data_8P5M
# 
_entry.id   8P5M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.393 
_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   8P5M         pdb_00008p5m 10.2210/pdb8p5m/pdb 
WWPDB D_1292127783 ?            ?                   
EMDB  EMD-17451    ?            ?                   
# 
_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       2024-06-05 
# 
_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                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8P5M 
_pdbx_database_status.recvd_initial_deposition_date   2023-05-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'SARS-CoV-2 Spike RBD in complex with Mab-23 (Fab)' 
_pdbx_database_related.db_id          EMD-17451 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              martin.hallberg@ki.se 
_pdbx_contact_author.name_first         'B. Martin' 
_pdbx_contact_author.name_last          Hallberg 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6781-0345 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Das, H.'        1 0000-0001-7495-7065 
'Hallberg, B.M.' 2 0000-0002-6781-0345 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'SARS-CoV-2 Spike RBD in complex with Mab-23 (Fab domains)' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Das, H.'        1 ? 
primary 'Hallberg, B.M.' 2 ? 
# 
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 'Spike protein S1'                     22002.676 1 ? ? ? ? 
2 polymer man 'Mab-23 (Heavy chain variable domain)' 48500.398 1 ? ? ? ? 
3 polymer man 'Mab-23 (Light chain variable domain)' 23234.852 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 
;TNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAP
GQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPL
QSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPK
;
;TNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAP
GQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPL
QSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPK
;
I ? 
2 'polypeptide(L)' no no 
;EVQLVESGGGLVQPGGSLRLSCTASGFTFSNYGFHWVRQAPGKGLEWVTIISYDGITKHYADSVKDRFTVSRDNSKTMVY
LQMNNLKLDDTAVYYCARDLGTYDDSWGQGVLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGLVKDYFPEVTSWNSGAL
TSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKVEPKSCDKTHTCPPCPAPELLGGPSVFLFP
PKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS
NKALPAPIEKTISKAKGQPREPQVYTLPPSRDETKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFF
LYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
;
;EVQLVESGGGLVQPGGSLRLSCTASGFTFSNYGFHWVRQAPGKGLEWVTIISYDGITKHYADSVKDRFTVSRDNSKTMVY
LQMNNLKLDDTAVYYCARDLGTYDDSWGQGVLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGLVKDYFPEVTSWNSGAL
TSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKVEPKSCDKTHTCPPCPAPELLGGPSVFLFP
PKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVS
NKALPAPIEKTISKAKGQPREPQVYTLPPSRDETKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFF
LYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
;
G ? 
3 'polypeptide(L)' no no 
;DIQMTQSPSALSASVGDRVTISCRASQNIDGFLAWYQQKPGKAPKLLIYAASRLQSGIPSRFSGSGSGTDFTLTISSLQP
EDFAAYYCQQVYSAPLTFGGGTKVEFKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;DIQMTQSPSALSASVGDRVTISCRASQNIDGFLAWYQQKPGKAPKLLIYAASRLQSGIPSRFSGSGSGTDFTLTISSLQP
EDFAAYYCQQVYSAPLTFGGGTKVEFKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQ
ESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
L ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   ASN n 
1 3   LEU n 
1 4   CYS n 
1 5   PRO n 
1 6   PHE n 
1 7   GLY n 
1 8   GLU n 
1 9   VAL n 
1 10  PHE n 
1 11  ASN n 
1 12  ALA n 
1 13  THR n 
1 14  ARG n 
1 15  PHE n 
1 16  ALA n 
1 17  SER n 
1 18  VAL n 
1 19  TYR n 
1 20  ALA n 
1 21  TRP n 
1 22  ASN n 
1 23  ARG n 
1 24  LYS n 
1 25  ARG n 
1 26  ILE n 
1 27  SER n 
1 28  ASN n 
1 29  CYS n 
1 30  VAL n 
1 31  ALA n 
1 32  ASP n 
1 33  TYR n 
1 34  SER n 
1 35  VAL n 
1 36  LEU n 
1 37  TYR n 
1 38  ASN n 
1 39  SER n 
1 40  ALA n 
1 41  SER n 
1 42  PHE n 
1 43  SER n 
1 44  THR n 
1 45  PHE n 
1 46  LYS n 
1 47  CYS n 
1 48  TYR n 
1 49  GLY n 
1 50  VAL n 
1 51  SER n 
1 52  PRO n 
1 53  THR n 
1 54  LYS n 
1 55  LEU n 
1 56  ASN n 
1 57  ASP n 
1 58  LEU n 
1 59  CYS n 
1 60  PHE n 
1 61  THR n 
1 62  ASN n 
1 63  VAL n 
1 64  TYR n 
1 65  ALA n 
1 66  ASP n 
1 67  SER n 
1 68  PHE n 
1 69  VAL n 
1 70  ILE n 
1 71  ARG n 
1 72  GLY n 
1 73  ASP n 
1 74  GLU n 
1 75  VAL n 
1 76  ARG n 
1 77  GLN n 
1 78  ILE n 
1 79  ALA n 
1 80  PRO n 
1 81  GLY n 
1 82  GLN n 
1 83  THR n 
1 84  GLY n 
1 85  LYS n 
1 86  ILE n 
1 87  ALA n 
1 88  ASP n 
1 89  TYR n 
1 90  ASN n 
1 91  TYR n 
1 92  LYS n 
1 93  LEU n 
1 94  PRO n 
1 95  ASP n 
1 96  ASP n 
1 97  PHE n 
1 98  THR n 
1 99  GLY n 
1 100 CYS n 
1 101 VAL n 
1 102 ILE n 
1 103 ALA n 
1 104 TRP n 
1 105 ASN n 
1 106 SER n 
1 107 ASN n 
1 108 ASN n 
1 109 LEU n 
1 110 ASP n 
1 111 SER n 
1 112 LYS n 
1 113 VAL n 
1 114 GLY n 
1 115 GLY n 
1 116 ASN n 
1 117 TYR n 
1 118 ASN n 
1 119 TYR n 
1 120 LEU n 
1 121 TYR n 
1 122 ARG n 
1 123 LEU n 
1 124 PHE n 
1 125 ARG n 
1 126 LYS n 
1 127 SER n 
1 128 ASN n 
1 129 LEU n 
1 130 LYS n 
1 131 PRO n 
1 132 PHE n 
1 133 GLU n 
1 134 ARG n 
1 135 ASP n 
1 136 ILE n 
1 137 SER n 
1 138 THR n 
1 139 GLU n 
1 140 ILE n 
1 141 TYR n 
1 142 GLN n 
1 143 ALA n 
1 144 GLY n 
1 145 SER n 
1 146 THR n 
1 147 PRO n 
1 148 CYS n 
1 149 ASN n 
1 150 GLY n 
1 151 VAL n 
1 152 GLU n 
1 153 GLY n 
1 154 PHE n 
1 155 ASN n 
1 156 CYS n 
1 157 TYR n 
1 158 PHE n 
1 159 PRO n 
1 160 LEU n 
1 161 GLN n 
1 162 SER n 
1 163 TYR n 
1 164 GLY n 
1 165 PHE n 
1 166 GLN n 
1 167 PRO n 
1 168 THR n 
1 169 ASN n 
1 170 GLY n 
1 171 VAL n 
1 172 GLY n 
1 173 TYR n 
1 174 GLN n 
1 175 PRO n 
1 176 TYR n 
1 177 ARG n 
1 178 VAL n 
1 179 VAL n 
1 180 VAL n 
1 181 LEU n 
1 182 SER n 
1 183 PHE n 
1 184 GLU n 
1 185 LEU n 
1 186 LEU n 
1 187 HIS n 
1 188 ALA n 
1 189 PRO n 
1 190 ALA n 
1 191 THR n 
1 192 VAL n 
1 193 CYS n 
1 194 GLY n 
1 195 PRO n 
1 196 LYS n 
2 1   GLU n 
2 2   VAL n 
2 3   GLN n 
2 4   LEU n 
2 5   VAL n 
2 6   GLU n 
2 7   SER n 
2 8   GLY n 
2 9   GLY n 
2 10  GLY n 
2 11  LEU n 
2 12  VAL n 
2 13  GLN n 
2 14  PRO n 
2 15  GLY n 
2 16  GLY n 
2 17  SER n 
2 18  LEU n 
2 19  ARG n 
2 20  LEU n 
2 21  SER n 
2 22  CYS n 
2 23  THR n 
2 24  ALA n 
2 25  SER n 
2 26  GLY n 
2 27  PHE n 
2 28  THR n 
2 29  PHE n 
2 30  SER n 
2 31  ASN n 
2 32  TYR n 
2 33  GLY n 
2 34  PHE n 
2 35  HIS n 
2 36  TRP n 
2 37  VAL n 
2 38  ARG n 
2 39  GLN n 
2 40  ALA n 
2 41  PRO n 
2 42  GLY n 
2 43  LYS n 
2 44  GLY n 
2 45  LEU n 
2 46  GLU n 
2 47  TRP n 
2 48  VAL n 
2 49  THR n 
2 50  ILE n 
2 51  ILE n 
2 52  SER n 
2 53  TYR n 
2 54  ASP n 
2 55  GLY n 
2 56  ILE n 
2 57  THR n 
2 58  LYS n 
2 59  HIS n 
2 60  TYR n 
2 61  ALA n 
2 62  ASP n 
2 63  SER n 
2 64  VAL n 
2 65  LYS n 
2 66  ASP n 
2 67  ARG n 
2 68  PHE n 
2 69  THR n 
2 70  VAL n 
2 71  SER n 
2 72  ARG n 
2 73  ASP n 
2 74  ASN n 
2 75  SER n 
2 76  LYS n 
2 77  THR n 
2 78  MET n 
2 79  VAL n 
2 80  TYR n 
2 81  LEU n 
2 82  GLN n 
2 83  MET n 
2 84  ASN n 
2 85  ASN n 
2 86  LEU n 
2 87  LYS n 
2 88  LEU n 
2 89  ASP n 
2 90  ASP n 
2 91  THR n 
2 92  ALA n 
2 93  VAL n 
2 94  TYR n 
2 95  TYR n 
2 96  CYS n 
2 97  ALA n 
2 98  ARG n 
2 99  ASP n 
2 100 LEU n 
2 101 GLY n 
2 102 THR n 
2 103 TYR n 
2 104 ASP n 
2 105 ASP n 
2 106 SER n 
2 107 TRP n 
2 108 GLY n 
2 109 GLN n 
2 110 GLY n 
2 111 VAL n 
2 112 LEU n 
2 113 VAL n 
2 114 THR n 
2 115 VAL n 
2 116 SER n 
2 117 SER n 
2 118 ALA n 
2 119 SER n 
2 120 THR n 
2 121 LYS n 
2 122 GLY n 
2 123 PRO n 
2 124 SER n 
2 125 VAL n 
2 126 PHE n 
2 127 PRO n 
2 128 LEU n 
2 129 ALA n 
2 130 PRO n 
2 131 SER n 
2 132 SER n 
2 133 LYS n 
2 134 SER n 
2 135 THR n 
2 136 SER n 
2 137 GLY n 
2 138 GLY n 
2 139 THR n 
2 140 ALA n 
2 141 ALA n 
2 142 LEU n 
2 143 GLY n 
2 144 LEU n 
2 145 VAL n 
2 146 LYS n 
2 147 ASP n 
2 148 TYR n 
2 149 PHE n 
2 150 PRO n 
2 151 GLU n 
2 152 VAL n 
2 153 THR n 
2 154 SER n 
2 155 TRP n 
2 156 ASN n 
2 157 SER n 
2 158 GLY n 
2 159 ALA n 
2 160 LEU n 
2 161 THR n 
2 162 SER n 
2 163 GLY n 
2 164 VAL n 
2 165 HIS n 
2 166 THR n 
2 167 PHE n 
2 168 PRO n 
2 169 ALA n 
2 170 VAL n 
2 171 LEU n 
2 172 GLN n 
2 173 SER n 
2 174 SER n 
2 175 GLY n 
2 176 LEU n 
2 177 TYR n 
2 178 SER n 
2 179 LEU n 
2 180 SER n 
2 181 SER n 
2 182 VAL n 
2 183 VAL n 
2 184 THR n 
2 185 VAL n 
2 186 PRO n 
2 187 SER n 
2 188 SER n 
2 189 SER n 
2 190 LEU n 
2 191 GLY n 
2 192 THR n 
2 193 GLN n 
2 194 THR n 
2 195 TYR n 
2 196 ILE n 
2 197 CYS n 
2 198 ASN n 
2 199 VAL n 
2 200 ASN n 
2 201 HIS n 
2 202 LYS n 
2 203 PRO n 
2 204 SER n 
2 205 ASN n 
2 206 THR n 
2 207 LYS n 
2 208 VAL n 
2 209 ASP n 
2 210 LYS n 
2 211 VAL n 
2 212 GLU n 
2 213 PRO n 
2 214 LYS n 
2 215 SER n 
2 216 CYS n 
2 217 ASP n 
2 218 LYS n 
2 219 THR n 
2 220 HIS n 
2 221 THR n 
2 222 CYS n 
2 223 PRO n 
2 224 PRO n 
2 225 CYS n 
2 226 PRO n 
2 227 ALA n 
2 228 PRO n 
2 229 GLU n 
2 230 LEU n 
2 231 LEU n 
2 232 GLY n 
2 233 GLY n 
2 234 PRO n 
2 235 SER n 
2 236 VAL n 
2 237 PHE n 
2 238 LEU n 
2 239 PHE n 
2 240 PRO n 
2 241 PRO n 
2 242 LYS n 
2 243 PRO n 
2 244 LYS n 
2 245 ASP n 
2 246 THR n 
2 247 LEU n 
2 248 MET n 
2 249 ILE n 
2 250 SER n 
2 251 ARG n 
2 252 THR n 
2 253 PRO n 
2 254 GLU n 
2 255 VAL n 
2 256 THR n 
2 257 CYS n 
2 258 VAL n 
2 259 VAL n 
2 260 VAL n 
2 261 ASP n 
2 262 VAL n 
2 263 SER n 
2 264 HIS n 
2 265 GLU n 
2 266 ASP n 
2 267 PRO n 
2 268 GLU n 
2 269 VAL n 
2 270 LYS n 
2 271 PHE n 
2 272 ASN n 
2 273 TRP n 
2 274 TYR n 
2 275 VAL n 
2 276 ASP n 
2 277 GLY n 
2 278 VAL n 
2 279 GLU n 
2 280 VAL n 
2 281 HIS n 
2 282 ASN n 
2 283 ALA n 
2 284 LYS n 
2 285 THR n 
2 286 LYS n 
2 287 PRO n 
2 288 ARG n 
2 289 GLU n 
2 290 GLU n 
2 291 GLN n 
2 292 TYR n 
2 293 ASN n 
2 294 SER n 
2 295 THR n 
2 296 TYR n 
2 297 ARG n 
2 298 VAL n 
2 299 VAL n 
2 300 SER n 
2 301 VAL n 
2 302 LEU n 
2 303 THR n 
2 304 VAL n 
2 305 LEU n 
2 306 HIS n 
2 307 GLN n 
2 308 ASP n 
2 309 TRP n 
2 310 LEU n 
2 311 ASN n 
2 312 GLY n 
2 313 LYS n 
2 314 GLU n 
2 315 TYR n 
2 316 LYS n 
2 317 CYS n 
2 318 LYS n 
2 319 VAL n 
2 320 SER n 
2 321 ASN n 
2 322 LYS n 
2 323 ALA n 
2 324 LEU n 
2 325 PRO n 
2 326 ALA n 
2 327 PRO n 
2 328 ILE n 
2 329 GLU n 
2 330 LYS n 
2 331 THR n 
2 332 ILE n 
2 333 SER n 
2 334 LYS n 
2 335 ALA n 
2 336 LYS n 
2 337 GLY n 
2 338 GLN n 
2 339 PRO n 
2 340 ARG n 
2 341 GLU n 
2 342 PRO n 
2 343 GLN n 
2 344 VAL n 
2 345 TYR n 
2 346 THR n 
2 347 LEU n 
2 348 PRO n 
2 349 PRO n 
2 350 SER n 
2 351 ARG n 
2 352 ASP n 
2 353 GLU n 
2 354 THR n 
2 355 LYS n 
2 356 ASN n 
2 357 GLN n 
2 358 VAL n 
2 359 SER n 
2 360 LEU n 
2 361 THR n 
2 362 CYS n 
2 363 LEU n 
2 364 VAL n 
2 365 LYS n 
2 366 GLY n 
2 367 PHE n 
2 368 TYR n 
2 369 PRO n 
2 370 SER n 
2 371 ASP n 
2 372 ILE n 
2 373 ALA n 
2 374 VAL n 
2 375 GLU n 
2 376 TRP n 
2 377 GLU n 
2 378 SER n 
2 379 ASN n 
2 380 GLY n 
2 381 GLN n 
2 382 PRO n 
2 383 GLU n 
2 384 ASN n 
2 385 ASN n 
2 386 TYR n 
2 387 LYS n 
2 388 THR n 
2 389 THR n 
2 390 PRO n 
2 391 PRO n 
2 392 VAL n 
2 393 LEU n 
2 394 ASP n 
2 395 SER n 
2 396 ASP n 
2 397 GLY n 
2 398 SER n 
2 399 PHE n 
2 400 PHE n 
2 401 LEU n 
2 402 TYR n 
2 403 SER n 
2 404 LYS n 
2 405 LEU n 
2 406 THR n 
2 407 VAL n 
2 408 ASP n 
2 409 LYS n 
2 410 SER n 
2 411 ARG n 
2 412 TRP n 
2 413 GLN n 
2 414 GLN n 
2 415 GLY n 
2 416 ASN n 
2 417 VAL n 
2 418 PHE n 
2 419 SER n 
2 420 CYS n 
2 421 SER n 
2 422 VAL n 
2 423 MET n 
2 424 HIS n 
2 425 GLU n 
2 426 ALA n 
2 427 LEU n 
2 428 HIS n 
2 429 ASN n 
2 430 HIS n 
2 431 TYR n 
2 432 THR n 
2 433 GLN n 
2 434 LYS n 
2 435 SER n 
2 436 LEU n 
2 437 SER n 
2 438 LEU n 
2 439 SER n 
2 440 PRO n 
2 441 GLY n 
2 442 LYS n 
3 1   ASP n 
3 2   ILE n 
3 3   GLN n 
3 4   MET n 
3 5   THR n 
3 6   GLN n 
3 7   SER n 
3 8   PRO n 
3 9   SER n 
3 10  ALA n 
3 11  LEU n 
3 12  SER n 
3 13  ALA n 
3 14  SER n 
3 15  VAL n 
3 16  GLY n 
3 17  ASP n 
3 18  ARG n 
3 19  VAL n 
3 20  THR n 
3 21  ILE n 
3 22  SER n 
3 23  CYS n 
3 24  ARG n 
3 25  ALA n 
3 26  SER n 
3 27  GLN n 
3 28  ASN n 
3 29  ILE n 
3 30  ASP n 
3 31  GLY n 
3 32  PHE n 
3 33  LEU n 
3 34  ALA n 
3 35  TRP n 
3 36  TYR n 
3 37  GLN n 
3 38  GLN n 
3 39  LYS n 
3 40  PRO n 
3 41  GLY n 
3 42  LYS n 
3 43  ALA n 
3 44  PRO n 
3 45  LYS n 
3 46  LEU n 
3 47  LEU n 
3 48  ILE n 
3 49  TYR n 
3 50  ALA n 
3 51  ALA n 
3 52  SER n 
3 53  ARG n 
3 54  LEU n 
3 55  GLN n 
3 56  SER n 
3 57  GLY n 
3 58  ILE n 
3 59  PRO n 
3 60  SER n 
3 61  ARG n 
3 62  PHE n 
3 63  SER n 
3 64  GLY n 
3 65  SER n 
3 66  GLY n 
3 67  SER n 
3 68  GLY n 
3 69  THR n 
3 70  ASP n 
3 71  PHE n 
3 72  THR n 
3 73  LEU n 
3 74  THR n 
3 75  ILE n 
3 76  SER n 
3 77  SER n 
3 78  LEU n 
3 79  GLN n 
3 80  PRO n 
3 81  GLU n 
3 82  ASP n 
3 83  PHE n 
3 84  ALA n 
3 85  ALA n 
3 86  TYR n 
3 87  TYR n 
3 88  CYS n 
3 89  GLN n 
3 90  GLN n 
3 91  VAL n 
3 92  TYR n 
3 93  SER n 
3 94  ALA n 
3 95  PRO n 
3 96  LEU n 
3 97  THR n 
3 98  PHE n 
3 99  GLY n 
3 100 GLY n 
3 101 GLY n 
3 102 THR n 
3 103 LYS n 
3 104 VAL n 
3 105 GLU n 
3 106 PHE n 
3 107 LYS n 
3 108 ARG n 
3 109 THR n 
3 110 VAL n 
3 111 ALA n 
3 112 ALA n 
3 113 PRO n 
3 114 SER n 
3 115 VAL n 
3 116 PHE n 
3 117 ILE n 
3 118 PHE n 
3 119 PRO n 
3 120 PRO n 
3 121 SER n 
3 122 ASP n 
3 123 GLU n 
3 124 GLN n 
3 125 LEU n 
3 126 LYS n 
3 127 SER n 
3 128 GLY n 
3 129 THR n 
3 130 ALA n 
3 131 SER n 
3 132 VAL n 
3 133 VAL n 
3 134 CYS n 
3 135 LEU n 
3 136 LEU n 
3 137 ASN n 
3 138 ASN n 
3 139 PHE n 
3 140 TYR n 
3 141 PRO n 
3 142 ARG n 
3 143 GLU n 
3 144 ALA n 
3 145 LYS n 
3 146 VAL n 
3 147 GLN n 
3 148 TRP n 
3 149 LYS n 
3 150 VAL n 
3 151 ASP n 
3 152 ASN n 
3 153 ALA n 
3 154 LEU n 
3 155 GLN n 
3 156 SER n 
3 157 GLY n 
3 158 ASN n 
3 159 SER n 
3 160 GLN n 
3 161 GLU n 
3 162 SER n 
3 163 VAL n 
3 164 THR n 
3 165 GLU n 
3 166 GLN n 
3 167 ASP n 
3 168 SER n 
3 169 LYS n 
3 170 ASP n 
3 171 SER n 
3 172 THR n 
3 173 TYR n 
3 174 SER n 
3 175 LEU n 
3 176 SER n 
3 177 SER n 
3 178 THR n 
3 179 LEU n 
3 180 THR n 
3 181 LEU n 
3 182 SER n 
3 183 LYS n 
3 184 ALA n 
3 185 ASP n 
3 186 TYR n 
3 187 GLU n 
3 188 LYS n 
3 189 HIS n 
3 190 LYS n 
3 191 VAL n 
3 192 TYR n 
3 193 ALA n 
3 194 CYS n 
3 195 GLU n 
3 196 VAL n 
3 197 THR n 
3 198 HIS n 
3 199 GLN n 
3 200 GLY n 
3 201 LEU n 
3 202 SER n 
3 203 SER n 
3 204 PRO n 
3 205 VAL n 
3 206 THR n 
3 207 LYS n 
3 208 SER n 
3 209 PHE n 
3 210 ASN n 
3 211 ARG n 
3 212 GLY n 
3 213 GLU n 
3 214 CYS 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' 1 196 ? ? 'S, 2' ? ? ? ? ? ? 'Severe acute respiratory syndrome coronavirus 2' 2697049 ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 442 ? ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 214 ? ? ?      ? ? ? ? ? ? 'Homo sapiens'                                    9606    ? ? ? ? ? 
? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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   THR 1   333 333 THR THR I . n 
A 1 2   ASN 2   334 334 ASN ASN I . n 
A 1 3   LEU 3   335 335 LEU LEU I . n 
A 1 4   CYS 4   336 336 CYS CYS I . n 
A 1 5   PRO 5   337 337 PRO PRO I . n 
A 1 6   PHE 6   338 338 PHE PHE I . n 
A 1 7   GLY 7   339 339 GLY GLY I . n 
A 1 8   GLU 8   340 340 GLU GLU I . n 
A 1 9   VAL 9   341 341 VAL VAL I . n 
A 1 10  PHE 10  342 342 PHE PHE I . n 
A 1 11  ASN 11  343 343 ASN ASN I . n 
A 1 12  ALA 12  344 344 ALA ALA I . n 
A 1 13  THR 13  345 345 THR THR I . n 
A 1 14  ARG 14  346 346 ARG ARG I . n 
A 1 15  PHE 15  347 347 PHE PHE I . n 
A 1 16  ALA 16  348 348 ALA ALA I . n 
A 1 17  SER 17  349 349 SER SER I . n 
A 1 18  VAL 18  350 350 VAL VAL I . n 
A 1 19  TYR 19  351 351 TYR TYR I . n 
A 1 20  ALA 20  352 352 ALA ALA I . n 
A 1 21  TRP 21  353 353 TRP TRP I . n 
A 1 22  ASN 22  354 354 ASN ASN I . n 
A 1 23  ARG 23  355 355 ARG ARG I . n 
A 1 24  LYS 24  356 356 LYS LYS I . n 
A 1 25  ARG 25  357 357 ARG ARG I . n 
A 1 26  ILE 26  358 358 ILE ILE I . n 
A 1 27  SER 27  359 359 SER SER I . n 
A 1 28  ASN 28  360 360 ASN ASN I . n 
A 1 29  CYS 29  361 361 CYS CYS I . n 
A 1 30  VAL 30  362 362 VAL VAL I . n 
A 1 31  ALA 31  363 363 ALA ALA I . n 
A 1 32  ASP 32  364 364 ASP ASP I . n 
A 1 33  TYR 33  365 365 TYR TYR I . n 
A 1 34  SER 34  366 366 SER SER I . n 
A 1 35  VAL 35  367 367 VAL VAL I . n 
A 1 36  LEU 36  368 368 LEU LEU I . n 
A 1 37  TYR 37  369 369 TYR TYR I . n 
A 1 38  ASN 38  370 370 ASN ASN I . n 
A 1 39  SER 39  371 371 SER SER I . n 
A 1 40  ALA 40  372 372 ALA ALA I . n 
A 1 41  SER 41  373 373 SER SER I . n 
A 1 42  PHE 42  374 374 PHE PHE I . n 
A 1 43  SER 43  375 375 SER SER I . n 
A 1 44  THR 44  376 376 THR THR I . n 
A 1 45  PHE 45  377 377 PHE PHE I . n 
A 1 46  LYS 46  378 378 LYS LYS I . n 
A 1 47  CYS 47  379 379 CYS CYS I . n 
A 1 48  TYR 48  380 380 TYR TYR I . n 
A 1 49  GLY 49  381 381 GLY GLY I . n 
A 1 50  VAL 50  382 382 VAL VAL I . n 
A 1 51  SER 51  383 383 SER SER I . n 
A 1 52  PRO 52  384 384 PRO PRO I . n 
A 1 53  THR 53  385 385 THR THR I . n 
A 1 54  LYS 54  386 386 LYS LYS I . n 
A 1 55  LEU 55  387 387 LEU LEU I . n 
A 1 56  ASN 56  388 388 ASN ASN I . n 
A 1 57  ASP 57  389 389 ASP ASP I . n 
A 1 58  LEU 58  390 390 LEU LEU I . n 
A 1 59  CYS 59  391 391 CYS CYS I . n 
A 1 60  PHE 60  392 392 PHE PHE I . n 
A 1 61  THR 61  393 393 THR THR I . n 
A 1 62  ASN 62  394 394 ASN ASN I . n 
A 1 63  VAL 63  395 395 VAL VAL I . n 
A 1 64  TYR 64  396 396 TYR TYR I . n 
A 1 65  ALA 65  397 397 ALA ALA I . n 
A 1 66  ASP 66  398 398 ASP ASP I . n 
A 1 67  SER 67  399 399 SER SER I . n 
A 1 68  PHE 68  400 400 PHE PHE I . n 
A 1 69  VAL 69  401 401 VAL VAL I . n 
A 1 70  ILE 70  402 402 ILE ILE I . n 
A 1 71  ARG 71  403 403 ARG ARG I . n 
A 1 72  GLY 72  404 404 GLY GLY I . n 
A 1 73  ASP 73  405 405 ASP ASP I . n 
A 1 74  GLU 74  406 406 GLU GLU I . n 
A 1 75  VAL 75  407 407 VAL VAL I . n 
A 1 76  ARG 76  408 408 ARG ARG I . n 
A 1 77  GLN 77  409 409 GLN GLN I . n 
A 1 78  ILE 78  410 410 ILE ILE I . n 
A 1 79  ALA 79  411 411 ALA ALA I . n 
A 1 80  PRO 80  412 412 PRO PRO I . n 
A 1 81  GLY 81  413 413 GLY GLY I . n 
A 1 82  GLN 82  414 414 GLN GLN I . n 
A 1 83  THR 83  415 415 THR THR I . n 
A 1 84  GLY 84  416 416 GLY GLY I . n 
A 1 85  LYS 85  417 417 LYS LYS I . n 
A 1 86  ILE 86  418 418 ILE ILE I . n 
A 1 87  ALA 87  419 419 ALA ALA I . n 
A 1 88  ASP 88  420 420 ASP ASP I . n 
A 1 89  TYR 89  421 421 TYR TYR I . n 
A 1 90  ASN 90  422 422 ASN ASN I . n 
A 1 91  TYR 91  423 423 TYR TYR I . n 
A 1 92  LYS 92  424 424 LYS LYS I . n 
A 1 93  LEU 93  425 425 LEU LEU I . n 
A 1 94  PRO 94  426 426 PRO PRO I . n 
A 1 95  ASP 95  427 427 ASP ASP I . n 
A 1 96  ASP 96  428 428 ASP ASP I . n 
A 1 97  PHE 97  429 429 PHE PHE I . n 
A 1 98  THR 98  430 430 THR THR I . n 
A 1 99  GLY 99  431 431 GLY GLY I . n 
A 1 100 CYS 100 432 432 CYS CYS I . n 
A 1 101 VAL 101 433 433 VAL VAL I . n 
A 1 102 ILE 102 434 434 ILE ILE I . n 
A 1 103 ALA 103 435 435 ALA ALA I . n 
A 1 104 TRP 104 436 436 TRP TRP I . n 
A 1 105 ASN 105 437 437 ASN ASN I . n 
A 1 106 SER 106 438 438 SER SER I . n 
A 1 107 ASN 107 439 439 ASN ASN I . n 
A 1 108 ASN 108 440 440 ASN ASN I . n 
A 1 109 LEU 109 441 441 LEU LEU I . n 
A 1 110 ASP 110 442 442 ASP ASP I . n 
A 1 111 SER 111 443 443 SER SER I . n 
A 1 112 LYS 112 444 444 LYS LYS I . n 
A 1 113 VAL 113 445 445 VAL VAL I . n 
A 1 114 GLY 114 446 446 GLY GLY I . n 
A 1 115 GLY 115 447 447 GLY GLY I . n 
A 1 116 ASN 116 448 448 ASN ASN I . n 
A 1 117 TYR 117 449 449 TYR TYR I . n 
A 1 118 ASN 118 450 450 ASN ASN I . n 
A 1 119 TYR 119 451 451 TYR TYR I . n 
A 1 120 LEU 120 452 452 LEU LEU I . n 
A 1 121 TYR 121 453 453 TYR TYR I . n 
A 1 122 ARG 122 454 454 ARG ARG I . n 
A 1 123 LEU 123 455 455 LEU LEU I . n 
A 1 124 PHE 124 456 456 PHE PHE I . n 
A 1 125 ARG 125 457 457 ARG ARG I . n 
A 1 126 LYS 126 458 458 LYS LYS I . n 
A 1 127 SER 127 459 459 SER SER I . n 
A 1 128 ASN 128 460 460 ASN ASN I . n 
A 1 129 LEU 129 461 461 LEU LEU I . n 
A 1 130 LYS 130 462 462 LYS LYS I . n 
A 1 131 PRO 131 463 463 PRO PRO I . n 
A 1 132 PHE 132 464 464 PHE PHE I . n 
A 1 133 GLU 133 465 465 GLU GLU I . n 
A 1 134 ARG 134 466 466 ARG ARG I . n 
A 1 135 ASP 135 467 467 ASP ASP I . n 
A 1 136 ILE 136 468 468 ILE ILE I . n 
A 1 137 SER 137 469 469 SER SER I . n 
A 1 138 THR 138 470 470 THR THR I . n 
A 1 139 GLU 139 471 471 GLU GLU I . n 
A 1 140 ILE 140 472 472 ILE ILE I . n 
A 1 141 TYR 141 473 473 TYR TYR I . n 
A 1 142 GLN 142 474 474 GLN GLN I . n 
A 1 143 ALA 143 475 475 ALA ALA I . n 
A 1 144 GLY 144 476 476 GLY GLY I . n 
A 1 145 SER 145 477 477 SER SER I . n 
A 1 146 THR 146 478 478 THR THR I . n 
A 1 147 PRO 147 479 479 PRO PRO I . n 
A 1 148 CYS 148 480 480 CYS CYS I . n 
A 1 149 ASN 149 481 481 ASN ASN I . n 
A 1 150 GLY 150 482 482 GLY GLY I . n 
A 1 151 VAL 151 483 483 VAL VAL I . n 
A 1 152 GLU 152 484 484 GLU GLU I . n 
A 1 153 GLY 153 485 485 GLY GLY I . n 
A 1 154 PHE 154 486 486 PHE PHE I . n 
A 1 155 ASN 155 487 487 ASN ASN I . n 
A 1 156 CYS 156 488 488 CYS CYS I . n 
A 1 157 TYR 157 489 489 TYR TYR I . n 
A 1 158 PHE 158 490 490 PHE PHE I . n 
A 1 159 PRO 159 491 491 PRO PRO I . n 
A 1 160 LEU 160 492 492 LEU LEU I . n 
A 1 161 GLN 161 493 493 GLN GLN I . n 
A 1 162 SER 162 494 494 SER SER I . n 
A 1 163 TYR 163 495 495 TYR TYR I . n 
A 1 164 GLY 164 496 496 GLY GLY I . n 
A 1 165 PHE 165 497 497 PHE PHE I . n 
A 1 166 GLN 166 498 498 GLN GLN I . n 
A 1 167 PRO 167 499 499 PRO PRO I . n 
A 1 168 THR 168 500 500 THR THR I . n 
A 1 169 ASN 169 501 501 ASN ASN I . n 
A 1 170 GLY 170 502 502 GLY GLY I . n 
A 1 171 VAL 171 503 503 VAL VAL I . n 
A 1 172 GLY 172 504 504 GLY GLY I . n 
A 1 173 TYR 173 505 505 TYR TYR I . n 
A 1 174 GLN 174 506 506 GLN GLN I . n 
A 1 175 PRO 175 507 507 PRO PRO I . n 
A 1 176 TYR 176 508 508 TYR TYR I . n 
A 1 177 ARG 177 509 509 ARG ARG I . n 
A 1 178 VAL 178 510 510 VAL VAL I . n 
A 1 179 VAL 179 511 511 VAL VAL I . n 
A 1 180 VAL 180 512 512 VAL VAL I . n 
A 1 181 LEU 181 513 513 LEU LEU I . n 
A 1 182 SER 182 514 514 SER SER I . n 
A 1 183 PHE 183 515 515 PHE PHE I . n 
A 1 184 GLU 184 516 516 GLU GLU I . n 
A 1 185 LEU 185 517 517 LEU LEU I . n 
A 1 186 LEU 186 518 518 LEU LEU I . n 
A 1 187 HIS 187 519 519 HIS HIS I . n 
A 1 188 ALA 188 520 520 ALA ALA I . n 
A 1 189 PRO 189 521 521 PRO PRO I . n 
A 1 190 ALA 190 522 522 ALA ALA I . n 
A 1 191 THR 191 523 523 THR THR I . n 
A 1 192 VAL 192 524 524 VAL VAL I . n 
A 1 193 CYS 193 525 525 CYS CYS I . n 
A 1 194 GLY 194 526 526 GLY GLY I . n 
A 1 195 PRO 195 527 527 PRO PRO I . n 
A 1 196 LYS 196 528 ?   ?   ?   I . n 
B 2 1   GLU 1   1   1   GLU GLU G . n 
B 2 2   VAL 2   2   2   VAL VAL G . n 
B 2 3   GLN 3   3   3   GLN GLN G . n 
B 2 4   LEU 4   4   4   LEU LEU G . n 
B 2 5   VAL 5   5   5   VAL VAL G . n 
B 2 6   GLU 6   6   6   GLU GLU G . n 
B 2 7   SER 7   7   7   SER SER G . n 
B 2 8   GLY 8   8   8   GLY GLY G . n 
B 2 9   GLY 9   9   9   GLY GLY G . n 
B 2 10  GLY 10  10  10  GLY GLY G . n 
B 2 11  LEU 11  11  11  LEU LEU G . n 
B 2 12  VAL 12  12  12  VAL VAL G . n 
B 2 13  GLN 13  13  13  GLN GLN G . n 
B 2 14  PRO 14  14  14  PRO PRO G . n 
B 2 15  GLY 15  15  15  GLY GLY G . n 
B 2 16  GLY 16  16  16  GLY GLY G . n 
B 2 17  SER 17  17  17  SER SER G . n 
B 2 18  LEU 18  18  18  LEU LEU G . n 
B 2 19  ARG 19  19  19  ARG ARG G . n 
B 2 20  LEU 20  20  20  LEU LEU G . n 
B 2 21  SER 21  21  21  SER SER G . n 
B 2 22  CYS 22  22  22  CYS CYS G . n 
B 2 23  THR 23  23  23  THR THR G . n 
B 2 24  ALA 24  24  24  ALA ALA G . n 
B 2 25  SER 25  25  25  SER SER G . n 
B 2 26  GLY 26  26  26  GLY GLY G . n 
B 2 27  PHE 27  27  27  PHE PHE G . n 
B 2 28  THR 28  28  28  THR THR G . n 
B 2 29  PHE 29  29  29  PHE PHE G . n 
B 2 30  SER 30  30  30  SER SER G . n 
B 2 31  ASN 31  31  31  ASN ASN G . n 
B 2 32  TYR 32  32  32  TYR TYR G . n 
B 2 33  GLY 33  33  33  GLY GLY G . n 
B 2 34  PHE 34  34  34  PHE PHE G . n 
B 2 35  HIS 35  35  35  HIS HIS G . n 
B 2 36  TRP 36  36  36  TRP TRP G . n 
B 2 37  VAL 37  37  37  VAL VAL G . n 
B 2 38  ARG 38  38  38  ARG ARG G . n 
B 2 39  GLN 39  39  39  GLN GLN G . n 
B 2 40  ALA 40  40  40  ALA ALA G . n 
B 2 41  PRO 41  41  41  PRO PRO G . n 
B 2 42  GLY 42  42  42  GLY GLY G . n 
B 2 43  LYS 43  43  43  LYS LYS G . n 
B 2 44  GLY 44  44  44  GLY GLY G . n 
B 2 45  LEU 45  45  45  LEU LEU G . n 
B 2 46  GLU 46  46  46  GLU GLU G . n 
B 2 47  TRP 47  47  47  TRP TRP G . n 
B 2 48  VAL 48  48  48  VAL VAL G . n 
B 2 49  THR 49  49  49  THR THR G . n 
B 2 50  ILE 50  50  50  ILE ILE G . n 
B 2 51  ILE 51  51  51  ILE ILE G . n 
B 2 52  SER 52  52  52  SER SER G . n 
B 2 53  TYR 53  53  53  TYR TYR G . n 
B 2 54  ASP 54  54  54  ASP ASP G . n 
B 2 55  GLY 55  55  55  GLY GLY G . n 
B 2 56  ILE 56  56  56  ILE ILE G . n 
B 2 57  THR 57  57  57  THR THR G . n 
B 2 58  LYS 58  58  58  LYS LYS G . n 
B 2 59  HIS 59  59  59  HIS HIS G . n 
B 2 60  TYR 60  60  60  TYR TYR G . n 
B 2 61  ALA 61  61  61  ALA ALA G . n 
B 2 62  ASP 62  62  62  ASP ASP G . n 
B 2 63  SER 63  63  63  SER SER G . n 
B 2 64  VAL 64  64  64  VAL VAL G . n 
B 2 65  LYS 65  65  65  LYS LYS G . n 
B 2 66  ASP 66  66  66  ASP ASP G . n 
B 2 67  ARG 67  67  67  ARG ARG G . n 
B 2 68  PHE 68  68  68  PHE PHE G . n 
B 2 69  THR 69  69  69  THR THR G . n 
B 2 70  VAL 70  70  70  VAL VAL G . n 
B 2 71  SER 71  71  71  SER SER G . n 
B 2 72  ARG 72  72  72  ARG ARG G . n 
B 2 73  ASP 73  73  73  ASP ASP G . n 
B 2 74  ASN 74  74  74  ASN ASN G . n 
B 2 75  SER 75  75  75  SER SER G . n 
B 2 76  LYS 76  76  76  LYS LYS G . n 
B 2 77  THR 77  77  77  THR THR G . n 
B 2 78  MET 78  78  78  MET MET G . n 
B 2 79  VAL 79  79  79  VAL VAL G . n 
B 2 80  TYR 80  80  80  TYR TYR G . n 
B 2 81  LEU 81  81  81  LEU LEU G . n 
B 2 82  GLN 82  82  82  GLN GLN G . n 
B 2 83  MET 83  83  83  MET MET G . n 
B 2 84  ASN 84  84  84  ASN ASN G . n 
B 2 85  ASN 85  85  85  ASN ASN G . n 
B 2 86  LEU 86  86  86  LEU LEU G . n 
B 2 87  LYS 87  87  87  LYS LYS G . n 
B 2 88  LEU 88  88  88  LEU LEU G . n 
B 2 89  ASP 89  89  89  ASP ASP G . n 
B 2 90  ASP 90  90  90  ASP ASP G . n 
B 2 91  THR 91  91  91  THR THR G . n 
B 2 92  ALA 92  92  92  ALA ALA G . n 
B 2 93  VAL 93  93  93  VAL VAL G . n 
B 2 94  TYR 94  94  94  TYR TYR G . n 
B 2 95  TYR 95  95  95  TYR TYR G . n 
B 2 96  CYS 96  96  96  CYS CYS G . n 
B 2 97  ALA 97  97  97  ALA ALA G . n 
B 2 98  ARG 98  98  98  ARG ARG G . n 
B 2 99  ASP 99  99  99  ASP ASP G . n 
B 2 100 LEU 100 100 100 LEU LEU G . n 
B 2 101 GLY 101 101 101 GLY GLY G . n 
B 2 102 THR 102 102 102 THR THR G . n 
B 2 103 TYR 103 103 103 TYR TYR G . n 
B 2 104 ASP 104 104 104 ASP ASP G . n 
B 2 105 ASP 105 105 105 ASP ASP G . n 
B 2 106 SER 106 106 106 SER SER G . n 
B 2 107 TRP 107 107 107 TRP TRP G . n 
B 2 108 GLY 108 108 108 GLY GLY G . n 
B 2 109 GLN 109 109 109 GLN GLN G . n 
B 2 110 GLY 110 110 110 GLY GLY G . n 
B 2 111 VAL 111 111 111 VAL VAL G . n 
B 2 112 LEU 112 112 112 LEU LEU G . n 
B 2 113 VAL 113 113 113 VAL VAL G . n 
B 2 114 THR 114 114 114 THR THR G . n 
B 2 115 VAL 115 115 115 VAL VAL G . n 
B 2 116 SER 116 116 116 SER SER G . n 
B 2 117 SER 117 117 117 SER SER G . n 
B 2 118 ALA 118 118 ?   ?   ?   G . n 
B 2 119 SER 119 119 ?   ?   ?   G . n 
B 2 120 THR 120 120 ?   ?   ?   G . n 
B 2 121 LYS 121 121 ?   ?   ?   G . n 
B 2 122 GLY 122 122 ?   ?   ?   G . n 
B 2 123 PRO 123 123 ?   ?   ?   G . n 
B 2 124 SER 124 124 ?   ?   ?   G . n 
B 2 125 VAL 125 125 ?   ?   ?   G . n 
B 2 126 PHE 126 126 ?   ?   ?   G . n 
B 2 127 PRO 127 127 ?   ?   ?   G . n 
B 2 128 LEU 128 128 ?   ?   ?   G . n 
B 2 129 ALA 129 129 ?   ?   ?   G . n 
B 2 130 PRO 130 130 ?   ?   ?   G . n 
B 2 131 SER 131 131 ?   ?   ?   G . n 
B 2 132 SER 132 132 ?   ?   ?   G . n 
B 2 133 LYS 133 133 ?   ?   ?   G . n 
B 2 134 SER 134 134 ?   ?   ?   G . n 
B 2 135 THR 135 135 ?   ?   ?   G . n 
B 2 136 SER 136 136 ?   ?   ?   G . n 
B 2 137 GLY 137 137 ?   ?   ?   G . n 
B 2 138 GLY 138 138 ?   ?   ?   G . n 
B 2 139 THR 139 139 ?   ?   ?   G . n 
B 2 140 ALA 140 140 ?   ?   ?   G . n 
B 2 141 ALA 141 141 ?   ?   ?   G . n 
B 2 142 LEU 142 142 ?   ?   ?   G . n 
B 2 143 GLY 143 143 ?   ?   ?   G . n 
B 2 144 LEU 144 144 ?   ?   ?   G . n 
B 2 145 VAL 145 145 ?   ?   ?   G . n 
B 2 146 LYS 146 146 ?   ?   ?   G . n 
B 2 147 ASP 147 147 ?   ?   ?   G . n 
B 2 148 TYR 148 148 ?   ?   ?   G . n 
B 2 149 PHE 149 149 ?   ?   ?   G . n 
B 2 150 PRO 150 150 ?   ?   ?   G . n 
B 2 151 GLU 151 151 ?   ?   ?   G . n 
B 2 152 VAL 152 152 ?   ?   ?   G . n 
B 2 153 THR 153 153 ?   ?   ?   G . n 
B 2 154 SER 154 154 ?   ?   ?   G . n 
B 2 155 TRP 155 155 ?   ?   ?   G . n 
B 2 156 ASN 156 156 ?   ?   ?   G . n 
B 2 157 SER 157 157 ?   ?   ?   G . n 
B 2 158 GLY 158 158 ?   ?   ?   G . n 
B 2 159 ALA 159 159 ?   ?   ?   G . n 
B 2 160 LEU 160 160 ?   ?   ?   G . n 
B 2 161 THR 161 161 ?   ?   ?   G . n 
B 2 162 SER 162 162 ?   ?   ?   G . n 
B 2 163 GLY 163 163 ?   ?   ?   G . n 
B 2 164 VAL 164 164 ?   ?   ?   G . n 
B 2 165 HIS 165 165 ?   ?   ?   G . n 
B 2 166 THR 166 166 ?   ?   ?   G . n 
B 2 167 PHE 167 167 ?   ?   ?   G . n 
B 2 168 PRO 168 168 ?   ?   ?   G . n 
B 2 169 ALA 169 169 ?   ?   ?   G . n 
B 2 170 VAL 170 170 ?   ?   ?   G . n 
B 2 171 LEU 171 171 ?   ?   ?   G . n 
B 2 172 GLN 172 172 ?   ?   ?   G . n 
B 2 173 SER 173 173 ?   ?   ?   G . n 
B 2 174 SER 174 174 ?   ?   ?   G . n 
B 2 175 GLY 175 175 ?   ?   ?   G . n 
B 2 176 LEU 176 176 ?   ?   ?   G . n 
B 2 177 TYR 177 177 ?   ?   ?   G . n 
B 2 178 SER 178 178 ?   ?   ?   G . n 
B 2 179 LEU 179 179 ?   ?   ?   G . n 
B 2 180 SER 180 180 ?   ?   ?   G . n 
B 2 181 SER 181 181 ?   ?   ?   G . n 
B 2 182 VAL 182 182 ?   ?   ?   G . n 
B 2 183 VAL 183 183 ?   ?   ?   G . n 
B 2 184 THR 184 184 ?   ?   ?   G . n 
B 2 185 VAL 185 185 ?   ?   ?   G . n 
B 2 186 PRO 186 186 ?   ?   ?   G . n 
B 2 187 SER 187 187 ?   ?   ?   G . n 
B 2 188 SER 188 188 ?   ?   ?   G . n 
B 2 189 SER 189 189 ?   ?   ?   G . n 
B 2 190 LEU 190 190 ?   ?   ?   G . n 
B 2 191 GLY 191 191 ?   ?   ?   G . n 
B 2 192 THR 192 192 ?   ?   ?   G . n 
B 2 193 GLN 193 193 ?   ?   ?   G . n 
B 2 194 THR 194 194 ?   ?   ?   G . n 
B 2 195 TYR 195 195 ?   ?   ?   G . n 
B 2 196 ILE 196 196 ?   ?   ?   G . n 
B 2 197 CYS 197 197 ?   ?   ?   G . n 
B 2 198 ASN 198 198 ?   ?   ?   G . n 
B 2 199 VAL 199 199 ?   ?   ?   G . n 
B 2 200 ASN 200 200 ?   ?   ?   G . n 
B 2 201 HIS 201 201 ?   ?   ?   G . n 
B 2 202 LYS 202 202 ?   ?   ?   G . n 
B 2 203 PRO 203 203 ?   ?   ?   G . n 
B 2 204 SER 204 204 ?   ?   ?   G . n 
B 2 205 ASN 205 205 ?   ?   ?   G . n 
B 2 206 THR 206 206 ?   ?   ?   G . n 
B 2 207 LYS 207 207 ?   ?   ?   G . n 
B 2 208 VAL 208 208 ?   ?   ?   G . n 
B 2 209 ASP 209 209 ?   ?   ?   G . n 
B 2 210 LYS 210 210 ?   ?   ?   G . n 
B 2 211 VAL 211 211 ?   ?   ?   G . n 
B 2 212 GLU 212 212 ?   ?   ?   G . n 
B 2 213 PRO 213 213 ?   ?   ?   G . n 
B 2 214 LYS 214 214 ?   ?   ?   G . n 
B 2 215 SER 215 215 ?   ?   ?   G . n 
B 2 216 CYS 216 216 ?   ?   ?   G . n 
B 2 217 ASP 217 217 ?   ?   ?   G . n 
B 2 218 LYS 218 218 ?   ?   ?   G . n 
B 2 219 THR 219 219 ?   ?   ?   G . n 
B 2 220 HIS 220 220 ?   ?   ?   G . n 
B 2 221 THR 221 221 ?   ?   ?   G . n 
B 2 222 CYS 222 222 ?   ?   ?   G . n 
B 2 223 PRO 223 223 ?   ?   ?   G . n 
B 2 224 PRO 224 224 ?   ?   ?   G . n 
B 2 225 CYS 225 225 ?   ?   ?   G . n 
B 2 226 PRO 226 226 ?   ?   ?   G . n 
B 2 227 ALA 227 227 ?   ?   ?   G . n 
B 2 228 PRO 228 228 ?   ?   ?   G . n 
B 2 229 GLU 229 229 ?   ?   ?   G . n 
B 2 230 LEU 230 230 ?   ?   ?   G . n 
B 2 231 LEU 231 231 ?   ?   ?   G . n 
B 2 232 GLY 232 232 ?   ?   ?   G . n 
B 2 233 GLY 233 233 ?   ?   ?   G . n 
B 2 234 PRO 234 234 ?   ?   ?   G . n 
B 2 235 SER 235 235 ?   ?   ?   G . n 
B 2 236 VAL 236 236 ?   ?   ?   G . n 
B 2 237 PHE 237 237 ?   ?   ?   G . n 
B 2 238 LEU 238 238 ?   ?   ?   G . n 
B 2 239 PHE 239 239 ?   ?   ?   G . n 
B 2 240 PRO 240 240 ?   ?   ?   G . n 
B 2 241 PRO 241 241 ?   ?   ?   G . n 
B 2 242 LYS 242 242 ?   ?   ?   G . n 
B 2 243 PRO 243 243 ?   ?   ?   G . n 
B 2 244 LYS 244 244 ?   ?   ?   G . n 
B 2 245 ASP 245 245 ?   ?   ?   G . n 
B 2 246 THR 246 246 ?   ?   ?   G . n 
B 2 247 LEU 247 247 ?   ?   ?   G . n 
B 2 248 MET 248 248 ?   ?   ?   G . n 
B 2 249 ILE 249 249 ?   ?   ?   G . n 
B 2 250 SER 250 250 ?   ?   ?   G . n 
B 2 251 ARG 251 251 ?   ?   ?   G . n 
B 2 252 THR 252 252 ?   ?   ?   G . n 
B 2 253 PRO 253 253 ?   ?   ?   G . n 
B 2 254 GLU 254 254 ?   ?   ?   G . n 
B 2 255 VAL 255 255 ?   ?   ?   G . n 
B 2 256 THR 256 256 ?   ?   ?   G . n 
B 2 257 CYS 257 257 ?   ?   ?   G . n 
B 2 258 VAL 258 258 ?   ?   ?   G . n 
B 2 259 VAL 259 259 ?   ?   ?   G . n 
B 2 260 VAL 260 260 ?   ?   ?   G . n 
B 2 261 ASP 261 261 ?   ?   ?   G . n 
B 2 262 VAL 262 262 ?   ?   ?   G . n 
B 2 263 SER 263 263 ?   ?   ?   G . n 
B 2 264 HIS 264 264 ?   ?   ?   G . n 
B 2 265 GLU 265 265 ?   ?   ?   G . n 
B 2 266 ASP 266 266 ?   ?   ?   G . n 
B 2 267 PRO 267 267 ?   ?   ?   G . n 
B 2 268 GLU 268 268 ?   ?   ?   G . n 
B 2 269 VAL 269 269 ?   ?   ?   G . n 
B 2 270 LYS 270 270 ?   ?   ?   G . n 
B 2 271 PHE 271 271 ?   ?   ?   G . n 
B 2 272 ASN 272 272 ?   ?   ?   G . n 
B 2 273 TRP 273 273 ?   ?   ?   G . n 
B 2 274 TYR 274 274 ?   ?   ?   G . n 
B 2 275 VAL 275 275 ?   ?   ?   G . n 
B 2 276 ASP 276 276 ?   ?   ?   G . n 
B 2 277 GLY 277 277 ?   ?   ?   G . n 
B 2 278 VAL 278 278 ?   ?   ?   G . n 
B 2 279 GLU 279 279 ?   ?   ?   G . n 
B 2 280 VAL 280 280 ?   ?   ?   G . n 
B 2 281 HIS 281 281 ?   ?   ?   G . n 
B 2 282 ASN 282 282 ?   ?   ?   G . n 
B 2 283 ALA 283 283 ?   ?   ?   G . n 
B 2 284 LYS 284 284 ?   ?   ?   G . n 
B 2 285 THR 285 285 ?   ?   ?   G . n 
B 2 286 LYS 286 286 ?   ?   ?   G . n 
B 2 287 PRO 287 287 ?   ?   ?   G . n 
B 2 288 ARG 288 288 ?   ?   ?   G . n 
B 2 289 GLU 289 289 ?   ?   ?   G . n 
B 2 290 GLU 290 290 ?   ?   ?   G . n 
B 2 291 GLN 291 291 ?   ?   ?   G . n 
B 2 292 TYR 292 292 ?   ?   ?   G . n 
B 2 293 ASN 293 293 ?   ?   ?   G . n 
B 2 294 SER 294 294 ?   ?   ?   G . n 
B 2 295 THR 295 295 ?   ?   ?   G . n 
B 2 296 TYR 296 296 ?   ?   ?   G . n 
B 2 297 ARG 297 297 ?   ?   ?   G . n 
B 2 298 VAL 298 298 ?   ?   ?   G . n 
B 2 299 VAL 299 299 ?   ?   ?   G . n 
B 2 300 SER 300 300 ?   ?   ?   G . n 
B 2 301 VAL 301 301 ?   ?   ?   G . n 
B 2 302 LEU 302 302 ?   ?   ?   G . n 
B 2 303 THR 303 303 ?   ?   ?   G . n 
B 2 304 VAL 304 304 ?   ?   ?   G . n 
B 2 305 LEU 305 305 ?   ?   ?   G . n 
B 2 306 HIS 306 306 ?   ?   ?   G . n 
B 2 307 GLN 307 307 ?   ?   ?   G . n 
B 2 308 ASP 308 308 ?   ?   ?   G . n 
B 2 309 TRP 309 309 ?   ?   ?   G . n 
B 2 310 LEU 310 310 ?   ?   ?   G . n 
B 2 311 ASN 311 311 ?   ?   ?   G . n 
B 2 312 GLY 312 312 ?   ?   ?   G . n 
B 2 313 LYS 313 313 ?   ?   ?   G . n 
B 2 314 GLU 314 314 ?   ?   ?   G . n 
B 2 315 TYR 315 315 ?   ?   ?   G . n 
B 2 316 LYS 316 316 ?   ?   ?   G . n 
B 2 317 CYS 317 317 ?   ?   ?   G . n 
B 2 318 LYS 318 318 ?   ?   ?   G . n 
B 2 319 VAL 319 319 ?   ?   ?   G . n 
B 2 320 SER 320 320 ?   ?   ?   G . n 
B 2 321 ASN 321 321 ?   ?   ?   G . n 
B 2 322 LYS 322 322 ?   ?   ?   G . n 
B 2 323 ALA 323 323 ?   ?   ?   G . n 
B 2 324 LEU 324 324 ?   ?   ?   G . n 
B 2 325 PRO 325 325 ?   ?   ?   G . n 
B 2 326 ALA 326 326 ?   ?   ?   G . n 
B 2 327 PRO 327 327 ?   ?   ?   G . n 
B 2 328 ILE 328 328 ?   ?   ?   G . n 
B 2 329 GLU 329 329 ?   ?   ?   G . n 
B 2 330 LYS 330 330 ?   ?   ?   G . n 
B 2 331 THR 331 331 ?   ?   ?   G . n 
B 2 332 ILE 332 332 ?   ?   ?   G . n 
B 2 333 SER 333 333 ?   ?   ?   G . n 
B 2 334 LYS 334 334 ?   ?   ?   G . n 
B 2 335 ALA 335 335 ?   ?   ?   G . n 
B 2 336 LYS 336 336 ?   ?   ?   G . n 
B 2 337 GLY 337 337 ?   ?   ?   G . n 
B 2 338 GLN 338 338 ?   ?   ?   G . n 
B 2 339 PRO 339 339 ?   ?   ?   G . n 
B 2 340 ARG 340 340 ?   ?   ?   G . n 
B 2 341 GLU 341 341 ?   ?   ?   G . n 
B 2 342 PRO 342 342 ?   ?   ?   G . n 
B 2 343 GLN 343 343 ?   ?   ?   G . n 
B 2 344 VAL 344 344 ?   ?   ?   G . n 
B 2 345 TYR 345 345 ?   ?   ?   G . n 
B 2 346 THR 346 346 ?   ?   ?   G . n 
B 2 347 LEU 347 347 ?   ?   ?   G . n 
B 2 348 PRO 348 348 ?   ?   ?   G . n 
B 2 349 PRO 349 349 ?   ?   ?   G . n 
B 2 350 SER 350 350 ?   ?   ?   G . n 
B 2 351 ARG 351 351 ?   ?   ?   G . n 
B 2 352 ASP 352 352 ?   ?   ?   G . n 
B 2 353 GLU 353 353 ?   ?   ?   G . n 
B 2 354 THR 354 354 ?   ?   ?   G . n 
B 2 355 LYS 355 355 ?   ?   ?   G . n 
B 2 356 ASN 356 356 ?   ?   ?   G . n 
B 2 357 GLN 357 357 ?   ?   ?   G . n 
B 2 358 VAL 358 358 ?   ?   ?   G . n 
B 2 359 SER 359 359 ?   ?   ?   G . n 
B 2 360 LEU 360 360 ?   ?   ?   G . n 
B 2 361 THR 361 361 ?   ?   ?   G . n 
B 2 362 CYS 362 362 ?   ?   ?   G . n 
B 2 363 LEU 363 363 ?   ?   ?   G . n 
B 2 364 VAL 364 364 ?   ?   ?   G . n 
B 2 365 LYS 365 365 ?   ?   ?   G . n 
B 2 366 GLY 366 366 ?   ?   ?   G . n 
B 2 367 PHE 367 367 ?   ?   ?   G . n 
B 2 368 TYR 368 368 ?   ?   ?   G . n 
B 2 369 PRO 369 369 ?   ?   ?   G . n 
B 2 370 SER 370 370 ?   ?   ?   G . n 
B 2 371 ASP 371 371 ?   ?   ?   G . n 
B 2 372 ILE 372 372 ?   ?   ?   G . n 
B 2 373 ALA 373 373 ?   ?   ?   G . n 
B 2 374 VAL 374 374 ?   ?   ?   G . n 
B 2 375 GLU 375 375 ?   ?   ?   G . n 
B 2 376 TRP 376 376 ?   ?   ?   G . n 
B 2 377 GLU 377 377 ?   ?   ?   G . n 
B 2 378 SER 378 378 ?   ?   ?   G . n 
B 2 379 ASN 379 379 ?   ?   ?   G . n 
B 2 380 GLY 380 380 ?   ?   ?   G . n 
B 2 381 GLN 381 381 ?   ?   ?   G . n 
B 2 382 PRO 382 382 ?   ?   ?   G . n 
B 2 383 GLU 383 383 ?   ?   ?   G . n 
B 2 384 ASN 384 384 ?   ?   ?   G . n 
B 2 385 ASN 385 385 ?   ?   ?   G . n 
B 2 386 TYR 386 386 ?   ?   ?   G . n 
B 2 387 LYS 387 387 ?   ?   ?   G . n 
B 2 388 THR 388 388 ?   ?   ?   G . n 
B 2 389 THR 389 389 ?   ?   ?   G . n 
B 2 390 PRO 390 390 ?   ?   ?   G . n 
B 2 391 PRO 391 391 ?   ?   ?   G . n 
B 2 392 VAL 392 392 ?   ?   ?   G . n 
B 2 393 LEU 393 393 ?   ?   ?   G . n 
B 2 394 ASP 394 394 ?   ?   ?   G . n 
B 2 395 SER 395 395 ?   ?   ?   G . n 
B 2 396 ASP 396 396 ?   ?   ?   G . n 
B 2 397 GLY 397 397 ?   ?   ?   G . n 
B 2 398 SER 398 398 ?   ?   ?   G . n 
B 2 399 PHE 399 399 ?   ?   ?   G . n 
B 2 400 PHE 400 400 ?   ?   ?   G . n 
B 2 401 LEU 401 401 ?   ?   ?   G . n 
B 2 402 TYR 402 402 ?   ?   ?   G . n 
B 2 403 SER 403 403 ?   ?   ?   G . n 
B 2 404 LYS 404 404 ?   ?   ?   G . n 
B 2 405 LEU 405 405 ?   ?   ?   G . n 
B 2 406 THR 406 406 ?   ?   ?   G . n 
B 2 407 VAL 407 407 ?   ?   ?   G . n 
B 2 408 ASP 408 408 ?   ?   ?   G . n 
B 2 409 LYS 409 409 ?   ?   ?   G . n 
B 2 410 SER 410 410 ?   ?   ?   G . n 
B 2 411 ARG 411 411 ?   ?   ?   G . n 
B 2 412 TRP 412 412 ?   ?   ?   G . n 
B 2 413 GLN 413 413 ?   ?   ?   G . n 
B 2 414 GLN 414 414 ?   ?   ?   G . n 
B 2 415 GLY 415 415 ?   ?   ?   G . n 
B 2 416 ASN 416 416 ?   ?   ?   G . n 
B 2 417 VAL 417 417 ?   ?   ?   G . n 
B 2 418 PHE 418 418 ?   ?   ?   G . n 
B 2 419 SER 419 419 ?   ?   ?   G . n 
B 2 420 CYS 420 420 ?   ?   ?   G . n 
B 2 421 SER 421 421 ?   ?   ?   G . n 
B 2 422 VAL 422 422 ?   ?   ?   G . n 
B 2 423 MET 423 423 ?   ?   ?   G . n 
B 2 424 HIS 424 424 ?   ?   ?   G . n 
B 2 425 GLU 425 425 ?   ?   ?   G . n 
B 2 426 ALA 426 426 ?   ?   ?   G . n 
B 2 427 LEU 427 427 ?   ?   ?   G . n 
B 2 428 HIS 428 428 ?   ?   ?   G . n 
B 2 429 ASN 429 429 ?   ?   ?   G . n 
B 2 430 HIS 430 430 ?   ?   ?   G . n 
B 2 431 TYR 431 431 ?   ?   ?   G . n 
B 2 432 THR 432 432 ?   ?   ?   G . n 
B 2 433 GLN 433 433 ?   ?   ?   G . n 
B 2 434 LYS 434 434 ?   ?   ?   G . n 
B 2 435 SER 435 435 ?   ?   ?   G . n 
B 2 436 LEU 436 436 ?   ?   ?   G . n 
B 2 437 SER 437 437 ?   ?   ?   G . n 
B 2 438 LEU 438 438 ?   ?   ?   G . n 
B 2 439 SER 439 439 ?   ?   ?   G . n 
B 2 440 PRO 440 440 ?   ?   ?   G . n 
B 2 441 GLY 441 441 ?   ?   ?   G . n 
B 2 442 LYS 442 442 ?   ?   ?   G . n 
C 3 1   ASP 1   1   1   ASP ASP L . n 
C 3 2   ILE 2   2   2   ILE ILE L . n 
C 3 3   GLN 3   3   3   GLN GLN L . n 
C 3 4   MET 4   4   4   MET MET L . n 
C 3 5   THR 5   5   5   THR THR L . n 
C 3 6   GLN 6   6   6   GLN GLN L . n 
C 3 7   SER 7   7   7   SER SER L . n 
C 3 8   PRO 8   8   8   PRO PRO L . n 
C 3 9   SER 9   9   9   SER SER L . n 
C 3 10  ALA 10  10  10  ALA ALA L . n 
C 3 11  LEU 11  11  11  LEU LEU L . n 
C 3 12  SER 12  12  12  SER SER L . n 
C 3 13  ALA 13  13  13  ALA ALA L . n 
C 3 14  SER 14  14  14  SER SER L . n 
C 3 15  VAL 15  15  15  VAL VAL L . n 
C 3 16  GLY 16  16  16  GLY GLY L . n 
C 3 17  ASP 17  17  17  ASP ASP L . n 
C 3 18  ARG 18  18  18  ARG ARG L . n 
C 3 19  VAL 19  19  19  VAL VAL L . n 
C 3 20  THR 20  20  20  THR THR L . n 
C 3 21  ILE 21  21  21  ILE ILE L . n 
C 3 22  SER 22  22  22  SER SER L . n 
C 3 23  CYS 23  23  23  CYS CYS L . n 
C 3 24  ARG 24  24  24  ARG ARG L . n 
C 3 25  ALA 25  25  25  ALA ALA L . n 
C 3 26  SER 26  26  26  SER SER L . n 
C 3 27  GLN 27  27  27  GLN GLN L . n 
C 3 28  ASN 28  28  28  ASN ASN L . n 
C 3 29  ILE 29  29  29  ILE ILE L . n 
C 3 30  ASP 30  30  30  ASP ASP L . n 
C 3 31  GLY 31  31  31  GLY GLY L . n 
C 3 32  PHE 32  32  32  PHE PHE L . n 
C 3 33  LEU 33  33  33  LEU LEU L . n 
C 3 34  ALA 34  34  34  ALA ALA L . n 
C 3 35  TRP 35  35  35  TRP TRP L . n 
C 3 36  TYR 36  36  36  TYR TYR L . n 
C 3 37  GLN 37  37  37  GLN GLN L . n 
C 3 38  GLN 38  38  38  GLN GLN L . n 
C 3 39  LYS 39  39  39  LYS LYS L . n 
C 3 40  PRO 40  40  40  PRO PRO L . n 
C 3 41  GLY 41  41  41  GLY GLY L . n 
C 3 42  LYS 42  42  42  LYS LYS L . n 
C 3 43  ALA 43  43  43  ALA ALA L . n 
C 3 44  PRO 44  44  44  PRO PRO L . n 
C 3 45  LYS 45  45  45  LYS LYS L . n 
C 3 46  LEU 46  46  46  LEU LEU L . n 
C 3 47  LEU 47  47  47  LEU LEU L . n 
C 3 48  ILE 48  48  48  ILE ILE L . n 
C 3 49  TYR 49  49  49  TYR TYR L . n 
C 3 50  ALA 50  50  50  ALA ALA L . n 
C 3 51  ALA 51  51  51  ALA ALA L . n 
C 3 52  SER 52  52  52  SER SER L . n 
C 3 53  ARG 53  53  53  ARG ARG L . n 
C 3 54  LEU 54  54  54  LEU LEU L . n 
C 3 55  GLN 55  55  55  GLN GLN L . n 
C 3 56  SER 56  56  56  SER SER L . n 
C 3 57  GLY 57  57  57  GLY GLY L . n 
C 3 58  ILE 58  58  58  ILE ILE L . n 
C 3 59  PRO 59  59  59  PRO PRO L . n 
C 3 60  SER 60  60  60  SER SER L . n 
C 3 61  ARG 61  61  61  ARG ARG L . n 
C 3 62  PHE 62  62  62  PHE PHE L . n 
C 3 63  SER 63  63  63  SER SER L . n 
C 3 64  GLY 64  64  64  GLY GLY L . n 
C 3 65  SER 65  65  65  SER SER L . n 
C 3 66  GLY 66  66  66  GLY GLY L . n 
C 3 67  SER 67  67  67  SER SER L . n 
C 3 68  GLY 68  68  68  GLY GLY L . n 
C 3 69  THR 69  69  69  THR THR L . n 
C 3 70  ASP 70  70  70  ASP ASP L . n 
C 3 71  PHE 71  71  71  PHE PHE L . n 
C 3 72  THR 72  72  72  THR THR L . n 
C 3 73  LEU 73  73  73  LEU LEU L . n 
C 3 74  THR 74  74  74  THR THR L . n 
C 3 75  ILE 75  75  75  ILE ILE L . n 
C 3 76  SER 76  76  76  SER SER L . n 
C 3 77  SER 77  77  77  SER SER L . n 
C 3 78  LEU 78  78  78  LEU LEU L . n 
C 3 79  GLN 79  79  79  GLN GLN L . n 
C 3 80  PRO 80  80  80  PRO PRO L . n 
C 3 81  GLU 81  81  81  GLU GLU L . n 
C 3 82  ASP 82  82  82  ASP ASP L . n 
C 3 83  PHE 83  83  83  PHE PHE L . n 
C 3 84  ALA 84  84  84  ALA ALA L . n 
C 3 85  ALA 85  85  85  ALA ALA L . n 
C 3 86  TYR 86  86  86  TYR TYR L . n 
C 3 87  TYR 87  87  87  TYR TYR L . n 
C 3 88  CYS 88  88  88  CYS CYS L . n 
C 3 89  GLN 89  89  89  GLN GLN L . n 
C 3 90  GLN 90  90  90  GLN GLN L . n 
C 3 91  VAL 91  91  91  VAL VAL L . n 
C 3 92  TYR 92  92  92  TYR TYR L . n 
C 3 93  SER 93  93  93  SER SER L . n 
C 3 94  ALA 94  94  94  ALA ALA L . n 
C 3 95  PRO 95  95  95  PRO PRO L . n 
C 3 96  LEU 96  96  96  LEU LEU L . n 
C 3 97  THR 97  97  97  THR THR L . n 
C 3 98  PHE 98  98  98  PHE PHE L . n 
C 3 99  GLY 99  99  99  GLY GLY L . n 
C 3 100 GLY 100 100 100 GLY GLY L . n 
C 3 101 GLY 101 101 101 GLY GLY L . n 
C 3 102 THR 102 102 102 THR THR L . n 
C 3 103 LYS 103 103 103 LYS LYS L . n 
C 3 104 VAL 104 104 104 VAL VAL L . n 
C 3 105 GLU 105 105 105 GLU GLU L . n 
C 3 106 PHE 106 106 106 PHE PHE L . n 
C 3 107 LYS 107 107 107 LYS LYS L . n 
C 3 108 ARG 108 108 ?   ?   ?   L . n 
C 3 109 THR 109 109 ?   ?   ?   L . n 
C 3 110 VAL 110 110 ?   ?   ?   L . n 
C 3 111 ALA 111 111 ?   ?   ?   L . n 
C 3 112 ALA 112 112 ?   ?   ?   L . n 
C 3 113 PRO 113 113 ?   ?   ?   L . n 
C 3 114 SER 114 114 ?   ?   ?   L . n 
C 3 115 VAL 115 115 ?   ?   ?   L . n 
C 3 116 PHE 116 116 ?   ?   ?   L . n 
C 3 117 ILE 117 117 ?   ?   ?   L . n 
C 3 118 PHE 118 118 ?   ?   ?   L . n 
C 3 119 PRO 119 119 ?   ?   ?   L . n 
C 3 120 PRO 120 120 ?   ?   ?   L . n 
C 3 121 SER 121 121 ?   ?   ?   L . n 
C 3 122 ASP 122 122 ?   ?   ?   L . n 
C 3 123 GLU 123 123 ?   ?   ?   L . n 
C 3 124 GLN 124 124 ?   ?   ?   L . n 
C 3 125 LEU 125 125 ?   ?   ?   L . n 
C 3 126 LYS 126 126 ?   ?   ?   L . n 
C 3 127 SER 127 127 ?   ?   ?   L . n 
C 3 128 GLY 128 128 ?   ?   ?   L . n 
C 3 129 THR 129 129 ?   ?   ?   L . n 
C 3 130 ALA 130 130 ?   ?   ?   L . n 
C 3 131 SER 131 131 ?   ?   ?   L . n 
C 3 132 VAL 132 132 ?   ?   ?   L . n 
C 3 133 VAL 133 133 ?   ?   ?   L . n 
C 3 134 CYS 134 134 ?   ?   ?   L . n 
C 3 135 LEU 135 135 ?   ?   ?   L . n 
C 3 136 LEU 136 136 ?   ?   ?   L . n 
C 3 137 ASN 137 137 ?   ?   ?   L . n 
C 3 138 ASN 138 138 ?   ?   ?   L . n 
C 3 139 PHE 139 139 ?   ?   ?   L . n 
C 3 140 TYR 140 140 ?   ?   ?   L . n 
C 3 141 PRO 141 141 ?   ?   ?   L . n 
C 3 142 ARG 142 142 ?   ?   ?   L . n 
C 3 143 GLU 143 143 ?   ?   ?   L . n 
C 3 144 ALA 144 144 ?   ?   ?   L . n 
C 3 145 LYS 145 145 ?   ?   ?   L . n 
C 3 146 VAL 146 146 ?   ?   ?   L . n 
C 3 147 GLN 147 147 ?   ?   ?   L . n 
C 3 148 TRP 148 148 ?   ?   ?   L . n 
C 3 149 LYS 149 149 ?   ?   ?   L . n 
C 3 150 VAL 150 150 ?   ?   ?   L . n 
C 3 151 ASP 151 151 ?   ?   ?   L . n 
C 3 152 ASN 152 152 ?   ?   ?   L . n 
C 3 153 ALA 153 153 ?   ?   ?   L . n 
C 3 154 LEU 154 154 ?   ?   ?   L . n 
C 3 155 GLN 155 155 ?   ?   ?   L . n 
C 3 156 SER 156 156 ?   ?   ?   L . n 
C 3 157 GLY 157 157 ?   ?   ?   L . n 
C 3 158 ASN 158 158 ?   ?   ?   L . n 
C 3 159 SER 159 159 ?   ?   ?   L . n 
C 3 160 GLN 160 160 ?   ?   ?   L . n 
C 3 161 GLU 161 161 ?   ?   ?   L . n 
C 3 162 SER 162 162 ?   ?   ?   L . n 
C 3 163 VAL 163 163 ?   ?   ?   L . n 
C 3 164 THR 164 164 ?   ?   ?   L . n 
C 3 165 GLU 165 165 ?   ?   ?   L . n 
C 3 166 GLN 166 166 ?   ?   ?   L . n 
C 3 167 ASP 167 167 ?   ?   ?   L . n 
C 3 168 SER 168 168 ?   ?   ?   L . n 
C 3 169 LYS 169 169 ?   ?   ?   L . n 
C 3 170 ASP 170 170 ?   ?   ?   L . n 
C 3 171 SER 171 171 ?   ?   ?   L . n 
C 3 172 THR 172 172 ?   ?   ?   L . n 
C 3 173 TYR 173 173 ?   ?   ?   L . n 
C 3 174 SER 174 174 ?   ?   ?   L . n 
C 3 175 LEU 175 175 ?   ?   ?   L . n 
C 3 176 SER 176 176 ?   ?   ?   L . n 
C 3 177 SER 177 177 ?   ?   ?   L . n 
C 3 178 THR 178 178 ?   ?   ?   L . n 
C 3 179 LEU 179 179 ?   ?   ?   L . n 
C 3 180 THR 180 180 ?   ?   ?   L . n 
C 3 181 LEU 181 181 ?   ?   ?   L . n 
C 3 182 SER 182 182 ?   ?   ?   L . n 
C 3 183 LYS 183 183 ?   ?   ?   L . n 
C 3 184 ALA 184 184 ?   ?   ?   L . n 
C 3 185 ASP 185 185 ?   ?   ?   L . n 
C 3 186 TYR 186 186 ?   ?   ?   L . n 
C 3 187 GLU 187 187 ?   ?   ?   L . n 
C 3 188 LYS 188 188 ?   ?   ?   L . n 
C 3 189 HIS 189 189 ?   ?   ?   L . n 
C 3 190 LYS 190 190 ?   ?   ?   L . n 
C 3 191 VAL 191 191 ?   ?   ?   L . n 
C 3 192 TYR 192 192 ?   ?   ?   L . n 
C 3 193 ALA 193 193 ?   ?   ?   L . n 
C 3 194 CYS 194 194 ?   ?   ?   L . n 
C 3 195 GLU 195 195 ?   ?   ?   L . n 
C 3 196 VAL 196 196 ?   ?   ?   L . n 
C 3 197 THR 197 197 ?   ?   ?   L . n 
C 3 198 HIS 198 198 ?   ?   ?   L . n 
C 3 199 GLN 199 199 ?   ?   ?   L . n 
C 3 200 GLY 200 200 ?   ?   ?   L . n 
C 3 201 LEU 201 201 ?   ?   ?   L . n 
C 3 202 SER 202 202 ?   ?   ?   L . n 
C 3 203 SER 203 203 ?   ?   ?   L . n 
C 3 204 PRO 204 204 ?   ?   ?   L . n 
C 3 205 VAL 205 205 ?   ?   ?   L . n 
C 3 206 THR 206 206 ?   ?   ?   L . n 
C 3 207 LYS 207 207 ?   ?   ?   L . n 
C 3 208 SER 208 208 ?   ?   ?   L . n 
C 3 209 PHE 209 209 ?   ?   ?   L . n 
C 3 210 ASN 210 210 ?   ?   ?   L . n 
C 3 211 ARG 211 211 ?   ?   ?   L . n 
C 3 212 GLY 212 212 ?   ?   ?   L . n 
C 3 213 GLU 213 213 ?   ?   ?   L . n 
C 3 214 CYS 214 214 ?   ?   ?   L . n 
# 
_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                     8P5M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         8P5M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_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                   8P5M 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 8P5M 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.006 ? 3342 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 1.025 ? 4541 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 4.642 ? 463  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.069 ? 487  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.007 ? 591  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     8P5M 
_struct.title                        'SARS-CoV-2 Spike RBD in complex with Mab-23 (Fab)' 
_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        8P5M 
_struct_keywords.text            'Antibody, Spike, Complex, VIRAL PROTEIN' 
_struct_keywords.pdbx_keywords   'VIRAL 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 SPIKE_SARS2 P0DTC2 ? 1 
;TNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAP
GQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPL
QSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPK
;
333 
2 PDB 8P5M        8P5M   ? 2 ? 1   
3 PDB 8P5M        8P5M   ? 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 8P5M I 1 ? 196 ? P0DTC2 333 ? 528 ? 333 528 
2 2 8P5M G 1 ? 442 ? 8P5M   1   ? 442 ? 1   442 
3 3 8P5M L 1 ? 214 ? 8P5M   1   ? 214 ? 1   214 
# 
_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   ? 
