.1354 -0.0769 23  ALA C CB  
4287 N N   . ALA C 26  ? 0.7591 0.7662 0.7955 0.0176  -0.1032 -0.0547 24  ALA C N   
4288 C CA  . ALA C 26  ? 0.7321 0.7518 0.7774 0.0335  -0.0992 -0.0516 24  ALA C CA  
4289 C C   . ALA C 26  ? 0.7068 0.7946 0.7780 0.0336  -0.1037 -0.0589 24  ALA C C   
4290 O O   . ALA C 26  ? 0.7254 0.8447 0.8158 0.0093  -0.0992 -0.0567 24  ALA C O   
4291 C CB  . ALA C 26  ? 0.7352 0.7273 0.7835 0.0236  -0.0850 -0.0389 24  ALA C CB  
4292 N N   . SER C 27  ? 0.7415 0.8510 0.8108 0.0615  -0.1121 -0.0671 25  SER C N   
4293 C CA  . SER C 27  ? 0.7661 0.9470 0.8601 0.0701  -0.1150 -0.0759 25  SER C CA  
4294 C C   . SER C 27  ? 0.7906 0.9627 0.8774 0.0921  -0.1098 -0.0766 25  SER C C   
4295 O O   . SER C 27  ? 0.7858 0.9149 0.8463 0.1176  -0.1161 -0.0784 25  SER C O   
4296 C CB  . SER C 27  ? 0.8123 1.0330 0.9097 0.0898  -0.1318 -0.0878 25  SER C CB  
4297 O OG  . SER C 27  ? 0.8155 0.9931 0.8833 0.1236  -0.1413 -0.0906 25  SER C OG  
4298 N N   . GLY C 28  ? 0.6967 0.9046 0.8015 0.0804  -0.0991 -0.0748 26  GLY C N   
4299 C CA  . GLY C 28  ? 0.7452 0.9448 0.8393 0.0991  -0.0945 -0.0772 26  GLY C CA  
4300 C C   . GLY C 28  ? 0.7573 0.9876 0.8671 0.0764  -0.0810 -0.0711 26  GLY C C   
4301 O O   . GLY C 28  ? 0.7081 0.9632 0.8362 0.0457  -0.0754 -0.0638 26  GLY C O   
4302 N N   . ARG C 29  ? 0.7718 0.9943 0.8684 0.0912  -0.0769 -0.0741 27  ARG C N   
4303 C CA  . ARG C 29  ? 0.8180 1.0660 0.9220 0.0725  -0.0647 -0.0684 27  ARG C CA  
4304 C C   . ARG C 29  ? 0.8962 1.0881 0.9898 0.0494  -0.0607 -0.0512 27  ARG C C   
4305 O O   . ARG C 29  ? 0.8893 1.0233 0.9636 0.0577  -0.0657 -0.0475 27  ARG C O   
4306 C CB  . ARG C 29  ? 0.7940 1.0579 0.8835 0.0996  -0.0625 -0.0810 27  ARG C CB  
4307 C CG  . ARG C 29  ? 0.8733 1.0715 0.9280 0.1290  -0.0728 -0.0876 27  ARG C CG  
4308 C CD  . ARG C 29  ? 0.9249 1.1033 0.9539 0.1369  -0.0692 -0.0918 27  ARG C CD  
4309 N NE  . ARG C 29  ? 1.0293 1.1499 1.0438 0.1136  -0.0694 -0.0764 27  ARG C NE  
4310 C CZ  . ARG C 29  ? 1.0965 1.1765 1.0805 0.1175  -0.0722 -0.0780 27  ARG C CZ  
4311 N NH1 . ARG C 29  ? 1.1539 1.2341 1.1123 0.1452  -0.0743 -0.0955 27  ARG C NH1 
4312 N NH2 . ARG C 29  ? 1.0663 1.1054 1.0443 0.0938  -0.0735 -0.0623 27  ARG C NH2 
4313 N N   . THR C 30  ? 0.8077 1.0194 0.9138 0.0203  -0.0521 -0.0397 28  THR C N   
4314 C CA  . THR C 30  ? 0.7385 0.9052 0.8380 0.0002  -0.0490 -0.0221 28  THR C CA  
4315 C C   . THR C 30  ? 0.6917 0.8064 0.7868 0.0008  -0.0540 -0.0164 28  THR C C   
4316 O O   . THR C 30  ? 0.6816 0.7531 0.7653 0.0049  -0.0552 -0.0091 28  THR C O   
4317 C CB  . THR C 30  ? 0.6888 0.8363 0.7705 0.0073  -0.0481 -0.0198 28  THR C CB  
4318 O OG1 . THR C 30  ? 0.7892 0.8958 0.8529 0.0296  -0.0561 -0.0266 28  THR C OG1 
4319 C CG2 . THR C 30  ? 0.6890 0.8875 0.7687 0.0126  -0.0422 -0.0293 28  THR C CG2 
4320 N N   . ALA C 31  ? 0.7063 0.8293 0.8101 -0.0046 -0.0568 -0.0200 29  ALA C N   
4321 C CA  . ALA C 31  ? 0.6416 0.7179 0.7372 -0.0027 -0.0602 -0.0169 29  ALA C CA  
4322 C C   . ALA C 31  ? 0.6711 0.7099 0.7650 -0.0192 -0.0545 -0.0011 29  ALA C C   
4323 O O   . ALA C 31  ? 0.6701 0.6690 0.7555 -0.0130 -0.0543 0.0027  29  ALA C O   
4324 C CB  . ALA C 31  ? 0.6276 0.7222 0.7287 -0.0064 -0.0660 -0.0257 29  ALA C CB  
4325 N N   . TYR C 32  ? 0.6284 0.6800 0.7284 -0.0383 -0.0497 0.0086  30  TYR C N   
4326 C CA  . TYR C 32  ? 0.6270 0.6411 0.7233 -0.0492 -0.0461 0.0244  30  TYR C CA  
4327 C C   . TYR C 32  ? 0.6133 0.6070 0.7067 -0.0374 -0.0453 0.0330  30  TYR C C   
4328 O O   . TYR C 32  ? 0.6530 0.6180 0.7462 -0.0391 -0.0432 0.0455  30  TYR C O   
4329 C CB  . TYR C 32  ? 0.6722 0.7011 0.7701 -0.0738 -0.0431 0.0344  30  TYR C CB  
4330 C CG  . TYR C 32  ? 0.6484 0.7074 0.7470 -0.0760 -0.0405 0.0388  30  TYR C CG  
4331 C CD1 . TYR C 32  ? 0.6626 0.7737 0.7665 -0.0741 -0.0388 0.0269  30  TYR C CD1 
4332 C CD2 . TYR C 32  ? 0.6496 0.6871 0.7420 -0.0783 -0.0400 0.0542  30  TYR C CD2 
4333 C CE1 . TYR C 32  ? 0.6548 0.7914 0.7538 -0.0748 -0.0352 0.0290  30  TYR C CE1 
4334 C CE2 . TYR C 32  ? 0.6273 0.6900 0.7149 -0.0814 -0.0387 0.0576  30  TYR C CE2 
4335 C CZ  . TYR C 32  ? 0.6327 0.7425 0.7214 -0.0800 -0.0355 0.0443  30  TYR C CZ  
4336 O OH  . TYR C 32  ? 0.5996 0.7325 0.6782 -0.0817 -0.0329 0.0458  30  TYR C OH  
4337 N N   . ARG C 33  ? 0.6109 0.6185 0.7010 -0.0253 -0.0479 0.0264  31  ARG C N   
4338 C CA  . ARG C 33  ? 0.6265 0.6172 0.7121 -0.0198 -0.0494 0.0342  31  ARG C CA  
4339 C C   . ARG C 33  ? 0.6134 0.5758 0.6940 -0.0080 -0.0508 0.0332  31  ARG C C   
4340 O O   . ARG C 33  ? 0.6221 0.5727 0.7011 -0.0077 -0.0523 0.0414  31  ARG C O   
4341 C CB  . ARG C 33  ? 0.6569 0.6676 0.7330 -0.0153 -0.0526 0.0269  31  ARG C CB  
4342 C CG  . ARG C 33  ? 0.6314 0.6812 0.7099 -0.0242 -0.0489 0.0234  31  ARG C CG  
4343 C CD  . ARG C 33  ? 0.6217 0.6786 0.6912 -0.0316 -0.0491 0.0311  31  ARG C CD  
4344 N NE  . ARG C 33  ? 0.6386 0.7363 0.7024 -0.0325 -0.0448 0.0216  31  ARG C NE  
4345 C CZ  . ARG C 33  ? 0.7127 0.8186 0.7590 -0.0287 -0.0457 0.0176  31  ARG C CZ  
4346 N NH1 . ARG C 33  ? 0.6705 0.7452 0.7031 -0.0271 -0.0531 0.0227  31  ARG C NH1 
4347 N NH2 . ARG C 33  ? 0.7496 0.8986 0.7910 -0.0275 -0.0389 0.0077  31  ARG C NH2 
4348 N N   . TYR C 34  ? 0.6438 0.5974 0.7204 -0.0008 -0.0509 0.0243  32  TYR C N   
4349 C CA  . TYR C 34  ? 0.6387 0.5658 0.7048 0.0092  -0.0516 0.0234  32  TYR C CA  
4350 C C   . TYR C 34  ? 0.6566 0.5650 0.7276 0.0072  -0.0443 0.0313  32  TYR C C   
4351 O O   . TYR C 34  ? 0.6218 0.5267 0.6926 0.0047  -0.0426 0.0271  32  TYR C O   
4352 C CB  . TYR C 34  ? 0.6326 0.5590 0.6849 0.0216  -0.0577 0.0087  32  TYR C CB  
4353 C CG  . TYR C 34  ? 0.6497 0.5881 0.6921 0.0318  -0.0649 -0.0010 32  TYR C CG  
4354 C CD1 . TYR C 34  ? 0.6835 0.6600 0.7357 0.0307  -0.0649 -0.0077 32  TYR C CD1 
4355 C CD2 . TYR C 34  ? 0.6690 0.5784 0.6884 0.0427  -0.0711 -0.0035 32  TYR C CD2 
4356 C CE1 . TYR C 34  ? 0.7345 0.7228 0.7751 0.0450  -0.0699 -0.0187 32  TYR C CE1 
4357 C CE2 . TYR C 34  ? 0.7591 0.6698 0.7626 0.0560  -0.0784 -0.0142 32  TYR C CE2 
4358 C CZ  . TYR C 34  ? 0.7643 0.7161 0.7791 0.0595  -0.0772 -0.0228 32  TYR C CZ  
4359 O OH  . TYR C 34  ? 0.7649 0.7193 0.7618 0.0775  -0.0829 -0.0356 32  TYR C OH  
4360 N N   . GLY C 35  ? 0.7961 0.6942 0.8705 0.0082  -0.0402 0.0423  33  GLY C N   
4361 C CA  . GLY C 35  ? 0.8231 0.7061 0.8999 0.0126  -0.0314 0.0478  33  GLY C CA  
4362 C C   . GLY C 35  ? 0.8795 0.7446 0.9374 0.0201  -0.0299 0.0392  33  GLY C C   
4363 O O   . GLY C 35  ? 0.9047 0.7644 0.9492 0.0219  -0.0346 0.0364  33  GLY C O   
4364 N N   . MET C 36  ? 0.7366 0.5865 0.7879 0.0242  -0.0244 0.0350  34  MET C N   
4365 C CA  . MET C 36  ? 0.7589 0.5910 0.7875 0.0305  -0.0243 0.0256  34  MET C CA  
4366 C C   . MET C 36  ? 0.7131 0.5304 0.7348 0.0378  -0.0110 0.0306  34  MET C C   
4367 O O   . MET C 36  ? 0.7254 0.5414 0.7586 0.0416  -0.0025 0.0363  34  MET C O   
4368 C CB  . MET C 36  ? 0.7197 0.5477 0.7399 0.0276  -0.0308 0.0131  34  MET C CB  
4369 C CG  . MET C 36  ? 0.7230 0.5776 0.7577 0.0185  -0.0396 0.0102  34  MET C CG  
4370 S SD  . MET C 36  ? 0.9025 0.7763 0.9292 0.0258  -0.0523 -0.0012 34  MET C SD  
4371 C CE  . MET C 36  ? 0.8246 0.7385 0.8702 0.0137  -0.0580 -0.0071 34  MET C CE  
4372 N N   . GLY C 37  ? 0.7377 0.5437 0.7385 0.0414  -0.0091 0.0289  35  GLY C N   
4373 C CA  . GLY C 37  ? 0.7731 0.5702 0.7637 0.0482  0.0057  0.0328  35  GLY C CA  
4374 C C   . GLY C 37  ? 0.7790 0.5524 0.7337 0.0522  0.0043  0.0236  35  GLY C C   
4375 O O   . GLY C 37  ? 0.7813 0.5478 0.7204 0.0502  -0.0091 0.0183  35  GLY C O   
4376 N N   . TRP C 38  ? 0.8262 0.5870 0.7655 0.0603  0.0180  0.0213  36  TRP C N   
4377 C CA  . TRP C 38  ? 0.8469 0.5833 0.7465 0.0643  0.0183  0.0128  36  TRP C CA  
4378 C C   . TRP C 38  ? 0.8239 0.5636 0.7095 0.0640  0.0326  0.0237  36  TRP C C   
4379 O O   . TRP C 38  ? 0.8631 0.6227 0.7664 0.0675  0.0502  0.0323  36  TRP C O   
4380 C CB  . TRP C 38  ? 0.8479 0.5619 0.7301 0.0726  0.0235  0.0001  36  TRP C CB  
4381 C CG  . TRP C 38  ? 0.8390 0.5448 0.7240 0.0661  0.0070  -0.0113 36  TRP C CG  
4382 C CD1 . TRP C 38  ? 0.8578 0.5651 0.7647 0.0625  0.0055  -0.0113 36  TRP C CD1 
4383 C CD2 . TRP C 38  ? 0.8645 0.5629 0.7292 0.0603  -0.0108 -0.0228 36  TRP C CD2 
4384 N NE1 . TRP C 38  ? 0.8424 0.5450 0.7441 0.0510  -0.0108 -0.0218 36  TRP C NE1 
4385 C CE2 . TRP C 38  ? 0.8315 0.5334 0.7105 0.0503  -0.0212 -0.0295 36  TRP C CE2 
4386 C CE3 . TRP C 38  ? 0.8454 0.5363 0.6804 0.0625  -0.0199 -0.0269 36  TRP C CE3 
4387 C CZ2 . TRP C 38  ? 0.8317 0.5391 0.7019 0.0411  -0.0396 -0.0407 36  TRP C CZ2 
4388 C CZ3 . TRP C 38  ? 0.8746 0.5683 0.7001 0.0577  -0.0398 -0.0384 36  TRP C CZ3 