_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 PRO A 5  ? ASN A 11 ? PRO I 337 ASN I 343 1 ? 7 
HELX_P HELX_P2 AA2 ASP A 32 ? ALA A 40 ? ASP I 364 ALA I 372 1 ? 9 
HELX_P HELX_P3 AA3 ASP A 73 ? ARG A 76 ? ASP I 405 ARG I 408 5 ? 4 
HELX_P HELX_P4 AA4 GLY A 84 ? ASN A 90 ? GLY I 416 ASN I 422 1 ? 7 
HELX_P HELX_P5 AA5 LYS B 87 ? THR B 91 ? LYS G 87  THR G 91  5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 4   SG ? ? ? 1_555 A CYS 29  SG ? ? I CYS 336 I CYS 361 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf2 disulf ? ? A CYS 47  SG ? ? ? 1_555 A CYS 100 SG ? ? I CYS 379 I CYS 432 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf3 disulf ? ? A CYS 59  SG ? ? ? 1_555 A CYS 193 SG ? ? I CYS 391 I CYS 525 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
disulf4 disulf ? ? A CYS 148 SG ? ? ? 1_555 A CYS 156 SG ? ? I CYS 480 I CYS 488 1_555 ? ? ? ? ? ? ? 2.024 ? ? 
disulf5 disulf ? ? B CYS 22  SG ? ? ? 1_555 B CYS 96  SG ? ? G CYS 22  G CYS 96  1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf6 disulf ? ? C CYS 23  SG ? ? ? 1_555 C CYS 88  SG ? ? L CYS 23  L CYS 88  1_555 ? ? ? ? ? ? ? 2.029 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          SER 
_struct_mon_prot_cis.label_seq_id           7 
_struct_mon_prot_cis.label_asym_id          C 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           SER 
_struct_mon_prot_cis.auth_seq_id            7 
_struct_mon_prot_cis.auth_asym_id           L 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    8 
_struct_mon_prot_cis.pdbx_label_asym_id_2   C 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     8 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    L 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       4.88 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 6 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 2 ? 
AA9 ? 5 ? 
AB1 ? 5 ? 
# 
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 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? 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 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? parallel      
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AA9 4 5 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB1 4 5 ? 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 ASN A 22  ? ILE A 26  ? ASN I 354 ILE I 358 
AA1 2 ASN A 62  ? ARG A 71  ? ASN I 394 ARG I 403 
AA1 3 PRO A 175 ? GLU A 184 ? PRO I 507 GLU I 516 
AA1 4 GLY A 99  ? ASN A 105 ? GLY I 431 ASN I 437 
AA1 5 THR A 44  ? TYR A 48  ? THR I 376 TYR I 380 
AA2 1 TYR A 121 ? ARG A 122 ? TYR I 453 ARG I 454 
AA2 2 LEU A 160 ? GLN A 161 ? LEU I 492 GLN I 493 
AA3 1 TYR A 141 ? GLN A 142 ? TYR I 473 GLN I 474 
AA3 2 CYS A 156 ? TYR A 157 ? CYS I 488 TYR I 489 
AA4 1 GLN B 3   ? SER B 7   ? GLN G 3   SER G 7   
AA4 2 LEU B 18  ? SER B 25  ? LEU G 18  SER G 25  
AA4 3 MET B 78  ? MET B 83  ? MET G 78  MET G 83  
AA4 4 PHE B 68  ? ASP B 73  ? PHE G 68  ASP G 73  
AA5 1 LEU B 11  ? VAL B 12  ? LEU G 11  VAL G 12  
AA5 2 VAL B 111 ? VAL B 115 ? VAL G 111 VAL G 115 
AA5 3 ALA B 92  ? ARG B 98  ? ALA G 92  ARG G 98  
AA5 4 PHE B 34  ? GLN B 39  ? PHE G 34  GLN G 39  
AA5 5 LEU B 45  ? ILE B 51  ? LEU G 45  ILE G 51  
AA5 6 LYS B 58  ? TYR B 60  ? LYS G 58  TYR G 60  
AA6 1 LEU B 11  ? VAL B 12  ? LEU G 11  VAL G 12  
AA6 2 VAL B 111 ? VAL B 115 ? VAL G 111 VAL G 115 
AA6 3 ALA B 92  ? ARG B 98  ? ALA G 92  ARG G 98  
AA6 4 SER B 106 ? TRP B 107 ? SER G 106 TRP G 107 
AA7 1 MET C 4   ? SER C 7   ? MET L 4   SER L 7   
AA7 2 VAL C 19  ? ALA C 25  ? VAL L 19  ALA L 25  
AA7 3 ASP C 70  ? ILE C 75  ? ASP L 70  ILE L 75  
AA7 4 PHE C 62  ? SER C 67  ? PHE L 62  SER L 67  
AA8 1 SER C 12  ? ALA C 13  ? SER L 12  ALA L 13  
AA8 2 GLU C 105 ? PHE C 106 ? GLU L 105 PHE L 106 
AA9 1 ARG C 53  ? LEU C 54  ? ARG L 53  LEU L 54  
AA9 2 LYS C 45  ? TYR C 49  ? LYS L 45  TYR L 49  
AA9 3 LEU C 33  ? GLN C 38  ? LEU L 33  GLN L 38  
AA9 4 ALA C 85  ? GLN C 90  ? ALA L 85  GLN L 90  
AA9 5 THR C 97  ? PHE C 98  ? THR L 97  PHE L 98  
AB1 1 ARG C 53  ? LEU C 54  ? ARG L 53  LEU L 54  
AB1 2 LYS C 45  ? TYR C 49  ? LYS L 45  TYR L 49  
AB1 3 LEU C 33  ? GLN C 38  ? LEU L 33  GLN L 38  
AB1 4 ALA C 85  ? GLN C 90  ? ALA L 85  GLN L 90  
AB1 5 THR C 102 ? LYS C 103 ? THR L 102 LYS L 103 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 26  ? N ILE I 358 O VAL A 63  ? O VAL I 395 
AA1 2 3 N PHE A 68  ? N PHE I 400 O VAL A 178 ? O VAL I 510 
AA1 3 4 O VAL A 179 ? O VAL I 511 N ILE A 102 ? N ILE I 434 
AA1 4 5 O GLY A 99  ? O GLY I 431 N TYR A 48  ? N TYR I 380 
AA2 1 2 N TYR A 121 ? N TYR I 453 O GLN A 161 ? O GLN I 493 
AA3 1 2 N TYR A 141 ? N TYR I 473 O TYR A 157 ? O TYR I 489 
AA4 1 2 N GLN B 3   ? N GLN G 3   O SER B 25  ? O SER G 25  
AA4 2 3 N CYS B 22  ? N CYS G 22  O VAL B 79  ? O VAL G 79  
AA4 3 4 O GLN B 82  ? O GLN G 82  N THR B 69  ? N THR G 69  
AA5 1 2 N VAL B 12  ? N VAL G 12  O THR B 114 ? O THR G 114 
AA5 2 3 O VAL B 111 ? O VAL G 111 N TYR B 94  ? N TYR G 94  
AA5 3 4 O TYR B 95  ? O TYR G 95  N VAL B 37  ? N VAL G 37  
AA5 4 5 N TRP B 36  ? N TRP G 36  O VAL B 48  ? O VAL G 48  
AA5 5 6 N ILE B 50  ? N ILE G 50  O HIS B 59  ? O HIS G 59  
AA6 1 2 N VAL B 12  ? N VAL G 12  O THR B 114 ? O THR G 114 
AA6 2 3 O VAL B 111 ? O VAL G 111 N TYR B 94  ? N TYR G 94  
AA6 3 4 N ARG B 98  ? N ARG G 98  O SER B 106 ? O SER G 106 
AA7 1 2 N THR C 5   ? N THR L 5   O ARG C 24  ? O ARG L 24  
AA7 2 3 N ILE C 21  ? N ILE L 21  O LEU C 73  ? O LEU L 73  
AA7 3 4 O THR C 74  ? O THR L 74  N SER C 63  ? N SER L 63  
AA8 1 2 N ALA C 13  ? N ALA L 13  O GLU C 105 ? O GLU L 105 
AA9 1 2 O ARG C 53  ? O ARG L 53  N TYR C 49  ? N TYR L 49  
AA9 2 3 O LYS C 45  ? O LYS L 45  N GLN C 37  ? N GLN L 37  
AA9 3 4 N TYR C 36  ? N TYR L 36  O TYR C 87  ? O TYR L 87  
AA9 4 5 N GLN C 90  ? N GLN L 90  O THR C 97  ? O THR L 97  
AB1 1 2 O ARG C 53  ? O ARG L 53  N TYR C 49  ? N TYR L 49  
AB1 2 3 O LYS C 45  ? O LYS L 45  N GLN C 37  ? N GLN L 37  
AB1 3 4 N TYR C 36  ? N TYR L 36  O TYR C 87  ? O TYR L 87  
AB1 4 5 N TYR C 86  ? N TYR L 86  O THR C 102 ? O THR L 102 
# 
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 I 352 ? ? -97.19  57.67   
2 1 ASP I 442 ? ? -102.05 55.18   
3 1 ASP G 66  ? ? 80.00   -2.41   
4 1 ASP L 30  ? ? 57.34   -130.23 
5 1 ALA L 51  ? ? 72.58   -46.50  
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8P5M 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      OTHER 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  7KSG 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                7KSG 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    8P5M 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.8 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               135612 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7.4 
# 
loop_
_em_entity_assembly.id 
_em_entity_assembly.parent_id 
_em_entity_assembly.source 
_em_entity_assembly.type 
_em_entity_assembly.name 
_em_entity_assembly.details 
_em_entity_assembly.synonym 
_em_entity_assembly.oligomeric_details 
_em_entity_assembly.entity_id_list 
1 0 'MULTIPLE SOURCES' COMPLEX 'Spike RBD (two molecules) in complex with two FU2 nanobodies' ? ? ? '1, 2' 
2 1 RECOMBINANT        COMPLEX 'SARS-CoV-2 spike (RBD)'                                       ? ? ? 1      
3 1 RECOMBINANT        COMPLEX 'Monoclonal Antibody Mab-23'                                   ? ? ? '2, 3' 
# 
_em_imaging.entry_id                        8P5M 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      2.7 
_em_imaging.nominal_defocus_min             300 
_em_imaging.nominal_defocus_max             2500 
_em_imaging.calibrated_defocus_min          300 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           165000 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             'ZEMLIN TABLEAU' 
_em_imaging.c2_aperture_diameter            20 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         NITROGEN 
# 
_em_vitrification.entry_id              8P5M 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8P5M 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      2 
# 
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 I LYS 528 ? A LYS 196 
2   1 Y 1 G ALA 118 ? B ALA 118 
3   1 Y 1 G SER 119 ? B SER 119 
4   1 Y 1 G THR 120 ? B THR 120 
5   1 Y 1 G LYS 121 ? B LYS 121 
6   1 Y 1 G GLY 122 ? B GLY 122 
7   1 Y 1 G PRO 123 ? B PRO 123 
8   1 Y 1 G SER 124 ? B SER 124 
9   1 Y 1 G VAL 125 ? B VAL 125 
10  1 Y 1 G PHE 126 ? B PHE 126 
11  1 Y 1 G PRO 127 ? B PRO 127 
12  1 Y 1 G LEU 128 ? B LEU 128 
13  1 Y 1 G ALA 129 ? B ALA 129 
14  1 Y 1 G PRO 130 ? B PRO 130 
15  1 Y 1 G SER 131 ? B SER 131 
16  1 Y 1 G SER 132 ? B SER 132 
17  1 Y 1 G LYS 133 ? B LYS 133 
18  1 Y 1 G SER 134 ? B SER 134 
19  1 Y 1 G THR 135 ? B THR 135 
20  1 Y 1 G SER 136 ? B SER 136 
21  1 Y 1 G GLY 137 ? B GLY 137 
22  1 Y 1 G GLY 138 ? B GLY 138 
23  1 Y 1 G THR 139 ? B THR 139 
24  1 Y 1 G ALA 140 ? B ALA 140 
25  1 Y 1 G ALA 141 ? B ALA 141 
26  1 Y 1 G LEU 142 ? B LEU 142 
27  1 Y 1 G GLY 143 ? B GLY 143 
28  1 Y 1 G LEU 144 ? B LEU 144 
29  1 Y 1 G VAL 145 ? B VAL 145 
30  1 Y 1 G LYS 146 ? B LYS 146 
31  1 Y 1 G ASP 147 ? B ASP 147 
32  1 Y 1 G TYR 148 ? B TYR 148 
33  1 Y 1 G PHE 149 ? B PHE 149 
34  1 Y 1 G PRO 150 ? B PRO 150 
35  1 Y 1 G GLU 151 ? B GLU 151 
36  1 Y 1 G VAL 152 ? B VAL 152 
37  1 Y 1 G THR 153 ? B THR 153 
38  1 Y 1 G SER 154 ? B SER 154 
39  1 Y 1 G TRP 155 ? B TRP 155 
40  1 Y 1 G ASN 156 ? B ASN 156 
41  1 Y 1 G SER 157 ? B SER 157 
42  1 Y 1 G GLY 158 ? B GLY 158 
43  1 Y 1 G ALA 159 ? B ALA 159 
44  1 Y 1 G LEU 160 ? B LEU 160 
45  1 Y 1 G THR 161 ? B THR 161 
46  1 Y 1 G SER 162 ? B SER 162 
47  1 Y 1 G GLY 163 ? B GLY 163 
48  1 Y 1 G VAL 164 ? B VAL 164 
49  1 Y 1 G HIS 165 ? B HIS 165 
50  1 Y 1 G THR 166 ? B THR 166 
51  1 Y 1 G PHE 167 ? B PHE 167 
52  1 Y 1 G PRO 168 ? B PRO 168 
53  1 Y 1 G ALA 169 ? B ALA 169 
54  1 Y 1 G VAL 170 ? B VAL 170 
55  1 Y 1 G LEU 171 ? B LEU 171 
56  1 Y 1 G GLN 172 ? B GLN 172 
57  1 Y 1 G SER 173 ? B SER 173 
58  1 Y 1 G SER 174 ? B SER 174 
59  1 Y 1 G GLY 175 ? B GLY 175 
60  1 Y 1 G LEU 176 ? B LEU 176 
61  1 Y 1 G TYR 177 ? B TYR 177 
62  1 Y 1 G SER 178 ? B SER 178 
63  1 Y 1 G LEU 179 ? B LEU 179 
64  1 Y 1 G SER 180 ? B SER 180 
65  1 Y 1 G SER 181 ? B SER 181 
66  1 Y 1 G VAL 182 ? B VAL 182 
67  1 Y 1 G VAL 183 ? B VAL 183 
68  1 Y 1 G THR 184 ? B THR 184 
69  1 Y 1 G VAL 185 ? B VAL 185 
70  1 Y 1 G PRO 186 ? B PRO 186 
71  1 Y 1 G SER 187 ? B SER 187 
72  1 Y 1 G SER 188 ? B SER 188 
73  1 Y 1 G SER 189 ? B SER 189 
74  1 Y 1 G LEU 190 ? B LEU 190 
75  1 Y 1 G GLY 191 ? B GLY 191 
76  1 Y 1 G THR 192 ? B THR 192 
77  1 Y 1 G GLN 193 ? B GLN 193 
78  1 Y 1 G THR 194 ? B THR 194 
79  1 Y 1 G TYR 195 ? B TYR 195 
80  1 Y 1 G ILE 196 ? B ILE 196 
81  1 Y 1 G CYS 197 ? B CYS 197 
82  1 Y 1 G ASN 198 ? B ASN 198 
83  1 Y 1 G VAL 199 ? B VAL 199 
84  1 Y 1 G ASN 200 ? B ASN 200 
85  1 Y 1 G HIS 201 ? B HIS 201 
86  1 Y 1 G LYS 202 ? B LYS 202 
87  1 Y 1 G PRO 203 ? B PRO 203 
88  1 Y 1 G SER 204 ? B SER 204 
89  1 Y 1 G ASN 205 ? B ASN 205 
90  1 Y 1 G THR 206 ? B THR 206 
91  1 Y 1 G LYS 207 ? B LYS 207 
92  1 Y 1 G VAL 208 ? B VAL 208 
93  1 Y 1 G ASP 209 ? B ASP 209 
94  1 Y 1 G LYS 210 ? B LYS 210 
95  1 Y 1 G VAL 211 ? B VAL 211 
96  1 Y 1 G GLU 212 ? B GLU 212 
97  1 Y 1 G PRO 213 ? B PRO 213 
98  1 Y 1 G LYS 214 ? B LYS 214 
99  1 Y 1 G SER 215 ? B SER 215 
100 1 Y 1 G CYS 216 ? B CYS 216 
101 1 Y 1 G ASP 217 ? B ASP 217 
102 1 Y 1 G LYS 218 ? B LYS 218 
103 1 Y 1 G THR 219 ? B THR 219 
104 1 Y 1 G HIS 220 ? B HIS 220 
105 1 Y 1 G THR 221 ? B THR 221 
106 1 Y 1 G CYS 222 ? B CYS 222 
107 1 Y 1 G PRO 223 ? B PRO 223 
108 1 Y 1 G PRO 224 ? B PRO 224 
109 1 Y 1 G CYS 225 ? B CYS 225 
110 1 Y 1 G PRO 226 ? B PRO 226 
111 1 Y 1 G ALA 227 ? B ALA 227 
112 1 Y 1 G PRO 228 ? B PRO 228 
113 1 Y 1 G GLU 229 ? B GLU 229 
114 1 Y 1 G LEU 230 ? B LEU 230 
115 1 Y 1 G LEU 231 ? B LEU 231 
116 1 Y 1 G GLY 232 ? B GLY 232 
117 1 Y 1 G GLY 233 ? B GLY 233 
118 1 Y 1 G PRO 234 ? B PRO 234 
119 1 Y 1 G SER 235 ? B SER 235 
120 1 Y 1 G VAL 236 ? B VAL 236 
121 1 Y 1 G PHE 237 ? B PHE 237 
122 1 Y 1 G LEU 238 ? B LEU 238 
123 1 Y 1 G PHE 239 ? B PHE 239 
124 1 Y 1 G PRO 240 ? B PRO 240 
125 1 Y 1 G PRO 241 ? B PRO 241 
126 1 Y 1 G LYS 242 ? B LYS 242 
127 1 Y 1 G PRO 243 ? B PRO 243 
128 1 Y 1 G LYS 244 ? B LYS 244 
129 1 Y 1 G ASP 245 ? B ASP 245 
130 1 Y 1 G THR 246 ? B THR 246 
131 1 Y 1 G LEU 247 ? B LEU 247 
132 1 Y 1 G MET 248 ? B MET 248 
133 1 Y 1 G ILE 249 ? B ILE 249 
134 1 Y 1 G SER 250 ? B SER 250 
135 1 Y 1 G ARG 251 ? B ARG 251 
136 1 Y 1 G THR 252 ? B THR 252 
137 1 Y 1 G PRO 253 ? B PRO 253 
138 1 Y 1 G GLU 254 ? B GLU 254 
139 1 Y 1 G VAL 255 ? B VAL 255 
140 1 Y 1 G THR 256 ? B THR 256 
141 1 Y 1 G CYS 257 ? B CYS 257 
142 1 Y 1 G VAL 258 ? B VAL 258 
143 1 Y 1 G VAL 259 ? B VAL 259 
144 1 Y 1 G VAL 260 ? B VAL 260 
145 1 Y 1 G ASP 261 ? B ASP 261 
146 1 Y 1 G VAL 262 ? B VAL 262 
147 1 Y 1 G SER 263 ? B SER 263 
148 1 Y 1 G HIS 264 ? B HIS 264 
149 1 Y 1 G GLU 265 ? B GLU 265 
150 1 Y 1 G ASP 266 ? B ASP 266 
151 1 Y 1 G PRO 267 ? B PRO 267 
152 1 Y 1 G GLU 268 ? B GLU 268 
153 1 Y 1 G VAL 269 ? B VAL 269 
154 1 Y 1 G LYS 270 ? B LYS 270 
155 1 Y 1 G PHE 271 ? B PHE 271 
156 1 Y 1 G ASN 272 ? B ASN 272 
157 1 Y 1 G TRP 273 ? B TRP 273 
158 1 Y 1 G TYR 274 ? B TYR 274 
159 1 Y 1 G VAL 275 ? B VAL 275 
160 1 Y 1 G ASP 276 ? B ASP 276 
161 1 Y 1 G GLY 277 ? B GLY 277 
162 1 Y 1 G VAL 278 ? B VAL 278 
163 1 Y 1 G GLU 279 ? B GLU 279 
164 1 Y 1 G VAL 280 ? B VAL 280 
165 1 Y 1 G HIS 281 ? B HIS 281 
166 1 Y 1 G ASN 282 ? B ASN 282 
167 1 Y 1 G ALA 283 ? B ALA 283 
168 1 Y 1 G LYS 284 ? B LYS 284 
169 1 Y 1 G THR 285 ? B THR 285 
170 1 Y 1 G LYS 286 ? B LYS 286 
171 1 Y 1 G PRO 287 ? B PRO 287 
172 1 Y 1 G ARG 288 ? B ARG 288 
173 1 Y 1 G GLU 289 ? B GLU 289 
174 1 Y 1 G GLU 290 ? B GLU 290 
175 1 Y 1 G GLN 291 ? B GLN 291 
176 1 Y 1 G TYR 292 ? B TYR 292 
177 1 Y 1 G ASN 293 ? B ASN 293 
178 1 Y 1 G SER 294 ? B SER 294 
179 1 Y 1 G THR 295 ? B THR 295 
180 1 Y 1 G TYR 296 ? B TYR 296 
181 1 Y 1 G ARG 297 ? B ARG 297 
182 1 Y 1 G VAL 298 ? B VAL 298 
183 1 Y 1 G VAL 299 ? B VAL 299 
184 1 Y 1 G SER 300 ? B SER 300 
185 1 Y 1 G VAL 301 ? B VAL 301 
186 1 Y 1 G LEU 302 ? B LEU 302 
187 1 Y 1 G THR 303 ? B THR 303 
188 1 Y 1 G VAL 304 ? B VAL 304 
189 1 Y 1 G LEU 305 ? B LEU 305 
190 1 Y 1 G HIS 306 ? B HIS 306 
191 1 Y 1 G GLN 307 ? B GLN 307 
192 1 Y 1 G ASP 308 ? B ASP 308 
193 1 Y 1 G TRP 309 ? B TRP 309 
194 1 Y 1 G LEU 310 ? B LEU 310 
195 1 Y 1 G ASN 311 ? B ASN 311 
196 1 Y 1 G GLY 312 ? B GLY 312 
197 1 Y 1 G LYS 313 ? B LYS 313 
198 1 Y 1 G GLU 314 ? B GLU 314 
199 1 Y 1 G TYR 315 ? B TYR 315 
200 1 Y 1 G LYS 316 ? B LYS 316 
201 1 Y 1 G CYS 317 ? B CYS 317 
202 1 Y 1 G LYS 318 ? B LYS 318 
203 1 Y 1 G VAL 319 ? B VAL 319 
204 1 Y 1 G SER 320 ? B SER 320 
205 1 Y 1 G ASN 321 ? B ASN 321 
206 1 Y 1 G LYS 322 ? B LYS 322 
207 1 Y 1 G ALA 323 ? B ALA 323 
208 1 Y 1 G LEU 324 ? B LEU 324 
209 1 Y 1 G PRO 325 ? B PRO 325 
210 1 Y 1 G ALA 326 ? B ALA 326 
211 1 Y 1 G PRO 327 ? B PRO 327 
212 1 Y 1 G ILE 328 ? B ILE 328 
213 1 Y 1 G GLU 329 ? B GLU 329 
214 1 Y 1 G LYS 330 ? B LYS 330 
215 1 Y 1 G THR 331 ? B THR 331 
216 1 Y 1 G ILE 332 ? B ILE 332 
217 1 Y 1 G SER 333 ? B SER 333 
218 1 Y 1 G LYS 334 ? B LYS 334 
219 1 Y 1 G ALA 335 ? B ALA 335 
220 1 Y 1 G LYS 336 ? B LYS 336 
221 1 Y 1 G GLY 337 ? B GLY 337 
222 1 Y 1 G GLN 338 ? B GLN 338 
223 1 Y 1 G PRO 339 ? B PRO 339 
224 1 Y 1 G ARG 340 ? B ARG 340 
225 1 Y 1 G GLU 341 ? B GLU 341 
226 1 Y 1 G PRO 342 ? B PRO 342 
227 1 Y 1 G GLN 343 ? B GLN 343 
228 1 Y 1 G VAL 344 ? B VAL 344 
229 1 Y 1 G TYR 345 ? B TYR 345 
230 1 Y 1 G THR 346 ? B THR 346 
231 1 Y 1 G LEU 347 ? B LEU 347 
232 1 Y 1 G PRO 348 ? B PRO 348 
233 1 Y 1 G PRO 349 ? B PRO 349 
234 1 Y 1 G SER 350 ? B SER 350 
235 1 Y 1 G ARG 351 ? B ARG 351 
236 1 Y 1 G ASP 352 ? B ASP 352 
237 1 Y 1 G GLU 353 ? B GLU 353 
238 1 Y 1 G THR 354 ? B THR 354 
239 1 Y 1 G LYS 355 ? B LYS 355 
240 1 Y 1 G ASN 356 ? B ASN 356 
241 1 Y 1 G GLN 357 ? B GLN 357 
242 1 Y 1 G VAL 358 ? B VAL 358 
243 1 Y 1 G SER 359 ? B SER 359 
244 1 Y 1 G LEU 360 ? B LEU 360 
245 1 Y 1 G THR 361 ? B THR 361 
246 1 Y 1 G CYS 362 ? B CYS 362 
247 1 Y 1 G LEU 363 ? B LEU 363 
248 1 Y 1 G VAL 364 ? B VAL 364 
249 1 Y 1 G LYS 365 ? B LYS 365 
250 1 Y 1 G GLY 366 ? B GLY 366 
251 1 Y 1 G PHE 367 ? B PHE 367 
252 1 Y 1 G TYR 368 ? B TYR 368 
253 1 Y 1 G PRO 369 ? B PRO 369 
254 1 Y 1 G SER 370 ? B SER 370 
255 1 Y 1 G ASP 371 ? B ASP 371 
256 1 Y 1 G ILE 372 ? B ILE 372 
257 1 Y 1 G ALA 373 ? B ALA 373 
258 1 Y 1 G VAL 374 ? B VAL 374 
259 1 Y 1 G GLU 375 ? B GLU 375 
260 1 Y 1 G TRP 376 ? B TRP 376 
261 1 Y 1 G GLU 377 ? B GLU 377 
262 1 Y 1 G SER 378 ? B SER 378 
263 1 Y 1 G ASN 379 ? B ASN 379 
264 1 Y 1 G GLY 380 ? B GLY 380 
265 1 Y 1 G GLN 381 ? B GLN 381 
266 1 Y 1 G PRO 382 ? B PRO 382 
267 1 Y 1 G GLU 383 ? B GLU 383 
268 1 Y 1 G ASN 384 ? B ASN 384 
269 1 Y 1 G ASN 385 ? B ASN 385 
270 1 Y 1 G TYR 386 ? B TYR 386 
271 1 Y 1 G LYS 387 ? B LYS 387 
272 1 Y 1 G THR 388 ? B THR 388 
273 1 Y 1 G THR 389 ? B THR 389 
274 1 Y 1 G PRO 390 ? B PRO 390 
275 1 Y 1 G PRO 391 ? B PRO 391 
276 1 Y 1 G VAL 392 ? B VAL 392 
277 1 Y 1 G LEU 393 ? B LEU 393 
278 1 Y 1 G ASP 394 ? B ASP 394 
279 1 Y 1 G SER 395 ? B SER 395 
280 1 Y 1 G ASP 396 ? B ASP 396 
281 1 Y 1 G GLY 397 ? B GLY 397 
282 1 Y 1 G SER 398 ? B SER 398 
283 1 Y 1 G PHE 399 ? B PHE 399 
284 1 Y 1 G PHE 400 ? B PHE 400 
285 1 Y 1 G LEU 401 ? B LEU 401 
286 1 Y 1 G TYR 402 ? B TYR 402 
287 1 Y 1 G SER 403 ? B SER 403 
288 1 Y 1 G LYS 404 ? B LYS 404 
289 1 Y 1 G LEU 405 ? B LEU 405 
290 1 Y 1 G THR 406 ? B THR 406 
291 1 Y 1 G VAL 407 ? B VAL 407 
292 1 Y 1 G ASP 408 ? B ASP 408 
293 1 Y 1 G LYS 409 ? B LYS 409 
294 1 Y 1 G SER 410 ? B SER 410 
295 1 Y 1 G ARG 411 ? B ARG 411 
296 1 Y 1 G TRP 412 ? B TRP 412 
297 1 Y 1 G GLN 413 ? B GLN 413 
298 1 Y 1 G GLN 414 ? B GLN 414 
299 1 Y 1 G GLY 415 ? B GLY 415 
300 1 Y 1 G ASN 416 ? B ASN 416 
301 1 Y 1 G VAL 417 ? B VAL 417 
302 1 Y 1 G PHE 418 ? B PHE 418 
303 1 Y 1 G SER 419 ? B SER 419 
304 1 Y 1 G CYS 420 ? B CYS 420 
305 1 Y 1 G SER 421 ? B SER 421 
306 1 Y 1 G VAL 422 ? B VAL 422 
307 1 Y 1 G MET 423 ? B MET 423 
308 1 Y 1 G HIS 424 ? B HIS 424 
309 1 Y 1 G GLU 425 ? B GLU 425 
310 1 Y 1 G ALA 426 ? B ALA 426 
311 1 Y 1 G LEU 427 ? B LEU 427 
312 1 Y 1 G HIS 428 ? B HIS 428 
313 1 Y 1 G ASN 429 ? B ASN 429 
314 1 Y 1 G HIS 430 ? B HIS 430 
315 1 Y 1 G TYR 431 ? B TYR 431 
316 1 Y 1 G THR 432 ? B THR 432 
317 1 Y 1 G GLN 433 ? B GLN 433 
318 1 Y 1 G LYS 434 ? B LYS 434 
319 1 Y 1 G SER 435 ? B SER 435 
320 1 Y 1 G LEU 436 ? B LEU 436 
321 1 Y 1 G SER 437 ? B SER 437 
322 1 Y 1 G LEU 438 ? B LEU 438 
323 1 Y 1 G SER 439 ? B SER 439 
324 1 Y 1 G PRO 440 ? B PRO 440 
325 1 Y 1 G GLY 441 ? B GLY 441 
326 1 Y 1 G LYS 442 ? B LYS 442 
327 1 Y 1 L ARG 108 ? C ARG 108 
328 1 Y 1 L THR 109 ? C THR 109 
329 1 Y 1 L VAL 110 ? C VAL 110 
330 1 Y 1 L ALA 111 ? C ALA 111 
331 1 Y 1 L ALA 112 ? C ALA 112 
332 1 Y 1 L PRO 113 ? C PRO 113 
333 1 Y 1 L SER 114 ? C SER 114 
334 1 Y 1 L VAL 115 ? C VAL 115 
335 1 Y 1 L PHE 116 ? C PHE 116 
336 1 Y 1 L ILE 117 ? C ILE 117 
337 1 Y 1 L PHE 118 ? C PHE 118 
338 1 Y 1 L PRO 119 ? C PRO 119 
339 1 Y 1 L PRO 120 ? C PRO 120 
340 1 Y 1 L SER 121 ? C SER 121 
341 1 Y 1 L ASP 122 ? C ASP 122 
342 1 Y 1 L GLU 123 ? C GLU 123 
343 1 Y 1 L GLN 124 ? C GLN 124 
344 1 Y 1 L LEU 125 ? C LEU 125 
345 1 Y 1 L LYS 126 ? C LYS 126 
346 1 Y 1 L SER 127 ? C SER 127 
347 1 Y 1 L GLY 128 ? C GLY 128 
348 1 Y 1 L THR 129 ? C THR 129 
349 1 Y 1 L ALA 130 ? C ALA 130 
350 1 Y 1 L SER 131 ? C SER 131 
351 1 Y 1 L VAL 132 ? C VAL 132 
352 1 Y 1 L VAL 133 ? C VAL 133 
353 1 Y 1 L CYS 134 ? C CYS 134 
354 1 Y 1 L LEU 135 ? C LEU 135 
355 1 Y 1 L LEU 136 ? C LEU 136 
356 1 Y 1 L ASN 137 ? C ASN 137 
357 1 Y 1 L ASN 138 ? C ASN 138 
358 1 Y 1 L PHE 139 ? C PHE 139 
359 1 Y 1 L TYR 140 ? C TYR 140 
360 1 Y 1 L PRO 141 ? C PRO 141 
361 1 Y 1 L ARG 142 ? C ARG 142 
362 1 Y 1 L GLU 143 ? C GLU 143 
363 1 Y 1 L ALA 144 ? C ALA 144 
364 1 Y 1 L LYS 145 ? C LYS 145 
365 1 Y 1 L VAL 146 ? C VAL 146 
366 1 Y 1 L GLN 147 ? C GLN 147 
367 1 Y 1 L TRP 148 ? C TRP 148 
368 1 Y 1 L LYS 149 ? C LYS 149 
369 1 Y 1 L VAL 150 ? C VAL 150 
370 1 Y 1 L ASP 151 ? C ASP 151 
371 1 Y 1 L ASN 152 ? C ASN 152 
372 1 Y 1 L ALA 153 ? C ALA 153 
373 1 Y 1 L LEU 154 ? C LEU 154 
374 1 Y 1 L GLN 155 ? C GLN 155 
375 1 Y 1 L SER 156 ? C SER 156 
376 1 Y 1 L GLY 157 ? C GLY 157 
377 1 Y 1 L ASN 158 ? C ASN 158 
378 1 Y 1 L SER 159 ? C SER 159 
379 1 Y 1 L GLN 160 ? C GLN 160 
380 1 Y 1 L GLU 161 ? C GLU 161 
381 1 Y 1 L SER 162 ? C SER 162 
382 1 Y 1 L VAL 163 ? C VAL 163 
383 1 Y 1 L THR 164 ? C THR 164 
384 1 Y 1 L GLU 165 ? C GLU 165 
385 1 Y 1 L GLN 166 ? C GLN 166 
386 1 Y 1 L ASP 167 ? C ASP 167 
387 1 Y 1 L SER 168 ? C SER 168 
388 1 Y 1 L LYS 169 ? C LYS 169 
389 1 Y 1 L ASP 170 ? C ASP 170 
390 1 Y 1 L SER 171 ? C SER 171 
391 1 Y 1 L THR 172 ? C THR 172 
392 1 Y 1 L TYR 173 ? C TYR 173 
393 1 Y 1 L SER 174 ? C SER 174 
394 1 Y 1 L LEU 175 ? C LEU 175 
395 1 Y 1 L SER 176 ? C SER 176 
396 1 Y 1 L SER 177 ? C SER 177 
397 1 Y 1 L THR 178 ? C THR 178 
398 1 Y 1 L LEU 179 ? C LEU 179 
399 1 Y 1 L THR 180 ? C THR 180 
400 1 Y 1 L LEU 181 ? C LEU 181 
401 1 Y 1 L SER 182 ? C SER 182 
402 1 Y 1 L LYS 183 ? C LYS 183 
403 1 Y 1 L ALA 184 ? C ALA 184 
404 1 Y 1 L ASP 185 ? C ASP 185 
405 1 Y 1 L TYR 186 ? C TYR 186 
406 1 Y 1 L GLU 187 ? C GLU 187 
407 1 Y 1 L LYS 188 ? C LYS 188 
408 1 Y 1 L HIS 189 ? C HIS 189 
409 1 Y 1 L LYS 190 ? C LYS 190 
410 1 Y 1 L VAL 191 ? C VAL 191 
411 1 Y 1 L TYR 192 ? C TYR 192 
412 1 Y 1 L ALA 193 ? C ALA 193 
413 1 Y 1 L CYS 194 ? C CYS 194 
414 1 Y 1 L GLU 195 ? C GLU 195 
415 1 Y 1 L VAL 196 ? C VAL 196 
416 1 Y 1 L THR 197 ? C THR 197 
417 1 Y 1 L HIS 198 ? C HIS 198 
418 1 Y 1 L GLN 199 ? C GLN 199 
419 1 Y 1 L GLY 200 ? C GLY 200 
420 1 Y 1 L LEU 201 ? C LEU 201 
421 1 Y 1 L SER 202 ? C SER 202 
422 1 Y 1 L SER 203 ? C SER 203 
423 1 Y 1 L PRO 204 ? C PRO 204 
424 1 Y 1 L VAL 205 ? C VAL 205 
425 1 Y 1 L THR 206 ? C THR 206 
426 1 Y 1 L LYS 207 ? C LYS 207 
427 1 Y 1 L SER 208 ? C SER 208 
428 1 Y 1 L PHE 209 ? C PHE 209 
429 1 Y 1 L ASN 210 ? C ASN 210 
430 1 Y 1 L ARG 211 ? C ARG 211 
431 1 Y 1 L GLY 212 ? C GLY 212 
432 1 Y 1 L GLU 213 ? C GLU 213 
433 1 Y 1 L CYS 214 ? C CYS 214 
# 
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 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
loop_
_em_entity_assembly_molwt.entity_assembly_id 
_em_entity_assembly_molwt.experimental_flag 
_em_entity_assembly_molwt.id 
_em_entity_assembly_molwt.units 
_em_entity_assembly_molwt.value 
1 YES 1 MEGADALTONS 0.0846 
1 NO  2 MEGADALTONS 0.0957 
# 
loop_
_em_entity_assembly_naturalsource.cell 
_em_entity_assembly_naturalsource.cellular_location 
_em_entity_assembly_naturalsource.entity_assembly_id 
_em_entity_assembly_naturalsource.id 
_em_entity_assembly_naturalsource.ncbi_tax_id 
_em_entity_assembly_naturalsource.organism 
_em_entity_assembly_naturalsource.organelle 
_em_entity_assembly_naturalsource.organ 
_em_entity_assembly_naturalsource.strain 
_em_entity_assembly_naturalsource.tissue 
? ? 2 2 2697049 'Severe acute respiratory syndrome coronavirus 2' ? ? ? ? 
? ? 3 2 10665   'Enterobacteria phage T4'                         ? ? ? ? 
? ? 3 3 9606    'Homo sapiens'                                    ? ? ? ? 
# 
loop_
_em_entity_assembly_recombinant.cell 
_em_entity_assembly_recombinant.entity_assembly_id 
_em_entity_assembly_recombinant.id 
_em_entity_assembly_recombinant.ncbi_tax_id 
_em_entity_assembly_recombinant.organism 
_em_entity_assembly_recombinant.plasmid 
_em_entity_assembly_recombinant.strain 
? 2 2 9606 'Homo sapiens' ? ? 
? 3 2 9606 'Homo sapiens' ? ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               1.5 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         48.6 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     4774 
# 
_em_imaging_optics.chr_aberration_corrector   ? 
_em_imaging_optics.energyfilter_lower         ? 
_em_imaging_optics.energyfilter_slit_width    10 
_em_imaging_optics.energyfilter_name          'GIF Bioquantum' 
_em_imaging_optics.energyfilter_upper         ? 
_em_imaging_optics.id                         1 
_em_imaging_optics.imaging_id                 1 
_em_imaging_optics.phase_plate                ? 
_em_imaging_optics.sph_aberration_corrector   ? 
_em_imaging_optics.details                    ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'PARTICLE SELECTION'            ? 1  1 ? ? Warp      1.0.7 
'IMAGE ACQUISITION'             ? 2  ? ? 1 EPU       2.7   
MASKING                         ? 3  ? ? ? ?         ?     
'CTF CORRECTION'                ? 4  1 ? ? Warp      1.0.7 
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ?     
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ?     
'MODEL FITTING'                 ? 7  ? 1 ? Coot      0.9   
OTHER                           ? 8  ? ? ? ?         ?     
'MODEL REFINEMENT'              ? 9  ? 1 ? PHENIX    1.19  
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ?         ?     
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? cryoSPARC 3.2.0 
CLASSIFICATION                  ? 12 1 ? ? cryoSPARC 3.0.1 
RECONSTRUCTION                  ? 13 1 ? ? cryoSPARC 3.2.0 
RECONSTRUCTION                  ? 14 1 ? ? cryoSPARC 4.1.1 
'VOLUME SELECTION'              ? 15 1 1 1 ?         ?     
'SERIES ALIGNMENT'              ? 16 1 1 1 ?         ?     
'MOLECULAR REPLACEMENT'         ? 17 1 1 1 ?         ?     
'LATTICE DISTORTION CORRECTION' ? 18 1 1 1 ?         ?     
'SYMMETRY DETERMINATION'        ? 19 1 1 1 ?         ?     
'CRYSTALLOGRAPHY MERGING'       ? 20 1 1 1 ?         ?     
# 
_em_specimen.concentration           2.1 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7KSG 
# 
_atom_sites.entry_id                    8P5M 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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   . THR A 1 1   ? 293.772 236.244 279.263 1.00 55560. ? 333 THR I N   1 
ATOM 2    C CA  . THR A 1 1   ? 292.360 236.129 279.604 1.00 55519. ? 333 THR I CA  1 
ATOM 3    C C   . THR A 1 1   ? 291.991 237.407 280.367 1.00 55364. ? 333 THR I C   1 
ATOM 4    O O   . THR A 1 1   ? 291.427 237.367 281.463 1.00 55375. ? 333 THR I O   1 
ATOM 5    C CB  . THR A 1 1   ? 292.071 234.853 280.431 1.00 55582. ? 333 THR I CB  1 
ATOM 6    O OG1 . THR A 1 1   ? 292.803 233.758 279.869 1.00 55591. ? 333 THR I OG1 1 
ATOM 7    C CG2 . THR A 1 1   ? 290.588 234.478 280.353 1.00 55600. ? 333 THR I CG2 1 
ATOM 8    N N   . ASN A 1 2   ? 292.416 238.535 279.796 1.00 49488. ? 334 ASN I N   1 
ATOM 9    C CA  . ASN A 1 2   ? 292.225 239.843 280.411 1.00 49295. ? 334 ASN I CA  1 
ATOM 10   C C   . ASN A 1 2   ? 290.743 240.163 280.565 1.00 49132. ? 334 ASN I C   1 
ATOM 11   O O   . ASN A 1 2   ? 289.939 239.902 279.667 1.00 49099. ? 334 ASN I O   1 
ATOM 12   C CB  . ASN A 1 2   ? 292.911 240.918 279.571 1.00 49243. ? 334 ASN I CB  1 
ATOM 13   C CG  . ASN A 1 2   ? 293.356 242.102 280.393 1.00 49213. ? 334 ASN I CG  1 
ATOM 14   O OD1 . ASN A 1 2   ? 293.037 242.204 281.575 1.00 49213. ? 334 ASN I OD1 1 
ATOM 15   N ND2 . ASN A 1 2   ? 294.097 243.009 279.770 1.00 49190. ? 334 ASN I ND2 1 
ATOM 16   N N   . LEU A 1 3   ? 290.379 240.719 281.715 1.00 47139. ? 335 LEU I N   1 
ATOM 17   C CA  . LEU A 1 3   ? 288.997 241.063 282.005 1.00 47004. ? 335 LEU I CA  1 
ATOM 18   C C   . LEU A 1 3   ? 288.894 242.543 282.343 1.00 46889. ? 335 LEU I C   1 
ATOM 19   O O   . LEU A 1 3   ? 289.739 243.087 283.059 1.00 46938. ? 335 LEU I O   1 
ATOM 20   C CB  . LEU A 1 3   ? 288.449 240.221 283.158 1.00 47056. ? 335 LEU I CB  1 
ATOM 21   C CG  . LEU A 1 3   ? 288.271 238.731 282.868 1.00 47099. ? 335 LEU I CG  1 
ATOM 22   C CD1 . LEU A 1 3   ? 287.873 237.992 284.131 1.00 47080. ? 335 LEU I CD1 1 
ATOM 23   C CD2 . LEU A 1 3   ? 287.238 238.517 281.782 1.00 47011. ? 335 LEU I CD2 1 
ATOM 24   N N   . CYS A 1 4   ? 287.874 243.187 281.782 1.00 45139. ? 336 CYS I N   1 
ATOM 25   C CA  . CYS A 1 4   ? 287.664 244.614 281.976 1.00 44968. ? 336 CYS I CA  1 
ATOM 26   C C   . CYS A 1 4   ? 287.295 244.930 283.420 1.00 44804. ? 336 CYS I C   1 
ATOM 27   O O   . CYS A 1 4   ? 286.567 244.164 284.060 1.00 44855. ? 336 CYS I O   1 
ATOM 28   C CB  . CYS A 1 4   ? 286.588 245.124 281.033 1.00 44912. ? 336 CYS I CB  1 
ATOM 29   S SG  . CYS A 1 4   ? 287.070 244.912 279.336 1.00 45075. ? 336 CYS I SG  1 
ATOM 30   N N   . PRO A 1 5   ? 287.769 246.049 283.957 1.00 39905. ? 337 PRO I N   1 
ATOM 31   C CA  . PRO A 1 5   ? 287.475 246.381 285.357 1.00 39658. ? 337 PRO I CA  1 
ATOM 32   C C   . PRO A 1 5   ? 286.120 247.058 285.536 1.00 39457. ? 337 PRO I C   1 
ATOM 33   O O   . PRO A 1 5   ? 286.024 248.223 285.929 1.00 39353. ? 337 PRO I O   1 
ATOM 34   C CB  . PRO A 1 5   ? 288.647 247.299 285.724 1.00 39569. ? 337 PRO I CB  1 
ATOM 35   C CG  . PRO A 1 5   ? 288.999 247.972 284.452 1.00 39590. ? 337 PRO I CG  1 
ATOM 36   C CD  . PRO A 1 5   ? 288.700 247.013 283.342 1.00 39728. ? 337 PRO I CD  1 
ATOM 37   N N   . PHE A 1 6   ? 285.051 246.327 285.203 1.00 37498. ? 338 PHE I N   1 
ATOM 38   C CA  . PHE A 1 6   ? 283.708 246.813 285.497 1.00 37307. ? 338 PHE I CA  1 
ATOM 39   C C   . PHE A 1 6   ? 283.467 246.879 286.992 1.00 37106. ? 338 PHE I C   1 
ATOM 40   O O   . PHE A 1 6   ? 282.688 247.719 287.442 1.00 37164. ? 338 PHE I O   1 
ATOM 41   C CB  . PHE A 1 6   ? 282.631 245.958 284.830 1.00 37319. ? 338 PHE I CB  1 
ATOM 42   C CG  . PHE A 1 6   ? 282.494 246.181 283.353 1.00 37317. ? 338 PHE I CG  1 
ATOM 43   C CD1 . PHE A 1 6   ? 283.050 247.292 282.741 1.00 37283. ? 338 PHE I CD1 1 
ATOM 44   C CD2 . PHE A 1 6   ? 281.765 245.295 282.583 1.00 37341. ? 338 PHE I CD2 1 
ATOM 45   C CE1 . PHE A 1 6   ? 282.899 247.495 281.385 1.00 37266. ? 338 PHE I CE1 1 
ATOM 46   C CE2 . PHE A 1 6   ? 281.605 245.499 281.232 1.00 37512. ? 338 PHE I CE2 1 
ATOM 47   C CZ  . PHE A 1 6   ? 282.179 246.598 280.630 1.00 37395. ? 338 PHE I CZ  1 
ATOM 48   N N   . GLY A 1 7   ? 284.048 245.946 287.752 1.00 34470. ? 339 GLY I N   1 
ATOM 49   C CA  . GLY A 1 7   ? 283.851 245.929 289.194 1.00 34340. ? 339 GLY I CA  1 
ATOM 50   C C   . GLY A 1 7   ? 284.353 247.193 289.862 1.00 34385. ? 339 GLY I C   1 
ATOM 51   O O   . GLY A 1 7   ? 283.774 247.657 290.844 1.00 34338. ? 339 GLY I O   1 
ATOM 52   N N   . GLU A 1 8   ? 285.462 247.741 289.357 1.00 35383. ? 340 GLU I N   1 
ATOM 53   C CA  . GLU A 1 8   ? 285.997 248.999 289.871 1.00 35317. ? 340 GLU I CA  1 
ATOM 54   C C   . GLU A 1 8   ? 285.029 250.153 289.641 1.00 35253. ? 340 GLU I C   1 
ATOM 55   O O   . GLU A 1 8   ? 284.829 250.992 290.525 1.00 35295. ? 340 GLU I O   1 
ATOM 56   C CB  . GLU A 1 8   ? 287.341 249.300 289.211 1.00 35364. ? 340 GLU I CB  1 
ATOM 57   C CG  . GLU A 1 8   ? 288.434 248.317 289.573 1.00 35373. ? 340 GLU I CG  1 
ATOM 58   C CD  . GLU A 1 8   ? 289.747 248.638 288.896 1.00 35402. ? 340 GLU I CD  1 
ATOM 59   O OE1 . GLU A 1 8   ? 289.761 249.519 288.011 1.00 35397. ? 340 GLU I OE1 1 
ATOM 60   O OE2 . GLU A 1 8   ? 290.765 248.002 289.241 1.00 35403. ? 340 GLU I OE2 1 
ATOM 61   N N   . VAL A 1 9   ? 284.455 250.233 288.439 1.00 34233. ? 341 VAL I N   1 
ATOM 62   C CA  . VAL A 1 9   ? 283.518 251.304 288.114 1.00 34069. ? 341 VAL I CA  1 
ATOM 63   C C   . VAL A 1 9   ? 282.204 251.145 288.871 1.00 34013. ? 341 VAL I C   1 
ATOM 64   O O   . VAL A 1 9   ? 281.707 252.096 289.474 1.00 34027. ? 341 VAL I O   1 
ATOM 65   C CB  . VAL A 1 9   ? 283.283 251.354 286.594 1.00 34028. ? 341 VAL I CB  1 
ATOM 66   C CG1 . VAL A 1 9   ? 282.589 252.626 286.223 1.00 34012. ? 341 VAL I CG1 1 
ATOM 67   C CG2 . VAL A 1 9   ? 284.600 251.253 285.853 1.00 34120. ? 341 VAL I CG2 1 
ATOM 68   N N   . PHE A 1 10  ? 281.616 249.950 288.835 1.00 34035. ? 342 PHE I N   1 
ATOM 69   C CA  . PHE A 1 10  ? 280.303 249.726 289.438 1.00 33984. ? 342 PHE I CA  1 
ATOM 70   C C   . PHE A 1 10  ? 280.351 249.678 290.961 1.00 33973. ? 342 PHE I C   1 
ATOM 71   O O   . PHE A 1 10  ? 279.428 250.160 291.626 1.00 33960. ? 342 PHE I O   1 
ATOM 72   C CB  . PHE A 1 10  ? 279.678 248.456 288.863 1.00 33964. ? 342 PHE I CB  1 
ATOM 73   C CG  . PHE A 1 10  ? 279.080 248.648 287.496 1.00 33991. ? 342 PHE I CG  1 
ATOM 74   C CD1 . PHE A 1 10  ? 279.874 248.640 286.362 1.00 34061. ? 342 PHE I CD1 1 
ATOM 75   C CD2 . PHE A 1 10  ? 277.721 248.848 287.349 1.00 34040. ? 342 PHE I CD2 1 
ATOM 76   C CE1 . PHE A 1 10  ? 279.327 248.831 285.114 1.00 34097. ? 342 PHE I CE1 1 
ATOM 77   C CE2 . PHE A 1 10  ? 277.168 249.038 286.105 1.00 34066. ? 342 PHE I CE2 1 
ATOM 78   C CZ  . PHE A 1 10  ? 277.973 249.028 284.986 1.00 34052. ? 342 PHE I CZ  1 
ATOM 79   N N   . ASN A 1 11  ? 281.402 249.100 291.537 1.00 34051. ? 343 ASN I N   1 
ATOM 80   C CA  . ASN A 1 11  ? 281.465 248.857 292.971 1.00 33917. ? 343 ASN I CA  1 
ATOM 81   C C   . ASN A 1 11  ? 282.378 249.835 293.698 1.00 33860. ? 343 ASN I C   1 
ATOM 82   O O   . ASN A 1 11  ? 282.845 249.524 294.798 1.00 33819. ? 343 ASN I O   1 
ATOM 83   C CB  . ASN A 1 11  ? 281.905 247.419 293.245 1.00 33974. ? 343 ASN I CB  1 
ATOM 84   C CG  . ASN A 1 11  ? 280.781 246.417 293.060 1.00 34064. ? 343 ASN I CG  1 
ATOM 85   O OD1 . ASN A 1 11  ? 279.705 246.564 293.634 1.00 34012. ? 343 ASN I OD1 1 
ATOM 86   N ND2 . ASN A 1 11  ? 281.032 245.385 292.269 1.00 34012. ? 343 ASN I ND2 1 
ATOM 87   N N   . ALA A 1 12  ? 282.678 250.979 293.082 1.00 34052. ? 344 ALA I N   1 
ATOM 88   C CA  . ALA A 1 12  ? 283.437 252.035 293.738 1.00 33938. ? 344 ALA I CA  1 
ATOM 89   C C   . ALA A 1 12  ? 282.703 252.539 294.975 1.00 33801. ? 344 ALA I C   1 
ATOM 90   O O   . ALA A 1 12  ? 281.471 252.602 294.997 1.00 33819. ? 344 ALA I O   1 
ATOM 91   C CB  . ALA A 1 12  ? 283.687 253.189 292.773 1.00 33980. ? 344 ALA I CB  1 
ATOM 92   N N   . THR A 1 13  ? 283.473 252.831 296.028 1.00 33957. ? 345 THR I N   1 
ATOM 93   C CA  . THR A 1 13  ? 282.900 253.245 297.308 1.00 33764. ? 345 THR I CA  1 
ATOM 94   C C   . THR A 1 13  ? 282.137 254.558 297.188 1.00 33935. ? 345 THR I C   1 
ATOM 95   O O   . THR A 1 13  ? 281.025 254.691 297.712 1.00 33573. ? 345 THR I O   1 
ATOM 96   C CB  . THR A 1 13  ? 284.012 253.377 298.351 1.00 33790. ? 345 THR I CB  1 
ATOM 97   O OG1 . THR A 1 13  ? 284.723 252.139 298.455 1.00 33888. ? 345 THR I OG1 1 
ATOM 98   C CG2 . THR A 1 13  ? 283.447 253.728 299.708 1.00 33427. ? 345 THR I CG2 1 
ATOM 99   N N   . ARG A 1 14  ? 282.703 255.526 296.478 1.00 33952. ? 346 ARG I N   1 
ATOM 100  C CA  . ARG A 1 14  ? 282.072 256.819 296.264 1.00 33913. ? 346 ARG I CA  1 
ATOM 101  C C   . ARG A 1 14  ? 281.999 257.132 294.784 1.00 33960. ? 346 ARG I C   1 
ATOM 102  O O   . ARG A 1 14  ? 283.016 257.062 294.088 1.00 33973. ? 346 ARG I O   1 
ATOM 103  C CB  . ARG A 1 14  ? 282.860 257.915 296.973 1.00 33942. ? 346 ARG I CB  1 
ATOM 104  C CG  . ARG A 1 14  ? 282.652 257.909 298.439 1.00 33439. ? 346 ARG I CG  1 
ATOM 105  C CD  . ARG A 1 14  ? 283.668 258.718 299.207 1.00 33624. ? 346 ARG I CD  1 
ATOM 106  N NE  . ARG A 1 14  ? 284.838 257.918 299.538 1.00 33756. ? 346 ARG I NE  1 
ATOM 107  C CZ  . ARG A 1 14  ? 285.209 257.624 300.775 1.00 33388. ? 346 ARG I CZ  1 
ATOM 108  N NH1 . ARG A 1 14  ? 284.530 258.059 301.822 1.00 32672. ? 346 ARG I NH1 1 
ATOM 109  N NH2 . ARG A 1 14  ? 286.288 256.872 300.967 1.00 33880. ? 346 ARG I NH2 1 
ATOM 110  N N   . PHE A 1 15  ? 280.807 257.455 294.293 1.00 33951. ? 347 PHE I N   1 
ATOM 111  C CA  . PHE A 1 15  ? 280.793 257.925 292.924 1.00 33941. ? 347 PHE I CA  1 
ATOM 112  C C   . PHE A 1 15  ? 281.099 259.412 292.888 1.00 33997. ? 347 PHE I C   1 
ATOM 113  O O   . PHE A 1 15  ? 280.967 260.129 293.881 1.00 34015. ? 347 PHE I O   1 
ATOM 114  C CB  . PHE A 1 15  ? 279.479 257.673 292.192 1.00 33995. ? 347 PHE I CB  1 
ATOM 115  C CG  . PHE A 1 15  ? 279.343 256.289 291.654 1.00 33976. ? 347 PHE I CG  1 
ATOM 116  C CD1 . PHE A 1 15  ? 280.349 255.364 291.825 1.00 34053. ? 347 PHE I CD1 1 
ATOM 117  C CD2 . PHE A 1 15  ? 278.317 255.984 290.788 1.00 33963. ? 347 PHE I CD2 1 
ATOM 118  C CE1 . PHE A 1 15  ? 280.237 254.115 291.308 1.00 33998. ? 347 PHE I CE1 1 
ATOM 119  C CE2 . PHE A 1 15  ? 278.223 254.734 290.229 1.00 34003. ? 347 PHE I CE2 1 
ATOM 120  C CZ  . PHE A 1 15  ? 279.181 253.800 290.493 1.00 33980. ? 347 PHE I CZ  1 
ATOM 121  N N   . ALA A 1 16  ? 281.513 259.868 291.719 1.00 33957. ? 348 ALA I N   1 
ATOM 122  C CA  . ALA A 1 16  ? 281.842 261.261 291.523 1.00 33957. ? 348 ALA I CA  1 
ATOM 123  C C   . ALA A 1 16  ? 280.576 262.098 291.407 1.00 33982. ? 348 ALA I C   1 
ATOM 124  O O   . ALA A 1 16  ? 279.465 261.589 291.265 1.00 34139. ? 348 ALA I O   1 
ATOM 125  C CB  . ALA A 1 16  ? 282.710 261.430 290.283 1.00 34009. ? 348 ALA I CB  1 
ATOM 126  N N   . SER A 1 17  ? 280.758 263.405 291.525 1.00 34006. ? 349 SER I N   1 
ATOM 127  C CA  . SER A 1 17  ? 279.668 264.348 291.349 1.00 33984. ? 349 SER I CA  1 
ATOM 128  C C   . SER A 1 17  ? 279.243 264.410 289.889 1.00 34024. ? 349 SER I C   1 
ATOM 129  O O   . SER A 1 17  ? 280.020 264.094 288.985 1.00 34151. ? 349 SER I O   1 
ATOM 130  C CB  . SER A 1 17  ? 280.108 265.724 291.817 1.00 34060. ? 349 SER I CB  1 
ATOM 131  O OG  . SER A 1 17  ? 280.708 265.647 293.093 1.00 33967. ? 349 SER I OG  1 
ATOM 132  N N   . VAL A 1 18  ? 277.975 264.770 289.666 1.00 33867. ? 350 VAL I N   1 
ATOM 133  C CA  . VAL A 1 18  ? 277.445 264.814 288.304 1.00 33930. ? 350 VAL I CA  1 
ATOM 134  C C   . VAL A 1 18  ? 278.151 265.889 287.480 1.00 34042. ? 350 VAL I C   1 
ATOM 135  O O   . VAL A 1 18  ? 278.469 265.670 286.307 1.00 34154. ? 350 VAL I O   1 
ATOM 136  C CB  . VAL A 1 18  ? 275.906 264.943 288.300 1.00 33944. ? 350 VAL I CB  1 
ATOM 137  C CG1 . VAL A 1 18  ? 275.405 266.161 289.046 1.00 34095. ? 350 VAL I CG1 1 
ATOM 138  C CG2 . VAL A 1 18  ? 275.367 264.872 286.880 1.00 33916. ? 350 VAL I CG2 1 
ATOM 139  N N   . TYR A 1 19  ? 278.396 267.064 288.068 1.00 34035. ? 351 TYR I N   1 
ATOM 140  C CA  . TYR A 1 19  ? 279.159 268.093 287.371 1.00 33956. ? 351 TYR I CA  1 
ATOM 141  C C   . TYR A 1 19  ? 280.607 267.648 287.160 1.00 34013. ? 351 TYR I C   1 
ATOM 142  O O   . TYR A 1 19  ? 281.164 267.821 286.073 1.00 34106. ? 351 TYR I O   1 
ATOM 143  C CB  . TYR A 1 19  ? 279.050 269.434 288.117 1.00 33978. ? 351 TYR I CB  1 
ATOM 144  C CG  . TYR A 1 19  ? 280.029 269.673 289.245 1.00 33955. ? 351 TYR I CG  1 
ATOM 145  C CD1 . TYR A 1 19  ? 279.848 269.072 290.478 1.00 33961. ? 351 TYR I CD1 1 
ATOM 146  C CD2 . TYR A 1 19  ? 281.150 270.471 289.064 1.00 34072. ? 351 TYR I CD2 1 
ATOM 147  C CE1 . TYR A 1 19  ? 280.737 269.272 291.506 1.00 33997. ? 351 TYR I CE1 1 
ATOM 148  C CE2 . TYR A 1 19  ? 282.048 270.676 290.088 1.00 34049. ? 351 TYR I CE2 1 
ATOM 149  C CZ  . TYR A 1 19  ? 281.836 270.070 291.306 1.00 34001. ? 351 TYR I CZ  1 
ATOM 150  O OH  . TYR A 1 19  ? 282.724 270.268 292.334 1.00 33992. ? 351 TYR I OH  1 
ATOM 151  N N   . ALA A 1 20  ? 281.232 267.083 288.190 1.00 34019. ? 352 ALA I N   1 
ATOM 152  C CA  . ALA A 1 20  ? 282.580 266.530 288.096 1.00 33884. ? 352 ALA I CA  1 
ATOM 153  C C   . ALA A 1 20  ? 282.534 265.021 287.872 1.00 34031. ? 352 ALA I C   1 
ATOM 154  O O   . ALA A 1 20  ? 283.076 264.252 288.659 1.00 34120. ? 352 ALA I O   1 
ATOM 155  C CB  . ALA A 1 20  ? 283.374 266.871 289.351 1.00 33953. ? 352 ALA I CB  1 
ATOM 156  N N   . TRP A 1 21  ? 281.870 264.604 286.797 1.00 34072. ? 353 TRP I N   1 
ATOM 157  C CA  . TRP A 1 21  ? 281.706 263.187 286.502 1.00 33912. ? 353 TRP I CA  1 
ATOM 158  C C   . TRP A 1 21  ? 283.044 262.560 286.126 1.00 33988. ? 353 TRP I C   1 
ATOM 159  O O   . TRP A 1 21  ? 283.933 263.219 285.584 1.00 34086. ? 353 TRP I O   1 
ATOM 160  C CB  . TRP A 1 21  ? 280.686 262.973 285.381 1.00 33943. ? 353 TRP I CB  1 
ATOM 161  C CG  . TRP A 1 21  ? 280.864 263.831 284.165 1.00 33910. ? 353 TRP I CG  1 
ATOM 162  C CD1 . TRP A 1 21  ? 280.394 265.090 283.974 1.00 33974. ? 353 TRP I CD1 1 
ATOM 163  C CD2 . TRP A 1 21  ? 281.544 263.472 282.958 1.00 33922. ? 353 TRP I CD2 1 
ATOM 164  N NE1 . TRP A 1 21  ? 280.745 265.546 282.734 1.00 33966. ? 353 TRP I NE1 1 
ATOM 165  C CE2 . TRP A 1 21  ? 281.452 264.569 282.088 1.00 33963. ? 353 TRP I CE2 1 
ATOM 166  C CE3 . TRP A 1 21  ? 282.225 262.332 282.532 1.00 33981. ? 353 TRP I CE3 1 
ATOM 167  C CZ2 . TRP A 1 21  ? 282.014 264.560 280.821 1.00 34019. ? 353 TRP I CZ2 1 
ATOM 168  C CZ3 . TRP A 1 21  ? 282.783 262.327 281.279 1.00 34011. ? 353 TRP I CZ3 1 
ATOM 169  C CH2 . TRP A 1 21  ? 282.675 263.432 280.436 1.00 34001. ? 353 TRP I CH2 1 
ATOM 170  N N   . ASN A 1 22  ? 283.185 261.275 286.433 1.00 33962. ? 354 ASN I N   1 
ATOM 171  C CA  . ASN A 1 22  ? 284.440 260.561 286.248 1.00 33939. ? 354 ASN I CA  1 
ATOM 172  C C   . ASN A 1 22  ? 284.375 259.707 284.994 1.00 33978. ? 354 ASN I C   1 
ATOM 173  O O   . ASN A 1 22  ? 283.475 258.882 284.858 1.00 34109. ? 354 ASN I O   1 
ATOM 174  C CB  . ASN A 1 22  ? 284.730 259.674 287.459 1.00 33982. ? 354 ASN I CB  1 
ATOM 175  C CG  . ASN A 1 22  ? 286.198 259.624 287.805 1.00 34072. ? 354 ASN I CG  1 
ATOM 176  O OD1 . ASN A 1 22  ? 286.892 260.639 287.775 1.00 34066. ? 354 ASN I OD1 1 
ATOM 177  N ND2 . ASN A 1 22  ? 286.689 258.431 288.117 1.00 34117. ? 354 ASN I ND2 1 
ATOM 178  N N   . ARG A 1 23  ? 285.351 259.874 284.108 1.00 33977. ? 355 ARG I N   1 
ATOM 179  C CA  . ARG A 1 23  ? 285.447 259.110 282.871 1.00 33980. ? 355 ARG I CA  1 
ATOM 180  C C   . ARG A 1 23  ? 286.621 258.152 282.968 1.00 34056. ? 355 ARG I C   1 
ATOM 181  O O   . ARG A 1 23  ? 287.754 258.577 283.214 1.00 34029. ? 355 ARG I O   1 
ATOM 182  C CB  . ARG A 1 23  ? 285.625 260.033 281.668 1.00 33932. ? 355 ARG I CB  1 
ATOM 183  C CG  . ARG A 1 23  ? 285.975 259.299 280.399 1.00 33981. ? 355 ARG I CG  1 
ATOM 184  C CD  . ARG A 1 23  ? 285.585 260.068 279.159 1.00 33993. ? 355 ARG I CD  1 
ATOM 185  N NE  . ARG A 1 23  ? 284.292 259.649 278.638 1.00 34073. ? 355 ARG I NE  1 
ATOM 186  C CZ  . ARG A 1 23  ? 283.576 260.349 277.771 1.00 34032. ? 355 ARG I CZ  1 
ATOM 187  N NH1 . ARG A 1 23  ? 284.001 261.508 277.302 1.00 34012. ? 355 ARG I NH1 1 
ATOM 188  N NH2 . ARG A 1 23  ? 282.404 259.873 277.366 1.00 34084. ? 355 ARG I NH2 1 
ATOM 189  N N   . LYS A 1 24  ? 286.354 256.867 282.766 1.00 34072. ? 356 LYS I N   1 
ATOM 190  C CA  . LYS A 1 24  ? 287.378 255.835 282.804 1.00 33997. ? 356 LYS I CA  1 
ATOM 191  C C   . LYS A 1 24  ? 287.482 255.175 281.439 1.00 34085. ? 356 LYS I C   1 
ATOM 192  O O   . LYS A 1 24  ? 286.480 254.692 280.907 1.00 34212. ? 356 LYS I O   1 
ATOM 193  C CB  . LYS A 1 24  ? 287.046 254.802 283.877 1.00 34003. ? 356 LYS I CB  1 
ATOM 194  C CG  . LYS A 1 24  ? 287.961 253.609 283.899 1.00 34089. ? 356 LYS I CG  1 
ATOM 195  C CD  . LYS A 1 24  ? 287.996 252.997 285.283 1.00 34070. ? 356 LYS I CD  1 
ATOM 196  C CE  . LYS A 1 24  ? 288.425 251.551 285.227 1.00 34148. ? 356 LYS I CE  1 
ATOM 197  N NZ  . LYS A 1 24  ? 289.704 251.396 284.489 1.00 34157. ? 356 LYS I NZ  1 
ATOM 198  N N   . ARG A 1 25  ? 288.685 255.153 280.872 1.00 36395. ? 357 ARG I N   1 
ATOM 199  C CA  . ARG A 1 25  ? 288.902 254.470 279.604 1.00 36490. ? 357 ARG I CA  1 
ATOM 200  C C   . ARG A 1 25  ? 289.100 252.982 279.853 1.00 36597. ? 357 ARG I C   1 
ATOM 201  O O   . ARG A 1 25  ? 289.881 252.588 280.723 1.00 36656. ? 357 ARG I O   1 
ATOM 202  C CB  . ARG A 1 25  ? 290.104 255.056 278.869 1.00 36554. ? 357 ARG I CB  1 
ATOM 203  C CG  . ARG A 1 25  ? 290.342 254.429 277.510 1.00 36658. ? 357 ARG I CG  1 
ATOM 204  C CD  . ARG A 1 25  ? 290.741 255.464 276.476 1.00 36681. ? 357 ARG I CD  1 
ATOM 205  N NE  . ARG A 1 25  ? 291.166 254.845 275.227 1.00 36772. ? 357 ARG I NE  1 
ATOM 206  C CZ  . ARG A 1 25  ? 291.600 255.516 274.169 1.00 36773. ? 357 ARG I CZ  1 
ATOM 207  N NH1 . ARG A 1 25  ? 291.680 256.836 274.172 1.00 36729. ? 357 ARG I NH1 1 
ATOM 208  N NH2 . ARG A 1 25  ? 291.964 254.845 273.079 1.00 36749. ? 357 ARG I NH2 1 
ATOM 209  N N   . ILE A 1 26  ? 288.384 252.157 279.095 1.00 36427. ? 358 ILE I N   1 
ATOM 210  C CA  . ILE A 1 26  ? 288.465 250.704 279.191 1.00 36509. ? 358 ILE I CA  1 
ATOM 211  C C   . ILE A 1 26  ? 289.005 250.150 277.879 1.00 36806. ? 358 ILE I C   1 
ATOM 212  O O   . ILE A 1 26  ? 288.438 250.416 276.813 1.00 36833. ? 358 ILE I O   1 
ATOM 213  C CB  . ILE A 1 26  ? 287.090 250.115 279.528 1.00 36414. ? 358 ILE I CB  1 
ATOM 214  C CG1 . ILE A 1 26  ? 286.635 250.655 280.886 1.00 36355. ? 358 ILE I CG1 1 
ATOM 215  C CG2 . ILE A 1 26  ? 287.129 248.615 279.511 1.00 36660. ? 358 ILE I CG2 1 
ATOM 216  C CD1 . ILE A 1 26  ? 285.346 250.100 281.380 1.00 36394. ? 358 ILE I CD1 1 
ATOM 217  N N   . SER A 1 27  ? 290.095 249.384 277.949 1.00 42061. ? 359 SER I N   1 
ATOM 218  C CA  . SER A 1 27  ? 290.723 248.864 276.739 1.00 42326. ? 359 SER I CA  1 
ATOM 219  C C   . SER A 1 27  ? 291.472 247.566 277.024 1.00 42537. ? 359 SER I C   1 
ATOM 220  O O   . SER A 1 27  ? 291.791 247.248 278.173 1.00 42458. ? 359 SER I O   1 
ATOM 221  C CB  . SER A 1 27  ? 291.672 249.897 276.120 1.00 42320. ? 359 SER I CB  1 
ATOM 222  O OG  . SER A 1 27  ? 292.641 250.326 277.058 1.00 42315. ? 359 SER I OG  1 
ATOM 223  N N   . ASN A 1 28  ? 291.743 246.825 275.934 1.00 45993. ? 360 ASN I N   1 
ATOM 224  C CA  . ASN A 1 28  ? 292.549 245.591 275.916 1.00 46091. ? 360 ASN I CA  1 
ATOM 225  C C   . ASN A 1 28  ? 292.042 244.505 276.866 1.00 46021. ? 360 ASN I C   1 
ATOM 226  O O   . ASN A 1 28  ? 292.829 243.848 277.549 1.00 46112. ? 360 ASN I O   1 
ATOM 227  C CB  . ASN A 1 28  ? 294.024 245.891 276.198 1.00 46089. ? 360 ASN I CB  1 
ATOM 228  C CG  . ASN A 1 28  ? 294.511 247.137 275.491 1.00 46102. ? 360 ASN I CG  1 
ATOM 229  O OD1 . ASN A 1 28  ? 294.768 248.163 276.119 1.00 46115. ? 360 ASN I OD1 1 
ATOM 230  N ND2 . ASN A 1 28  ? 294.651 247.050 274.176 1.00 46118. ? 360 ASN I ND2 1 
ATOM 231  N N   . CYS A 1 29  ? 290.727 244.308 276.919 1.00 43553. ? 361 CYS I N   1 
ATOM 232  C CA  . CYS A 1 29  ? 290.168 243.358 277.869 1.00 43515. ? 361 CYS I CA  1 
ATOM 233  C C   . CYS A 1 29  ? 288.853 242.790 277.356 1.00 43425. ? 361 CYS I C   1 
ATOM 234  O O   . CYS A 1 29  ? 288.188 243.383 276.509 1.00 43557. ? 361 CYS I O   1 
ATOM 235  C CB  . CYS A 1 29  ? 289.977 244.005 279.236 1.00 43581. ? 361 CYS I CB  1 
ATOM 236  S SG  . CYS A 1 29  ? 289.005 245.517 279.233 1.00 43382. ? 361 CYS I SG  1 
ATOM 237  N N   . VAL A 1 30  ? 288.488 241.623 277.882 1.00 42125. ? 362 VAL I N   1 
ATOM 238  C CA  . VAL A 1 30  ? 287.222 240.962 277.572 1.00 42020. ? 362 VAL I CA  1 
ATOM 239  C C   . VAL A 1 30  ? 286.203 241.327 278.644 1.00 42030. ? 362 VAL I C   1 
ATOM 240  O O   . VAL A 1 30  ? 286.461 241.149 279.840 1.00 42163. ? 362 VAL I O   1 
ATOM 241  C CB  . VAL A 1 30  ? 287.407 239.438 277.484 1.00 41998. ? 362 VAL I CB  1 
ATOM 242  C CG1 . VAL A 1 30  ? 286.089 238.749 277.205 1.00 42052. ? 362 VAL I CG1 1 
ATOM 243  C CG2 . VAL A 1 30  ? 288.419 239.094 276.418 1.00 41997. ? 362 VAL I CG2 1 
ATOM 244  N N   . ALA A 1 31  ? 285.043 241.833 278.224 1.00 41839. ? 363 ALA I N   1 
ATOM 245  C CA  . ALA A 1 31  ? 283.987 242.261 279.135 1.00 41842. ? 363 ALA I CA  1 
ATOM 246  C C   . ALA A 1 31  ? 282.717 241.455 278.908 1.00 41947. ? 363 ALA I C   1 
ATOM 247  O O   . ALA A 1 31  ? 282.155 241.476 277.811 1.00 42039. ? 363 ALA I O   1 
ATOM 248  C CB  . ALA A 1 31  ? 283.686 243.744 278.940 1.00 41862. ? 363 ALA I CB  1 
ATOM 249  N N   . ASP A 1 32  ? 282.251 240.767 279.948 1.00 44333. ? 364 ASP I N   1 
ATOM 250  C CA  . ASP A 1 32  ? 280.975 240.054 279.891 1.00 44431. ? 364 ASP I CA  1 
ATOM 251  C C   . ASP A 1 32  ? 279.858 240.985 280.352 1.00 44428. ? 364 ASP I C   1 
ATOM 252  O O   . ASP A 1 32  ? 279.537 241.069 281.538 1.00 44395. ? 364 ASP I O   1 
ATOM 253  C CB  . ASP A 1 32  ? 281.031 238.776 280.712 1.00 44475. ? 364 ASP I CB  1 
ATOM 254  C CG  . ASP A 1 32  ? 280.158 237.682 280.132 1.00 44486. ? 364 ASP I CG  1 
ATOM 255  O OD1 . ASP A 1 32  ? 279.302 237.994 279.278 1.00 44514. ? 364 ASP I OD1 1 
ATOM 256  O OD2 . ASP A 1 32  ? 280.335 236.510 280.520 1.00 44499. ? 364 ASP I OD2 1 
ATOM 257  N N   . TYR A 1 33  ? 279.282 241.716 279.395 1.00 43967. ? 365 TYR I N   1 
ATOM 258  C CA  . TYR A 1 33  ? 278.167 242.624 279.660 1.00 43924. ? 365 TYR I CA  1 
ATOM 259  C C   . TYR A 1 33  ? 276.930 241.857 280.122 1.00 44008. ? 365 TYR I C   1 
ATOM 260  O O   . TYR A 1 33  ? 276.105 242.378 280.898 1.00 43943. ? 365 TYR I O   1 
ATOM 261  C CB  . TYR A 1 33  ? 277.849 243.420 278.400 1.00 43960. ? 365 TYR I CB  1 
ATOM 262  C CG  . TYR A 1 33  ? 279.061 243.881 277.616 1.00 43941. ? 365 TYR I CG  1 
ATOM 263  C CD1 . TYR A 1 33  ? 279.730 245.054 277.935 1.00 43806. ? 365 TYR I CD1 1 
ATOM 264  C CD2 . TYR A 1 33  ? 279.513 243.144 276.525 1.00 44023. ? 365 TYR I CD2 1 
ATOM 265  C CE1 . TYR A 1 33  ? 280.832 245.463 277.204 1.00 43802. ? 365 TYR I CE1 1 
ATOM 266  C CE2 . TYR A 1 33  ? 280.608 243.542 275.795 1.00 44025. ? 365 TYR I CE2 1 
ATOM 267  C CZ  . TYR A 1 33  ? 281.262 244.701 276.136 1.00 43970. ? 365 TYR I CZ  1 
ATOM 268  O OH  . TYR A 1 33  ? 282.354 245.092 275.403 1.00 44056. ? 365 TYR I OH  1 
ATOM 269  N N   . SER A 1 34  ? 276.756 240.645 279.584 1.00 45990. ? 366 SER I N   1 
ATOM 270  C CA  . SER A 1 34  ? 275.605 239.809 279.900 1.00 46030. ? 366 SER I CA  1 
ATOM 271  C C   . SER A 1 34  ? 275.559 239.472 281.383 1.00 46004. ? 366 SER I C   1 
ATOM 272  O O   . SER A 1 34  ? 274.475 239.310 281.943 1.00 46058. ? 366 SER I O   1 
ATOM 273  C CB  . SER A 1 34  ? 275.633 238.533 279.060 1.00 46086. ? 366 SER I CB  1 
ATOM 274  O OG  . SER A 1 34  ? 274.668 237.604 279.520 1.00 46094. ? 366 SER I OG  1 
ATOM 275  N N   . VAL A 1 35  ? 276.729 239.283 282.008 1.00 45168. ? 367 VAL I N   1 
ATOM 276  C CA  . VAL A 1 35  ? 276.807 239.030 283.448 1.00 45120. ? 367 VAL I CA  1 
ATOM 277  C C   . VAL A 1 35  ? 276.199 240.189 284.231 1.00 45009. ? 367 VAL I C   1 
ATOM 278  O O   . VAL A 1 35  ? 275.472 239.980 285.213 1.00 45149. ? 367 VAL I O   1 
ATOM 279  C CB  . VAL A 1 35  ? 278.269 238.754 283.854 1.00 45130. ? 367 VAL I CB  1 
ATOM 280  C CG1 . VAL A 1 35  ? 278.450 238.764 285.364 1.00 45122. ? 367 VAL I CG1 1 
ATOM 281  C CG2 . VAL A 1 35  ? 278.699 237.409 283.317 1.00 45182. ? 367 VAL I CG2 1 
ATOM 282  N N   . LEU A 1 36  ? 276.474 241.427 283.799 1.00 40329. ? 368 LEU I N   1 
ATOM 283  C CA  . LEU A 1 36  ? 275.865 242.600 284.423 1.00 40174. ? 368 LEU I CA  1 
ATOM 284  C C   . LEU A 1 36  ? 274.354 242.607 284.243 1.00 40258. ? 368 LEU I C   1 
ATOM 285  O O   . LEU A 1 36  ? 273.615 242.944 285.174 1.00 40107. ? 368 LEU I O   1 
ATOM 286  C CB  . LEU A 1 36  ? 276.445 243.886 283.838 1.00 39900. ? 368 LEU I CB  1 
ATOM 287  C CG  . LEU A 1 36  ? 277.748 244.489 284.345 1.00 39743. ? 368 LEU I CG  1 
ATOM 288  C CD1 . LEU A 1 36  ? 278.258 245.445 283.294 1.00 39725. ? 368 LEU I CD1 1 
ATOM 289  C CD2 . LEU A 1 36  ? 277.533 245.202 285.660 1.00 39686. ? 368 LEU I CD2 1 
ATOM 290  N N   . TYR A 1 37  ? 273.882 242.270 283.039 1.00 44543. ? 369 TYR I N   1 
ATOM 291  C CA  . TYR A 1 37  ? 272.434 242.178 282.823 1.00 44624. ? 369 TYR I CA  1 
ATOM 292  C C   . TYR A 1 37  ? 271.783 241.071 283.657 1.00 44816. ? 369 TYR I C   1 
ATOM 293  O O   . TYR A 1 37  ? 270.653 241.233 284.133 1.00 44849. ? 369 TYR I O   1 
ATOM 294  C CB  . TYR A 1 37  ? 272.111 241.979 281.345 1.00 44675. ? 369 TYR I CB  1 
ATOM 295  C CG  . TYR A 1 37  ? 270.753 242.537 280.987 1.00 44636. ? 369 TYR I CG  1 
ATOM 296  C CD1 . TYR A 1 37  ? 270.586 243.882 280.700 1.00 44541. ? 369 TYR I CD1 1 
ATOM 297  C CD2 . TYR A 1 37  ? 269.629 241.718 280.966 1.00 44748. ? 369 TYR I CD2 1 
ATOM 298  C CE1 . TYR A 1 37  ? 269.340 244.398 280.389 1.00 44537. ? 369 TYR I CE1 1 
ATOM 299  C CE2 . TYR A 1 37  ? 268.379 242.224 280.651 1.00 44749. ? 369 TYR I CE2 1 
ATOM 300  C CZ  . TYR A 1 37  ? 268.244 243.565 280.361 1.00 44706. ? 369 TYR I CZ  1 
ATOM 301  O OH  . TYR A 1 37  ? 267.007 244.079 280.048 1.00 44719. ? 369 TYR I OH  1 
ATOM 302  N N   . ASN A 1 38  ? 272.467 239.931 283.810 1.00 46837. ? 370 ASN I N   1 
ATOM 303  C CA  . ASN A 1 38  ? 271.934 238.787 284.554 1.00 46927. ? 370 ASN I CA  1 
ATOM 304  C C   . ASN A 1 38  ? 271.707 239.105 286.026 1.00 46901. ? 370 ASN I C   1 
ATOM 305  O O   . ASN A 1 38  ? 270.787 238.552 286.641 1.00 46981. ? 370 ASN I O   1 
ATOM 306  C CB  . ASN A 1 38  ? 272.854 237.575 284.412 1.00 46984. ? 370 ASN I CB  1 
ATOM 307  C CG  . ASN A 1 38  ? 272.816 236.974 283.023 1.00 47001. ? 370 ASN I CG  1 
ATOM 308  O OD1 . ASN A 1 38  ? 271.846 237.151 282.286 1.00 47023. ? 370 ASN I OD1 1 
ATOM 309  N ND2 . ASN A 1 38  ? 273.874 236.259 282.657 1.00 46986. ? 370 ASN I ND2 1 
ATOM 310  N N   . SER A 1 39  ? 272.586 239.920 286.623 1.00 45766. ? 371 SER I N   1 
ATOM 311  C CA  . SER A 1 39  ? 272.431 240.311 288.025 1.00 45749. ? 371 SER I CA  1 
ATOM 312  C C   . SER A 1 39  ? 271.109 241.038 288.258 1.00 45689. ? 371 SER I C   1 
ATOM 313  O O   . SER A 1 39  ? 270.424 240.777 289.255 1.00 45695. ? 371 SER I O   1 
ATOM 314  C CB  . SER A 1 39  ? 273.611 241.181 288.457 1.00 45664. ? 371 SER I CB  1 
ATOM 315  O OG  . SER A 1 39  ? 273.359 242.549 288.201 1.00 45476. ? 371 SER I OG  1 
ATOM 316  N N   . ALA A 1 40  ? 270.738 241.932 287.331 1.00 44497. ? 372 ALA I N   1 
ATOM 317  C CA  . ALA A 1 40  ? 269.439 242.622 287.283 1.00 44425. ? 372 ALA I CA  1 
ATOM 318  C C   . ALA A 1 40  ? 269.111 243.375 288.572 1.00 44233. ? 372 ALA I C   1 
ATOM 319  O O   . ALA A 1 40  ? 267.959 243.430 289.005 1.00 44295. ? 372 ALA I O   1 
ATOM 320  C CB  . ALA A 1 40  ? 268.312 241.649 286.925 1.00 44516. ? 372 ALA I CB  1 
ATOM 321  N N   . SER A 1 41  ? 270.130 243.963 289.186 1.00 38092. ? 373 SER I N   1 
ATOM 322  C CA  . SER A 1 41  ? 269.939 244.809 290.352 1.00 37774. ? 373 SER I CA  1 
ATOM 323  C C   . SER A 1 41  ? 269.814 246.274 289.969 1.00 37509. ? 373 SER I C   1 
ATOM 324  O O   . SER A 1 41  ? 269.716 247.133 290.850 1.00 37481. ? 373 SER I O   1 
ATOM 325  C CB  . SER A 1 41  ? 271.093 244.610 291.338 1.00 37776. ? 373 SER I CB  1 
ATOM 326  O OG  . SER A 1 41  ? 272.326 245.027 290.780 1.00 37736. ? 373 SER I OG  1 
ATOM 327  N N   . PHE A 1 42  ? 269.807 246.564 288.673 1.00 34380. ? 374 PHE I N   1 
ATOM 328  C CA  . PHE A 1 42  ? 269.788 247.918 288.146 1.00 34142. ? 374 PHE I CA  1 
ATOM 329  C C   . PHE A 1 42  ? 268.371 248.303 287.754 1.00 33989. ? 374 PHE I C   1 
ATOM 330  O O   . PHE A 1 42  ? 267.714 247.576 287.003 1.00 34095. ? 374 PHE I O   1 
ATOM 331  C CB  . PHE A 1 42  ? 270.722 248.033 286.944 1.00 34038. ? 374 PHE I CB  1 
ATOM 332  C CG  . PHE A 1 42  ? 272.067 247.419 287.169 1.00 34074. ? 374 PHE I CG  1 
ATOM 333  C CD1 . PHE A 1 42  ? 272.911 247.923 288.142 1.00 34145. ? 374 PHE I CD1 1 
ATOM 334  C CD2 . PHE A 1 42  ? 272.496 246.353 286.404 1.00 34169. ? 374 PHE I CD2 1 
ATOM 335  C CE1 . PHE A 1 42  ? 274.157 247.374 288.352 1.00 34074. ? 374 PHE I CE1 1 
ATOM 336  C CE2 . PHE A 1 42  ? 273.742 245.798 286.610 1.00 34279. ? 374 PHE I CE2 1 
ATOM 337  C CZ  . PHE A 1 42  ? 274.572 246.309 287.585 1.00 34123. ? 374 PHE I CZ  1 
ATOM 338  N N   . SER A 1 43  ? 267.900 249.429 288.295 1.00 34044. ? 375 SER I N   1 
ATOM 339  C CA  . SER A 1 43  ? 266.569 249.929 287.968 1.00 33985. ? 375 SER I CA  1 
ATOM 340  C C   . SER A 1 43  ? 266.460 250.298 286.496 1.00 33995. ? 375 SER I C   1 
ATOM 341  O O   . SER A 1 43  ? 265.433 250.043 285.858 1.00 34085. ? 375 SER I O   1 
ATOM 342  C CB  . SER A 1 43  ? 266.239 251.135 288.847 1.00 34007. ? 375 SER I CB  1 
ATOM 343  O OG  . SER A 1 43  ? 266.409 250.826 290.219 1.00 34041. ? 375 SER I OG  1 
ATOM 344  N N   . THR A 1 44  ? 267.502 250.911 285.944 1.00 34003. ? 376 THR I N   1 
ATOM 345  C CA  . THR A 1 44  ? 267.538 251.309 284.546 1.00 33972. ? 376 THR I CA  1 
ATOM 346  C C   . THR A 1 44  ? 268.713 250.630 283.863 1.00 34005. ? 376 THR I C   1 
ATOM 347  O O   . THR A 1 44  ? 269.843 250.719 284.345 1.00 34136. ? 376 THR I O   1 
ATOM 348  C CB  . THR A 1 44  ? 267.667 252.829 284.419 1.00 33988. ? 376 THR I CB  1 
ATOM 349  O OG1 . THR A 1 44  ? 266.527 253.457 285.016 1.00 33985. ? 376 THR I OG1 1 
ATOM 350  C CG2 . THR A 1 44  ? 267.776 253.250 282.963 1.00 33998. ? 376 THR I CG2 1 
ATOM 351  N N   . PHE A 1 45  ? 268.443 249.912 282.769 1.00 34001. ? 377 PHE I N   1 
ATOM 352  C CA  . PHE A 1 45  ? 269.491 249.358 281.925 1.00 34015. ? 377 PHE I CA  1 
ATOM 353  C C   . PHE A 1 45  ? 269.074 249.608 280.476 1.00 34011. ? 377 PHE I C   1 
ATOM 354  O O   . PHE A 1 45  ? 268.684 248.699 279.751 1.00 34157. ? 377 PHE I O   1 
ATOM 355  C CB  . PHE A 1 45  ? 269.706 247.866 282.177 1.00 34108. ? 377 PHE I CB  1 
ATOM 356  C CG  . PHE A 1 45  ? 271.100 247.391 281.879 1.00 34124. ? 377 PHE I CG  1 
ATOM 357  C CD1 . PHE A 1 45  ? 271.535 247.249 280.573 1.00 34204. ? 377 PHE I CD1 1 
ATOM 358  C CD2 . PHE A 1 45  ? 271.945 247.011 282.902 1.00 34183. ? 377 PHE I CD2 1 
ATOM 359  C CE1 . PHE A 1 45  ? 272.805 246.794 280.295 1.00 34163. ? 377 PHE I CE1 1 
ATOM 360  C CE2 . PHE A 1 45  ? 273.216 246.543 282.631 1.00 34299. ? 377 PHE I CE2 1 
ATOM 361  C CZ  . PHE A 1 45  ? 273.645 246.440 281.325 1.00 34200. ? 377 PHE I CZ  1 
ATOM 362  N N   . LYS A 1 46  ? 269.157 250.855 280.032 1.00 33973. ? 378 LYS I N   1 
ATOM 363  C CA  . LYS A 1 46  ? 268.693 251.222 278.702 1.00 33957. ? 378 LYS I CA  1 
ATOM 364  C C   . LYS A 1 46  ? 269.884 251.345 277.767 1.00 33955. ? 378 LYS I C   1 
ATOM 365  O O   . LYS A 1 46  ? 270.810 252.113 278.037 1.00 34092. ? 378 LYS I O   1 
ATOM 366  C CB  . LYS A 1 46  ? 267.899 252.525 278.734 1.00 34009. ? 378 LYS I CB  1 
ATOM 367  C CG  . LYS A 1 46  ? 266.528 252.383 279.360 1.00 34090. ? 378 LYS I CG  1 
ATOM 368  C CD  . LYS A 1 46  ? 265.716 253.652 279.213 1.00 34103. ? 378 LYS I CD  1 
ATOM 369  C CE  . LYS A 1 46  ? 264.358 253.505 279.875 1.00 34058. ? 378 LYS I CE  1 
ATOM 370  N NZ  . LYS A 1 46  ? 263.545 254.743 279.766 1.00 34021. ? 378 LYS I NZ  1 
ATOM 371  N N   . CYS A 1 47  ? 269.851 250.606 276.666 1.00 33995. ? 379 CYS I N   1 
ATOM 372  C CA  . CYS A 1 47  ? 270.914 250.629 275.676 1.00 34007. ? 379 CYS I CA  1 
ATOM 373  C C   . CYS A 1 47  ? 270.394 251.275 274.404 1.00 34003. ? 379 CYS I C   1 
ATOM 374  O O   . CYS A 1 47  ? 269.297 250.951 273.940 1.00 34101. ? 379 CYS I O   1 
ATOM 375  C CB  . CYS A 1 47  ? 271.453 249.226 275.400 1.00 34180. ? 379 CYS I CB  1 
ATOM 376  S SG  . CYS A 1 47  ? 272.300 248.483 276.809 1.00 34307. ? 379 CYS I SG  1 
ATOM 377  N N   . TYR A 1 48  ? 271.169 252.202 273.862 1.00 33925. ? 380 TYR I N   1 
ATOM 378  C CA  . TYR A 1 48  ? 270.806 252.961 272.676 1.00 33964. ? 380 TYR I CA  1 
ATOM 379  C C   . TYR A 1 48  ? 271.765 252.586 271.561 1.00 33964. ? 380 TYR I C   1 
ATOM 380  O O   . TYR A 1 48  ? 272.977 252.568 271.770 1.00 34064. ? 380 TYR I O   1 
ATOM 381  C CB  . TYR A 1 48  ? 270.824 254.476 272.933 1.00 33954. ? 380 TYR I CB  1 
ATOM 382  C CG  . TYR A 1 48  ? 270.152 254.925 274.223 1.00 33954. ? 380 TYR I CG  1 
ATOM 383  C CD1 . TYR A 1 48  ? 270.811 254.877 275.448 1.00 34005. ? 380 TYR I CD1 1 
ATOM 384  C CD2 . TYR A 1 48  ? 268.837 255.366 274.213 1.00 34004. ? 380 TYR I CD2 1 
ATOM 385  C CE1 . TYR A 1 48  ? 270.185 255.262 276.606 1.00 34062. ? 380 TYR I CE1 1 
ATOM 386  C CE2 . TYR A 1 48  ? 268.205 255.754 275.372 1.00 33998. ? 380 TYR I CE2 1 
ATOM 387  C CZ  . TYR A 1 48  ? 268.885 255.702 276.563 1.00 34033. ? 380 TYR I CZ  1 
ATOM 388  O OH  . TYR A 1 48  ? 268.266 256.090 277.725 1.00 34013. ? 380 TYR I OH  1 
ATOM 389  N N   . GLY A 1 49  ? 271.221 252.213 270.408 1.00 33979. ? 381 GLY I N   1 
ATOM 390  C CA  . GLY A 1 49  ? 272.029 251.809 269.278 1.00 33972. ? 381 GLY I CA  1 
ATOM 391  C C   . GLY A 1 49  ? 272.555 250.397 269.357 1.00 33999. ? 381 GLY I C   1 
ATOM 392  O O   . GLY A 1 49  ? 273.263 249.963 268.441 1.00 33969. ? 381 GLY I O   1 
ATOM 393  N N   . VAL A 1 50  ? 272.227 249.669 270.423 1.00 34052. ? 382 VAL I N   1 
ATOM 394  C CA  . VAL A 1 50  ? 272.723 248.323 270.670 1.00 34057. ? 382 VAL I CA  1 
ATOM 395  C C   . VAL A 1 50  ? 271.673 247.656 271.549 1.00 34173. ? 382 VAL I C   1 
ATOM 396  O O   . VAL A 1 50  ? 270.868 248.325 272.199 1.00 34172. ? 382 VAL I O   1 
ATOM 397  C CB  . VAL A 1 50  ? 274.132 248.344 271.322 1.00 34095. ? 382 VAL I CB  1 
ATOM 398  C CG1 . VAL A 1 50  ? 274.079 248.859 272.753 1.00 34122. ? 382 VAL I CG1 1 
ATOM 399  C CG2 . VAL A 1 50  ? 274.855 247.001 271.204 1.00 34358. ? 382 VAL I CG2 1 
ATOM 400  N N   . SER A 1 51  ? 271.649 246.336 271.538 1.00 36904. ? 383 SER I N   1 
ATOM 401  C CA  . SER A 1 51  ? 270.692 245.626 272.375 1.00 37143. ? 383 SER I CA  1 
ATOM 402  C C   . SER A 1 51  ? 271.342 245.171 273.668 1.00 37427. ? 383 SER I C   1 
ATOM 403  O O   . SER A 1 51  ? 272.476 244.674 273.634 1.00 37557. ? 383 SER I O   1 
ATOM 404  C CB  . SER A 1 51  ? 270.115 244.424 271.636 1.00 37234. ? 383 SER I CB  1 
ATOM 405  O OG  . SER A 1 51  ? 269.162 244.839 270.674 1.00 37091. ? 383 SER I OG  1 
ATOM 406  N N   . PRO A 1 52  ? 270.669 245.394 274.809 1.00 41892. ? 384 PRO I N   1 
ATOM 407  C CA  . PRO A 1 52  ? 271.256 245.039 276.118 1.00 42060. ? 384 PRO I CA  1 
ATOM 408  C C   . PRO A 1 52  ? 271.567 243.563 276.248 1.00 42348. ? 384 PRO I C   1 
ATOM 409  O O   . PRO A 1 52  ? 272.490 243.181 276.973 1.00 42300. ? 384 PRO I O   1 
ATOM 410  C CB  . PRO A 1 52  ? 270.183 245.486 277.116 1.00 42076. ? 384 PRO I CB  1 
ATOM 411  C CG  . PRO A 1 52  ? 268.931 245.576 276.330 1.00 42107. ? 384 PRO I CG  1 
ATOM 412  C CD  . PRO A 1 52  ? 269.326 245.975 274.950 1.00 41947. ? 384 PRO I CD  1 
ATOM 413  N N   . THR A 1 53  ? 270.736 242.720 275.661 1.00 46802. ? 385 THR I N   1 
ATOM 414  C CA  . THR A 1 53  ? 270.955 241.286 275.642 1.00 46990. ? 385 THR I CA  1 
ATOM 415  C C   . THR A 1 53  ? 271.572 240.945 274.293 1.00 46974. ? 385 THR I C   1 
ATOM 416  O O   . THR A 1 53  ? 271.193 241.535 273.276 1.00 46932. ? 385 THR I O   1 
ATOM 417  C CB  . THR A 1 53  ? 269.648 240.521 275.850 1.00 47089. ? 385 THR I CB  1 
ATOM 418  O OG1 . THR A 1 53  ? 268.779 240.745 274.733 1.00 47084. ? 385 THR I OG1 1 
ATOM 419  C CG2 . THR A 1 53  ? 268.959 240.992 277.121 1.00 47031. ? 385 THR I CG2 1 
ATOM 420  N N   . LYS A 1 54  ? 272.593 240.076 274.319 1.00 47206. ? 386 LYS I N   1 
ATOM 421  C CA  . LYS A 1 54  ? 273.323 239.519 273.168 1.00 47291. ? 386 LYS I CA  1 
ATOM 422  C C   . LYS A 1 54  ? 274.333 240.477 272.538 1.00 47188. ? 386 LYS I C   1 
ATOM 423  O O   . LYS A 1 54  ? 274.670 240.305 271.363 1.00 47261. ? 386 LYS I O   1 
ATOM 424  C CB  . LYS A 1 54  ? 272.409 238.951 272.066 1.00 47333. ? 386 LYS I CB  1 
ATOM 425  C CG  . LYS A 1 54  ? 271.528 237.730 272.422 1.00 47334. ? 386 LYS I CG  1 
ATOM 426  C CD  . LYS A 1 54  ? 272.297 236.405 272.595 1.00 47317. ? 386 LYS I CD  1 
ATOM 427  C CE  . LYS A 1 54  ? 272.681 236.075 274.039 1.00 47325. ? 386 LYS I CE  1 
ATOM 428  N NZ  . LYS A 1 54  ? 273.322 234.738 274.142 1.00 47343. ? 386 LYS I NZ  1 
ATOM 429  N N   . LEU A 1 55  ? 274.825 241.496 273.246 1.00 44987. ? 387 LEU I N   1 
ATOM 430  C CA  . LEU A 1 55  ? 275.756 242.441 272.633 1.00 44941. ? 387 LEU I CA  1 
ATOM 431  C C   . LEU A 1 55  ? 277.201 241.951 272.701 1.00 44997. ? 387 LEU I C   1 
ATOM 432  O O   . LEU A 1 55  ? 278.120 242.721 272.401 1.00 45000. ? 387 LEU I O   1 
ATOM 433  C CB  . LEU A 1 55  ? 275.672 243.832 273.277 1.00 44875. ? 387 LEU I CB  1 
ATOM 434  C CG  . LEU A 1 55  ? 276.246 244.169 274.656 1.00 44858. ? 387 LEU I CG  1 
ATOM 435  C CD1 . LEU A 1 55  ? 276.386 245.679 274.804 1.00 44674. ? 387 LEU I CD1 1 
ATOM 436  C CD2 . LEU A 1 55  ? 275.401 243.623 275.746 1.00 44879. ? 387 LEU I CD2 1 
ATOM 437  N N   . ASN A 1 56  ? 277.411 240.695 273.107 1.00 45895. ? 388 ASN I N   1 
ATOM 438  C CA  . ASN A 1 56  ? 278.747 240.123 273.240 1.00 45930. ? 388 ASN I CA  1 
ATOM 439  C C   . ASN A 1 56  ? 279.438 240.010 271.887 1.00 45976. ? 388 ASN I C   1 
ATOM 440  O O   . ASN A 1 56  ? 280.654 240.210 271.791 1.00 46064. ? 388 ASN I O   1 
ATOM 441  C CB  . ASN A 1 56  ? 278.663 238.762 273.920 1.00 45919. ? 388 ASN I CB  1 
ATOM 442  C CG  . ASN A 1 56  ? 278.072 238.848 275.307 1.00 45890. ? 388 ASN I CG  1 
ATOM 443  O OD1 . ASN A 1 56  ? 276.911 238.509 275.520 1.00 45890. ? 388 ASN I OD1 1 
ATOM 444  N ND2 . ASN A 1 56  ? 278.869 239.305 276.262 1.00 45873. ? 388 ASN I ND2 1 
ATOM 445  N N   . ASP A 1 57  ? 278.679 239.637 270.848 1.00 46695. ? 389 ASP I N   1 
ATOM 446  C CA  . ASP A 1 57  ? 279.237 239.427 269.514 1.00 46734. ? 389 ASP I CA  1 
ATOM 447  C C   . ASP A 1 57  ? 279.843 240.708 268.956 1.00 46780. ? 389 ASP I C   1 
ATOM 448  O O   . ASP A 1 57  ? 280.873 240.665 268.274 1.00 46834. ? 389 ASP I O   1 
ATOM 449  C CB  . ASP A 1 57  ? 278.152 238.906 268.574 1.00 46780. ? 389 ASP I CB  1 
ATOM 450  C CG  . ASP A 1 57  ? 277.655 237.531 268.963 1.00 46771. ? 389 ASP I CG  1 
ATOM 451  O OD1 . ASP A 1 57  ? 278.439 236.759 269.553 1.00 46780. ? 389 ASP I OD1 1 
ATOM 452  O OD2 . ASP A 1 57  ? 276.479 237.222 268.678 1.00 46758. ? 389 ASP I OD2 1 
ATOM 453  N N   . LEU A 1 58  ? 279.180 241.843 269.183 1.00 46076. ? 390 LEU I N   1 
ATOM 454  C CA  . LEU A 1 58  ? 279.649 243.132 268.689 1.00 46059. ? 390 LEU I CA  1 
ATOM 455  C C   . LEU A 1 58  ? 280.980 243.503 269.337 1.00 46142. ? 390 LEU I C   1 
ATOM 456  O O   . LEU A 1 58  ? 281.187 243.287 270.533 1.00 46086. ? 390 LEU I O   1 
ATOM 457  C CB  . LEU A 1 58  ? 278.619 244.232 268.968 1.00 45996. ? 390 LEU I CB  1 
ATOM 458  C CG  . LEU A 1 58  ? 277.311 244.303 268.176 1.00 46003. ? 390 LEU I CG  1 
ATOM 459  C CD1 . LEU A 1 58  ? 276.254 243.339 268.707 1.00 45995. ? 390 LEU I CD1 1 
ATOM 460  C CD2 . LEU A 1 58  ? 276.775 245.727 268.134 1.00 45985. ? 390 LEU I CD2 1 
ATOM 461  N N   . CYS A 1 59  ? 281.892 244.041 268.533 1.00 49352. ? 391 CYS I N   1 
ATOM 462  C CA  . CYS A 1 59  ? 283.227 244.407 268.987 1.00 49367. ? 391 CYS I CA  1 
ATOM 463  C C   . CYS A 1 59  ? 283.342 245.924 269.045 1.00 49245. ? 391 CYS I C   1 
ATOM 464  O O   . CYS A 1 59  ? 283.018 246.614 268.072 1.00 49379. ? 391 CYS I O   1 
ATOM 465  C CB  . CYS A 1 59  ? 284.302 243.849 268.056 1.00 49538. ? 391 CYS I CB  1 
ATOM 466  S SG  . CYS A 1 59  ? 284.581 242.074 268.129 1.00 49545. ? 391 CYS I SG  1 
ATOM 467  N N   . PHE A 1 60  ? 283.807 246.433 270.179 1.00 43818. ? 392 PHE I N   1 
ATOM 468  C CA  . PHE A 1 60  ? 283.916 247.861 270.446 1.00 43568. ? 392 PHE I CA  1 
ATOM 469  C C   . PHE A 1 60  ? 285.381 248.240 270.570 1.00 43712. ? 392 PHE I C   1 
ATOM 470  O O   . PHE A 1 60  ? 286.157 247.509 271.186 1.00 43875. ? 392 PHE I O   1 
ATOM 471  C CB  . PHE A 1 60  ? 283.156 248.257 271.711 1.00 43352. ? 392 PHE I CB  1 
ATOM 472  C CG  . PHE A 1 60  ? 281.803 247.627 271.829 1.00 43336. ? 392 PHE I CG  1 
ATOM 473  C CD1 . PHE A 1 60  ? 280.835 247.860 270.866 1.00 43439. ? 392 PHE I CD1 1 
ATOM 474  C CD2 . PHE A 1 60  ? 281.495 246.813 272.900 1.00 43335. ? 392 PHE I CD2 1 
ATOM 475  C CE1 . PHE A 1 60  ? 279.583 247.291 270.973 1.00 43427. ? 392 PHE I CE1 1 
ATOM 476  C CE2 . PHE A 1 60  ? 280.246 246.237 273.015 1.00 43336. ? 392 PHE I CE2 1 
ATOM 477  C CZ  . PHE A 1 60  ? 279.289 246.474 272.051 1.00 43353. ? 392 PHE I CZ  1 
ATOM 478  N N   . THR A 1 61  ? 285.780 249.326 269.911 1.00 46025. ? 393 THR I N   1 
ATOM 479  C CA  . THR A 1 61  ? 287.170 249.755 270.021 1.00 46074. ? 393 THR I CA  1 
ATOM 480  C C   . THR A 1 61  ? 287.429 250.512 271.317 1.00 45910. ? 393 THR I C   1 
ATOM 481  O O   . THR A 1 61  ? 288.340 250.166 272.079 1.00 45980. ? 393 THR I O   1 
ATOM 482  C CB  . THR A 1 61  ? 287.545 250.635 268.830 1.00 46139. ? 393 THR I CB  1 
ATOM 483  O OG1 . THR A 1 61  ? 287.594 249.845 267.636 1.00 46522. ? 393 THR I OG1 1 
ATOM 484  C CG2 . THR A 1 61  ? 288.885 251.316 269.068 1.00 46247. ? 393 THR I CG2 1 
ATOM 485  N N   . ASN A 1 62  ? 286.616 251.523 271.602 1.00 42560. ? 394 ASN I N   1 
ATOM 486  C CA  . ASN A 1 62  ? 286.823 252.412 272.738 1.00 42322. ? 394 ASN I CA  1 
ATOM 487  C C   . ASN A 1 62  ? 285.592 252.379 273.627 1.00 41988. ? 394 ASN I C   1 
ATOM 488  O O   . ASN A 1 62  ? 284.512 252.806 273.207 1.00 42093. ? 394 ASN I O   1 
ATOM 489  C CB  . ASN A 1 62  ? 287.104 253.836 272.266 1.00 42399. ? 394 ASN I CB  1 
ATOM 490  C CG  . ASN A 1 62  ? 287.994 254.595 273.220 1.00 42136. ? 394 ASN I CG  1 
ATOM 491  O OD1 . ASN A 1 62  ? 288.170 254.197 274.371 1.00 41973. ? 394 ASN I OD1 1 
ATOM 492  N ND2 . ASN A 1 62  ? 288.556 255.703 272.750 1.00 42195. ? 394 ASN I ND2 1 
ATOM 493  N N   . VAL A 1 63  ? 285.744 251.874 274.847 1.00 34566. ? 395 VAL I N   1 
ATOM 494  C CA  . VAL A 1 63  ? 284.668 251.880 275.828 1.00 34252. ? 395 VAL I CA  1 
ATOM 495  C C   . VAL A 1 63  ? 285.030 252.866 276.929 1.00 34195. ? 395 VAL I C   1 
ATOM 496  O O   . VAL A 1 63  ? 286.145 252.836 277.458 1.00 34364. ? 395 VAL I O   1 
ATOM 497  C CB  . VAL A 1 63  ? 284.398 250.470 276.380 1.00 34142. ? 395 VAL I CB  1 
ATOM 498  C CG1 . VAL A 1 63  ? 283.372 250.504 277.498 1.00 34024. ? 395 VAL I CG1 1 
ATOM 499  C CG2 . VAL A 1 63  ? 283.877 249.591 275.276 1.00 34420. ? 395 VAL I CG2 1 
ATOM 500  N N   . TYR A 1 64  ? 284.088 253.746 277.262 1.00 34037. ? 396 TYR I N   1 
ATOM 501  C CA  . TYR A 1 64  ? 284.241 254.745 278.309 1.00 33896. ? 396 TYR I CA  1 
ATOM 502  C C   . TYR A 1 64  ? 283.138 254.540 279.329 1.00 33925. ? 396 TYR I C   1 
ATOM 503  O O   . TYR A 1 64  ? 281.969 254.417 278.958 1.00 34128. ? 396 TYR I O   1 
ATOM 504  C CB  . TYR A 1 64  ? 284.145 256.166 277.754 1.00 33988. ? 396 TYR I CB  1 
ATOM 505  C CG  . TYR A 1 64  ? 285.371 256.682 277.048 1.00 34015. ? 396 TYR I CG  1 
ATOM 506  C CD1 . TYR A 1 64  ? 286.563 256.860 277.731 1.00 34131. ? 396 TYR I CD1 1 
ATOM 507  C CD2 . TYR A 1 64  ? 285.321 257.036 275.709 1.00 34085. ? 396 TYR I CD2 1 
ATOM 508  C CE1 . TYR A 1 64  ? 287.681 257.348 277.093 1.00 34166. ? 396 TYR I CE1 1 
ATOM 509  C CE2 . TYR A 1 64  ? 286.432 257.526 275.062 1.00 34164. ? 396 TYR I CE2 1 
ATOM 510  C CZ  . TYR A 1 64  ? 287.609 257.679 275.758 1.00 34159. ? 396 TYR I CZ  1 
ATOM 511  O OH  . TYR A 1 64  ? 288.721 258.167 275.114 1.00 34183. ? 396 TYR I OH  1 
ATOM 512  N N   . ALA A 1 65  ? 283.497 254.509 280.604 1.00 33898. ? 397 ALA I N   1 
ATOM 513  C CA  . ALA A 1 65  ? 282.526 254.391 281.681 1.00 33891. ? 397 ALA I CA  1 
ATOM 514  C C   . ALA A 1 65  ? 282.466 255.704 282.451 1.00 33971. ? 397 ALA I C   1 
ATOM 515  O O   . ALA A 1 65  ? 283.476 256.146 283.004 1.00 34093. ? 397 ALA I O   1 
ATOM 516  C CB  . ALA A 1 65  ? 282.883 253.230 282.602 1.00 33969. ? 397 ALA I CB  1 
ATOM 517  N N   . ASP A 1 66  ? 281.287 256.319 282.487 1.00 34024. ? 398 ASP I N   1 
ATOM 518  C CA  . ASP A 1 66  ? 281.070 257.597 283.155 1.00 33900. ? 398 ASP I CA  1 
ATOM 519  C C   . ASP A 1 66  ? 280.195 257.378 284.381 1.00 33888. ? 398 ASP I C   1 
ATOM 520  O O   . ASP A 1 66  ? 279.071 256.894 284.254 1.00 34126. ? 398 ASP I O   1 
ATOM 521  C CB  . ASP A 1 66  ? 280.420 258.598 282.204 1.00 33977. ? 398 ASP I CB  1 
ATOM 522  C CG  . ASP A 1 66  ? 281.284 258.906 281.004 1.00 33978. ? 398 ASP I CG  1 
ATOM 523  O OD1 . ASP A 1 66  ? 282.451 258.480 280.979 1.00 33969. ? 398 ASP I OD1 1 
ATOM 524  O OD2 . ASP A 1 66  ? 280.792 259.571 280.075 1.00 34036. ? 398 ASP I OD2 1 
ATOM 525  N N   . SER A 1 67  ? 280.686 257.769 285.554 1.00 33831. ? 399 SER I N   1 
ATOM 526  C CA  . SER A 1 67  ? 280.003 257.501 286.813 1.00 33862. ? 399 SER I CA  1 
ATOM 527  C C   . SER A 1 67  ? 279.659 258.786 287.550 1.00 33965. ? 399 SER I C   1 
ATOM 528  O O   . SER A 1 67  ? 280.519 259.651 287.736 1.00 34135. ? 399 SER I O   1 
ATOM 529  C CB  . SER A 1 67  ? 280.864 256.622 287.713 1.00 33983. ? 399 SER I CB  1 
ATOM 530  O OG  . SER A 1 67  ? 280.996 255.335 287.163 1.00 34095. ? 399 SER I OG  1 
ATOM 531  N N   . PHE A 1 68  ? 278.404 258.896 287.980 1.00 33961. ? 400 PHE I N   1 
ATOM 532  C CA  . PHE A 1 68  ? 277.932 260.049 288.730 1.00 33892. ? 400 PHE I CA  1 
ATOM 533  C C   . PHE A 1 68  ? 276.707 259.639 289.533 1.00 33882. ? 400 PHE I C   1 
ATOM 534  O O   . PHE A 1 68  ? 276.100 258.600 289.272 1.00 34139. ? 400 PHE I O   1 
ATOM 535  C CB  . PHE A 1 68  ? 277.641 261.236 287.809 1.00 33971. ? 400 PHE I CB  1 
ATOM 536  C CG  . PHE A 1 68  ? 276.855 260.898 286.576 1.00 33949. ? 400 PHE I CG  1 
ATOM 537  C CD1 . PHE A 1 68  ? 275.475 260.875 286.603 1.00 33988. ? 400 PHE I CD1 1 
ATOM 538  C CD2 . PHE A 1 68  ? 277.500 260.625 285.382 1.00 33955. ? 400 PHE I CD2 1 
ATOM 539  C CE1 . PHE A 1 68  ? 274.762 260.581 285.475 1.00 34033. ? 400 PHE I CE1 1 
ATOM 540  C CE2 . PHE A 1 68  ? 276.788 260.320 284.255 1.00 33972. ? 400 PHE I CE2 1 
ATOM 541  C CZ  . PHE A 1 68  ? 275.419 260.297 284.300 1.00 34031. ? 400 PHE I CZ  1 
ATOM 542  N N   . VAL A 1 69  ? 276.357 260.458 290.524 1.00 33820. ? 401 VAL I N   1 
ATOM 543  C CA  . VAL A 1 69  ? 275.154 260.257 291.328 1.00 33895. ? 401 VAL I CA  1 
ATOM 544  C C   . VAL A 1 69  ? 274.191 261.411 291.085 1.00 33951. ? 401 VAL I C   1 
ATOM 545  O O   . VAL A 1 69  ? 274.590 262.580 291.118 1.00 34050. ? 401 VAL I O   1 
ATOM 546  C CB  . VAL A 1 69  ? 275.498 260.129 292.822 1.00 33890. ? 401 VAL I CB  1 
ATOM 547  C CG1 . VAL A 1 69  ? 274.303 260.422 293.727 1.00 34006. ? 401 VAL I CG1 1 
ATOM 548  C CG2 . VAL A 1 69  ? 276.050 258.776 293.115 1.00 33958. ? 401 VAL I CG2 1 
ATOM 549  N N   . ILE A 1 70  ? 272.929 261.075 290.814 1.00 33972. ? 402 ILE I N   1 
ATOM 550  C CA  . ILE A 1 70  ? 271.857 262.033 290.592 1.00 33910. ? 402 ILE I CA  1 
ATOM 551  C C   . ILE A 1 70  ? 270.603 261.529 291.289 1.00 33982. ? 402 ILE I C   1 
ATOM 552  O O   . ILE A 1 70  ? 270.529 260.389 291.746 1.00 34125. ? 402 ILE I O   1 
ATOM 553  C CB  . ILE A 1 70  ? 271.513 262.231 289.107 1.00 33930. ? 402 ILE I CB  1 
ATOM 554  C CG1 . ILE A 1 70  ? 271.446 260.877 288.424 1.00 33918. ? 402 ILE I CG1 1 
ATOM 555  C CG2 . ILE A 1 70  ? 272.525 263.108 288.432 1.00 34056. ? 402 ILE I CG2 1 
ATOM 556  C CD1 . ILE A 1 70  ? 270.866 260.936 287.084 1.00 33962. ? 402 ILE I CD1 1 
ATOM 557  N N   . ARG A 1 71  ? 269.625 262.417 291.392 1.00 33991. ? 403 ARG I N   1 
ATOM 558  C CA  . ARG A 1 71  ? 268.301 262.086 291.888 1.00 33938. ? 403 ARG I CA  1 
ATOM 559  C C   . ARG A 1 71  ? 267.567 261.166 290.924 1.00 34015. ? 403 ARG I C   1 
ATOM 560  O O   . ARG A 1 71  ? 267.921 261.041 289.749 1.00 34165. ? 403 ARG I O   1 
ATOM 561  C CB  . ARG A 1 71  ? 267.514 263.373 292.097 1.00 33985. ? 403 ARG I CB  1 
ATOM 562  C CG  . ARG A 1 71  ? 267.752 264.077 293.385 1.00 34086. ? 403 ARG I CG  1 
ATOM 563  C CD  . ARG A 1 71  ? 266.909 265.331 293.420 1.00 34051. ? 403 ARG I CD  1 
ATOM 564  N NE  . ARG A 1 71  ? 265.475 265.189 293.288 1.00 34108. ? 403 ARG I NE  1 
ATOM 565  C CZ  . ARG A 1 71  ? 264.824 265.783 292.299 1.00 34122. ? 403 ARG I CZ  1 
ATOM 566  N NH1 . ARG A 1 71  ? 265.462 266.527 291.411 1.00 34078. ? 403 ARG I NH1 1 
ATOM 567  N NH2 . ARG A 1 71  ? 263.512 265.616 292.183 1.00 34180. ? 403 ARG I NH2 1 
ATOM 568  N N   . GLY A 1 72  ? 266.566 260.469 291.472 1.00 34039. ? 404 GLY I N   1 
ATOM 569  C CA  . GLY A 1 72  ? 265.785 259.523 290.688 1.00 34095. ? 404 GLY I CA  1 
ATOM 570  C C   . GLY A 1 72  ? 265.072 260.164 289.516 1.00 34157. ? 404 GLY I C   1 
ATOM 571  O O   . GLY A 1 72  ? 264.886 259.536 288.472 1.00 34063. ? 404 GLY I O   1 
ATOM 572  N N   . ASP A 1 73  ? 264.611 261.401 289.703 1.00 36844. ? 405 ASP I N   1 
ATOM 573  C CA  . ASP A 1 73  ? 263.949 262.144 288.638 1.00 36908. ? 405 ASP I CA  1 
ATOM 574  C C   . ASP A 1 73  ? 264.883 262.425 287.462 1.00 36802. ? 405 ASP I C   1 
ATOM 575  O O   . ASP A 1 73  ? 264.449 262.420 286.307 1.00 36851. ? 405 ASP I O   1 
ATOM 576  C CB  . ASP A 1 73  ? 263.392 263.442 289.212 1.00 36999. ? 405 ASP I CB  1 
ATOM 577  C CG  . ASP A 1 73  ? 262.159 263.214 290.060 1.00 37057. ? 405 ASP I CG  1 
ATOM 578  O OD1 . ASP A 1 73  ? 261.615 262.090 290.022 1.00 37103. ? 405 ASP I OD1 1 
ATOM 579  O OD2 . ASP A 1 73  ? 261.737 264.151 290.771 1.00 36985. ? 405 ASP I OD2 1 
ATOM 580  N N   . GLU A 1 74  ? 266.163 262.697 287.735 1.00 34154. ? 406 GLU I N   1 
ATOM 581  C CA  . GLU A 1 74  ? 267.128 263.081 286.704 1.00 34003. ? 406 GLU I CA  1 
ATOM 582  C C   . GLU A 1 74  ? 267.568 261.922 285.809 1.00 34074. ? 406 GLU I C   1 
ATOM 583  O O   . GLU A 1 74  ? 268.252 262.158 284.793 1.00 34131. ? 406 GLU I O   1 
ATOM 584  C CB  . GLU A 1 74  ? 268.349 263.707 287.371 1.00 34045. ? 406 GLU I CB  1 
ATOM 585  C CG  . GLU A 1 74  ? 268.039 264.566 288.598 1.00 34107. ? 406 GLU I CG  1 
ATOM 586  C CD  . GLU A 1 74  ? 267.180 265.777 288.309 1.00 34132. ? 406 GLU I CD  1 
ATOM 587  O OE1 . GLU A 1 74  ? 267.272 266.343 287.203 1.00 34137. ? 406 GLU I OE1 1 
ATOM 588  O OE2 . GLU A 1 74  ? 266.403 266.173 289.200 1.00 34213. ? 406 GLU I OE2 1 
ATOM 589  N N   . VAL A 1 75  ? 267.221 260.685 286.182 1.00 34103. ? 407 VAL I N   1 
ATOM 590  C CA  . VAL A 1 75  ? 267.631 259.500 285.431 1.00 34011. ? 407 VAL I CA  1 
ATOM 591  C C   . VAL A 1 75  ? 267.050 259.542 284.022 1.00 34018. ? 407 VAL I C   1 
ATOM 592  O O   . VAL A 1 75  ? 267.696 259.116 283.056 1.00 34059. ? 407 VAL I O   1 
ATOM 593  C CB  . VAL A 1 75  ? 267.232 258.226 286.204 1.00 34029. ? 407 VAL I CB  1 
ATOM 594  C CG1 . VAL A 1 75  ? 267.617 256.965 285.452 1.00 34034. ? 407 VAL I CG1 1 
ATOM 595  C CG2 . VAL A 1 75  ? 267.870 258.230 287.579 1.00 34034. ? 407 VAL I CG2 1 
ATOM 596  N N   . ARG A 1 76  ? 265.819 260.054 283.887 1.00 34049. ? 408 ARG I N   1 
ATOM 597  C CA  . ARG A 1 76  ? 265.227 260.245 282.566 1.00 33995. ? 408 ARG I CA  1 
ATOM 598  C C   . ARG A 1 76  ? 266.037 261.252 281.750 1.00 34043. ? 408 ARG I C   1 
ATOM 599  O O   . ARG A 1 76  ? 266.157 261.114 280.529 1.00 34156. ? 408 ARG I O   1 
ATOM 600  C CB  . ARG A 1 76  ? 263.744 260.648 282.682 1.00 34009. ? 408 ARG I CB  1 
ATOM 601  C CG  . ARG A 1 76  ? 263.394 262.046 283.230 1.00 34070. ? 408 ARG I CG  1 
ATOM 602  C CD  . ARG A 1 76  ? 263.210 263.083 282.115 1.00 34068. ? 408 ARG I CD  1 
ATOM 603  N NE  . ARG A 1 76  ? 262.971 264.431 282.612 1.00 34086. ? 408 ARG I NE  1 
ATOM 604  C CZ  . ARG A 1 76  ? 262.971 265.511 281.844 1.00 34070. ? 408 ARG I CZ  1 
ATOM 605  N NH1 . ARG A 1 76  ? 263.201 265.434 280.545 1.00 34056. ? 408 ARG I NH1 1 
ATOM 606  N NH2 . ARG A 1 76  ? 262.745 266.700 282.396 1.00 34090. ? 408 ARG I NH2 1 
ATOM 607  N N   . GLN A 1 77  ? 266.556 262.299 282.407 1.00 34052. ? 409 GLN I N   1 
ATOM 608  C CA  . GLN A 1 77  ? 267.369 263.302 281.725 1.00 34005. ? 409 GLN I CA  1 
ATOM 609  C C   . GLN A 1 77  ? 268.678 262.715 281.222 1.00 34055. ? 409 GLN I C   1 
ATOM 610  O O   . GLN A 1 77  ? 269.260 263.242 280.269 1.00 34031. ? 409 GLN I O   1 
ATOM 611  C CB  . GLN A 1 77  ? 267.635 264.499 282.632 1.00 34010. ? 409 GLN I CB  1 
ATOM 612  C CG  . GLN A 1 77  ? 266.458 264.881 283.487 1.00 34128. ? 409 GLN I CG  1 
ATOM 613  C CD  . GLN A 1 77  ? 266.640 266.224 284.131 1.00 34031. ? 409 GLN I CD  1 
ATOM 614  O OE1 . GLN A 1 77  ? 267.704 266.822 284.038 1.00 34048. ? 409 GLN I OE1 1 
ATOM 615  N NE2 . GLN A 1 77  ? 265.608 266.699 284.812 1.00 34051. ? 409 GLN I NE2 1 
ATOM 616  N N   . ILE A 1 78  ? 269.171 261.647 281.848 1.00 34129. ? 410 ILE I N   1 
ATOM 617  C CA  . ILE A 1 78  ? 270.384 261.024 281.314 1.00 33991. ? 410 ILE I CA  1 
ATOM 618  C C   . ILE A 1 78  ? 269.966 260.092 280.175 1.00 33964. ? 410 ILE I C   1 
ATOM 619  O O   . ILE A 1 78  ? 269.859 258.873 280.344 1.00 34040. ? 410 ILE I O   1 
ATOM 620  C CB  . ILE A 1 78  ? 271.189 260.287 282.402 1.00 33949. ? 410 ILE I CB  1 
ATOM 621  C CG1 . ILE A 1 78  ? 271.520 261.244 283.540 1.00 33952. ? 410 ILE I CG1 1 
ATOM 622  C CG2 . ILE A 1 78  ? 272.522 259.762 281.853 1.00 34004. ? 410 ILE I CG2 1 
ATOM 623  C CD1 . ILE A 1 78  ? 272.452 262.371 283.173 1.00 33980. ? 410 ILE I CD1 1 
ATOM 624  N N   . ALA A 1 79  ? 269.635 260.682 279.031 1.00 34007. ? 411 ALA I N   1 
ATOM 625  C CA  . ALA A 1 79  ? 269.266 259.972 277.816 1.00 33960. ? 411 ALA I CA  1 
ATOM 626  C C   . ALA A 1 79  ? 269.568 260.887 276.639 1.00 34004. ? 411 ALA I C   1 
ATOM 627  O O   . ALA A 1 79  ? 269.670 262.105 276.819 1.00 34133. ? 411 ALA I O   1 
ATOM 628  C CB  . ALA A 1 79  ? 267.780 259.576 277.848 1.00 34026. ? 411 ALA I CB  1 
ATOM 629  N N   . PRO A 1 80  ? 269.770 260.335 275.432 1.00 33957. ? 412 PRO I N   1 
ATOM 630  C CA  . PRO A 1 80  ? 270.061 261.197 274.274 1.00 34005. ? 412 PRO I CA  1 
ATOM 631  C C   . PRO A 1 80  ? 268.890 262.101 273.913 1.00 34144. ? 412 PRO I C   1 
ATOM 632  O O   . PRO A 1 80  ? 267.731 261.680 273.925 1.00 34140. ? 412 PRO I O   1 
ATOM 633  C CB  . PRO A 1 80  ? 270.367 260.198 273.154 1.00 33982. ? 412 PRO I CB  1 
ATOM 634  C CG  . PRO A 1 80  ? 270.756 258.972 273.840 1.00 34027. ? 412 PRO I CG  1 
ATOM 635  C CD  . PRO A 1 80  ? 269.944 258.915 275.079 1.00 34023. ? 412 PRO I CD  1 
ATOM 636  N N   . GLY A 1 81  ? 269.217 263.339 273.550 1.00 35067. ? 413 GLY I N   1 
ATOM 637  C CA  . GLY A 1 81  ? 268.228 264.340 273.172 1.00 35065. ? 413 GLY I CA  1 
ATOM 638  C C   . GLY A 1 81  ? 267.203 264.653 274.240 1.00 35059. ? 413 GLY I C   1 
ATOM 639  O O   . GLY A 1 81  ? 266.010 264.770 273.937 1.00 35056. ? 413 GLY I O   1 
ATOM 640  N N   . GLN A 1 82  ? 267.644 264.794 275.486 1.00 35045. ? 414 GLN I N   1 
ATOM 641  C CA  . GLN A 1 82  ? 266.784 265.121 276.614 1.00 35038. ? 414 GLN I CA  1 
ATOM 642  C C   . GLN A 1 82  ? 267.181 266.467 277.196 1.00 35182. ? 414 GLN I C   1 
ATOM 643  O O   . GLN A 1 82  ? 268.365 266.812 277.229 1.00 35137. ? 414 GLN I O   1 
ATOM 644  C CB  . GLN A 1 82  ? 266.859 264.053 277.703 1.00 34970. ? 414 GLN I CB  1 
ATOM 645  C CG  . GLN A 1 82  ? 266.034 262.819 277.425 1.00 34985. ? 414 GLN I CG  1 
ATOM 646  C CD  . GLN A 1 82  ? 264.580 262.991 277.794 1.00 35031. ? 414 GLN I CD  1 
ATOM 647  O OE1 . GLN A 1 82  ? 264.168 262.649 278.900 1.00 35068. ? 414 GLN I OE1 1 
ATOM 648  N NE2 . GLN A 1 82  ? 263.788 263.508 276.864 1.00 35080. ? 414 GLN I NE2 1 
ATOM 649  N N   . THR A 1 83  ? 266.187 267.232 277.633 1.00 37174. ? 415 THR I N   1 
ATOM 650  C CA  . THR A 1 83  ? 266.400 268.560 278.191 1.00 37181. ? 415 THR I CA  1 
ATOM 651  C C   . THR A 1 83  ? 266.015 268.566 279.668 1.00 37058. ? 415 THR I C   1 
ATOM 652  O O   . THR A 1 83  ? 264.961 268.050 280.055 1.00 37098. ? 415 THR I O   1 
ATOM 653  C CB  . THR A 1 83  ? 265.644 269.631 277.381 1.00 37294. ? 415 THR I CB  1 
ATOM 654  O OG1 . THR A 1 83  ? 265.904 270.933 277.922 1.00 37303. ? 415 THR I OG1 1 
ATOM 655  C CG2 . THR A 1 83  ? 264.135 269.368 277.273 1.00 37283. ? 415 THR I CG2 1 
ATOM 656  N N   . GLY A 1 84  ? 266.931 269.046 280.496 1.00 34180. ? 416 GLY I N   1 
ATOM 657  C CA  . GLY A 1 84  ? 266.725 269.124 281.929 1.00 34109. ? 416 GLY I CA  1 
ATOM 658  C C   . GLY A 1 84  ? 267.819 269.977 282.523 1.00 34045. ? 416 GLY I C   1 
ATOM 659  O O   . GLY A 1 84  ? 268.710 270.447 281.818 1.00 34156. ? 416 GLY I O   1 
ATOM 660  N N   . LYS A 1 85  ? 267.724 270.207 283.833 1.00 33949. ? 417 LYS I N   1 
ATOM 661  C CA  . LYS A 1 85  ? 268.795 270.915 284.530 1.00 33990. ? 417 LYS I CA  1 
ATOM 662  C C   . LYS A 1 85  ? 270.100 270.125 284.476 1.00 34037. ? 417 LYS I C   1 
ATOM 663  O O   . LYS A 1 85  ? 271.162 270.679 284.156 1.00 34079. ? 417 LYS I O   1 
ATOM 664  C CB  . LYS A 1 85  ? 268.370 271.170 285.978 1.00 34005. ? 417 LYS I CB  1 
ATOM 665  C CG  . LYS A 1 85  ? 269.283 272.063 286.792 1.00 34041. ? 417 LYS I CG  1 
ATOM 666  C CD  . LYS A 1 85  ? 269.417 273.441 286.165 1.00 34104. ? 417 LYS I CD  1 
ATOM 667  C CE  . LYS A 1 85  ? 268.079 274.176 286.068 1.00 34046. ? 417 LYS I CE  1 
ATOM 668  N NZ  . LYS A 1 85  ? 267.598 274.688 287.375 1.00 34038. ? 417 LYS I NZ  1 
ATOM 669  N N   . ILE A 1 86  ? 270.015 268.813 284.724 1.00 34076. ? 418 ILE I N   1 
ATOM 670  C CA  . ILE A 1 86  ? 271.175 267.925 284.704 1.00 33993. ? 418 ILE I CA  1 
ATOM 671  C C   . ILE A 1 86  ? 271.742 267.811 283.296 1.00 33946. ? 418 ILE I C   1 
ATOM 672  O O   . ILE A 1 86  ? 272.958 267.886 283.097 1.00 34049. ? 418 ILE I O   1 
ATOM 673  C CB  . ILE A 1 86  ? 270.790 266.548 285.276 1.00 33930. ? 418 ILE I CB  1 
ATOM 674  C CG1 . ILE A 1 86  ? 270.510 266.647 286.769 1.00 33932. ? 418 ILE I CG1 1 
ATOM 675  C CG2 . ILE A 1 86  ? 271.884 265.533 285.051 1.00 33981. ? 418 ILE I CG2 1 
ATOM 676  C CD1 . ILE A 1 86  ? 271.661 267.117 287.561 1.00 34012. ? 418 ILE I CD1 1 
ATOM 677  N N   . ALA A 1 87  ? 270.869 267.654 282.299 1.00 33957. ? 419 ALA I N   1 
ATOM 678  C CA  . ALA A 1 87  ? 271.318 267.555 280.915 1.00 33964. ? 419 ALA I CA  1 
ATOM 679  C C   . ALA A 1 87  ? 271.951 268.852 280.431 1.00 33974. ? 419 ALA I C   1 
ATOM 680  O O   . ALA A 1 87  ? 273.011 268.828 279.799 1.00 33981. ? 419 ALA I O   1 
ATOM 681  C CB  . ALA A 1 87  ? 270.151 267.165 280.018 1.00 34028. ? 419 ALA I CB  1 
ATOM 682  N N   . ASP A 1 88  ? 271.327 269.991 280.730 1.00 34061. ? 420 ASP I N   1 
ATOM 683  C CA  . ASP A 1 88  ? 271.826 271.266 280.230 1.00 33981. ? 420 ASP I CA  1 
ATOM 684  C C   . ASP A 1 88  ? 273.139 271.677 280.883 1.00 33975. ? 420 ASP I C   1 
ATOM 685  O O   . ASP A 1 88  ? 274.042 272.163 280.193 1.00 34031. ? 420 ASP I O   1 
ATOM 686  C CB  . ASP A 1 88  ? 270.773 272.355 280.417 1.00 34045. ? 420 ASP I CB  1 
ATOM 687  C CG  . ASP A 1 88  ? 269.591 272.187 279.485 1.00 34067. ? 420 ASP I CG  1 
ATOM 688  O OD1 . ASP A 1 88  ? 269.666 271.336 278.574 1.00 34129. ? 420 ASP I OD1 1 
ATOM 689  O OD2 . ASP A 1 88  ? 268.584 272.900 279.669 1.00 34042. ? 420 ASP I OD2 1 
ATOM 690  N N   . TYR A 1 89  ? 273.286 271.508 282.204 1.00 34029. ? 421 TYR I N   1 
ATOM 691  C CA  . TYR A 1 89  ? 274.460 272.073 282.855 1.00 34020. ? 421 TYR I CA  1 
ATOM 692  C C   . TYR A 1 89  ? 275.407 271.073 283.506 1.00 33972. ? 421 TYR I C   1 
ATOM 693  O O   . TYR A 1 89  ? 276.485 271.485 283.945 1.00 33997. ? 421 TYR I O   1 
ATOM 694  C CB  . TYR A 1 89  ? 274.042 273.099 283.923 1.00 34078. ? 421 TYR I CB  1 
ATOM 695  C CG  . TYR A 1 89  ? 273.122 274.210 283.451 1.00 34060. ? 421 TYR I CG  1 
ATOM 696  C CD1 . TYR A 1 89  ? 273.231 274.751 282.172 1.00 34087. ? 421 TYR I CD1 1 
ATOM 697  C CD2 . TYR A 1 89  ? 272.157 274.730 284.294 1.00 34031. ? 421 TYR I CD2 1 
ATOM 698  C CE1 . TYR A 1 89  ? 272.401 275.760 281.748 1.00 34055. ? 421 TYR I CE1 1 
ATOM 699  C CE2 . TYR A 1 89  ? 271.318 275.742 283.878 1.00 34044. ? 421 TYR I CE2 1 
ATOM 700  C CZ  . TYR A 1 89  ? 271.446 276.254 282.604 1.00 34027. ? 421 TYR I CZ  1 
ATOM 701  O OH  . TYR A 1 89  ? 270.616 277.266 282.183 1.00 34035. ? 421 TYR I OH  1 
ATOM 702  N N   . ASN A 1 90  ? 275.061 269.787 283.582 1.00 34004. ? 422 ASN I N   1 
ATOM 703  C CA  . ASN A 1 90  ? 275.889 268.808 284.283 1.00 33979. ? 422 ASN I CA  1 
ATOM 704  C C   . ASN A 1 90  ? 276.460 267.728 283.373 1.00 33979. ? 422 ASN I C   1 
ATOM 705  O O   . ASN A 1 90  ? 277.677 267.672 283.194 1.00 33977. ? 422 ASN I O   1 
ATOM 706  C CB  . ASN A 1 90  ? 275.054 268.211 285.412 1.00 34020. ? 422 ASN I CB  1 
ATOM 707  C CG  . ASN A 1 90  ? 274.887 269.157 286.553 1.00 33979. ? 422 ASN I CG  1 
ATOM 708  O OD1 . ASN A 1 90  ? 275.863 269.529 287.177 1.00 34053. ? 422 ASN I OD1 1 
ATOM 709  N ND2 . ASN A 1 90  ? 273.676 269.627 286.779 1.00 34033. ? 422 ASN I ND2 1 
ATOM 710  N N   . TYR A 1 91  ? 275.631 266.855 282.810 1.00 34047. ? 423 TYR I N   1 
ATOM 711  C CA  . TYR A 1 91  ? 276.091 265.786 281.935 1.00 33966. ? 423 TYR I CA  1 
ATOM 712  C C   . TYR A 1 91  ? 275.241 265.784 280.677 1.00 33962. ? 423 TYR I C   1 
ATOM 713  O O   . TYR A 1 91  ? 274.015 265.702 280.762 1.00 34107. ? 423 TYR I O   1 
ATOM 714  C CB  . TYR A 1 91  ? 276.010 264.434 282.650 1.00 33992. ? 423 TYR I CB  1 
ATOM 715  C CG  . TYR A 1 91  ? 276.568 263.275 281.865 1.00 33941. ? 423 TYR I CG  1 
ATOM 716  C CD1 . TYR A 1 91  ? 277.934 263.072 281.779 1.00 33958. ? 423 TYR I CD1 1 
ATOM 717  C CD2 . TYR A 1 91  ? 275.729 262.378 281.219 1.00 34042. ? 423 TYR I CD2 1 
ATOM 718  C CE1 . TYR A 1 91  ? 278.452 262.019 281.067 1.00 33929. ? 423 TYR I CE1 1 
ATOM 719  C CE2 . TYR A 1 91  ? 276.239 261.324 280.503 1.00 34033. ? 423 TYR I CE2 1 
ATOM 720  C CZ  . TYR A 1 91  ? 277.603 261.151 280.435 1.00 33949. ? 423 TYR I CZ  1 
ATOM 721  O OH  . TYR A 1 91  ? 278.128 260.101 279.729 1.00 34077. ? 423 TYR I OH  1 
ATOM 722  N N   . LYS A 1 92  ? 275.887 265.803 279.518 1.00 33936. ? 424 LYS I N   1 
ATOM 723  C CA  . LYS A 1 92  ? 275.209 265.775 278.229 1.00 33968. ? 424 LYS I CA  1 
ATOM 724  C C   . LYS A 1 92  ? 275.575 264.528 277.447 1.00 34027. ? 424 LYS I C   1 
ATOM 725  O O   . LYS A 1 92  ? 276.754 264.185 277.323 1.00 34150. ? 424 LYS I O   1 
ATOM 726  C CB  . LYS A 1 92  ? 275.540 267.013 277.396 1.00 33992. ? 424 LYS I CB  1 
ATOM 727  C CG  . LYS A 1 92  ? 274.526 267.330 276.303 1.00 34043. ? 424 LYS I CG  1 
ATOM 728  C CD  . LYS A 1 92  ? 273.146 267.653 276.803 1.00 34093. ? 424 LYS I CD  1 
ATOM 729  C CE  . LYS A 1 92  ? 272.229 268.027 275.651 1.00 34048. ? 424 LYS I CE  1 
ATOM 730  N NZ  . LYS A 1 92  ? 270.833 268.284 276.099 1.00 34137. ? 424 LYS I NZ  1 
ATOM 731  N N   . LEU A 1 93  ? 274.564 263.866 276.930 1.00 33963. ? 425 LEU I N   1 
ATOM 732  C CA  . LEU A 1 93  ? 274.709 262.709 276.074 1.00 33908. ? 425 LEU I CA  1 
ATOM 733  C C   . LEU A 1 93  ? 274.427 263.127 274.644 1.00 33962. ? 425 LEU I C   1 
ATOM 734  O O   . LEU A 1 93  ? 273.426 263.817 274.405 1.00 34139. ? 425 LEU I O   1 
ATOM 735  C CB  . LEU A 1 93  ? 273.732 261.615 276.489 1.00 33949. ? 425 LEU I CB  1 
ATOM 736  C CG  . LEU A 1 93  ? 274.246 260.542 277.443 1.00 33928. ? 425 LEU I CG  1 
ATOM 737  C CD1 . LEU A 1 93  ? 273.159 259.543 277.750 1.00 34006. ? 425 LEU I CD1 1 
ATOM 738  C CD2 . LEU A 1 93  ? 275.472 259.871 276.910 1.00 34100. ? 425 LEU I CD2 1 
ATOM 739  N N   . PRO A 1 94  ? 275.288 262.776 273.689 1.00 33890. ? 426 PRO I N   1 
ATOM 740  C CA  . PRO A 1 94  ? 275.069 263.181 272.293 1.00 34059. ? 426 PRO I CA  1 
ATOM 741  C C   . PRO A 1 94  ? 273.819 262.547 271.696 1.00 34281. ? 426 PRO I C   1 
ATOM 742  O O   . PRO A 1 94  ? 273.323 261.532 272.184 1.00 34307. ? 426 PRO I O   1 
ATOM 743  C CB  . PRO A 1 94  ? 276.341 262.708 271.579 1.00 34080. ? 426 PRO I CB  1 
ATOM 744  C CG  . PRO A 1 94  ? 276.937 261.699 272.468 1.00 34020. ? 426 PRO I CG  1 
ATOM 745  C CD  . PRO A 1 94  ? 276.563 262.067 273.863 1.00 33990. ? 426 PRO I CD  1 
ATOM 746  N N   . ASP A 1 95  ? 273.237 263.235 270.710 1.00 36327. ? 427 ASP I N   1 
ATOM 747  C CA  . ASP A 1 95  ? 272.023 262.741 270.058 1.00 36361. ? 427 ASP I CA  1 
ATOM 748  C C   . ASP A 1 95  ? 272.261 261.407 269.354 1.00 36370. ? 427 ASP I C   1 
ATOM 749  O O   . ASP A 1 95  ? 271.382 260.540 269.337 1.00 36339. ? 427 ASP I O   1 
ATOM 750  C CB  . ASP A 1 95  ? 271.502 263.780 269.069 1.00 36406. ? 427 ASP I CB  1 
ATOM 751  C CG  . ASP A 1 95  ? 271.250 265.123 269.716 1.00 36397. ? 427 ASP I CG  1 
ATOM 752  O OD1 . ASP A 1 95  ? 270.883 265.149 270.910 1.00 36377. ? 427 ASP I OD1 1 
ATOM 753  O OD2 . ASP A 1 95  ? 271.423 266.153 269.034 1.00 36400. ? 427 ASP I OD2 1 
ATOM 754  N N   . ASP A 1 96  ? 273.447 261.228 268.773 1.00 37750. ? 428 ASP I N   1 
ATOM 755  C CA  . ASP A 1 96  ? 273.815 260.036 268.022 1.00 37776. ? 428 ASP I CA  1 
ATOM 756  C C   . ASP A 1 96  ? 274.492 258.978 268.886 1.00 37680. ? 428 ASP I C   1 
ATOM 757  O O   . ASP A 1 96  ? 275.162 258.092 268.344 1.00 37768. ? 428 ASP I O   1 