4389 C CH2 . TRP C 38  ? 0.9001 0.6065 0.7459 0.0465  -0.0491 -0.0455 36  TRP C CH2 
4390 N N   . PHE C 39  ? 0.8804 0.6027 0.7338 0.0598  0.0248  0.0243  37  PHE C N   
4391 C CA  . PHE C 39  ? 0.9327 0.6526 0.7638 0.0544  0.0375  0.0360  37  PHE C CA  
4392 C C   . PHE C 39  ? 0.8897 0.5787 0.6699 0.0595  0.0364  0.0285  37  PHE C C   
4393 O O   . PHE C 39  ? 0.9095 0.5787 0.6713 0.0642  0.0182  0.0167  37  PHE C O   
4394 C CB  . PHE C 39  ? 0.8784 0.5971 0.7097 0.0401  0.0275  0.0489  37  PHE C CB  
4395 C CG  . PHE C 39  ? 0.8408 0.5908 0.7161 0.0316  0.0296  0.0583  37  PHE C CG  
4396 C CD1 . PHE C 39  ? 0.8119 0.5704 0.7144 0.0344  0.0165  0.0520  37  PHE C CD1 
4397 C CD2 . PHE C 39  ? 0.8614 0.6366 0.7502 0.0190  0.0443  0.0742  37  PHE C CD2 
4398 C CE1 . PHE C 39  ? 0.7930 0.5786 0.7311 0.0263  0.0170  0.0609  37  PHE C CE1 
4399 C CE2 . PHE C 39  ? 0.8664 0.6731 0.7950 0.0100  0.0434  0.0831  37  PHE C CE2 
4400 C CZ  . PHE C 39  ? 0.7911 0.6001 0.7422 0.0145  0.0292  0.0762  37  PHE C CZ  
4401 N N   . ARG C 40  ? 0.9934 0.6830 0.7509 0.0580  0.0560  0.0360  38  ARG C N   
4402 C CA  . ARG C 40  ? 1.0163 0.6761 0.7189 0.0614  0.0572  0.0311  38  ARG C CA  
4403 C C   . ARG C 40  ? 1.0695 0.7225 0.7430 0.0466  0.0640  0.0491  38  ARG C C   
4404 O O   . ARG C 40  ? 1.1301 0.8111 0.8279 0.0341  0.0778  0.0643  38  ARG C O   
4405 C CB  . ARG C 40  ? 0.9476 0.6078 0.6369 0.0752  0.0772  0.0196  38  ARG C CB  
4406 C CG  . ARG C 40  ? 0.9814 0.6726 0.6788 0.0761  0.1083  0.0305  38  ARG C CG  
4407 C CD  . ARG C 40  ? 1.0114 0.7011 0.7000 0.0972  0.1268  0.0154  38  ARG C CD  
4408 N NE  . ARG C 40  ? 1.0832 0.8158 0.7920 0.1044  0.1574  0.0245  38  ARG C NE  
4409 C CZ  . ARG C 40  ? 1.0776 0.8157 0.7841 0.1282  0.1776  0.0129  38  ARG C CZ  
4410 N NH1 . ARG C 40  ? 1.0451 0.7398 0.7251 0.1437  0.1700  -0.0083 38  ARG C NH1 
4411 N NH2 . ARG C 40  ? 1.0140 0.8025 0.7441 0.1367  0.2057  0.0226  38  ARG C NH2 
4412 N N   . GLN C 41  ? 1.1396 0.7550 0.7589 0.0463  0.0527  0.0484  39  GLN C N   
4413 C CA  . GLN C 41  ? 1.1365 0.7316 0.7160 0.0301  0.0548  0.0668  39  GLN C CA  
4414 C C   . GLN C 41  ? 1.1578 0.7305 0.6780 0.0333  0.0647  0.0652  39  GLN C C   
4415 O O   . GLN C 41  ? 1.1858 0.7300 0.6732 0.0458  0.0477  0.0519  39  GLN C O   
4416 C CB  . GLN C 41  ? 1.1999 0.7591 0.7626 0.0270  0.0251  0.0712  39  GLN C CB  
4417 C CG  . GLN C 41  ? 1.2984 0.8147 0.8001 0.0135  0.0209  0.0882  39  GLN C CG  
4418 C CD  . GLN C 41  ? 1.2826 0.7532 0.7584 0.0203  -0.0116 0.0885  39  GLN C CD  
4419 O OE1 . GLN C 41  ? 1.2144 0.6863 0.7193 0.0190  -0.0235 0.0890  39  GLN C OE1 
4420 N NE2 . GLN C 41  ? 1.3422 0.7719 0.7605 0.0301  -0.0268 0.0876  39  GLN C NE2 
4421 N N   . HIS C 42  ? 1.2665 0.8561 0.7725 0.0208  0.0917  0.0789  40  HIS C N   
4422 C CA  . HIS C 42  ? 1.3453 0.9160 0.7898 0.0209  0.1050  0.0801  40  HIS C CA  
4423 C C   . HIS C 42  ? 1.3898 0.9093 0.7742 0.0069  0.0860  0.0952  40  HIS C C   
4424 O O   . HIS C 42  ? 1.4028 0.9051 0.7960 -0.0045 0.0680  0.1067  40  HIS C O   
4425 C CB  . HIS C 42  ? 1.3293 0.9473 0.7857 0.0131  0.1435  0.0899  40  HIS C CB  
4426 C CG  . HIS C 42  ? 1.2914 0.9476 0.7885 0.0358  0.1624  0.0723  40  HIS C CG  
4427 N ND1 . HIS C 42  ? 1.2593 0.9721 0.8181 0.0359  0.1809  0.0781  40  HIS C ND1 
4428 C CD2 . HIS C 42  ? 1.2651 0.9058 0.7460 0.0598  0.1634  0.0491  40  HIS C CD2 
4429 C CE1 . HIS C 42  ? 1.1819 0.9094 0.7595 0.0622  0.1930  0.0597  40  HIS C CE1 
4430 N NE2 . HIS C 42  ? 1.2349 0.9159 0.7641 0.0756  0.1829  0.0415  40  HIS C NE2 
4431 N N   . PRO C 43  ? 1.3909 0.8789 0.7071 0.0092  0.0877  0.0951  41  PRO C N   
4432 C CA  . PRO C 43  ? 1.3579 0.7877 0.6112 0.0012  0.0636  0.1085  41  PRO C CA  
4433 C C   . PRO C 43  ? 1.5195 0.9362 0.7616 -0.0281 0.0677  0.1361  41  PRO C C   
4434 O O   . PRO C 43  ? 1.5595 0.9858 0.7732 -0.0498 0.0933  0.1531  41  PRO C O   
4435 C CB  . PRO C 43  ? 1.4306 0.8398 0.6141 0.0054  0.0733  0.1057  41  PRO C CB  
4436 C CG  . PRO C 43  ? 1.4554 0.9160 0.6627 0.0065  0.1123  0.0990  41  PRO C CG  
4437 C CD  . PRO C 43  ? 1.4440 0.9441 0.7317 0.0196  0.1119  0.0837  41  PRO C CD  
4438 N N   . GLY C 44  ? 1.6451 1.0399 0.9071 -0.0305 0.0429  0.1404  42  GLY C N   
4439 C CA  . GLY C 44  ? 1.5910 0.9604 0.8368 -0.0599 0.0410  0.1648  42  GLY C CA  
4440 C C   . GLY C 44  ? 1.6151 1.0410 0.9213 -0.0828 0.0642  0.1736  42  GLY C C   
4441 O O   . GLY C 44  ? 1.6254 1.0311 0.9222 -0.1115 0.0599  0.1930  42  GLY C O   
4442 N N   . LYS C 45  ? 1.6314 1.1246 0.9964 -0.0713 0.0866  0.1603  43  LYS C N   
4443 C CA  . LYS C 45  ? 1.5698 1.1256 0.9958 -0.0892 0.1079  0.1687  43  LYS C CA  
4444 C C   . LYS C 45  ? 1.5232 1.0886 1.0069 -0.0807 0.0884  0.1591  43  LYS C C   
4445 O O   . LYS C 45  ? 1.5517 1.0811 1.0307 -0.0602 0.0617  0.1451  43  LYS C O   
4446 C CB  . LYS C 45  ? 1.5005 1.1223 0.9566 -0.0768 0.1422  0.1603  43  LYS C CB  
4447 C CG  . LYS C 45  ? 1.6094 1.2288 1.0075 -0.0850 0.1658  0.1691  43  LYS C CG  
4448 C CD  . LYS C 45  ? 1.6188 1.2915 1.0381 -0.0607 0.1963  0.1531  43  LYS C CD  
4449 C CE  . LYS C 45  ? 1.5301 1.2864 1.0190 -0.0670 0.2235  0.1600  43  LYS C CE  
4450 N NZ  . LYS C 45  ? 1.4459 1.2508 0.9459 -0.0403 0.2562  0.1458  43  LYS C NZ  
4451 N N   . GLU C 46  ? 1.4509 1.0705 0.9897 -0.0969 0.1021  0.1671  44  GLU C N   
4452 C CA  . GLU C 46  ? 1.4560 1.0865 1.0459 -0.0929 0.0851  0.1605  44  GLU C CA  
4453 C C   . GLU C 46  ? 1.4548 1.1100 1.0862 -0.0582 0.0837  0.1368  44  GLU C C   
4454 O O   . GLU C 46  ? 1.5145 1.1914 1.1474 -0.0403 0.1011  0.1268  44  GLU C O   
4455 C CB  . GLU C 46  ? 1.5035 1.1896 1.1394 -0.1212 0.0992  0.1765  44  GLU C CB  
4456 C CG  . GLU C 46  ? 1.5084 1.1818 1.1695 -0.1318 0.0760  0.1774  44  GLU C CG  
4457 C CD  . GLU C 46  ? 1.5655 1.3145 1.2968 -0.1403 0.0881  0.1815  44  GLU C CD  
4458 O OE1 . GLU C 46  ? 1.6423 1.4554 1.4017 -0.1416 0.1155  0.1875  44  GLU C OE1 
4459 O OE2 . GLU C 46  ? 1.5041 1.2500 1.2614 -0.1434 0.0701  0.1784  44  GLU C OE2 
4460 N N   . ARG C 47  ? 1.2884 0.9364 0.9492 -0.0500 0.0626  0.1279  45  ARG C N   
4461 C CA  . ARG C 47  ? 1.1941 0.8639 0.8943 -0.0233 0.0595  0.1082  45  ARG C CA  
4462 C C   . ARG C 47  ? 1.1757 0.9091 0.9327 -0.0220 0.0813  0.1100  45  ARG C C   
4463 O O   . ARG C 47  ? 1.1819 0.9465 0.9700 -0.0407 0.0849  0.1233  45  ARG C O   
4464 C CB  . ARG C 47  ? 1.0801 0.7283 0.7931 -0.0169 0.0323  0.0998  45  ARG C CB  
4465 C CG  . ARG C 47  ? 1.0369 0.6761 0.7521 0.0089  0.0193  0.0791  45  ARG C CG  
4466 C CD  . ARG C 47  ? 0.9779 0.5916 0.6899 0.0154  -0.0077 0.0725  45  ARG C CD  
4467 N NE  . ARG C 47  ? 1.0572 0.6202 0.7177 0.0085  -0.0217 0.0819  45  ARG C NE  
4468 C CZ  . ARG C 47  ? 1.1287 0.6549 0.7581 0.0251  -0.0449 0.0738  45  ARG C CZ  
4469 N NH1 . ARG C 47  ? 1.0676 0.6105 0.7163 0.0464  -0.0564 0.0563  45  ARG C NH1 
4470 N NH2 . ARG C 47  ? 1.1968 0.6688 0.7737 0.0199  -0.0576 0.0844  45  ARG C NH2 
4471 N N   . GLU C 48  ? 1.1512 0.9013 0.9190 0.0007  0.0942  0.0965  46  GLU C N   
4472 C CA  . GLU C 48  ? 1.1560 0.9605 0.9716 0.0103  0.1148  0.0967  46  GLU C CA  
4473 C C   . GLU C 48  ? 1.1508 0.9565 1.0002 0.0294  0.1035  0.0821  46  GLU C C   
4474 O O   . GLU C 48  ? 1.1320 0.9012 0.9636 0.0383  0.0859  0.0681  46  GLU C O   
4475 C CB  . GLU C 48  ? 1.1680 0.9868 0.9634 0.0236  0.1417  0.0930  46  GLU C CB  
4476 C CG  . GLU C 48  ? 1.2793 1.1045 1.0405 0.0022  0.1573  0.1095  46  GLU C CG  
4477 C CD  . GLU C 48  ? 1.4444 1.2501 1.1546 0.0156  0.1730  0.1005  46  GLU C CD  
4478 O OE1 . GLU C 48  ? 1.4603 1.2903 1.1819 0.0397  0.1930  0.0890  46  GLU C OE1 
4479 O OE2 . GLU C 48  ? 1.3903 1.1523 1.0448 0.0036  0.1646  0.1047  46  GLU C OE2 
4480 N N   . PHE C 49  ? 0.9860 0.8370 0.8844 0.0346  0.1134  0.0867  47  PHE C N   
4481 C CA  . PHE C 49  ? 0.8846 0.7370 0.8146 0.0495  0.1035  0.0771  47  PHE C CA  
4482 C C   . PHE C 49  ? 0.8884 0.7298 0.8096 0.0758  0.1154  0.0620  47  PHE C C   
4483 O O   . PHE C 49  ? 0.9153 0.7748 0.8297 0.0876  0.1381  0.0625  47  PHE C O   
4484 C CB  . PHE C 49  ? 0.8094 0.7110 0.7915 0.0439  0.1055  0.0903  47  PHE C CB  
4485 C CG  . PHE C 49  ? 0.7890 0.6900 0.7996 0.0574  0.0950  0.0835  47  PHE C CG  
4486 C CD1 . PHE C 49  ? 0.7811 0.6563 0.7894 0.0494  0.0727  0.0781  47  PHE C CD1 
4487 C CD2 . PHE C 49  ? 0.7608 0.6862 0.7977 0.0792  0.1078  0.0830  47  PHE C CD2 
4488 C CE1 . PHE C 49  ? 0.7353 0.6105 0.7661 0.0580  0.0642  0.0738  47  PHE C CE1 
4489 C CE2 . PHE C 49  ? 0.7164 0.6335 0.7728 0.0897  0.0970  0.0790  47  PHE C CE2 
4490 C CZ  . PHE C 49  ? 0.7597 0.6524 0.8128 0.0766  0.0756  0.0751  47  PHE C CZ  