ATOM 758  C CB  . ASP A 1 96  ? 274.724 260.417 266.853 1.00 37874. ? 428 ASP I CB  1 
ATOM 759  C CG  . ASP A 1 96  ? 275.881 261.294 267.280 1.00 37950. ? 428 ASP I CG  1 
ATOM 760  O OD1 . ASP A 1 96  ? 275.692 262.524 267.379 1.00 37934. ? 428 ASP I OD1 1 
ATOM 761  O OD2 . ASP A 1 96  ? 276.984 260.757 267.505 1.00 37954. ? 428 ASP I OD2 1 
ATOM 762  N N   . PHE A 1 97  ? 274.379 259.096 270.209 1.00 34291. ? 429 PHE I N   1 
ATOM 763  C CA  . PHE A 1 97  ? 275.072 258.224 271.153 1.00 34094. ? 429 PHE I CA  1 
ATOM 764  C C   . PHE A 1 97  ? 274.677 256.761 271.020 1.00 34067. ? 429 PHE I C   1 
ATOM 765  O O   . PHE A 1 97  ? 273.495 256.421 270.942 1.00 34072. ? 429 PHE I O   1 
ATOM 766  C CB  . PHE A 1 97  ? 274.798 258.732 272.573 1.00 34004. ? 429 PHE I CB  1 
ATOM 767  C CG  . PHE A 1 97  ? 275.200 257.803 273.678 1.00 33926. ? 429 PHE I CG  1 
ATOM 768  C CD1 . PHE A 1 97  ? 276.494 257.809 274.162 1.00 34017. ? 429 PHE I CD1 1 
ATOM 769  C CD2 . PHE A 1 97  ? 274.246 257.051 274.347 1.00 33957. ? 429 PHE I CD2 1 
ATOM 770  C CE1 . PHE A 1 97  ? 276.854 256.993 275.208 1.00 34069. ? 429 PHE I CE1 1 
ATOM 771  C CE2 . PHE A 1 97  ? 274.600 256.244 275.397 1.00 33976. ? 429 PHE I CE2 1 
ATOM 772  C CZ  . PHE A 1 97  ? 275.904 256.219 275.831 1.00 34050. ? 429 PHE I CZ  1 
ATOM 773  N N   . THR A 1 98  ? 275.690 255.899 271.005 1.00 34069. ? 430 THR I N   1 
ATOM 774  C CA  . THR A 1 98  ? 275.517 254.456 271.061 1.00 34033. ? 430 THR I CA  1 
ATOM 775  C C   . THR A 1 98  ? 276.162 253.954 272.348 1.00 33938. ? 430 THR I C   1 
ATOM 776  O O   . THR A 1 98  ? 277.338 254.220 272.613 1.00 33982. ? 430 THR I O   1 
ATOM 777  C CB  . THR A 1 98  ? 276.051 253.765 269.791 1.00 34025. ? 430 THR I CB  1 
ATOM 778  O OG1 . THR A 1 98  ? 275.860 252.346 269.875 1.00 34031. ? 430 THR I OG1 1 
ATOM 779  C CG2 . THR A 1 98  ? 277.487 254.127 269.433 1.00 34058. ? 430 THR I CG2 1 
ATOM 780  N N   . GLY A 1 99  ? 275.363 253.314 273.189 1.00 33921. ? 431 GLY I N   1 
ATOM 781  C CA  . GLY A 1 99  ? 275.860 252.858 274.467 1.00 33887. ? 431 GLY I CA  1 
ATOM 782  C C   . GLY A 1 99  ? 274.720 252.500 275.395 1.00 33965. ? 431 GLY I C   1 
ATOM 783  O O   . GLY A 1 99  ? 273.556 252.500 275.000 1.00 34196. ? 431 GLY I O   1 
ATOM 784  N N   . CYS A 1 100 ? 275.079 252.214 276.643 1.00 33871. ? 432 CYS I N   1 
ATOM 785  C CA  . CYS A 1 100 ? 274.127 251.770 277.652 1.00 33930. ? 432 CYS I CA  1 
ATOM 786  C C   . CYS A 1 100 ? 274.196 252.650 278.891 1.00 33966. ? 432 CYS I C   1 
ATOM 787  O O   . CYS A 1 100 ? 275.283 252.904 279.414 1.00 34190. ? 432 CYS I O   1 
ATOM 788  C CB  . CYS A 1 100 ? 274.382 250.310 278.038 1.00 34005. ? 432 CYS I CB  1 
ATOM 789  S SG  . CYS A 1 100 ? 274.218 249.142 276.676 1.00 34189. ? 432 CYS I SG  1 
ATOM 790  N N   . VAL A 1 101 ? 273.037 253.111 279.352 1.00 33919. ? 433 VAL I N   1 
ATOM 791  C CA  . VAL A 1 101 ? 272.908 253.870 280.591 1.00 33915. ? 433 VAL I CA  1 
ATOM 792  C C   . VAL A 1 101 ? 272.411 252.926 281.675 1.00 33949. ? 433 VAL I C   1 
ATOM 793  O O   . VAL A 1 101 ? 271.309 252.378 281.571 1.00 34086. ? 433 VAL I O   1 
ATOM 794  C CB  . VAL A 1 101 ? 271.959 255.064 280.426 1.00 33931. ? 433 VAL I CB  1 
ATOM 795  C CG1 . VAL A 1 101 ? 271.841 255.819 281.732 1.00 33977. ? 433 VAL I CG1 1 
ATOM 796  C CG2 . VAL A 1 101 ? 272.460 255.979 279.327 1.00 33992. ? 433 VAL I CG2 1 
ATOM 797  N N   . ILE A 1 102 ? 273.210 252.745 282.722 1.00 33978. ? 434 ILE I N   1 
ATOM 798  C CA  . ILE A 1 102 ? 272.895 251.833 283.816 1.00 33970. ? 434 ILE I CA  1 
ATOM 799  C C   . ILE A 1 102 ? 272.729 252.662 285.078 1.00 33961. ? 434 ILE I C   1 
ATOM 800  O O   . ILE A 1 102 ? 273.663 253.358 285.484 1.00 34133. ? 434 ILE I O   1 
ATOM 801  C CB  . ILE A 1 102 ? 273.985 250.766 284.025 1.00 33947. ? 434 ILE I CB  1 
ATOM 802  C CG1 . ILE A 1 102 ? 274.286 249.949 282.762 1.00 33932. ? 434 ILE I CG1 1 
ATOM 803  C CG2 . ILE A 1 102 ? 273.599 249.841 285.139 1.00 34025. ? 434 ILE I CG2 1 
ATOM 804  C CD1 . ILE A 1 102 ? 275.415 250.465 281.892 1.00 33986. ? 434 ILE I CD1 1 
ATOM 805  N N   . ALA A 1 103 ? 271.557 252.585 285.703 1.00 33902. ? 435 ALA I N   1 
ATOM 806  C CA  . ALA A 1 103 ? 271.277 253.320 286.930 1.00 33861. ? 435 ALA I CA  1 
ATOM 807  C C   . ALA A 1 103 ? 270.666 252.402 287.979 1.00 33890. ? 435 ALA I C   1 
ATOM 808  O O   . ALA A 1 103 ? 269.789 251.595 287.667 1.00 34129. ? 435 ALA I O   1 
ATOM 809  C CB  . ALA A 1 103 ? 270.341 254.497 286.670 1.00 33973. ? 435 ALA I CB  1 
ATOM 810  N N   . TRP A 1 104 ? 271.138 252.513 289.221 1.00 33944. ? 436 TRP I N   1 
ATOM 811  C CA  . TRP A 1 104 ? 270.563 251.753 290.322 1.00 33953. ? 436 TRP I CA  1 
ATOM 812  C C   . TRP A 1 104 ? 270.398 252.672 291.522 1.00 33978. ? 436 TRP I C   1 
ATOM 813  O O   . TRP A 1 104 ? 271.179 253.605 291.712 1.00 34182. ? 436 TRP I O   1 
ATOM 814  C CB  . TRP A 1 104 ? 271.411 250.534 290.719 1.00 33989. ? 436 TRP I CB  1 
ATOM 815  C CG  . TRP A 1 104 ? 272.843 250.800 291.080 1.00 33990. ? 436 TRP I CG  1 
ATOM 816  C CD1 . TRP A 1 104 ? 273.362 250.846 292.336 1.00 33979. ? 436 TRP I CD1 1 
ATOM 817  C CD2 . TRP A 1 104 ? 273.935 251.058 290.189 1.00 34011. ? 436 TRP I CD2 1 
ATOM 818  N NE1 . TRP A 1 104 ? 274.703 251.105 292.287 1.00 33930. ? 436 TRP I NE1 1 
ATOM 819  C CE2 . TRP A 1 104 ? 275.080 251.241 290.980 1.00 33898. ? 436 TRP I CE2 1 
ATOM 820  C CE3 . TRP A 1 104 ? 274.055 251.152 288.803 1.00 34079. ? 436 TRP I CE3 1 
ATOM 821  C CZ2 . TRP A 1 104 ? 276.322 251.509 290.433 1.00 33892. ? 436 TRP I CZ2 1 
ATOM 822  C CZ3 . TRP A 1 104 ? 275.286 251.420 288.266 1.00 34041. ? 436 TRP I CZ3 1 
ATOM 823  C CH2 . TRP A 1 104 ? 276.403 251.594 289.078 1.00 33967. ? 436 TRP I CH2 1 
ATOM 824  N N   . ASN A 1 105 ? 269.354 252.421 292.310 1.00 33935. ? 437 ASN I N   1 
ATOM 825  C CA  . ASN A 1 105 ? 269.129 253.181 293.533 1.00 34005. ? 437 ASN I CA  1 
ATOM 826  C C   . ASN A 1 105 ? 270.243 252.928 294.538 1.00 34064. ? 437 ASN I C   1 
ATOM 827  O O   . ASN A 1 105 ? 270.598 251.779 294.817 1.00 34112. ? 437 ASN I O   1 
ATOM 828  C CB  . ASN A 1 105 ? 267.783 252.802 294.145 1.00 34013. ? 437 ASN I CB  1 
ATOM 829  C CG  . ASN A 1 105 ? 267.446 253.618 295.373 1.00 33940. ? 437 ASN I CG  1 
ATOM 830  O OD1 . ASN A 1 105 ? 267.380 253.087 296.478 1.00 33916. ? 437 ASN I OD1 1 
ATOM 831  N ND2 . ASN A 1 105 ? 267.221 254.906 295.189 1.00 33956. ? 437 ASN I ND2 1 
ATOM 832  N N   . SER A 1 106 ? 270.793 254.003 295.084 1.00 34070. ? 438 SER I N   1 
ATOM 833  C CA  . SER A 1 106 ? 271.844 253.935 296.087 1.00 33923. ? 438 SER I CA  1 
ATOM 834  C C   . SER A 1 106 ? 271.451 254.709 297.331 1.00 33945. ? 438 SER I C   1 
ATOM 835  O O   . SER A 1 106 ? 272.242 255.488 297.864 1.00 34017. ? 438 SER I O   1 
ATOM 836  C CB  . SER A 1 106 ? 273.167 254.450 295.536 1.00 33934. ? 438 SER I CB  1 
ATOM 837  O OG  . SER A 1 106 ? 273.027 255.751 295.014 1.00 34059. ? 438 SER I OG  1 
ATOM 838  N N   . ASN A 1 107 ? 270.195 254.549 297.761 1.00 34001. ? 439 ASN I N   1 
ATOM 839  C CA  . ASN A 1 107 ? 269.703 255.277 298.926 1.00 33888. ? 439 ASN I CA  1 
ATOM 840  C C   . ASN A 1 107 ? 270.460 254.880 300.180 1.00 33744. ? 439 ASN I C   1 
ATOM 841  O O   . ASN A 1 107 ? 270.837 255.738 300.976 1.00 33696. ? 439 ASN I O   1 
ATOM 842  C CB  . ASN A 1 107 ? 268.210 255.039 299.118 1.00 33905. ? 439 ASN I CB  1 
ATOM 843  C CG  . ASN A 1 107 ? 267.603 255.981 300.132 1.00 33759. ? 439 ASN I CG  1 
ATOM 844  O OD1 . ASN A 1 107 ? 268.062 257.105 300.301 1.00 33730. ? 439 ASN I OD1 1 
ATOM 845  N ND2 . ASN A 1 107 ? 266.580 255.516 300.833 1.00 33724. ? 439 ASN I ND2 1 
ATOM 846  N N   . ASN A 1 108 ? 270.779 253.599 300.327 1.00 33808. ? 440 ASN I N   1 
ATOM 847  C CA  . ASN A 1 108 ? 271.394 253.150 301.565 1.00 33448. ? 440 ASN I CA  1 
ATOM 848  C C   . ASN A 1 108 ? 272.877 253.469 301.583 1.00 33648. ? 440 ASN I C   1 
ATOM 849  O O   . ASN A 1 108 ? 273.484 253.510 302.658 1.00 33572. ? 440 ASN I O   1 
ATOM 850  C CB  . ASN A 1 108 ? 271.148 251.655 301.778 1.00 33001. ? 440 ASN I CB  1 
ATOM 851  C CG  . ASN A 1 108 ? 271.754 250.798 300.690 1.00 33644. ? 440 ASN I CG  1 
ATOM 852  O OD1 . ASN A 1 108 ? 271.965 251.250 299.565 1.00 34040. ? 440 ASN I OD1 1 
ATOM 853  N ND2 . ASN A 1 108 ? 272.042 249.545 301.022 1.00 33413. ? 440 ASN I ND2 1 
ATOM 854  N N   . LEU A 1 109 ? 273.466 253.685 300.411 1.00 33927. ? 441 LEU I N   1 
ATOM 855  C CA  . LEU A 1 109 ? 274.872 254.040 300.296 1.00 33847. ? 441 LEU I CA  1 
ATOM 856  C C   . LEU A 1 109 ? 275.106 255.544 300.411 1.00 33693. ? 441 LEU I C   1 
ATOM 857  O O   . LEU A 1 109 ? 275.838 255.992 301.295 1.00 33563. ? 441 LEU I O   1 
ATOM 858  C CB  . LEU A 1 109 ? 275.406 253.533 298.955 1.00 34018. ? 441 LEU I CB  1 
ATOM 859  C CG  . LEU A 1 109 ? 276.068 252.167 298.940 1.00 33445. ? 441 LEU I CG  1 
ATOM 860  C CD1 . LEU A 1 109 ? 276.147 251.681 297.518 1.00 33546. ? 441 LEU I CD1 1 
ATOM 861  C CD2 . LEU A 1 109 ? 277.442 252.277 299.544 1.00 32839. ? 441 LEU I CD2 1 
ATOM 862  N N   . ASP A 1 110 ? 274.456 256.335 299.559 1.00 33870. ? 442 ASP I N   1 
ATOM 863  C CA  . ASP A 1 110 ? 274.714 257.776 299.492 1.00 33669. ? 442 ASP I CA  1 
ATOM 864  C C   . ASP A 1 110 ? 273.640 258.600 300.200 1.00 33857. ? 442 ASP I C   1 
ATOM 865  O O   . ASP A 1 110 ? 273.066 259.511 299.620 1.00 34086. ? 442 ASP I O   1 
ATOM 866  C CB  . ASP A 1 110 ? 274.817 258.210 298.034 1.00 33924. ? 442 ASP I CB  1 
ATOM 867  C CG  . ASP A 1 110 ? 275.738 257.335 297.220 1.00 33794. ? 442 ASP I CG  1 
ATOM 868  O OD1 . ASP A 1 110 ? 276.768 256.883 297.750 1.00 33695. ? 442 ASP I OD1 1 
ATOM 869  O OD2 . ASP A 1 110 ? 275.428 257.099 296.037 1.00 33992. ? 442 ASP I OD2 1 
ATOM 870  N N   . SER A 1 111 ? 273.380 258.321 301.471 1.00 33938. ? 443 SER I N   1 
ATOM 871  C CA  . SER A 1 111 ? 272.468 259.165 302.232 1.00 33892. ? 443 SER I CA  1 
ATOM 872  C C   . SER A 1 111 ? 272.968 259.293 303.658 1.00 33975. ? 443 SER I C   1 
ATOM 873  O O   . SER A 1 111 ? 273.508 258.339 304.223 1.00 33839. ? 443 SER I O   1 
ATOM 874  C CB  . SER A 1 111 ? 271.038 258.639 302.234 1.00 33821. ? 443 SER I CB  1 
ATOM 875  O OG  . SER A 1 111 ? 270.420 258.859 300.981 1.00 33924. ? 443 SER I OG  1 
ATOM 876  N N   . LYS A 1 112 ? 272.781 260.476 304.232 1.00 34012. ? 444 LYS I N   1 
ATOM 877  C CA  . LYS A 1 112 ? 273.155 260.754 305.607 1.00 34033. ? 444 LYS I CA  1 
ATOM 878  C C   . LYS A 1 112 ? 272.035 261.557 306.245 1.00 34088. ? 444 LYS I C   1 
ATOM 879  O O   . LYS A 1 112 ? 271.299 262.261 305.550 1.00 34101. ? 444 LYS I O   1 
ATOM 880  C CB  . LYS A 1 112 ? 274.472 261.541 305.676 1.00 33900. ? 444 LYS I CB  1 
ATOM 881  C CG  . LYS A 1 112 ? 275.689 260.802 305.154 1.00 33543. ? 444 LYS I CG  1 
ATOM 882  C CD  . LYS A 1 112 ? 276.870 261.728 305.020 1.00 33374. ? 444 LYS I CD  1 
ATOM 883  C CE  . LYS A 1 112 ? 278.045 261.034 304.379 1.00 32851. ? 444 LYS I CE  1 
ATOM 884  N NZ  . LYS A 1 112 ? 279.161 261.982 304.144 1.00 32801. ? 444 LYS I NZ  1 
ATOM 885  N N   . VAL A 1 113 ? 271.874 261.407 307.562 1.00 34037. ? 445 VAL I N   1 
ATOM 886  C CA  . VAL A 1 113 ? 270.904 262.220 308.287 1.00 33907. ? 445 VAL I CA  1 
ATOM 887  C C   . VAL A 1 113 ? 271.368 263.669 308.249 1.00 33862. ? 445 VAL I C   1 
ATOM 888  O O   . VAL A 1 113 ? 272.544 263.969 308.487 1.00 33683. ? 445 VAL I O   1 
ATOM 889  C CB  . VAL A 1 113 ? 270.740 261.709 309.725 1.00 33572. ? 445 VAL I CB  1 
ATOM 890  C CG1 . VAL A 1 113 ? 269.641 262.468 310.451 1.00 33295. ? 445 VAL I CG1 1 
ATOM 891  C CG2 . VAL A 1 113 ? 270.435 260.242 309.719 1.00 33234. ? 445 VAL I CG2 1 
ATOM 892  N N   . GLY A 1 114 ? 270.444 264.577 307.957 1.00 33963. ? 446 GLY I N   1 
ATOM 893  C CA  . GLY A 1 114 ? 270.794 265.965 307.785 1.00 33792. ? 446 GLY I CA  1 
ATOM 894  C C   . GLY A 1 114 ? 271.305 266.289 306.402 1.00 33814. ? 446 GLY I C   1 
ATOM 895  O O   . GLY A 1 114 ? 271.621 267.453 306.130 1.00 33528. ? 446 GLY I O   1 
ATOM 896  N N   . GLY A 1 115 ? 271.390 265.299 305.526 1.00 33940. ? 447 GLY I N   1 
ATOM 897  C CA  . GLY A 1 115 ? 271.804 265.422 304.142 1.00 33911. ? 447 GLY I CA  1 
ATOM 898  C C   . GLY A 1 115 ? 273.291 265.221 303.955 1.00 33882. ? 447 GLY I C   1 
ATOM 899  O O   . GLY A 1 115 ? 274.104 265.481 304.838 1.00 33796. ? 447 GLY I O   1 
ATOM 900  N N   . ASN A 1 116 ? 273.649 264.734 302.773 1.00 33914. ? 448 ASN I N   1 
ATOM 901  C CA  . ASN A 1 116 ? 275.037 264.587 302.373 1.00 33915. ? 448 ASN I CA  1 
ATOM 902  C C   . ASN A 1 116 ? 275.365 265.753 301.447 1.00 33810. ? 448 ASN I C   1 
ATOM 903  O O   . ASN A 1 116 ? 274.572 266.089 300.568 1.00 33869. ? 448 ASN I O   1 
ATOM 904  C CB  . ASN A 1 116 ? 275.236 263.237 301.680 1.00 33975. ? 448 ASN I CB  1 
ATOM 905  C CG  . ASN A 1 116 ? 276.667 262.978 301.279 1.00 33945. ? 448 ASN I CG  1 
ATOM 906  O OD1 . ASN A 1 116 ? 277.594 263.611 301.778 1.00 34039. ? 448 ASN I OD1 1 
ATOM 907  N ND2 . ASN A 1 116 ? 276.857 262.016 300.392 1.00 33761. ? 448 ASN I ND2 1 
ATOM 908  N N   . TYR A 1 117 ? 276.541 266.353 301.618 1.00 33615. ? 449 TYR I N   1 
ATOM 909  C CA  . TYR A 1 117 ? 276.884 267.534 300.836 1.00 33447. ? 449 TYR I CA  1 
ATOM 910  C C   . TYR A 1 117 ? 277.750 267.228 299.618 1.00 33992. ? 449 TYR I C   1 
ATOM 911  O O   . TYR A 1 117 ? 277.833 268.064 298.716 1.00 34138. ? 449 TYR I O   1 
ATOM 912  C CB  . TYR A 1 117 ? 277.596 268.558 301.761 1.00 33027. ? 449 TYR I CB  1 
ATOM 913  C CG  . TYR A 1 117 ? 278.248 269.755 301.083 1.00 33236. ? 449 TYR I CG  1 
ATOM 914  C CD1 . TYR A 1 117 ? 277.497 270.863 300.726 1.00 33587. ? 449 TYR I CD1 1 
ATOM 915  C CD2 . TYR A 1 117 ? 279.602 269.756 300.769 1.00 33299. ? 449 TYR I CD2 1 
ATOM 916  C CE1 . TYR A 1 117 ? 278.071 271.941 300.090 1.00 33862. ? 449 TYR I CE1 1 
ATOM 917  C CE2 . TYR A 1 117 ? 280.180 270.825 300.124 1.00 33502. ? 449 TYR I CE2 1 
ATOM 918  C CZ  . TYR A 1 117 ? 279.414 271.917 299.793 1.00 33838. ? 449 TYR I CZ  1 
ATOM 919  O OH  . TYR A 1 117 ? 279.997 272.989 299.158 1.00 34033. ? 449 TYR I OH  1 
ATOM 920  N N   . ASN A 1 118 ? 278.257 266.004 299.502 1.00 33967. ? 450 ASN I N   1 
ATOM 921  C CA  . ASN A 1 118 ? 279.287 265.679 298.516 1.00 33948. ? 450 ASN I CA  1 
ATOM 922  C C   . ASN A 1 118 ? 278.836 265.803 297.059 1.00 33978. ? 450 ASN I C   1 
ATOM 923  O O   . ASN A 1 118 ? 279.644 266.161 296.195 1.00 34066. ? 450 ASN I O   1 
ATOM 924  C CB  . ASN A 1 118 ? 279.828 264.285 298.805 1.00 33984. ? 450 ASN I CB  1 
ATOM 925  C CG  . ASN A 1 118 ? 280.509 264.204 300.165 1.00 33701. ? 450 ASN I CG  1 
ATOM 926  O OD1 . ASN A 1 118 ? 280.820 265.225 300.779 1.00 33401. ? 450 ASN I OD1 1 
ATOM 927  N ND2 . ASN A 1 118 ? 280.749 262.985 300.635 1.00 33330. ? 450 ASN I ND2 1 
ATOM 928  N N   . TYR A 1 119 ? 277.586 265.453 296.752 1.00 33941. ? 451 TYR I N   1 
ATOM 929  C CA  . TYR A 1 119 ? 277.168 265.330 295.352 1.00 34046. ? 451 TYR I CA  1 
ATOM 930  C C   . TYR A 1 119 ? 277.117 266.649 294.563 1.00 34134. ? 451 TYR I C   1 
ATOM 931  O O   . TYR A 1 119 ? 277.581 266.675 293.423 1.00 34181. ? 451 TYR I O   1 
ATOM 932  C CB  . TYR A 1 119 ? 275.905 264.494 295.299 1.00 33989. ? 451 TYR I CB  1 
ATOM 933  C CG  . TYR A 1 119 ? 276.397 263.119 295.667 1.00 33910. ? 451 TYR I CG  1 
ATOM 934  C CD1 . TYR A 1 119 ? 277.342 262.491 294.866 1.00 34005. ? 451 TYR I CD1 1 
ATOM 935  C CD2 . TYR A 1 119 ? 276.017 262.493 296.840 1.00 33951. ? 451 TYR I CD2 1 
ATOM 936  C CE1 . TYR A 1 119 ? 277.860 261.269 295.196 1.00 33996. ? 451 TYR I CE1 1 
ATOM 937  C CE2 . TYR A 1 119 ? 276.526 261.253 297.172 1.00 33916. ? 451 TYR I CE2 1 
ATOM 938  C CZ  . TYR A 1 119 ? 277.443 260.648 296.338 1.00 33845. ? 451 TYR I CZ  1 
ATOM 939  O OH  . TYR A 1 119 ? 277.965 259.419 296.642 1.00 33669. ? 451 TYR I OH  1 
ATOM 940  N N   . LEU A 1 120 ? 276.544 267.726 295.110 1.00 34008. ? 452 LEU I N   1 
ATOM 941  C CA  . LEU A 1 120 ? 276.684 269.111 294.581 1.00 34005. ? 452 LEU I CA  1 
ATOM 942  C C   . LEU A 1 120 ? 276.453 269.327 293.071 1.00 33969. ? 452 LEU I C   1 
ATOM 943  O O   . LEU A 1 120 ? 277.384 269.669 292.346 1.00 34097. ? 452 LEU I O   1 
ATOM 944  C CB  . LEU A 1 120 ? 278.073 269.645 294.925 1.00 34013. ? 452 LEU I CB  1 
ATOM 945  C CG  . LEU A 1 120 ? 278.365 270.198 296.303 1.00 33960. ? 452 LEU I CG  1 
ATOM 946  C CD1 . LEU A 1 120 ? 279.840 270.023 296.574 1.00 34001. ? 452 LEU I CD1 1 
ATOM 947  C CD2 . LEU A 1 120 ? 277.960 271.651 296.391 1.00 34020. ? 452 LEU I CD2 1 
ATOM 948  N N   . TYR A 1 121 ? 275.236 269.095 292.583 1.00 33892. ? 453 TYR I N   1 
ATOM 949  C CA  . TYR A 1 121 ? 274.940 269.373 291.172 1.00 33919. ? 453 TYR I CA  1 
ATOM 950  C C   . TYR A 1 121 ? 275.023 270.865 290.824 1.00 33956. ? 453 TYR I C   1 
ATOM 951  O O   . TYR A 1 121 ? 274.740 271.736 291.644 1.00 34119. ? 453 TYR I O   1 
ATOM 952  C CB  . TYR A 1 121 ? 273.558 268.837 290.794 1.00 34054. ? 453 TYR I CB  1 
ATOM 953  C CG  . TYR A 1 121 ? 272.373 269.655 291.250 1.00 33998. ? 453 TYR I CG  1 
ATOM 954  C CD1 . TYR A 1 121 ? 271.876 269.526 292.534 1.00 34053. ? 453 TYR I CD1 1 
ATOM 955  C CD2 . TYR A 1 121 ? 271.709 270.505 290.374 1.00 33970. ? 453 TYR I CD2 1 
ATOM 956  C CE1 . TYR A 1 121 ? 270.785 270.244 292.951 1.00 34001. ? 453 TYR I CE1 1 
ATOM 957  C CE2 . TYR A 1 121 ? 270.620 271.235 290.784 1.00 33989. ? 453 TYR I CE2 1 
ATOM 958  C CZ  . TYR A 1 121 ? 270.163 271.100 292.074 1.00 34032. ? 453 TYR I CZ  1 
ATOM 959  O OH  . TYR A 1 121 ? 269.067 271.820 292.484 1.00 34123. ? 453 TYR I OH  1 
ATOM 960  N N   . ARG A 1 122 ? 275.421 271.151 289.581 1.00 33984. ? 454 ARG I N   1 
ATOM 961  C CA  . ARG A 1 122 ? 275.510 272.530 289.102 1.00 33980. ? 454 ARG I CA  1 
ATOM 962  C C   . ARG A 1 122 ? 274.123 273.095 288.833 1.00 34023. ? 454 ARG I C   1 
ATOM 963  O O   . ARG A 1 122 ? 273.322 272.485 288.121 1.00 34084. ? 454 ARG I O   1 
ATOM 964  C CB  . ARG A 1 122 ? 276.317 272.608 287.810 1.00 33945. ? 454 ARG I CB  1 
ATOM 965  C CG  . ARG A 1 122 ? 276.379 273.979 287.184 1.00 33921. ? 454 ARG I CG  1 
ATOM 966  C CD  . ARG A 1 122 ? 277.594 274.116 286.306 1.00 33989. ? 454 ARG I CD  1 
ATOM 967  N NE  . ARG A 1 122 ? 278.815 273.786 287.020 1.00 33971. ? 454 ARG I NE  1 
ATOM 968  C CZ  . ARG A 1 122 ? 279.820 274.622 287.218 1.00 34081. ? 454 ARG I CZ  1 
ATOM 969  N NH1 . ARG A 1 122 ? 279.783 275.864 286.772 1.00 34099. ? 454 ARG I NH1 1 
ATOM 970  N NH2 . ARG A 1 122 ? 280.891 274.197 287.875 1.00 34200. ? 454 ARG I NH2 1 
ATOM 971  N N   . LEU A 1 123 ? 273.850 274.280 289.367 1.00 34054. ? 455 LEU I N   1 
ATOM 972  C CA  . LEU A 1 123 ? 272.544 274.894 289.191 1.00 33989. ? 455 LEU I CA  1 
ATOM 973  C C   . LEU A 1 123 ? 272.526 275.974 288.123 1.00 34093. ? 455 LEU I C   1 
ATOM 974  O O   . LEU A 1 123 ? 271.521 276.112 287.420 1.00 34136. ? 455 LEU I O   1 
ATOM 975  C CB  . LEU A 1 123 ? 272.069 275.495 290.517 1.00 33999. ? 455 LEU I CB  1 
ATOM 976  C CG  . LEU A 1 123 ? 270.586 275.824 290.670 1.00 34065. ? 455 LEU I CG  1 
ATOM 977  C CD1 . LEU A 1 123 ? 269.716 274.743 290.056 1.00 34102. ? 455 LEU I CD1 1 
ATOM 978  C CD2 . LEU A 1 123 ? 270.242 276.020 292.127 1.00 34025. ? 455 LEU I CD2 1 
ATOM 979  N N   . PHE A 1 124 ? 273.608 276.736 287.979 1.00 34714. ? 456 PHE I N   1 
ATOM 980  C CA  . PHE A 1 124 ? 273.661 277.871 287.068 1.00 34741. ? 456 PHE I CA  1 
ATOM 981  C C   . PHE A 1 124 ? 274.855 277.764 286.133 1.00 34812. ? 456 PHE I C   1 
ATOM 982  O O   . PHE A 1 124 ? 275.987 277.570 286.582 1.00 34922. ? 456 PHE I O   1 
ATOM 983  C CB  . PHE A 1 124 ? 273.739 279.193 287.834 1.00 34931. ? 456 PHE I CB  1 
ATOM 984  C CG  . PHE A 1 124 ? 272.703 279.347 288.904 1.00 34885. ? 456 PHE I CG  1 
ATOM 985  C CD1 . PHE A 1 124 ? 271.391 279.641 288.576 1.00 34843. ? 456 PHE I CD1 1 
ATOM 986  C CD2 . PHE A 1 124 ? 273.039 279.203 290.236 1.00 34944. ? 456 PHE I CD2 1 
ATOM 987  C CE1 . PHE A 1 124 ? 270.434 279.786 289.557 1.00 34794. ? 456 PHE I CE1 1 
ATOM 988  C CE2 . PHE A 1 124 ? 272.084 279.341 291.221 1.00 34916. ? 456 PHE I CE2 1 
ATOM 989  C CZ  . PHE A 1 124 ? 270.781 279.638 290.881 1.00 34827. ? 456 PHE I CZ  1 
ATOM 990  N N   . ARG A 1 125 ? 274.595 277.898 284.837 1.00 35361. ? 457 ARG I N   1 
ATOM 991  C CA  . ARG A 1 125 ? 275.627 278.000 283.817 1.00 35494. ? 457 ARG I CA  1 
ATOM 992  C C   . ARG A 1 125 ? 275.135 278.967 282.752 1.00 35688. ? 457 ARG I C   1 
ATOM 993  O O   . ARG A 1 125 ? 273.931 279.083 282.515 1.00 35603. ? 457 ARG I O   1 
ATOM 994  C CB  . ARG A 1 125 ? 275.980 276.644 283.203 1.00 35409. ? 457 ARG I CB  1 
ATOM 995  C CG  . ARG A 1 125 ? 277.439 276.454 282.854 1.00 35363. ? 457 ARG I CG  1 
ATOM 996  C CD  . ARG A 1 125 ? 277.632 275.178 282.066 1.00 35322. ? 457 ARG I CD  1 
ATOM 997  N NE  . ARG A 1 125 ? 279.001 275.026 281.591 1.00 35335. ? 457 ARG I NE  1 
ATOM 998  C CZ  . ARG A 1 125 ? 279.404 275.325 280.365 1.00 35356. ? 457 ARG I CZ  1 
ATOM 999  N NH1 . ARG A 1 125 ? 278.567 275.794 279.458 1.00 35380. ? 457 ARG I NH1 1 
ATOM 1000 N NH2 . ARG A 1 125 ? 280.681 275.150 280.042 1.00 35373. ? 457 ARG I NH2 1 
ATOM 1001 N N   . LYS A 1 126 ? 276.080 279.698 282.152 1.00 39308. ? 458 LYS I N   1 
ATOM 1002 C CA  . LYS A 1 126 ? 275.739 280.691 281.137 1.00 39410. ? 458 LYS I CA  1 
ATOM 1003 C C   . LYS A 1 126 ? 275.145 280.050 279.888 1.00 39302. ? 458 LYS I C   1 
ATOM 1004 O O   . LYS A 1 126 ? 274.177 280.567 279.320 1.00 39353. ? 458 LYS I O   1 
ATOM 1005 C CB  . LYS A 1 126 ? 276.978 281.507 280.775 1.00 39455. ? 458 LYS I CB  1 
ATOM 1006 C CG  . LYS A 1 126 ? 277.055 282.861 281.455 1.00 39563. ? 458 LYS I CG  1 
ATOM 1007 C CD  . LYS A 1 126 ? 275.951 283.782 280.971 1.00 39592. ? 458 LYS I CD  1 
ATOM 1008 C CE  . LYS A 1 126 ? 276.029 285.139 281.649 1.00 39595. ? 458 LYS I CE  1 
ATOM 1009 N NZ  . LYS A 1 126 ? 274.888 286.016 281.264 1.00 39571. ? 458 LYS I NZ  1 
ATOM 1010 N N   . SER A 1 127 ? 275.706 278.929 279.448 1.00 36561. ? 459 SER I N   1 
ATOM 1011 C CA  . SER A 1 127 ? 275.272 278.259 278.234 1.00 36420. ? 459 SER I CA  1 
ATOM 1012 C C   . SER A 1 127 ? 275.133 276.767 278.494 1.00 36268. ? 459 SER I C   1 
ATOM 1013 O O   . SER A 1 127 ? 275.715 276.223 279.435 1.00 36287. ? 459 SER I O   1 
ATOM 1014 C CB  . SER A 1 127 ? 276.250 278.502 277.080 1.00 36415. ? 459 SER I CB  1 
ATOM 1015 O OG  . SER A 1 127 ? 277.590 278.389 277.519 1.00 36416. ? 459 SER I OG  1 
ATOM 1016 N N   . ASN A 1 128 ? 274.328 276.119 277.655 1.00 34191. ? 460 ASN I N   1 
ATOM 1017 C CA  . ASN A 1 128 ? 274.136 274.679 277.744 1.00 34123. ? 460 ASN I CA  1 
ATOM 1018 C C   . ASN A 1 128 ? 275.422 273.937 277.415 1.00 34121. ? 460 ASN I C   1 
ATOM 1019 O O   . ASN A 1 128 ? 276.179 274.334 276.525 1.00 34097. ? 460 ASN I O   1 
ATOM 1020 C CB  . ASN A 1 128 ? 273.021 274.225 276.807 1.00 34045. ? 460 ASN I CB  1 
ATOM 1021 C CG  . ASN A 1 128 ? 271.651 274.457 277.384 1.00 34026. ? 460 ASN I CG  1 
ATOM 1022 O OD1 . ASN A 1 128 ? 271.512 274.970 278.491 1.00 34083. ? 460 ASN I OD1 1 
ATOM 1023 N ND2 . ASN A 1 128 ? 270.625 274.067 276.644 1.00 33988. ? 460 ASN I ND2 1 
ATOM 1024 N N   . LEU A 1 129 ? 275.676 272.868 278.163 1.00 34137. ? 461 LEU I N   1 
ATOM 1025 C CA  . LEU A 1 129 ? 276.876 272.071 277.970 1.00 34077. ? 461 LEU I CA  1 
ATOM 1026 C C   . LEU A 1 129 ? 276.838 271.318 276.647 1.00 34118. ? 461 LEU I C   1 
ATOM 1027 O O   . LEU A 1 129 ? 275.793 270.818 276.222 1.00 34146. ? 461 LEU I O   1 
ATOM 1028 C CB  . LEU A 1 129 ? 277.041 271.075 279.115 1.00 33996. ? 461 LEU I CB  1 
ATOM 1029 C CG  . LEU A 1 129 ? 277.990 271.449 280.247 1.00 34015. ? 461 LEU I CG  1 
ATOM 1030 C CD1 . LEU A 1 129 ? 278.018 270.333 281.237 1.00 34019. ? 461 LEU I CD1 1 
ATOM 1031 C CD2 . LEU A 1 129 ? 279.376 271.712 279.728 1.00 34164. ? 461 LEU I CD2 1 
ATOM 1032 N N   . LYS A 1 130 ? 277.993 271.247 276.000 1.00 35121. ? 462 LYS I N   1 
ATOM 1033 C CA  . LYS A 1 130 ? 278.200 270.483 274.785 1.00 35146. ? 462 LYS I CA  1 
ATOM 1034 C C   . LYS A 1 130 ? 278.264 269.009 275.193 1.00 35243. ? 462 LYS I C   1 
ATOM 1035 O O   . LYS A 1 130 ? 278.491 268.717 276.370 1.00 35306. ? 462 LYS I O   1 
ATOM 1036 C CB  . LYS A 1 130 ? 279.506 270.971 274.148 1.00 35171. ? 462 LYS I CB  1 
ATOM 1037 C CG  . LYS A 1 130 ? 279.724 270.813 272.655 1.00 35264. ? 462 LYS I CG  1 
ATOM 1038 C CD  . LYS A 1 130 ? 280.800 271.760 272.160 1.00 35260. ? 462 LYS I CD  1 
ATOM 1039 C CE  . LYS A 1 130 ? 282.178 271.300 272.601 1.00 35315. ? 462 LYS I CE  1 
ATOM 1040 N NZ  . LYS A 1 130 ? 282.561 270.014 271.958 1.00 35337. ? 462 LYS I NZ  1 
ATOM 1041 N N   . PRO A 1 131 ? 277.992 268.060 274.281 1.00 34120. ? 463 PRO I N   1 
ATOM 1042 C CA  . PRO A 1 131 ? 278.035 266.640 274.676 1.00 34051. ? 463 PRO I CA  1 
ATOM 1043 C C   . PRO A 1 131 ? 279.417 266.188 275.129 1.00 34074. ? 463 PRO I C   1 
ATOM 1044 O O   . PRO A 1 131 ? 280.429 266.515 274.505 1.00 34138. ? 463 PRO I O   1 
ATOM 1045 C CB  . PRO A 1 131 ? 277.583 265.905 273.411 1.00 33995. ? 463 PRO I CB  1 
ATOM 1046 C CG  . PRO A 1 131 ? 276.739 266.877 272.720 1.00 34010. ? 463 PRO I CG  1 
ATOM 1047 C CD  . PRO A 1 131 ? 277.356 268.207 272.959 1.00 34047. ? 463 PRO I CD  1 
ATOM 1048 N N   . PHE A 1 132 ? 279.425 265.429 276.235 1.00 34022. ? 464 PHE I N   1 
ATOM 1049 C CA  . PHE A 1 132 ? 280.629 264.890 276.880 1.00 33999. ? 464 PHE I CA  1 
ATOM 1050 C C   . PHE A 1 132 ? 281.606 265.994 277.280 1.00 34132. ? 464 PHE I C   1 
ATOM 1051 O O   . PHE A 1 132 ? 282.821 265.856 277.135 1.00 34171. ? 464 PHE I O   1 
ATOM 1052 C CB  . PHE A 1 132 ? 281.316 263.836 276.007 1.00 34032. ? 464 PHE I CB  1 
ATOM 1053 C CG  . PHE A 1 132 ? 280.537 262.561 275.873 1.00 34001. ? 464 PHE I CG  1 
ATOM 1054 C CD1 . PHE A 1 132 ? 279.716 262.127 276.897 1.00 33984. ? 464 PHE I CD1 1 
ATOM 1055 C CD2 . PHE A 1 132 ? 280.614 261.805 274.718 1.00 34043. ? 464 PHE I CD2 1 
ATOM 1056 C CE1 . PHE A 1 132 ? 278.997 260.960 276.775 1.00 34003. ? 464 PHE I CE1 1 
ATOM 1057 C CE2 . PHE A 1 132 ? 279.894 260.639 274.595 1.00 34015. ? 464 PHE I CE2 1 
ATOM 1058 C CZ  . PHE A 1 132 ? 279.087 260.217 275.628 1.00 33984. ? 464 PHE I CZ  1 
ATOM 1059 N N   . GLU A 1 133 ? 281.071 267.100 277.794 1.00 35013. ? 465 GLU I N   1 
ATOM 1060 C CA  . GLU A 1 133 ? 281.870 268.223 278.266 1.00 35037. ? 465 GLU I CA  1 
ATOM 1061 C C   . GLU A 1 133 ? 281.652 268.393 279.760 1.00 35049. ? 465 GLU I C   1 
ATOM 1062 O O   . GLU A 1 133 ? 280.511 268.366 280.229 1.00 35127. ? 465 GLU I O   1 
ATOM 1063 C CB  . GLU A 1 133 ? 281.505 269.521 277.544 1.00 35100. ? 465 GLU I CB  1 
ATOM 1064 C CG  . GLU A 1 133 ? 282.610 270.561 277.553 1.00 35168. ? 465 GLU I CG  1 
ATOM 1065 C CD  . GLU A 1 133 ? 282.085 271.979 277.446 1.00 35165. ? 465 GLU I CD  1 
ATOM 1066 O OE1 . GLU A 1 133 ? 281.063 272.192 276.767 1.00 35204. ? 465 GLU I OE1 1 
ATOM 1067 O OE2 . GLU A 1 133 ? 282.698 272.887 278.044 1.00 35087. ? 465 GLU I OE2 1 
ATOM 1068 N N   . ARG A 1 134 ? 282.741 268.554 280.502 1.00 34100. ? 466 ARG I N   1 
ATOM 1069 C CA  . ARG A 1 134 ? 282.699 268.654 281.953 1.00 34044. ? 466 ARG I CA  1 
ATOM 1070 C C   . ARG A 1 134 ? 283.157 270.041 282.379 1.00 34091. ? 466 ARG I C   1 
ATOM 1071 O O   . ARG A 1 134 ? 284.216 270.507 281.946 1.00 34123. ? 466 ARG I O   1 
ATOM 1072 C CB  . ARG A 1 134 ? 283.578 267.573 282.581 1.00 33993. ? 466 ARG I CB  1 
ATOM 1073 C CG  . ARG A 1 134 ? 283.803 267.702 284.066 1.00 34036. ? 466 ARG I CG  1 
ATOM 1074 C CD  . ARG A 1 134 ? 285.008 266.899 284.522 1.00 34006. ? 466 ARG I CD  1 
ATOM 1075 N NE  . ARG A 1 134 ? 284.871 265.464 284.312 1.00 34033. ? 466 ARG I NE  1 
ATOM 1076 C CZ  . ARG A 1 134 ? 285.479 264.786 283.348 1.00 34024. ? 466 ARG I CZ  1 
ATOM 1077 N NH1 . ARG A 1 134 ? 286.274 265.385 282.478 1.00 33985. ? 466 ARG I NH1 1 
ATOM 1078 N NH2 . ARG A 1 134 ? 285.299 263.472 283.266 1.00 34087. ? 466 ARG I NH2 1 
ATOM 1079 N N   . ASP A 1 135 ? 282.363 270.700 283.221 1.00 34603. ? 467 ASP I N   1 
ATOM 1080 C CA  . ASP A 1 135 ? 282.713 271.996 283.789 1.00 34646. ? 467 ASP I CA  1 
ATOM 1081 C C   . ASP A 1 135 ? 282.849 271.850 285.297 1.00 34735. ? 467 ASP I C   1 
ATOM 1082 O O   . ASP A 1 135 ? 281.896 271.447 285.969 1.00 34768. ? 467 ASP I O   1 
ATOM 1083 C CB  . ASP A 1 135 ? 281.657 273.045 283.434 1.00 34666. ? 467 ASP I CB  1 
ATOM 1084 C CG  . ASP A 1 135 ? 282.106 274.460 283.747 1.00 34757. ? 467 ASP I CG  1 
ATOM 1085 O OD1 . ASP A 1 135 ? 283.328 274.710 283.779 1.00 34751. ? 467 ASP I OD1 1 
ATOM 1086 O OD2 . ASP A 1 135 ? 281.232 275.326 283.946 1.00 34803. ? 467 ASP I OD2 1 
ATOM 1087 N N   . ILE A 1 136 ? 284.022 272.190 285.827 1.00 35815. ? 468 ILE I N   1 
ATOM 1088 C CA  . ILE A 1 136 ? 284.279 272.145 287.262 1.00 35862. ? 468 ILE I CA  1 
ATOM 1089 C C   . ILE A 1 136 ? 284.467 273.536 287.855 1.00 36012. ? 468 ILE I C   1 
ATOM 1090 O O   . ILE A 1 136 ? 284.906 273.657 289.003 1.00 36055. ? 468 ILE I O   1 
ATOM 1091 C CB  . ILE A 1 136 ? 285.481 271.244 287.585 1.00 35841. ? 468 ILE I CB  1 
ATOM 1092 C CG1 . ILE A 1 136 ? 286.685 271.638 286.728 1.00 35877. ? 468 ILE I CG1 1 
ATOM 1093 C CG2 . ILE A 1 136 ? 285.118 269.785 287.371 1.00 35832. ? 468 ILE I CG2 1 
ATOM 1094 C CD1 . ILE A 1 136 ? 287.894 270.757 286.928 1.00 35896. ? 468 ILE I CD1 1 
ATOM 1095 N N   . SER A 1 137 ? 284.177 274.586 287.089 1.00 37250. ? 469 SER I N   1 
ATOM 1096 C CA  . SER A 1 137 ? 284.368 275.961 287.541 1.00 37341. ? 469 SER I CA  1 
ATOM 1097 C C   . SER A 1 137 ? 283.427 276.308 288.688 1.00 37562. ? 469 SER I C   1 
ATOM 1098 O O   . SER A 1 137 ? 282.275 275.877 288.719 1.00 37399. ? 469 SER I O   1 
ATOM 1099 C CB  . SER A 1 137 ? 284.151 276.933 286.385 1.00 37399. ? 469 SER I CB  1 
ATOM 1100 O OG  . SER A 1 137 ? 282.779 277.033 286.054 1.00 37383. ? 469 SER I OG  1 
ATOM 1101 N N   . THR A 1 138 ? 283.923 277.098 289.637 1.00 42006. ? 470 THR I N   1 
ATOM 1102 C CA  . THR A 1 138 ? 283.119 277.558 290.763 1.00 42098. ? 470 THR I CA  1 
ATOM 1103 C C   . THR A 1 138 ? 282.854 279.058 290.703 1.00 42270. ? 470 THR I C   1 
ATOM 1104 O O   . THR A 1 138 ? 282.530 279.665 291.729 1.00 42292. ? 470 THR I O   1 
ATOM 1105 C CB  . THR A 1 138 ? 283.789 277.189 292.086 1.00 42176. ? 470 THR I CB  1 
ATOM 1106 O OG1 . THR A 1 138 ? 285.123 277.711 292.111 1.00 42243. ? 470 THR I OG1 1 
ATOM 1107 C CG2 . THR A 1 138 ? 283.837 275.680 292.255 1.00 42085. ? 470 THR I CG2 1 
ATOM 1108 N N   . GLU A 1 139 ? 283.036 279.665 289.528 1.00 45507. ? 471 GLU I N   1 
ATOM 1109 C CA  . GLU A 1 139 ? 282.863 281.102 289.347 1.00 45727. ? 471 GLU I CA  1 
ATOM 1110 C C   . GLU A 1 139 ? 281.425 281.528 289.613 1.00 45787. ? 471 GLU I C   1 
ATOM 1111 O O   . GLU A 1 139 ? 280.478 280.817 289.269 1.00 45696. ? 471 GLU I O   1 
ATOM 1112 C CB  . GLU A 1 139 ? 283.271 281.504 287.932 1.00 45788. ? 471 GLU I CB  1 
ATOM 1113 C CG  . GLU A 1 139 ? 284.764 281.447 287.686 1.00 45833. ? 471 GLU I CG  1 
ATOM 1114 C CD  . GLU A 1 139 ? 285.515 282.524 288.444 1.00 45869. ? 471 GLU I CD  1 
ATOM 1115 O OE1 . GLU A 1 139 ? 284.967 283.636 288.601 1.00 45889. ? 471 GLU I OE1 1 
ATOM 1116 O OE2 . GLU A 1 139 ? 286.655 282.259 288.882 1.00 45860. ? 471 GLU I OE2 1 
ATOM 1117 N N   . ILE A 1 140 ? 281.280 282.695 290.252 1.00 47574. ? 472 ILE I N   1 
ATOM 1118 C CA  . ILE A 1 140 ? 279.975 283.209 290.657 1.00 47593. ? 472 ILE I CA  1 
ATOM 1119 C C   . ILE A 1 140 ? 279.122 283.507 289.432 1.00 47604. ? 472 ILE I C   1 
ATOM 1120 O O   . ILE A 1 140 ? 279.621 283.985 288.405 1.00 47730. ? 472 ILE I O   1 
ATOM 1121 C CB  . ILE A 1 140 ? 280.165 284.464 291.524 1.00 47819. ? 472 ILE I CB  1 
ATOM 1122 C CG1 . ILE A 1 140 ? 281.361 284.280 292.460 1.00 47916. ? 472 ILE I CG1 1 
ATOM 1123 C CG2 . ILE A 1 140 ? 278.907 284.774 292.324 1.00 47864. ? 472 ILE I CG2 1 
ATOM 1124 C CD1 . ILE A 1 140 ? 281.153 283.282 293.562 1.00 47905. ? 472 ILE I CD1 1 
ATOM 1125 N N   . TYR A 1 141 ? 277.826 283.228 289.532 1.00 44297. ? 473 TYR I N   1 
ATOM 1126 C CA  . TYR A 1 141 ? 276.918 283.407 288.407 1.00 44293. ? 473 TYR I CA  1 
ATOM 1127 C C   . TYR A 1 141 ? 276.310 284.803 288.432 1.00 44575. ? 473 TYR I C   1 
ATOM 1128 O O   . TYR A 1 141 ? 275.670 285.193 289.412 1.00 44548. ? 473 TYR I O   1 
ATOM 1129 C CB  . TYR A 1 141 ? 275.815 282.354 288.420 1.00 44094. ? 473 TYR I CB  1 
ATOM 1130 C CG  . TYR A 1 141 ? 275.011 282.351 287.147 1.00 44018. ? 473 TYR I CG  1 
ATOM 1131 C CD1 . TYR A 1 141 ? 275.584 281.957 285.947 1.00 43895. ? 473 TYR I CD1 1 
ATOM 1132 C CD2 . TYR A 1 141 ? 273.681 282.749 287.144 1.00 44108. ? 473 TYR I CD2 1 
ATOM 1133 C CE1 . TYR A 1 141 ? 274.854 281.957 284.779 1.00 43878. ? 473 TYR I CE1 1 
ATOM 1134 C CE2 . TYR A 1 141 ? 272.942 282.750 285.980 1.00 44133. ? 473 TYR I CE2 1 
ATOM 1135 C CZ  . TYR A 1 141 ? 273.534 282.353 284.802 1.00 44004. ? 473 TYR I CZ  1 
ATOM 1136 O OH  . TYR A 1 141 ? 272.803 282.354 283.639 1.00 43970. ? 473 TYR I OH  1 
ATOM 1137 N N   . GLN A 1 142 ? 276.503 285.541 287.342 1.00 51271. ? 474 GLN I N   1 
ATOM 1138 C CA  . GLN A 1 142 ? 275.988 286.901 287.201 1.00 51459. ? 474 GLN I CA  1 
ATOM 1139 C C   . GLN A 1 142 ? 274.583 286.899 286.599 1.00 51491. ? 474 GLN I C   1 
ATOM 1140 O O   . GLN A 1 142 ? 274.378 287.178 285.416 1.00 51499. ? 474 GLN I O   1 
ATOM 1141 C CB  . GLN A 1 142 ? 276.944 287.738 286.365 1.00 51590. ? 474 GLN I CB  1 
ATOM 1142 C CG  . GLN A 1 142 ? 276.979 289.195 286.756 1.00 51765. ? 474 GLN I CG  1 
ATOM 1143 C CD  . GLN A 1 142 ? 277.708 290.041 285.741 1.00 51785. ? 474 GLN I CD  1 
ATOM 1144 O OE1 . GLN A 1 142 ? 278.616 289.567 285.059 1.00 51667. ? 474 GLN I OE1 1 
ATOM 1145 N NE2 . GLN A 1 142 ? 277.293 291.293 285.609 1.00 51946. ? 474 GLN I NE2 1 
ATOM 1146 N N   . ALA A 1 143 ? 273.606 286.523 287.429 1.00 50533. ? 475 ALA I N   1 
ATOM 1147 C CA  . ALA A 1 143 ? 272.212 286.629 287.004 1.00 50582. ? 475 ALA I CA  1 
ATOM 1148 C C   . ALA A 1 143 ? 271.814 288.089 286.816 1.00 50768. ? 475 ALA I C   1 
ATOM 1149 O O   . ALA A 1 143 ? 271.134 288.438 285.845 1.00 50707. ? 475 ALA I O   1 
ATOM 1150 C CB  . ALA A 1 143 ? 271.294 285.944 288.014 1.00 50544. ? 475 ALA I CB  1 
ATOM 1151 N N   . GLY A 1 144 ? 272.224 288.948 287.747 1.00 55066. ? 476 GLY I N   1 
ATOM 1152 C CA  . GLY A 1 144 ? 271.955 290.364 287.645 1.00 55211. ? 476 GLY I CA  1 
ATOM 1153 C C   . GLY A 1 144 ? 272.899 291.082 286.700 1.00 55379. ? 476 GLY I C   1 
ATOM 1154 O O   . GLY A 1 144 ? 273.957 290.572 286.329 1.00 55298. ? 476 GLY I O   1 
ATOM 1155 N N   . SER A 1 145 ? 272.462 292.273 286.277 1.00 59800. ? 477 SER I N   1 
ATOM 1156 C CA  . SER A 1 145 ? 273.289 293.128 285.429 1.00 59904. ? 477 SER I CA  1 
ATOM 1157 C C   . SER A 1 145 ? 274.564 293.567 286.145 1.00 59909. ? 477 SER I C   1 
ATOM 1158 O O   . SER A 1 145 ? 275.626 293.679 285.520 1.00 59897. ? 477 SER I O   1 
ATOM 1159 C CB  . SER A 1 145 ? 272.483 294.345 284.976 1.00 59950. ? 477 SER I CB  1 
ATOM 1160 O OG  . SER A 1 145 ? 271.316 293.949 284.277 1.00 59949. ? 477 SER I OG  1 
ATOM 1161 N N   . THR A 1 146 ? 274.464 293.863 287.440 1.00 59785. ? 478 THR I N   1 
ATOM 1162 C CA  . THR A 1 146 ? 275.622 294.276 288.225 1.00 59792. ? 478 THR I CA  1 
ATOM 1163 C C   . THR A 1 146 ? 276.644 293.140 288.334 1.00 59751. ? 478 THR I C   1 
ATOM 1164 O O   . THR A 1 146 ? 276.264 291.968 288.447 1.00 59675. ? 478 THR I O   1 
ATOM 1165 C CB  . THR A 1 146 ? 275.181 294.759 289.615 1.00 59824. ? 478 THR I CB  1 
ATOM 1166 O OG1 . THR A 1 146 ? 276.328 295.112 290.400 1.00 59821. ? 478 THR I OG1 1 
ATOM 1167 C CG2 . THR A 1 146 ? 274.330 293.720 290.353 1.00 59793. ? 478 THR I CG2 1 
ATOM 1168 N N   . PRO A 1 147 ? 277.942 293.441 288.239 1.00 59807. ? 479 PRO I N   1 
ATOM 1169 C CA  . PRO A 1 147 ? 278.954 292.384 288.361 1.00 59788. ? 479 PRO I CA  1 
ATOM 1170 C C   . PRO A 1 147 ? 279.065 291.847 289.780 1.00 59784. ? 479 PRO I C   1 
ATOM 1171 O O   . PRO A 1 147 ? 278.969 292.590 290.759 1.00 59835. ? 479 PRO I O   1 
ATOM 1172 C CB  . PRO A 1 147 ? 280.247 293.079 287.923 1.00 59806. ? 479 PRO I CB  1 
ATOM 1173 C CG  . PRO A 1 147 ? 280.016 294.514 288.228 1.00 59834. ? 479 PRO I CG  1 
ATOM 1174 C CD  . PRO A 1 147 ? 278.552 294.758 287.981 1.00 59835. ? 479 PRO I CD  1 
ATOM 1175 N N   . CYS A 1 148 ? 279.242 290.527 289.871 1.00 59027. ? 480 CYS I N   1 
ATOM 1176 C CA  . CYS A 1 148 ? 279.428 289.863 291.158 1.00 59009. ? 480 CYS I CA  1 
ATOM 1177 C C   . CYS A 1 148 ? 280.730 290.270 291.831 1.00 58999. ? 480 CYS I C   1 
ATOM 1178 O O   . CYS A 1 148 ? 280.782 290.366 293.064 1.00 58985. ? 480 CYS I O   1 
ATOM 1179 C CB  . CYS A 1 148 ? 279.393 288.350 290.971 1.00 58904. ? 480 CYS I CB  1 
ATOM 1180 S SG  . CYS A 1 148 ? 277.884 287.782 290.214 1.00 58651. ? 480 CYS I SG  1 
ATOM 1181 N N   . ASN A 1 149 ? 281.802 290.419 291.038 1.00 58833. ? 481 ASN I N   1 
ATOM 1182 C CA  . ASN A 1 149 ? 283.171 290.735 291.459 1.00 58813. ? 481 ASN I CA  1 
ATOM 1183 C C   . ASN A 1 149 ? 283.799 289.588 292.243 1.00 58736. ? 481 ASN I C   1 
ATOM 1184 O O   . ASN A 1 149 ? 284.709 289.810 293.048 1.00 58756. ? 481 ASN I O   1 
ATOM 1185 C CB  . ASN A 1 149 ? 283.281 292.051 292.248 1.00 58835. ? 481 ASN I CB  1 
ATOM 1186 C CG  . ASN A 1 149 ? 282.637 293.217 291.530 1.00 58859. ? 481 ASN I CG  1 
ATOM 1187 O OD1 . ASN A 1 149 ? 282.848 293.420 290.335 1.00 58863. ? 481 ASN I OD1 1 
ATOM 1188 N ND2 . ASN A 1 149 ? 281.843 293.992 292.257 1.00 58862. ? 481 ASN I ND2 1 
ATOM 1189 N N   . GLY A 1 150 ? 283.324 288.362 292.022 1.00 55789. ? 482 GLY I N   1 
ATOM 1190 C CA  . GLY A 1 150 ? 283.843 287.184 292.685 1.00 55678. ? 482 GLY I CA  1 
ATOM 1191 C C   . GLY A 1 150 ? 283.285 286.914 294.063 1.00 55642. ? 482 GLY I C   1 
ATOM 1192 O O   . GLY A 1 150 ? 283.773 286.004 294.742 1.00 55631. ? 482 GLY I O   1 
ATOM 1193 N N   . VAL A 1 151 ? 282.281 287.670 294.500 1.00 55130. ? 483 VAL I N   1 
ATOM 1194 C CA  . VAL A 1 151 ? 281.707 287.541 295.834 1.00 55086. ? 483 VAL I CA  1 
ATOM 1195 C C   . VAL A 1 151 ? 280.200 287.325 295.715 1.00 55042. ? 483 VAL I C   1 
ATOM 1196 O O   . VAL A 1 151 ? 279.566 287.817 294.774 1.00 55062. ? 483 VAL I O   1 
ATOM 1197 C CB  . VAL A 1 151 ? 282.064 288.762 296.723 1.00 55074. ? 483 VAL I CB  1 
ATOM 1198 C CG1 . VAL A 1 151 ? 281.281 290.017 296.347 1.00 55106. ? 483 VAL I CG1 1 
ATOM 1199 C CG2 . VAL A 1 151 ? 281.894 288.430 298.203 1.00 55054. ? 483 VAL I CG2 1 
ATOM 1200 N N   . GLU A 1 152 ? 279.654 286.483 296.595 1.00 54082. ? 484 GLU I N   1 
ATOM 1201 C CA  . GLU A 1 152 ? 278.209 286.284 296.647 1.00 54056. ? 484 GLU I CA  1 
ATOM 1202 C C   . GLU A 1 152 ? 277.511 287.582 297.033 1.00 54066. ? 484 GLU I C   1 
ATOM 1203 O O   . GLU A 1 152 ? 277.964 288.312 297.919 1.00 54096. ? 484 GLU I O   1 
ATOM 1204 C CB  . GLU A 1 152 ? 277.839 285.205 297.667 1.00 54078. ? 484 GLU I CB  1 
ATOM 1205 C CG  . GLU A 1 152 ? 278.608 283.899 297.618 1.00 54061. ? 484 GLU I CG  1 
ATOM 1206 C CD  . GLU A 1 152 ? 278.200 283.022 296.457 1.00 53844. ? 484 GLU I CD  1 
ATOM 1207 O OE1 . GLU A 1 152 ? 276.990 282.968 296.154 1.00 53771. ? 484 GLU I OE1 1 
ATOM 1208 O OE2 . GLU A 1 152 ? 279.073 282.344 295.885 1.00 53740. ? 484 GLU I OE2 1 
ATOM 1209 N N   . GLY A 1 153 ? 276.396 287.862 296.367 1.00 53416. ? 485 GLY I N   1 
ATOM 1210 C CA  . GLY A 1 153 ? 275.678 289.101 296.584 1.00 53444. ? 485 GLY I CA  1 
ATOM 1211 C C   . GLY A 1 153 ? 274.257 288.963 296.091 1.00 53443. ? 485 GLY I C   1 
ATOM 1212 O O   . GLY A 1 153 ? 273.819 287.879 295.699 1.00 53378. ? 485 GLY I O   1 
ATOM 1213 N N   . PHE A 1 154 ? 273.511 290.063 296.199 1.00 55923. ? 486 PHE I N   1 
ATOM 1214 C CA  . PHE A 1 154 ? 272.187 290.134 295.594 1.00 55945. ? 486 PHE I CA  1 
ATOM 1215 C C   . PHE A 1 154 ? 272.324 289.960 294.086 1.00 55827. ? 486 PHE I C   1 
ATOM 1216 O O   . PHE A 1 154 ? 273.138 290.638 293.452 1.00 55885. ? 486 PHE I O   1 
ATOM 1217 C CB  . PHE A 1 154 ? 271.542 291.474 295.960 1.00 56018. ? 486 PHE I CB  1 
ATOM 1218 C CG  . PHE A 1 154 ? 270.262 291.779 295.232 1.00 56017. ? 486 PHE I CG  1 
ATOM 1219 C CD1 . PHE A 1 154 ? 269.082 291.128 295.564 1.00 56017. ? 486 PHE I CD1 1 
ATOM 1220 C CD2 . PHE A 1 154 ? 270.224 292.775 294.265 1.00 56000. ? 486 PHE I CD2 1 
ATOM 1221 C CE1 . PHE A 1 154 ? 267.899 291.428 294.910 1.00 56004. ? 486 PHE I CE1 1 
ATOM 1222 C CE2 . PHE A 1 154 ? 269.045 293.088 293.613 1.00 55988. ? 486 PHE I CE2 1 
ATOM 1223 C CZ  . PHE A 1 154 ? 267.882 292.410 293.932 1.00 55995. ? 486 PHE I CZ  1 
ATOM 1224 N N   . ASN A 1 155 ? 271.573 288.990 293.543 1.00 51643. ? 487 ASN I N   1 
ATOM 1225 C CA  . ASN A 1 155 ? 271.488 288.583 292.135 1.00 51497. ? 487 ASN I CA  1 
ATOM 1226 C C   . ASN A 1 155 ? 272.720 287.815 291.673 1.00 51367. ? 487 ASN I C   1 
ATOM 1227 O O   . ASN A 1 155 ? 272.859 287.547 290.476 1.00 51395. ? 487 ASN I O   1 
ATOM 1228 C CB  . ASN A 1 155 ? 271.194 289.729 291.159 1.00 51572. ? 487 ASN I CB  1 
ATOM 1229 C CG  . ASN A 1 155 ? 269.713 289.965 290.974 1.00 51585. ? 487 ASN I CG  1 
ATOM 1230 O OD1 . ASN A 1 155 ? 269.213 291.058 291.217 1.00 51631. ? 487 ASN I OD1 1 
ATOM 1231 N ND2 . ASN A 1 155 ? 269.000 288.931 290.545 1.00 51494. ? 487 ASN I ND2 1 
ATOM 1232 N N   . CYS A 1 156 ? 273.626 287.468 292.583 1.00 49879. ? 488 CYS I N   1 
ATOM 1233 C CA  . CYS A 1 156 ? 274.828 286.706 292.276 1.00 49732. ? 488 CYS I CA  1 
ATOM 1234 C C   . CYS A 1 156 ? 274.780 285.423 293.088 1.00 49529. ? 488 CYS I C   1 
ATOM 1235 O O   . CYS A 1 156 ? 274.596 285.467 294.306 1.00 49706. ? 488 CYS I O   1 
ATOM 1236 C CB  . CYS A 1 156 ? 276.080 287.513 292.593 1.00 49921. ? 488 CYS I CB  1 
ATOM 1237 S SG  . CYS A 1 156 ? 276.461 288.712 291.313 1.00 50074. ? 488 CYS I SG  1 
ATOM 1238 N N   . TYR A 1 157 ? 274.957 284.284 292.426 1.00 43380. ? 489 TYR I N   1 
ATOM 1239 C CA  . TYR A 1 157 ? 274.691 283.015 293.077 1.00 43088. ? 489 TYR I CA  1 
ATOM 1240 C C   . TYR A 1 157 ? 275.846 282.053 292.848 1.00 42883. ? 489 TYR I C   1 
ATOM 1241 O O   . TYR A 1 157 ? 276.508 282.099 291.808 1.00 42965. ? 489 TYR I O   1 
ATOM 1242 C CB  . TYR A 1 157 ? 273.422 282.405 292.493 1.00 42930. ? 489 TYR I CB  1 
ATOM 1243 C CG  . TYR A 1 157 ? 272.194 283.266 292.662 1.00 43006. ? 489 TYR I CG  1 
ATOM 1244 C CD1 . TYR A 1 157 ? 271.509 283.337 293.864 1.00 43014. ? 489 TYR I CD1 1 
ATOM 1245 C CD2 . TYR A 1 157 ? 271.718 284.009 291.589 1.00 43076. ? 489 TYR I CD2 1 
ATOM 1246 C CE1 . TYR A 1 157 ? 270.385 284.142 293.994 1.00 43054. ? 489 TYR I CE1 1 
ATOM 1247 C CE2 . TYR A 1 157 ? 270.605 284.805 291.705 1.00 43201. ? 489 TYR I CE2 1 
ATOM 1248 C CZ  . TYR A 1 157 ? 269.940 284.870 292.907 1.00 43130. ? 489 TYR I CZ  1 
ATOM 1249 O OH  . TYR A 1 157 ? 268.827 285.669 293.014 1.00 43114. ? 489 TYR I OH  1 
ATOM 1250 N N   . PHE A 1 158 ? 276.105 281.205 293.843 1.00 39140. ? 490 PHE I N   1 
ATOM 1251 C CA  . PHE A 1 158 ? 277.104 280.157 293.681 1.00 38891. ? 490 PHE I CA  1 
ATOM 1252 C C   . PHE A 1 158 ? 276.607 279.152 292.639 1.00 38522. ? 490 PHE I C   1 
ATOM 1253 O O   . PHE A 1 158 ? 275.424 278.796 292.646 1.00 38587. ? 490 PHE I O   1 
ATOM 1254 C CB  . PHE A 1 158 ? 277.380 279.472 295.023 1.00 38886. ? 490 PHE I CB  1 
ATOM 1255 C CG  . PHE A 1 158 ? 278.618 278.616 295.032 1.00 38803. ? 490 PHE I CG  1 
ATOM 1256 C CD1 . PHE A 1 158 ? 279.875 279.199 294.996 1.00 38877. ? 490 PHE I CD1 1 
ATOM 1257 C CD2 . PHE A 1 158 ? 278.529 277.237 295.100 1.00 38636. ? 490 PHE I CD2 1 
ATOM 1258 C CE1 . PHE A 1 158 ? 281.017 278.420 295.004 1.00 38817. ? 490 PHE I CE1 1 
ATOM 1259 C CE2 . PHE A 1 158 ? 279.669 276.453 295.112 1.00 38612. ? 490 PHE I CE2 1 
ATOM 1260 C CZ  . PHE A 1 158 ? 280.911 277.046 295.064 1.00 38717. ? 490 PHE I CZ  1 
ATOM 1261 N N   . PRO A 1 159 ? 277.471 278.707 291.719 1.00 34375. ? 491 PRO I N   1 
ATOM 1262 C CA  . PRO A 1 159 ? 277.002 277.811 290.643 1.00 34136. ? 491 PRO I CA  1 
ATOM 1263 C C   . PRO A 1 159 ? 276.524 276.441 291.100 1.00 34085. ? 491 PRO I C   1 
ATOM 1264 O O   . PRO A 1 159 ? 275.536 275.933 290.558 1.00 34161. ? 491 PRO I O   1 
ATOM 1265 C CB  . PRO A 1 159 ? 278.229 277.711 289.728 1.00 34067. ? 491 PRO I CB  1 
ATOM 1266 C CG  . PRO A 1 159 ? 279.375 277.991 290.614 1.00 34412. ? 491 PRO I CG  1 
ATOM 1267 C CD  . PRO A 1 159 ? 278.895 279.035 291.566 1.00 34629. ? 491 PRO I CD  1 
ATOM 1268 N N   . LEU A 1 160 ? 277.178 275.830 292.079 1.00 34123. ? 492 LEU I N   1 
ATOM 1269 C CA  . LEU A 1 160 ? 276.880 274.462 292.479 1.00 33990. ? 492 LEU I CA  1 
ATOM 1270 C C   . LEU A 1 160 ? 275.938 274.440 293.674 1.00 33948. ? 492 LEU I C   1 
ATOM 1271 O O   . LEU A 1 160 ? 276.165 275.138 294.665 1.00 34169. ? 492 LEU I O   1 
ATOM 1272 C CB  . LEU A 1 160 ? 278.167 273.709 292.806 1.00 34029. ? 492 LEU I CB  1 
ATOM 1273 C CG  . LEU A 1 160 ? 279.232 273.859 291.725 1.00 34061. ? 492 LEU I CG  1 
ATOM 1274 C CD1 . LEU A 1 160 ? 280.617 273.653 292.293 1.00 34114. ? 492 LEU I CD1 1 
ATOM 1275 C CD2 . LEU A 1 160 ? 278.961 272.903 290.591 1.00 34047. ? 492 LEU I CD2 1 
ATOM 1276 N N   . GLN A 1 161 ? 274.888 273.632 293.574 1.00 33842. ? 493 GLN I N   1 
ATOM 1277 C CA  . GLN A 1 161 ? 273.907 273.459 294.633 1.00 33937. ? 493 GLN I CA  1 
ATOM 1278 C C   . GLN A 1 161 ? 273.955 272.015 295.110 1.00 34041. ? 493 GLN I C   1 
ATOM 1279 O O   . GLN A 1 161 ? 273.950 271.089 294.299 1.00 34167. ? 493 GLN I O   1 
ATOM 1280 C CB  . GLN A 1 161 ? 272.504 273.838 294.152 1.00 33999. ? 493 GLN I CB  1 
ATOM 1281 C CG  . GLN A 1 161 ? 271.366 273.175 294.901 1.00 34059. ? 493 GLN I CG  1 
ATOM 1282 C CD  . GLN A 1 161 ? 270.975 273.943 296.143 1.00 34061. ? 493 GLN I CD  1 
ATOM 1283 O OE1 . GLN A 1 161 ? 271.190 275.150 296.230 1.00 33985. ? 493 GLN I OE1 1 
ATOM 1284 N NE2 . GLN A 1 161 ? 270.408 273.244 297.119 1.00 34064. ? 493 GLN I NE2 1 
ATOM 1285 N N   . SER A 1 162 ? 274.033 271.826 296.417 1.00 34000. ? 494 SER I N   1 
ATOM 1286 C CA  . SER A 1 162 ? 274.195 270.499 296.992 1.00 33951. ? 494 SER I CA  1 
ATOM 1287 C C   . SER A 1 162 ? 272.873 269.756 297.097 1.00 34035. ? 494 SER I C   1 
ATOM 1288 O O   . SER A 1 162 ? 271.884 270.305 297.589 1.00 34088. ? 494 SER I O   1 
ATOM 1289 C CB  . SER A 1 162 ? 274.823 270.595 298.373 1.00 33837. ? 494 SER I CB  1 
ATOM 1290 O OG  . SER A 1 162 ? 274.881 269.315 298.959 1.00 33799. ? 494 SER I OG  1 
ATOM 1291 N N   . TYR A 1 163 ? 272.853 268.517 296.604 1.00 34022. ? 495 TYR I N   1 
ATOM 1292 C CA  . TYR A 1 163 ? 271.669 267.682 296.741 1.00 33990. ? 495 TYR I CA  1 
ATOM 1293 C C   . TYR A 1 163 ? 271.527 267.318 298.207 1.00 34010. ? 495 TYR I C   1 
ATOM 1294 O O   . TYR A 1 163 ? 272.485 266.856 298.827 1.00 33935. ? 495 TYR I O   1 
ATOM 1295 C CB  . TYR A 1 163 ? 271.831 266.376 295.968 1.00 34018. ? 495 TYR I CB  1 
ATOM 1296 C CG  . TYR A 1 163 ? 271.527 266.350 294.498 1.00 33994. ? 495 TYR I CG  1 
ATOM 1297 C CD1 . TYR A 1 163 ? 270.289 266.722 294.014 1.00 34100. ? 495 TYR I CD1 1 
ATOM 1298 C CD2 . TYR A 1 163 ? 272.454 265.837 293.602 1.00 33939. ? 495 TYR I CD2 1 
ATOM 1299 C CE1 . TYR A 1 163 ? 270.015 266.662 292.669 1.00 34102. ? 495 TYR I CE1 1 
ATOM 1300 C CE2 . TYR A 1 163 ? 272.179 265.765 292.260 1.00 33933. ? 495 TYR I CE2 1 
ATOM 1301 C CZ  . TYR A 1 163 ? 270.952 266.173 291.805 1.00 33951. ? 495 TYR I CZ  1 
ATOM 1302 O OH  . TYR A 1 163 ? 270.652 266.119 290.475 1.00 33946. ? 495 TYR I OH  1 
ATOM 1303 N N   . GLY A 1 164 ? 270.344 267.492 298.771 1.00 34235. ? 496 GLY I N   1 
ATOM 1304 C CA  . GLY A 1 164 ? 270.211 267.023 300.132 1.00 34116. ? 496 GLY I CA  1 
ATOM 1305 C C   . GLY A 1 164 ? 269.723 265.596 300.114 1.00 34233. ? 496 GLY I C   1 
ATOM 1306 O O   . GLY A 1 164 ? 268.550 265.351 299.813 1.00 34298. ? 496 GLY I O   1 
ATOM 1307 N N   . PHE A 1 165 ? 270.591 264.644 300.427 1.00 34070. ? 497 PHE I N   1 
ATOM 1308 C CA  . PHE A 1 165 ? 270.223 263.241 300.352 1.00 34011. ? 497 PHE I CA  1 
ATOM 1309 C C   . PHE A 1 165 ? 269.906 262.740 301.752 1.00 34068. ? 497 PHE I C   1 
ATOM 1310 O O   . PHE A 1 165 ? 270.786 262.692 302.613 1.00 34136. ? 497 PHE I O   1 
ATOM 1311 C CB  . PHE A 1 165 ? 271.328 262.421 299.693 1.00 33987. ? 497 PHE I CB  1 
ATOM 1312 C CG  . PHE A 1 165 ? 271.345 262.529 298.193 1.00 33905. ? 497 PHE I CG  1 
ATOM 1313 C CD1 . PHE A 1 165 ? 270.163 262.623 297.480 1.00 33986. ? 497 PHE I CD1 1 
ATOM 1314 C CD2 . PHE A 1 165 ? 272.538 262.535 297.497 1.00 33958. ? 497 PHE I CD2 1 
ATOM 1315 C CE1 . PHE A 1 165 ? 270.172 262.721 296.101 1.00 33979. ? 497 PHE I CE1 1 
ATOM 1316 C CE2 . PHE A 1 165 ? 272.549 262.631 296.117 1.00 33961. ? 497 PHE I CE2 1 
ATOM 1317 C CZ  . PHE A 1 165 ? 271.365 262.726 295.424 1.00 33933. ? 497 PHE I CZ  1 
ATOM 1318 N N   . GLN A 1 166 ? 268.659 262.343 301.960 1.00 34045. ? 498 GLN I N   1 
ATOM 1319 C CA  . GLN A 1 166 ? 268.140 261.884 303.229 1.00 34017. ? 498 GLN I CA  1 
ATOM 1320 C C   . GLN A 1 166 ? 267.574 260.486 303.052 1.00 34102. ? 498 GLN I C   1 
ATOM 1321 O O   . GLN A 1 166 ? 267.113 260.138 301.960 1.00 34123. ? 498 GLN I O   1 
ATOM 1322 C CB  . GLN A 1 166 ? 267.030 262.793 303.773 1.00 34083. ? 498 GLN I CB  1 
ATOM 1323 C CG  . GLN A 1 166 ? 267.378 264.261 303.901 1.00 33992. ? 498 GLN I CG  1 
ATOM 1324 C CD  . GLN A 1 166 ? 267.974 264.607 305.236 1.00 34026. ? 498 GLN I CD  1 
ATOM 1325 O OE1 . GLN A 1 166 ? 268.406 263.734 305.983 1.00 34140. ? 498 GLN I OE1 1 
ATOM 1326 N NE2 . GLN A 1 166 ? 267.982 265.892 305.559 1.00 33997. ? 498 GLN I NE2 1 
ATOM 1327 N N   . PRO A 1 167 ? 267.670 259.641 304.080 1.00 33996. ? 499 PRO I N   1 
ATOM 1328 C CA  . PRO A 1 167 ? 267.024 258.323 304.010 1.00 33596. ? 499 PRO I CA  1 
ATOM 1329 C C   . PRO A 1 167 ? 265.519 258.401 303.825 1.00 33865. ? 499 PRO I C   1 
ATOM 1330 O O   . PRO A 1 167 ? 264.935 257.589 303.098 1.00 33780. ? 499 PRO I O   1 
ATOM 1331 C CB  . PRO A 1 167 ? 267.400 257.705 305.361 1.00 32927. ? 499 PRO I CB  1 
ATOM 1332 C CG  . PRO A 1 167 ? 268.687 258.348 305.695 1.00 33103. ? 499 PRO I CG  1 
ATOM 1333 C CD  . PRO A 1 167 ? 268.503 259.766 305.285 1.00 33802. ? 499 PRO I CD  1 
ATOM 1334 N N   . THR A 1 168 ? 264.878 259.372 304.473 1.00 35145. ? 500 THR I N   1 
ATOM 1335 C CA  . THR A 1 168 ? 263.438 259.570 304.397 1.00 35188. ? 500 THR I CA  1 
ATOM 1336 C C   . THR A 1 168 ? 262.950 260.134 303.064 1.00 35334. ? 500 THR I C   1 
ATOM 1337 O O   . THR A 1 168 ? 261.734 260.132 302.848 1.00 35446. ? 500 THR I O   1 
ATOM 1338 C CB  . THR A 1 168 ? 262.994 260.476 305.540 1.00 35435. ? 500 THR I CB  1 
ATOM 1339 O OG1 . THR A 1 168 ? 263.668 261.735 305.440 1.00 35444. ? 500 THR I OG1 1 
ATOM 1340 C CG2 . THR A 1 168 ? 263.339 259.833 306.869 1.00 35109. ? 500 THR I CG2 1 
ATOM 1341 N N   . ASN A 1 169 ? 263.834 260.666 302.210 1.00 34160. ? 501 ASN I N   1 
ATOM 1342 C CA  . ASN A 1 169 ? 263.404 261.271 300.949 1.00 34176. ? 501 ASN I CA  1 
ATOM 1343 C C   . ASN A 1 169 ? 262.718 260.275 300.026 1.00 34230. ? 501 ASN I C   1 
ATOM 1344 O O   . ASN A 1 169 ? 263.023 259.080 300.026 1.00 34226. ? 501 ASN I O   1 
ATOM 1345 C CB  . ASN A 1 169 ? 264.562 261.878 300.147 1.00 34136. ? 501 ASN I CB  1 
ATOM 1346 C CG  . ASN A 1 169 ? 264.977 263.241 300.625 1.00 34179. ? 501 ASN I CG  1 
ATOM 1347 O OD1 . ASN A 1 169 ? 266.156 263.507 300.810 1.00 34274. ? 501 ASN I OD1 1 
ATOM 1348 N ND2 . ASN A 1 169 ? 264.005 264.117 300.834 1.00 34152. ? 501 ASN I ND2 1 
ATOM 1349 N N   . GLY A 1 170 ? 261.733 260.788 299.285 1.00 34640. ? 502 GLY I N   1 
ATOM 1350 C CA  . GLY A 1 170 ? 261.002 259.982 298.328 1.00 34650. ? 502 GLY I CA  1 
ATOM 1351 C C   . GLY A 1 170 ? 261.913 259.427 297.249 1.00 34683. ? 502 GLY I C   1 
ATOM 1352 O O   . GLY A 1 170 ? 263.013 259.934 297.017 1.00 34797. ? 502 GLY I O   1 
ATOM 1353 N N   . VAL A 1 171 ? 261.434 258.353 296.605 1.00 34052. ? 503 VAL I N   1 
ATOM 1354 C CA  . VAL A 1 171 ? 262.173 257.630 295.563 1.00 34059. ? 503 VAL I CA  1 
ATOM 1355 C C   . VAL A 1 171 ? 262.643 258.567 294.450 1.00 34068. ? 503 VAL I C   1 
ATOM 1356 O O   . VAL A 1 171 ? 263.746 258.410 293.910 1.00 34107. ? 503 VAL I O   1 
ATOM 1357 C CB  . VAL A 1 171 ? 261.304 256.475 295.028 1.00 34044. ? 503 VAL I CB  1 
ATOM 1358 C CG1 . VAL A 1 171 ? 262.000 255.704 293.916 1.00 34061. ? 503 VAL I CG1 1 
ATOM 1359 C CG2 . VAL A 1 171 ? 260.931 255.543 296.164 1.00 34019. ? 503 VAL I CG2 1 
ATOM 1360 N N   . GLY A 1 172 ? 261.818 259.557 294.098 1.00 34032. ? 504 GLY I N   1 
ATOM 1361 C CA  . GLY A 1 172 ? 262.218 260.542 293.104 1.00 34065. ? 504 GLY I CA  1 
ATOM 1362 C C   . GLY A 1 172 ? 263.414 261.372 293.537 1.00 34074. ? 504 GLY I C   1 
ATOM 1363 O O   . GLY A 1 172 ? 264.266 261.724 292.720 1.00 34207. ? 504 GLY I O   1 
ATOM 1364 N N   . TYR A 1 173 ? 263.483 261.711 294.821 1.00 33996. ? 505 TYR I N   1 
ATOM 1365 C CA  . TYR A 1 173 ? 264.569 262.511 295.374 1.00 34029. ? 505 TYR I CA  1 
ATOM 1366 C C   . TYR A 1 173 ? 265.703 261.670 295.951 1.00 34029. ? 505 TYR I C   1 
ATOM 1367 O O   . TYR A 1 173 ? 266.687 262.236 296.434 1.00 34075. ? 505 TYR I O   1 
ATOM 1368 C CB  . TYR A 1 173 ? 264.023 263.467 296.445 1.00 34067. ? 505 TYR I CB  1 
ATOM 1369 C CG  . TYR A 1 173 ? 263.175 264.601 295.896 1.00 34042. ? 505 TYR I CG  1 
ATOM 1370 C CD1 . TYR A 1 173 ? 261.863 264.392 295.485 1.00 34028. ? 505 TYR I CD1 1 
ATOM 1371 C CD2 . TYR A 1 173 ? 263.685 265.890 295.815 1.00 34016. ? 505 TYR I CD2 1 
ATOM 1372 C CE1 . TYR A 1 173 ? 261.099 265.425 294.980 1.00 34075. ? 505 TYR I CE1 1 
ATOM 1373 C CE2 . TYR A 1 173 ? 262.932 266.927 295.307 1.00 34013. ? 505 TYR I CE2 1 
ATOM 1374 C CZ  . TYR A 1 173 ? 261.639 266.690 294.897 1.00 34098. ? 505 TYR I CZ  1 
ATOM 1375 O OH  . TYR A 1 173 ? 260.884 267.725 294.400 1.00 34121. ? 505 TYR I OH  1 
ATOM 1376 N N   . GLN A 1 174 ? 265.586 260.347 295.920 1.00 33997. ? 506 GLN I N   1 
ATOM 1377 C CA  . GLN A 1 174 ? 266.620 259.465 296.436 1.00 33935. ? 506 GLN I CA  1 
ATOM 1378 C C   . GLN A 1 174 ? 267.828 259.431 295.495 1.00 33964. ? 506 GLN I C   1 
ATOM 1379 O O   . GLN A 1 174 ? 267.683 259.637 294.289 1.00 34012. ? 506 GLN I O   1 
ATOM 1380 C CB  . GLN A 1 174 ? 266.049 258.063 296.631 1.00 33982. ? 506 GLN I CB  1 
ATOM 1381 C CG  . GLN A 1 174 ? 265.425 257.872 297.997 1.00 34038. ? 506 GLN I CG  1 
ATOM 1382 C CD  . GLN A 1 174 ? 264.724 256.546 298.145 1.00 34042. ? 506 GLN I CD  1 
ATOM 1383 O OE1 . GLN A 1 174 ? 265.098 255.559 297.517 1.00 34095. ? 506 GLN I OE1 1 
ATOM 1384 N NE2 . GLN A 1 174 ? 263.698 256.514 298.982 1.00 34032. ? 506 GLN I NE2 1 
ATOM 1385 N N   . PRO A 1 175 ? 269.036 259.207 296.027 1.00 33989. ? 507 PRO I N   1 
ATOM 1386 C CA  . PRO A 1 175 ? 270.221 259.116 295.163 1.00 33948. ? 507 PRO I CA  1 
ATOM 1387 C C   . PRO A 1 175 ? 270.204 257.891 294.264 1.00 33908. ? 507 PRO I C   1 
ATOM 1388 O O   . PRO A 1 175 ? 269.771 256.809 294.662 1.00 34066. ? 507 PRO I O   1 
ATOM 1389 C CB  . PRO A 1 175 ? 271.383 259.046 296.158 1.00 33947. ? 507 PRO I CB  1 
ATOM 1390 C CG  . PRO A 1 175 ? 270.793 258.561 297.393 1.00 34001. ? 507 PRO I CG  1 
ATOM 1391 C CD  . PRO A 1 175 ? 269.405 259.090 297.448 1.00 34047. ? 507 PRO I CD  1 
ATOM 1392 N N   . TYR A 1 176 ? 270.674 258.078 293.033 1.00 33909. ? 508 TYR I N   1 
ATOM 1393 C CA  . TYR A 1 176 ? 270.815 256.998 292.069 1.00 33917. ? 508 TYR I CA  1 
ATOM 1394 C C   . TYR A 1 176 ? 272.222 257.022 291.502 1.00 33932. ? 508 TYR I C   1 
ATOM 1395 O O   . TYR A 1 176 ? 272.676 258.059 291.015 1.00 34073. ? 508 TYR I O   1 
ATOM 1396 C CB  . TYR A 1 176 ? 269.801 257.132 290.929 1.00 33958. ? 508 TYR I CB  1 
ATOM 1397 C CG  . TYR A 1 176 ? 268.497 256.420 291.173 1.00 33957. ? 508 TYR I CG  1 
ATOM 1398 C CD1 . TYR A 1 176 ? 267.605 256.881 292.124 1.00 34048. ? 508 TYR I CD1 1 
ATOM 1399 C CD2 . TYR A 1 176 ? 268.150 255.297 290.442 1.00 33972. ? 508 TYR I CD2 1 
ATOM 1400 C CE1 . TYR A 1 176 ? 266.408 256.246 292.346 1.00 34011. ? 508 TYR I CE1 1 
ATOM 1401 C CE2 . TYR A 1 176 ? 266.956 254.649 290.661 1.00 34034. ? 508 TYR I CE2 1 
ATOM 1402 C CZ  . TYR A 1 176 ? 266.090 255.128 291.617 1.00 34028. ? 508 TYR I CZ  1 
ATOM 1403 O OH  . TYR A 1 176 ? 264.894 254.488 291.842 1.00 34070. ? 508 TYR I OH  1 
ATOM 1404 N N   . ARG A 1 177 ? 272.893 255.879 291.535 1.00 33903. ? 509 ARG I N   1 
ATOM 1405 C CA  . ARG A 1 177 ? 274.217 255.740 290.947 1.00 33847. ? 509 ARG I CA  1 
ATOM 1406 C C   . ARG A 1 177 ? 274.062 255.380 289.480 1.00 33896. ? 509 ARG I C   1 
ATOM 1407 O O   . ARG A 1 177 ? 273.426 254.379 289.152 1.00 34112. ? 509 ARG I O   1 
ATOM 1408 C CB  . ARG A 1 177 ? 275.032 254.682 291.681 1.00 33984. ? 509 ARG I CB  1 
ATOM 1409 C CG  . ARG A 1 177 ? 275.652 255.152 292.963 1.00 33984. ? 509 ARG I CG  1 
ATOM 1410 C CD  . ARG A 1 177 ? 276.610 254.136 293.522 1.00 34000. ? 509 ARG I CD  1 
ATOM 1411 N NE  . ARG A 1 177 ? 276.764 254.279 294.961 1.00 33884. ? 509 ARG I NE  1 
ATOM 1412 C CZ  . ARG A 1 177 ? 277.930 254.462 295.563 1.00 33778. ? 509 ARG I CZ  1 
ATOM 1413 N NH1 . ARG A 1 177 ? 279.056 254.519 294.879 1.00 33860. ? 509 ARG I NH1 1 
ATOM 1414 N NH2 . ARG A 1 177 ? 277.964 254.607 296.881 1.00 33712. ? 509 ARG I NH2 1 
ATOM 1415 N N   . VAL A 1 178 ? 274.656 256.180 288.601 1.00 33875. ? 510 VAL I N   1 
ATOM 1416 C CA  . VAL A 1 178 ? 274.493 256.028 287.161 1.00 33896. ? 510 VAL I CA  1 
ATOM 1417 C C   . VAL A 1 178 ? 275.847 255.775 286.524 1.00 33944. ? 510 VAL I C   1 
ATOM 1418 O O   . VAL A 1 178 ? 276.786 256.547 286.731 1.00 34149. ? 510 VAL I O   1 
ATOM 1419 C CB  . VAL A 1 178 ? 273.830 257.266 286.531 1.00 33872. ? 510 VAL I CB  1 
ATOM 1420 C CG1 . VAL A 1 178 ? 273.632 257.066 285.048 1.00 33978. ? 510 VAL I CG1 1 
ATOM 1421 C CG2 . VAL A 1 178 ? 272.505 257.552 287.185 1.00 34028. ? 510 VAL I CG2 1 
ATOM 1422 N N   . VAL A 1 179 ? 275.947 254.693 285.759 1.00 33949. ? 511 VAL I N   1 
ATOM 1423 C CA  . VAL A 1 179 ? 277.125 254.396 284.955 1.00 33904. ? 511 VAL I CA  1 
ATOM 1424 C C   . VAL A 1 179 ? 276.690 254.412 283.498 1.00 33923. ? 511 VAL I C   1 
ATOM 1425 O O   . VAL A 1 179 ? 275.781 253.670 283.109 1.00 34042. ? 511 VAL I O   1 
ATOM 1426 C CB  . VAL A 1 179 ? 277.766 253.050 285.328 1.00 33920. ? 511 VAL I CB  1 
ATOM 1427 C CG1 . VAL A 1 179 ? 278.726 252.596 284.243 1.00 33946. ? 511 VAL I CG1 1 
ATOM 1428 C CG2 . VAL A 1 179 ? 278.501 253.169 286.637 1.00 33986. ? 511 VAL I CG2 1 
ATOM 1429 N N   . VAL A 1 180 ? 277.319 255.268 282.700 1.00 33940. ? 512 VAL I N   1 
ATOM 1430 C CA  . VAL A 1 180 ? 277.047 255.363 281.272 1.00 33873. ? 512 VAL I CA  1 
ATOM 1431 C C   . VAL A 1 180 ? 278.218 254.743 280.528 1.00 33911. ? 512 VAL I C   1 
ATOM 1432 O O   . VAL A 1 180 ? 279.356 255.203 280.657 1.00 34080. ? 512 VAL I O   1 
ATOM 1433 C CB  . VAL A 1 180 ? 276.824 256.817 280.835 1.00 33895. ? 512 VAL I CB  1 
ATOM 1434 C CG1 . VAL A 1 180 ? 276.479 256.877 279.370 1.00 33970. ? 512 VAL I CG1 1 
ATOM 1435 C CG2 . VAL A 1 180 ? 275.730 257.453 281.663 1.00 33987. ? 512 VAL I CG2 1 
ATOM 1436 N N   . LEU A 1 181 ? 277.939 253.712 279.739 1.00 33899. ? 513 LEU I N   1 
ATOM 1437 C CA  . LEU A 1 181 ? 278.952 253.031 278.946 1.00 33894. ? 513 LEU I CA  1 
ATOM 1438 C C   . LEU A 1 181 ? 278.849 253.542 277.518 1.00 33908. ? 513 LEU I C   1 
ATOM 1439 O O   . LEU A 1 181 ? 277.774 253.501 276.926 1.00 34059. ? 513 LEU I O   1 
ATOM 1440 C CB  . LEU A 1 181 ? 278.762 251.516 278.991 1.00 34002. ? 513 LEU I CB  1 
ATOM 1441 C CG  . LEU A 1 181 ? 278.912 250.814 280.341 1.00 33975. ? 513 LEU I CG  1 
ATOM 1442 C CD1 . LEU A 1 181 ? 278.573 249.349 280.212 1.00 34052. ? 513 LEU I CD1 1 
ATOM 1443 C CD2 . LEU A 1 181 ? 280.313 250.980 280.881 1.00 34044. ? 513 LEU I CD2 1 
ATOM 1444 N N   . SER A 1 182 ? 279.945 254.069 276.987 1.00 33903. ? 514 SER I N   1 
ATOM 1445 C CA  . SER A 1 182 ? 279.990 254.604 275.632 1.00 33923. ? 514 SER I CA  1 
ATOM 1446 C C   . SER A 1 182 ? 280.819 253.674 274.760 1.00 34019. ? 514 SER I C   1 
ATOM 1447 O O   . SER A 1 182 ? 282.013 253.511 275.001 1.00 34222. ? 514 SER I O   1 
ATOM 1448 C CB  . SER A 1 182 ? 280.593 256.006 275.623 1.00 34000. ? 514 SER I CB  1 
ATOM 1449 O OG  . SER A 1 182 ? 279.845 256.892 276.430 1.00 33986. ? 514 SER I OG  1 
ATOM 1450 N N   . PHE A 1 183 ? 280.216 253.125 273.715 1.00 34046. ? 515 PHE I N   1 
ATOM 1451 C CA  . PHE A 1 183 ? 280.889 252.178 272.838 1.00 34286. ? 515 PHE I CA  1 
ATOM 1452 C C   . PHE A 1 183 ? 281.185 252.838 271.502 1.00 34667. ? 515 PHE I C   1 
ATOM 1453 O O   . PHE A 1 183 ? 280.324 253.517 270.940 1.00 34558. ? 515 PHE I O   1 
ATOM 1454 C CB  . PHE A 1 183 ? 280.038 250.929 272.603 1.00 34433. ? 515 PHE I CB  1 
ATOM 1455 C CG  . PHE A 1 183 ? 279.434 250.355 273.843 1.00 34242. ? 515 PHE I CG  1 
ATOM 1456 C CD1 . PHE A 1 183 ? 280.225 250.017 274.923 1.00 34260. ? 515 PHE I CD1 1 
ATOM 1457 C CD2 . PHE A 1 183 ? 278.078 250.116 273.912 1.00 34172. ? 515 PHE I CD2 1 
ATOM 1458 C CE1 . PHE A 1 183 ? 279.667 249.473 276.062 1.00 34134. ? 515 PHE I CE1 1 
ATOM 1459 C CE2 . PHE A 1 183 ? 277.514 249.577 275.046 1.00 34058. ? 515 PHE I CE2 1 
ATOM 1460 C CZ  . PHE A 1 183 ? 278.309 249.257 276.122 1.00 34076. ? 515 PHE I CZ  1 
ATOM 1461 N N   . GLU A 1 184 ? 282.406 252.667 271.010 1.00 45874. ? 516 GLU I N   1 
ATOM 1462 C CA  . GLU A 1 184 ? 282.793 253.161 269.696 1.00 46313. ? 516 GLU I CA  1 
ATOM 1463 C C   . GLU A 1 184 ? 283.018 251.982 268.760 1.00 46553. ? 516 GLU I C   1 
ATOM 1464 O O   . GLU A 1 184 ? 283.788 251.071 269.081 1.00 46534. ? 516 GLU I O   1 
ATOM 1465 C CB  . GLU A 1 184 ? 284.058 254.015 269.787 1.00 46429. ? 516 GLU I CB  1 
ATOM 1466 C CG  . GLU A 1 184 ? 284.525 254.590 268.461 1.00 46600. ? 516 GLU I CG  1 
ATOM 1467 C CD  . GLU A 1 184 ? 285.903 255.214 268.556 1.00 46609. ? 516 GLU I CD  1 
ATOM 1468 O OE1 . GLU A 1 184 ? 286.234 255.762 269.628 1.00 46508. ? 516 GLU I OE1 1 
ATOM 1469 O OE2 . GLU A 1 184 ? 286.656 255.154 267.562 1.00 46641. ? 516 GLU I OE2 1 
ATOM 1470 N N   . LEU A 1 185 ? 282.356 251.999 267.606 1.00 50778. ? 517 LEU I N   1 
ATOM 1471 C CA  . LEU A 1 185 ? 282.547 250.982 266.576 1.00 51018. ? 517 LEU I CA  1 
ATOM 1472 C C   . LEU A 1 185 ? 283.161 251.638 265.344 1.00 51294. ? 517 LEU I C   1 
ATOM 1473 O O   . LEU A 1 185 ? 282.472 252.355 264.611 1.00 51185. ? 517 LEU I O   1 
ATOM 1474 C CB  . LEU A 1 185 ? 281.230 250.289 266.222 1.00 51001. ? 517 LEU I CB  1 
ATOM 1475 C CG  . LEU A 1 185 ? 280.523 249.363 267.223 1.00 50928. ? 517 LEU I CG  1 
ATOM 1476 C CD1 . LEU A 1 185 ? 279.682 250.112 268.249 1.00 50718. ? 517 LEU I CD1 1 
ATOM 1477 C CD2 . LEU A 1 185 ? 279.681 248.332 266.489 1.00 50934. ? 517 LEU I CD2 1 
ATOM 1478 N N   . LEU A 1 186 ? 284.452 251.392 265.112 1.00 59752. ? 518 LEU I N   1 
ATOM 1479 C CA  . LEU A 1 186 ? 285.154 251.962 263.968 1.00 60070. ? 518 LEU I CA  1 
ATOM 1480 C C   . LEU A 1 186 ? 286.131 250.922 263.425 1.00 60226. ? 518 LEU I C   1 
ATOM 1481 O O   . LEU A 1 186 ? 286.188 249.784 263.903 1.00 60137. ? 518 LEU I O   1 
ATOM 1482 C CB  . LEU A 1 186 ? 285.861 253.264 264.368 1.00 60040. ? 518 LEU I CB  1 
ATOM 1483 C CG  . LEU A 1 186 ? 285.982 254.394 263.340 1.00 60135. ? 518 LEU I CG  1 
ATOM 1484 C CD1 . LEU A 1 186 ? 284.606 254.900 262.938 1.00 60109. ? 518 LEU I CD1 1 
ATOM 1485 C CD2 . LEU A 1 186 ? 286.839 255.524 263.886 1.00 60106. ? 518 LEU I CD2 1 
ATOM 1486 N N   . HIS A 1 187 ? 286.911 251.316 262.416 1.00 65664. ? 519 HIS I N   1 
ATOM 1487 C CA  . HIS A 1 187 ? 287.987 250.484 261.875 1.00 65764. ? 519 HIS I CA  1 
ATOM 1488 C C   . HIS A 1 187 ? 289.241 250.759 262.710 1.00 65710. ? 519 HIS I C   1 
ATOM 1489 O O   . HIS A 1 187 ? 289.975 251.725 262.479 1.00 65782. ? 519 HIS I O   1 
ATOM 1490 C CB  . HIS A 1 187 ? 288.139 250.705 260.365 1.00 65853. ? 519 HIS I CB  1 
ATOM 1491 C CG  . HIS A 1 187 ? 288.486 252.107 259.956 1.00 65878. ? 519 HIS I CG  1 
ATOM 1492 N ND1 . HIS A 1 187 ? 287.549 253.115 259.879 1.00 65842. ? 519 HIS I ND1 1 
ATOM 1493 C CD2 . HIS A 1 187 ? 289.661 252.656 259.564 1.00 65891. ? 519 HIS I CD2 1 
ATOM 1494 C CE1 . HIS A 1 187 ? 288.136 254.230 259.484 1.00 65867. ? 519 HIS I CE1 1 
ATOM 1495 N NE2 . HIS A 1 187 ? 289.417 253.979 259.285 1.00 65896. ? 519 HIS I NE2 1 
ATOM 1496 N N   . ALA A 1 188 ? 289.491 249.882 263.686 1.00 60883. ? 520 ALA I N   1 
ATOM 1497 C CA  . ALA A 1 188 ? 290.528 250.067 264.692 1.00 60737. ? 520 ALA I CA  1 
ATOM 1498 C C   . ALA A 1 188 ? 290.754 248.703 265.364 1.00 60637. ? 520 ALA I C   1 
ATOM 1499 O O   . ALA A 1 188 ? 290.124 247.744 264.897 1.00 60686. ? 520 ALA I O   1 
ATOM 1500 C CB  . ALA A 1 188 ? 290.027 251.181 265.628 1.00 60683. ? 520 ALA I CB  1 
ATOM 1501 N N   . PRO A 1 189 ? 291.672 248.519 266.362 1.00 58409. ? 521 PRO I N   1 
ATOM 1502 C CA  . PRO A 1 189 ? 291.889 247.161 266.923 1.00 58366. ? 521 PRO I CA  1 
ATOM 1503 C C   . PRO A 1 189 ? 290.665 246.418 267.459 1.00 58216. ? 521 PRO I C   1 
ATOM 1504 O O   . PRO A 1 189 ? 290.657 245.181 267.375 1.00 58249. ? 521 PRO I O   1 
ATOM 1505 C CB  . PRO A 1 189 ? 292.929 247.398 268.029 1.00 58338. ? 521 PRO I CB  1 
ATOM 1506 C CG  . PRO A 1 189 ? 292.974 248.849 268.253 1.00 58359. ? 521 PRO I CG  1 
ATOM 1507 C CD  . PRO A 1 189 ? 292.714 249.419 266.906 1.00 58395. ? 521 PRO I CD  1 
ATOM 1508 N N   . ALA A 1 190 ? 289.651 247.126 267.982 1.00 54115. ? 522 ALA I N   1 
ATOM 1509 C CA  . ALA A 1 190 ? 288.448 246.529 268.593 1.00 53887. ? 522 ALA I CA  1 
ATOM 1510 C C   . ALA A 1 190 ? 288.799 245.538 269.702 1.00 53822. ? 522 ALA I C   1 
ATOM 1511 O O   . ALA A 1 190 ? 288.243 244.439 269.774 1.00 53829. ? 522 ALA I O   1 
ATOM 1512 C CB  . ALA A 1 190 ? 287.538 245.882 267.543 1.00 53907. ? 522 ALA I CB  1 
ATOM 1513 N N   . THR A 1 191 ? 289.781 245.918 270.530 1.00 51392. ? 523 THR I N   1 
ATOM 1514 C CA  . THR A 1 191 ? 290.295 245.036 271.577 1.00 51288. ? 523 THR I CA  1 
ATOM 1515 C C   . THR A 1 191 ? 289.231 244.693 272.611 1.00 51099. ? 523 THR I C   1 
ATOM 1516 O O   . THR A 1 191 ? 289.123 243.537 273.035 1.00 51181. ? 523 THR I O   1 
ATOM 1517 C CB  . THR A 1 191 ? 291.490 245.686 272.266 1.00 51263. ? 523 THR I CB  1 
ATOM 1518 O OG1 . THR A 1 191 ? 291.150 247.027 272.642 1.00 51148. ? 523 THR I OG1 1 
ATOM 1519 C CG2 . THR A 1 191 ? 292.696 245.703 271.342 1.00 51357. ? 523 THR I CG2 1 
ATOM 1520 N N   . VAL A 1 192 ? 288.434 245.670 273.033 1.00 46091. ? 524 VAL I N   1 
ATOM 1521 C CA  . VAL A 1 192 ? 287.429 245.413 274.058 1.00 45958. ? 524 VAL I CA  1 
ATOM 1522 C C   . VAL A 1 192 ? 286.136 244.943 273.373 1.00 46072. ? 524 VAL I C   1 
ATOM 1523 O O   . VAL A 1 192 ? 285.069 245.564 273.454 1.00 45943. ? 524 VAL I O   1 
ATOM 1524 C CB  . VAL A 1 192 ? 287.323 246.649 274.994 1.00 45676. ? 524 VAL I CB  1 
ATOM 1525 C CG1 . VAL A 1 192 ? 287.011 247.943 274.263 1.00 45610. ? 524 VAL I CG1 1 
ATOM 1526 C CG2 . VAL A 1 192 ? 286.380 246.431 276.178 1.00 45604. ? 524 VAL I CG2 1 
ATOM 1527 N N   . CYS A 1 193 ? 286.250 243.834 272.635 1.00 52343. ? 525 CYS I N   1 
ATOM 1528 C CA  . CYS A 1 193 ? 285.081 243.214 272.023 1.00 52478. ? 525 CYS I CA  1 
ATOM 1529 C C   . CYS A 1 193 ? 284.155 242.609 273.064 1.00 52359. ? 525 CYS I C   1 
ATOM 1530 O O   . CYS A 1 193 ? 282.928 242.701 272.943 1.00 52381. ? 525 CYS I O   1 
ATOM 1531 C CB  . CYS A 1 193 ? 285.502 242.152 271.012 1.00 52598. ? 525 CYS I CB  1 
ATOM 1532 S SG  . CYS A 1 193 ? 284.107 241.565 270.027 1.00 52641. ? 525 CYS I SG  1 
ATOM 1533 N N   . GLY A 1 194 ? 284.729 242.007 274.096 1.00 46389. ? 526 GLY I N   1 
ATOM 1534 C CA  . GLY A 1 194 ? 283.977 241.321 275.119 1.00 46235. ? 526 GLY I CA  1 
ATOM 1535 C C   . GLY A 1 194 ? 283.016 240.206 274.721 1.00 46247. ? 526 GLY I C   1 
ATOM 1536 O O   . GLY A 1 194 ? 281.828 240.295 275.045 1.00 46207. ? 526 GLY I O   1 
ATOM 1537 N N   . PRO A 1 195 ? 283.464 239.178 273.947 1.00 48042. ? 527 PRO I N   1 
ATOM 1538 C CA  . PRO A 1 195 ? 282.544 238.071 273.628 1.00 48109. ? 527 PRO I CA  1 
ATOM 1539 C C   . PRO A 1 195 ? 281.986 237.323 274.845 1.00 48061. ? 527 PRO I C   1 
ATOM 1540 O O   . PRO A 1 195 ? 282.758 237.012 275.751 1.00 48013. ? 527 PRO I O   1 
ATOM 1541 C CB  . PRO A 1 195 ? 283.410 237.118 272.795 1.00 48108. ? 527 PRO I CB  1 
ATOM 1542 C CG  . PRO A 1 195 ? 284.528 237.933 272.296 1.00 48140. ? 527 PRO I CG  1 
ATOM 1543 C CD  . PRO A 1 195 ? 284.803 238.905 273.389 1.00 48102. ? 527 PRO I CD  1 
ATOM 1544 N N   . GLU B 2 1   ? 294.988 262.509 306.478 1.00 93.01  ? 1   GLU G N   1 
ATOM 1545 C CA  . GLU B 2 1   ? 294.280 261.574 307.342 1.00 93.32  ? 1   GLU G CA  1 
ATOM 1546 C C   . GLU B 2 1   ? 293.285 262.312 308.231 1.00 91.97  ? 1   GLU G C   1 
ATOM 1547 O O   . GLU B 2 1   ? 293.644 263.282 308.900 1.00 86.17  ? 1   GLU G O   1 
ATOM 1548 C CB  . GLU B 2 1   ? 295.267 260.774 308.196 1.00 95.49  ? 1   GLU G CB  1 
ATOM 1549 C CG  . GLU B 2 1   ? 294.630 260.065 309.381 1.00 95.02  ? 1   GLU G CG  1 
ATOM 1550 C CD  . GLU B 2 1   ? 295.548 259.045 310.018 1.00 93.19  ? 1   GLU G CD  1 
ATOM 1551 O OE1 . GLU B 2 1   ? 295.555 257.885 309.558 1.00 97.65  ? 1   GLU G OE1 1 
ATOM 1552 O OE2 . GLU B 2 1   ? 296.258 259.401 310.982 1.00 89.18  ? 1   GLU G OE2 1 
ATOM 1553 N N   . VAL B 2 2   ? 292.028 261.859 308.190 1.00 80.60  ? 2   VAL G N   1 
ATOM 1554 C CA  . VAL B 2 2   ? 290.971 262.441 309.008 1.00 81.35  ? 2   VAL G CA  1 
ATOM 1555 C C   . VAL B 2 2   ? 291.282 262.208 310.481 1.00 82.54  ? 2   VAL G C   1 
ATOM 1556 O O   . VAL B 2 2   ? 291.575 261.082 310.899 1.00 76.55  ? 2   VAL G O   1 
ATOM 1557 C CB  . VAL B 2 2   ? 289.618 261.835 308.605 1.00 78.03  ? 2   VAL G CB  1 
ATOM 1558 C CG1 . VAL B 2 2   ? 288.557 262.145 309.635 1.00 76.91  ? 2   VAL G CG1 1 
ATOM 1559 C CG2 . VAL B 2 2   ? 289.209 262.313 307.226 1.00 75.42  ? 2   VAL G CG2 1 
ATOM 1560 N N   . GLN B 2 3   ? 291.228 263.276 311.278 1.00 80.14  ? 3   GLN G N   1 
ATOM 1561 C CA  . GLN B 2 3   ? 291.536 263.187 312.699 1.00 79.04  ? 3   GLN G CA  1 
ATOM 1562 C C   . GLN B 2 3   ? 290.512 263.958 313.516 1.00 77.98  ? 3   GLN G C   1 
ATOM 1563 O O   . GLN B 2 3   ? 290.237 265.123 313.223 1.00 80.49  ? 3   GLN G O   1 
ATOM 1564 C CB  . GLN B 2 3   ? 292.938 263.732 312.979 1.00 85.75  ? 3   GLN G CB  1 
ATOM 1565 C CG  . GLN B 2 3   ? 294.042 262.712 312.793 1.00 89.43  ? 3   GLN G CG  1 
ATOM 1566 C CD  . GLN B 2 3   ? 295.312 263.334 312.253 1.00 89.70  ? 3   GLN G CD  1 
ATOM 1567 O OE1 . GLN B 2 3   ? 295.511 264.544 312.352 1.00 87.39  ? 3   GLN G OE1 1 
ATOM 1568 N NE2 . GLN B 2 3   ? 296.176 262.510 311.671 1.00 84.02  ? 3   GLN G NE2 1 
ATOM 1569 N N   . LEU B 2 4   ? 289.946 263.307 314.529 1.00 62.33  ? 4   LEU G N   1 
ATOM 1570 C CA  . LEU B 2 4   ? 289.025 263.935 315.466 1.00 62.34  ? 4   LEU G CA  1 
ATOM 1571 C C   . LEU B 2 4   ? 289.588 263.781 316.872 1.00 66.35  ? 4   LEU G C   1 
ATOM 1572 O O   . LEU B 2 4   ? 289.953 262.673 317.276 1.00 75.21  ? 4   LEU G O   1 
ATOM 1573 C CB  . LEU B 2 4   ? 287.623 263.324 315.378 1.00 61.29  ? 4   LEU G CB  1 
ATOM 1574 C CG  . LEU B 2 4   ? 286.988 263.183 313.994 1.00 58.79  ? 4   LEU G CG  1 
ATOM 1575 C CD1 . LEU B 2 4   ? 285.624 262.561 314.110 1.00 64.93  ? 4   LEU G CD1 1 
ATOM 1576 C CD2 . LEU B 2 4   ? 286.884 264.521 313.315 1.00 66.27  ? 4   LEU G CD2 1 
ATOM 1577 N N   . VAL B 2 5   ? 289.667 264.887 317.612 1.00 67.10  ? 5   VAL G N   1 
ATOM 1578 C CA  . VAL B 2 5   ? 290.191 264.896 318.976 1.00 74.25  ? 5   VAL G CA  1 
ATOM 1579 C C   . VAL B 2 5   ? 289.188 265.596 319.884 1.00 65.62  ? 5   VAL G C   1 
ATOM 1580 O O   . VAL B 2 5   ? 288.783 266.730 319.610 1.00 75.64  ? 5   VAL G O   1 
ATOM 1581 C CB  . VAL B 2 5   ? 291.564 265.597 319.058 1.00 77.12  ? 5   VAL G CB  1 
ATOM 1582 C CG1 . VAL B 2 5   ? 292.044 265.683 320.499 1.00 72.27  ? 5   VAL G CG1 1 
ATOM 1583 C CG2 . VAL B 2 5   ? 292.605 264.880 318.207 1.00 73.84  ? 5   VAL G CG2 1 
ATOM 1584 N N   . GLU B 2 6   ? 288.804 264.932 320.971 1.00 68.60  ? 6   GLU G N   1 
ATOM 1585 C CA  . GLU B 2 6   ? 287.834 265.460 321.921 1.00 78.19  ? 6   GLU G CA  1 
ATOM 1586 C C   . GLU B 2 6   ? 288.564 266.064 323.111 1.00 80.82  ? 6   GLU G C   1 
ATOM 1587 O O   . GLU B 2 6   ? 289.475 265.444 323.668 1.00 78.13  ? 6   GLU G O   1 
ATOM 1588 C CB  . GLU B 2 6   ? 286.867 264.380 322.418 1.00 65.92  ? 6   GLU G CB  1 
ATOM 1589 C CG  . GLU B 2 6   ? 285.850 263.882 321.413 1.00 67.54  ? 6   GLU G CG  1 
ATOM 1590 C CD  . GLU B 2 6   ? 286.447 262.961 320.381 1.00 73.85  ? 6   GLU G CD  1 
ATOM 1591 O OE1 . GLU B 2 6   ? 286.749 261.805 320.724 1.00 72.32  ? 6   GLU G OE1 1 
ATOM 1592 O OE2 . GLU B 2 6   ? 286.642 263.400 319.232 1.00 76.44  ? 6   GLU G OE2 1 
ATOM 1593 N N   . SER B 2 7   ? 288.159 267.270 323.497 1.00 62.78  ? 7   SER G N   1 
ATOM 1594 C CA  . SER B 2 7   ? 288.760 267.974 324.616 1.00 68.88  ? 7   SER G CA  1 
ATOM 1595 C C   . SER B 2 7   ? 287.652 268.631 325.422 1.00 70.57  ? 7   SER G C   1 
ATOM 1596 O O   . SER B 2 7   ? 286.508 268.731 324.975 1.00 74.81  ? 7   SER G O   1 
ATOM 1597 C CB  . SER B 2 7   ? 289.779 269.014 324.145 1.00 75.34  ? 7   SER G CB  1 
ATOM 1598 O OG  . SER B 2 7   ? 289.137 270.225 323.793 1.00 69.51  ? 7   SER G OG  1 
ATOM 1599 N N   . GLY B 2 8   ? 287.994 269.070 326.627 1.00 71.63  ? 8   GLY G N   1 
ATOM 1600 C CA  . GLY B 2 8   ? 287.031 269.697 327.504 1.00 66.76  ? 8   GLY G CA  1 
ATOM 1601 C C   . GLY B 2 8   ? 286.311 268.760 328.443 1.00 70.16  ? 8   GLY G C   1 
ATOM 1602 O O   . GLY B 2 8   ? 285.458 269.217 329.212 1.00 61.22  ? 8   GLY G O   1 
ATOM 1603 N N   . GLY B 2 9   ? 286.622 267.466 328.408 1.00 83.67  ? 9   GLY G N   1 
ATOM 1604 C CA  . GLY B 2 9   ? 286.029 266.526 329.344 1.00 78.84  ? 9   GLY G CA  1 
ATOM 1605 C C   . GLY B 2 9   ? 286.752 266.543 330.672 1.00 80.77  ? 9   GLY G C   1 
ATOM 1606 O O   . GLY B 2 9   ? 287.980 266.430 330.727 1.00 81.48  ? 9   GLY G O   1 
ATOM 1607 N N   . GLY B 2 10  ? 285.990 266.692 331.750 1.00 81.87  ? 10  GLY G N   1 
ATOM 1608 C CA  . GLY B 2 10  ? 286.579 266.794 333.071 1.00 76.04  ? 10  GLY G CA  1 
ATOM 1609 C C   . GLY B 2 10  ? 285.528 266.576 334.133 1.00 78.29  ? 10  GLY G C   1 
ATOM 1610 O O   . GLY B 2 10  ? 284.344 266.401 333.840 1.00 87.59  ? 10  GLY G O   1 
ATOM 1611 N N   . LEU B 2 11  ? 285.998 266.546 335.380 1.00 89.63  ? 11  LEU G N   1 
ATOM 1612 C CA  . LEU B 2 11  ? 285.113 266.398 336.528 1.00 89.20  ? 11  LEU G CA  1 
ATOM 1613 C C   . LEU B 2 11  ? 284.161 267.585 336.638 1.00 87.22  ? 11  LEU G C   1 
ATOM 1614 O O   . LEU B 2 11  ? 284.557 268.739 336.456 1.00 85.38  ? 11  LEU G O   1 
ATOM 1615 C CB  . LEU B 2 11  ? 285.942 266.270 337.804 1.00 91.73  ? 11  LEU G CB  1 
ATOM 1616 C CG  . LEU B 2 11  ? 285.173 265.942 339.077 1.00 91.06  ? 11  LEU G CG  1 
ATOM 1617 C CD1 . LEU B 2 11  ? 284.601 264.554 338.935 1.00 87.75  ? 11  LEU G CD1 1 
ATOM 1618 C CD2 . LEU B 2 11  ? 286.068 266.042 340.297 1.00 92.63  ? 11  LEU G CD2 1 
ATOM 1619 N N   . VAL B 2 12  ? 282.892 267.293 336.929 1.00 89.92  ? 12  VAL G N   1 
ATOM 1620 C CA  . VAL B 2 12  ? 281.862 268.311 337.083 1.00 92.47  ? 12  VAL G CA  1 
ATOM 1621 C C   . VAL B 2 12  ? 280.912 267.859 338.190 1.00 90.32  ? 12  VAL G C   1 
ATOM 1622 O O   . VAL B 2 12  ? 280.835 266.677 338.527 1.00 92.34  ? 12  VAL G O   1 
ATOM 1623 C CB  . VAL B 2 12  ? 281.124 268.558 335.740 1.00 90.41  ? 12  VAL G CB  1 
ATOM 1624 C CG1 . VAL B 2 12  ? 280.227 267.395 335.393 1.00 90.15  ? 12  VAL G CG1 1 
ATOM 1625 C CG2 . VAL B 2 12  ? 280.386 269.900 335.700 1.00 89.69  ? 12  VAL G CG2 1 
ATOM 1626 N N   . GLN B 2 13  ? 280.224 268.825 338.796 1.00 90.69  ? 13  GLN G N   1 
ATOM 1627 C CA  . GLN B 2 13  ? 279.217 268.576 339.814 1.00 91.67  ? 13  GLN G CA  1 
ATOM 1628 C C   . GLN B 2 13  ? 277.857 268.385 339.155 1.00 98.11  ? 13  GLN G C   1 
ATOM 1629 O O   . GLN B 2 13  ? 277.651 268.828 338.021 1.00 101.11 ? 13  GLN G O   1 
ATOM 1630 C CB  . GLN B 2 13  ? 279.175 269.750 340.791 1.00 93.43  ? 13  GLN G CB  1 
ATOM 1631 C CG  . GLN B 2 13  ? 280.474 269.982 341.536 1.00 97.01  ? 13  GLN G CG  1 
ATOM 1632 C CD  . GLN B 2 13  ? 280.593 269.121 342.777 1.00 97.55  ? 13  GLN G CD  1 
ATOM 1633 O OE1 . GLN B 2 13  ? 279.649 269.001 343.557 1.00 98.35  ? 13  GLN G OE1 1 
ATOM 1634 N NE2 . GLN B 2 13  ? 281.759 268.515 342.967 1.00 96.00  ? 13  GLN G NE2 1 
ATOM 1635 N N   . PRO B 2 14  ? 276.926 267.669 339.801 1.00 96.06  ? 14  PRO G N   1 
ATOM 1636 C CA  . PRO B 2 14  ? 275.565 267.576 339.253 1.00 96.84  ? 14  PRO G CA  1 
ATOM 1637 C C   . PRO B 2 14  ? 274.893 268.940 339.202 1.00 96.88  ? 14  PRO G C   1 
ATOM 1638 O O   . PRO B 2 14  ? 274.978 269.735 340.139 1.00 94.98  ? 14  PRO G O   1 
ATOM 1639 C CB  . PRO B 2 14  ? 274.853 266.621 340.218 1.00 94.85  ? 14  PRO G CB  1 
ATOM 1640 C CG  . PRO B 2 14  ? 275.943 265.869 340.884 1.00 89.83  ? 14  PRO G CG  1 
ATOM 1641 C CD  . PRO B 2 14  ? 277.087 266.815 340.989 1.00 94.95  ? 14  PRO G CD  1 
ATOM 1642 N N   . GLY B 2 15  ? 274.221 269.202 338.085 1.00 96.23  ? 15  GLY G N   1 
ATOM 1643 C CA  . GLY B 2 15  ? 273.644 270.500 337.828 1.00 97.86  ? 15  GLY G CA  1 
ATOM 1644 C C   . GLY B 2 15  ? 274.614 271.483 337.213 1.00 98.70  ? 15  GLY G C   1 
ATOM 1645 O O   . GLY B 2 15  ? 274.217 272.614 336.908 1.00 98.61  ? 15  GLY G O   1 
ATOM 1646 N N   . GLY B 2 16  ? 275.872 271.081 337.019 1.00 97.62  ? 16  GLY G N   1 
ATOM 1647 C CA  . GLY B 2 16  ? 276.875 271.926 336.413 1.00 93.34  ? 16  GLY G CA  1 
ATOM 1648 C C   . GLY B 2 16  ? 276.790 271.932 334.902 1.00 90.12  ? 16  GLY G C   1 
ATOM 1649 O O   . GLY B 2 16  ? 276.089 271.134 334.284 1.00 93.84  ? 16  GLY G O   1 
ATOM 1650 N N   . SER B 2 17  ? 277.525 272.860 334.297 1.00 83.99  ? 17  SER G N   1 
ATOM 1651 C CA  . SER B 2 17  ? 277.571 272.995 332.849 1.00 86.06  ? 17  SER G CA  1 
ATOM 1652 C C   . SER B 2 17  ? 278.986 272.757 332.342 1.00 84.98  ? 17  SER G C   1 
ATOM 1653 O O   . SER B 2 17  ? 279.941 273.359 332.841 1.00 90.73  ? 17  SER G O   1 
ATOM 1654 C CB  . SER B 2 17  ? 277.078 274.375 332.409 1.00 86.85  ? 17  SER G CB  1 
ATOM 1655 O OG  . SER B 2 17  ? 275.663 274.445 332.453 1.00 83.85  ? 17  SER G OG  1 
ATOM 1656 N N   . LEU B 2 18  ? 279.110 271.879 331.347 1.00 75.66  ? 18  LEU G N   1 
ATOM 1657 C CA  . LEU B 2 18  ? 280.384 271.529 330.738 1.00 76.96  ? 18  LEU G CA  1 
ATOM 1658 C C   . LEU B 2 18  ? 280.231 271.529 329.223 1.00 74.58  ? 18  LEU G C   1 
ATOM 1659 O O   . LEU B 2 18  ? 279.181 271.146 328.702 1.00 77.20  ? 18  LEU G O   1 
ATOM 1660 C CB  . LEU B 2 18  ? 280.857 270.155 331.231 1.00 83.70  ? 18  LEU G CB  1 
ATOM 1661 C CG  . LEU B 2 18  ? 282.244 269.661 330.830 1.00 83.59  ? 18  LEU G CG  1 
ATOM 1662 C CD1 . LEU B 2 18  ? 283.307 270.581 331.397 1.00 79.78  ? 18  LEU G CD1 1 
ATOM 1663 C CD2 . LEU B 2 18  ? 282.452 268.240 331.310 1.00 77.01  ? 18  LEU G CD2 1 
ATOM 1664 N N   . ARG B 2 19  ? 281.267 271.979 328.518 1.00 66.57  ? 19  ARG G N   1 
ATOM 1665 C CA  . ARG B 2 19  ? 281.277 272.016 327.061 1.00 69.74  ? 19  ARG G CA  1 
ATOM 1666 C C   . ARG B 2 19  ? 282.457 271.216 326.531 1.00 74.25  ? 19  ARG G C   1 
ATOM 1667 O O   . ARG B 2 19  ? 283.592 271.414 326.973 1.00 85.51  ? 19  ARG G O   1 
ATOM 1668 C CB  . ARG B 2 19  ? 281.338 273.457 326.557 1.00 71.96  ? 19  ARG G CB  1 
ATOM 1669 C CG  . ARG B 2 19  ? 280.892 273.636 325.122 1.00 71.63  ? 19  ARG G CG  1 
ATOM 1670 C CD  . ARG B 2 19  ? 281.401 274.949 324.566 1.00 66.59  ? 19  ARG G CD  1 
ATOM 1671 N NE  . ARG B 2 19  ? 282.826 274.893 324.268 1.00 75.20  ? 19  ARG G NE  1 
ATOM 1672 C CZ  . ARG B 2 19  ? 283.522 275.893 323.747 1.00 81.84  ? 19  ARG G CZ  1 
ATOM 1673 N NH1 . ARG B 2 19  ? 282.951 277.047 323.443 1.00 75.45  ? 19  ARG G NH1 1 
ATOM 1674 N NH2 . ARG B 2 19  ? 284.823 275.733 323.528 1.00 78.82  ? 19  ARG G NH2 1 
ATOM 1675 N N   . LEU B 2 20  ? 282.189 270.325 325.577 1.00 57.78  ? 20  LEU G N   1 
ATOM 1676 C CA  . LEU B 2 20  ? 283.201 269.465 324.972 1.00 56.14  ? 20  LEU G CA  1 
ATOM 1677 C C   . LEU B 2 20  ? 283.445 269.896 323.535 1.00 53.66  ? 20  LEU G C   1 
ATOM 1678 O O   . LEU B 2 20  ? 282.519 269.885 322.723 1.00 66.63  ? 20  LEU G O   1 
ATOM 1679 C CB  . LEU B 2 20  ? 282.772 267.999 325.011 1.00 71.21  ? 20  LEU G CB  1 
ATOM 1680 C CG  . LEU B 2 20  ? 282.094 267.521 326.289 1.00 68.71  ? 20  LEU G CG  1 
ATOM 1681 C CD1 . LEU B 2 20  ? 281.610 266.097 326.126 1.00 65.48  ? 20  LEU G CD1 1 
ATOM 1682 C CD2 . LEU B 2 20  ? 283.030 267.648 327.465 1.00 73.95  ? 20  LEU G CD2 1 
ATOM 1683 N N   . SER B 2 21  ? 284.688 270.242 323.215 1.00 61.19  ? 21  SER G N   1 
ATOM 1684 C CA  . SER B 2 21  ? 285.057 270.715 321.886 1.00 59.60  ? 21  SER G CA  1 
ATOM 1685 C C   . SER B 2 21  ? 285.754 269.607 321.104 1.00 64.55  ? 21  SER G C   1 
ATOM 1686 O O   . SER B 2 21  ? 286.729 269.021 321.582 1.00 64.55  ? 21  SER G O   1 
ATOM 1687 C CB  . SER B 2 21  ? 285.961 271.942 321.979 1.00 70.32  ? 21  SER G CB  1 
ATOM 1688 O OG  . SER B 2 21  ? 287.225 271.601 322.513 1.00 79.09  ? 21  SER G OG  1 
ATOM 1689 N N   . CYS B 2 22  ? 285.240 269.320 319.910 1.00 67.23  ? 22  CYS G N   1 
ATOM 1690 C CA  . CYS B 2 22  ? 285.763 268.277 319.028 1.00 58.46  ? 22  CYS G CA  1 
ATOM 1691 C C   . CYS B 2 22  ? 286.582 268.906 317.906 1.00 64.84  ? 22  CYS G C   1 
ATOM 1692 O O   . CYS B 2 22  ? 286.029 269.369 316.908 1.00 71.74  ? 22  CYS G O   1 
ATOM 1693 C CB  . CYS B 2 22  ? 284.596 267.471 318.474 1.00 62.55  ? 22  CYS G CB  1 
ATOM 1694 S SG  . CYS B 2 22  ? 284.948 266.224 317.234 1.00 67.83  ? 22  CYS G SG  1 
ATOM 1695 N N   . THR B 2 23  ? 287.904 268.904 318.059 1.00 71.69  ? 23  THR G N   1 
ATOM 1696 C CA  . THR B 2 23  ? 288.786 269.433 317.027 1.00 73.56  ? 23  THR G CA  1 
ATOM 1697 C C   . THR B 2 23  ? 288.836 268.460 315.849 1.00 76.94  ? 23  THR G C   1 
ATOM 1698 O O   . THR B 2 23  ? 288.847 267.242 316.039 1.00 79.29  ? 23  THR G O   1 
ATOM 1699 C CB  . THR B 2 23  ? 290.180 269.663 317.624 1.00 80.65  ? 23  THR G CB  1 
ATOM 1700 O OG1 . THR B 2 23  ? 290.066 270.553 318.740 1.00 82.27  ? 23  THR G OG1 1 
ATOM 1701 C CG2 . THR B 2 23  ? 291.134 270.305 316.625 1.00 79.93  ? 23  THR G CG2 1 
ATOM 1702 N N   . ALA B 2 24  ? 288.885 268.994 314.628 1.00 75.71  ? 24  ALA G N   1 
ATOM 1703 C CA  . ALA B 2 24  ? 288.889 268.186 313.417 1.00 69.96  ? 24  ALA G CA  1 
ATOM 1704 C C   . ALA B 2 24  ? 289.999 268.644 312.483 1.00 75.14  ? 24  ALA G C   1 
ATOM 1705 O O   . ALA B 2 24  ? 290.280 269.842 312.385 1.00 80.73  ? 24  ALA G O   1 
ATOM 1706 C CB  . ALA B 2 24  ? 287.541 268.263 312.703 1.00 74.57  ? 24  ALA G CB  1 
ATOM 1707 N N   . SER B 2 25  ? 290.630 267.691 311.797 1.00 74.89  ? 25  SER G N   1 
ATOM 1708 C CA  . SER B 2 25  ? 291.729 268.007 310.895 1.00 76.51  ? 25  SER G CA  1 
ATOM 1709 C C   . SER B 2 25  ? 291.806 266.971 309.782 1.00 78.61  ? 25  SER G C   1 
ATOM 1710 O O   . SER B 2 25  ? 291.315 265.848 309.915 1.00 83.49  ? 25  SER G O   1 
ATOM 1711 C CB  . SER B 2 25  ? 293.066 268.069 311.637 1.00 70.63  ? 25  SER G CB  1 
ATOM 1712 O OG  . SER B 2 25  ? 293.648 266.783 311.739 1.00 76.25  ? 25  SER G OG  1 
ATOM 1713 N N   . GLY B 2 26  ? 292.438 267.366 308.679 1.00 69.03  ? 26  GLY G N   1 
ATOM 1714 C CA  . GLY B 2 26  ? 292.676 266.480 307.560 1.00 65.95  ? 26  GLY G CA  1 
ATOM 1715 C C   . GLY B 2 26  ? 291.557 266.354 306.554 1.00 73.14  ? 26  GLY G C   1 
ATOM 1716 O O   . GLY B 2 26  ? 291.649 265.506 305.659 1.00 76.87  ? 26  GLY G O   1 
ATOM 1717 N N   . PHE B 2 27  ? 290.512 267.171 306.659 1.00 66.43  ? 27  PHE G N   1 
ATOM 1718 C CA  . PHE B 2 27  ? 289.380 267.115 305.743 1.00 66.90  ? 27  PHE G CA  1 
ATOM 1719 C C   . PHE B 2 27  ? 288.664 268.455 305.794 1.00 64.74  ? 27  PHE G C   1 
ATOM 1720 O O   . PHE B 2 27  ? 288.943 269.297 306.650 1.00 54.39  ? 27  PHE G O   1 
ATOM 1721 C CB  . PHE B 2 27  ? 288.432 265.950 306.079 1.00 52.76  ? 27  PHE G CB  1 
ATOM 1722 C CG  . PHE B 2 27  ? 287.770 266.055 307.428 1.00 56.44  ? 27  PHE G CG  1 
ATOM 1723 C CD1 . PHE B 2 27  ? 288.407 265.590 308.561 1.00 59.06  ? 27  PHE G CD1 1 
ATOM 1724 C CD2 . PHE B 2 27  ? 286.494 266.571 307.556 1.00 58.18  ? 27  PHE G CD2 1 
ATOM 1725 C CE1 . PHE B 2 27  ? 287.805 265.672 309.794 1.00 57.08  ? 27  PHE G CE1 1 
ATOM 1726 C CE2 . PHE B 2 27  ? 285.887 266.652 308.785 1.00 54.46  ? 27  PHE G CE2 1 
ATOM 1727 C CZ  . PHE B 2 27  ? 286.545 266.201 309.902 1.00 52.79  ? 27  PHE G CZ  1 
ATOM 1728 N N   . THR B 2 28  ? 287.735 268.647 304.859 1.00 71.68  ? 28  THR G N   1 
ATOM 1729 C CA  . THR B 2 28  ? 286.926 269.860 304.831 1.00 67.50  ? 28  THR G CA  1 
ATOM 1730 C C   . THR B 2 28  ? 285.830 269.719 305.877 1.00 64.67  ? 28  THR G C   1 
ATOM 1731 O O   . THR B 2 28  ? 284.924 268.896 305.728 1.00 63.31  ? 28  THR G O   1 
ATOM 1732 C CB  . THR B 2 28  ? 286.337 270.091 303.445 1.00 61.08  ? 28  THR G CB  1 
ATOM 1733 O OG1 . THR B 2 28  ? 287.380 270.027 302.466 1.00 59.61  ? 28  THR G OG1 1 
ATOM 1734 C CG2 . THR B 2 28  ? 285.690 271.460 303.380 1.00 65.39  ? 28  THR G CG2 1 
ATOM 1735 N N   . PHE B 2 29  ? 285.933 270.521 306.939 1.00 59.08  ? 29  PHE G N   1 
ATOM 1736 C CA  . PHE B 2 29  ? 285.033 270.429 308.087 1.00 63.12  ? 29  PHE G CA  1 
ATOM 1737 C C   . PHE B 2 29  ? 283.582 270.723 307.719 1.00 61.63  ? 29  PHE G C   1 
ATOM 1738 O O   . PHE B 2 29  ? 282.667 270.049 308.205 1.00 66.82  ? 29  PHE G O   1 
ATOM 1739 C CB  . PHE B 2 29  ? 285.537 271.375 309.179 1.00 60.87  ? 29  PHE G CB  1 
ATOM 1740 C CG  . PHE B 2 29  ? 284.677 271.425 310.402 1.00 55.56  ? 29  PHE G CG  1 
ATOM 1741 C CD1 . PHE B 2 29  ? 284.853 270.511 311.420 1.00 54.84  ? 29  PHE G CD1 1 
ATOM 1742 C CD2 . PHE B 2 29  ? 283.739 272.430 310.565 1.00 58.25  ? 29  PHE G CD2 1 
ATOM 1743 C CE1 . PHE B 2 29  ? 284.075 270.569 312.547 1.00 53.69  ? 29  PHE G CE1 1 
ATOM 1744 C CE2 . PHE B 2 29  ? 282.960 272.488 311.688 1.00 62.33  ? 29  PHE G CE2 1 
ATOM 1745 C CZ  . PHE B 2 29  ? 283.132 271.566 312.679 1.00 58.70  ? 29  PHE G CZ  1 
ATOM 1746 N N   . SER B 2 30  ? 283.357 271.747 306.893 1.00 57.20  ? 30  SER G N   1 
ATOM 1747 C CA  . SER B 2 30  ? 282.008 272.189 306.540 1.00 63.76  ? 30  SER G CA  1 
ATOM 1748 C C   . SER B 2 30  ? 281.210 271.116 305.801 1.00 58.95  ? 30  SER G C   1 
ATOM 1749 O O   . SER B 2 30  ? 279.985 271.045 305.945 1.00 54.09  ? 30  SER G O   1 
ATOM 1750 C CB  . SER B 2 30  ? 282.091 273.469 305.713 1.00 60.52  ? 30  SER G CB  1 
ATOM 1751 O OG  . SER B 2 30  ? 283.047 273.343 304.678 1.00 67.01  ? 30  SER G OG  1 
ATOM 1752 N N   . ASN B 2 31  ? 281.881 270.315 304.968 1.00 58.57  ? 31  ASN G N   1 
ATOM 1753 C CA  . ASN B 2 31  ? 281.207 269.340 304.111 1.00 58.70  ? 31  ASN G CA  1 
ATOM 1754 C C   . ASN B 2 31  ? 280.474 268.254 304.898 1.00 59.72  ? 31  ASN G C   1 
ATOM 1755 O O   . ASN B 2 31  ? 279.410 267.791 304.474 1.00 60.13  ? 31  ASN G O   1 
ATOM 1756 C CB  . ASN B 2 31  ? 282.219 268.690 303.169 1.00 55.28  ? 31  ASN G CB  1 
ATOM 1757 C CG  . ASN B 2 31  ? 282.824 269.670 302.196 1.00 54.90  ? 31  ASN G CG  1 
ATOM 1758 O OD1 . ASN B 2 31  ? 282.542 270.864 302.241 1.00 53.92  ? 31  ASN G OD1 1 
ATOM 1759 N ND2 . ASN B 2 31  ? 283.667 269.169 301.305 1.00 57.46  ? 31  ASN G ND2 1 
ATOM 1760 N N   . TYR B 2 32  ? 281.029 267.812 306.021 1.00 55.38  ? 32  TYR G N   1 
ATOM 1761 C CA  . TYR B 2 32  ? 280.529 266.640 306.730 1.00 58.59  ? 32  TYR G CA  1 
ATOM 1762 C C   . TYR B 2 32  ? 279.817 266.981 308.034 1.00 56.61  ? 32  TYR G C   1 
ATOM 1763 O O   . TYR B 2 32  ? 280.256 267.852 308.786 1.00 54.15  ? 32  TYR G O   1 
ATOM 1764 C CB  . TYR B 2 32  ? 281.677 265.673 307.021 1.00 57.66  ? 32  TYR G CB  1 
ATOM 1765 C CG  . TYR B 2 32  ? 282.523 265.326 305.819 1.00 50.19  ? 32  TYR G CG  1 
ATOM 1766 C CD1 . TYR B 2 32  ? 282.116 264.354 304.921 1.00 56.38  ? 32  TYR G CD1 1 
ATOM 1767 C CD2 . TYR B 2 32  ? 283.718 265.976 305.575 1.00 52.75  ? 32  TYR G CD2 1 
ATOM 1768 C CE1 . TYR B 2 32  ? 282.876 264.033 303.823 1.00 55.30  ? 32  TYR G CE1 1 
ATOM 1769 C CE2 . TYR B 2 32  ? 284.488 265.665 304.476 1.00 57.80  ? 32  TYR G CE2 1 
ATOM 1770 C CZ  . TYR B 2 32  ? 284.060 264.692 303.604 1.00 50.41  ? 32  TYR G CZ  1 
ATOM 1771 O OH  . TYR B 2 32  ? 284.820 264.371 302.506 1.00 54.70  ? 32  TYR G OH  1 
ATOM 1772 N N   . GLY B 2 33  ? 278.694 266.290 308.280 1.00 61.72  ? 33  GLY G N   1 
ATOM 1773 C CA  . GLY B 2 33  ? 277.993 266.396 309.544 1.00 51.12  ? 33  GLY G CA  1 
ATOM 1774 C C   . GLY B 2 33  ? 278.684 265.630 310.660 1.00 51.77  ? 33  GLY G C   1 
ATOM 1775 O O   . GLY B 2 33  ? 279.458 264.707 310.424 1.00 68.79  ? 33  GLY G O   1 
ATOM 1776 N N   . PHE B 2 34  ? 278.387 266.010 311.904 1.00 53.01  ? 34  PHE G N   1 
ATOM 1777 C CA  . PHE B 2 34  ? 279.044 265.426 313.066 1.00 44.84  ? 34  PHE G CA  1 
ATOM 1778 C C   . PHE B 2 34  ? 278.045 264.881 314.076 1.00 50.36  ? 34  PHE G C   1 
ATOM 1779 O O   . PHE B 2 34  ? 276.925 265.378 314.207 1.00 58.23  ? 34  PHE G O   1 
ATOM 1780 C CB  . PHE B 2 34  ? 279.983 266.429 313.729 1.00 37.69  ? 34  PHE G CB  1 
ATOM 1781 C CG  . PHE B 2 34  ? 281.244 266.641 312.961 1.00 45.84  ? 34  PHE G CG  1 
ATOM 1782 C CD1 . PHE B 2 34  ? 281.290 267.548 311.917 1.00 49.78  ? 34  PHE G CD1 1 
ATOM 1783 C CD2 . PHE B 2 34  ? 282.371 265.895 313.247 1.00 57.58  ? 34  PHE G CD2 1 
ATOM 1784 C CE1 . PHE B 2 34  ? 282.439 267.723 311.189 1.00 49.25  ? 34  PHE G CE1 1 
ATOM 1785 C CE2 . PHE B 2 34  ? 283.525 266.069 312.522 1.00 60.79  ? 34  PHE G CE2 1 
ATOM 1786 C CZ  . PHE B 2 34  ? 283.556 266.986 311.492 1.00 53.36  ? 34  PHE G CZ  1 
ATOM 1787 N N   . HIS B 2 35  ? 278.488 263.857 314.804 1.00 46.45  ? 35  HIS G N   1 
ATOM 1788 C CA  . HIS B 2 35  ? 277.694 263.136 315.787 1.00 40.60  ? 35  HIS G CA  1 
ATOM 1789 C C   . HIS B 2 35  ? 278.423 263.060 317.117 1.00 28.57  ? 35  HIS G C   1 
ATOM 1790 O O   . HIS B 2 35  ? 279.648 263.147 317.181 1.00 48.58  ? 35  HIS G O   1 
ATOM 1791 C CB  . HIS B 2 35  ? 277.440 261.709 315.341 1.00 36.25  ? 35  HIS G CB  1 
ATOM 1792 C CG  . HIS B 2 35  ? 276.911 261.581 313.953 1.00 38.07  ? 35  HIS G CG  1 
ATOM 1793 N ND1 . HIS B 2 35  ? 275.567 261.555 313.666 1.00 47.11  ? 35  HIS G ND1 1 
ATOM 1794 C CD2 . HIS B 2 35  ? 277.552 261.534 312.764 1.00 47.18  ? 35  HIS G CD2 1 
ATOM 1795 C CE1 . HIS B 2 35  ? 275.405 261.426 312.363 1.00 43.56  ? 35  HIS G CE1 1 
ATOM 1796 N NE2 . HIS B 2 35  ? 276.592 261.439 311.790 1.00 47.92  ? 35  HIS G NE2 1 
ATOM 1797 N N   . TRP B 2 36  ? 277.651 262.897 318.186 1.00 33.67  ? 36  TRP G N   1 
ATOM 1798 C CA  . TRP B 2 36  ? 278.188 262.661 319.519 1.00 44.10  ? 36  TRP G CA  1 
ATOM 1799 C C   . TRP B 2 36  ? 277.613 261.351 320.033 1.00 53.66  ? 36  TRP G C   1 
ATOM 1800 O O   . TRP B 2 36  ? 276.402 261.133 319.959 1.00 62.63  ? 36  TRP G O   1 
ATOM 1801 C CB  . TRP B 2 36  ? 277.860 263.813 320.464 1.00 52.96  ? 36  TRP G CB  1 
ATOM 1802 C CG  . TRP B 2 36  ? 278.815 264.950 320.332 1.00 40.31  ? 36  TRP G CG  1 
ATOM 1803 C CD1 . TRP B 2 36  ? 278.643 266.073 319.587 1.00 37.28  ? 36  TRP G CD1 1 
ATOM 1804 C CD2 . TRP B 2 36  ? 280.096 265.074 320.955 1.00 43.10  ? 36  TRP G CD2 1 
ATOM 1805 N NE1 . TRP B 2 36  ? 279.735 266.890 319.701 1.00 54.73  ? 36  TRP G NE1 1 
ATOM 1806 C CE2 . TRP B 2 36  ? 280.643 266.301 320.538 1.00 37.72  ? 36  TRP G CE2 1 
ATOM 1807 C CE3 . TRP B 2 36  ? 280.835 264.269 321.823 1.00 64.32  ? 36  TRP G CE3 1 
ATOM 1808 C CZ2 . TRP B 2 36  ? 281.891 266.743 320.962 1.00 32.51  ? 36  TRP G CZ2 1 
ATOM 1809 C CZ3 . TRP B 2 36  ? 282.074 264.710 322.240 1.00 60.42  ? 36  TRP G CZ3 1 
ATOM 1810 C CH2 . TRP B 2 36  ? 282.589 265.933 321.810 1.00 37.84  ? 36  TRP G CH2 1 
ATOM 1811 N N   . VAL B 2 37  ? 278.484 260.467 320.515 1.00 57.02  ? 37  VAL G N   1 
ATOM 1812 C CA  . VAL B 2 37  ? 278.104 259.176 321.078 1.00 46.23  ? 37  VAL G CA  1 
ATOM 1813 C C   . VAL B 2 37  ? 278.760 259.056 322.445 1.00 44.73  ? 37  VAL G C   1 