4491 N N   . VAL C 50  ? 0.8426 0.6538 0.7618 0.0842  0.1001  0.0484  48  VAL C N   
4492 C CA  . VAL C 50  ? 0.8718 0.6587 0.7756 0.1055  0.1068  0.0328  48  VAL C CA  
4493 C C   . VAL C 50  ? 0.8748 0.6666 0.8131 0.1147  0.1012  0.0323  48  VAL C C   
4494 O O   . VAL C 50  ? 0.8682 0.6759 0.8232 0.1342  0.1161  0.0342  48  VAL C O   
4495 C CB  . VAL C 50  ? 0.9213 0.6602 0.7806 0.1030  0.0923  0.0165  48  VAL C CB  
4496 C CG1 . VAL C 50  ? 0.9393 0.6454 0.7815 0.1196  0.0943  -0.0004 48  VAL C CG1 
4497 C CG2 . VAL C 50  ? 0.9373 0.6660 0.7546 0.0981  0.0988  0.0175  48  VAL C CG2 
4498 N N   . ALA C 51  ? 0.9507 0.7297 0.8979 0.1024  0.0800  0.0303  49  ALA C N   
4499 C CA  . ALA C 51  ? 0.8380 0.6170 0.8116 0.1066  0.0729  0.0315  49  ALA C CA  
4500 C C   . ALA C 51  ? 0.8477 0.6391 0.8412 0.0873  0.0541  0.0374  49  ALA C C   
4501 O O   . ALA C 51  ? 0.8977 0.6871 0.8786 0.0744  0.0446  0.0360  49  ALA C O   
4502 C CB  . ALA C 51  ? 0.8265 0.5586 0.7734 0.1153  0.0688  0.0155  49  ALA C CB  
4503 N N   . SER C 52  ? 0.7981 0.6002 0.8192 0.0876  0.0488  0.0439  50  SER C N   
4504 C CA  . SER C 52  ? 0.7535 0.5682 0.7910 0.0710  0.0327  0.0483  50  SER C CA  
4505 C C   . SER C 52  ? 0.7306 0.5392 0.7825 0.0727  0.0270  0.0511  50  SER C C   
4506 O O   . SER C 52  ? 0.7189 0.5145 0.7713 0.0884  0.0350  0.0524  50  SER C O   
4507 C CB  . SER C 52  ? 0.7313 0.5816 0.7901 0.0616  0.0327  0.0621  50  SER C CB  
4508 O OG  . SER C 52  ? 0.7505 0.6302 0.8395 0.0691  0.0399  0.0750  50  SER C OG  
4509 N N   . ILE C 53  ? 0.7568 0.5725 0.8165 0.0576  0.0133  0.0519  51  ILE C N   
4510 C CA  . ILE C 53  ? 0.7438 0.5546 0.8134 0.0537  0.0067  0.0569  51  ILE C CA  
4511 C C   . ILE C 53  ? 0.6839 0.5267 0.7746 0.0420  -0.0016 0.0669  51  ILE C C   
4512 O O   . ILE C 53  ? 0.6723 0.5294 0.7615 0.0335  -0.0067 0.0636  51  ILE C O   
4513 C CB  . ILE C 53  ? 0.7426 0.5254 0.7915 0.0429  -0.0013 0.0449  51  ILE C CB  
4514 C CG1 . ILE C 53  ? 0.7600 0.5151 0.8049 0.0437  -0.0026 0.0501  51  ILE C CG1 
4515 C CG2 . ILE C 53  ? 0.7443 0.5499 0.7978 0.0257  -0.0128 0.0409  51  ILE C CG2 
4516 C CD1 . ILE C 53  ? 0.6738 0.4045 0.6991 0.0248  -0.0117 0.0410  51  ILE C CD1 
4517 N N   . TRP C 54  ? 0.6985 0.5481 0.8044 0.0434  -0.0039 0.0789  52  TRP C N   
4518 C CA  . TRP C 54  ? 0.6760 0.5530 0.7970 0.0319  -0.0128 0.0883  52  TRP C CA  
4519 C C   . TRP C 54  ? 0.6576 0.5311 0.7678 0.0161  -0.0215 0.0811  52  TRP C C   
4520 O O   . TRP C 54  ? 0.6840 0.5354 0.7805 0.0120  -0.0219 0.0740  52  TRP C O   
4521 C CB  . TRP C 54  ? 0.6583 0.5444 0.7963 0.0400  -0.0138 0.1046  52  TRP C CB  
4522 C CG  . TRP C 54  ? 0.6367 0.5516 0.7879 0.0282  -0.0240 0.1155  52  TRP C CG  
4523 C CD1 . TRP C 54  ? 0.5666 0.4796 0.7169 0.0225  -0.0321 0.1251  52  TRP C CD1 
4524 C CD2 . TRP C 54  ? 0.6270 0.5718 0.7880 0.0190  -0.0280 0.1180  52  TRP C CD2 
4525 N NE1 . TRP C 54  ? 0.5646 0.5072 0.7239 0.0119  -0.0407 0.1323  52  TRP C NE1 
4526 C CE2 . TRP C 54  ? 0.6103 0.5708 0.7758 0.0090  -0.0390 0.1274  52  TRP C CE2 
4527 C CE3 . TRP C 54  ? 0.6582 0.6128 0.8195 0.0159  -0.0244 0.1138  52  TRP C CE3 
4528 C CZ2 . TRP C 54  ? 0.5400 0.5243 0.7097 -0.0035 -0.0471 0.1306  52  TRP C CZ2 
4529 C CZ3 . TRP C 54  ? 0.5883 0.5635 0.7536 0.0018  -0.0326 0.1184  52  TRP C CZ3 
4530 C CH2 . TRP C 54  ? 0.5591 0.5483 0.7283 -0.0075 -0.0442 0.1257  52  TRP C CH2 
4531 N N   . TRP C 55  ? 0.6227 0.5198 0.7376 0.0062  -0.0285 0.0824  53  TRP C N   
4532 C CA  . TRP C 55  ? 0.6140 0.5184 0.7200 -0.0056 -0.0344 0.0734  53  TRP C CA  
4533 C C   . TRP C 55  ? 0.6771 0.5755 0.7804 -0.0158 -0.0360 0.0792  53  TRP C C   
4534 O O   . TRP C 55  ? 0.6709 0.5760 0.7672 -0.0272 -0.0379 0.0709  53  TRP C O   
4535 C CB  . TRP C 55  ? 0.6270 0.5533 0.7334 -0.0104 -0.0406 0.0726  53  TRP C CB  
4536 C CG  . TRP C 55  ? 0.6009 0.5413 0.7140 -0.0174 -0.0452 0.0857  53  TRP C CG  
4537 C CD1 . TRP C 55  ? 0.5684 0.5173 0.6927 -0.0161 -0.0478 0.0983  53  TRP C CD1 
4538 C CD2 . TRP C 55  ? 0.5945 0.5463 0.7024 -0.0284 -0.0485 0.0880  53  TRP C CD2 
4539 N NE1 . TRP C 55  ? 0.6820 0.6435 0.8066 -0.0241 -0.0544 0.1082  53  TRP C NE1 
4540 C CE2 . TRP C 55  ? 0.6620 0.6232 0.7744 -0.0319 -0.0539 0.1023  53  TRP C CE2 
4541 C CE3 . TRP C 55  ? 0.5829 0.5426 0.6829 -0.0373 -0.0472 0.0802  53  TRP C CE3 
4542 C CZ2 . TRP C 55  ? 0.6137 0.5856 0.7179 -0.0430 -0.0579 0.1091  53  TRP C CZ2 
4543 C CZ3 . TRP C 55  ? 0.6066 0.5812 0.7011 -0.0499 -0.0490 0.0872  53  TRP C CZ3 
4544 C CH2 . TRP C 55  ? 0.6119 0.5893 0.7060 -0.0522 -0.0542 0.1015  53  TRP C CH2 
4545 N N   . THR C 56  ? 0.6834 0.5705 0.7914 -0.0123 -0.0357 0.0941  54  THR C N   
4546 C CA  . THR C 56  ? 0.7064 0.5745 0.8040 -0.0228 -0.0380 0.1018  54  THR C CA  
4547 C C   . THR C 56  ? 0.7566 0.5830 0.8394 -0.0196 -0.0346 0.0971  54  THR C C   
4548 O O   . THR C 56  ? 0.7901 0.5916 0.8573 -0.0333 -0.0375 0.1018  54  THR C O   
4549 C CB  . THR C 56  ? 0.6796 0.5470 0.7824 -0.0185 -0.0423 0.1213  54  THR C CB  
4550 O OG1 . THR C 56  ? 0.6789 0.5349 0.7919 0.0038  -0.0389 0.1274  54  THR C OG1 
4551 C CG2 . THR C 56  ? 0.6461 0.5510 0.7577 -0.0247 -0.0478 0.1253  54  THR C CG2 
4552 N N   . GLY C 57  ? 0.6798 0.4947 0.7625 -0.0041 -0.0287 0.0881  55  GLY C N   
4553 C CA  . GLY C 57  ? 0.6944 0.4651 0.7571 0.0006  -0.0256 0.0811  55  GLY C CA  
4554 C C   . GLY C 57  ? 0.7649 0.4975 0.8196 0.0173  -0.0237 0.0923  55  GLY C C   
4555 O O   . GLY C 57  ? 0.8334 0.5161 0.8621 0.0160  -0.0244 0.0882  55  GLY C O   
4556 N N   . THR C 58  ? 0.7602 0.5135 0.8349 0.0336  -0.0226 0.1060  56  THR C N   
4557 C CA  . THR C 58  ? 0.7350 0.4584 0.8052 0.0558  -0.0221 0.1178  56  THR C CA  
4558 C C   . THR C 58  ? 0.7409 0.4757 0.8251 0.0869  -0.0111 0.1160  56  THR C C   
4559 O O   . THR C 58  ? 0.7425 0.4434 0.8160 0.1119  -0.0079 0.1191  56  THR C O   
4560 C CB  . THR C 58  ? 0.7527 0.4955 0.8355 0.0534  -0.0312 0.1377  56  THR C CB  
4561 O OG1 . THR C 58  ? 0.7065 0.5072 0.8212 0.0583  -0.0304 0.1424  56  THR C OG1 
4562 C CG2 . THR C 58  ? 0.7786 0.5190 0.8473 0.0213  -0.0395 0.1404  56  THR C CG2 
4563 N N   . THR C 59  ? 0.7372 0.5178 0.8424 0.0864  -0.0050 0.1114  57  THR C N   
4564 C CA  . THR C 59  ? 0.7291 0.5322 0.8499 0.1108  0.0075  0.1111  57  THR C CA  
4565 C C   . THR C 59  ? 0.7665 0.5661 0.8738 0.1061  0.0164  0.0944  57  THR C C   
4566 O O   . THR C 59  ? 0.6911 0.5069 0.7984 0.0851  0.0119  0.0891  57  THR C O   
4567 C CB  . THR C 59  ? 0.7174 0.5822 0.8749 0.1107  0.0057  0.1254  57  THR C CB  
4568 O OG1 . THR C 59  ? 0.7808 0.6502 0.9461 0.1067  -0.0074 0.1404  57  THR C OG1 
4569 C CG2 . THR C 59  ? 0.7078 0.6023 0.8862 0.1387  0.0187  0.1299  57  THR C CG2 
4570 N N   . THR C 60  ? 0.8748 0.6504 0.9667 0.1280  0.0286  0.0858  58  THR C N   
4571 C CA  . THR C 60  ? 0.7666 0.5374 0.8411 0.1269  0.0381  0.0712  58  THR C CA  
4572 C C   . THR C 60  ? 0.7673 0.5785 0.8604 0.1462  0.0545  0.0758  58  THR C C   
4573 O O   . THR C 60  ? 0.7586 0.5810 0.8657 0.1724  0.0624  0.0829  58  THR C O   
4574 C CB  . THR C 60  ? 0.7878 0.4960 0.8209 0.1332  0.0396  0.0551  58  THR C CB  
4575 O OG1 . THR C 60  ? 0.9387 0.6164 0.9636 0.1617  0.0453  0.0576  58  THR C OG1 
4576 C CG2 . THR C 60  ? 0.7418 0.4206 0.7579 0.1058  0.0237  0.0501  58  THR C CG2 
4577 N N   . TYR C 61  ? 0.7453 0.5797 0.8374 0.1335  0.0594  0.0724  59  TYR C N   
4578 C CA  . TYR C 61  ? 0.6682 0.5468 0.7765 0.1428  0.0755  0.0785  59  TYR C CA  
4579 C C   . TYR C 61  ? 0.7710 0.6260 0.8447 0.1482  0.0883  0.0642  59  TYR C C   
4580 O O   . TYR C 61  ? 0.7994 0.6226 0.8447 0.1326  0.0800  0.0533  59  TYR C O   
4581 C CB  . TYR C 61  ? 0.6545 0.5788 0.7868 0.1181  0.0692  0.0906  59  TYR C CB  
4582 C CG  . TYR C 61  ? 0.6893 0.6341 0.8489 0.1079  0.0537  0.1030  59  TYR C CG  
4583 C CD1 . TYR C 61  ? 0.7122 0.6260 0.8601 0.0961  0.0380  0.0988  59  TYR C CD1 
4584 C CD2 . TYR C 61  ? 0.7177 0.7174 0.9140 0.1089  0.0549  0.1192  59  TYR C CD2 
4585 C CE1 . TYR C 61  ? 0.7406 0.6724 0.9079 0.0868  0.0249  0.1100  59  TYR C CE1 
4586 C CE2 . TYR C 61  ? 0.7360 0.7531 0.9525 0.0992  0.0392  0.1303  59  TYR C CE2 
4587 C CZ  . TYR C 61  ? 0.7488 0.7293 0.9485 0.0888  0.0248  0.1255  59  TYR C CZ  
4588 O OH  . TYR C 61  ? 0.6937 0.6910 0.9084 0.0789  0.0103  0.1366  59  TYR C OH  
4589 N N   . TYR C 62  ? 0.7981 0.6725 0.8737 0.1717  0.1086  0.0642  60  TYR C N   
4590 C CA  . TYR C 62  ? 0.7904 0.6422 0.8283 0.1800  0.1232  0.0505  60  TYR C CA  
4591 C C   . TYR C 62  ? 0.8022 0.7117 0.8559 0.1838  0.1443  0.0597  60  TYR C C   