ATOM 1814 O O   . VAL B 2 37  ? 279.924 259.432 322.613 1.00 62.77  ? 37  VAL G O   1 
ATOM 1815 C CB  . VAL B 2 37  ? 278.530 258.004 320.159 1.00 42.20  ? 37  VAL G CB  1 
ATOM 1816 C CG1 . VAL B 2 37  ? 278.069 256.666 320.699 1.00 44.07  ? 37  VAL G CG1 1 
ATOM 1817 C CG2 . VAL B 2 37  ? 277.987 258.179 318.755 1.00 40.81  ? 37  VAL G CG2 1 
ATOM 1818 N N   . ARG B 2 38  ? 278.020 258.546 323.425 1.00 52.51  ? 38  ARG G N   1 
ATOM 1819 C CA  . ARG B 2 38  ? 278.539 258.360 324.772 1.00 50.67  ? 38  ARG G CA  1 
ATOM 1820 C C   . ARG B 2 38  ? 278.414 256.897 325.175 1.00 50.88  ? 38  ARG G C   1 
ATOM 1821 O O   . ARG B 2 38  ? 277.435 256.226 324.836 1.00 51.81  ? 38  ARG G O   1 
ATOM 1822 C CB  . ARG B 2 38  ? 277.839 259.274 325.802 1.00 48.47  ? 38  ARG G CB  1 
ATOM 1823 C CG  . ARG B 2 38  ? 276.438 258.884 326.255 1.00 52.21  ? 38  ARG G CG  1 
ATOM 1824 C CD  . ARG B 2 38  ? 275.833 259.963 327.118 1.00 49.61  ? 38  ARG G CD  1 
ATOM 1825 N NE  . ARG B 2 38  ? 274.424 259.735 327.398 1.00 54.20  ? 38  ARG G NE  1 
ATOM 1826 C CZ  . ARG B 2 38  ? 273.671 260.540 328.133 1.00 56.48  ? 38  ARG G CZ  1 
ATOM 1827 N NH1 . ARG B 2 38  ? 274.164 261.637 328.679 1.00 46.85  ? 38  ARG G NH1 1 
ATOM 1828 N NH2 . ARG B 2 38  ? 272.393 260.234 328.328 1.00 63.42  ? 38  ARG G NH2 1 
ATOM 1829 N N   . GLN B 2 39  ? 279.468 256.370 325.780 1.00 58.82  ? 39  GLN G N   1 
ATOM 1830 C CA  . GLN B 2 39  ? 279.440 255.038 326.366 1.00 56.26  ? 39  GLN G CA  1 
ATOM 1831 C C   . GLN B 2 39  ? 279.585 255.172 327.874 1.00 51.82  ? 39  GLN G C   1 
ATOM 1832 O O   . GLN B 2 39  ? 280.645 255.570 328.365 1.00 63.13  ? 39  GLN G O   1 
ATOM 1833 C CB  . GLN B 2 39  ? 280.544 254.157 325.793 1.00 56.99  ? 39  GLN G CB  1 
ATOM 1834 C CG  . GLN B 2 39  ? 280.470 252.724 326.263 1.00 59.30  ? 39  GLN G CG  1 
ATOM 1835 C CD  . GLN B 2 39  ? 281.309 251.796 325.429 1.00 60.20  ? 39  GLN G CD  1 
ATOM 1836 O OE1 . GLN B 2 39  ? 282.529 251.921 325.382 1.00 63.86  ? 39  GLN G OE1 1 
ATOM 1837 N NE2 . GLN B 2 39  ? 280.662 250.852 324.761 1.00 68.54  ? 39  GLN G NE2 1 
ATOM 1838 N N   . ALA B 2 40  ? 278.530 254.827 328.603 1.00 47.71  ? 40  ALA G N   1 
ATOM 1839 C CA  . ALA B 2 40  ? 278.572 254.866 330.054 1.00 57.87  ? 40  ALA G CA  1 
ATOM 1840 C C   . ALA B 2 40  ? 279.443 253.713 330.555 1.00 71.50  ? 40  ALA G C   1 
ATOM 1841 O O   . ALA B 2 40  ? 279.628 252.733 329.828 1.00 77.48  ? 40  ALA G O   1 
ATOM 1842 C CB  . ALA B 2 40  ? 277.154 254.767 330.615 1.00 61.94  ? 40  ALA G CB  1 
ATOM 1843 N N   . PRO B 2 41  ? 280.067 253.845 331.737 1.00 69.74  ? 41  PRO G N   1 
ATOM 1844 C CA  . PRO B 2 41  ? 280.943 252.767 332.233 1.00 76.57  ? 41  PRO G CA  1 
ATOM 1845 C C   . PRO B 2 41  ? 280.193 251.452 332.410 1.00 78.73  ? 41  PRO G C   1 
ATOM 1846 O O   . PRO B 2 41  ? 279.164 251.390 333.088 1.00 76.89  ? 41  PRO G O   1 
ATOM 1847 C CB  . PRO B 2 41  ? 281.460 253.312 333.569 1.00 70.86  ? 41  PRO G CB  1 
ATOM 1848 C CG  . PRO B 2 41  ? 281.319 254.773 333.463 1.00 68.23  ? 41  PRO G CG  1 
ATOM 1849 C CD  . PRO B 2 41  ? 280.120 255.025 332.621 1.00 64.43  ? 41  PRO G CD  1 
ATOM 1850 N N   . GLY B 2 42  ? 280.760 250.395 331.834 1.00 74.48  ? 42  GLY G N   1 
ATOM 1851 C CA  . GLY B 2 42  ? 280.147 249.074 331.816 1.00 67.95  ? 42  GLY G CA  1 
ATOM 1852 C C   . GLY B 2 42  ? 278.776 249.059 331.173 1.00 82.43  ? 42  GLY G C   1 
ATOM 1853 O O   . GLY B 2 42  ? 277.874 248.362 331.653 1.00 90.23  ? 42  GLY G O   1 
ATOM 1854 N N   . LYS B 2 43  ? 278.596 249.821 330.093 1.00 75.18  ? 43  LYS G N   1 
ATOM 1855 C CA  . LYS B 2 43  ? 277.320 249.934 329.399 1.00 71.39  ? 43  LYS G CA  1 
ATOM 1856 C C   . LYS B 2 43  ? 277.563 249.996 327.897 1.00 70.86  ? 43  LYS G C   1 
ATOM 1857 O O   . LYS B 2 43  ? 278.687 250.189 327.432 1.00 78.68  ? 43  LYS G O   1 
ATOM 1858 C CB  . LYS B 2 43  ? 276.525 251.176 329.830 1.00 73.85  ? 43  LYS G CB  1 
ATOM 1859 C CG  . LYS B 2 43  ? 276.089 251.226 331.288 1.00 77.86  ? 43  LYS G CG  1 
ATOM 1860 C CD  . LYS B 2 43  ? 274.977 250.243 331.587 1.00 68.62  ? 43  LYS G CD  1 
ATOM 1861 C CE  . LYS B 2 43  ? 274.576 250.317 333.048 1.00 69.56  ? 43  LYS G CE  1 
ATOM 1862 N NZ  . LYS B 2 43  ? 273.808 249.120 333.478 1.00 72.27  ? 43  LYS G NZ  1 
ATOM 1863 N N   . GLY B 2 44  ? 276.484 249.810 327.140 1.00 62.77  ? 44  GLY G N   1 
ATOM 1864 C CA  . GLY B 2 44  ? 276.540 249.882 325.697 1.00 70.32  ? 44  GLY G CA  1 
ATOM 1865 C C   . GLY B 2 44  ? 276.554 251.307 325.181 1.00 65.13  ? 44  GLY G C   1 
ATOM 1866 O O   . GLY B 2 44  ? 276.359 252.265 325.927 1.00 70.68  ? 44  GLY G O   1 
ATOM 1867 N N   . LEU B 2 45  ? 276.831 251.431 323.885 1.00 48.02  ? 45  LEU G N   1 
ATOM 1868 C CA  . LEU B 2 45  ? 276.895 252.726 323.222 1.00 49.30  ? 45  LEU G CA  1 
ATOM 1869 C C   . LEU B 2 45  ? 275.532 253.411 323.192 1.00 53.91  ? 45  LEU G C   1 
ATOM 1870 O O   . LEU B 2 45  ? 274.489 252.763 323.088 1.00 58.52  ? 45  LEU G O   1 
ATOM 1871 C CB  . LEU B 2 45  ? 277.417 252.570 321.798 1.00 46.75  ? 45  LEU G CB  1 
ATOM 1872 C CG  . LEU B 2 45  ? 278.881 252.173 321.652 1.00 56.87  ? 45  LEU G CG  1 
ATOM 1873 C CD1 . LEU B 2 45  ? 279.114 251.595 320.279 1.00 56.77  ? 45  LEU G CD1 1 
ATOM 1874 C CD2 . LEU B 2 45  ? 279.794 253.351 321.915 1.00 67.31  ? 45  LEU G CD2 1 
ATOM 1875 N N   . GLU B 2 46  ? 275.548 254.739 323.304 1.00 57.74  ? 46  GLU G N   1 
ATOM 1876 C CA  . GLU B 2 46  ? 274.327 255.540 323.270 1.00 57.36  ? 46  GLU G CA  1 
ATOM 1877 C C   . GLU B 2 46  ? 274.571 256.797 322.446 1.00 50.42  ? 46  GLU G C   1 
ATOM 1878 O O   . GLU B 2 46  ? 275.359 257.654 322.849 1.00 65.26  ? 46  GLU G O   1 
ATOM 1879 C CB  . GLU B 2 46  ? 273.866 255.901 324.680 1.00 58.92  ? 46  GLU G CB  1 
ATOM 1880 C CG  . GLU B 2 46  ? 272.634 256.777 324.710 1.00 51.10  ? 46  GLU G CG  1 
ATOM 1881 C CD  . GLU B 2 46  ? 272.305 257.260 326.099 1.00 52.62  ? 46  GLU G CD  1 
ATOM 1882 O OE1 . GLU B 2 46  ? 273.079 256.954 327.028 1.00 49.74  ? 46  GLU G OE1 1 
ATOM 1883 O OE2 . GLU B 2 46  ? 271.277 257.945 326.265 1.00 62.01  ? 46  GLU G OE2 1 
ATOM 1884 N N   . TRP B 2 47  ? 273.923 256.885 321.285 1.00 35.82  ? 47  TRP G N   1 
ATOM 1885 C CA  . TRP B 2 47  ? 274.019 258.064 320.431 1.00 50.72  ? 47  TRP G CA  1 
ATOM 1886 C C   . TRP B 2 47  ? 273.394 259.268 321.132 1.00 56.83  ? 47  TRP G C   1 
ATOM 1887 O O   . TRP B 2 47  ? 272.287 259.176 321.667 1.00 65.97  ? 47  TRP G O   1 
ATOM 1888 C CB  . TRP B 2 47  ? 273.329 257.779 319.097 1.00 67.40  ? 47  TRP G CB  1 
ATOM 1889 C CG  . TRP B 2 47  ? 273.144 258.945 318.172 1.00 53.87  ? 47  TRP G CG  1 
ATOM 1890 C CD1 . TRP B 2 47  ? 273.995 259.344 317.190 1.00 47.66  ? 47  TRP G CD1 1 
ATOM 1891 C CD2 . TRP B 2 47  ? 272.033 259.845 318.128 1.00 45.08  ? 47  TRP G CD2 1 
ATOM 1892 N NE1 . TRP B 2 47  ? 273.490 260.436 316.541 1.00 55.81  ? 47  TRP G NE1 1 
ATOM 1893 C CE2 . TRP B 2 47  ? 272.285 260.766 317.100 1.00 53.66  ? 47  TRP G CE2 1 
ATOM 1894 C CE3 . TRP B 2 47  ? 270.853 259.965 318.862 1.00 60.27  ? 47  TRP G CE3 1 
ATOM 1895 C CZ2 . TRP B 2 47  ? 271.402 261.791 316.788 1.00 53.89  ? 47  TRP G CZ2 1 
ATOM 1896 C CZ3 . TRP B 2 47  ? 269.986 260.985 318.554 1.00 62.08  ? 47  TRP G CZ3 1 
ATOM 1897 C CH2 . TRP B 2 47  ? 270.261 261.882 317.525 1.00 47.28  ? 47  TRP G CH2 1 
ATOM 1898 N N   . VAL B 2 48  ? 274.104 260.397 321.142 1.00 57.95  ? 48  VAL G N   1 
ATOM 1899 C CA  . VAL B 2 48  ? 273.630 261.585 321.846 1.00 47.24  ? 48  VAL G CA  1 
ATOM 1900 C C   . VAL B 2 48  ? 272.948 262.586 320.919 1.00 57.40  ? 48  VAL G C   1 
ATOM 1901 O O   . VAL B 2 48  ? 271.780 262.929 321.126 1.00 69.25  ? 48  VAL G O   1 
ATOM 1902 C CB  . VAL B 2 48  ? 274.788 262.253 322.611 1.00 47.05  ? 48  VAL G CB  1 
ATOM 1903 C CG1 . VAL B 2 48  ? 274.311 263.480 323.341 1.00 61.66  ? 48  VAL G CG1 1 
ATOM 1904 C CG2 . VAL B 2 48  ? 275.395 261.277 323.585 1.00 54.64  ? 48  VAL G CG2 1 
ATOM 1905 N N   . THR B 2 49  ? 273.657 263.063 319.896 1.00 45.36  ? 49  THR G N   1 
ATOM 1906 C CA  . THR B 2 49  ? 273.146 264.155 319.074 1.00 42.13  ? 49  THR G CA  1 
ATOM 1907 C C   . THR B 2 49  ? 273.833 264.161 317.716 1.00 46.56  ? 49  THR G C   1 
ATOM 1908 O O   . THR B 2 49  ? 274.854 263.506 317.507 1.00 62.30  ? 49  THR G O   1 
ATOM 1909 C CB  . THR B 2 49  ? 273.321 265.514 319.758 1.00 53.19  ? 49  THR G CB  1 
ATOM 1910 O OG1 . THR B 2 49  ? 272.906 266.551 318.864 1.00 64.37  ? 49  THR G OG1 1 
ATOM 1911 C CG2 . THR B 2 49  ? 274.758 265.749 320.143 1.00 57.87  ? 49  THR G CG2 1 
ATOM 1912 N N   . ILE B 2 50  ? 273.242 264.917 316.792 1.00 47.84  ? 50  ILE G N   1 
ATOM 1913 C CA  . ILE B 2 50  ? 273.766 265.156 315.451 1.00 45.40  ? 50  ILE G CA  1 
ATOM 1914 C C   . ILE B 2 50  ? 273.661 266.640 315.123 1.00 61.23  ? 50  ILE G C   1 
ATOM 1915 O O   . ILE B 2 50  ? 272.711 267.317 315.533 1.00 73.34  ? 50  ILE G O   1 
ATOM 1916 C CB  . ILE B 2 50  ? 273.019 264.322 314.375 1.00 41.15  ? 50  ILE G CB  1 
ATOM 1917 C CG1 . ILE B 2 50  ? 273.646 264.480 312.982 1.00 50.34  ? 50  ILE G CG1 1 
ATOM 1918 C CG2 . ILE B 2 50  ? 271.548 264.583 314.346 1.00 50.41  ? 50  ILE G CG2 1 
ATOM 1919 C CD1 . ILE B 2 50  ? 272.954 263.719 311.912 1.00 59.19  ? 50  ILE G CD1 1 
ATOM 1920 N N   . ILE B 2 51  ? 274.680 267.165 314.450 1.00 59.28  ? 51  ILE G N   1 
ATOM 1921 C CA  . ILE B 2 51  ? 274.632 268.488 313.851 1.00 51.46  ? 51  ILE G CA  1 
ATOM 1922 C C   . ILE B 2 51  ? 274.934 268.309 312.366 1.00 54.36  ? 51  ILE G C   1 
ATOM 1923 O O   . ILE B 2 51  ? 275.872 267.595 311.993 1.00 64.10  ? 51  ILE G O   1 
ATOM 1924 C CB  . ILE B 2 51  ? 275.567 269.499 314.553 1.00 49.47  ? 51  ILE G CB  1 
ATOM 1925 C CG1 . ILE B 2 51  ? 275.301 270.909 314.029 1.00 58.06  ? 51  ILE G CG1 1 
ATOM 1926 C CG2 . ILE B 2 51  ? 277.050 269.117 314.513 1.00 53.94  ? 51  ILE G CG2 1 
ATOM 1927 C CD1 . ILE B 2 51  ? 275.673 271.981 314.986 1.00 55.91  ? 51  ILE G CD1 1 
ATOM 1928 N N   . SER B 2 52  ? 274.077 268.868 311.522 1.00 64.03  ? 52  SER G N   1 
ATOM 1929 C CA  . SER B 2 52  ? 274.217 268.717 310.085 1.00 58.66  ? 52  SER G CA  1 
ATOM 1930 C C   . SER B 2 52  ? 275.347 269.597 309.560 1.00 66.83  ? 52  SER G C   1 
ATOM 1931 O O   . SER B 2 52  ? 275.906 270.428 310.278 1.00 74.37  ? 52  SER G O   1 
ATOM 1932 C CB  . SER B 2 52  ? 272.905 269.040 309.382 1.00 62.93  ? 52  SER G CB  1 
ATOM 1933 O OG  . SER B 2 52  ? 272.510 270.367 309.653 1.00 70.84  ? 52  SER G OG  1 
ATOM 1934 N N   . TYR B 2 53  ? 275.719 269.347 308.300 1.00 62.71  ? 53  TYR G N   1 
ATOM 1935 C CA  . TYR B 2 53  ? 276.788 270.100 307.647 1.00 63.17  ? 53  TYR G CA  1 
ATOM 1936 C C   . TYR B 2 53  ? 276.470 271.591 307.574 1.00 66.90  ? 53  TYR G C   1 
ATOM 1937 O O   . TYR B 2 53  ? 277.349 272.429 307.807 1.00 72.20  ? 53  TYR G O   1 
ATOM 1938 C CB  . TYR B 2 53  ? 277.075 269.481 306.269 1.00 70.40  ? 53  TYR G CB  1 
ATOM 1939 C CG  . TYR B 2 53  ? 276.062 269.727 305.167 1.00 69.43  ? 53  TYR G CG  1 
ATOM 1940 C CD1 . TYR B 2 53  ? 276.146 270.840 304.334 1.00 58.68  ? 53  TYR G CD1 1 
ATOM 1941 C CD2 . TYR B 2 53  ? 275.015 268.839 304.965 1.00 71.02  ? 53  TYR G CD2 1 
ATOM 1942 C CE1 . TYR B 2 53  ? 275.213 271.058 303.341 1.00 69.25  ? 53  TYR G CE1 1 
ATOM 1943 C CE2 . TYR B 2 53  ? 274.082 269.047 303.972 1.00 70.66  ? 53  TYR G CE2 1 
ATOM 1944 C CZ  . TYR B 2 53  ? 274.188 270.155 303.163 1.00 71.12  ? 53  TYR G CZ  1 
ATOM 1945 O OH  . TYR B 2 53  ? 273.261 270.366 302.171 1.00 64.81  ? 53  TYR G OH  1 
ATOM 1946 N N   . ASP B 2 54  ? 275.227 271.941 307.234 1.00 70.42  ? 54  ASP G N   1 
ATOM 1947 C CA  . ASP B 2 54  ? 274.810 273.339 307.255 1.00 73.12  ? 54  ASP G CA  1 
ATOM 1948 C C   . ASP B 2 54  ? 274.766 273.883 308.680 1.00 71.94  ? 54  ASP G C   1 
ATOM 1949 O O   . ASP B 2 54  ? 275.105 275.046 308.922 1.00 73.17  ? 54  ASP G O   1 
ATOM 1950 C CB  . ASP B 2 54  ? 273.469 273.502 306.532 1.00 77.35  ? 54  ASP G CB  1 
ATOM 1951 C CG  . ASP B 2 54  ? 272.422 272.484 306.961 1.00 70.19  ? 54  ASP G CG  1 
ATOM 1952 O OD1 . ASP B 2 54  ? 272.405 272.058 308.128 1.00 73.31  ? 54  ASP G OD1 1 
ATOM 1953 O OD2 . ASP B 2 54  ? 271.605 272.091 306.103 1.00 70.53  ? 54  ASP G OD2 1 
ATOM 1954 N N   . GLY B 2 55  ? 274.354 273.051 309.633 1.00 64.47  ? 55  GLY G N   1 
ATOM 1955 C CA  . GLY B 2 55  ? 274.270 273.425 311.026 1.00 68.28  ? 55  GLY G CA  1 
ATOM 1956 C C   . GLY B 2 55  ? 272.903 273.885 311.473 1.00 75.78  ? 55  GLY G C   1 
ATOM 1957 O O   . GLY B 2 55  ? 272.694 274.064 312.677 1.00 80.01  ? 55  GLY G O   1 
ATOM 1958 N N   . ILE B 2 56  ? 271.983 274.115 310.538 1.00 84.29  ? 56  ILE G N   1 
ATOM 1959 C CA  . ILE B 2 56  ? 270.612 274.464 310.896 1.00 84.99  ? 56  ILE G CA  1 
ATOM 1960 C C   . ILE B 2 56  ? 269.905 273.280 311.553 1.00 79.81  ? 56  ILE G C   1 
ATOM 1961 O O   . ILE B 2 56  ? 269.191 273.440 312.550 1.00 73.83  ? 56  ILE G O   1 
ATOM 1962 C CB  . ILE B 2 56  ? 269.861 274.963 309.647 1.00 85.43  ? 56  ILE G CB  1 
ATOM 1963 C CG1 . ILE B 2 56  ? 270.565 276.189 309.065 1.00 83.49  ? 56  ILE G CG1 1 
ATOM 1964 C CG2 . ILE B 2 56  ? 268.422 275.315 309.974 1.00 80.63  ? 56  ILE G CG2 1 
ATOM 1965 C CD1 . ILE B 2 56  ? 270.569 276.228 307.552 1.00 81.13  ? 56  ILE G CD1 1 
ATOM 1966 N N   . THR B 2 57  ? 270.117 272.074 311.027 1.00 79.65  ? 57  THR G N   1 
ATOM 1967 C CA  . THR B 2 57  ? 269.420 270.879 311.491 1.00 80.19  ? 57  THR G CA  1 
ATOM 1968 C C   . THR B 2 57  ? 270.173 270.225 312.644 1.00 79.32  ? 57  THR G C   1 
ATOM 1969 O O   . THR B 2 57  ? 271.338 269.848 312.495 1.00 82.05  ? 57  THR G O   1 
ATOM 1970 C CB  . THR B 2 57  ? 269.259 269.887 310.340 1.00 77.87  ? 57  THR G CB  1 
ATOM 1971 O OG1 . THR B 2 57  ? 268.597 270.527 309.243 1.00 82.02  ? 57  THR G OG1 1 
ATOM 1972 C CG2 . THR B 2 57  ? 268.443 268.693 310.780 1.00 77.80  ? 57  THR G CG2 1 
ATOM 1973 N N   . LYS B 2 58  ? 269.504 270.090 313.790 1.00 74.31  ? 58  LYS G N   1 
ATOM 1974 C CA  . LYS B 2 58  ? 270.059 269.437 314.968 1.00 64.56  ? 58  LYS G CA  1 
ATOM 1975 C C   . LYS B 2 58  ? 269.009 268.510 315.562 1.00 72.97  ? 58  LYS G C   1 
ATOM 1976 O O   . LYS B 2 58  ? 267.846 268.895 315.700 1.00 79.86  ? 58  LYS G O   1 
ATOM 1977 C CB  . LYS B 2 58  ? 270.490 270.458 316.032 1.00 66.59  ? 58  LYS G CB  1 
ATOM 1978 C CG  . LYS B 2 58  ? 271.495 271.497 315.570 1.00 68.92  ? 58  LYS G CG  1 
ATOM 1979 C CD  . LYS B 2 58  ? 271.492 272.697 316.490 1.00 71.52  ? 58  LYS G CD  1 
ATOM 1980 C CE  . LYS B 2 58  ? 272.409 273.788 315.978 1.00 69.29  ? 58  LYS G CE  1 
ATOM 1981 N NZ  . LYS B 2 58  ? 272.798 274.729 317.064 1.00 69.70  ? 58  LYS G NZ  1 
ATOM 1982 N N   . HIS B 2 59  ? 269.418 267.297 315.928 1.00 64.30  ? 59  HIS G N   1 
ATOM 1983 C CA  . HIS B 2 59  ? 268.522 266.307 316.512 1.00 65.68  ? 59  HIS G CA  1 
ATOM 1984 C C   . HIS B 2 59  ? 269.161 265.744 317.770 1.00 64.67  ? 59  HIS G C   1 
ATOM 1985 O O   . HIS B 2 59  ? 270.363 265.479 317.794 1.00 72.92  ? 59  HIS G O   1 
ATOM 1986 C CB  . HIS B 2 59  ? 268.198 265.166 315.548 1.00 69.89  ? 59  HIS G CB  1 
ATOM 1987 C CG  . HIS B 2 59  ? 267.495 265.601 314.302 1.00 80.89  ? 59  HIS G CG  1 
ATOM 1988 N ND1 . HIS B 2 59  ? 266.241 266.171 314.314 1.00 76.95  ? 59  HIS G ND1 1 
ATOM 1989 C CD2 . HIS B 2 59  ? 267.865 265.533 313.002 1.00 78.16  ? 59  HIS G CD2 1 
ATOM 1990 C CE1 . HIS B 2 59  ? 265.873 266.444 313.076 1.00 72.98  ? 59  HIS G CE1 1 
ATOM 1991 N NE2 . HIS B 2 59  ? 266.839 266.064 312.260 1.00 78.06  ? 59  HIS G NE2 1 
ATOM 1992 N N   . TYR B 2 60  ? 268.363 265.580 318.819 1.00 67.94  ? 60  TYR G N   1 
ATOM 1993 C CA  . TYR B 2 60  ? 268.856 265.102 320.102 1.00 69.90  ? 60  TYR G CA  1 
ATOM 1994 C C   . TYR B 2 60  ? 268.023 263.930 320.589 1.00 71.06  ? 60  TYR G C   1 
ATOM 1995 O O   . TYR B 2 60  ? 266.813 263.878 320.357 1.00 74.62  ? 60  TYR G O   1 
ATOM 1996 C CB  . TYR B 2 60  ? 268.811 266.196 321.180 1.00 72.02  ? 60  TYR G CB  1 
ATOM 1997 C CG  . TYR B 2 60  ? 269.441 267.512 320.805 1.00 66.53  ? 60  TYR G CG  1 
ATOM 1998 C CD1 . TYR B 2 60  ? 268.691 268.515 320.207 1.00 66.79  ? 60  TYR G CD1 1 
ATOM 1999 C CD2 . TYR B 2 60  ? 270.776 267.765 321.077 1.00 67.01  ? 60  TYR G CD2 1 
ATOM 2000 C CE1 . TYR B 2 60  ? 269.259 269.720 319.867 1.00 66.36  ? 60  TYR G CE1 1 
ATOM 2001 C CE2 . TYR B 2 60  ? 271.353 268.969 320.740 1.00 72.66  ? 60  TYR G CE2 1 
ATOM 2002 C CZ  . TYR B 2 60  ? 270.588 269.943 320.138 1.00 71.49  ? 60  TYR G CZ  1 
ATOM 2003 O OH  . TYR B 2 60  ? 271.151 271.150 319.800 1.00 72.83  ? 60  TYR G OH  1 
ATOM 2004 N N   . ALA B 2 61  ? 268.682 262.981 321.246 1.00 68.94  ? 61  ALA G N   1 
ATOM 2005 C CA  . ALA B 2 61  ? 267.973 261.894 321.900 1.00 72.81  ? 61  ALA G CA  1 
ATOM 2006 C C   . ALA B 2 61  ? 267.259 262.454 323.124 1.00 78.15  ? 61  ALA G C   1 
ATOM 2007 O O   . ALA B 2 61  ? 267.675 263.475 323.676 1.00 78.57  ? 61  ALA G O   1 
ATOM 2008 C CB  . ALA B 2 61  ? 268.938 260.783 322.301 1.00 73.65  ? 61  ALA G CB  1 
ATOM 2009 N N   . ASP B 2 62  ? 266.158 261.795 323.522 1.00 89.13  ? 62  ASP G N   1 
ATOM 2010 C CA  . ASP B 2 62  ? 265.309 262.299 324.607 1.00 92.33  ? 62  ASP G CA  1 
ATOM 2011 C C   . ASP B 2 62  ? 266.073 262.431 325.919 1.00 90.97  ? 62  ASP G C   1 
ATOM 2012 O O   . ASP B 2 62  ? 265.852 263.386 326.673 1.00 84.93  ? 62  ASP G O   1 
ATOM 2013 C CB  . ASP B 2 62  ? 264.084 261.406 324.790 1.00 90.82  ? 62  ASP G CB  1 
ATOM 2014 C CG  . ASP B 2 62  ? 263.171 261.421 323.584 1.00 93.98  ? 62  ASP G CG  1 
ATOM 2015 O OD1 . ASP B 2 62  ? 263.449 262.187 322.638 1.00 94.68  ? 62  ASP G OD1 1 
ATOM 2016 O OD2 . ASP B 2 62  ? 262.163 260.683 323.591 1.00 91.88  ? 62  ASP G OD2 1 
ATOM 2017 N N   . SER B 2 63  ? 266.944 261.459 326.226 1.00 87.66  ? 63  SER G N   1 
ATOM 2018 C CA  . SER B 2 63  ? 267.687 261.427 327.486 1.00 86.56  ? 63  SER G CA  1 
ATOM 2019 C C   . SER B 2 63  ? 268.592 262.646 327.674 1.00 85.07  ? 63  SER G C   1 
ATOM 2020 O O   . SER B 2 63  ? 269.008 262.927 328.803 1.00 90.18  ? 63  SER G O   1 
ATOM 2021 C CB  . SER B 2 63  ? 268.518 260.147 327.573 1.00 87.93  ? 63  SER G CB  1 
ATOM 2022 O OG  . SER B 2 63  ? 269.477 260.092 326.535 1.00 89.61  ? 63  SER G OG  1 
ATOM 2023 N N   . VAL B 2 64  ? 268.908 263.363 326.596 1.00 83.00  ? 64  VAL G N   1 
ATOM 2024 C CA  . VAL B 2 64  ? 269.681 264.598 326.662 1.00 87.49  ? 64  VAL G CA  1 
ATOM 2025 C C   . VAL B 2 64  ? 268.933 265.788 326.084 1.00 90.59  ? 64  VAL G C   1 
ATOM 2026 O O   . VAL B 2 64  ? 269.456 266.911 326.151 1.00 82.19  ? 64  VAL G O   1 
ATOM 2027 C CB  . VAL B 2 64  ? 271.041 264.454 325.946 1.00 79.98  ? 64  VAL G CB  1 
ATOM 2028 C CG1 . VAL B 2 64  ? 271.837 263.283 326.499 1.00 85.75  ? 64  VAL G CG1 1 
ATOM 2029 C CG2 . VAL B 2 64  ? 270.833 264.324 324.448 1.00 83.21  ? 64  VAL G CG2 1 
ATOM 2030 N N   . LYS B 2 65  ? 267.756 265.577 325.486 1.00 99.31  ? 65  LYS G N   1 
ATOM 2031 C CA  . LYS B 2 65  ? 266.996 266.651 324.848 1.00 93.41  ? 65  LYS G CA  1 
ATOM 2032 C C   . LYS B 2 65  ? 266.541 267.666 325.887 1.00 94.30  ? 65  LYS G C   1 
ATOM 2033 O O   . LYS B 2 65  ? 266.118 267.289 326.984 1.00 92.24  ? 65  LYS G O   1 
ATOM 2034 C CB  . LYS B 2 65  ? 265.792 266.078 324.101 1.00 91.86  ? 65  LYS G CB  1 
ATOM 2035 C CG  . LYS B 2 65  ? 265.064 267.070 323.219 1.00 94.08  ? 65  LYS G CG  1 
ATOM 2036 C CD  . LYS B 2 65  ? 263.677 266.562 322.865 1.00 97.68  ? 65  LYS G CD  1 
ATOM 2037 C CE  . LYS B 2 65  ? 262.883 267.612 322.104 1.00 96.67  ? 65  LYS G CE  1 
ATOM 2038 N NZ  . LYS B 2 65  ? 261.627 267.054 321.530 1.00 94.83  ? 65  LYS G NZ  1 
ATOM 2039 N N   . ASP B 2 66  ? 266.711 268.950 325.552 1.00 105.73 ? 66  ASP G N   1 
ATOM 2040 C CA  . ASP B 2 66  ? 266.379 270.189 326.279 1.00 102.22 ? 66  ASP G CA  1 
ATOM 2041 C C   . ASP B 2 66  ? 267.449 270.481 327.329 1.00 106.63 ? 66  ASP G C   1 
ATOM 2042 O O   . ASP B 2 66  ? 267.362 271.506 328.013 1.00 103.80 ? 66  ASP G O   1 
ATOM 2043 C CB  . ASP B 2 66  ? 264.983 270.218 326.931 1.00 101.24 ? 66  ASP G CB  1 
ATOM 2044 C CG  . ASP B 2 66  ? 263.893 269.695 326.011 1.00 105.12 ? 66  ASP G CG  1 
ATOM 2045 O OD1 . ASP B 2 66  ? 263.702 270.278 324.923 1.00 103.94 ? 66  ASP G OD1 1 
ATOM 2046 O OD2 . ASP B 2 66  ? 263.230 268.700 326.374 1.00 105.11 ? 66  ASP G OD2 1 
ATOM 2047 N N   . ARG B 2 67  ? 268.449 269.613 327.480 1.00 95.90  ? 67  ARG G N   1 
ATOM 2048 C CA  . ARG B 2 67  ? 269.571 269.816 328.383 1.00 91.71  ? 67  ARG G CA  1 
ATOM 2049 C C   . ARG B 2 67  ? 270.899 269.968 327.662 1.00 89.58  ? 67  ARG G C   1 
ATOM 2050 O O   . ARG B 2 67  ? 271.790 270.642 328.178 1.00 89.24  ? 67  ARG G O   1 
ATOM 2051 C CB  . ARG B 2 67  ? 269.689 268.656 329.379 1.00 88.69  ? 67  ARG G CB  1 
ATOM 2052 C CG  . ARG B 2 67  ? 268.390 268.233 330.035 1.00 88.75  ? 67  ARG G CG  1 
ATOM 2053 C CD  . ARG B 2 67  ? 268.577 267.191 331.153 1.00 92.47  ? 67  ARG G CD  1 
ATOM 2054 N NE  . ARG B 2 67  ? 269.234 265.954 330.738 1.00 90.47  ? 67  ARG G NE  1 
ATOM 2055 C CZ  . ARG B 2 67  ? 270.520 265.676 330.917 1.00 88.14  ? 67  ARG G CZ  1 
ATOM 2056 N NH1 . ARG B 2 67  ? 271.335 266.530 331.510 1.00 88.24  ? 67  ARG G NH1 1 
ATOM 2057 N NH2 . ARG B 2 67  ? 270.995 264.507 330.499 1.00 80.14  ? 67  ARG G NH2 1 
ATOM 2058 N N   . PHE B 2 68  ? 271.050 269.362 326.485 1.00 84.02  ? 68  PHE G N   1 
ATOM 2059 C CA  . PHE B 2 68  ? 272.297 269.383 325.729 1.00 78.60  ? 68  PHE G CA  1 
ATOM 2060 C C   . PHE B 2 68  ? 272.078 270.173 324.448 1.00 72.74  ? 68  PHE G C   1 
ATOM 2061 O O   . PHE B 2 68  ? 271.071 269.976 323.763 1.00 72.64  ? 68  PHE G O   1 
ATOM 2062 C CB  . PHE B 2 68  ? 272.776 267.970 325.358 1.00 79.35  ? 68  PHE G CB  1 
ATOM 2063 C CG  . PHE B 2 68  ? 273.422 267.178 326.484 1.00 80.04  ? 68  PHE G CG  1 
ATOM 2064 C CD1 . PHE B 2 68  ? 273.208 267.475 327.822 1.00 80.59  ? 68  PHE G CD1 1 
ATOM 2065 C CD2 . PHE B 2 68  ? 274.253 266.114 326.175 1.00 79.01  ? 68  PHE G CD2 1 
ATOM 2066 C CE1 . PHE B 2 68  ? 273.802 266.727 328.818 1.00 78.82  ? 68  PHE G CE1 1 
ATOM 2067 C CE2 . PHE B 2 68  ? 274.849 265.365 327.168 1.00 79.90  ? 68  PHE G CE2 1 
ATOM 2068 C CZ  . PHE B 2 68  ? 274.626 265.674 328.489 1.00 77.73  ? 68  PHE G CZ  1 
ATOM 2069 N N   . THR B 2 69  ? 273.008 271.072 324.134 1.00 71.36  ? 69  THR G N   1 
ATOM 2070 C CA  . THR B 2 69  ? 272.962 271.863 322.910 1.00 74.12  ? 69  THR G CA  1 
ATOM 2071 C C   . THR B 2 69  ? 274.200 271.579 322.069 1.00 75.67  ? 69  THR G C   1 
ATOM 2072 O O   . THR B 2 69  ? 275.325 271.658 322.571 1.00 80.83  ? 69  THR G O   1 
ATOM 2073 C CB  . THR B 2 69  ? 272.874 273.357 323.239 1.00 77.92  ? 69  THR G CB  1 
ATOM 2074 O OG1 . THR B 2 69  ? 271.718 273.599 324.050 1.00 80.68  ? 69  THR G OG1 1 
ATOM 2075 C CG2 . THR B 2 69  ? 272.772 274.188 321.971 1.00 72.75  ? 69  THR G CG2 1 
ATOM 2076 N N   . VAL B 2 70  ? 273.997 271.278 320.790 1.00 63.44  ? 70  VAL G N   1 
ATOM 2077 C CA  . VAL B 2 70  ? 275.087 270.981 319.866 1.00 64.77  ? 70  VAL G CA  1 
ATOM 2078 C C   . VAL B 2 70  ? 275.321 272.184 318.953 1.00 66.72  ? 70  VAL G C   1 
ATOM 2079 O O   . VAL B 2 70  ? 274.371 272.830 318.492 1.00 71.20  ? 70  VAL G O   1 
ATOM 2080 C CB  . VAL B 2 70  ? 274.833 269.663 319.100 1.00 53.20  ? 70  VAL G CB  1 
ATOM 2081 C CG1 . VAL B 2 70  ? 273.757 269.767 318.028 1.00 59.28  ? 70  VAL G CG1 1 
ATOM 2082 C CG2 . VAL B 2 70  ? 276.128 269.149 318.497 1.00 52.95  ? 70  VAL G CG2 1 
ATOM 2083 N N   . SER B 2 71  ? 276.586 272.570 318.806 1.00 57.02  ? 71  SER G N   1 
ATOM 2084 C CA  . SER B 2 71  ? 276.967 273.718 317.999 1.00 63.41  ? 71  SER G CA  1 
ATOM 2085 C C   . SER B 2 71  ? 278.273 273.411 317.279 1.00 56.66  ? 71  SER G C   1 
ATOM 2086 O O   . SER B 2 71  ? 279.010 272.501 317.659 1.00 59.78  ? 71  SER G O   1 
ATOM 2087 C CB  . SER B 2 71  ? 277.103 274.987 318.849 1.00 69.45  ? 71  SER G CB  1 
ATOM 2088 O OG  . SER B 2 71  ? 277.787 274.720 320.058 1.00 77.57  ? 71  SER G OG  1 
ATOM 2089 N N   . ARG B 2 72  ? 278.553 274.174 316.223 1.00 50.74  ? 72  ARG G N   1 
ATOM 2090 C CA  . ARG B 2 72  ? 279.804 274.005 315.499 1.00 48.97  ? 72  ARG G CA  1 
ATOM 2091 C C   . ARG B 2 72  ? 280.277 275.353 314.979 1.00 53.30  ? 72  ARG G C   1 
ATOM 2092 O O   . ARG B 2 72  ? 279.474 276.251 314.714 1.00 61.88  ? 72  ARG G O   1 
ATOM 2093 C CB  . ARG B 2 72  ? 279.668 273.022 314.327 1.00 53.41  ? 72  ARG G CB  1 
ATOM 2094 C CG  . ARG B 2 72  ? 278.674 273.432 313.249 1.00 55.39  ? 72  ARG G CG  1 
ATOM 2095 C CD  . ARG B 2 72  ? 278.386 272.288 312.300 1.00 54.49  ? 72  ARG G CD  1 
ATOM 2096 N NE  . ARG B 2 72  ? 279.444 272.095 311.318 1.00 55.25  ? 72  ARG G NE  1 
ATOM 2097 C CZ  . ARG B 2 72  ? 279.602 270.991 310.602 1.00 56.62  ? 72  ARG G CZ  1 
ATOM 2098 N NH1 . ARG B 2 72  ? 278.785 269.962 310.733 1.00 41.22  ? 72  ARG G NH1 1 
ATOM 2099 N NH2 . ARG B 2 72  ? 280.608 270.916 309.739 1.00 64.51  ? 72  ARG G NH2 1 
ATOM 2100 N N   . ASP B 2 73  ? 281.597 275.497 314.875 1.00 61.35  ? 73  ASP G N   1 
ATOM 2101 C CA  . ASP B 2 73  ? 282.233 276.659 314.261 1.00 69.50  ? 73  ASP G CA  1 
ATOM 2102 C C   . ASP B 2 73  ? 283.090 276.148 313.109 1.00 67.79  ? 73  ASP G C   1 
ATOM 2103 O O   . ASP B 2 73  ? 284.071 275.433 313.337 1.00 70.02  ? 73  ASP G O   1 
ATOM 2104 C CB  . ASP B 2 73  ? 283.070 277.430 315.283 1.00 77.79  ? 73  ASP G CB  1 
ATOM 2105 C CG  . ASP B 2 73  ? 283.326 278.874 314.875 1.00 76.46  ? 73  ASP G CG  1 
ATOM 2106 O OD1 . ASP B 2 73  ? 283.570 279.144 313.680 1.00 78.46  ? 73  ASP G OD1 1 
ATOM 2107 O OD2 . ASP B 2 73  ? 283.282 279.751 315.761 1.00 69.16  ? 73  ASP G OD2 1 
ATOM 2108 N N   . ASN B 2 74  ? 282.711 276.501 311.876 1.00 69.25  ? 74  ASN G N   1 
ATOM 2109 C CA  . ASN B 2 74  ? 283.435 276.022 310.700 1.00 75.09  ? 74  ASN G CA  1 
ATOM 2110 C C   . ASN B 2 74  ? 284.843 276.598 310.620 1.00 77.82  ? 74  ASN G C   1 
ATOM 2111 O O   . ASN B 2 74  ? 285.773 275.904 310.188 1.00 63.85  ? 74  ASN G O   1 
ATOM 2112 C CB  . ASN B 2 74  ? 282.655 276.335 309.425 1.00 70.87  ? 74  ASN G CB  1 
ATOM 2113 C CG  . ASN B 2 74  ? 281.376 275.538 309.318 1.00 73.38  ? 74  ASN G CG  1 
ATOM 2114 O OD1 . ASN B 2 74  ? 280.966 274.871 310.265 1.00 70.97  ? 74  ASN G OD1 1 
ATOM 2115 N ND2 . ASN B 2 74  ? 280.745 275.588 308.153 1.00 74.14  ? 74  ASN G ND2 1 
ATOM 2116 N N   . SER B 2 75  ? 285.005 277.878 310.979 1.00 91.21  ? 75  SER G N   1 
ATOM 2117 C CA  . SER B 2 75  ? 286.312 278.531 310.917 1.00 80.71  ? 75  SER G CA  1 
ATOM 2118 C C   . SER B 2 75  ? 287.310 277.884 311.869 1.00 80.49  ? 75  SER G C   1 
ATOM 2119 O O   . SER B 2 75  ? 288.485 277.710 311.525 1.00 79.63  ? 75  SER G O   1 
ATOM 2120 C CB  . SER B 2 75  ? 286.165 280.018 311.229 1.00 74.39  ? 75  SER G CB  1 
ATOM 2121 O OG  . SER B 2 75  ? 286.115 280.237 312.627 1.00 64.30  ? 75  SER G OG  1 
ATOM 2122 N N   . LYS B 2 76  ? 286.864 277.528 313.068 1.00 81.64  ? 76  LYS G N   1 
ATOM 2123 C CA  . LYS B 2 76  ? 287.725 276.906 314.061 1.00 80.65  ? 76  LYS G CA  1 
ATOM 2124 C C   . LYS B 2 76  ? 287.785 275.393 313.921 1.00 84.13  ? 76  LYS G C   1 
ATOM 2125 O O   . LYS B 2 76  ? 288.618 274.766 314.586 1.00 83.14  ? 76  LYS G O   1 
ATOM 2126 C CB  . LYS B 2 76  ? 287.249 277.261 315.470 1.00 77.33  ? 76  LYS G CB  1 
ATOM 2127 C CG  . LYS B 2 76  ? 287.087 278.743 315.724 1.00 81.85  ? 76  LYS G CG  1 
ATOM 2128 C CD  . LYS B 2 76  ? 286.523 278.988 317.108 1.00 77.71  ? 76  LYS G CD  1 
ATOM 2129 C CE  . LYS B 2 76  ? 286.619 280.450 317.502 1.00 78.70  ? 76  LYS G CE  1 
ATOM 2130 N NZ  . LYS B 2 76  ? 285.673 280.779 318.605 1.00 77.85  ? 76  LYS G NZ  1 
ATOM 2131 N N   . THR B 2 77  ? 286.938 274.817 313.054 1.00 73.77  ? 77  THR G N   1 
ATOM 2132 C CA  . THR B 2 77  ? 286.817 273.371 312.809 1.00 78.18  ? 77  THR G CA  1 
ATOM 2133 C C   . THR B 2 77  ? 286.569 272.598 314.102 1.00 73.65  ? 77  THR G C   1 
ATOM 2134 O O   . THR B 2 77  ? 287.177 271.558 314.356 1.00 80.00  ? 77  THR G O   1 
ATOM 2135 C CB  . THR B 2 77  ? 288.027 272.804 312.055 1.00 77.26  ? 77  THR G CB  1 
ATOM 2136 O OG1 . THR B 2 77  ? 289.191 272.843 312.888 1.00 69.88  ? 77  THR G OG1 1 
ATOM 2137 C CG2 . THR B 2 77  ? 288.285 273.601 310.789 1.00 76.24  ? 77  THR G CG2 1 
ATOM 2138 N N   . MET B 2 78  ? 285.672 273.119 314.934 1.00 67.45  ? 78  MET G N   1 
ATOM 2139 C CA  . MET B 2 78  ? 285.356 272.504 316.213 1.00 73.01  ? 78  MET G CA  1 
ATOM 2140 C C   . MET B 2 78  ? 283.852 272.359 316.391 1.00 73.19  ? 78  MET G C   1 
ATOM 2141 O O   . MET B 2 78  ? 283.087 273.272 316.071 1.00 85.01  ? 78  MET G O   1 
ATOM 2142 C CB  . MET B 2 78  ? 285.936 273.302 317.389 1.00 73.38  ? 78  MET G CB  1 
ATOM 2143 C CG  . MET B 2 78  ? 287.356 272.906 317.755 1.00 76.19  ? 78  MET G CG  1 
ATOM 2144 S SD  . MET B 2 78  ? 287.995 273.756 319.207 1.00 75.25  ? 78  MET G SD  1 
ATOM 2145 C CE  . MET B 2 78  ? 287.966 275.456 318.661 1.00 77.05  ? 78  MET G CE  1 
ATOM 2146 N N   . VAL B 2 79  ? 283.441 271.201 316.903 1.00 52.75  ? 79  VAL G N   1 
ATOM 2147 C CA  . VAL B 2 79  ? 282.054 270.911 317.246 1.00 58.24  ? 79  VAL G CA  1 
ATOM 2148 C C   . VAL B 2 79  ? 281.954 270.918 318.760 1.00 53.61  ? 79  VAL G C   1 
ATOM 2149 O O   . VAL B 2 79  ? 282.733 270.242 319.439 1.00 67.92  ? 79  VAL G O   1 
ATOM 2150 C CB  . VAL B 2 79  ? 281.594 269.552 316.689 1.00 57.72  ? 79  VAL G CB  1 
ATOM 2151 C CG1 . VAL B 2 79  ? 280.139 269.301 317.028 1.00 61.98  ? 79  VAL G CG1 1 
ATOM 2152 C CG2 . VAL B 2 79  ? 281.790 269.485 315.206 1.00 56.75  ? 79  VAL G CG2 1 
ATOM 2153 N N   . TYR B 2 80  ? 281.015 271.690 319.290 1.00 60.25  ? 80  TYR G N   1 
ATOM 2154 C CA  . TYR B 2 80  ? 280.861 271.850 320.727 1.00 68.31  ? 80  TYR G CA  1 
ATOM 2155 C C   . TYR B 2 80  ? 279.574 271.182 321.180 1.00 64.54  ? 80  TYR G C   1 
ATOM 2156 O O   . TYR B 2 80  ? 278.500 271.473 320.649 1.00 70.44  ? 80  TYR G O   1 
ATOM 2157 C CB  . TYR B 2 80  ? 280.873 273.323 321.132 1.00 63.19  ? 80  TYR G CB  1 
ATOM 2158 C CG  . TYR B 2 80  ? 281.848 274.168 320.354 1.00 55.37  ? 80  TYR G CG  1 
ATOM 2159 C CD1 . TYR B 2 80  ? 283.182 274.230 320.727 1.00 68.57  ? 80  TYR G CD1 1 
ATOM 2160 C CD2 . TYR B 2 80  ? 281.434 274.921 319.265 1.00 66.07  ? 80  TYR G CD2 1 
ATOM 2161 C CE1 . TYR B 2 80  ? 284.080 275.002 320.031 1.00 72.40  ? 80  TYR G CE1 1 
ATOM 2162 C CE2 . TYR B 2 80  ? 282.327 275.697 318.559 1.00 69.81  ? 80  TYR G CE2 1 
ATOM 2163 C CZ  . TYR B 2 80  ? 283.649 275.734 318.949 1.00 73.15  ? 80  TYR G CZ  1 
ATOM 2164 O OH  . TYR B 2 80  ? 284.546 276.506 318.250 1.00 80.89  ? 80  TYR G OH  1 
ATOM 2165 N N   . LEU B 2 81  ? 279.689 270.273 322.137 1.00 53.42  ? 81  LEU G N   1 
ATOM 2166 C CA  . LEU B 2 81  ? 278.530 269.677 322.790 1.00 56.07  ? 81  LEU G CA  1 
ATOM 2167 C C   . LEU B 2 81  ? 278.371 270.395 324.125 1.00 67.04  ? 81  LEU G C   1 
ATOM 2168 O O   . LEU B 2 81  ? 279.044 270.062 325.103 1.00 75.07  ? 81  LEU G O   1 
ATOM 2169 C CB  . LEU B 2 81  ? 278.704 268.174 322.980 1.00 60.21  ? 81  LEU G CB  1 
ATOM 2170 C CG  . LEU B 2 81  ? 277.611 267.428 323.753 1.00 58.98  ? 81  LEU G CG  1 
ATOM 2171 C CD1 . LEU B 2 81  ? 276.236 267.717 323.174 1.00 64.74  ? 81  LEU G CD1 1 
ATOM 2172 C CD2 . LEU B 2 81  ? 277.879 265.943 323.788 1.00 66.97  ? 81  LEU G CD2 1 
ATOM 2173 N N   . GLN B 2 82  ? 277.517 271.411 324.157 1.00 70.12  ? 82  GLN G N   1 
ATOM 2174 C CA  . GLN B 2 82  ? 277.216 272.063 325.421 1.00 69.64  ? 82  GLN G CA  1 
ATOM 2175 C C   . GLN B 2 82  ? 276.332 271.136 326.239 1.00 69.08  ? 82  GLN G C   1 
ATOM 2176 O O   . GLN B 2 82  ? 275.349 270.599 325.728 1.00 68.15  ? 82  GLN G O   1 
ATOM 2177 C CB  . GLN B 2 82  ? 276.522 273.402 325.179 1.00 76.54  ? 82  GLN G CB  1 
ATOM 2178 C CG  . GLN B 2 82  ? 276.168 274.176 326.437 1.00 75.64  ? 82  GLN G CG  1 
ATOM 2179 C CD  . GLN B 2 82  ? 277.384 274.562 327.250 1.00 75.18  ? 82  GLN G CD  1 
ATOM 2180 O OE1 . GLN B 2 82  ? 278.215 275.353 326.807 1.00 70.26  ? 82  GLN G OE1 1 
ATOM 2181 N NE2 . GLN B 2 82  ? 277.491 274.013 328.452 1.00 80.60  ? 82  GLN G NE2 1 
ATOM 2182 N N   . MET B 2 83  ? 276.673 270.946 327.507 1.00 73.05  ? 83  MET G N   1 
ATOM 2183 C CA  . MET B 2 83  ? 275.915 270.074 328.391 1.00 78.58  ? 83  MET G CA  1 
ATOM 2184 C C   . MET B 2 83  ? 275.495 270.860 329.619 1.00 76.80  ? 83  MET G C   1 
ATOM 2185 O O   . MET B 2 83  ? 276.330 271.499 330.260 1.00 82.36  ? 83  MET G O   1 
ATOM 2186 C CB  . MET B 2 83  ? 276.742 268.854 328.809 1.00 80.33  ? 83  MET G CB  1 
ATOM 2187 C CG  . MET B 2 83  ? 277.327 268.054 327.658 1.00 73.83  ? 83  MET G CG  1 
ATOM 2188 S SD  . MET B 2 83  ? 278.144 266.545 328.200 1.00 69.25  ? 83  MET G SD  1 
ATOM 2189 C CE  . MET B 2 83  ? 279.537 267.219 329.085 1.00 83.46  ? 83  MET G CE  1 
ATOM 2190 N N   . ASN B 2 84  ? 274.208 270.804 329.946 1.00 78.72  ? 84  ASN G N   1 
ATOM 2191 C CA  . ASN B 2 84  ? 273.641 271.526 331.075 1.00 80.74  ? 84  ASN G CA  1 
ATOM 2192 C C   . ASN B 2 84  ? 272.728 270.582 331.836 1.00 87.23  ? 84  ASN G C   1 
ATOM 2193 O O   . ASN B 2 84  ? 272.246 269.591 331.281 1.00 90.34  ? 84  ASN G O   1 
ATOM 2194 C CB  . ASN B 2 84  ? 272.841 272.768 330.641 1.00 83.37  ? 84  ASN G CB  1 
ATOM 2195 C CG  . ASN B 2 84  ? 273.514 273.555 329.531 1.00 87.95  ? 84  ASN G CG  1 
ATOM 2196 O OD1 . ASN B 2 84  ? 274.703 273.861 329.602 1.00 84.35  ? 84  ASN G OD1 1 
ATOM 2197 N ND2 . ASN B 2 84  ? 272.754 273.878 328.493 1.00 92.15  ? 84  ASN G ND2 1 
ATOM 2198 N N   . ASN B 2 85  ? 272.494 270.921 333.110 1.00 98.09  ? 85  ASN G N   1 
ATOM 2199 C CA  . ASN B 2 85  ? 271.703 270.119 334.054 1.00 99.43  ? 85  ASN G CA  1 
ATOM 2200 C C   . ASN B 2 85  ? 272.250 268.693 334.142 1.00 100.18 ? 85  ASN G C   1 
ATOM 2201 O O   . ASN B 2 85  ? 271.520 267.706 334.016 1.00 98.23  ? 85  ASN G O   1 
ATOM 2202 C CB  . ASN B 2 85  ? 270.211 270.141 333.699 1.00 97.70  ? 85  ASN G CB  1 
ATOM 2203 C CG  . ASN B 2 85  ? 269.330 269.645 334.832 1.00 96.16  ? 85  ASN G CG  1 
ATOM 2204 O OD1 . ASN B 2 85  ? 269.171 270.318 335.849 1.00 98.21  ? 85  ASN G OD1 1 
ATOM 2205 N ND2 . ASN B 2 85  ? 268.763 268.456 334.664 1.00 96.63  ? 85  ASN G ND2 1 
ATOM 2206 N N   . LEU B 2 86  ? 273.573 268.603 334.272 1.00 93.72  ? 86  LEU G N   1 
ATOM 2207 C CA  . LEU B 2 86  ? 274.265 267.321 334.295 1.00 92.49  ? 86  LEU G CA  1 
ATOM 2208 C C   . LEU B 2 86  ? 273.844 266.476 335.491 1.00 94.88  ? 86  LEU G C   1 
ATOM 2209 O O   . LEU B 2 86  ? 273.507 266.986 336.562 1.00 95.11  ? 86  LEU G O   1 
ATOM 2210 C CB  . LEU B 2 86  ? 275.775 267.539 334.284 1.00 90.42  ? 86  LEU G CB  1 
ATOM 2211 C CG  . LEU B 2 86  ? 276.260 268.014 332.914 1.00 87.38  ? 86  LEU G CG  1 
ATOM 2212 C CD1 . LEU B 2 86  ? 277.694 268.479 332.939 1.00 83.45  ? 86  LEU G CD1 1 
ATOM 2213 C CD2 . LEU B 2 86  ? 276.103 266.882 331.923 1.00 93.86  ? 86  LEU G CD2 1 
ATOM 2214 N N   . LYS B 2 87  ? 273.863 265.163 335.284 1.00 88.07  ? 87  LYS G N   1 
ATOM 2215 C CA  . LYS B 2 87  ? 273.385 264.184 336.241 1.00 84.02  ? 87  LYS G CA  1 
ATOM 2216 C C   . LYS B 2 87  ? 274.426 263.088 336.388 1.00 87.99  ? 87  LYS G C   1 
ATOM 2217 O O   . LYS B 2 87  ? 275.338 262.971 335.570 1.00 88.43  ? 87  LYS G O   1 
ATOM 2218 C CB  . LYS B 2 87  ? 272.054 263.573 335.770 1.00 83.73  ? 87  LYS G CB  1 
ATOM 2219 C CG  . LYS B 2 87  ? 270.888 264.536 335.800 1.00 84.23  ? 87  LYS G CG  1 
ATOM 2220 C CD  . LYS B 2 87  ? 269.576 263.938 335.292 1.00 88.65  ? 87  LYS G CD  1 
ATOM 2221 C CE  . LYS B 2 87  ? 269.185 264.466 333.926 1.00 88.19  ? 87  LYS G CE  1 
ATOM 2222 N NZ  . LYS B 2 87  ? 268.364 263.511 333.130 1.00 90.86  ? 87  LYS G NZ  1 
ATOM 2223 N N   . LEU B 2 88  ? 274.300 262.308 337.469 1.00 88.80  ? 88  LEU G N   1 
ATOM 2224 C CA  . LEU B 2 88  ? 275.199 261.178 337.700 1.00 84.56  ? 88  LEU G CA  1 
ATOM 2225 C C   . LEU B 2 88  ? 275.109 260.154 336.576 1.00 89.82  ? 88  LEU G C   1 
ATOM 2226 O O   . LEU B 2 88  ? 276.109 259.509 336.240 1.00 99.55  ? 88  LEU G O   1 
ATOM 2227 C CB  . LEU B 2 88  ? 274.886 260.519 339.042 1.00 80.14  ? 88  LEU G CB  1 
ATOM 2228 C CG  . LEU B 2 88  ? 275.010 261.385 340.295 1.00 82.85  ? 88  LEU G CG  1 
ATOM 2229 C CD1 . LEU B 2 88  ? 274.639 260.579 341.524 1.00 85.47  ? 88  LEU G CD1 1 
ATOM 2230 C CD2 . LEU B 2 88  ? 276.408 261.942 340.426 1.00 86.83  ? 88  LEU G CD2 1 
ATOM 2231 N N   . ASP B 2 89  ? 273.909 259.977 336.014 1.00 84.91  ? 89  ASP G N   1 
ATOM 2232 C CA  . ASP B 2 89  ? 273.694 259.087 334.878 1.00 73.08  ? 89  ASP G CA  1 
ATOM 2233 C C   . ASP B 2 89  ? 274.475 259.537 333.648 1.00 80.01  ? 89  ASP G C   1 
ATOM 2234 O O   . ASP B 2 89  ? 274.889 258.700 332.839 1.00 80.58  ? 89  ASP G O   1 
ATOM 2235 C CB  . ASP B 2 89  ? 272.203 259.010 334.559 1.00 83.68  ? 89  ASP G CB  1 
ATOM 2236 C CG  . ASP B 2 89  ? 271.412 258.304 335.643 1.00 89.72  ? 89  ASP G CG  1 
ATOM 2237 O OD1 . ASP B 2 89  ? 271.141 258.933 336.689 1.00 87.65  ? 89  ASP G OD1 1 
ATOM 2238 O OD2 . ASP B 2 89  ? 271.058 257.123 335.451 1.00 93.16  ? 89  ASP G OD2 1 
ATOM 2239 N N   . ASP B 2 90  ? 274.637 260.854 333.468 1.00 79.31  ? 90  ASP G N   1 
ATOM 2240 C CA  . ASP B 2 90  ? 275.310 261.419 332.300 1.00 83.65  ? 90  ASP G CA  1 
ATOM 2241 C C   . ASP B 2 90  ? 276.777 261.019 332.181 1.00 85.32  ? 90  ASP G C   1 
ATOM 2242 O O   . ASP B 2 90  ? 277.339 261.176 331.092 1.00 93.63  ? 90  ASP G O   1 
ATOM 2243 C CB  . ASP B 2 90  ? 275.202 262.943 332.311 1.00 78.38  ? 90  ASP G CB  1 
ATOM 2244 C CG  . ASP B 2 90  ? 273.775 263.424 332.176 1.00 84.34  ? 90  ASP G CG  1 
ATOM 2245 O OD1 . ASP B 2 90  ? 272.861 262.577 332.180 1.00 88.09  ? 90  ASP G OD1 1 
ATOM 2246 O OD2 . ASP B 2 90  ? 273.565 264.649 332.073 1.00 86.15  ? 90  ASP G OD2 1 
ATOM 2247 N N   . THR B 2 91  ? 277.424 260.622 333.287 1.00 72.69  ? 91  THR G N   1 
ATOM 2248 C CA  . THR B 2 91  ? 278.833 260.221 333.310 1.00 66.47  ? 91  THR G CA  1 
ATOM 2249 C C   . THR B 2 91  ? 279.115 259.133 332.285 1.00 56.82  ? 91  THR G C   1 
ATOM 2250 O O   . THR B 2 91  ? 278.555 258.036 332.373 1.00 78.84  ? 91  THR G O   1 
ATOM 2251 C CB  . THR B 2 91  ? 279.198 259.723 334.709 1.00 71.20  ? 91  THR G CB  1 
ATOM 2252 O OG1 . THR B 2 91  ? 279.014 260.777 335.661 1.00 72.13  ? 91  THR G OG1 1 
ATOM 2253 C CG2 . THR B 2 91  ? 280.639 259.247 334.757 1.00 74.27  ? 91  THR G CG2 1 
ATOM 2254 N N   . ALA B 2 92  ? 280.034 259.418 331.364 1.00 43.50  ? 92  ALA G N   1 
ATOM 2255 C CA  . ALA B 2 92  ? 280.334 258.536 330.242 1.00 55.52  ? 92  ALA G CA  1 
ATOM 2256 C C   . ALA B 2 92  ? 281.563 259.049 329.510 1.00 48.47  ? 92  ALA G C   1 
ATOM 2257 O O   . ALA B 2 92  ? 282.053 260.149 329.770 1.00 66.66  ? 92  ALA G O   1 
ATOM 2258 C CB  . ALA B 2 92  ? 279.162 258.461 329.260 1.00 63.35  ? 92  ALA G CB  1 
ATOM 2259 N N   . VAL B 2 93  ? 282.061 258.226 328.594 1.00 37.45  ? 93  VAL G N   1 
ATOM 2260 C CA  . VAL B 2 93  ? 283.115 258.624 327.669 1.00 47.32  ? 93  VAL G CA  1 
ATOM 2261 C C   . VAL B 2 93  ? 282.424 259.114 326.408 1.00 37.14  ? 93  VAL G C   1 
ATOM 2262 O O   . VAL B 2 93  ? 281.708 258.353 325.754 1.00 31.39  ? 93  VAL G O   1 
ATOM 2263 C CB  . VAL B 2 93  ? 284.066 257.461 327.357 1.00 51.34  ? 93  VAL G CB  1 
ATOM 2264 C CG1 . VAL B 2 93  ? 284.995 257.832 326.230 1.00 56.23  ? 93  VAL G CG1 1 
ATOM 2265 C CG2 . VAL B 2 93  ? 284.855 257.067 328.585 1.00 53.63  ? 93  VAL G CG2 1 
ATOM 2266 N N   . TYR B 2 94  ? 282.622 260.382 326.070 1.00 54.67  ? 94  TYR G N   1 
ATOM 2267 C CA  . TYR B 2 94  ? 281.931 261.007 324.950 1.00 51.02  ? 94  TYR G CA  1 
ATOM 2268 C C   . TYR B 2 94  ? 282.820 260.984 323.717 1.00 50.87  ? 94  TYR G C   1 
ATOM 2269 O O   . TYR B 2 94  ? 283.915 261.553 323.724 1.00 62.36  ? 94  TYR G O   1 
ATOM 2270 C CB  . TYR B 2 94  ? 281.519 262.438 325.291 1.00 43.44  ? 94  TYR G CB  1 
ATOM 2271 C CG  . TYR B 2 94  ? 280.310 262.514 326.188 1.00 51.71  ? 94  TYR G CG  1 
ATOM 2272 C CD1 . TYR B 2 94  ? 280.417 262.277 327.552 1.00 51.77  ? 94  TYR G CD1 1 
ATOM 2273 C CD2 . TYR B 2 94  ? 279.057 262.791 325.668 1.00 55.44  ? 94  TYR G CD2 1 
ATOM 2274 C CE1 . TYR B 2 94  ? 279.316 262.329 328.373 1.00 49.38  ? 94  TYR G CE1 1 
ATOM 2275 C CE2 . TYR B 2 94  ? 277.950 262.850 326.482 1.00 62.89  ? 94  TYR G CE2 1 
ATOM 2276 C CZ  . TYR B 2 94  ? 278.087 262.614 327.834 1.00 60.22  ? 94  TYR G CZ  1 
ATOM 2277 O OH  . TYR B 2 94  ? 276.988 262.670 328.654 1.00 63.33  ? 94  TYR G OH  1 
ATOM 2278 N N   . TYR B 2 95  ? 282.346 260.336 322.662 1.00 43.61  ? 95  TYR G N   1 
ATOM 2279 C CA  . TYR B 2 95  ? 283.069 260.244 321.404 1.00 46.61  ? 95  TYR G CA  1 
ATOM 2280 C C   . TYR B 2 95  ? 282.399 261.126 320.365 1.00 45.56  ? 95  TYR G C   1 
ATOM 2281 O O   . TYR B 2 95  ? 281.174 261.122 320.234 1.00 36.71  ? 95  TYR G O   1 
ATOM 2282 C CB  . TYR B 2 95  ? 283.135 258.815 320.864 1.00 46.96  ? 95  TYR G CB  1 
ATOM 2283 C CG  . TYR B 2 95  ? 283.424 257.703 321.840 1.00 43.90  ? 95  TYR G CG  1 
ATOM 2284 C CD1 . TYR B 2 95  ? 282.399 257.043 322.494 1.00 52.93  ? 95  TYR G CD1 1 
ATOM 2285 C CD2 . TYR B 2 95  ? 284.724 257.278 322.062 1.00 48.62  ? 95  TYR G CD2 1 
ATOM 2286 C CE1 . TYR B 2 95  ? 282.663 256.017 323.370 1.00 53.75  ? 95  TYR G CE1 1 
ATOM 2287 C CE2 . TYR B 2 95  ? 284.997 256.254 322.935 1.00 47.50  ? 95  TYR G CE2 1 
ATOM 2288 C CZ  . TYR B 2 95  ? 283.965 255.627 323.586 1.00 43.57  ? 95  TYR G CZ  1 
ATOM 2289 O OH  . TYR B 2 95  ? 284.237 254.603 324.460 1.00 57.69  ? 95  TYR G OH  1 
ATOM 2290 N N   . CYS B 2 96  ? 283.209 261.872 319.633 1.00 46.05  ? 96  CYS G N   1 
ATOM 2291 C CA  . CYS B 2 96  ? 282.755 262.699 318.529 1.00 54.22  ? 96  CYS G CA  1 
ATOM 2292 C C   . CYS B 2 96  ? 282.992 261.949 317.230 1.00 61.06  ? 96  CYS G C   1 
ATOM 2293 O O   . CYS B 2 96  ? 284.111 261.505 316.962 1.00 80.13  ? 96  CYS G O   1 
ATOM 2294 C CB  . CYS B 2 96  ? 283.510 264.022 318.532 1.00 60.65  ? 96  CYS G CB  1 
ATOM 2295 S SG  . CYS B 2 96  ? 283.221 265.156 317.191 1.00 64.41  ? 96  CYS G SG  1 
ATOM 2296 N N   . ALA B 2 97  ? 281.946 261.809 316.429 1.00 34.42  ? 97  ALA G N   1 
ATOM 2297 C CA  . ALA B 2 97  ? 282.037 261.054 315.197 1.00 31.96  ? 97  ALA G CA  1 
ATOM 2298 C C   . ALA B 2 97  ? 281.590 261.899 314.017 1.00 52.94  ? 97  ALA G C   1 
ATOM 2299 O O   . ALA B 2 97  ? 280.817 262.846 314.156 1.00 50.36  ? 97  ALA G O   1 
ATOM 2300 C CB  . ALA B 2 97  ? 281.199 259.781 315.265 1.00 48.94  ? 97  ALA G CB  1 
ATOM 2301 N N   . ARG B 2 98  ? 282.089 261.532 312.848 1.00 60.30  ? 98  ARG G N   1 
ATOM 2302 C CA  . ARG B 2 98  ? 281.735 262.161 311.587 1.00 42.80  ? 98  ARG G CA  1 
ATOM 2303 C C   . ARG B 2 98  ? 280.996 261.146 310.731 1.00 47.85  ? 98  ARG G C   1 
ATOM 2304 O O   . ARG B 2 98  ? 281.584 260.125 310.377 1.00 56.27  ? 98  ARG G O   1 
ATOM 2305 C CB  . ARG B 2 98  ? 283.003 262.635 310.881 1.00 37.38  ? 98  ARG G CB  1 
ATOM 2306 C CG  . ARG B 2 98  ? 282.782 263.285 309.552 1.00 39.03  ? 98  ARG G CG  1 
ATOM 2307 C CD  . ARG B 2 98  ? 284.082 263.445 308.786 1.00 55.05  ? 98  ARG G CD  1 
ATOM 2308 N NE  . ARG B 2 98  ? 284.522 262.202 308.168 1.00 48.78  ? 98  ARG G NE  1 
ATOM 2309 C CZ  . ARG B 2 98  ? 285.355 262.129 307.140 1.00 44.91  ? 98  ARG G CZ  1 
ATOM 2310 N NH1 . ARG B 2 98  ? 285.858 263.214 306.581 1.00 54.64  ? 98  ARG G NH1 1 
ATOM 2311 N NH2 . ARG B 2 98  ? 285.695 260.938 306.663 1.00 48.28  ? 98  ARG G NH2 1 
ATOM 2312 N N   . ASP B 2 99  ? 279.747 261.453 310.359 1.00 46.01  ? 99  ASP G N   1 
ATOM 2313 C CA  . ASP B 2 99  ? 278.912 260.652 309.443 1.00 49.03  ? 99  ASP G CA  1 
ATOM 2314 C C   . ASP B 2 99  ? 278.843 259.172 309.832 1.00 51.10  ? 99  ASP G C   1 
ATOM 2315 O O   . ASP B 2 99  ? 279.388 258.307 309.152 1.00 58.45  ? 99  ASP G O   1 
ATOM 2316 C CB  . ASP B 2 99  ? 279.375 260.796 307.995 1.00 57.28  ? 99  ASP G CB  1 
ATOM 2317 C CG  . ASP B 2 99  ? 279.458 262.223 307.561 1.00 63.75  ? 99  ASP G CG  1 
ATOM 2318 O OD1 . ASP B 2 99  ? 278.508 262.978 307.844 1.00 58.06  ? 99  ASP G OD1 1 
ATOM 2319 O OD2 . ASP B 2 99  ? 280.460 262.587 306.925 1.00 57.88  ? 99  ASP G OD2 1 
ATOM 2320 N N   . LEU B 2 100 ? 278.221 258.933 310.987 1.00 62.85  ? 100 LEU G N   1 
ATOM 2321 C CA  . LEU B 2 100 ? 278.076 257.593 311.545 1.00 42.75  ? 100 LEU G CA  1 
ATOM 2322 C C   . LEU B 2 100 ? 277.419 256.610 310.591 1.00 39.93  ? 100 LEU G C   1 
ATOM 2323 O O   . LEU B 2 100 ? 276.430 256.926 309.927 1.00 26.74  ? 100 LEU G O   1 
ATOM 2324 C CB  . LEU B 2 100 ? 277.233 257.629 312.813 1.00 50.59  ? 100 LEU G CB  1 
ATOM 2325 C CG  . LEU B 2 100 ? 277.943 258.046 314.071 1.00 44.59  ? 100 LEU G CG  1 
ATOM 2326 C CD1 . LEU B 2 100 ? 276.944 258.117 315.186 1.00 49.70  ? 100 LEU G CD1 1 
ATOM 2327 C CD2 . LEU B 2 100 ? 278.940 257.004 314.302 1.00 54.98  ? 100 LEU G CD2 1 
ATOM 2328 N N   . GLY B 2 101 ? 277.971 255.399 310.568 1.00 47.71  ? 101 GLY G N   1 
ATOM 2329 C CA  . GLY B 2 101 ? 277.441 254.303 309.785 1.00 47.96  ? 101 GLY G CA  1 
ATOM 2330 C C   . GLY B 2 101 ? 277.434 254.524 308.296 1.00 57.13  ? 101 GLY G C   1 
ATOM 2331 O O   . GLY B 2 101 ? 276.540 254.029 307.603 1.00 61.07  ? 101 GLY G O   1 
ATOM 2332 N N   . THR B 2 102 ? 278.423 255.240 307.781 1.00 52.37  ? 102 THR G N   1 
ATOM 2333 C CA  . THR B 2 102 ? 278.565 255.507 306.362 1.00 48.64  ? 102 THR G CA  1 
ATOM 2334 C C   . THR B 2 102 ? 280.017 255.277 305.994 1.00 46.88  ? 102 THR G C   1 
ATOM 2335 O O   . THR B 2 102 ? 280.854 254.977 306.843 1.00 49.95  ? 102 THR G O   1 
ATOM 2336 C CB  . THR B 2 102 ? 278.175 256.947 305.958 1.00 48.43  ? 102 THR G CB  1 
ATOM 2337 O OG1 . THR B 2 102 ? 279.266 257.833 306.224 1.00 53.04  ? 102 THR G OG1 1 
ATOM 2338 C CG2 . THR B 2 102 ? 276.923 257.468 306.657 1.00 56.07  ? 102 THR G CG2 1 
ATOM 2339 N N   . TYR B 2 103 ? 280.295 255.355 304.697 1.00 49.52  ? 103 TYR G N   1 
ATOM 2340 C CA  . TYR B 2 103 ? 281.665 255.300 304.208 1.00 46.62  ? 103 TYR G CA  1 
ATOM 2341 C C   . TYR B 2 103 ? 282.540 256.440 304.731 1.00 64.47  ? 103 TYR G C   1 
ATOM 2342 O O   . TYR B 2 103 ? 283.763 256.282 304.791 1.00 55.21  ? 103 TYR G O   1 
ATOM 2343 C CB  . TYR B 2 103 ? 281.635 255.192 302.682 1.00 46.49  ? 103 TYR G CB  1 
ATOM 2344 C CG  . TYR B 2 103 ? 280.821 256.253 301.989 1.00 52.40  ? 103 TYR G CG  1 
ATOM 2345 C CD1 . TYR B 2 103 ? 281.302 257.524 301.762 1.00 62.85  ? 103 TYR G CD1 1 
ATOM 2346 C CD2 . TYR B 2 103 ? 279.577 255.932 301.477 1.00 56.84  ? 103 TYR G CD2 1 
ATOM 2347 C CE1 . TYR B 2 103 ? 280.526 258.468 301.118 1.00 55.87  ? 103 TYR G CE1 1 
ATOM 2348 C CE2 . TYR B 2 103 ? 278.816 256.858 300.816 1.00 62.06  ? 103 TYR G CE2 1 
ATOM 2349 C CZ  . TYR B 2 103 ? 279.294 258.122 300.635 1.00 53.94  ? 103 TYR G CZ  1 
ATOM 2350 O OH  . TYR B 2 103 ? 278.527 259.052 299.980 1.00 65.22  ? 103 TYR G OH  1 
ATOM 2351 N N   . ASP B 2 104 ? 281.957 257.572 305.115 1.00 63.43  ? 104 ASP G N   1 
ATOM 2352 C CA  . ASP B 2 104 ? 282.710 258.697 305.650 1.00 45.80  ? 104 ASP G CA  1 
ATOM 2353 C C   . ASP B 2 104 ? 282.921 258.612 307.159 1.00 47.50  ? 104 ASP G C   1 
ATOM 2354 O O   . ASP B 2 104 ? 283.350 259.603 307.755 1.00 63.94  ? 104 ASP G O   1 
ATOM 2355 C CB  . ASP B 2 104 ? 282.018 260.020 305.325 1.00 44.26  ? 104 ASP G CB  1 
ATOM 2356 C CG  . ASP B 2 104 ? 282.235 260.457 303.902 1.00 60.14  ? 104 ASP G CG  1 
ATOM 2357 O OD1 . ASP B 2 104 ? 283.404 260.621 303.499 1.00 61.17  ? 104 ASP G OD1 1 
ATOM 2358 O OD2 . ASP B 2 104 ? 281.235 260.697 303.201 1.00 69.99  ? 104 ASP G OD2 1 
ATOM 2359 N N   . ASP B 2 105 ? 282.570 257.485 307.783 1.00 44.72  ? 105 ASP G N   1 
ATOM 2360 C CA  . ASP B 2 105 ? 282.655 257.323 309.235 1.00 42.25  ? 105 ASP G CA  1 
ATOM 2361 C C   . ASP B 2 105 ? 284.064 257.517 309.787 1.00 49.52  ? 105 ASP G C   1 
ATOM 2362 O O   . ASP B 2 105 ? 285.034 256.960 309.270 1.00 60.85  ? 105 ASP G O   1 
ATOM 2363 C CB  . ASP B 2 105 ? 282.143 255.942 309.636 1.00 46.07  ? 105 ASP G CB  1 
ATOM 2364 C CG  . ASP B 2 105 ? 282.429 255.614 311.079 1.00 44.15  ? 105 ASP G CG  1 
ATOM 2365 O OD1 . ASP B 2 105 ? 281.770 256.194 311.960 1.00 45.90  ? 105 ASP G OD1 1 
ATOM 2366 O OD2 . ASP B 2 105 ? 283.333 254.799 311.337 1.00 52.64  ? 105 ASP G OD2 1 
ATOM 2367 N N   . SER B 2 106 ? 284.164 258.322 310.841 1.00 53.24  ? 106 SER G N   1 
ATOM 2368 C CA  . SER B 2 106 ? 285.401 258.528 311.575 1.00 53.98  ? 106 SER G CA  1 
ATOM 2369 C C   . SER B 2 106 ? 285.043 258.724 313.036 1.00 47.54  ? 106 SER G C   1 
ATOM 2370 O O   . SER B 2 106 ? 283.968 259.224 313.352 1.00 57.30  ? 106 SER G O   1 
ATOM 2371 C CB  . SER B 2 106 ? 286.189 259.720 311.053 1.00 46.49  ? 106 SER G CB  1 
ATOM 2372 O OG  . SER B 2 106 ? 286.713 259.435 309.775 1.00 65.84  ? 106 SER G OG  1 
ATOM 2373 N N   . TRP B 2 107 ? 285.949 258.333 313.921 1.00 41.41  ? 107 TRP G N   1 
ATOM 2374 C CA  . TRP B 2 107 ? 285.725 258.403 315.357 1.00 43.40  ? 107 TRP G CA  1 
ATOM 2375 C C   . TRP B 2 107 ? 286.927 258.989 316.076 1.00 41.57  ? 107 TRP G C   1 
ATOM 2376 O O   . TRP B 2 107 ? 288.073 258.704 315.724 1.00 58.10  ? 107 TRP G O   1 
ATOM 2377 C CB  . TRP B 2 107 ? 285.439 257.022 315.933 1.00 56.37  ? 107 TRP G CB  1 
ATOM 2378 C CG  . TRP B 2 107 ? 284.070 256.480 315.710 1.00 53.29  ? 107 TRP G CG  1 
ATOM 2379 C CD1 . TRP B 2 107 ? 283.585 255.918 314.573 1.00 49.90  ? 107 TRP G CD1 1 
ATOM 2380 C CD2 . TRP B 2 107 ? 283.053 256.316 316.700 1.00 51.66  ? 107 TRP G CD2 1 
ATOM 2381 N NE1 . TRP B 2 107 ? 282.301 255.480 314.772 1.00 41.14  ? 107 TRP G NE1 1 
ATOM 2382 C CE2 . TRP B 2 107 ? 281.955 255.704 316.076 1.00 38.86  ? 107 TRP G CE2 1 
ATOM 2383 C CE3 . TRP B 2 107 ? 282.956 256.648 318.049 1.00 61.60  ? 107 TRP G CE3 1 
ATOM 2384 C CZ2 . TRP B 2 107 ? 280.782 255.407 316.762 1.00 43.51  ? 107 TRP G CZ2 1 
ATOM 2385 C CZ3 . TRP B 2 107 ? 281.782 256.365 318.718 1.00 59.89  ? 107 TRP G CZ3 1 
ATOM 2386 C CH2 . TRP B 2 107 ? 280.712 255.757 318.073 1.00 46.25  ? 107 TRP G CH2 1 
ATOM 2387 N N   . GLY B 2 108 ? 286.655 259.807 317.079 1.00 40.99  ? 108 GLY G N   1 
ATOM 2388 C CA  . GLY B 2 108 ? 287.698 260.285 317.956 1.00 56.51  ? 108 GLY G CA  1 
ATOM 2389 C C   . GLY B 2 108 ? 287.978 259.288 319.062 1.00 71.82  ? 108 GLY G C   1 
ATOM 2390 O O   . GLY B 2 108 ? 287.245 258.320 319.245 1.00 86.30  ? 108 GLY G O   1 
ATOM 2391 N N   . GLN B 2 109 ? 289.090 259.516 319.768 1.00 70.14  ? 109 GLN G N   1 
ATOM 2392 C CA  . GLN B 2 109 ? 289.499 258.622 320.852 1.00 70.83  ? 109 GLN G CA  1 
ATOM 2393 C C   . GLN B 2 109 ? 288.483 258.600 321.988 1.00 71.85  ? 109 GLN G C   1 
ATOM 2394 O O   . GLN B 2 109 ? 288.264 257.558 322.614 1.00 64.53  ? 109 GLN G O   1 
ATOM 2395 C CB  . GLN B 2 109 ? 290.876 259.026 321.374 1.00 75.78  ? 109 GLN G CB  1 
ATOM 2396 C CG  . GLN B 2 109 ? 291.996 258.977 320.343 1.00 80.76  ? 109 GLN G CG  1 
ATOM 2397 C CD  . GLN B 2 109 ? 291.922 257.760 319.437 1.00 76.75  ? 109 GLN G CD  1 
ATOM 2398 O OE1 . GLN B 2 109 ? 292.273 256.652 319.841 1.00 76.48  ? 109 GLN G OE1 1 
ATOM 2399 N NE2 . GLN B 2 109 ? 291.498 257.967 318.194 1.00 70.25  ? 109 GLN G NE2 1 
ATOM 2400 N N   . GLY B 2 110 ? 287.876 259.732 322.280 1.00 73.50  ? 110 GLY G N   1 
ATOM 2401 C CA  . GLY B 2 110 ? 286.886 259.859 323.327 1.00 71.96  ? 110 GLY G CA  1 
ATOM 2402 C C   . GLY B 2 110 ? 287.453 260.583 324.529 1.00 69.53  ? 110 GLY G C   1 
ATOM 2403 O O   . GLY B 2 110 ? 288.653 260.518 324.822 1.00 80.67  ? 110 GLY G O   1 
ATOM 2404 N N   . VAL B 2 111 ? 286.581 261.293 325.236 1.00 47.16  ? 111 VAL G N   1 
ATOM 2405 C CA  . VAL B 2 111 ? 286.969 262.015 326.439 1.00 55.20  ? 111 VAL G CA  1 
ATOM 2406 C C   . VAL B 2 111 ? 286.019 261.630 327.569 1.00 50.88  ? 111 VAL G C   1 
ATOM 2407 O O   . VAL B 2 111 ? 284.804 261.522 327.367 1.00 55.88  ? 111 VAL G O   1 
ATOM 2408 C CB  . VAL B 2 111 ? 287.059 263.543 326.197 1.00 72.78  ? 111 VAL G CB  1 
ATOM 2409 C CG1 . VAL B 2 111 ? 285.705 264.258 326.093 1.00 69.70  ? 111 VAL G CG1 1 
ATOM 2410 C CG2 . VAL B 2 111 ? 287.948 264.190 327.243 1.00 68.66  ? 111 VAL G CG2 1 
ATOM 2411 N N   . LEU B 2 112 ? 286.590 261.282 328.717 1.00 52.70  ? 112 LEU G N   1 
ATOM 2412 C CA  . LEU B 2 112 ? 285.798 260.874 329.867 1.00 57.80  ? 112 LEU G CA  1 
ATOM 2413 C C   . LEU B 2 112 ? 285.220 262.094 330.571 1.00 64.91  ? 112 LEU G C   1 
ATOM 2414 O O   . LEU B 2 112 ? 285.954 263.011 330.946 1.00 76.46  ? 112 LEU G O   1 
ATOM 2415 C CB  . LEU B 2 112 ? 286.649 260.057 330.837 1.00 63.80  ? 112 LEU G CB  1 
ATOM 2416 C CG  . LEU B 2 112 ? 286.002 259.652 332.163 1.00 66.51  ? 112 LEU G CG  1 
ATOM 2417 C CD1 . LEU B 2 112 ? 284.823 258.721 331.960 1.00 60.89  ? 112 LEU G CD1 1 
ATOM 2418 C CD2 . LEU B 2 112 ? 287.032 259.014 333.073 1.00 66.93  ? 112 LEU G CD2 1 
ATOM 2419 N N   . VAL B 2 113 ? 283.905 262.094 330.763 1.00 61.88  ? 113 VAL G N   1 
ATOM 2420 C CA  . VAL B 2 113 ? 283.209 263.136 331.504 1.00 60.97  ? 113 VAL G CA  1 
ATOM 2421 C C   . VAL B 2 113 ? 282.678 262.494 332.775 1.00 60.47  ? 113 VAL G C   1 
ATOM 2422 O O   . VAL B 2 113 ? 281.911 261.527 332.712 1.00 82.12  ? 113 VAL G O   1 
ATOM 2423 C CB  . VAL B 2 113 ? 282.073 263.752 330.675 1.00 59.15  ? 113 VAL G CB  1 
ATOM 2424 C CG1 . VAL B 2 113 ? 281.136 264.567 331.553 1.00 59.38  ? 113 VAL G CG1 1 
ATOM 2425 C CG2 . VAL B 2 113 ? 282.641 264.590 329.553 1.00 61.27  ? 113 VAL G CG2 1 
ATOM 2426 N N   . THR B 2 114 ? 283.073 263.030 333.926 1.00 69.59  ? 114 THR G N   1 
ATOM 2427 C CA  . THR B 2 114 ? 282.680 262.479 335.216 1.00 76.88  ? 114 THR G CA  1 
ATOM 2428 C C   . THR B 2 114 ? 281.820 263.494 335.950 1.00 75.54  ? 114 THR G C   1 
ATOM 2429 O O   . THR B 2 114 ? 282.241 264.636 336.154 1.00 82.22  ? 114 THR G O   1 
ATOM 2430 C CB  . THR B 2 114 ? 283.905 262.114 336.057 1.00 85.71  ? 114 THR G CB  1 
ATOM 2431 O OG1 . THR B 2 114 ? 284.783 261.283 335.291 1.00 82.60  ? 114 THR G OG1 1 
ATOM 2432 C CG2 . THR B 2 114 ? 283.481 261.356 337.304 1.00 84.13  ? 114 THR G CG2 1 
ATOM 2433 N N   . VAL B 2 115 ? 280.623 263.077 336.345 1.00 75.45  ? 115 VAL G N   1 
ATOM 2434 C CA  . VAL B 2 115 ? 279.724 263.894 337.148 1.00 82.92  ? 115 VAL G CA  1 
ATOM 2435 C C   . VAL B 2 115 ? 279.701 263.308 338.553 1.00 84.43  ? 115 VAL G C   1 
ATOM 2436 O O   . VAL B 2 115 ? 279.255 262.172 338.748 1.00 87.00  ? 115 VAL G O   1 
ATOM 2437 C CB  . VAL B 2 115 ? 278.317 263.943 336.539 1.00 87.37  ? 115 VAL G CB  1 
ATOM 2438 C CG1 . VAL B 2 115 ? 277.488 265.022 337.199 1.00 82.67  ? 115 VAL G CG1 1 
ATOM 2439 C CG2 . VAL B 2 115 ? 278.399 264.168 335.039 1.00 89.39  ? 115 VAL G CG2 1 
ATOM 2440 N N   . SER B 2 116 ? 280.185 264.074 339.530 1.00 94.68  ? 116 SER G N   1 
ATOM 2441 C CA  . SER B 2 116 ? 280.283 263.595 340.902 1.00 97.45  ? 116 SER G CA  1 
ATOM 2442 C C   . SER B 2 116 ? 279.906 264.705 341.869 1.00 97.05  ? 116 SER G C   1 
ATOM 2443 O O   . SER B 2 116 ? 280.277 265.863 341.668 1.00 93.98  ? 116 SER G O   1 
ATOM 2444 C CB  . SER B 2 116 ? 281.691 263.107 341.248 1.00 97.70  ? 116 SER G CB  1 
ATOM 2445 O OG  . SER B 2 116 ? 282.556 264.207 341.452 1.00 93.11  ? 116 SER G OG  1 
ATOM 2446 N N   . SER B 2 117 ? 279.172 264.343 342.915 1.00 100.30 ? 117 SER G N   1 
ATOM 2447 C CA  . SER B 2 117 ? 278.761 265.307 343.928 1.00 102.32 ? 117 SER G CA  1 
ATOM 2448 C C   . SER B 2 117 ? 279.675 265.216 345.141 1.00 101.63 ? 117 SER G C   1 
ATOM 2449 O O   . SER B 2 117 ? 279.640 264.242 345.891 1.00 109.83 ? 117 SER G O   1 
ATOM 2450 C CB  . SER B 2 117 ? 277.308 265.071 344.343 1.00 102.21 ? 117 SER G CB  1 
ATOM 2451 O OG  . SER B 2 117 ? 276.911 265.981 345.354 1.00 98.12  ? 117 SER G OG  1 
ATOM 2452 N N   . ASP C 3 1   ? 260.366 256.483 317.200 1.00 94.99  ? 1   ASP L N   1 
ATOM 2453 C CA  . ASP C 3 1   ? 261.641 255.873 317.557 1.00 95.74  ? 1   ASP L CA  1 
ATOM 2454 C C   . ASP C 3 1   ? 261.771 254.474 316.968 1.00 97.24  ? 1   ASP L C   1 
ATOM 2455 O O   . ASP C 3 1   ? 260.778 253.777 316.769 1.00 93.75  ? 1   ASP L O   1 
ATOM 2456 C CB  . ASP C 3 1   ? 261.799 255.817 319.077 1.00 98.35  ? 1   ASP L CB  1 
ATOM 2457 C CG  . ASP C 3 1   ? 260.735 254.962 319.745 1.00 100.83 ? 1   ASP L CG  1 
ATOM 2458 O OD1 . ASP C 3 1   ? 259.605 254.889 319.215 1.00 98.43  ? 1   ASP L OD1 1 
ATOM 2459 O OD2 . ASP C 3 1   ? 261.028 254.356 320.797 1.00 100.06 ? 1   ASP L OD2 1 
ATOM 2460 N N   . ILE C 3 2   ? 263.007 254.072 316.680 1.00 89.21  ? 2   ILE L N   1 
ATOM 2461 C CA  . ILE C 3 2   ? 263.320 252.737 316.186 1.00 87.49  ? 2   ILE L CA  1 
ATOM 2462 C C   . ILE C 3 2   ? 264.197 252.059 317.227 1.00 85.28  ? 2   ILE L C   1 
ATOM 2463 O O   . ILE C 3 2   ? 265.048 252.706 317.846 1.00 85.38  ? 2   ILE L O   1 
ATOM 2464 C CB  . ILE C 3 2   ? 263.999 252.796 314.800 1.00 83.47  ? 2   ILE L CB  1 
ATOM 2465 C CG1 . ILE C 3 2   ? 263.194 253.724 313.886 1.00 82.77  ? 2   ILE L CG1 1 
ATOM 2466 C CG2 . ILE C 3 2   ? 264.110 251.415 314.177 1.00 75.91  ? 2   ILE L CG2 1 
ATOM 2467 C CD1 . ILE C 3 2   ? 263.611 253.744 312.453 1.00 81.26  ? 2   ILE L CD1 1 
ATOM 2468 N N   . GLN C 3 3   ? 263.978 250.760 317.437 1.00 86.58  ? 3   GLN L N   1 
ATOM 2469 C CA  . GLN C 3 3   ? 264.624 250.013 318.508 1.00 85.45  ? 3   GLN L CA  1 
ATOM 2470 C C   . GLN C 3 3   ? 265.349 248.809 317.931 1.00 87.22  ? 3   GLN L C   1 
ATOM 2471 O O   . GLN C 3 3   ? 264.773 248.050 317.148 1.00 93.85  ? 3   GLN L O   1 
ATOM 2472 C CB  . GLN C 3 3   ? 263.601 249.555 319.555 1.00 87.70  ? 3   GLN L CB  1 
ATOM 2473 C CG  . GLN C 3 3   ? 262.522 250.583 319.867 1.00 90.79  ? 3   GLN L CG  1 
ATOM 2474 C CD  . GLN C 3 3   ? 261.904 250.400 321.233 1.00 89.58  ? 3   GLN L CD  1 
ATOM 2475 O OE1 . GLN C 3 3   ? 262.023 249.340 321.847 1.00 89.67  ? 3   GLN L OE1 1 
ATOM 2476 N NE2 . GLN C 3 3   ? 261.233 251.438 321.719 1.00 86.69  ? 3   GLN L NE2 1 
ATOM 2477 N N   . MET C 3 4   ? 266.611 248.644 318.316 1.00 81.25  ? 4   MET L N   1 
ATOM 2478 C CA  . MET C 3 4   ? 267.477 247.590 317.807 1.00 81.40  ? 4   MET L CA  1 
ATOM 2479 C C   . MET C 3 4   ? 267.676 246.532 318.883 1.00 87.58  ? 4   MET L C   1 
ATOM 2480 O O   . MET C 3 4   ? 268.076 246.855 320.005 1.00 84.98  ? 4   MET L O   1 
ATOM 2481 C CB  . MET C 3 4   ? 268.834 248.166 317.393 1.00 77.03  ? 4   MET L CB  1 
ATOM 2482 C CG  . MET C 3 4   ? 268.768 249.350 316.438 1.00 80.86  ? 4   MET L CG  1 
ATOM 2483 S SD  . MET C 3 4   ? 267.642 249.156 315.056 1.00 76.36  ? 4   MET L SD  1 
ATOM 2484 C CE  . MET C 3 4   ? 268.440 247.812 314.193 1.00 80.70  ? 4   MET L CE  1 
ATOM 2485 N N   . THR C 3 5   ? 267.395 245.277 318.546 1.00 87.27  ? 5   THR L N   1 
ATOM 2486 C CA  . THR C 3 5   ? 267.612 244.153 319.449 1.00 83.07  ? 5   THR L CA  1 
ATOM 2487 C C   . THR C 3 5   ? 268.750 243.303 318.901 1.00 75.91  ? 5   THR L C   1 
ATOM 2488 O O   . THR C 3 5   ? 268.649 242.771 317.794 1.00 79.10  ? 5   THR L O   1 
ATOM 2489 C CB  . THR C 3 5   ? 266.343 243.318 319.606 1.00 79.34  ? 5   THR L CB  1 
ATOM 2490 O OG1 . THR C 3 5   ? 265.260 244.166 320.003 1.00 70.78  ? 5   THR L OG1 1 
ATOM 2491 C CG2 . THR C 3 5   ? 266.544 242.247 320.662 1.00 80.02  ? 5   THR L CG2 1 
ATOM 2492 N N   . GLN C 3 6   ? 269.810 243.153 319.686 1.00 78.03  ? 6   GLN L N   1 
ATOM 2493 C CA  . GLN C 3 6   ? 271.009 242.424 319.284 1.00 76.88  ? 6   GLN L CA  1 
ATOM 2494 C C   . GLN C 3 6   ? 271.154 241.161 320.125 1.00 76.98  ? 6   GLN L C   1 
ATOM 2495 O O   . GLN C 3 6   ? 271.481 241.237 321.314 1.00 72.89  ? 6   GLN L O   1 
ATOM 2496 C CB  . GLN C 3 6   ? 272.244 243.307 319.427 1.00 75.34  ? 6   GLN L CB  1 
ATOM 2497 C CG  . GLN C 3 6   ? 273.514 242.664 318.936 1.00 75.30  ? 6   GLN L CG  1 
ATOM 2498 C CD  . GLN C 3 6   ? 274.625 243.659 318.761 1.00 71.78  ? 6   GLN L CD  1 
ATOM 2499 O OE1 . GLN C 3 6   ? 274.489 244.822 319.127 1.00 71.06  ? 6   GLN L OE1 1 
ATOM 2500 N NE2 . GLN C 3 6   ? 275.742 243.207 318.208 1.00 74.02  ? 6   GLN L NE2 1 
ATOM 2501 N N   . SER C 3 7   ? 270.917 240.006 319.513 1.00 85.00  ? 7   SER L N   1 
ATOM 2502 C CA  . SER C 3 7   ? 271.073 238.722 320.176 1.00 83.85  ? 7   SER L CA  1 
ATOM 2503 C C   . SER C 3 7   ? 271.898 237.788 319.301 1.00 81.67  ? 7   SER L C   1 
ATOM 2504 O O   . SER C 3 7   ? 271.821 237.868 318.072 1.00 84.71  ? 7   SER L O   1 
ATOM 2505 C CB  . SER C 3 7   ? 269.695 238.100 320.453 1.00 85.60  ? 7   SER L CB  1 
ATOM 2506 O OG  . SER C 3 7   ? 268.963 237.934 319.251 1.00 83.44  ? 7   SER L OG  1 
ATOM 2507 N N   . PRO C 3 8   ? 272.696 236.880 319.900 1.00 90.23  ? 8   PRO L N   1 
ATOM 2508 C CA  . PRO C 3 8   ? 272.857 236.548 321.326 1.00 96.73  ? 8   PRO L CA  1 
ATOM 2509 C C   . PRO C 3 8   ? 273.984 237.327 321.989 1.00 94.47  ? 8   PRO L C   1 
ATOM 2510 O O   . PRO C 3 8   ? 275.113 237.277 321.525 1.00 93.47  ? 8   PRO L O   1 
ATOM 2511 C CB  . PRO C 3 8   ? 273.179 235.041 321.295 1.00 99.07  ? 8   PRO L CB  1 
ATOM 2512 C CG  . PRO C 3 8   ? 273.333 234.656 319.815 1.00 94.73  ? 8   PRO L CG  1 
ATOM 2513 C CD  . PRO C 3 8   ? 273.466 235.947 319.070 1.00 91.50  ? 8   PRO L CD  1 
ATOM 2514 N N   . SER C 3 9   ? 273.687 238.036 323.084 1.00 93.43  ? 9   SER L N   1 
ATOM 2515 C CA  . SER C 3 9   ? 274.679 238.874 323.756 1.00 93.90  ? 9   SER L CA  1 
ATOM 2516 C C   . SER C 3 9   ? 275.842 238.078 324.345 1.00 94.32  ? 9   SER L C   1 
ATOM 2517 O O   . SER C 3 9   ? 276.979 238.560 324.350 1.00 98.65  ? 9   SER L O   1 
ATOM 2518 C CB  . SER C 3 9   ? 274.003 239.700 324.847 1.00 94.20  ? 9   SER L CB  1 
ATOM 2519 O OG  . SER C 3 9   ? 273.375 238.865 325.801 1.00 93.29  ? 9   SER L OG  1 
ATOM 2520 N N   . ALA C 3 10  ? 275.588 236.868 324.841 1.00 97.46  ? 10  ALA L N   1 
ATOM 2521 C CA  . ALA C 3 10  ? 276.590 236.090 325.562 1.00 103.94 ? 10  ALA L CA  1 
ATOM 2522 C C   . ALA C 3 10  ? 277.281 235.043 324.693 1.00 103.35 ? 10  ALA L C   1 
ATOM 2523 O O   . ALA C 3 10  ? 277.718 234.012 325.218 1.00 106.52 ? 10  ALA L O   1 
ATOM 2524 C CB  . ALA C 3 10  ? 275.957 235.423 326.784 1.00 107.74 ? 10  ALA L CB  1 
ATOM 2525 N N   . LEU C 3 11  ? 277.330 235.261 323.376 1.00 95.23  ? 11  LEU L N   1 
ATOM 2526 C CA  . LEU C 3 11  ? 277.900 234.291 322.440 1.00 98.80  ? 11  LEU L CA  1 
ATOM 2527 C C   . LEU C 3 11  ? 279.375 234.009 322.720 1.00 97.86  ? 11  LEU L C   1 
ATOM 2528 O O   . LEU C 3 11  ? 280.165 234.927 322.948 1.00 98.71  ? 11  LEU L O   1 
ATOM 2529 C CB  . LEU C 3 11  ? 277.721 234.801 321.012 1.00 97.22  ? 11  LEU L CB  1 
ATOM 2530 C CG  . LEU C 3 11  ? 277.843 233.785 319.881 1.00 95.74  ? 11  LEU L CG  1 
ATOM 2531 C CD1 . LEU C 3 11  ? 277.031 232.538 320.183 1.00 100.83 ? 11  LEU L CD1 1 
ATOM 2532 C CD2 . LEU C 3 11  ? 277.343 234.422 318.612 1.00 92.43  ? 11  LEU L CD2 1 
ATOM 2533 N N   . SER C 3 12  ? 279.739 232.725 322.710 1.00 99.15  ? 12  SER L N   1 
ATOM 2534 C CA  . SER C 3 12  ? 281.115 232.288 322.907 1.00 102.60 ? 12  SER L CA  1 
ATOM 2535 C C   . SER C 3 12  ? 281.489 231.256 321.852 1.00 101.95 ? 12  SER L C   1 
ATOM 2536 O O   . SER C 3 12  ? 280.649 230.462 321.420 1.00 98.05  ? 12  SER L O   1 
ATOM 2537 C CB  . SER C 3 12  ? 281.315 231.691 324.305 1.00 100.17 ? 12  SER L CB  1 
ATOM 2538 O OG  . SER C 3 12  ? 282.682 231.418 324.553 1.00 101.16 ? 12  SER L OG  1 
ATOM 2539 N N   . ALA C 3 13  ? 282.768 231.249 321.474 1.00 100.58 ? 13  ALA L N   1 
ATOM 2540 C CA  . ALA C 3 13  ? 283.276 230.375 320.421 1.00 98.42  ? 13  ALA L CA  1 
ATOM 2541 C C   . ALA C 3 13  ? 284.796 230.361 320.472 1.00 101.54 ? 13  ALA L C   1 
ATOM 2542 O O   . ALA C 3 13  ? 285.427 231.298 320.968 1.00 101.49 ? 13  ALA L O   1 
ATOM 2543 C CB  . ALA C 3 13  ? 282.804 230.818 319.032 1.00 94.66  ? 13  ALA L CB  1 
ATOM 2544 N N   . SER C 3 14  ? 285.373 229.278 319.953 1.00 97.84  ? 14  SER L N   1 
ATOM 2545 C CA  . SER C 3 14  ? 286.815 229.110 319.850 1.00 96.87  ? 14  SER L CA  1 
ATOM 2546 C C   . SER C 3 14  ? 287.337 229.779 318.581 1.00 96.73  ? 14  SER L C   1 
ATOM 2547 O O   . SER C 3 14  ? 286.570 230.178 317.705 1.00 98.42  ? 14  SER L O   1 
ATOM 2548 C CB  . SER C 3 14  ? 287.187 227.630 319.866 1.00 94.09  ? 14  SER L CB  1 
ATOM 2549 O OG  . SER C 3 14  ? 286.691 226.994 321.031 1.00 94.47  ? 14  SER L OG  1 
ATOM 2550 N N   . VAL C 3 15  ? 288.665 229.916 318.505 1.00 99.44  ? 15  VAL L N   1 
ATOM 2551 C CA  . VAL C 3 15  ? 289.308 230.499 317.330 1.00 98.38  ? 15  VAL L CA  1 
ATOM 2552 C C   . VAL C 3 15  ? 289.053 229.620 316.109 1.00 99.84  ? 15  VAL L C   1 
ATOM 2553 O O   . VAL C 3 15  ? 289.152 228.389 316.171 1.00 103.03 ? 15  VAL L O   1 
ATOM 2554 C CB  . VAL C 3 15  ? 290.811 230.678 317.617 1.00 96.90  ? 15  VAL L CB  1 
ATOM 2555 C CG1 . VAL C 3 15  ? 291.610 231.020 316.363 1.00 95.64  ? 15  VAL L CG1 1 
ATOM 2556 C CG2 . VAL C 3 15  ? 291.020 231.736 318.688 1.00 99.15  ? 15  VAL L CG2 1 
ATOM 2557 N N   . GLY C 3 16  ? 288.728 230.258 314.984 1.00 93.99  ? 16  GLY L N   1 
ATOM 2558 C CA  . GLY C 3 16  ? 288.444 229.557 313.752 1.00 95.39  ? 16  GLY L CA  1 
ATOM 2559 C C   . GLY C 3 16  ? 286.995 229.170 313.566 1.00 97.03  ? 16  GLY L C   1 
ATOM 2560 O O   . GLY C 3 16  ? 286.642 228.652 312.499 1.00 97.53  ? 16  GLY L O   1 
ATOM 2561 N N   . ASP C 3 17  ? 286.146 229.410 314.559 1.00 95.39  ? 17  ASP L N   1 
ATOM 2562 C CA  . ASP C 3 17  ? 284.728 229.109 314.460 1.00 98.34  ? 17  ASP L CA  1 
ATOM 2563 C C   . ASP C 3 17  ? 284.005 230.176 313.644 1.00 97.67  ? 17  ASP L C   1 
ATOM 2564 O O   . ASP C 3 17  ? 284.483 231.299 313.473 1.00 99.35  ? 17  ASP L O   1 
ATOM 2565 C CB  . ASP C 3 17  ? 284.102 229.009 315.850 1.00 97.25  ? 17  ASP L CB  1 
ATOM 2566 C CG  . ASP C 3 17  ? 284.549 227.774 316.603 1.00 98.95  ? 17  ASP L CG  1 
ATOM 2567 O OD1 . ASP C 3 17  ? 285.583 227.186 316.222 1.00 100.00 ? 17  ASP L OD1 1 
ATOM 2568 O OD2 . ASP C 3 17  ? 283.872 227.397 317.582 1.00 97.89  ? 17  ASP L OD2 1 
ATOM 2569 N N   . ARG C 3 18  ? 282.842 229.803 313.120 1.00 91.08  ? 18  ARG L N   1 
ATOM 2570 C CA  . ARG C 3 18  ? 281.979 230.740 312.416 1.00 91.58  ? 18  ARG L CA  1 
ATOM 2571 C C   . ARG C 3 18  ? 280.973 231.325 313.402 1.00 92.41  ? 18  ARG L C   1 
ATOM 2572 O O   . ARG C 3 18  ? 280.235 230.583 314.059 1.00 89.95  ? 18  ARG L O   1 
ATOM 2573 C CB  . ARG C 3 18  ? 281.272 230.051 311.252 1.00 88.49  ? 18  ARG L CB  1 
ATOM 2574 C CG  . ARG C 3 18  ? 280.216 230.901 310.589 1.00 95.82  ? 18  ARG L CG  1 
ATOM 2575 C CD  . ARG C 3 18  ? 280.244 230.728 309.085 1.00 97.47  ? 18  ARG L CD  1 
ATOM 2576 N NE  . ARG C 3 18  ? 278.970 231.092 308.482 1.00 95.92  ? 18  ARG L NE  1 
ATOM 2577 C CZ  . ARG C 3 18  ? 278.780 231.258 307.182 1.00 93.04  ? 18  ARG L CZ  1 
ATOM 2578 N NH1 . ARG C 3 18  ? 279.767 231.102 306.315 1.00 90.31  ? 18  ARG L NH1 1 
ATOM 2579 N NH2 . ARG C 3 18  ? 277.571 231.593 306.741 1.00 93.80  ? 18  ARG L NH2 1 
ATOM 2580 N N   . VAL C 3 19  ? 280.946 232.653 313.500 1.00 83.97  ? 19  VAL L N   1 
ATOM 2581 C CA  . VAL C 3 19  ? 280.089 233.381 314.430 1.00 82.22  ? 19  VAL L CA  1 
ATOM 2582 C C   . VAL C 3 19  ? 278.985 234.071 313.641 1.00 88.22  ? 19  VAL L C   1 
ATOM 2583 O O   . VAL C 3 19  ? 279.213 234.525 312.517 1.00 89.02  ? 19  VAL L O   1 
ATOM 2584 C CB  . VAL C 3 19  ? 280.940 234.391 315.226 1.00 84.57  ? 19  VAL L CB  1 
ATOM 2585 C CG1 . VAL C 3 19  ? 280.152 235.078 316.324 1.00 86.39  ? 19  VAL L CG1 1 
ATOM 2586 C CG2 . VAL C 3 19  ? 282.130 233.692 315.813 1.00 83.02  ? 19  VAL L CG2 1 
ATOM 2587 N N   . THR C 3 20  ? 277.787 234.144 314.224 1.00 88.38  ? 20  THR L N   1 
ATOM 2588 C CA  . THR C 3 20  ? 276.676 234.881 313.637 1.00 77.91  ? 20  THR L CA  1 
ATOM 2589 C C   . THR C 3 20  ? 276.020 235.759 314.695 1.00 75.62  ? 20  THR L C   1 
ATOM 2590 O O   . THR C 3 20  ? 275.715 235.289 315.794 1.00 73.77  ? 20  THR L O   1 
ATOM 2591 C CB  . THR C 3 20  ? 275.663 233.903 313.032 1.00 80.76  ? 20  THR L CB  1 
ATOM 2592 O OG1 . THR C 3 20  ? 276.283 233.185 311.958 1.00 82.28  ? 20  THR L OG1 1 
ATOM 2593 C CG2 . THR C 3 20  ? 274.434 234.616 312.517 1.00 82.41  ? 20  THR L CG2 1 
ATOM 2594 N N   . ILE C 3 21  ? 275.810 237.034 314.360 1.00 84.57  ? 21  ILE L N   1 
ATOM 2595 C CA  . ILE C 3 21  ? 275.207 238.027 315.247 1.00 77.75  ? 21  ILE L CA  1 
ATOM 2596 C C   . ILE C 3 21  ? 274.010 238.632 314.524 1.00 67.05  ? 21  ILE L C   1 
ATOM 2597 O O   . ILE C 3 21  ? 274.155 239.154 313.414 1.00 71.27  ? 21  ILE L O   1 
ATOM 2598 C CB  . ILE C 3 21  ? 276.209 239.118 315.658 1.00 65.97  ? 21  ILE L CB  1 
ATOM 2599 C CG1 . ILE C 3 21  ? 277.502 238.496 316.188 1.00 70.77  ? 21  ILE L CG1 1 
ATOM 2600 C CG2 . ILE C 3 21  ? 275.596 240.029 316.701 1.00 75.01  ? 21  ILE L CG2 1 
ATOM 2601 C CD1 . ILE C 3 21  ? 278.555 239.489 316.567 1.00 74.85  ? 21  ILE L CD1 1 
ATOM 2602 N N   . SER C 3 22  ? 272.833 238.556 315.140 1.00 71.42  ? 22  SER L N   1 
ATOM 2603 C CA  . SER C 3 22  ? 271.588 239.000 314.520 1.00 76.06  ? 22  SER L CA  1 
ATOM 2604 C C   . SER C 3 22  ? 271.060 240.258 315.198 1.00 74.05  ? 22  SER L C   1 
ATOM 2605 O O   . SER C 3 22  ? 270.986 240.321 316.429 1.00 83.21  ? 22  SER L O   1 
ATOM 2606 C CB  . SER C 3 22  ? 270.529 237.897 314.574 1.00 76.85  ? 22  SER L CB  1 
ATOM 2607 O OG  . SER C 3 22  ? 271.059 236.657 314.144 1.00 73.31  ? 22  SER L OG  1 
ATOM 2608 N N   . CYS C 3 23  ? 270.708 241.258 314.392 1.00 73.04  ? 23  CYS L N   1 
ATOM 2609 C CA  . CYS C 3 23  ? 270.130 242.511 314.861 1.00 73.83  ? 23  CYS L CA  1 
ATOM 2610 C C   . CYS C 3 23  ? 268.752 242.683 314.238 1.00 71.26  ? 23  CYS L C   1 
ATOM 2611 O O   . CYS C 3 23  ? 268.589 242.484 313.030 1.00 78.38  ? 23  CYS L O   1 
ATOM 2612 C CB  . CYS C 3 23  ? 271.024 243.699 314.506 1.00 78.99  ? 23  CYS L CB  1 
ATOM 2613 S SG  . CYS C 3 23  ? 270.682 245.200 315.431 1.00 75.23  ? 23  CYS L SG  1 
ATOM 2614 N N   . ARG C 3 24  ? 267.759 243.041 315.053 1.00 81.27  ? 24  ARG L N   1 
ATOM 2615 C CA  . ARG C 3 24  ? 266.392 243.223 314.573 1.00 86.57  ? 24  ARG L CA  1 
ATOM 2616 C C   . ARG C 3 24  ? 265.901 244.642 314.829 1.00 85.12  ? 24  ARG L C   1 
ATOM 2617 O O   . ARG C 3 24  ? 265.897 245.106 315.974 1.00 80.79  ? 24  ARG L O   1 
ATOM 2618 C CB  . ARG C 3 24  ? 265.442 242.216 315.222 1.00 86.71  ? 24  ARG L CB  1 
ATOM 2619 C CG  . ARG C 3 24  ? 264.153 242.039 314.441 1.00 82.77  ? 24  ARG L CG  1 
ATOM 2620 C CD  . ARG C 3 24  ? 263.196 241.072 315.103 1.00 82.48  ? 24  ARG L CD  1 
ATOM 2621 N NE  . ARG C 3 24  ? 262.028 240.832 314.263 1.00 92.47  ? 24  ARG L NE  1 
ATOM 2622 C CZ  . ARG C 3 24  ? 261.045 239.993 314.562 1.00 90.35  ? 24  ARG L CZ  1 
ATOM 2623 N NH1 . ARG C 3 24  ? 261.055 239.290 315.682 1.00 90.15  ? 24  ARG L NH1 1 
ATOM 2624 N NH2 . ARG C 3 24  ? 260.029 239.854 313.715 1.00 82.48  ? 24  ARG L NH2 1 
ATOM 2625 N N   . ALA C 3 25  ? 265.488 245.318 313.760 1.00 81.61  ? 25  ALA L N   1 
ATOM 2626 C CA  . ALA C 3 25  ? 264.888 246.642 313.851 1.00 82.98  ? 25  ALA L CA  1 
ATOM 2627 C C   . ALA C 3 25  ? 263.397 246.531 314.136 1.00 86.75  ? 25  ALA L C   1 
ATOM 2628 O O   . ALA C 3 25  ? 262.725 245.629 313.628 1.00 88.31  ? 25  ALA L O   1 
ATOM 2629 C CB  . ALA C 3 25  ? 265.113 247.420 312.557 1.00 87.61  ? 25  ALA L CB  1 
ATOM 2630 N N   . SER C 3 26  ? 262.888 247.438 314.979 1.00 88.86  ? 26  SER L N   1 
ATOM 2631 C CA  . SER C 3 26  ? 261.461 247.451 315.297 1.00 89.88  ? 26  SER L CA  1 
ATOM 2632 C C   . SER C 3 26  ? 260.616 247.769 314.067 1.00 87.95  ? 26  SER L C   1 
ATOM 2633 O O   . SER C 3 26  ? 259.549 247.178 313.866 1.00 88.84  ? 26  SER L O   1 
ATOM 2634 C CB  . SER C 3 26  ? 261.179 248.453 316.415 1.00 88.56  ? 26  SER L CB  1 
ATOM 2635 O OG  . SER C 3 26  ? 261.413 249.780 315.985 1.00 88.44  ? 26  SER L OG  1 
ATOM 2636 N N   . GLN C 3 27  ? 261.075 248.701 313.239 1.00 87.51  ? 27  GLN L N   1 
ATOM 2637 C CA  . GLN C 3 27  ? 260.387 249.096 312.020 1.00 83.91  ? 27  GLN L CA  1 
ATOM 2638 C C   . GLN C 3 27  ? 261.412 249.152 310.899 1.00 84.46  ? 27  GLN L C   1 
ATOM 2639 O O   . GLN C 3 27  ? 262.618 249.099 311.151 1.00 93.68  ? 27  GLN L O   1 
ATOM 2640 C CB  . GLN C 3 27  ? 259.652 250.436 312.162 1.00 85.35  ? 27  GLN L CB  1 
ATOM 2641 C CG  . GLN C 3 27  ? 260.501 251.578 312.643 1.00 91.97  ? 27  GLN L CG  1 
ATOM 2642 C CD  . GLN C 3 27  ? 259.699 252.605 313.413 1.00 91.59  ? 27  GLN L CD  1 
ATOM 2643 O OE1 . GLN C 3 27  ? 259.283 253.624 312.864 1.00 91.42  ? 27  GLN L OE1 1 
ATOM 2644 N NE2 . GLN C 3 27  ? 259.476 252.341 314.694 1.00 92.03  ? 27  GLN L NE2 1 
ATOM 2645 N N   . ASN C 3 28  ? 260.910 249.167 309.660 1.00 78.34  ? 28  ASN L N   1 
ATOM 2646 C CA  . ASN C 3 28  ? 261.751 249.124 308.465 1.00 88.60  ? 28  ASN L CA  1 
ATOM 2647 C C   . ASN C 3 28  ? 262.737 250.288 308.441 1.00 92.60  ? 28  ASN L C   1 
ATOM 2648 O O   . ASN C 3 28  ? 262.354 251.449 308.609 1.00 85.38  ? 28  ASN L O   1 
ATOM 2649 C CB  . ASN C 3 28  ? 260.864 249.158 307.216 1.00 86.78  ? 28  ASN L CB  1 
ATOM 2650 C CG  . ASN C 3 28  ? 261.631 248.906 305.920 1.00 81.33  ? 28  ASN L CG  1 
ATOM 2651 O OD1 . ASN C 3 28  ? 262.831 248.639 305.917 1.00 83.38  ? 28  ASN L OD1 1 
ATOM 2652 N ND2 . ASN C 3 28  ? 260.923 248.995 304.803 1.00 79.75  ? 28  ASN L ND2 1 
ATOM 2653 N N   . ILE C 3 29  ? 264.013 249.961 308.234 1.00 84.93  ? 29  ILE L N   1 
ATOM 2654 C CA  . ILE C 3 29  ? 265.077 250.947 308.121 1.00 74.32  ? 29  ILE L CA  1 
ATOM 2655 C C   . ILE C 3 29  ? 265.819 250.821 306.795 1.00 74.21  ? 29  ILE L C   1 
ATOM 2656 O O   . ILE C 3 29  ? 266.903 251.370 306.661 1.00 77.24  ? 29  ILE L O   1 
ATOM 2657 C CB  . ILE C 3 29  ? 266.072 250.837 309.292 1.00 69.91  ? 29  ILE L CB  1 
ATOM 2658 C CG1 . ILE C 3 29  ? 266.676 249.438 309.355 1.00 74.55  ? 29  ILE L CG1 1 
ATOM 2659 C CG2 . ILE C 3 29  ? 265.402 251.137 310.600 1.00 72.81  ? 29  ILE L CG2 1 
ATOM 2660 C CD1 . ILE C 3 29  ? 267.859 249.349 310.276 1.00 76.47  ? 29  ILE L CD1 1 
ATOM 2661 N N   . ASP C 3 30  ? 265.230 250.123 305.821 1.00 76.25  ? 30  ASP L N   1 
ATOM 2662 C CA  . ASP C 3 30  ? 265.805 249.843 304.485 1.00 73.61  ? 30  ASP L CA  1 
ATOM 2663 C C   . ASP C 3 30  ? 267.135 249.126 304.709 1.00 72.28  ? 30  ASP L C   1 
ATOM 2664 O O   . ASP C 3 30  ? 267.177 248.155 305.480 1.00 80.91  ? 30  ASP L O   1 
ATOM 2665 C CB  . ASP C 3 30  ? 265.874 251.113 303.640 1.00 74.86  ? 30  ASP L CB  1 
ATOM 2666 C CG  . ASP C 3 30  ? 264.587 251.907 303.673 1.00 85.05  ? 30  ASP L CG  1 
ATOM 2667 O OD1 . ASP C 3 30  ? 263.544 251.370 303.247 1.00 84.54  ? 30  ASP L OD1 1 
ATOM 2668 O OD2 . ASP C 3 30  ? 264.620 253.072 304.114 1.00 79.55  ? 30  ASP L OD2 1 
ATOM 2669 N N   . GLY C 3 31  ? 268.225 249.554 304.085 1.00 66.71  ? 31  GLY L N   1 
ATOM 2670 C CA  . GLY C 3 31  ? 269.536 248.984 304.302 1.00 69.24  ? 31  GLY L CA  1 
ATOM 2671 C C   . GLY C 3 31  ? 270.422 249.797 305.219 1.00 63.39  ? 31  GLY L C   1 
ATOM 2672 O O   . GLY C 3 31  ? 271.632 249.555 305.262 1.00 64.06  ? 31  GLY L O   1 
ATOM 2673 N N   . PHE C 3 32  ? 269.859 250.750 305.958 1.00 62.24  ? 32  PHE L N   1 
ATOM 2674 C CA  . PHE C 3 32  ? 270.611 251.675 306.804 1.00 60.25  ? 32  PHE L CA  1 
ATOM 2675 C C   . PHE C 3 32  ? 270.973 251.042 308.147 1.00 57.53  ? 32  PHE L C   1 
ATOM 2676 O O   . PHE C 3 32  ? 270.468 251.420 309.205 1.00 55.65  ? 32  PHE L O   1 
ATOM 2677 C CB  . PHE C 3 32  ? 269.793 252.934 307.028 1.00 58.30  ? 32  PHE L CB  1 
ATOM 2678 C CG  . PHE C 3 32  ? 269.589 253.756 305.806 1.00 56.61  ? 32  PHE L CG  1 
ATOM 2679 C CD1 . PHE C 3 32  ? 270.589 254.584 305.341 1.00 51.96  ? 32  PHE L CD1 1 
ATOM 2680 C CD2 . PHE C 3 32  ? 268.395 253.698 305.119 1.00 64.92  ? 32  PHE L CD2 1 
ATOM 2681 C CE1 . PHE C 3 32  ? 270.388 255.347 304.225 1.00 65.99  ? 32  PHE L CE1 1 
ATOM 2682 C CE2 . PHE C 3 32  ? 268.195 254.447 303.999 1.00 68.00  ? 32  PHE L CE2 1 
ATOM 2683 C CZ  . PHE C 3 32  ? 269.189 255.269 303.553 1.00 72.10  ? 32  PHE L CZ  1 
ATOM 2684 N N   . LEU C 3 33  ? 271.894 250.085 308.106 1.00 49.34  ? 33  LEU L N   1 
ATOM 2685 C CA  . LEU C 3 33  ? 272.395 249.488 309.334 1.00 46.76  ? 33  LEU L CA  1 
ATOM 2686 C C   . LEU C 3 33  ? 273.916 249.443 309.269 1.00 55.97  ? 33  LEU L C   1 
ATOM 2687 O O   . LEU C 3 33  ? 274.494 249.222 308.203 1.00 66.17  ? 33  LEU L O   1 
ATOM 2688 C CB  . LEU C 3 33  ? 271.843 248.065 309.565 1.00 55.24  ? 33  LEU L CB  1 
ATOM 2689 C CG  . LEU C 3 33  ? 272.168 247.533 310.971 1.00 53.43  ? 33  LEU L CG  1 
ATOM 2690 C CD1 . LEU C 3 33  ? 271.421 248.332 312.017 1.00 59.60  ? 33  LEU L CD1 1 
ATOM 2691 C CD2 . LEU C 3 33  ? 272.025 246.084 311.203 1.00 63.84  ? 33  LEU L CD2 1 
ATOM 2692 N N   . ALA C 3 34  ? 274.559 249.647 310.417 1.00 43.10  ? 34  ALA L N   1 
ATOM 2693 C CA  . ALA C 3 34  ? 276.003 249.647 310.547 1.00 40.76  ? 34  ALA L CA  1 
ATOM 2694 C C   . ALA C 3 34  ? 276.424 248.689 311.644 1.00 48.08  ? 34  ALA L C   1 
ATOM 2695 O O   . ALA C 3 34  ? 275.728 248.545 312.647 1.00 70.54  ? 34  ALA L O   1 
ATOM 2696 C CB  . ALA C 3 34  ? 276.502 251.021 310.887 1.00 54.87  ? 34  ALA L CB  1 
ATOM 2697 N N   . TRP C 3 35  ? 277.558 248.030 311.450 1.00 28.44  ? 35  TRP L N   1 
ATOM 2698 C CA  . TRP C 3 35  ? 278.117 247.122 312.439 1.00 37.17  ? 35  TRP L CA  1 
ATOM 2699 C C   . TRP C 3 35  ? 279.438 247.678 312.948 1.00 41.51  ? 35  TRP L C   1 
ATOM 2700 O O   . TRP C 3 35  ? 280.283 248.101 312.156 1.00 65.03  ? 35  TRP L O   1 
ATOM 2701 C CB  . TRP C 3 35  ? 278.308 245.718 311.864 1.00 54.77  ? 35  TRP L CB  1 
ATOM 2702 C CG  . TRP C 3 35  ? 277.018 244.994 311.643 1.00 56.15  ? 35  TRP L CG  1 
ATOM 2703 C CD1 . TRP C 3 35  ? 276.299 244.938 310.492 1.00 54.83  ? 35  TRP L CD1 1 
ATOM 2704 C CD2 . TRP C 3 35  ? 276.282 244.244 312.611 1.00 56.38  ? 35  TRP L CD2 1 
ATOM 2705 N NE1 . TRP C 3 35  ? 275.166 244.192 310.676 1.00 54.45  ? 35  TRP L NE1 1 
ATOM 2706 C CE2 . TRP C 3 35  ? 275.132 243.754 311.973 1.00 50.02  ? 35  TRP L CE2 1 
ATOM 2707 C CE3 . TRP C 3 35  ? 276.488 243.935 313.960 1.00 52.90  ? 35  TRP L CE3 1 
ATOM 2708 C CZ2 . TRP C 3 35  ? 274.192 242.971 312.632 1.00 48.70  ? 35  TRP L CZ2 1 
ATOM 2709 C CZ3 . TRP C 3 35  ? 275.554 243.160 314.611 1.00 52.08  ? 35  TRP L CZ3 1 
ATOM 2710 C CH2 . TRP C 3 35  ? 274.423 242.685 313.948 1.00 49.95  ? 35  TRP L CH2 1 
ATOM 2711 N N   . TYR C 3 36  ? 279.607 247.681 314.267 1.00 32.15  ? 36  TYR L N   1 
ATOM 2712 C CA  . TYR C 3 36  ? 280.796 248.213 314.915 1.00 36.92  ? 36  TYR L CA  1 
ATOM 2713 C C   . TYR C 3 36  ? 281.405 247.150 315.809 1.00 45.96  ? 36  TYR L C   1 
ATOM 2714 O O   . TYR C 3 36  ? 280.704 246.288 316.332 1.00 56.58  ? 36  TYR L O   1 
ATOM 2715 C CB  . TYR C 3 36  ? 280.531 249.461 315.784 1.00 44.30  ? 36  TYR L CB  1 
ATOM 2716 C CG  . TYR C 3 36  ? 279.821 250.616 315.124 1.00 52.34  ? 36  TYR L CG  1 
ATOM 2717 C CD1 . TYR C 3 36  ? 278.450 250.604 314.932 1.00 50.95  ? 36  TYR L CD1 1 
ATOM 2718 C CD2 . TYR C 3 36  ? 280.533 251.731 314.709 1.00 38.82  ? 36  TYR L CD2 1 
ATOM 2719 C CE1 . TYR C 3 36  ? 277.813 251.659 314.333 1.00 41.40  ? 36  TYR L CE1 1 
ATOM 2720 C CE2 . TYR C 3 36  ? 279.902 252.792 314.114 1.00 37.38  ? 36  TYR L CE2 1 
ATOM 2721 C CZ  . TYR C 3 36  ? 278.543 252.749 313.927 1.00 43.88  ? 36  TYR L CZ  1 
ATOM 2722 O OH  . TYR C 3 36  ? 277.904 253.805 313.331 1.00 51.82  ? 36  TYR L OH  1 
ATOM 2723 N N   . GLN C 3 37  ? 282.723 247.209 315.964 1.00 54.05  ? 37  GLN L N   1 
ATOM 2724 C CA  . GLN C 3 37  ? 283.448 246.354 316.895 1.00 47.68  ? 37  GLN L CA  1 
ATOM 2725 C C   . GLN C 3 37  ? 284.192 247.235 317.883 1.00 54.92  ? 37  GLN L C   1 
ATOM 2726 O O   . GLN C 3 37  ? 284.999 248.075 317.480 1.00 71.79  ? 37  GLN L O   1 
ATOM 2727 C CB  . GLN C 3 37  ? 284.426 245.436 316.163 1.00 63.40  ? 37  GLN L CB  1 
ATOM 2728 C CG  . GLN C 3 37  ? 285.090 244.412 317.061 1.00 69.13  ? 37  GLN L CG  1 
ATOM 2729 C CD  . GLN C 3 37  ? 286.454 244.000 316.563 1.00 63.76  ? 37  GLN L CD  1 
ATOM 2730 O OE1 . GLN C 3 37  ? 287.473 244.467 317.062 1.00 62.38  ? 37  GLN L OE1 1 
ATOM 2731 N NE2 . GLN C 3 37  ? 286.481 243.120 315.575 1.00 65.96  ? 37  GLN L NE2 1 
ATOM 2732 N N   . GLN C 3 38  ? 283.925 247.045 319.170 1.00 64.62  ? 38  GLN L N   1 
ATOM 2733 C CA  . GLN C 3 38  ? 284.576 247.818 320.218 1.00 64.48  ? 38  GLN L CA  1 
ATOM 2734 C C   . GLN C 3 38  ? 285.432 246.925 321.100 1.00 63.77  ? 38  GLN L C   1 
ATOM 2735 O O   . GLN C 3 38  ? 284.914 246.036 321.781 1.00 69.03  ? 38  GLN L O   1 
ATOM 2736 C CB  . GLN C 3 38  ? 283.557 248.545 321.093 1.00 60.99  ? 38  GLN L CB  1 
ATOM 2737 C CG  . GLN C 3 38  ? 284.160 249.717 321.827 1.00 53.34  ? 38  GLN L CG  1 
ATOM 2738 C CD  . GLN C 3 38  ? 283.149 250.521 322.595 1.00 56.62  ? 38  GLN L CD  1 
ATOM 2739 O OE1 . GLN C 3 38  ? 282.000 250.118 322.741 1.00 72.52  ? 38  GLN L OE1 1 
ATOM 2740 N NE2 . GLN C 3 38  ? 283.576 251.664 323.107 1.00 58.80  ? 38  GLN L NE2 1 
ATOM 2741 N N   . LYS C 3 39  ? 286.729 247.176 321.097 1.00 78.28  ? 39  LYS L N   1 
ATOM 2742 C CA  . LYS C 3 39  ? 287.641 246.519 322.008 1.00 75.19  ? 39  LYS L CA  1 
ATOM 2743 C C   . LYS C 3 39  ? 287.597 247.293 323.325 1.00 75.20  ? 39  LYS L C   1 
ATOM 2744 O O   . LYS C 3 39  ? 287.138 248.438 323.337 1.00 85.19  ? 39  LYS L O   1 
ATOM 2745 C CB  . LYS C 3 39  ? 289.039 246.497 321.392 1.00 71.77  ? 39  LYS L CB  1 
ATOM 2746 C CG  . LYS C 3 39  ? 289.110 245.705 320.100 1.00 73.63  ? 39  LYS L CG  1 
ATOM 2747 C CD  . LYS C 3 39  ? 290.535 245.354 319.737 1.00 72.71  ? 39  LYS L CD  1 
ATOM 2748 C CE  . LYS C 3 39  ? 290.596 244.648 318.394 1.00 78.33  ? 39  LYS L CE  1 
ATOM 2749 N NZ  . LYS C 3 39  ? 291.974 244.192 318.070 1.00 79.40  ? 39  LYS L NZ  1 
ATOM 2750 N N   . PRO C 3 40  ? 287.981 246.680 324.455 1.00 65.45  ? 40  PRO L N   1 
ATOM 2751 C CA  . PRO C 3 40  ? 287.885 247.389 325.746 1.00 72.82  ? 40  PRO L CA  1 
ATOM 2752 C C   . PRO C 3 40  ? 288.746 248.648 325.806 1.00 82.49  ? 40  PRO L C   1 
ATOM 2753 O O   . PRO C 3 40  ? 289.931 248.630 325.467 1.00 76.84  ? 40  PRO L O   1 
ATOM 2754 C CB  . PRO C 3 40  ? 288.337 246.338 326.765 1.00 77.37  ? 40  PRO L CB  1 
ATOM 2755 C CG  . PRO C 3 40  ? 288.111 245.047 326.098 1.00 75.04  ? 40  PRO L CG  1 
ATOM 2756 C CD  . PRO C 3 40  ? 288.369 245.271 324.656 1.00 72.83  ? 40  PRO L CD  1 
ATOM 2757 N N   . GLY C 3 41  ? 288.132 249.730 326.279 1.00 81.29  ? 41  GLY L N   1 
ATOM 2758 C CA  . GLY C 3 41  ? 288.770 251.036 326.387 1.00 76.96  ? 41  GLY L CA  1 
ATOM 2759 C C   . GLY C 3 41  ? 289.248 251.600 325.066 1.00 80.26  ? 41  GLY L C   1 
ATOM 2760 O O   . GLY C 3 41  ? 290.290 252.265 325.015 1.00 84.37  ? 41  GLY L O   1 
ATOM 2761 N N   . LYS C 3 42  ? 288.499 251.355 323.991 1.00 63.45  ? 42  LYS L N   1 
ATOM 2762 C CA  . LYS C 3 42  ? 288.843 251.827 322.659 1.00 62.31  ? 42  LYS L CA  1 
ATOM 2763 C C   . LYS C 3 42  ? 287.590 252.357 321.982 1.00 71.58  ? 42  LYS L C   1 
ATOM 2764 O O   . LYS C 3 42  ? 286.469 252.005 322.349 1.00 76.87  ? 42  LYS L O   1 
ATOM 2765 C CB  . LYS C 3 42  ? 289.464 250.720 321.795 1.00 65.28  ? 42  LYS L CB  1 
ATOM 2766 C CG  . LYS C 3 42  ? 290.796 250.186 322.289 1.00 75.10  ? 42  LYS L CG  1 
ATOM 2767 C CD  . LYS C 3 42  ? 291.895 251.216 322.144 1.00 73.18  ? 42  LYS L CD  1 
ATOM 2768 C CE  . LYS C 3 42  ? 293.261 250.582 322.332 1.00 70.71  ? 42  LYS L CE  1 
ATOM 2769 N NZ  . LYS C 3 42  ? 294.339 251.604 322.404 1.00 74.72  ? 42  LYS L NZ  1 
ATOM 2770 N N   . ALA C 3 43  ? 287.791 253.231 321.001 1.00 61.00  ? 43  ALA L N   1 
ATOM 2771 C CA  . ALA C 3 43  ? 286.675 253.750 320.232 1.00 60.29  ? 43  ALA L CA  1 
ATOM 2772 C C   . ALA C 3 43  ? 286.118 252.657 319.320 1.00 67.33  ? 43  ALA L C   1 
ATOM 2773 O O   . ALA C 3 43  ? 286.849 251.747 318.922 1.00 72.48  ? 43  ALA L O   1 
ATOM 2774 C CB  . ALA C 3 43  ? 287.118 254.951 319.400 1.00 60.69  ? 43  ALA L CB  1 
ATOM 2775 N N   . PRO C 3 44  ? 284.817 252.696 319.020 1.00 64.97  ? 44  PRO L N   1 
ATOM 2776 C CA  . PRO C 3 44  ? 284.241 251.728 318.076 1.00 51.33  ? 44  PRO L CA  1 
ATOM 2777 C C   . PRO C 3 44  ? 284.820 251.851 316.673 1.00 49.00  ? 44  PRO L C   1 
ATOM 2778 O O   . PRO C 3 44  ? 285.108 252.945 316.189 1.00 56.36  ? 44  PRO L O   1 
ATOM 2779 C CB  . PRO C 3 44  ? 282.747 252.059 318.098 1.00 51.60  ? 44  PRO L CB  1 
ATOM 2780 C CG  . PRO C 3 44  ? 282.536 252.737 319.388 1.00 47.16  ? 44  PRO L CG  1 
ATOM 2781 C CD  . PRO C 3 44  ? 283.772 253.508 319.664 1.00 56.86  ? 44  PRO L CD  1 
ATOM 2782 N N   . LYS C 3 45  ? 284.987 250.702 316.027 1.00 41.58  ? 45  LYS L N   1 
ATOM 2783 C CA  . LYS C 3 45  ? 285.498 250.601 314.669 1.00 50.68  ? 45  LYS L CA  1 
ATOM 2784 C C   . LYS C 3 45  ? 284.396 250.065 313.770 1.00 49.76  ? 45  LYS L C   1 
ATOM 2785 O O   . LYS C 3 45  ? 283.828 249.011 314.056 1.00 63.97  ? 45  LYS L O   1 
ATOM 2786 C CB  . LYS C 3 45  ? 286.716 249.680 314.626 1.00 46.52  ? 45  LYS L CB  1 
ATOM 2787 C CG  . LYS C 3 45  ? 287.289 249.444 313.250 1.00 57.47  ? 45  LYS L CG  1 
ATOM 2788 C CD  . LYS C 3 45  ? 288.375 248.392 313.304 1.00 45.80  ? 45  LYS L CD  1 
ATOM 2789 C CE  . LYS C 3 45  ? 289.536 248.749 312.398 1.00 53.27  ? 45  LYS L CE  1 
ATOM 2790 N NZ  . LYS C 3 45  ? 290.485 247.615 312.242 1.00 59.31  ? 45  LYS L NZ  1 
ATOM 2791 N N   . LEU C 3 46  ? 284.125 250.761 312.669 1.00 47.60  ? 46  LEU L N   1 
ATOM 2792 C CA  . LEU C 3 46  ? 282.999 250.429 311.796 1.00 45.80  ? 46  LEU L CA  1 
ATOM 2793 C C   . LEU C 3 46  ? 283.399 249.294 310.869 1.00 45.09  ? 46  LEU L C   1 
ATOM 2794 O O   . LEU C 3 46  ? 284.152 249.492 309.917 1.00 50.68  ? 46  LEU L O   1 
ATOM 2795 C CB  . LEU C 3 46  ? 282.561 251.642 310.989 1.00 51.49  ? 46  LEU L CB  1 
ATOM 2796 C CG  . LEU C 3 46  ? 281.404 251.376 310.034 1.00 40.25  ? 46  LEU L CG  1 
ATOM 2797 C CD1 . LEU C 3 46  ? 280.143 251.494 310.801 1.00 35.01  ? 46  LEU L CD1 1 
ATOM 2798 C CD2 . LEU C 3 46  ? 281.391 252.325 308.872 1.00 56.18  ? 46  LEU L CD2 1 
ATOM 2799 N N   . LEU C 3 47  ? 282.938 248.084 311.179 1.00 51.98  ? 47  LEU L N   1 
ATOM 2800 C CA  . LEU C 3 47  ? 283.206 246.946 310.309 1.00 49.95  ? 47  LEU L CA  1 
ATOM 2801 C C   . LEU C 3 47  ? 282.376 246.989 309.031 1.00 49.30  ? 47  LEU L C   1 
ATOM 2802 O O   . LEU C 3 47  ? 282.900 246.774 307.935 1.00 56.72  ? 47  LEU L O   1 
ATOM 2803 C CB  . LEU C 3 47  ? 282.920 245.651 311.055 1.00 48.11  ? 47  LEU L CB  1 
ATOM 2804 C CG  . LEU C 3 47  ? 283.683 245.396 312.342 1.00 46.15  ? 47  LEU L CG  1 
ATOM 2805 C CD1 . LEU C 3 47  ? 283.055 244.191 312.957 1.00 57.73  ? 47  LEU L CD1 1 
ATOM 2806 C CD2 . LEU C 3 47  ? 285.159 245.192 312.117 1.00 52.35  ? 47  LEU L CD2 1 
ATOM 2807 N N   . ILE C 3 48  ? 281.077 247.273 309.151 1.00 51.23  ? 48  ILE L N   1 
ATOM 2808 C CA  . ILE C 3 48  ? 280.132 247.175 308.043 1.00 51.45  ? 48  ILE L CA  1 
ATOM 2809 C C   . ILE C 3 48  ? 279.274 248.431 308.031 1.00 54.71  ? 48  ILE L C   1 
ATOM 2810 O O   . ILE C 3 48  ? 278.948 248.990 309.080 1.00 58.13  ? 48  ILE L O   1 
ATOM 2811 C CB  . ILE C 3 48  ? 279.211 245.912 308.182 1.00 57.57  ? 48  ILE L CB  1 
ATOM 2812 C CG1 . ILE C 3 48  ? 279.979 244.625 308.489 1.00 53.56  ? 48  ILE L CG1 1 
ATOM 2813 C CG2 . ILE C 3 48  ? 278.381 245.629 306.935 1.00 55.61  ? 48  ILE L CG2 1 
ATOM 2814 C CD1 . ILE C 3 48  ? 280.847 244.147 307.374 1.00 58.45  ? 48  ILE L CD1 1 
ATOM 2815 N N   . TYR C 3 49  ? 278.860 248.840 306.835 1.00 44.81  ? 49  TYR L N   1 
ATOM 2816 C CA  . TYR C 3 49  ? 277.932 249.938 306.629 1.00 41.99  ? 49  TYR L CA  1 
ATOM 2817 C C   . TYR C 3 49  ? 277.021 249.520 305.488 1.00 53.40  ? 49  TYR L C   1 
ATOM 2818 O O   . TYR C 3 49  ? 277.353 248.611 304.728 1.00 58.50  ? 49  TYR L O   1 
ATOM 2819 C CB  . TYR C 3 49  ? 278.653 251.270 306.336 1.00 55.44  ? 49  TYR L CB  1 
ATOM 2820 C CG  . TYR C 3 49  ? 279.376 251.346 305.007 1.00 52.75  ? 49  TYR L CG  1 
ATOM 2821 C CD1 . TYR C 3 49  ? 280.694 250.934 304.898 1.00 45.24  ? 49  TYR L CD1 1 
ATOM 2822 C CD2 . TYR C 3 49  ? 278.756 251.859 303.873 1.00 54.06  ? 49  TYR L CD2 1 
ATOM 2823 C CE1 . TYR C 3 49  ? 281.363 250.999 303.699 1.00 44.57  ? 49  TYR L CE1 1 
ATOM 2824 C CE2 . TYR C 3 49  ? 279.416 251.920 302.669 1.00 54.96  ? 49  TYR L CE2 1 
ATOM 2825 C CZ  . TYR C 3 49  ? 280.722 251.490 302.590 1.00 56.04  ? 49  TYR L CZ  1 
ATOM 2826 O OH  . TYR C 3 49  ? 281.394 251.554 301.396 1.00 67.24  ? 49  TYR L OH  1 
ATOM 2827 N N   . ALA C 3 50  ? 275.853 250.168 305.409 1.00 56.30  ? 50  ALA L N   1 
ATOM 2828 C CA  . ALA C 3 50  ? 274.833 249.936 304.375 1.00 56.75  ? 50  ALA L CA  1 
ATOM 2829 C C   . ALA C 3 50  ? 274.382 248.477 304.331 1.00 57.39  ? 50  ALA L C   1 
ATOM 2830 O O   . ALA C 3 50  ? 274.131 247.933 303.252 1.00 66.94  ? 50  ALA L O   1 
ATOM 2831 C CB  . ALA C 3 50  ? 275.307 250.396 302.992 1.00 67.71  ? 50  ALA L CB  1 
ATOM 2832 N N   . ALA C 3 51  ? 274.363 247.854 305.516 1.00 54.50  ? 51  ALA L N   1 
ATOM 2833 C CA  . ALA C 3 51  ? 273.984 246.485 305.873 1.00 54.25  ? 51  ALA L CA  1 
ATOM 2834 C C   . ALA C 3 51  ? 275.007 245.445 305.426 1.00 59.03  ? 51  ALA L C   1 
ATOM 2835 O O   . ALA C 3 51  ? 275.356 244.560 306.211 1.00 68.41  ? 51  ALA L O   1 
ATOM 2836 C CB  . ALA C 3 51  ? 272.593 246.119 305.341 1.00 63.54  ? 51  ALA L CB  1 
ATOM 2837 N N   . SER C 3 52  ? 275.486 245.516 304.179 1.00 54.47  ? 52  SER L N   1 
ATOM 2838 C CA  . SER C 3 52  ? 276.398 244.507 303.658 1.00 52.95  ? 52  SER L CA  1 
ATOM 2839 C C   . SER C 3 52  ? 277.746 245.024 303.165 1.00 56.95  ? 52  SER L C   1 
ATOM 2840 O O   . SER C 3 52  ? 278.606 244.204 302.829 1.00 55.05  ? 52  SER L O   1 
ATOM 2841 C CB  . SER C 3 52  ? 275.727 243.732 302.514 1.00 65.53  ? 52  SER L CB  1 
ATOM 2842 O OG  . SER C 3 52  ? 275.559 244.551 301.374 1.00 62.82  ? 52  SER L OG  1 
ATOM 2843 N N   . ARG C 3 53  ? 277.967 246.334 303.119 1.00 62.44  ? 53  ARG L N   1 
ATOM 2844 C CA  . ARG C 3 53  ? 279.187 246.898 302.544 1.00 56.88  ? 53  ARG L CA  1 
ATOM 2845 C C   . ARG C 3 53  ? 280.306 246.998 303.572 1.00 51.29  ? 53  ARG L C   1 
ATOM 2846 O O   . ARG C 3 53  ? 280.180 247.709 304.572 1.00 48.13  ? 53  ARG L O   1 
ATOM 2847 C CB  . ARG C 3 53  ? 278.928 248.257 301.900 1.00 54.75  ? 53  ARG L CB  1 
ATOM 2848 C CG  . ARG C 3 53  ? 278.464 248.144 300.468 1.00 60.65  ? 53  ARG L CG  1 
ATOM 2849 C CD  . ARG C 3 53  ? 279.298 249.051 299.591 1.00 62.66  ? 53  ARG L CD  1 
ATOM 2850 N NE  . ARG C 3 53  ? 278.818 249.127 298.218 1.00 62.56  ? 53  ARG L NE  1 
ATOM 2851 C CZ  . ARG C 3 53  ? 279.293 249.971 297.313 1.00 71.01  ? 53  ARG L CZ  1 
ATOM 2852 N NH1 . ARG C 3 53  ? 280.258 250.825 297.606 1.00 73.37  ? 53  ARG L NH1 1 
ATOM 2853 N NH2 . ARG C 3 53  ? 278.785 249.959 296.084 1.00 63.73  ? 53  ARG L NH2 1 
ATOM 2854 N N   . LEU C 3 54  ? 281.388 246.269 303.325 1.00 57.24  ? 54  LEU L N   1 
ATOM 2855 C CA  . LEU C 3 54  ? 282.546 246.281 304.206 1.00 65.45  ? 54  LEU L CA  1 
ATOM 2856 C C   . LEU C 3 54  ? 283.290 247.609 304.097 1.00 63.53  ? 54  LEU L C   1 
ATOM 2857 O O   . LEU C 3 54  ? 283.525 248.116 302.998 1.00 74.61  ? 54  LEU L O   1 
ATOM 2858 C CB  . LEU C 3 54  ? 283.493 245.146 303.813 1.00 66.06  ? 54  LEU L CB  1 
ATOM 2859 C CG  . LEU C 3 54  ? 284.650 244.699 304.708 1.00 69.32  ? 54  LEU L CG  1 
ATOM 2860 C CD1 . LEU C 3 54  ? 284.156 243.819 305.826 1.00 57.49  ? 54  LEU L CD1 1 
ATOM 2861 C CD2 . LEU C 3 54  ? 285.736 244.009 303.911 1.00 60.11  ? 54  LEU L CD2 1 
ATOM 2862 N N   . GLN C 3 55  ? 283.671 248.168 305.243 1.00 58.22  ? 55  GLN L N   1 
ATOM 2863 C CA  . GLN C 3 55  ? 284.461 249.393 305.260 1.00 55.93  ? 55  GLN L CA  1 
ATOM 2864 C C   . GLN C 3 55  ? 285.890 249.084 304.819 1.00 59.41  ? 55  GLN L C   1 
ATOM 2865 O O   . GLN C 3 55  ? 286.355 247.947 304.923 1.00 64.70  ? 55  GLN L O   1 
ATOM 2866 C CB  . GLN C 3 55  ? 284.417 250.025 306.662 1.00 50.21  ? 55  GLN L CB  1 
ATOM 2867 C CG  . GLN C 3 55  ? 285.141 251.371 306.873 1.00 66.05  ? 55  GLN L CG  1 
ATOM 2868 C CD  . GLN C 3 55  ? 284.514 252.548 306.146 1.00 67.54  ? 55  GLN L CD  1 
ATOM 2869 O OE1 . GLN C 3 55  ? 284.642 252.685 304.930 1.00 80.52  ? 55  GLN L OE1 1 
ATOM 2870 N NE2 . GLN C 3 55  ? 283.886 253.437 306.899 1.00 61.27  ? 55  GLN L NE2 1 