4592 O O   . TYR C 62  ? 0.7948 0.7612 0.8901 0.1923  0.1516  0.0739  60  TYR C O   
4593 C CB  . TYR C 62  ? 0.8625 0.6642 0.8705 0.2100  0.1302  0.0354  60  TYR C CB  
4594 C CG  . TYR C 62  ? 0.8807 0.6178 0.8624 0.2004  0.1105  0.0249  60  TYR C CG  
4595 C CD1 . TYR C 62  ? 0.9012 0.5984 0.8447 0.1818  0.1013  0.0106  60  TYR C CD1 
4596 C CD2 . TYR C 62  ? 0.8215 0.5399 0.8156 0.2084  0.1003  0.0304  60  TYR C CD2 
4597 C CE1 . TYR C 62  ? 0.9020 0.5495 0.8247 0.1687  0.0834  0.0019  60  TYR C CE1 
4598 C CE2 . TYR C 62  ? 0.8506 0.5117 0.8190 0.1942  0.0831  0.0226  60  TYR C CE2 
4599 C CZ  . TYR C 62  ? 0.8832 0.5126 0.8181 0.1731  0.0752  0.0082  60  TYR C CZ  
4600 O OH  . TYR C 62  ? 0.9326 0.5143 0.8453 0.1547  0.0581  0.0013  60  TYR C OH  
4601 N N   . ALA C 63  ? 0.8385 0.7358 0.8576 0.1757  0.1533  0.0525  61  ALA C N   
4602 C CA  . ALA C 63  ? 0.8297 0.7770 0.8540 0.1779  0.1767  0.0603  61  ALA C CA  
4603 C C   . ALA C 63  ? 0.8931 0.8423 0.9055 0.2165  0.2007  0.0497  61  ALA C C   
4604 O O   . ALA C 63  ? 0.9866 0.8772 0.9665 0.2370  0.1978  0.0323  61  ALA C O   
4605 C CB  . ALA C 63  ? 0.8225 0.7507 0.8076 0.1532  0.1762  0.0586  61  ALA C CB  
4606 N N   . ASP C 64  ? 0.8576 0.8755 0.8948 0.2261  0.2245  0.0601  62  ASP C N   
4607 C CA  . ASP C 64  ? 0.8951 0.9268 0.9269 0.2692  0.2498  0.0503  62  ASP C CA  
4608 C C   . ASP C 64  ? 0.8866 0.8593 0.8520 0.2803  0.2611  0.0290  62  ASP C C   
4609 O O   . ASP C 64  ? 0.9252 0.8662 0.8663 0.3185  0.2723  0.0122  62  ASP C O   
4610 C CB  . ASP C 64  ? 0.8970 1.0293 0.9731 0.2738  0.2745  0.0668  62  ASP C CB  
4611 C CG  . ASP C 64  ? 0.9021 1.0966 1.0415 0.2551  0.2605  0.0890  62  ASP C CG  
4612 O OD1 . ASP C 64  ? 0.9208 1.1061 1.0625 0.2137  0.2410  0.0988  62  ASP C OD1 
4613 O OD2 . ASP C 64  ? 0.8616 1.1128 1.0460 0.2837  0.2681  0.0959  62  ASP C OD2 
4614 N N   . SER C 65  ? 0.9284 0.8807 0.8591 0.2489  0.2567  0.0288  63  SER C N   
4615 C CA  . SER C 65  ? 0.9866 0.8832 0.8505 0.2562  0.2642  0.0093  63  SER C CA  
4616 C C   . SER C 65  ? 1.0437 0.8534 0.8704 0.2596  0.2405  -0.0102 63  SER C C   
4617 O O   . SER C 65  ? 1.1445 0.9023 0.9150 0.2734  0.2460  -0.0302 63  SER C O   
4618 C CB  . SER C 65  ? 0.9725 0.8742 0.8088 0.2216  0.2644  0.0178  63  SER C CB  
4619 O OG  . SER C 65  ? 0.9302 0.7967 0.7641 0.1908  0.2333  0.0217  63  SER C OG  
4620 N N   . VAL C 66  ? 1.0488 0.8432 0.9034 0.2454  0.2147  -0.0050 64  VAL C N   
4621 C CA  . VAL C 66  ? 1.0545 0.7756 0.8796 0.2411  0.1912  -0.0204 64  VAL C CA  
4622 C C   . VAL C 66  ? 1.0873 0.7914 0.9360 0.2611  0.1843  -0.0211 64  VAL C C   
4623 O O   . VAL C 66  ? 1.1313 0.7829 0.9657 0.2510  0.1630  -0.0286 64  VAL C O   
4624 C CB  . VAL C 66  ? 1.0870 0.7990 0.9142 0.2034  0.1651  -0.0149 64  VAL C CB  
4625 C CG1 . VAL C 66  ? 1.1260 0.8562 0.9322 0.1857  0.1709  -0.0093 64  VAL C CG1 
4626 C CG2 . VAL C 66  ? 1.0173 0.7675 0.9012 0.1901  0.1526  0.0031  64  VAL C CG2 
4627 N N   . LYS C 67  ? 1.0927 0.8424 0.9759 0.2896  0.2023  -0.0125 65  LYS C N   
4628 C CA  . LYS C 67  ? 1.0456 0.7860 0.9559 0.3090  0.1937  -0.0078 65  LYS C CA  
4629 C C   . LYS C 67  ? 1.0763 0.7247 0.9357 0.3265  0.1853  -0.0280 65  LYS C C   
4630 O O   . LYS C 67  ? 1.0958 0.7026 0.9556 0.3147  0.1633  -0.0264 65  LYS C O   
4631 C CB  . LYS C 67  ? 1.0150 0.8247 0.9674 0.3431  0.2157  0.0032  65  LYS C CB  
4632 C CG  . LYS C 67  ? 1.0347 0.8888 1.0460 0.3413  0.2030  0.0239  65  LYS C CG  
4633 C CD  . LYS C 67  ? 0.9572 0.8764 1.0088 0.3013  0.1964  0.0430  65  LYS C CD  
4634 C CE  . LYS C 67  ? 0.8957 0.8585 1.0015 0.2981  0.1823  0.0625  65  LYS C CE  
4635 N NZ  . LYS C 67  ? 0.7907 0.8333 0.9391 0.2691  0.1838  0.0812  65  LYS C NZ  
4636 N N   . GLY C 68  ? 1.0244 0.6375 0.8353 0.3526  0.2024  -0.0473 66  GLY C N   
4637 C CA  . GLY C 68  ? 1.1252 0.6451 0.8825 0.3725  0.1956  -0.0674 66  GLY C CA  
4638 C C   . GLY C 68  ? 1.2816 0.7294 0.9852 0.3400  0.1754  -0.0836 66  GLY C C   
4639 O O   . GLY C 68  ? 1.3429 0.7151 1.0150 0.3363  0.1578  -0.0931 66  GLY C O   
4640 N N   . ARG C 69  ? 1.3568 0.8274 1.0484 0.3148  0.1764  -0.0858 67  ARG C N   
4641 C CA  . ARG C 69  ? 1.4118 0.8214 1.0495 0.2886  0.1585  -0.1029 67  ARG C CA  
4642 C C   . ARG C 69  ? 1.3927 0.8119 1.0548 0.2452  0.1305  -0.0932 67  ARG C C   
4643 O O   . ARG C 69  ? 1.4516 0.8217 1.0764 0.2225  0.1109  -0.1064 67  ARG C O   
4644 C CB  . ARG C 69  ? 1.3821 0.8034 0.9822 0.2895  0.1737  -0.1125 67  ARG C CB  
4645 C CG  . ARG C 69  ? 1.3461 0.8162 0.9550 0.3247  0.2082  -0.1094 67  ARG C CG  
4646 C CD  . ARG C 69  ? 1.4535 0.9333 1.0199 0.3195  0.2224  -0.1168 67  ARG C CD  
4647 N NE  . ARG C 69  ? 1.3484 0.8554 0.9274 0.2793  0.2058  -0.1039 67  ARG C NE  
4648 C CZ  . ARG C 69  ? 1.2960 0.8725 0.9117 0.2672  0.2163  -0.0831 67  ARG C CZ  
4649 N NH1 . ARG C 69  ? 1.2493 0.8865 0.8989 0.2877  0.2436  -0.0716 67  ARG C NH1 
4650 N NH2 . ARG C 69  ? 1.4321 1.0174 1.0496 0.2337  0.1980  -0.0735 67  ARG C NH2 
4651 N N   . PHE C 70  ? 1.3190 0.8019 1.0410 0.2335  0.1280  -0.0715 68  PHE C N   
4652 C CA  . PHE C 70  ? 1.2256 0.7249 0.9711 0.1968  0.1044  -0.0630 68  PHE C CA  
4653 C C   . PHE C 70  ? 1.2530 0.7431 1.0278 0.1898  0.0902  -0.0538 68  PHE C C   
4654 O O   . PHE C 70  ? 1.3324 0.8235 1.1250 0.2137  0.0993  -0.0466 68  PHE C O   
4655 C CB  . PHE C 70  ? 1.2713 0.8400 1.0542 0.1852  0.1092  -0.0462 68  PHE C CB  
4656 C CG  . PHE C 70  ? 1.3519 0.9215 1.1009 0.1755  0.1110  -0.0527 68  PHE C CG  
4657 C CD1 . PHE C 70  ? 1.3463 0.8950 1.0508 0.1945  0.1292  -0.0652 68  PHE C CD1 
4658 C CD2 . PHE C 70  ? 1.3392 0.9290 1.0973 0.1499  0.0945  -0.0462 68  PHE C CD2 
4659 C CE1 . PHE C 70  ? 1.3197 0.8671 0.9881 0.1848  0.1300  -0.0695 68  PHE C CE1 
4660 C CE2 . PHE C 70  ? 1.3045 0.8905 1.0273 0.1430  0.0939  -0.0503 68  PHE C CE2 
4661 C CZ  . PHE C 70  ? 1.2966 0.8613 0.9741 0.1588  0.1113  -0.0611 68  PHE C CZ  
4662 N N   . THR C 71  ? 1.1108 0.5953 0.8899 0.1577  0.0678  -0.0533 69  THR C N   
4663 C CA  . THR C 71  ? 1.0258 0.5044 0.8291 0.1445  0.0537  -0.0435 69  THR C CA  
4664 C C   . THR C 71  ? 0.9775 0.4939 0.8056 0.1118  0.0366  -0.0375 69  THR C C   
4665 O O   . THR C 71  ? 0.9998 0.5048 0.8050 0.0925  0.0242  -0.0491 69  THR C O   
4666 C CB  . THR C 71  ? 1.0885 0.4893 0.8488 0.1417  0.0440  -0.0559 69  THR C CB  
4667 O OG1 . THR C 71  ? 1.2581 0.6184 0.9909 0.1787  0.0604  -0.0633 69  THR C OG1 
4668 C CG2 . THR C 71  ? 1.0301 0.4243 0.8117 0.1241  0.0299  -0.0429 69  THR C CG2 
4669 N N   . ILE C 72  ? 0.9315 0.4943 0.8049 0.1073  0.0352  -0.0204 70  ILE C N   
4670 C CA  . ILE C 72  ? 0.8629 0.4625 0.7601 0.0814  0.0205  -0.0152 70  ILE C CA  
4671 C C   . ILE C 72  ? 0.8900 0.4769 0.7960 0.0639  0.0080  -0.0099 70  ILE C C   
4672 O O   . ILE C 72  ? 0.9457 0.5108 0.8544 0.0748  0.0117  -0.0019 70  ILE C O   
4673 C CB  . ILE C 72  ? 0.8241 0.4799 0.7580 0.0850  0.0264  -0.0010 70  ILE C CB  
4674 C CG1 . ILE C 72  ? 0.7732 0.4596 0.7215 0.0635  0.0117  0.0000  70  ILE C CG1 
4675 C CG2 . ILE C 72  ? 0.7760 0.4497 0.7411 0.0962  0.0327  0.0148  70  ILE C CG2 
4676 C CD1 . ILE C 72  ? 0.7602 0.4888 0.7349 0.0645  0.0147  0.0120  70  ILE C CD1 
4677 N N   . SER C 73  ? 0.8448 0.4464 0.7535 0.0376  -0.0069 -0.0138 71  SER C N   
4678 C CA  . SER C 73  ? 0.8110 0.4085 0.7271 0.0151  -0.0180 -0.0080 71  SER C CA  
4679 C C   . SER C 73  ? 0.8646 0.5150 0.8035 -0.0056 -0.0287 -0.0082 71  SER C C   
4680 O O   . SER C 73  ? 0.8969 0.5744 0.8386 -0.0015 -0.0303 -0.0148 71  SER C O   
4681 C CB  . SER C 73  ? 0.8348 0.3710 0.7113 0.0013  -0.0254 -0.0182 71  SER C CB  
4682 O OG  . SER C 73  ? 0.9800 0.5065 0.8305 -0.0060 -0.0314 -0.0354 71  SER C OG  
4683 N N   . ARG C 74  ? 0.8853 0.5492 0.8377 -0.0264 -0.0357 -0.0005 72  ARG C N   
4684 C CA  . ARG C 74  ? 0.8800 0.5995 0.8552 -0.0433 -0.0440 -0.0013 72  ARG C CA  
4685 C C   . ARG C 74  ? 0.8828 0.6033 0.8567 -0.0743 -0.0522 0.0020  72  ARG C C   
4686 O O   . ARG C 74  ? 0.9702 0.6627 0.9390 -0.0800 -0.0499 0.0140  72  ARG C O   
4687 C CB  . ARG C 74  ? 0.8427 0.6035 0.8475 -0.0311 -0.0390 0.0094  72  ARG C CB  
4688 C CG  . ARG C 74  ? 0.8722 0.6877 0.8961 -0.0412 -0.0462 0.0060  72  ARG C CG  
4689 C CD  . ARG C 74  ? 0.9019 0.7452 0.9466 -0.0440 -0.0438 0.0184  72  ARG C CD  
4690 N NE  . ARG C 74  ? 0.8005 0.6899 0.8598 -0.0388 -0.0471 0.0133  72  ARG C NE  
4691 C CZ  . ARG C 74  ? 0.7659 0.6711 0.8360 -0.0293 -0.0446 0.0200  72  ARG C CZ  
4692 N NH1 . ARG C 74  ? 0.7368 0.6254 0.8104 -0.0254 -0.0394 0.0332  72  ARG C NH1 
4693 N NH2 . ARG C 74  ? 0.7423 0.6799 0.8179 -0.0225 -0.0488 0.0126  72  ARG C NH2 
4694 N N   . ASP C 75  ? 0.9322 0.6870 0.9099 -0.0947 -0.0621 -0.0076 73  ASP C N   
4695 C CA  . ASP C 75  ? 0.9866 0.7615 0.9690 -0.1293 -0.0690 -0.0038 73  ASP C CA  
4696 C C   . ASP C 75  ? 1.0069 0.8550 1.0240 -0.1296 -0.0675 0.0006  73  ASP C C   
4697 O O   . ASP C 75  ? 0.9706 0.8677 1.0033 -0.1214 -0.0716 -0.0095 73  ASP C O   
4698 C CB  . ASP C 75  ? 0.9360 0.7116 0.9029 -0.1540 -0.0815 -0.0174 73  ASP C CB  
4699 C CG  . ASP C 75  ? 1.0000 0.8077 0.9750 -0.1954 -0.0883 -0.0126 73  ASP C CG  
4700 O OD1 . ASP C 75  ? 0.9965 0.7997 0.9752 -0.2071 -0.0827 0.0024  73  ASP C OD1 
4701 O OD2 . ASP C 75  ? 1.0419 0.8829 1.0191 -0.2177 -0.0996 -0.0230 73  ASP C OD2 
4702 N N   . ASP C 76  ? 1.1110 0.9634 1.1361 -0.1369 -0.0621 0.0153  74  ASP C N   
4703 C CA  . ASP C 76  ? 1.0144 0.9301 1.0661 -0.1352 -0.0590 0.0189  74  ASP C CA  
4704 C C   . ASP C 76  ? 0.9715 0.9480 1.0370 -0.1629 -0.0635 0.0142  74  ASP C C   
4705 O O   . ASP C 76  ? 0.9751 1.0123 1.0623 -0.1567 -0.0606 0.0123  74  ASP C O   
4706 C CB  . ASP C 76  ? 0.9698 0.8697 1.0211 -0.1348 -0.0527 0.0366  74  ASP C CB  
4707 C CG  . ASP C 76  ? 1.0107 0.8562 1.0514 -0.1101 -0.0488 0.0431  74  ASP C CG  
4708 O OD1 . ASP C 76  ? 1.0517 0.8419 1.0702 -0.1108 -0.0499 0.0427  74  ASP C OD1 
4709 O OD2 . ASP C 76  ? 1.0455 0.9053 1.0992 -0.0898 -0.0447 0.0479  74  ASP C OD2 
4710 N N   . VAL C 77  ? 0.9874 0.9510 1.0399 -0.1933 -0.0706 0.0115  75  VAL C N   
4711 C CA  . VAL C 77  ? 0.9618 0.9950 1.0319 -0.2226 -0.0752 0.0071  75  VAL C CA  
4712 C C   . VAL C 77  ? 0.9037 0.9905 0.9926 -0.2044 -0.0825 -0.0106 75  VAL C C   
4713 O O   . VAL C 77  ? 0.8505 1.0162 0.9674 -0.1999 -0.0816 -0.0156 75  VAL C O   
4714 C CB  . VAL C 77  ? 0.9945 0.9933 1.0414 -0.2674 -0.0824 0.0114  75  VAL C CB  
4715 C CG1 . VAL C 77  ? 0.9289 1.0113 0.9985 -0.3044 -0.0853 0.0107  75  VAL C CG1 
4716 C CG2 . VAL C 77  ? 1.0289 0.9549 1.0479 -0.2783 -0.0775 0.0295  75  VAL C CG2 
4717 N N   . LYS C 78  ? 0.8968 0.9411 0.9678 -0.1912 -0.0899 -0.0204 76  LYS C N   
4718 C CA  . LYS C 78  ? 0.8678 0.9514 0.9494 -0.1706 -0.0990 -0.0355 76  LYS C CA  
4719 C C   . LYS C 78  ? 0.8660 0.9389 0.9488 -0.1269 -0.0940 -0.0376 76  LYS C C   
4720 O O   . LYS C 78  ? 0.8955 0.9961 0.9833 -0.1056 -0.1019 -0.0484 76  LYS C O   
4721 C CB  . LYS C 78  ? 0.8957 0.9388 0.9510 -0.1823 -0.1113 -0.0452 76  LYS C CB  
4722 C CG  . LYS C 78  ? 0.9241 1.0121 0.9866 -0.2229 -0.1243 -0.0503 76  LYS C CG  
4723 C CD  . LYS C 78  ? 0.8978 0.9384 0.9276 -0.2345 -0.1385 -0.0614 76  LYS C CD  
4724 C CE  . LYS C 78  ? 0.8381 0.7897 0.8281 -0.2624 -0.1370 -0.0557 76  LYS C CE  
4725 N NZ  . LYS C 78  ? 0.7763 0.6786 0.7281 -0.2763 -0.1517 -0.0689 76  LYS C NZ  
4726 N N   . ASN C 79  ? 0.8739 0.9070 0.9505 -0.1146 -0.0826 -0.0267 77  ASN C N   
4727 C CA  . ASN C 79  ? 0.8612 0.8817 0.9373 -0.0800 -0.0778 -0.0264 77  ASN C CA  
4728 C C   . ASN C 79  ? 0.9016 0.8880 0.9577 -0.0615 -0.0832 -0.0349 77  ASN C C   
4729 O O   . ASN C 79  ? 0.9276 0.9323 0.9845 -0.0393 -0.0885 -0.0419 77  ASN C O   
4730 C CB  . ASN C 79  ? 0.7868 0.8680 0.8843 -0.0649 -0.0782 -0.0306 77  ASN C CB  
4731 C CG  . ASN C 79  ? 0.7726 0.8777 0.8829 -0.0769 -0.0693 -0.0207 77  ASN C CG  
4732 O OD1 . ASN C 79  ? 0.7590 0.8262 0.8616 -0.0774 -0.0620 -0.0088 77  ASN C OD1 
4733 N ND2 . ASN C 79  ? 0.7069 0.8799 0.8367 -0.0858 -0.0697 -0.0254 77  ASN C ND2 
4734 N N   . MET C 80  ? 0.9896 0.9215 1.0226 -0.0698 -0.0817 -0.0340 78  MET C N   
4735 C CA  . MET C 80  ? 0.9683 0.8648 0.9760 -0.0557 -0.0851 -0.0421 78  MET C CA  
4736 C C   . MET C 80  ? 0.9634 0.7986 0.9515 -0.0468 -0.0728 -0.0353 78  MET C C   
4737 O O   . MET C 80  ? 1.0522 0.8580 1.0348 -0.0602 -0.0683 -0.0293 78  MET C O   
4738 C CB  . MET C 80  ? 1.0375 0.9360 1.0312 -0.0757 -0.0985 -0.0537 78  MET C CB  
4739 C CG  . MET C 80  ? 0.9633 0.9293 0.9761 -0.0760 -0.1126 -0.0626 78  MET C CG  
4740 S SD  . MET C 80  ? 1.0931 1.0611 1.0861 -0.0975 -0.1317 -0.0766 78  MET C SD  
4741 C CE  . MET C 80  ? 1.0134 0.9019 0.9596 -0.0764 -0.1279 -0.0808 78  MET C CE  
4742 N N   . VAL C 81  ? 0.8417 0.6587 0.8181 -0.0237 -0.0675 -0.0355 79  VAL C N   
4743 C CA  . VAL C 81  ? 0.8319 0.6039 0.7936 -0.0112 -0.0539 -0.0295 79  VAL C CA  
4744 C C   . VAL C 81  ? 0.8733 0.6071 0.7993 -0.0070 -0.0548 -0.0407 79  VAL C C   
4745 O O   . VAL C 81  ? 0.8809 0.6249 0.7940 -0.0033 -0.0638 -0.0493 79  VAL C O   
4746 C CB  . VAL C 81  ? 0.8391 0.6222 0.8126 0.0074  -0.0451 -0.0200 79  VAL C CB  
4747 C CG1 . VAL C 81  ? 0.8448 0.5947 0.8072 0.0208  -0.0301 -0.0141 79  VAL C CG1 
4748 C CG2 . VAL C 81  ? 0.8554 0.6704 0.8580 0.0024  -0.0451 -0.0104 79  VAL C CG2 
4749 N N   . TYR C 82  ? 0.8871 0.5745 0.7936 -0.0055 -0.0464 -0.0410 80  TYR C N   
4750 C CA  . TYR C 82  ? 0.8877 0.5314 0.7534 -0.0014 -0.0461 -0.0536 80  TYR C CA  
4751 C C   . TYR C 82  ? 0.8917 0.5088 0.7447 0.0239  -0.0269 -0.0498 80  TYR C C   
4752 O O   . TYR C 82  ? 0.8988 0.5230 0.7745 0.0344  -0.0154 -0.0372 80  TYR C O   
4753 C CB  . TYR C 82  ? 0.9045 0.5083 0.7478 -0.0221 -0.0540 -0.0613 80  TYR C CB  
4754 C CG  . TYR C 82  ? 0.9091 0.5478 0.7678 -0.0524 -0.0718 -0.0639 80  TYR C CG  
4755 C CD1 . TYR C 82  ? 0.8963 0.5610 0.7477 -0.0621 -0.0871 -0.0754 80  TYR C CD1 
4756 C CD2 . TYR C 82  ? 0.9107 0.5616 0.7912 -0.0714 -0.0732 -0.0539 80  TYR C CD2 
4757 C CE1 . TYR C 82  ? 0.9251 0.6347 0.7961 -0.0892 -0.1027 -0.0776 80  TYR C CE1 
4758 C CE2 . TYR C 82  ? 0.8841 0.5765 0.7806 -0.1010 -0.0869 -0.0556 80  TYR C CE2 
4759 C CZ  . TYR C 82  ? 0.9083 0.6339 0.8027 -0.1094 -0.1013 -0.0678 80  TYR C CZ  
4760 O OH  . TYR C 82  ? 0.9613 0.7405 0.8769 -0.1382 -0.1144 -0.0693 80  TYR C OH  
4761 N N   . LEU C 83  ? 0.9449 0.5364 0.7614 0.0336  -0.0237 -0.0604 81  LEU C N   
4762 C CA  . LEU C 83  ? 0.9462 0.5164 0.7462 0.0577  -0.0032 -0.0590 81  LEU C CA  
4763 C C   . LEU C 83  ? 1.0412 0.5564 0.7891 0.0610  -0.0027 -0.0765 81  LEU C C   
4764 O O   . LEU C 83  ? 1.1090 0.6175 0.8255 0.0592  -0.0085 -0.0867 81  LEU C O   
4765 C CB  . LEU C 83  ? 0.9376 0.5388 0.7426 0.0678  0.0042  -0.0518 81  LEU C CB  
4766 C CG  . LEU C 83  ? 0.9444 0.5441 0.7449 0.0894  0.0283  -0.0455 81  LEU C CG  
4767 C CD1 . LEU C 83  ? 0.9004 0.5215 0.7420 0.0969  0.0385  -0.0313 81  LEU C CD1 
4768 C CD2 . LEU C 83  ? 0.9276 0.5493 0.7205 0.0914  0.0331  -0.0391 81  LEU C CD2 
4769 N N   . GLN C 84  ? 0.9948 0.4658 0.7286 0.0666  0.0027  -0.0802 82  GLN C N   
4770 C CA  . GLN C 84  ? 1.0572 0.4644 0.7347 0.0719  0.0035  -0.0987 82  GLN C CA  
4771 C C   . GLN C 84  ? 1.1260 0.5260 0.7818 0.1037  0.0272  -0.1018 82  GLN C C   
4772 O O   . GLN C 84  ? 1.1525 0.5634 0.8295 0.1274  0.0459  -0.0922 82  GLN C O   
4773 C CB  . GLN C 84  ? 1.1096 0.4623 0.7738 0.0684  0.0000  -0.1011 82  GLN C CB  
4774 C CG  . GLN C 84  ? 1.1290 0.4024 0.7269 0.0709  -0.0025 -0.1223 82  GLN C CG  
4775 C CD  . GLN C 84  ? 1.2171 0.4358 0.7942 0.1025  0.0136  -0.1241 82  GLN C CD  
4776 O OE1 . GLN C 84  ? 1.2450 0.4923 0.8450 0.1352  0.0350  -0.1153 82  GLN C OE1 
4777 N NE2 . GLN C 84  ? 1.2178 0.3577 0.7504 0.0927  0.0025  -0.1350 82  GLN C NE2 
4778 N N   . MET C 85  ? 1.1090 0.4956 0.7229 0.1040  0.0263  -0.1147 83  MET C N   
4779 C CA  . MET C 85  ? 1.1806 0.5666 0.7691 0.1304  0.0497  -0.1177 83  MET C CA  
4780 C C   . MET C 85  ? 1.2651 0.5804 0.7898 0.1442  0.0552  -0.1398 83  MET C C   
4781 O O   . MET C 85  ? 1.3206 0.5946 0.8028 0.1254  0.0361  -0.1559 83  MET C O   
4782 C CB  . MET C 85  ? 1.2559 0.6738 0.8349 0.1219  0.0457  -0.1149 83  MET C CB  
4783 C CG  . MET C 85  ? 1.1850 0.6644 0.8176 0.1141  0.0436  -0.0938 83  MET C CG  
4784 S SD  . MET C 85  ? 1.2048 0.7088 0.8159 0.1147  0.0484  -0.0868 83  MET C SD  
4785 C CE  . MET C 85  ? 1.1431 0.6258 0.7175 0.0953  0.0163  -0.1012 83  MET C CE  
4786 N N   . ASN C 86  ? 1.3086 0.6114 0.8258 0.1777  0.0807  -0.1413 84  ASN C N   
4787 C CA  . ASN C 86  ? 1.3902 0.6219 0.8432 0.1991  0.0896  -0.1637 84  ASN C CA  
4788 C C   . ASN C 86  ? 1.4019 0.6542 0.8345 0.2306  0.1201  -0.1668 84  ASN C C   
4789 O O   . ASN C 86  ? 1.3962 0.7161 0.8751 0.2413  0.1384  -0.1485 84  ASN C O   
4790 C CB  . ASN C 86  ? 1.3579 0.5475 0.8162 0.2156  0.0911  -0.1644 84  ASN C CB  
4791 C CG  . ASN C 86  ? 1.3285 0.4875 0.7928 0.1800  0.0613  -0.1631 84  ASN C CG  
4792 O OD1 . ASN C 86  ? 1.3685 0.5198 0.8172 0.1467  0.0400  -0.1694 84  ASN C OD1 
4793 N ND2 . ASN C 86  ? 1.3136 0.4586 0.8003 0.1864  0.0595  -0.1540 84  ASN C ND2 
4794 N N   . SER C 87  ? 1.4391 0.6371 0.8025 0.2419  0.1250  -0.1894 85  SER C N   
4795 C CA  . SER C 87  ? 1.4184 0.6343 0.7544 0.2712  0.1551  -0.1946 85  SER C CA  
4796 C C   . SER C 87  ? 1.4410 0.7248 0.7984 0.2616  0.1657  -0.1780 85  SER C C   
4797 O O   . SER C 87  ? 1.4290 0.7749 0.8264 0.2780  0.1907  -0.1619 85  SER C O   
4798 C CB  . SER C 87  ? 1.4205 0.6560 0.7848 0.3097  0.1796  -0.1901 85  SER C CB  
4799 O OG  . SER C 87  ? 1.5414 0.7277 0.9036 0.3101  0.1626  -0.1961 85  SER C OG  
4800 N N   . LEU C 88  ? 1.4913 0.7689 0.8258 0.2307  0.1429  -0.1796 86  LEU C N   
4801 C CA  . LEU C 88  ? 1.4234 0.7590 0.7768 0.2155  0.1447  -0.1608 86  LEU C CA  
4802 C C   . LEU C 88  ? 1.5061 0.8565 0.8207 0.2358  0.1765  -0.1626 86  LEU C C   
4803 O O   . LEU C 88  ? 1.5302 0.8334 0.7740 0.2447  0.1807  -0.1833 86  LEU C O   
4804 C CB  . LEU C 88  ? 1.4320 0.7521 0.7636 0.1836  0.1109  -0.1639 86  LEU C CB  
4805 C CG  . LEU C 88  ? 1.3181 0.6667 0.7093 0.1589  0.0843  -0.1501 86  LEU C CG  
4806 C CD1 . LEU C 88  ? 1.2183 0.6304 0.6740 0.1611  0.0976  -0.1245 86  LEU C CD1 
4807 C CD2 . LEU C 88  ? 1.4074 0.7196 0.8102 0.1535  0.0698  -0.1605 86  LEU C CD2 
4808 N N   . LYS C 89  ? 1.5049 0.9217 0.8638 0.2407  0.1986  -0.1407 87  LYS C N   
4809 C CA  . LYS C 89  ? 1.4401 0.8897 0.7756 0.2554  0.2321  -0.1363 87  LYS C CA  
4810 C C   . LYS C 89  ? 1.4391 0.9151 0.7645 0.2271  0.2252  -0.1180 87  LYS C C   
4811 O O   . LYS C 89  ? 1.4111 0.8918 0.7641 0.2018  0.1974  -0.1059 87  LYS C O   
4812 C CB  . LYS C 89  ? 1.4206 0.9328 0.8171 0.2775  0.2609  -0.1224 87  LYS C CB  
4813 C CG  . LYS C 89  ? 1.4458 0.9303 0.8329 0.3179  0.2772  -0.1420 87  LYS C CG  
4814 C CD  . LYS C 89  ? 1.3946 0.9404 0.8564 0.3376  0.2931  -0.1263 87  LYS C CD  
4815 C CE  . LYS C 89  ? 1.3734 1.0090 0.8669 0.3371  0.3232  -0.1054 87  LYS C CE  
4816 N NZ  . LYS C 89  ? 1.2828 0.9664 0.8039 0.3801  0.3562  -0.1069 87  LYS C NZ  
4817 N N   . PRO C 90  ? 1.4728 0.9640 0.7549 0.2316  0.2503  -0.1151 88  PRO C N   
4818 C CA  . PRO C 90  ? 1.4618 0.9617 0.7190 0.2039  0.2407  -0.0977 88  PRO C CA  
4819 C C   . PRO C 90  ? 1.3956 0.9477 0.7150 0.1819  0.2366  -0.0678 88  PRO C C   
4820 O O   . PRO C 90  ? 1.3788 0.9197 0.6835 0.1582  0.2146  -0.0553 88  PRO C O   
4821 C CB  . PRO C 90  ? 1.4068 0.9157 0.6051 0.2157  0.2752  -0.1005 88  PRO C CB  
4822 C CG  . PRO C 90  ? 1.4121 0.9579 0.6416 0.2475  0.3105  -0.1067 88  PRO C CG  
4823 C CD  . PRO C 90  ? 1.4606 0.9718 0.7210 0.2627  0.2916  -0.1236 88  PRO C CD  
4824 N N   . GLU C 91  ? 1.4029 1.0075 0.7883 0.1898  0.2543  -0.0566 89  GLU C N   
4825 C CA  . GLU C 91  ? 1.2752 0.9246 0.7172 0.1666  0.2478  -0.0298 89  GLU C CA  
4826 C C   . GLU C 91  ? 1.2763 0.9050 0.7541 0.1538  0.2110  -0.0293 89  GLU C C   
4827 O O   . GLU C 91  ? 1.3227 0.9795 0.8423 0.1350  0.2018  -0.0097 89  GLU C O   
4828 C CB  . GLU C 91  ? 1.2392 0.9581 0.7411 0.1781  0.2770  -0.0179 89  GLU C CB  
4829 C CG  . GLU C 91  ? 1.3628 1.1119 0.8389 0.2011  0.3174  -0.0237 89  GLU C CG  
4830 C CD  . GLU C 91  ? 1.3679 1.1002 0.8441 0.2419  0.3286  -0.0485 89  GLU C CD  
4831 O OE1 . GLU C 91  ? 1.4312 1.0975 0.8842 0.2483  0.3041  -0.0681 89  GLU C OE1 
4832 O OE2 . GLU C 91  ? 1.3647 1.1490 0.8616 0.2677  0.3617  -0.0484 89  GLU C OE2 
4833 N N   . ASP C 92  ? 1.2477 0.8291 0.7082 0.1619  0.1902  -0.0505 90  ASP C N   
4834 C CA  . ASP C 92  ? 1.2184 0.7858 0.7109 0.1493  0.1570  -0.0513 90  ASP C CA  
4835 C C   . ASP C 92  ? 1.2220 0.7625 0.6801 0.1310  0.1281  -0.0502 90  ASP C C   
4836 O O   . ASP C 92  ? 1.2195 0.7477 0.6950 0.1232  0.0997  -0.0556 90  ASP C O   
4837 C CB  . ASP C 92  ? 1.2728 0.8068 0.7670 0.1631  0.1485  -0.0729 90  ASP C CB  
4838 C CG  . ASP C 92  ? 1.2831 0.8374 0.8098 0.1868  0.1736  -0.0741 90  ASP C CG  
4839 O OD1 . ASP C 92  ? 1.2685 0.8750 0.8269 0.1912  0.1964  -0.0574 90  ASP C OD1 
4840 O OD2 . ASP C 92  ? 1.2621 0.7796 0.7811 0.2008  0.1694  -0.0912 90  ASP C OD2 
4841 N N   . THR C 93  ? 1.2430 0.7766 0.6522 0.1249  0.1346  -0.0426 91  THR C N   
4842 C CA  . THR C 93  ? 1.2002 0.7063 0.5714 0.1118  0.1062  -0.0398 91  THR C CA  
4843 C C   . THR C 93  ? 1.2268 0.7539 0.6311 0.0963  0.0963  -0.0164 91  THR C C   
4844 O O   . THR C 93  ? 1.2691 0.8096 0.6628 0.0868  0.1130  0.0025  91  THR C O   
4845 C CB  . THR C 93  ? 1.2614 0.7424 0.5561 0.1128  0.1163  -0.0416 91  THR C CB  
4846 O OG1 . THR C 93  ? 1.3121 0.8231 0.6050 0.1107  0.1504  -0.0249 91  THR C OG1 
4847 C CG2 . THR C 93  ? 1.3255 0.7752 0.5788 0.1278  0.1205  -0.0685 91  THR C CG2 
4848 N N   . ALA C 94  ? 1.2066 0.7353 0.6480 0.0926  0.0693  -0.0179 92  ALA C N   
4849 C CA  . ALA C 94  ? 1.1448 0.6865 0.6151 0.0809  0.0579  0.0008  92  ALA C CA  
4850 C C   . ALA C 94  ? 1.1169 0.6529 0.6078 0.0822  0.0244  -0.0074 92  ALA C C   
4851 O O   . ALA C 94  ? 1.0915 0.6207 0.5809 0.0879  0.0114  -0.0256 92  ALA C O   
4852 C CB  . ALA C 94  ? 1.0722 0.6538 0.5989 0.0765  0.0788  0.0130  92  ALA C CB  
4853 N N   . VAL C 95  ? 1.1133 0.6528 0.6214 0.0759  0.0107  0.0060  93  VAL C N   
4854 C CA  . VAL C 95  ? 1.0593 0.6046 0.5953 0.0797  -0.0173 -0.0004 93  VAL C CA  
4855 C C   . VAL C 95  ? 1.0448 0.6232 0.6447 0.0767  -0.0095 -0.0002 93  VAL C C   
4856 O O   . VAL C 95  ? 1.0555 0.6467 0.6774 0.0691  0.0033  0.0143  93  VAL C O   
4857 C CB  . VAL C 95  ? 1.0804 0.6047 0.5934 0.0797  -0.0374 0.0119  93  VAL C CB  
4858 C CG1 . VAL C 95  ? 1.1373 0.6761 0.6830 0.0883  -0.0635 0.0038  93  VAL C CG1 
4859 C CG2 . VAL C 95  ? 1.0914 0.5796 0.5362 0.0836  -0.0472 0.0134  93  VAL C CG2 
4860 N N   . TYR C 96  ? 1.0057 0.5974 0.6329 0.0802  -0.0179 -0.0152 94  TYR C N   
4861 C CA  . TYR C 96  ? 1.0291 0.6479 0.7105 0.0775  -0.0101 -0.0153 94  TYR C CA  
4862 C C   . TYR C 96  ? 0.9856 0.6224 0.6991 0.0759  -0.0303 -0.0143 94  TYR C C   
4863 O O   . TYR C 96  ? 1.0028 0.6436 0.7145 0.0787  -0.0510 -0.0251 94  TYR C O   
4864 C CB  . TYR C 96  ? 0.9938 0.6093 0.6799 0.0798  -0.0059 -0.0308 94  TYR C CB  
4865 C CG  . TYR C 96  ? 0.9610 0.5650 0.6287 0.0864  0.0205  -0.0317 94  TYR C CG  
4866 C CD1 . TYR C 96  ? 1.0468 0.6314 0.6649 0.0900  0.0301  -0.0312 94  TYR C CD1 
4867 C CD2 . TYR C 96  ? 0.9412 0.5549 0.6392 0.0915  0.0362  -0.0327 94  TYR C CD2 
4868 C CE1 . TYR C 96  ? 1.0680 0.6481 0.6690 0.0990  0.0568  -0.0333 94  TYR C CE1 
4869 C CE2 . TYR C 96  ? 1.0318 0.6387 0.7137 0.1037  0.0611  -0.0348 94  TYR C CE2 
4870 C CZ  . TYR C 96  ? 1.0508 0.6437 0.6853 0.1077  0.0725  -0.0358 94  TYR C CZ  
4871 O OH  . TYR C 96  ? 1.0179 0.6098 0.6361 0.1226  0.0997  -0.0392 94  TYR C OH  
4872 N N   . TYR C 97  ? 0.9747 0.6257 0.7167 0.0713  -0.0241 -0.0018 95  TYR C N   
4873 C CA  . TYR C 97  ? 0.9656 0.6322 0.7350 0.0712  -0.0398 -0.0011 95  TYR C CA  
4874 C C   . TYR C 97  ? 0.8997 0.5949 0.7168 0.0663  -0.0330 -0.0021 95  TYR C C   
4875 O O   . TYR C 97  ? 0.8554 0.5567 0.6869 0.0634  -0.0149 0.0027  95  TYR C O   
4876 C CB  . TYR C 97  ? 0.9329 0.5860 0.6915 0.0676  -0.0413 0.0133  95  TYR C CB  
4877 C CG  . TYR C 97  ? 1.0475 0.6636 0.7526 0.0705  -0.0483 0.0187  95  TYR C CG  
4878 C CD1 . TYR C 97  ? 1.0903 0.6891 0.7721 0.0833  -0.0725 0.0135  95  TYR C CD1 
4879 C CD2 . TYR C 97  ? 1.0384 0.6387 0.7153 0.0616  -0.0308 0.0300  95  TYR C CD2 
4880 C CE1 . TYR C 97  ? 1.0803 0.6390 0.7080 0.0874  -0.0811 0.0202  95  TYR C CE1 
4881 C CE2 . TYR C 97  ? 1.0819 0.6443 0.7042 0.0616  -0.0373 0.0372  95  TYR C CE2 
4882 C CZ  . TYR C 97  ? 1.0953 0.6329 0.6913 0.0747  -0.0636 0.0328  95  TYR C CZ  
4883 O OH  . TYR C 97  ? 1.1448 0.6386 0.6813 0.0763  -0.0723 0.0416  95  TYR C OH  
4884 N N   . CYS C 98  ? 0.9709 0.6855 0.8114 0.0670  -0.0476 -0.0077 96  CYS C N   
4885 C CA  . CYS C 98  ? 0.9784 0.7186 0.8598 0.0607  -0.0432 -0.0059 96  CYS C CA  
4886 C C   . CYS C 98  ? 0.9627 0.7118 0.8562 0.0605  -0.0497 0.0006  96  CYS C C   
4887 O O   . CYS C 98  ? 1.0198 0.7641 0.8987 0.0689  -0.0648 -0.0039 96  CYS C O   
4888 C CB  . CYS C 98  ? 0.9583 0.7165 0.8554 0.0573  -0.0523 -0.0181 96  CYS C CB  
4889 S SG  . CYS C 98  ? 1.2152 0.9995 1.1161 0.0633  -0.0753 -0.0284 96  CYS C SG  
4890 N N   . ALA C 99  ? 0.7989 0.5589 0.7160 0.0528  -0.0395 0.0108  97  ALA C N   
4891 C CA  . ALA C 99  ? 0.7975 0.5611 0.7217 0.0496  -0.0453 0.0169  97  ALA C CA  
4892 C C   . ALA C 99  ? 0.8187 0.6115 0.7774 0.0449  -0.0454 0.0162  97  ALA C C   
4893 O O   . ALA C 99  ? 0.8048 0.6109 0.7824 0.0417  -0.0384 0.0156  97  ALA C O   
4894 C CB  . ALA C 99  ? 0.7927 0.5447 0.7096 0.0397  -0.0355 0.0317  97  ALA C CB  
4895 N N   . ALA C 100 ? 0.8876 0.6847 0.8487 0.0447  -0.0540 0.0162  98  ALA C N   
4896 C CA  . ALA C 100 ? 0.7743 0.5989 0.7622 0.0398  -0.0546 0.0159  98  ALA C CA  
4897 C C   . ALA C 100 ? 0.7280 0.5473 0.7137 0.0335  -0.0577 0.0230  98  ALA C C   
4898 O O   . ALA C 100 ? 0.7749 0.5665 0.7339 0.0358  -0.0646 0.0231  98  ALA C O   
4899 C CB  . ALA C 100 ? 0.7160 0.5617 0.7078 0.0478  -0.0642 0.0022  98  ALA C CB  
4900 N N   . LYS C 101 ? 0.7189 0.5602 0.7285 0.0244  -0.0541 0.0294  99  LYS C N   
4901 C CA  . LYS C 101 ? 0.7332 0.5729 0.7406 0.0159  -0.0591 0.0350  99  LYS C CA  
4902 C C   . LYS C 101 ? 0.6915 0.5597 0.7190 0.0122  -0.0597 0.0346  99  LYS C C   
4903 O O   . LYS C 101 ? 0.6671 0.5535 0.7165 0.0086  -0.0527 0.0404  99  LYS C O   
4904 C CB  . LYS C 101 ? 0.6865 0.5237 0.7000 0.0023  -0.0530 0.0506  99  LYS C CB  
4905 C CG  . LYS C 101 ? 0.6765 0.5110 0.6851 -0.0117 -0.0610 0.0569  99  LYS C CG  
4906 C CD  . LYS C 101 ? 0.6632 0.4604 0.6336 -0.0077 -0.0739 0.0463  99  LYS C CD  
4907 C CE  . LYS C 101 ? 0.5995 0.3831 0.5564 -0.0255 -0.0831 0.0521  99  LYS C CE  
4908 N NZ  . LYS C 101 ? 0.5794 0.3566 0.5351 -0.0463 -0.0800 0.0677  99  LYS C NZ  
4909 N N   . PHE C 102 ? 0.7031 0.5706 0.7180 0.0138  -0.0681 0.0277  100 PHE C N   
4910 C CA  . PHE C 102 ? 0.6730 0.5679 0.7008 0.0091  -0.0682 0.0276  100 PHE C CA  
4911 C C   . PHE C 102 ? 0.6357 0.5410 0.6815 -0.0058 -0.0655 0.0443  100 PHE C C   
4912 O O   . PHE C 102 ? 0.6552 0.5494 0.6948 -0.0147 -0.0699 0.0516  100 PHE C O   
4913 C CB  . PHE C 102 ? 0.6393 0.5276 0.6436 0.0158  -0.0770 0.0158  100 PHE C CB  
4914 C CG  . PHE C 102 ? 0.6426 0.5625 0.6548 0.0127  -0.0754 0.0134  100 PHE C CG  
4915 C CD1 . PHE C 102 ? 0.6584 0.6090 0.6787 0.0211  -0.0714 0.0032  100 PHE C CD1 
4916 C CD2 . PHE C 102 ? 0.6413 0.5641 0.6521 -0.0007 -0.0782 0.0220  100 PHE C CD2 
4917 C CE1 . PHE C 102 ? 0.6269 0.6097 0.6521 0.0154  -0.0680 0.0023  100 PHE C CE1 
4918 C CE2 . PHE C 102 ? 0.6762 0.6266 0.6890 -0.0045 -0.0763 0.0208  100 PHE C CE2 
4919 C CZ  . PHE C 102 ? 0.6429 0.6229 0.6621 0.0031  -0.0701 0.0113  100 PHE C CZ  
4920 N N   . TYR C 103 ? 0.6004 0.5266 0.6670 -0.0091 -0.0598 0.0510  101 TYR C N   
4921 C CA  . TYR C 103 ? 0.6302 0.5681 0.7149 -0.0179 -0.0585 0.0678  101 TYR C CA  
4922 C C   . TYR C 103 ? 0.6301 0.5626 0.7248 -0.0178 -0.0543 0.0776  101 TYR C C   
4923 O O   . TYR C 103 ? 0.6568 0.6014 0.7617 -0.0261 -0.0575 0.0896  101 TYR C O   
4924 C CB  . TYR C 103 ? 0.6507 0.5983 0.7287 -0.0275 -0.0673 0.0715  101 TYR C CB  
4925 C CG  . TYR C 103 ? 0.6102 0.5741 0.6846 -0.0300 -0.0677 0.0687  101 TYR C CG  
4926 C CD1 . TYR C 103 ? 0.5977 0.5690 0.6780 -0.0272 -0.0608 0.0647  101 TYR C CD1 
4927 C CD2 . TYR C 103 ? 0.5763 0.5487 0.6387 -0.0380 -0.0750 0.0703  101 TYR C CD2 
4928 C CE1 . TYR C 103 ? 0.5909 0.5813 0.6672 -0.0340 -0.0597 0.0641  101 TYR C CE1 
4929 C CE2 . TYR C 103 ? 0.5627 0.5527 0.6187 -0.0415 -0.0734 0.0686  101 TYR C CE2 
4930 C CZ  . TYR C 103 ? 0.6225 0.6233 0.6865 -0.0403 -0.0649 0.0663  101 TYR C CZ  
4931 O OH  . TYR C 103 ? 0.6074 0.6300 0.6645 -0.0481 -0.0619 0.0665  101 TYR C OH  
4932 N N   . GLY C 104 ? 0.6670 0.5859 0.7585 -0.0094 -0.0471 0.0725  102 GLY C N   
4933 C CA  . GLY C 104 ? 0.6688 0.5859 0.7667 -0.0083 -0.0399 0.0803  102 GLY C CA  
4934 C C   . GLY C 104 ? 0.6975 0.6106 0.8033 0.0034  -0.0288 0.0800  102 GLY C C   
4935 O O   . GLY C 104 ? 0.6118 0.5254 0.7246 0.0071  -0.0278 0.0801  102 GLY C O   
4936 N N   . GLY C 105 ? 0.7156 0.6200 0.8147 0.0079  -0.0206 0.0796  103 GLY C N   
4937 C CA  . GLY C 105 ? 0.6999 0.5953 0.7991 0.0206  -0.0093 0.0772  103 GLY C CA  
4938 C C   . GLY C 105 ? 0.7438 0.6592 0.8645 0.0286  0.0019  0.0894  103 GLY C C   
4939 O O   . GLY C 105 ? 0.7091 0.6133 0.8286 0.0432  0.0110  0.0866  103 GLY C O   
4940 N N   . ASN C 106 ? 0.8485 0.7940 0.9878 0.0202  0.0009  0.1023  104 ASN C N   
4941 C CA  . ASN C 106 ? 0.8502 0.8292 1.0168 0.0295  0.0110  0.1150  104 ASN C CA  
4942 C C   . ASN C 106 ? 0.8019 0.8042 0.9716 0.0205  0.0200  0.1218  104 ASN C C   
4943 O O   . ASN C 106 ? 0.8010 0.8475 0.9995 0.0225  0.0268  0.1346  104 ASN C O   
4944 C CB  . ASN C 106 ? 0.8121 0.8197 1.0045 0.0261  0.0009  0.1276  104 ASN C CB  
4945 C CG  . ASN C 106 ? 0.7390 0.7576 0.9293 0.0018  -0.0129 0.1315  104 ASN C CG  
4946 O OD1 . ASN C 106 ? 0.7887 0.7836 0.9540 -0.0103 -0.0166 0.1229  104 ASN C OD1 
4947 N ND2 . ASN C 106 ? 0.7323 0.7828 0.9447 -0.0040 -0.0220 0.1441  104 ASN C ND2 
4948 N N   . SER C 107 ? 0.6692 0.6446 0.8091 0.0100  0.0197  0.1145  105 SER C N   
4949 C CA  . SER C 107 ? 0.6844 0.6738 0.8187 -0.0050 0.0267  0.1225  105 SER C CA  
4950 C C   . SER C 107 ? 0.7410 0.7124 0.8519 0.0060  0.0422  0.1158  105 SER C C   
4951 O O   . SER C 107 ? 0.7636 0.6968 0.8496 0.0176  0.0402  0.1018  105 SER C O   
4952 C CB  . SER C 107 ? 0.6975 0.6614 0.8068 -0.0289 0.0110  0.1221  105 SER C CB  
4953 O OG  . SER C 107 ? 0.7581 0.7420 0.8682 -0.0517 0.0143  0.1354  105 SER C OG  
4954 N N   . LYS C 108 ? 0.7114 0.7147 0.8298 0.0006  0.0576  0.1262  106 LYS C N   
4955 C CA  . LYS C 108 ? 0.6970 0.6871 0.7886 0.0077  0.0742  0.1218  106 LYS C CA  
4956 C C   . LYS C 108 ? 0.7204 0.6846 0.7755 -0.0172 0.0700  0.1261  106 LYS C C   
4957 O O   . LYS C 108 ? 0.7603 0.7196 0.7911 -0.0176 0.0845  0.1272  106 LYS C O   
4958 C CB  . LYS C 108 ? 0.6088 0.6539 0.7284 0.0202  0.0973  0.1303  106 LYS C CB  
4959 C CG  . LYS C 108 ? 0.6561 0.7263 0.8116 0.0471  0.0998  0.1291  106 LYS C CG  
4960 C CD  . LYS C 108 ? 0.6304 0.7258 0.7922 0.0756  0.1246  0.1265  106 LYS C CD  
4961 C CE  . LYS C 108 ? 0.6529 0.7662 0.8461 0.1061  0.1253  0.1264  106 LYS C CE  
4962 N NZ  . LYS C 108 ? 0.6330 0.6808 0.7975 0.1257  0.1188  0.1095  106 LYS C NZ  
4963 N N   . ARG C 109 ? 0.7488 0.6913 0.7942 -0.0370 0.0503  0.1284  107 ARG C N   
4964 C CA  . ARG C 109 ? 0.8254 0.7335 0.8313 -0.0608 0.0432  0.1339  107 ARG C CA  
4965 C C   . ARG C 109 ? 0.8721 0.7188 0.8400 -0.0528 0.0243  0.1196  107 ARG C C   
4966 O O   . ARG C 109 ? 0.8488 0.6905 0.8293 -0.0442 0.0110  0.1107  107 ARG C O   
4967 C CB  . ARG C 109 ? 0.7937 0.7233 0.8134 -0.0924 0.0347  0.1491  107 ARG C CB  
4968 C CG  . ARG C 109 ? 0.7506 0.7568 0.8246 -0.0954 0.0471  0.1616  107 ARG C CG  
4969 C CD  . ARG C 109 ? 0.8457 0.8766 0.9307 -0.1327 0.0372  0.1775  107 ARG C CD  
4970 N NE  . ARG C 109 ? 0.9060 1.0100 1.0249 -0.1462 0.0558  0.1943  107 ARG C NE  
4971 C CZ  . ARG C 109 ? 0.9052 1.0453 1.0374 -0.1841 0.0510  0.2111  107 ARG C CZ  
4972 N NH1 . ARG C 109 ? 0.9229 1.0241 1.0325 -0.2126 0.0271  0.2126  107 ARG C NH1 
4973 N NH2 . ARG C 109 ? 0.8357 1.0543 1.0037 -0.1940 0.0705  0.2261  107 ARG C NH2 
4974 N N   . PRO C 110 ? 0.8639 0.6668 0.7850 -0.0541 0.0226  0.1174  108 PRO C N   
4975 C CA  . PRO C 110 ? 0.8650 0.6159 0.7523 -0.0421 0.0032  0.1039  108 PRO C CA  
4976 C C   . PRO C 110 ? 0.8676 0.5916 0.7430 -0.0544 -0.0168 0.1045  108 PRO C C   
4977 O O   . PRO C 110 ? 0.8480 0.5442 0.7090 -0.0385 -0.0324 0.0910  108 PRO C O   
4978 C CB  . PRO C 110 ? 0.8343 0.5468 0.6718 -0.0424 0.0060  0.1058  108 PRO C CB  
4979 C CG  . PRO C 110 ? 0.8296 0.5800 0.6798 -0.0473 0.0313  0.1152  108 PRO C CG  
4980 C CD  . PRO C 110 ? 0.7898 0.5923 0.6863 -0.0633 0.0390  0.1271  108 PRO C CD  
4981 N N   . GLY C 111 ? 0.8544 0.5873 0.7339 -0.0821 -0.0172 0.1189  109 GLY C N   
4982 C CA  . GLY C 111 ? 0.8658 0.5652 0.7268 -0.0948 -0.0372 0.1179  109 GLY C CA  
4983 C C   . GLY C 111 ? 0.8222 0.5465 0.7166 -0.0835 -0.0450 0.1079  109 GLY C C   
4984 O O   . GLY C 111 ? 0.7835 0.4741 0.6565 -0.0808 -0.0620 0.0990  109 GLY C O   
4985 N N   . ASP C 112 ? 0.7945 0.5748 0.7373 -0.0753 -0.0325 0.1092  110 ASP C N   
4986 C CA  . ASP C 112 ? 0.7836 0.5888 0.7566 -0.0666 -0.0386 0.1027  110 ASP C CA  
4987 C C   . ASP C 112 ? 0.7660 0.5603 0.7364 -0.0399 -0.0419 0.0855  110 ASP C C   
4988 O O   . ASP C 112 ? 0.6600 0.4798 0.6571 -0.0322 -0.0428 0.0814  110 ASP C O   
4989 C CB  . ASP C 112 ? 0.7129 0.5784 0.7353 -0.0688 -0.0259 0.1136  110 ASP C CB  
4990 C CG  . ASP C 112 ? 0.7731 0.6659 0.8095 -0.0975 -0.0285 0.1298  110 ASP C CG  
4991 O OD1 . ASP C 112 ? 0.9301 0.7961 0.9442 -0.1154 -0.0449 0.1293  110 ASP C OD1 
4992 O OD2 . ASP C 112 ? 0.7010 0.6433 0.7697 -0.1018 -0.0145 0.1423  110 ASP C OD2 
4993 N N   . TYR C 113 ? 0.7489 0.5086 0.6874 -0.0274 -0.0445 0.0768  111 TYR C N   
4994 C CA  . TYR C 113 ? 0.7213 0.4764 0.6572 -0.0050 -0.0498 0.0606  111 TYR C CA  
4995 C C   . TYR C 113 ? 0.7356 0.4469 0.6307 0.0038  -0.0661 0.0512  111 TYR C C   
4996 O O   . TYR C 113 ? 0.9243 0.5961 0.7828 -0.0020 -0.0700 0.0566  111 TYR C O   
4997 C CB  . TYR C 113 ? 0.7306 0.4920 0.6687 0.0065  -0.0387 0.0574  111 TYR C CB  
4998 C CG  . TYR C 113 ? 0.7776 0.5761 0.7528 0.0066  -0.0241 0.0623  111 TYR C CG  
4999 C CD1 . TYR C 113 ? 0.7381 0.5546 0.7358 0.0152  -0.0250 0.0548  111 TYR C CD1 
5000 C CD2 . TYR C 113 ? 0.7628 0.5781 0.7486 -0.0012 -0.0093 0.0750  111 TYR C CD2 
5001 C CE1 . TYR C 113 ? 0.6540 0.4928 0.6784 0.0178  -0.0136 0.0597  111 TYR C CE1 
5002 C CE2 . TYR C 113 ? 0.7210 0.5675 0.7383 0.0054  0.0034  0.0785  111 TYR C CE2 
5003 C CZ  . TYR C 113 ? 0.6644 0.5169 0.6983 0.0158  0.0002  0.0708  111 TYR C CZ  
5004 O OH  . TYR C 113 ? 0.6696 0.5420 0.7280 0.0247  0.0110  0.0748  111 TYR C OH  
5005 N N   . ALA C 114 ? 0.6978 0.4156 0.5970 0.0185  -0.0754 0.0378  112 ALA C N   
5006 C CA  . ALA C 114 ? 0.8064 0.4862 0.6689 0.0324  -0.0913 0.0273  112 ALA C CA  
5007 C C   . ALA C 114 ? 0.8486 0.5239 0.6979 0.0575  -0.0976 0.0150  112 ALA C C   
5008 O O   . ALA C 114 ? 0.8988 0.5307 0.7077 0.0707  -0.1101 0.0110  112 ALA C O   
5009 C CB  . ALA C 114 ? 0.7790 0.4724 0.6504 0.0354  -0.0977 0.0189  112 ALA C CB  
5010 N N   . TYR C 115 ? 0.7905 0.5073 0.6705 0.0637  -0.0909 0.0093  113 TYR C N   
5011 C CA  . TYR C 115 ? 0.7958 0.5209 0.6698 0.0848  -0.0989 -0.0032 113 TYR C CA  
5012 C C   . TYR C 115 ? 0.7820 0.5081 0.6554 0.0807  -0.0917 0.0005  113 TYR C C   
5013 O O   . TYR C 115 ? 0.7583 0.5086 0.6586 0.0685  -0.0788 0.0045  113 TYR C O   
5014 C CB  . TYR C 115 ? 0.7699 0.5450 0.6764 0.0923  -0.0995 -0.0149 113 TYR C CB  
5015 C CG  . TYR C 115 ? 0.8386 0.6146 0.7408 0.1002  -0.1056 -0.0213 113 TYR C CG  
5016 C CD1 . TYR C 115 ? 0.8336 0.5815 0.7029 0.1241  -0.1196 -0.0310 113 TYR C CD1 
5017 C CD2 . TYR C 115 ? 0.7759 0.5765 0.7018 0.0858  -0.0981 -0.0179 113 TYR C CD2 
5018 C CE1 . TYR C 115 ? 0.8896 0.6332 0.7488 0.1344  -0.1245 -0.0394 113 TYR C CE1 
5019 C CE2 . TYR C 115 ? 0.7656 0.5648 0.6818 0.0930  -0.1033 -0.0251 113 TYR C CE2 
5020 C CZ  . TYR C 115 ? 0.8553 0.6253 0.7375 0.1177  -0.1159 -0.0369 113 TYR C CZ  
5021 O OH  . TYR C 115 ? 0.9268 0.6905 0.7934 0.1280  -0.1206 -0.0466 113 TYR C OH  
5022 N N   . TRP C 116 ? 0.8421 0.5379 0.6805 0.0927  -0.1009 -0.0012 114 TRP C N   
5023 C CA  . TRP C 116 ? 0.8631 0.5533 0.6898 0.0906  -0.0960 0.0009  114 TRP C CA  
5024 C C   . TRP C 116 ? 0.8859 0.5895 0.7060 0.1099  -0.1107 -0.0124 114 TRP C C   
5025 O O   . TRP C 116 ? 0.8739 0.5879 0.6944 0.1282  -0.1249 -0.0217 114 TRP C O   
5026 C CB  . TRP C 116 ? 0.8789 0.5207 0.6636 0.0834  -0.0937 0.0139  114 TRP C CB  
5027 C CG  . TRP C 116 ? 0.8512 0.4907 0.6460 0.0609  -0.0789 0.0281  114 TRP C CG  
5028 C CD1 . TRP C 116 ? 0.8418 0.4718 0.6390 0.0514  -0.0819 0.0335  114 TRP C CD1 
5029 C CD2 . TRP C 116 ? 0.8335 0.4849 0.6378 0.0455  -0.0594 0.0383  114 TRP C CD2 
5030 N NE1 . TRP C 116 ? 0.8739 0.5143 0.6851 0.0285  -0.0668 0.0477  114 TRP C NE1 
5031 C CE2 . TRP C 116 ? 0.8646 0.5212 0.6823 0.0266  -0.0518 0.0509  114 TRP C CE2 
5032 C CE3 . TRP C 116 ? 0.8175 0.4768 0.6186 0.0472  -0.0477 0.0370  114 TRP C CE3 
5033 C CZ2 . TRP C 116 ? 0.8360 0.5143 0.6700 0.0114  -0.0324 0.0630  114 TRP C CZ2 
5034 C CZ3 . TRP C 116 ? 0.8619 0.5359 0.6744 0.0346  -0.0271 0.0476  114 TRP C CZ3 
5035 C CH2 . TRP C 116 ? 0.8271 0.5148 0.6588 0.0177  -0.0193 0.0609  114 TRP C CH2 
5036 N N   . GLY C 117 ? 0.9849 0.6907 0.7982 0.1066  -0.1075 -0.0140 115 GLY C N   
5037 C CA  . GLY C 117 ? 1.1342 0.8531 0.9379 0.1210  -0.1233 -0.0253 115 GLY C CA  
5038 C C   . GLY C 117 ? 1.1925 0.8725 0.9500 0.1236  -0.1266 -0.0207 115 GLY C C   
5039 O O   . GLY C 117 ? 1.1206 0.7661 0.8547 0.1129  -0.1141 -0.0085 115 GLY C O   
5040 N N   . GLN C 118 ? 1.4001 1.0909 1.1449 0.1369  -0.1439 -0.0302 116 GLN C N   
5041 C CA  . GLN C 118 ? 1.4848 1.1412 1.1820 0.1400  -0.1497 -0.0270 116 GLN C CA  
5042 C C   . GLN C 118 ? 1.5214 1.1817 1.2198 0.1219  -0.1343 -0.0297 116 GLN C C   
5043 O O   . GLN C 118 ? 1.5756 1.2710 1.3044 0.1143  -0.1341 -0.0405 116 GLN C O   
5044 C CB  . GLN C 118 ? 1.5796 1.2483 1.2615 0.1629  -0.1771 -0.0361 116 GLN C CB  
5045 C CG  . GLN C 118 ? 1.6120 1.3386 1.3274 0.1600  -0.1864 -0.0512 116 GLN C CG  
5046 C CD  . GLN C 118 ? 1.5693 1.3501 1.3405 0.1577  -0.1834 -0.0583 116 GLN C CD  
5047 O OE1 . GLN C 118 ? 1.5039 1.2810 1.2863 0.1659  -0.1792 -0.0544 116 GLN C OE1 
5048 N NE2 . GLN C 118 ? 1.5112 1.3402 1.3135 0.1440  -0.1859 -0.0686 116 GLN C NE2 
5049 N N   . GLY C 119 ? 1.2372 0.8596 0.8995 0.1145  -0.1206 -0.0198 117 GLY C N   
5050 C CA  . GLY C 119 ? 1.1747 0.7963 0.8345 0.1015  -0.1023 -0.0228 117 GLY C CA  
5051 C C   . GLY C 119 ? 1.2737 0.8971 0.9114 0.1036  -0.1152 -0.0363 117 GLY C C   
5052 O O   . GLY C 119 ? 1.3244 0.9543 0.9485 0.1148  -0.1396 -0.0420 117 GLY C O   
5053 N N   . THR C 120 ? 1.2486 0.8662 0.8818 0.0934  -0.0993 -0.0422 118 THR C N   
5054 C CA  . THR C 120 ? 1.2140 0.8219 0.8159 0.0911  -0.1085 -0.0557 118 THR C CA  
5055 C C   . THR C 120 ? 1.1891 0.7586 0.7396 0.0911  -0.0909 -0.0518 118 THR C C   
5056 O O   . THR C 120 ? 1.1839 0.7462 0.7392 0.0886  -0.0651 -0.0424 118 THR C O   
5057 C CB  . THR C 120 ? 1.1545 0.7797 0.7858 0.0788  -0.1062 -0.0692 118 THR C CB  
5058 O OG1 . THR C 120 ? 1.1541 0.7689 0.8002 0.0747  -0.0790 -0.0647 118 THR C OG1 
5059 C CG2 . THR C 120 ? 1.1461 0.8159 0.8267 0.0758  -0.1220 -0.0722 118 THR C CG2 
5060 N N   . GLN C 121 ? 1.1316 0.6817 0.6330 0.0939  -0.1052 -0.0590 119 GLN C N   
5061 C CA  . GLN C 121 ? 1.1622 0.6763 0.6060 0.0942  -0.0897 -0.0570 119 GLN C CA  
5062 C C   . GLN C 121 ? 1.2112 0.7155 0.6489 0.0887  -0.0732 -0.0723 119 GLN C C   
5063 O O   . GLN C 121 ? 1.2242 0.7228 0.6460 0.0840  -0.0896 -0.0891 119 GLN C O   
5064 C CB  . GLN C 121 ? 1.2750 0.7684 0.6620 0.1002  -0.1137 -0.0581 119 GLN C CB  
5065 C CG  . GLN C 121 ? 1.2564 0.7111 0.5759 0.1003  -0.0975 -0.0518 119 GLN C CG  
5066 C CD  . GLN C 121 ? 1.3061 0.7548 0.6290 0.0971  -0.0678 -0.0325 119 GLN C CD  
5067 O OE1 . GLN C 121 ? 1.2716 0.7342 0.6330 0.0963  -0.0684 -0.0200 119 GLN C OE1 
5068 N NE2 . GLN C 121 ? 1.3279 0.7590 0.6102 0.0941  -0.0417 -0.0304 119 GLN C NE2 
5069 N N   . VAL C 122 ? 1.2035 0.7043 0.6502 0.0898  -0.0418 -0.0667 120 VAL C N   
5070 C CA  . VAL C 122 ? 1.2613 0.7457 0.6966 0.0913  -0.0230 -0.0808 120 VAL C CA  
5071 C C   . VAL C 122 ? 1.2403 0.7020 0.6210 0.0982  0.0006  -0.0779 120 VAL C C   
5072 O O   . VAL C 122 ? 1.2377 0.7131 0.6271 0.1000  0.0226  -0.0611 120 VAL C O   
5073 C CB  . VAL C 122 ? 1.2067 0.7112 0.6988 0.0922  -0.0052 -0.0776 120 VAL C CB  
5074 C CG1 . VAL C 122 ? 1.2370 0.7160 0.7111 0.0990  0.0123  -0.0929 120 VAL C CG1 
5075 C CG2 . VAL C 122 ? 1.0909 0.6206 0.6339 0.0834  -0.0269 -0.0784 120 VAL C CG2 
5076 N N   . THR C 123 ? 1.2937 0.7231 0.6166 0.1000  -0.0038 -0.0943 121 THR C N   
5077 C CA  . THR C 123 ? 1.3850 0.7927 0.6489 0.1073  0.0199  -0.0943 121 THR C CA  
5078 C C   . THR C 123 ? 1.4083 0.7819 0.6333 0.1140  0.0275  -0.1193 121 THR C C   
5079 O O   . THR C 123 ? 1.4469 0.8003 0.6589 0.1066  0.0019  -0.1366 121 THR C O   
5080 C CB  . THR C 123 ? 1.3824 0.7747 0.5911 0.1034  0.0033  -0.0857 121 THR C CB  
5081 O OG1 . THR C 123 ? 1.3317 0.6978 0.4718 0.1087  0.0238  -0.0907 121 THR C OG1 
5082 C CG2 . THR C 123 ? 1.4176 0.8021 0.6163 0.0978  -0.0379 -0.0971 121 THR C CG2 
5083 N N   . VAL C 124 ? 1.3782 0.7465 0.5841 0.1279  0.0627  -0.1215 122 VAL C N   
5084 C CA  . VAL C 124 ? 1.5243 0.8531 0.6859 0.1399  0.0740  -0.1464 122 VAL C CA  
5085 C C   . VAL C 124 ? 1.5886 0.8906 0.6668 0.1444  0.0832  -0.1527 122 VAL C C   
5086 O O   . VAL C 124 ? 1.5632 0.8840 0.6250 0.1415  0.0935  -0.1340 122 VAL C O   
5087 C CB  . VAL C 124 ? 1.4871 0.8280 0.6835 0.1596  0.1074  -0.1481 122 VAL C CB  
5088 C CG1 . VAL C 124 ? 1.3415 0.7187 0.6217 0.1537  0.1005  -0.1339 122 VAL C CG1 
5089 C CG2 . VAL C 124 ? 1.4573 0.8252 0.6387 0.1737  0.1458  -0.1366 122 VAL C CG2 
5090 N N   . SER C 125 ? 1.5774 0.8303 0.5964 0.1493  0.0783  -0.1792 123 SER C N   
5091 C CA  . SER C 125 ? 1.6924 0.9128 0.6224 0.1531  0.0839  -0.1894 123 SER C CA  
5092 C C   . SER C 125 ? 1.8010 0.9991 0.6980 0.1777  0.1202  -0.2075 123 SER C C   
5093 O O   . SER C 125 ? 1.9407 1.1068 0.8309 0.1796  0.1103  -0.2278 123 SER C O   
5094 C CB  . SER C 125 ? 1.7631 0.9449 0.6449 0.1364  0.0421  -0.2061 123 SER C CB  
5095 O OG  . SER C 125 ? 1.9224 1.0964 0.7433 0.1332  0.0388  -0.2025 123 SER C OG  
5096 N N   . SER C 126 ? 1.8008 1.0322 0.6981 0.1928  0.1598  -0.1944 124 SER C N   
5097 C CA  . SER C 126 ? 1.8307 1.0657 0.7163 0.2182  0.1956  -0.2059 124 SER C CA  
5098 C C   . SER C 126 ? 1.8857 1.0862 0.7038 0.2168  0.1881  -0.2227 124 SER C C   
5099 O O   . SER C 126 ? 1.9366 1.1002 0.7424 0.2241  0.1799  -0.2449 124 SER C O   
5100 C CB  . SER C 126 ? 1.7998 1.0917 0.7008 0.2301  0.2391  -0.1854 124 SER C CB  
5101 O OG  . SER C 126 ? 1.8133 1.1166 0.6716 0.2123  0.2401  -0.1674 124 SER C OG  
# 