ATOM 2871 N N   . SER C 3 56  ? 286.565 250.091 304.260 1.00 69.87  ? 56  SER L N   1 
ATOM 2872 C CA  . SER C 3 56  ? 287.944 249.927 303.818 1.00 73.95  ? 56  SER L CA  1 
ATOM 2873 C C   . SER C 3 56  ? 288.865 249.658 305.002 1.00 75.32  ? 56  SER L C   1 
ATOM 2874 O O   . SER C 3 56  ? 288.737 250.271 306.065 1.00 76.91  ? 56  SER L O   1 
ATOM 2875 C CB  . SER C 3 56  ? 288.408 251.175 303.070 1.00 78.01  ? 56  SER L CB  1 
ATOM 2876 O OG  . SER C 3 56  ? 288.865 252.163 303.977 1.00 75.41  ? 56  SER L OG  1 
ATOM 2877 N N   . GLY C 3 57  ? 289.809 248.743 304.803 1.00 68.00  ? 57  GLY L N   1 
ATOM 2878 C CA  . GLY C 3 57  ? 290.763 248.388 305.832 1.00 71.06  ? 57  GLY L CA  1 
ATOM 2879 C C   . GLY C 3 57  ? 290.248 247.399 306.850 1.00 73.95  ? 57  GLY L C   1 
ATOM 2880 O O   . GLY C 3 57  ? 290.943 247.126 307.834 1.00 73.56  ? 57  GLY L O   1 
ATOM 2881 N N   . ILE C 3 58  ? 289.054 246.856 306.642 1.00 71.08  ? 58  ILE L N   1 
ATOM 2882 C CA  . ILE C 3 58  ? 288.449 245.869 307.531 1.00 71.80  ? 58  ILE L CA  1 
ATOM 2883 C C   . ILE C 3 58  ? 288.787 244.503 306.947 1.00 76.57  ? 58  ILE L C   1 
ATOM 2884 O O   . ILE C 3 58  ? 288.842 244.369 305.716 1.00 74.59  ? 58  ILE L O   1 
ATOM 2885 C CB  . ILE C 3 58  ? 286.934 246.115 307.657 1.00 66.98  ? 58  ILE L CB  1 
ATOM 2886 C CG1 . ILE C 3 58  ? 286.672 247.523 308.186 1.00 65.36  ? 58  ILE L CG1 1 
ATOM 2887 C CG2 . ILE C 3 58  ? 286.255 245.121 308.571 1.00 66.36  ? 58  ILE L CG2 1 
ATOM 2888 C CD1 . ILE C 3 58  ? 287.310 247.806 309.520 1.00 62.75  ? 58  ILE L CD1 1 
ATOM 2889 N N   . PRO C 3 59  ? 289.089 243.494 307.771 1.00 73.90  ? 59  PRO L N   1 
ATOM 2890 C CA  . PRO C 3 59  ? 289.308 242.140 307.243 1.00 64.19  ? 59  PRO L CA  1 
ATOM 2891 C C   . PRO C 3 59  ? 288.085 241.566 306.539 1.00 76.58  ? 59  PRO L C   1 
ATOM 2892 O O   . PRO C 3 59  ? 286.943 241.806 306.934 1.00 80.54  ? 59  PRO L O   1 
ATOM 2893 C CB  . PRO C 3 59  ? 289.671 241.336 308.491 1.00 67.49  ? 59  PRO L CB  1 
ATOM 2894 C CG  . PRO C 3 59  ? 290.263 242.338 309.403 1.00 73.79  ? 59  PRO L CG  1 
ATOM 2895 C CD  . PRO C 3 59  ? 289.472 243.582 309.191 1.00 75.98  ? 59  PRO L CD  1 
ATOM 2896 N N   . SER C 3 60  ? 288.355 240.796 305.479 1.00 74.29  ? 60  SER L N   1 
ATOM 2897 C CA  . SER C 3 60  ? 287.326 240.210 304.625 1.00 66.15  ? 60  SER L CA  1 
ATOM 2898 C C   . SER C 3 60  ? 286.435 239.203 305.343 1.00 72.16  ? 60  SER L C   1 
ATOM 2899 O O   . SER C 3 60  ? 285.351 238.899 304.831 1.00 75.84  ? 60  SER L O   1 
ATOM 2900 C CB  . SER C 3 60  ? 287.977 239.542 303.414 1.00 72.03  ? 60  SER L CB  1 
ATOM 2901 O OG  . SER C 3 60  ? 289.084 238.751 303.805 1.00 75.12  ? 60  SER L OG  1 
ATOM 2902 N N   . ARG C 3 61  ? 286.903 238.627 306.458 1.00 75.91  ? 61  ARG L N   1 
ATOM 2903 C CA  . ARG C 3 61  ? 286.137 237.621 307.196 1.00 67.61  ? 61  ARG L CA  1 
ATOM 2904 C C   . ARG C 3 61  ? 284.780 238.157 307.664 1.00 73.30  ? 61  ARG L C   1 
ATOM 2905 O O   . ARG C 3 61  ? 283.789 237.418 307.676 1.00 70.90  ? 61  ARG L O   1 
ATOM 2906 C CB  . ARG C 3 61  ? 286.973 237.085 308.367 1.00 71.33  ? 61  ARG L CB  1 
ATOM 2907 C CG  . ARG C 3 61  ? 287.320 238.081 309.467 1.00 71.48  ? 61  ARG L CG  1 
ATOM 2908 C CD  . ARG C 3 61  ? 288.161 237.465 310.554 1.00 70.25  ? 61  ARG L CD  1 
ATOM 2909 N NE  . ARG C 3 61  ? 289.115 238.396 311.141 1.00 79.08  ? 61  ARG L NE  1 
ATOM 2910 C CZ  . ARG C 3 61  ? 290.302 238.683 310.628 1.00 78.89  ? 61  ARG L CZ  1 
ATOM 2911 N NH1 . ARG C 3 61  ? 290.721 238.130 309.502 1.00 78.32  ? 61  ARG L NH1 1 
ATOM 2912 N NH2 . ARG C 3 61  ? 291.091 239.543 311.264 1.00 71.79  ? 61  ARG L NH2 1 
ATOM 2913 N N   . PHE C 3 62  ? 284.725 239.421 308.080 1.00 70.88  ? 62  PHE L N   1 
ATOM 2914 C CA  . PHE C 3 62  ? 283.476 240.049 308.484 1.00 62.32  ? 62  PHE L CA  1 
ATOM 2915 C C   . PHE C 3 62  ? 282.551 240.222 307.286 1.00 71.80  ? 62  PHE L C   1 
ATOM 2916 O O   . PHE C 3 62  ? 282.985 240.615 306.201 1.00 80.14  ? 62  PHE L O   1 
ATOM 2917 C CB  . PHE C 3 62  ? 283.762 241.401 309.130 1.00 62.95  ? 62  PHE L CB  1 
ATOM 2918 C CG  . PHE C 3 62  ? 284.576 241.310 310.383 1.00 68.27  ? 62  PHE L CG  1 
ATOM 2919 C CD1 . PHE C 3 62  ? 284.008 240.869 311.562 1.00 67.40  ? 62  PHE L CD1 1 
ATOM 2920 C CD2 . PHE C 3 62  ? 285.920 241.629 310.373 1.00 64.97  ? 62  PHE L CD2 1 
ATOM 2921 C CE1 . PHE C 3 62  ? 284.759 240.778 312.710 1.00 65.78  ? 62  PHE L CE1 1 
ATOM 2922 C CE2 . PHE C 3 62  ? 286.676 241.536 311.520 1.00 60.57  ? 62  PHE L CE2 1 
ATOM 2923 C CZ  . PHE C 3 62  ? 286.094 241.112 312.687 1.00 62.86  ? 62  PHE L CZ  1 
ATOM 2924 N N   . SER C 3 63  ? 281.273 239.912 307.479 1.00 65.94  ? 63  SER L N   1 
ATOM 2925 C CA  . SER C 3 63  ? 280.301 240.071 306.409 1.00 59.83  ? 63  SER L CA  1 
ATOM 2926 C C   . SER C 3 63  ? 278.953 240.426 307.013 1.00 65.91  ? 63  SER L C   1 
ATOM 2927 O O   . SER C 3 63  ? 278.659 240.080 308.157 1.00 72.68  ? 63  SER L O   1 
ATOM 2928 C CB  . SER C 3 63  ? 280.184 238.805 305.557 1.00 65.66  ? 63  SER L CB  1 
ATOM 2929 O OG  . SER C 3 63  ? 279.528 237.772 306.267 1.00 75.83  ? 63  SER L OG  1 
ATOM 2930 N N   . GLY C 3 64  ? 278.126 241.099 306.217 1.00 58.35  ? 64  GLY L N   1 
ATOM 2931 C CA  . GLY C 3 64  ? 276.817 241.512 306.661 1.00 60.57  ? 64  GLY L CA  1 
ATOM 2932 C C   . GLY C 3 64  ? 275.757 241.100 305.661 1.00 52.88  ? 64  GLY L C   1 
ATOM 2933 O O   . GLY C 3 64  ? 276.024 240.920 304.474 1.00 58.87  ? 64  GLY L O   1 
ATOM 2934 N N   . SER C 3 65  ? 274.535 240.960 306.164 1.00 61.29  ? 65  SER L N   1 
ATOM 2935 C CA  . SER C 3 65  ? 273.428 240.488 305.351 1.00 65.07  ? 65  SER L CA  1 
ATOM 2936 C C   . SER C 3 65  ? 272.124 241.006 305.933 1.00 61.26  ? 65  SER L C   1 
ATOM 2937 O O   . SER C 3 65  ? 272.073 241.500 307.060 1.00 69.70  ? 65  SER L O   1 
ATOM 2938 C CB  . SER C 3 65  ? 273.401 238.957 305.274 1.00 69.34  ? 65  SER L CB  1 
ATOM 2939 O OG  . SER C 3 65  ? 274.488 238.450 304.519 1.00 76.92  ? 65  SER L OG  1 
ATOM 2940 N N   . GLY C 3 66  ? 271.070 240.899 305.139 1.00 68.40  ? 66  GLY L N   1 
ATOM 2941 C CA  . GLY C 3 66  ? 269.736 241.248 305.571 1.00 71.88  ? 66  GLY L CA  1 
ATOM 2942 C C   . GLY C 3 66  ? 269.320 242.643 305.140 1.00 69.36  ? 66  GLY L C   1 
ATOM 2943 O O   . GLY C 3 66  ? 270.138 243.499 304.799 1.00 74.86  ? 66  GLY L O   1 
ATOM 2944 N N   . SER C 3 67  ? 268.010 242.863 305.162 1.00 73.73  ? 67  SER L N   1 
ATOM 2945 C CA  . SER C 3 67  ? 267.406 244.132 304.784 1.00 82.55  ? 67  SER L CA  1 
ATOM 2946 C C   . SER C 3 67  ? 266.063 244.229 305.489 1.00 80.82  ? 67  SER L C   1 
ATOM 2947 O O   . SER C 3 67  ? 265.573 243.254 306.063 1.00 82.15  ? 67  SER L O   1 
ATOM 2948 C CB  . SER C 3 67  ? 267.254 244.260 303.267 1.00 80.85  ? 67  SER L CB  1 
ATOM 2949 O OG  . SER C 3 67  ? 268.503 244.541 302.662 1.00 79.63  ? 67  SER L OG  1 
ATOM 2950 N N   . GLY C 3 68  ? 265.461 245.412 305.419 1.00 76.55  ? 68  GLY L N   1 
ATOM 2951 C CA  . GLY C 3 68  ? 264.215 245.655 306.116 1.00 76.94  ? 68  GLY L CA  1 
ATOM 2952 C C   . GLY C 3 68  ? 264.370 245.623 307.622 1.00 81.28  ? 68  GLY L C   1 
ATOM 2953 O O   . GLY C 3 68  ? 265.101 246.438 308.187 1.00 90.14  ? 68  GLY L O   1 
ATOM 2954 N N   . THR C 3 69  ? 263.641 244.735 308.292 1.00 85.33  ? 69  THR L N   1 
ATOM 2955 C CA  . THR C 3 69  ? 263.677 244.668 309.745 1.00 85.79  ? 69  THR L CA  1 
ATOM 2956 C C   . THR C 3 69  ? 264.657 243.636 310.295 1.00 82.52  ? 69  THR L C   1 
ATOM 2957 O O   . THR C 3 69  ? 264.857 243.594 311.513 1.00 85.33  ? 69  THR L O   1 
ATOM 2958 C CB  . THR C 3 69  ? 262.276 244.375 310.294 1.00 88.56  ? 69  THR L CB  1 
ATOM 2959 O OG1 . THR C 3 69  ? 261.646 243.371 309.491 1.00 89.07  ? 69  THR L OG1 1 
ATOM 2960 C CG2 . THR C 3 69  ? 261.427 245.631 310.265 1.00 88.08  ? 69  THR L CG2 1 
ATOM 2961 N N   . ASP C 3 70  ? 265.288 242.820 309.449 1.00 76.04  ? 70  ASP L N   1 
ATOM 2962 C CA  . ASP C 3 70  ? 266.132 241.724 309.918 1.00 78.70  ? 70  ASP L CA  1 
ATOM 2963 C C   . ASP C 3 70  ? 267.503 241.801 309.267 1.00 80.87  ? 70  ASP L C   1 
ATOM 2964 O O   . ASP C 3 70  ? 267.605 241.963 308.048 1.00 84.47  ? 70  ASP L O   1 
ATOM 2965 C CB  . ASP C 3 70  ? 265.500 240.361 309.609 1.00 81.32  ? 70  ASP L CB  1 
ATOM 2966 C CG  . ASP C 3 70  ? 264.503 239.923 310.660 1.00 83.08  ? 70  ASP L CG  1 
ATOM 2967 O OD1 . ASP C 3 70  ? 264.021 240.776 311.427 1.00 86.45  ? 70  ASP L OD1 1 
ATOM 2968 O OD2 . ASP C 3 70  ? 264.205 238.714 310.722 1.00 85.25  ? 70  ASP L OD2 1 
ATOM 2969 N N   . PHE C 3 71  ? 268.551 241.655 310.079 1.00 70.52  ? 71  PHE L N   1 
ATOM 2970 C CA  . PHE C 3 71  ? 269.930 241.755 309.617 1.00 67.76  ? 71  PHE L CA  1 
ATOM 2971 C C   . PHE C 3 71  ? 270.795 240.749 310.359 1.00 68.18  ? 71  PHE L C   1 
ATOM 2972 O O   . PHE C 3 71  ? 270.444 240.278 311.441 1.00 72.50  ? 71  PHE L O   1 
ATOM 2973 C CB  . PHE C 3 71  ? 270.541 243.141 309.815 1.00 64.89  ? 71  PHE L CB  1 
ATOM 2974 C CG  . PHE C 3 71  ? 269.782 244.265 309.164 1.00 70.73  ? 71  PHE L CG  1 
ATOM 2975 C CD1 . PHE C 3 71  ? 268.728 244.882 309.816 1.00 64.44  ? 71  PHE L CD1 1 
ATOM 2976 C CD2 . PHE C 3 71  ? 270.131 244.705 307.900 1.00 70.77  ? 71  PHE L CD2 1 
ATOM 2977 C CE1 . PHE C 3 71  ? 268.041 245.903 309.220 1.00 61.50  ? 71  PHE L CE1 1 
ATOM 2978 C CE2 . PHE C 3 71  ? 269.443 245.734 307.300 1.00 62.05  ? 71  PHE L CE2 1 
ATOM 2979 C CZ  . PHE C 3 71  ? 268.396 246.332 307.959 1.00 61.13  ? 71  PHE L CZ  1 
ATOM 2980 N N   . THR C 3 72  ? 271.951 240.445 309.774 1.00 65.28  ? 72  THR L N   1 
ATOM 2981 C CA  . THR C 3 72  ? 272.868 239.474 310.350 1.00 66.75  ? 72  THR L CA  1 
ATOM 2982 C C   . THR C 3 72  ? 274.310 239.894 310.074 1.00 67.25  ? 72  THR L C   1 
ATOM 2983 O O   . THR C 3 72  ? 274.608 240.436 309.009 1.00 75.24  ? 72  THR L O   1 
ATOM 2984 C CB  . THR C 3 72  ? 272.524 238.091 309.748 1.00 75.19  ? 72  THR L CB  1 
ATOM 2985 O OG1 . THR C 3 72  ? 271.332 237.582 310.362 1.00 78.05  ? 72  THR L OG1 1 
ATOM 2986 C CG2 . THR C 3 72  ? 273.634 237.056 309.868 1.00 70.54  ? 72  THR L CG2 1 
ATOM 2987 N N   . LEU C 3 73  ? 275.200 239.635 311.038 1.00 64.43  ? 73  LEU L N   1 
ATOM 2988 C CA  . LEU C 3 73  ? 276.638 239.829 310.893 1.00 61.71  ? 73  LEU L CA  1 
ATOM 2989 C C   . LEU C 3 73  ? 277.312 238.480 311.077 1.00 68.11  ? 73  LEU L C   1 
ATOM 2990 O O   . LEU C 3 73  ? 277.089 237.809 312.087 1.00 79.60  ? 73  LEU L O   1 
ATOM 2991 C CB  . LEU C 3 73  ? 277.184 240.821 311.921 1.00 63.23  ? 73  LEU L CB  1 
ATOM 2992 C CG  . LEU C 3 73  ? 278.708 240.949 312.010 1.00 66.24  ? 73  LEU L CG  1 
ATOM 2993 C CD1 . LEU C 3 73  ? 279.272 241.818 310.907 1.00 66.49  ? 73  LEU L CD1 1 
ATOM 2994 C CD2 . LEU C 3 73  ? 279.129 241.470 313.365 1.00 70.36  ? 73  LEU L CD2 1 
ATOM 2995 N N   . THR C 3 74  ? 278.143 238.089 310.116 1.00 71.69  ? 74  THR L N   1 
ATOM 2996 C CA  . THR C 3 74  ? 278.799 236.790 310.141 1.00 76.03  ? 74  THR L CA  1 
ATOM 2997 C C   . THR C 3 74  ? 280.309 236.935 310.033 1.00 75.59  ? 74  THR L C   1 
ATOM 2998 O O   . THR C 3 74  ? 280.807 237.702 309.205 1.00 76.77  ? 74  THR L O   1 
ATOM 2999 C CB  . THR C 3 74  ? 278.276 235.908 309.002 1.00 75.15  ? 74  THR L CB  1 
ATOM 3000 O OG1 . THR C 3 74  ? 276.847 235.998 308.948 1.00 80.29  ? 74  THR L OG1 1 
ATOM 3001 C CG2 . THR C 3 74  ? 278.668 234.459 309.219 1.00 77.85  ? 74  THR L CG2 1 
ATOM 3002 N N   . ILE C 3 75  ? 281.028 236.204 310.880 1.00 80.80  ? 75  ILE L N   1 
ATOM 3003 C CA  . ILE C 3 75  ? 282.481 236.100 310.826 1.00 81.74  ? 75  ILE L CA  1 
ATOM 3004 C C   . ILE C 3 75  ? 282.808 234.707 310.304 1.00 82.78  ? 75  ILE L C   1 
ATOM 3005 O O   . ILE C 3 75  ? 282.449 233.708 310.939 1.00 77.98  ? 75  ILE L O   1 
ATOM 3006 C CB  . ILE C 3 75  ? 283.120 236.344 312.199 1.00 81.20  ? 75  ILE L CB  1 
ATOM 3007 C CG1 . ILE C 3 75  ? 282.505 237.581 312.856 1.00 73.50  ? 75  ILE L CG1 1 
ATOM 3008 C CG2 . ILE C 3 75  ? 284.622 236.501 312.059 1.00 83.04  ? 75  ILE L CG2 1 
ATOM 3009 C CD1 . ILE C 3 75  ? 282.988 237.832 314.260 1.00 75.41  ? 75  ILE L CD1 1 
ATOM 3010 N N   . SER C 3 76  ? 283.441 234.641 309.126 1.00 90.64  ? 76  SER L N   1 
ATOM 3011 C CA  . SER C 3 76  ? 283.723 233.357 308.483 1.00 90.37  ? 76  SER L CA  1 
ATOM 3012 C C   . SER C 3 76  ? 284.691 232.511 309.303 1.00 93.51  ? 76  SER L C   1 
ATOM 3013 O O   . SER C 3 76  ? 284.470 231.312 309.504 1.00 97.14  ? 76  SER L O   1 
ATOM 3014 C CB  . SER C 3 76  ? 284.283 233.591 307.082 1.00 89.43  ? 76  SER L CB  1 
ATOM 3015 O OG  . SER C 3 76  ? 285.518 234.280 307.141 1.00 92.39  ? 76  SER L OG  1 
ATOM 3016 N N   . SER C 3 77  ? 285.769 233.118 309.785 1.00 90.32  ? 77  SER L N   1 
ATOM 3017 C CA  . SER C 3 77  ? 286.735 232.442 310.639 1.00 90.33  ? 77  SER L CA  1 
ATOM 3018 C C   . SER C 3 77  ? 287.049 233.358 311.807 1.00 91.28  ? 77  SER L C   1 
ATOM 3019 O O   . SER C 3 77  ? 287.439 234.508 311.603 1.00 91.78  ? 77  SER L O   1 
ATOM 3020 C CB  . SER C 3 77  ? 288.012 232.093 309.872 1.00 92.42  ? 77  SER L CB  1 
ATOM 3021 O OG  . SER C 3 77  ? 289.069 231.778 310.760 1.00 95.56  ? 77  SER L OG  1 
ATOM 3022 N N   . LEU C 3 78  ? 286.880 232.857 313.022 1.00 96.49  ? 78  LEU L N   1 
ATOM 3023 C CA  . LEU C 3 78  ? 287.158 233.678 314.186 1.00 93.12  ? 78  LEU L CA  1 
ATOM 3024 C C   . LEU C 3 78  ? 288.671 233.791 314.387 1.00 93.13  ? 78  LEU L C   1 
ATOM 3025 O O   . LEU C 3 78  ? 289.444 232.939 313.946 1.00 95.62  ? 78  LEU L O   1 
ATOM 3026 C CB  . LEU C 3 78  ? 286.467 233.078 315.407 1.00 95.36  ? 78  LEU L CB  1 
ATOM 3027 C CG  . LEU C 3 78  ? 286.236 233.914 316.656 1.00 93.64  ? 78  LEU L CG  1 
ATOM 3028 C CD1 . LEU C 3 78  ? 285.597 235.199 316.243 1.00 90.89  ? 78  LEU L CD1 1 
ATOM 3029 C CD2 . LEU C 3 78  ? 285.308 233.174 317.566 1.00 97.14  ? 78  LEU L CD2 1 
ATOM 3030 N N   . GLN C 3 79  ? 289.092 234.859 315.052 1.00 90.35  ? 79  GLN L N   1 
ATOM 3031 C CA  . GLN C 3 79  ? 290.492 235.142 315.333 1.00 89.80  ? 79  GLN L CA  1 
ATOM 3032 C C   . GLN C 3 79  ? 290.610 235.629 316.770 1.00 90.53  ? 79  GLN L C   1 
ATOM 3033 O O   . GLN C 3 79  ? 289.595 235.950 317.397 1.00 95.59  ? 79  GLN L O   1 
ATOM 3034 C CB  . GLN C 3 79  ? 291.052 236.205 314.366 1.00 87.45  ? 79  GLN L CB  1 
ATOM 3035 C CG  . GLN C 3 79  ? 290.762 236.037 312.883 1.00 92.20  ? 79  GLN L CG  1 
ATOM 3036 C CD  . GLN C 3 79  ? 291.405 234.808 312.268 1.00 92.50  ? 79  GLN L CD  1 
ATOM 3037 O OE1 . GLN C 3 79  ? 292.399 234.288 312.774 1.00 92.32  ? 79  GLN L OE1 1 
ATOM 3038 N NE2 . GLN C 3 79  ? 290.844 234.345 311.157 1.00 92.71  ? 79  GLN L NE2 1 
ATOM 3039 N N   . PRO C 3 80  ? 291.830 235.632 317.348 1.00 88.37  ? 80  PRO L N   1 
ATOM 3040 C CA  . PRO C 3 80  ? 291.993 236.235 318.688 1.00 93.14  ? 80  PRO L CA  1 
ATOM 3041 C C   . PRO C 3 80  ? 291.627 237.710 318.769 1.00 92.39  ? 80  PRO L C   1 
ATOM 3042 O O   . PRO C 3 80  ? 291.102 238.152 319.798 1.00 94.61  ? 80  PRO L O   1 
ATOM 3043 C CB  . PRO C 3 80  ? 293.474 235.986 319.006 1.00 94.70  ? 80  PRO L CB  1 
ATOM 3044 C CG  . PRO C 3 80  ? 293.811 234.790 318.227 1.00 90.99  ? 80  PRO L CG  1 
ATOM 3045 C CD  . PRO C 3 80  ? 293.057 234.910 316.953 1.00 90.59  ? 80  PRO L CD  1 
ATOM 3046 N N   . GLU C 3 81  ? 291.933 238.490 317.727 1.00 91.12  ? 81  GLU L N   1 
ATOM 3047 C CA  . GLU C 3 81  ? 291.600 239.913 317.713 1.00 93.24  ? 81  GLU L CA  1 
ATOM 3048 C C   . GLU C 3 81  ? 290.095 240.156 317.722 1.00 97.58  ? 81  GLU L C   1 
ATOM 3049 O O   . GLU C 3 81  ? 289.634 241.167 318.261 1.00 99.14  ? 81  GLU L O   1 
ATOM 3050 C CB  . GLU C 3 81  ? 292.233 240.584 316.495 1.00 94.05  ? 81  GLU L CB  1 
ATOM 3051 C CG  . GLU C 3 81  ? 293.730 240.794 316.615 1.00 94.67  ? 81  GLU L CG  1 
ATOM 3052 C CD  . GLU C 3 81  ? 294.526 239.594 316.148 1.00 97.12  ? 81  GLU L CD  1 
ATOM 3053 O OE1 . GLU C 3 81  ? 293.911 238.633 315.638 1.00 97.85  ? 81  GLU L OE1 1 
ATOM 3054 O OE2 . GLU C 3 81  ? 295.767 239.610 316.290 1.00 98.35  ? 81  GLU L OE2 1 
ATOM 3055 N N   . ASP C 3 82  ? 289.320 239.248 317.128 1.00 85.12  ? 82  ASP L N   1 
ATOM 3056 C CA  . ASP C 3 82  ? 287.877 239.406 316.973 1.00 82.54  ? 82  ASP L CA  1 
ATOM 3057 C C   . ASP C 3 82  ? 287.098 239.328 318.281 1.00 84.42  ? 82  ASP L C   1 
ATOM 3058 O O   . ASP C 3 82  ? 285.905 239.644 318.280 1.00 85.09  ? 82  ASP L O   1 
ATOM 3059 C CB  . ASP C 3 82  ? 287.343 238.367 315.999 1.00 85.54  ? 82  ASP L CB  1 
ATOM 3060 C CG  . ASP C 3 82  ? 287.977 238.469 314.635 1.00 88.00  ? 82  ASP L CG  1 
ATOM 3061 O OD1 . ASP C 3 82  ? 288.769 239.406 314.413 1.00 88.23  ? 82  ASP L OD1 1 
ATOM 3062 O OD2 . ASP C 3 82  ? 287.680 237.612 313.783 1.00 88.19  ? 82  ASP L OD2 1 
ATOM 3063 N N   . PHE C 3 83  ? 287.715 238.895 319.376 1.00 84.88  ? 83  PHE L N   1 
ATOM 3064 C CA  . PHE C 3 83  ? 287.024 238.725 320.654 1.00 82.83  ? 83  PHE L CA  1 
ATOM 3065 C C   . PHE C 3 83  ? 286.818 240.097 321.280 1.00 89.13  ? 83  PHE L C   1 
ATOM 3066 O O   . PHE C 3 83  ? 287.642 240.587 322.053 1.00 93.74  ? 83  PHE L O   1 
ATOM 3067 C CB  . PHE C 3 83  ? 287.819 237.807 321.570 1.00 86.50  ? 83  PHE L CB  1 
ATOM 3068 C CG  . PHE C 3 83  ? 287.880 236.392 321.095 1.00 91.35  ? 83  PHE L CG  1 
ATOM 3069 C CD1 . PHE C 3 83  ? 286.726 235.646 320.977 1.00 93.18  ? 83  PHE L CD1 1 
ATOM 3070 C CD2 . PHE C 3 83  ? 289.084 235.813 320.745 1.00 92.10  ? 83  PHE L CD2 1 
ATOM 3071 C CE1 . PHE C 3 83  ? 286.771 234.347 320.540 1.00 86.51  ? 83  PHE L CE1 1 
ATOM 3072 C CE2 . PHE C 3 83  ? 289.137 234.507 320.294 1.00 89.42  ? 83  PHE L CE2 1 
ATOM 3073 C CZ  . PHE C 3 83  ? 287.976 233.775 320.190 1.00 85.66  ? 83  PHE L CZ  1 
ATOM 3074 N N   . ALA C 3 84  ? 285.686 240.713 320.946 1.00 84.07  ? 84  ALA L N   1 
ATOM 3075 C CA  . ALA C 3 84  ? 285.358 242.062 321.382 1.00 80.44  ? 84  ALA L CA  1 
ATOM 3076 C C   . ALA C 3 84  ? 283.850 242.243 321.291 1.00 79.80  ? 84  ALA L C   1 
ATOM 3077 O O   . ALA C 3 84  ? 283.130 241.358 320.831 1.00 79.74  ? 84  ALA L O   1 
ATOM 3078 C CB  . ALA C 3 84  ? 286.089 243.110 320.539 1.00 73.00  ? 84  ALA L CB  1 
ATOM 3079 N N   . ALA C 3 85  ? 283.373 243.368 321.815 1.00 64.44  ? 85  ALA L N   1 
ATOM 3080 C CA  . ALA C 3 85  ? 281.961 243.714 321.721 1.00 61.48  ? 85  ALA L CA  1 
ATOM 3081 C C   . ALA C 3 85  ? 281.579 244.082 320.289 1.00 57.33  ? 85  ALA L C   1 
ATOM 3082 O O   . ALA C 3 85  ? 282.397 244.583 319.518 1.00 67.01  ? 85  ALA L O   1 
ATOM 3083 C CB  . ALA C 3 85  ? 281.633 244.867 322.665 1.00 65.65  ? 85  ALA L CB  1 
ATOM 3084 N N   . TYR C 3 86  ? 280.325 243.807 319.925 1.00 51.43  ? 86  TYR L N   1 
ATOM 3085 C CA  . TYR C 3 86  ? 279.806 244.138 318.605 1.00 51.89  ? 86  TYR L CA  1 
ATOM 3086 C C   . TYR C 3 86  ? 278.487 244.885 318.752 1.00 61.38  ? 86  TYR L C   1 
ATOM 3087 O O   . TYR C 3 86  ? 277.634 244.487 319.547 1.00 68.36  ? 86  TYR L O   1 
ATOM 3088 C CB  . TYR C 3 86  ? 279.598 242.888 317.738 1.00 62.77  ? 86  TYR L CB  1 
ATOM 3089 C CG  . TYR C 3 86  ? 280.883 242.236 317.284 1.00 62.97  ? 86  TYR L CG  1 
ATOM 3090 C CD1 . TYR C 3 86  ? 281.557 241.356 318.111 1.00 64.74  ? 86  TYR L CD1 1 
ATOM 3091 C CD2 . TYR C 3 86  ? 281.441 242.524 316.051 1.00 61.17  ? 86  TYR L CD2 1 
ATOM 3092 C CE1 . TYR C 3 86  ? 282.737 240.767 317.722 1.00 65.96  ? 86  TYR L CE1 1 
ATOM 3093 C CE2 . TYR C 3 86  ? 282.627 241.937 315.658 1.00 58.55  ? 86  TYR L CE2 1 
ATOM 3094 C CZ  . TYR C 3 86  ? 283.268 241.063 316.500 1.00 60.59  ? 86  TYR L CZ  1 
ATOM 3095 O OH  . TYR C 3 86  ? 284.445 240.468 316.122 1.00 65.41  ? 86  TYR L OH  1 
ATOM 3096 N N   . TYR C 3 87  ? 278.304 245.944 317.958 1.00 54.18  ? 87  TYR L N   1 
ATOM 3097 C CA  . TYR C 3 87  ? 277.129 246.805 318.041 1.00 55.20  ? 87  TYR L CA  1 
ATOM 3098 C C   . TYR C 3 87  ? 276.515 247.031 316.669 1.00 51.38  ? 87  TYR L C   1 
ATOM 3099 O O   . TYR C 3 87  ? 277.230 247.155 315.673 1.00 53.56  ? 87  TYR L O   1 
ATOM 3100 C CB  . TYR C 3 87  ? 277.477 248.165 318.660 1.00 60.05  ? 87  TYR L CB  1 
ATOM 3101 C CG  . TYR C 3 87  ? 278.010 248.088 320.065 1.00 59.30  ? 87  TYR L CG  1 
ATOM 3102 C CD1 . TYR C 3 87  ? 277.151 248.123 321.150 1.00 55.43  ? 87  TYR L CD1 1 
ATOM 3103 C CD2 . TYR C 3 87  ? 279.371 247.968 320.307 1.00 46.75  ? 87  TYR L CD2 1 
ATOM 3104 C CE1 . TYR C 3 87  ? 277.628 248.048 322.433 1.00 50.42  ? 87  TYR L CE1 1 
ATOM 3105 C CE2 . TYR C 3 87  ? 279.856 247.889 321.588 1.00 39.36  ? 87  TYR L CE2 1 
ATOM 3106 C CZ  . TYR C 3 87  ? 278.978 247.931 322.648 1.00 45.40  ? 87  TYR L CZ  1 
ATOM 3107 O OH  . TYR C 3 87  ? 279.454 247.858 323.934 1.00 60.92  ? 87  TYR L OH  1 
ATOM 3108 N N   . CYS C 3 88  ? 275.185 247.085 316.624 1.00 53.27  ? 88  CYS L N   1 
ATOM 3109 C CA  . CYS C 3 88  ? 274.434 247.382 315.408 1.00 59.23  ? 88  CYS L CA  1 
ATOM 3110 C C   . CYS C 3 88  ? 273.657 248.678 315.596 1.00 68.51  ? 88  CYS L C   1 
ATOM 3111 O O   . CYS C 3 88  ? 272.853 248.791 316.525 1.00 75.86  ? 88  CYS L O   1 
ATOM 3112 C CB  . CYS C 3 88  ? 273.494 246.233 315.040 1.00 68.45  ? 88  CYS L CB  1 
ATOM 3113 S SG  . CYS C 3 88  ? 272.437 245.609 316.363 1.00 83.02  ? 88  CYS L SG  1 
ATOM 3114 N N   . GLN C 3 89  ? 273.906 249.658 314.732 1.00 56.98  ? 89  GLN L N   1 
ATOM 3115 C CA  . GLN C 3 89  ? 273.273 250.967 314.829 1.00 46.30  ? 89  GLN L CA  1 
ATOM 3116 C C   . GLN C 3 89  ? 272.518 251.307 313.554 1.00 46.03  ? 89  GLN L C   1 
ATOM 3117 O O   . GLN C 3 89  ? 273.090 251.261 312.462 1.00 57.79  ? 89  GLN L O   1 
ATOM 3118 C CB  . GLN C 3 89  ? 274.306 252.055 315.100 1.00 65.87  ? 89  GLN L CB  1 
ATOM 3119 C CG  . GLN C 3 89  ? 273.705 253.429 315.267 1.00 63.05  ? 89  GLN L CG  1 
ATOM 3120 C CD  . GLN C 3 89  ? 274.629 254.524 314.812 1.00 51.82  ? 89  GLN L CD  1 
ATOM 3121 O OE1 . GLN C 3 89  ? 275.317 254.391 313.804 1.00 49.61  ? 89  GLN L OE1 1 
ATOM 3122 N NE2 . GLN C 3 89  ? 274.643 255.624 315.546 1.00 52.69  ? 89  GLN L NE2 1 
ATOM 3123 N N   . GLN C 3 90  ? 271.236 251.635 313.690 1.00 51.40  ? 90  GLN L N   1 
ATOM 3124 C CA  . GLN C 3 90  ? 270.458 252.095 312.550 1.00 58.29  ? 90  GLN L CA  1 
ATOM 3125 C C   . GLN C 3 90  ? 270.766 253.563 312.281 1.00 70.49  ? 90  GLN L C   1 
ATOM 3126 O O   . GLN C 3 90  ? 270.956 254.354 313.209 1.00 82.75  ? 90  GLN L O   1 
ATOM 3127 C CB  . GLN C 3 90  ? 268.958 251.898 312.783 1.00 56.34  ? 90  GLN L CB  1 
ATOM 3128 C CG  . GLN C 3 90  ? 268.374 252.586 314.007 1.00 63.74  ? 90  GLN L CG  1 
ATOM 3129 C CD  . GLN C 3 90  ? 267.717 253.908 313.671 1.00 64.65  ? 90  GLN L CD  1 
ATOM 3130 O OE1 . GLN C 3 90  ? 267.517 254.232 312.505 1.00 54.58  ? 90  GLN L OE1 1 
ATOM 3131 N NE2 . GLN C 3 90  ? 267.381 254.678 314.694 1.00 67.38  ? 90  GLN L NE2 1 
ATOM 3132 N N   . VAL C 3 91  ? 270.862 253.921 311.004 1.00 67.24  ? 91  VAL L N   1 
ATOM 3133 C CA  . VAL C 3 91  ? 271.065 255.308 310.612 1.00 62.89  ? 91  VAL L CA  1 
ATOM 3134 C C   . VAL C 3 91  ? 269.901 255.883 309.817 1.00 65.14  ? 91  VAL L C   1 
ATOM 3135 O O   . VAL C 3 91  ? 269.989 257.024 309.366 1.00 73.93  ? 91  VAL L O   1 
ATOM 3136 C CB  . VAL C 3 91  ? 272.398 255.502 309.858 1.00 53.88  ? 91  VAL L CB  1 
ATOM 3137 C CG1 . VAL C 3 91  ? 273.553 255.431 310.831 1.00 53.87  ? 91  VAL L CG1 1 
ATOM 3138 C CG2 . VAL C 3 91  ? 272.586 254.452 308.812 1.00 59.99  ? 91  VAL L CG2 1 
ATOM 3139 N N   . TYR C 3 92  ? 268.841 255.105 309.575 1.00 58.34  ? 92  TYR L N   1 
ATOM 3140 C CA  . TYR C 3 92  ? 267.713 255.579 308.772 1.00 61.51  ? 92  TYR L CA  1 
ATOM 3141 C C   . TYR C 3 92  ? 266.958 256.727 309.441 1.00 61.65  ? 92  TYR L C   1 
ATOM 3142 O O   . TYR C 3 92  ? 266.658 257.741 308.802 1.00 73.58  ? 92  TYR L O   1 
ATOM 3143 C CB  . TYR C 3 92  ? 266.766 254.409 308.500 1.00 67.03  ? 92  TYR L CB  1 
ATOM 3144 C CG  . TYR C 3 92  ? 265.400 254.774 307.969 1.00 70.86  ? 92  TYR L CG  1 
ATOM 3145 C CD1 . TYR C 3 92  ? 265.229 255.171 306.652 1.00 68.47  ? 92  TYR L CD1 1 
ATOM 3146 C CD2 . TYR C 3 92  ? 264.277 254.700 308.781 1.00 72.16  ? 92  TYR L CD2 1 
ATOM 3147 C CE1 . TYR C 3 92  ? 263.982 255.500 306.161 1.00 70.13  ? 92  TYR L CE1 1 
ATOM 3148 C CE2 . TYR C 3 92  ? 263.027 255.027 308.301 1.00 72.44  ? 92  TYR L CE2 1 
ATOM 3149 C CZ  . TYR C 3 92  ? 262.885 255.425 306.990 1.00 72.22  ? 92  TYR L CZ  1 
ATOM 3150 O OH  . TYR C 3 92  ? 261.638 255.747 306.506 1.00 70.85  ? 92  TYR L OH  1 
ATOM 3151 N N   . SER C 3 93  ? 266.660 256.593 310.728 1.00 76.97  ? 93  SER L N   1 
ATOM 3152 C CA  . SER C 3 93  ? 265.878 257.583 311.452 1.00 82.64  ? 93  SER L CA  1 
ATOM 3153 C C   . SER C 3 93  ? 266.739 258.769 311.847 1.00 75.08  ? 93  SER L C   1 
ATOM 3154 O O   . SER C 3 93  ? 267.967 258.690 311.861 1.00 78.91  ? 93  SER L O   1 
ATOM 3155 C CB  . SER C 3 93  ? 265.254 256.978 312.704 1.00 88.78  ? 93  SER L CB  1 
ATOM 3156 O OG  . SER C 3 93  ? 264.158 257.753 313.157 1.00 83.52  ? 93  SER L OG  1 
ATOM 3157 N N   . ALA C 3 94  ? 266.080 259.899 312.106 1.00 74.58  ? 94  ALA L N   1 
ATOM 3158 C CA  . ALA C 3 94  ? 266.804 261.059 312.619 1.00 76.45  ? 94  ALA L CA  1 
ATOM 3159 C C   . ALA C 3 94  ? 267.455 260.798 313.983 1.00 74.41  ? 94  ALA L C   1 
ATOM 3160 O O   . ALA C 3 94  ? 268.623 261.191 314.144 1.00 79.33  ? 94  ALA L O   1 
ATOM 3161 C CB  . ALA C 3 94  ? 265.890 262.295 312.627 1.00 76.83  ? 94  ALA L CB  1 
ATOM 3162 N N   . PRO C 3 95  ? 266.794 260.167 315.014 1.00 74.28  ? 95  PRO L N   1 
ATOM 3163 C CA  . PRO C 3 95  ? 267.585 259.797 316.196 1.00 74.36  ? 95  PRO L CA  1 
ATOM 3164 C C   . PRO C 3 95  ? 268.182 258.402 316.057 1.00 79.52  ? 95  PRO L C   1 
ATOM 3165 O O   . PRO C 3 95  ? 267.456 257.404 316.053 1.00 81.76  ? 95  PRO L O   1 
ATOM 3166 C CB  . PRO C 3 95  ? 266.579 259.884 317.349 1.00 68.32  ? 95  PRO L CB  1 
ATOM 3167 C CG  . PRO C 3 95  ? 265.265 259.678 316.746 1.00 77.98  ? 95  PRO L CG  1 
ATOM 3168 C CD  . PRO C 3 95  ? 265.353 259.954 315.272 1.00 79.15  ? 95  PRO L CD  1 
ATOM 3169 N N   . LEU C 3 96  ? 269.506 258.320 315.950 1.00 80.62  ? 96  LEU L N   1 
ATOM 3170 C CA  . LEU C 3 96  ? 270.165 257.036 315.754 1.00 63.25  ? 96  LEU L CA  1 
ATOM 3171 C C   . LEU C 3 96  ? 270.160 256.247 317.056 1.00 59.64  ? 96  LEU L C   1 
ATOM 3172 O O   . LEU C 3 96  ? 270.343 256.808 318.137 1.00 59.51  ? 96  LEU L O   1 
ATOM 3173 C CB  . LEU C 3 96  ? 271.594 257.243 315.257 1.00 64.10  ? 96  LEU L CB  1 
ATOM 3174 C CG  . LEU C 3 96  ? 271.855 258.316 314.189 1.00 66.78  ? 96  LEU L CG  1 
ATOM 3175 C CD1 . LEU C 3 96  ? 273.326 258.328 313.794 1.00 77.09  ? 96  LEU L CD1 1 
ATOM 3176 C CD2 . LEU C 3 96  ? 270.994 258.156 312.970 1.00 56.32  ? 96  LEU L CD2 1 
ATOM 3177 N N   . THR C 3 97  ? 269.920 254.942 316.959 1.00 57.07  ? 97  THR L N   1 
ATOM 3178 C CA  . THR C 3 97  ? 269.919 254.056 318.117 1.00 63.38  ? 97  THR L CA  1 
ATOM 3179 C C   . THR C 3 97  ? 270.869 252.888 317.906 1.00 61.84  ? 97  THR L C   1 
ATOM 3180 O O   . THR C 3 97  ? 270.854 252.257 316.846 1.00 62.69  ? 97  THR L O   1 
ATOM 3181 C CB  . THR C 3 97  ? 268.512 253.523 318.427 1.00 66.70  ? 97  THR L CB  1 
ATOM 3182 O OG1 . THR C 3 97  ? 267.995 252.829 317.288 1.00 59.60  ? 97  THR L OG1 1 
ATOM 3183 C CG2 . THR C 3 97  ? 267.569 254.651 318.816 1.00 62.23  ? 97  THR L CG2 1 
ATOM 3184 N N   . PHE C 3 98  ? 271.690 252.607 318.911 1.00 50.43  ? 98  PHE L N   1 
ATOM 3185 C CA  . PHE C 3 98  ? 272.628 251.499 318.859 1.00 48.28  ? 98  PHE L CA  1 
ATOM 3186 C C   . PHE C 3 98  ? 271.966 250.234 319.392 1.00 51.90  ? 98  PHE L C   1 
ATOM 3187 O O   . PHE C 3 98  ? 270.920 250.275 320.041 1.00 54.04  ? 98  PHE L O   1 
ATOM 3188 C CB  . PHE C 3 98  ? 273.871 251.790 319.699 1.00 64.33  ? 98  PHE L CB  1 
ATOM 3189 C CG  . PHE C 3 98  ? 274.882 252.655 319.021 1.00 60.81  ? 98  PHE L CG  1 
ATOM 3190 C CD1 . PHE C 3 98  ? 274.826 254.029 319.145 1.00 51.46  ? 98  PHE L CD1 1 
ATOM 3191 C CD2 . PHE C 3 98  ? 275.910 252.092 318.287 1.00 56.53  ? 98  PHE L CD2 1 
ATOM 3192 C CE1 . PHE C 3 98  ? 275.761 254.826 318.530 1.00 50.03  ? 98  PHE L CE1 1 
ATOM 3193 C CE2 . PHE C 3 98  ? 276.848 252.885 317.669 1.00 50.72  ? 98  PHE L CE2 1 
ATOM 3194 C CZ  . PHE C 3 98  ? 276.773 254.253 317.790 1.00 56.26  ? 98  PHE L CZ  1 
ATOM 3195 N N   . GLY C 3 99  ? 272.592 249.101 319.107 1.00 69.69  ? 99  GLY L N   1 
ATOM 3196 C CA  . GLY C 3 99  ? 272.124 247.846 319.645 1.00 72.48  ? 99  GLY L CA  1 
ATOM 3197 C C   . GLY C 3 99  ? 272.649 247.625 321.045 1.00 72.53  ? 99  GLY L C   1 
ATOM 3198 O O   . GLY C 3 99  ? 273.489 248.383 321.531 1.00 63.44  ? 99  GLY L O   1 
ATOM 3199 N N   . GLY C 3 100 ? 272.089 246.610 321.705 1.00 80.45  ? 100 GLY L N   1 
ATOM 3200 C CA  . GLY C 3 100 ? 272.506 246.178 323.028 1.00 77.06  ? 100 GLY L CA  1 
ATOM 3201 C C   . GLY C 3 100 ? 273.990 245.901 323.140 1.00 75.51  ? 100 GLY L C   1 
ATOM 3202 O O   . GLY C 3 100 ? 274.680 246.472 323.989 1.00 72.83  ? 100 GLY L O   1 
ATOM 3203 N N   . GLY C 3 101 ? 274.483 245.005 322.294 1.00 78.58  ? 101 GLY L N   1 
ATOM 3204 C CA  . GLY C 3 101 ? 275.888 244.624 322.309 1.00 75.86  ? 101 GLY L CA  1 
ATOM 3205 C C   . GLY C 3 101 ? 276.056 243.128 322.481 1.00 82.07  ? 101 GLY L C   1 
ATOM 3206 O O   . GLY C 3 101 ? 275.410 242.491 323.311 1.00 86.15  ? 101 GLY L O   1 
ATOM 3207 N N   . THR C 3 102 ? 276.940 242.556 321.670 1.00 77.32  ? 102 THR L N   1 
ATOM 3208 C CA  . THR C 3 102 ? 277.265 241.140 321.730 1.00 75.43  ? 102 THR L CA  1 
ATOM 3209 C C   . THR C 3 102 ? 278.755 240.992 321.982 1.00 79.65  ? 102 THR L C   1 
ATOM 3210 O O   . THR C 3 102 ? 279.567 241.522 321.221 1.00 87.05  ? 102 THR L O   1 
ATOM 3211 C CB  . THR C 3 102 ? 276.874 240.442 320.421 1.00 77.99  ? 102 THR L CB  1 
ATOM 3212 O OG1 . THR C 3 102 ? 275.449 240.325 320.337 1.00 73.42  ? 102 THR L OG1 1 
ATOM 3213 C CG2 . THR C 3 102 ? 277.525 239.071 320.293 1.00 82.60  ? 102 THR L CG2 1 
ATOM 3214 N N   . LYS C 3 103 ? 279.115 240.251 323.024 1.00 84.13  ? 103 LYS L N   1 
ATOM 3215 C CA  . LYS C 3 103 ? 280.514 240.078 323.402 1.00 81.14  ? 103 LYS L CA  1 
ATOM 3216 C C   . LYS C 3 103 ? 280.975 238.694 322.965 1.00 88.47  ? 103 LYS L C   1 
ATOM 3217 O O   . LYS C 3 103 ? 280.678 237.698 323.626 1.00 88.00  ? 103 LYS L O   1 
ATOM 3218 C CB  . LYS C 3 103 ? 280.710 240.273 324.900 1.00 83.57  ? 103 LYS L CB  1 
ATOM 3219 C CG  . LYS C 3 103 ? 282.168 240.413 325.289 1.00 92.10  ? 103 LYS L CG  1 
ATOM 3220 C CD  . LYS C 3 103 ? 282.340 240.571 326.784 1.00 88.00  ? 103 LYS L CD  1 
ATOM 3221 C CE  . LYS C 3 103 ? 283.807 240.501 327.169 1.00 91.17  ? 103 LYS L CE  1 
ATOM 3222 N NZ  . LYS C 3 103 ? 283.994 240.488 328.647 1.00 89.68  ? 103 LYS L NZ  1 
ATOM 3223 N N   . VAL C 3 104 ? 281.698 238.628 321.849 1.00 89.14  ? 104 VAL L N   1 
ATOM 3224 C CA  . VAL C 3 104 ? 282.290 237.365 321.431 1.00 87.76  ? 104 VAL L CA  1 
ATOM 3225 C C   . VAL C 3 104 ? 283.454 237.053 322.360 1.00 93.23  ? 104 VAL L C   1 
ATOM 3226 O O   . VAL C 3 104 ? 284.358 237.878 322.546 1.00 95.61  ? 104 VAL L O   1 
ATOM 3227 C CB  . VAL C 3 104 ? 282.730 237.436 319.962 1.00 85.47  ? 104 VAL L CB  1 
ATOM 3228 C CG1 . VAL C 3 104 ? 283.454 236.175 319.562 1.00 85.87  ? 104 VAL L CG1 1 
ATOM 3229 C CG2 . VAL C 3 104 ? 281.524 237.645 319.075 1.00 87.33  ? 104 VAL L CG2 1 
ATOM 3230 N N   . GLU C 3 105 ? 283.439 235.861 322.955 1.00 100.85 ? 105 GLU L N   1 
ATOM 3231 C CA  . GLU C 3 105 ? 284.412 235.482 323.969 1.00 99.31  ? 105 GLU L CA  1 
ATOM 3232 C C   . GLU C 3 105 ? 285.018 234.128 323.636 1.00 104.19 ? 105 GLU L C   1 
ATOM 3233 O O   . GLU C 3 105 ? 284.367 233.268 323.037 1.00 103.34 ? 105 GLU L O   1 
ATOM 3234 C CB  . GLU C 3 105 ? 283.783 235.426 325.368 1.00 95.01  ? 105 GLU L CB  1 
ATOM 3235 C CG  . GLU C 3 105 ? 283.118 236.716 325.814 1.00 98.91  ? 105 GLU L CG  1 
ATOM 3236 C CD  . GLU C 3 105 ? 282.620 236.655 327.243 1.00 101.64 ? 105 GLU L CD  1 
ATOM 3237 O OE1 . GLU C 3 105 ? 283.428 236.885 328.167 1.00 102.03 ? 105 GLU L OE1 1 
ATOM 3238 O OE2 . GLU C 3 105 ? 281.420 236.374 327.441 1.00 104.18 ? 105 GLU L OE2 1 
ATOM 3239 N N   . PHE C 3 106 ? 286.286 233.966 324.011 1.00 104.01 ? 106 PHE L N   1 
ATOM 3240 C CA  . PHE C 3 106 ? 287.003 232.718 323.785 1.00 103.34 ? 106 PHE L CA  1 
ATOM 3241 C C   . PHE C 3 106 ? 286.397 231.584 324.603 1.00 102.13 ? 106 PHE L C   1 
ATOM 3242 O O   . PHE C 3 106 ? 285.977 231.773 325.747 1.00 104.44 ? 106 PHE L O   1 
ATOM 3243 C CB  . PHE C 3 106 ? 288.484 232.890 324.118 1.00 102.22 ? 106 PHE L CB  1 
ATOM 3244 C CG  . PHE C 3 106 ? 289.310 231.669 323.834 1.00 107.40 ? 106 PHE L CG  1 
ATOM 3245 C CD1 . PHE C 3 106 ? 289.516 231.248 322.527 1.00 105.84 ? 106 PHE L CD1 1 
ATOM 3246 C CD2 . PHE C 3 106 ? 289.882 230.943 324.868 1.00 104.64 ? 106 PHE L CD2 1 
ATOM 3247 C CE1 . PHE C 3 106 ? 290.275 230.124 322.255 1.00 103.58 ? 106 PHE L CE1 1 
ATOM 3248 C CE2 . PHE C 3 106 ? 290.644 229.816 324.603 1.00 103.47 ? 106 PHE L CE2 1 
ATOM 3249 C CZ  . PHE C 3 106 ? 290.840 229.408 323.294 1.00 104.59 ? 106 PHE L CZ  1 
ATOM 3250 N N   . LYS C 3 107 ? 286.347 230.400 324.002 1.00 99.80  ? 107 LYS L N   1 
ATOM 3251 C CA  . LYS C 3 107 ? 285.759 229.226 324.635 1.00 100.09 ? 107 LYS L CA  1 
ATOM 3252 C C   . LYS C 3 107 ? 286.824 228.253 325.134 1.00 100.71 ? 107 LYS L C   1 
ATOM 3253 O O   . LYS C 3 107 ? 287.823 227.997 324.462 1.00 99.95  ? 107 LYS L O   1 
ATOM 3254 C CB  . LYS C 3 107 ? 284.832 228.519 323.646 1.00 100.92 ? 107 LYS L CB  1 
ATOM 3255 C CG  . LYS C 3 107 ? 283.635 227.828 324.261 1.00 99.25  ? 107 LYS L CG  1 
ATOM 3256 C CD  . LYS C 3 107 ? 282.680 227.375 323.169 1.00 99.57  ? 107 LYS L CD  1 
ATOM 3257 C CE  . LYS C 3 107 ? 281.877 226.160 323.588 1.00 103.51 ? 107 LYS L CE  1 
ATOM 3258 N NZ  . LYS C 3 107 ? 281.050 225.651 322.461 1.00 104.56 ? 107 LYS L NZ  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   . THR A 1   ? 703.6859 703.6859 703.6859 0.0000 0.0000 0.0000 333 THR I N   
2    C CA  . THR A 1   ? 703.1590 703.1590 703.1590 0.0000 0.0000 0.0000 333 THR I CA  
3    C C   . THR A 1   ? 701.1988 701.1988 701.1988 0.0000 0.0000 0.0000 333 THR I C   
4    O O   . THR A 1   ? 701.3428 701.3428 701.3428 0.0000 0.0000 0.0000 333 THR I O   
5    C CB  . THR A 1   ? 703.9597 703.9597 703.9597 0.0000 0.0000 0.0000 333 THR I CB  
6    O OG1 . THR A 1   ? 704.0749 704.0749 704.0749 0.0000 0.0000 0.0000 333 THR I OG1 
7    C CG2 . THR A 1   ? 704.1868 704.1868 704.1868 0.0000 0.0000 0.0000 333 THR I CG2 
8    N N   . ASN A 2   ? 626.7836 626.7836 626.7836 0.0000 0.0000 0.0000 334 ASN I N   
9    C CA  . ASN A 2   ? 624.3407 624.3407 624.3407 0.0000 0.0000 0.0000 334 ASN I CA  
10   C C   . ASN A 2   ? 622.2734 622.2734 622.2734 0.0000 0.0000 0.0000 334 ASN I C   
11   O O   . ASN A 2   ? 621.8472 621.8472 621.8472 0.0000 0.0000 0.0000 334 ASN I O   
12   C CB  . ASN A 2   ? 623.6772 623.6772 623.6772 0.0000 0.0000 0.0000 334 ASN I CB  
13   C CG  . ASN A 2   ? 623.2973 623.2973 623.2973 0.0000 0.0000 0.0000 334 ASN I CG  
14   O OD1 . ASN A 2   ? 623.2910 623.2910 623.2910 0.0000 0.0000 0.0000 334 ASN I OD1 
15   N ND2 . ASN A 2   ? 623.0043 623.0043 623.0043 0.0000 0.0000 0.0000 334 ASN I ND2 
16   N N   . LEU A 3   ? 597.0226 597.0226 597.0226 0.0000 0.0000 0.0000 335 LEU I N   
17   C CA  . LEU A 3   ? 595.3188 595.3188 595.3188 0.0000 0.0000 0.0000 335 LEU I CA  
18   C C   . LEU A 3   ? 593.8643 593.8643 593.8643 0.0000 0.0000 0.0000 335 LEU I C   
19   O O   . LEU A 3   ? 594.4779 594.4779 594.4779 0.0000 0.0000 0.0000 335 LEU I O   
20   C CB  . LEU A 3   ? 595.9834 595.9834 595.9834 0.0000 0.0000 0.0000 335 LEU I CB  
21   C CG  . LEU A 3   ? 596.5179 596.5179 596.5179 0.0000 0.0000 0.0000 335 LEU I CG  
22   C CD1 . LEU A 3   ? 596.2821 596.2821 596.2821 0.0000 0.0000 0.0000 335 LEU I CD1 
23   C CD2 . LEU A 3   ? 595.4132 595.4132 595.4132 0.0000 0.0000 0.0000 335 LEU I CD2 
24   N N   . CYS A 4   ? 571.7012 571.7012 571.7012 0.0000 0.0000 0.0000 336 CYS I N   
25   C CA  . CYS A 4   ? 569.5313 569.5313 569.5313 0.0000 0.0000 0.0000 336 CYS I CA  
26   C C   . CYS A 4   ? 567.4570 567.4570 567.4570 0.0000 0.0000 0.0000 336 CYS I C   
27   O O   . CYS A 4   ? 568.0994 568.0994 568.0994 0.0000 0.0000 0.0000 336 CYS I O   
28   C CB  . CYS A 4   ? 568.8259 568.8259 568.8259 0.0000 0.0000 0.0000 336 CYS I CB  
29   S SG  . CYS A 4   ? 570.8853 570.8853 570.8853 0.0000 0.0000 0.0000 336 CYS I SG  
30   N N   . PRO A 5   ? 505.4123 505.4123 505.4123 0.0000 0.0000 0.0000 337 PRO I N   
31   C CA  . PRO A 5   ? 502.2816 502.2816 502.2816 0.0000 0.0000 0.0000 337 PRO I CA  
32   C C   . PRO A 5   ? 499.7295 499.7295 499.7295 0.0000 0.0000 0.0000 337 PRO I C   
33   O O   . PRO A 5   ? 498.4160 498.4160 498.4160 0.0000 0.0000 0.0000 337 PRO I O   
34   C CB  . PRO A 5   ? 501.1593 501.1593 501.1593 0.0000 0.0000 0.0000 337 PRO I CB  
35   C CG  . PRO A 5   ? 501.4253 501.4253 501.4253 0.0000 0.0000 0.0000 337 PRO I CG  
36   C CD  . PRO A 5   ? 503.1653 503.1653 503.1653 0.0000 0.0000 0.0000 337 PRO I CD  
37   N N   . PHE A 6   ? 474.9292 474.9292 474.9292 0.0000 0.0000 0.0000 338 PHE I N   
38   C CA  . PHE A 6   ? 472.5043 472.5043 472.5043 0.0000 0.0000 0.0000 338 PHE I CA  
39   C C   . PHE A 6   ? 469.9576 469.9576 469.9576 0.0000 0.0000 0.0000 338 PHE I C   
40   O O   . PHE A 6   ? 470.6901 470.6901 470.6901 0.0000 0.0000 0.0000 338 PHE I O   
41   C CB  . PHE A 6   ? 472.6514 472.6514 472.6514 0.0000 0.0000 0.0000 338 PHE I CB  
42   C CG  . PHE A 6   ? 472.6284 472.6284 472.6284 0.0000 0.0000 0.0000 338 PHE I CG  
43   C CD1 . PHE A 6   ? 472.1975 472.1975 472.1975 0.0000 0.0000 0.0000 338 PHE I CD1 
44   C CD2 . PHE A 6   ? 472.9381 472.9381 472.9381 0.0000 0.0000 0.0000 338 PHE I CD2 
45   C CE1 . PHE A 6   ? 471.9870 471.9870 471.9870 0.0000 0.0000 0.0000 338 PHE I CE1 
46   C CE2 . PHE A 6   ? 475.0971 475.0971 475.0971 0.0000 0.0000 0.0000 338 PHE I CE2 
47   C CZ  . PHE A 6   ? 473.6241 473.6241 473.6241 0.0000 0.0000 0.0000 338 PHE I CZ  
48   N N   . GLY A 7   ? 436.5744 436.5744 436.5744 0.0000 0.0000 0.0000 339 GLY I N   
49   C CA  . GLY A 7   ? 434.9273 434.9273 434.9273 0.0000 0.0000 0.0000 339 GLY I CA  
50   C C   . GLY A 7   ? 435.5007 435.5007 435.5007 0.0000 0.0000 0.0000 339 GLY I C   
51   O O   . GLY A 7   ? 434.9037 434.9037 434.9037 0.0000 0.0000 0.0000 339 GLY I O   
52   N N   . GLU A 8   ? 448.1363 448.1363 448.1363 0.0000 0.0000 0.0000 340 GLU I N   
53   C CA  . GLU A 8   ? 447.2958 447.2958 447.2958 0.0000 0.0000 0.0000 340 GLU I CA  
54   C C   . GLU A 8   ? 446.4893 446.4893 446.4893 0.0000 0.0000 0.0000 340 GLU I C   
55   O O   . GLU A 8   ? 447.0279 447.0279 447.0279 0.0000 0.0000 0.0000 340 GLU I O   
56   C CB  . GLU A 8   ? 447.8905 447.8905 447.8905 0.0000 0.0000 0.0000 340 GLU I CB  
57   C CG  . GLU A 8   ? 448.0078 448.0078 448.0078 0.0000 0.0000 0.0000 340 GLU I CG  
58   C CD  . GLU A 8   ? 448.3830 448.3830 448.3830 0.0000 0.0000 0.0000 340 GLU I CD  
59   O OE1 . GLU A 8   ? 448.3201 448.3201 448.3201 0.0000 0.0000 0.0000 340 GLU I OE1 
60   O OE2 . GLU A 8   ? 448.3955 448.3955 448.3955 0.0000 0.0000 0.0000 340 GLU I OE2 
61   N N   . VAL A 9   ? 433.5782 433.5782 433.5782 0.0000 0.0000 0.0000 341 VAL I N   
62   C CA  . VAL A 9   ? 431.4891 431.4891 431.4891 0.0000 0.0000 0.0000 341 VAL I CA  
63   C C   . VAL A 9   ? 430.7862 430.7862 430.7862 0.0000 0.0000 0.0000 341 VAL I C   
64   O O   . VAL A 9   ? 430.9612 430.9612 430.9612 0.0000 0.0000 0.0000 341 VAL I O   
65   C CB  . VAL A 9   ? 430.9755 430.9755 430.9755 0.0000 0.0000 0.0000 341 VAL I CB  
66   C CG1 . VAL A 9   ? 430.7763 430.7763 430.7763 0.0000 0.0000 0.0000 341 VAL I CG1 
67   C CG2 . VAL A 9   ? 432.1390 432.1390 432.1390 0.0000 0.0000 0.0000 341 VAL I CG2 
68   N N   . PHE A 10  ? 431.0671 431.0671 431.0671 0.0000 0.0000 0.0000 342 PHE I N   
69   C CA  . PHE A 10  ? 430.4186 430.4186 430.4186 0.0000 0.0000 0.0000 342 PHE I CA  
70   C C   . PHE A 10  ? 430.2780 430.2780 430.2780 0.0000 0.0000 0.0000 342 PHE I C   
71   O O   . PHE A 10  ? 430.1119 430.1119 430.1119 0.0000 0.0000 0.0000 342 PHE I O   
72   C CB  . PHE A 10  ? 430.1645 430.1645 430.1645 0.0000 0.0000 0.0000 342 PHE I CB  
73   C CG  . PHE A 10  ? 430.5107 430.5107 430.5107 0.0000 0.0000 0.0000 342 PHE I CG  
74   C CD1 . PHE A 10  ? 431.4001 431.4001 431.4001 0.0000 0.0000 0.0000 342 PHE I CD1 
75   C CD2 . PHE A 10  ? 431.1315 431.1315 431.1315 0.0000 0.0000 0.0000 342 PHE I CD2 
76   C CE1 . PHE A 10  ? 431.8514 431.8514 431.8514 0.0000 0.0000 0.0000 342 PHE I CE1 
77   C CE2 . PHE A 10  ? 431.4621 431.4621 431.4621 0.0000 0.0000 0.0000 342 PHE I CE2 
78   C CZ  . PHE A 10  ? 431.2813 431.2813 431.2813 0.0000 0.0000 0.0000 342 PHE I CZ  
79   N N   . ASN A 11  ? 431.2629 431.2629 431.2629 0.0000 0.0000 0.0000 343 ASN I N   
80   C CA  . ASN A 11  ? 429.5701 429.5701 429.5701 0.0000 0.0000 0.0000 343 ASN I CA  
81   C C   . ASN A 11  ? 428.8509 428.8509 428.8509 0.0000 0.0000 0.0000 343 ASN I C   
82   O O   . ASN A 11  ? 428.3237 428.3237 428.3237 0.0000 0.0000 0.0000 343 ASN I O   
83   C CB  . ASN A 11  ? 430.2927 430.2927 430.2927 0.0000 0.0000 0.0000 343 ASN I CB  
84   C CG  . ASN A 11  ? 431.4268 431.4268 431.4268 0.0000 0.0000 0.0000 343 ASN I CG  
85   O OD1 . ASN A 11  ? 430.7774 430.7774 430.7774 0.0000 0.0000 0.0000 343 ASN I OD1 
86   N ND2 . ASN A 11  ? 430.7726 430.7726 430.7726 0.0000 0.0000 0.0000 343 ASN I ND2 
87   N N   . ALA A 12  ? 431.2800 431.2800 431.2800 0.0000 0.0000 0.0000 344 ALA I N   
88   C CA  . ALA A 12  ? 429.8395 429.8395 429.8395 0.0000 0.0000 0.0000 344 ALA I CA  
89   C C   . ALA A 12  ? 428.1035 428.1035 428.1035 0.0000 0.0000 0.0000 344 ALA I C   
90   O O   . ALA A 12  ? 428.3256 428.3256 428.3256 0.0000 0.0000 0.0000 344 ALA I O   
91   C CB  . ALA A 12  ? 430.3627 430.3627 430.3627 0.0000 0.0000 0.0000 344 ALA I CB  
92   N N   . THR A 13  ? 430.0752 430.0752 430.0752 0.0000 0.0000 0.0000 345 THR I N   
93   C CA  . THR A 13  ? 427.6300 427.6300 427.6300 0.0000 0.0000 0.0000 345 THR I CA  
94   C C   . THR A 13  ? 429.8025 429.8025 429.8025 0.0000 0.0000 0.0000 345 THR I C   
95   O O   . THR A 13  ? 425.2095 425.2095 425.2095 0.0000 0.0000 0.0000 345 THR I O   
96   C CB  . THR A 13  ? 427.9601 427.9601 427.9601 0.0000 0.0000 0.0000 345 THR I CB  
97   O OG1 . THR A 13  ? 429.2020 429.2020 429.2020 0.0000 0.0000 0.0000 345 THR I OG1 
98   C CG2 . THR A 13  ? 423.3591 423.3591 423.3591 0.0000 0.0000 0.0000 345 THR I CG2 
99   N N   . ARG A 14  ? 430.0128 430.0128 430.0128 0.0000 0.0000 0.0000 346 ARG I N   
100  C CA  . ARG A 14  ? 429.5142 429.5142 429.5142 0.0000 0.0000 0.0000 346 ARG I CA  
101  C C   . ARG A 14  ? 430.1125 430.1125 430.1125 0.0000 0.0000 0.0000 346 ARG I C   
102  O O   . ARG A 14  ? 430.2840 430.2840 430.2840 0.0000 0.0000 0.0000 346 ARG I O   
103  C CB  . ARG A 14  ? 429.8861 429.8861 429.8861 0.0000 0.0000 0.0000 346 ARG I CB  
104  C CG  . ARG A 14  ? 423.5178 423.5178 423.5178 0.0000 0.0000 0.0000 346 ARG I CG  
105  C CD  . ARG A 14  ? 425.8536 425.8536 425.8536 0.0000 0.0000 0.0000 346 ARG I CD  
106  N NE  . ARG A 14  ? 427.5338 427.5338 427.5338 0.0000 0.0000 0.0000 346 ARG I NE  
107  C CZ  . ARG A 14  ? 422.8751 422.8751 422.8751 0.0000 0.0000 0.0000 346 ARG I CZ  
108  N NH1 . ARG A 14  ? 413.7989 413.7989 413.7989 0.0000 0.0000 0.0000 346 ARG I NH1 
109  N NH2 . ARG A 14  ? 429.0983 429.0983 429.0983 0.0000 0.0000 0.0000 346 ARG I NH2 
110  N N   . PHE A 15  ? 429.9981 429.9981 429.9981 0.0000 0.0000 0.0000 347 PHE I N   
111  C CA  . PHE A 15  ? 429.8707 429.8707 429.8707 0.0000 0.0000 0.0000 347 PHE I CA  
112  C C   . PHE A 15  ? 430.5847 430.5847 430.5847 0.0000 0.0000 0.0000 347 PHE I C   
113  O O   . PHE A 15  ? 430.8172 430.8172 430.8172 0.0000 0.0000 0.0000 347 PHE I O   
114  C CB  . PHE A 15  ? 430.5590 430.5590 430.5590 0.0000 0.0000 0.0000 347 PHE I CB  
115  C CG  . PHE A 15  ? 430.3201 430.3201 430.3201 0.0000 0.0000 0.0000 347 PHE I CG  
116  C CD1 . PHE A 15  ? 431.2927 431.2927 431.2927 0.0000 0.0000 0.0000 347 PHE I CD1 
117  C CD2 . PHE A 15  ? 430.1550 430.1550 430.1550 0.0000 0.0000 0.0000 347 PHE I CD2 
118  C CE1 . PHE A 15  ? 430.6004 430.6004 430.6004 0.0000 0.0000 0.0000 347 PHE I CE1 
119  C CE2 . PHE A 15  ? 430.6551 430.6551 430.6551 0.0000 0.0000 0.0000 347 PHE I CE2 
120  C CZ  . PHE A 15  ? 430.3736 430.3736 430.3736 0.0000 0.0000 0.0000 347 PHE I CZ  
121  N N   . ALA A 16  ? 430.0829 430.0829 430.0829 0.0000 0.0000 0.0000 348 ALA I N   
122  C CA  . ALA A 16  ? 430.0715 430.0715 430.0715 0.0000 0.0000 0.0000 348 ALA I CA  
123  C C   . ALA A 16  ? 430.3921 430.3921 430.3921 0.0000 0.0000 0.0000 348 ALA I C   
124  O O   . ALA A 16  ? 432.3831 432.3831 432.3831 0.0000 0.0000 0.0000 348 ALA I O   
125  C CB  . ALA A 16  ? 430.7294 430.7294 430.7294 0.0000 0.0000 0.0000 348 ALA I CB  
126  N N   . SER A 17  ? 430.7017 430.7017 430.7017 0.0000 0.0000 0.0000 349 SER I N   
127  C CA  . SER A 17  ? 430.4131 430.4131 430.4131 0.0000 0.0000 0.0000 349 SER I CA  
128  C C   . SER A 17  ? 430.9238 430.9238 430.9238 0.0000 0.0000 0.0000 349 SER I C   
129  O O   . SER A 17  ? 432.5368 432.5368 432.5368 0.0000 0.0000 0.0000 349 SER I O   
130  C CB  . SER A 17  ? 431.3846 431.3846 431.3846 0.0000 0.0000 0.0000 349 SER I CB  
131  O OG  . SER A 17  ? 430.1980 430.1980 430.1980 0.0000 0.0000 0.0000 349 SER I OG  
132  N N   . VAL A 18  ? 428.9417 428.9417 428.9417 0.0000 0.0000 0.0000 350 VAL I N   
133  C CA  . VAL A 18  ? 429.7301 429.7301 429.7301 0.0000 0.0000 0.0000 350 VAL I CA  
134  C C   . VAL A 18  ? 431.1563 431.1563 431.1563 0.0000 0.0000 0.0000 350 VAL I C   
135  O O   . VAL A 18  ? 432.5751 432.5751 432.5751 0.0000 0.0000 0.0000 350 VAL I O   
136  C CB  . VAL A 18  ? 429.9111 429.9111 429.9111 0.0000 0.0000 0.0000 350 VAL I CB  
137  C CG1 . VAL A 18  ? 431.8220 431.8220 431.8220 0.0000 0.0000 0.0000 350 VAL I CG1 
138  C CG2 . VAL A 18  ? 429.5611 429.5611 429.5611 0.0000 0.0000 0.0000 350 VAL I CG2 
139  N N   . TYR A 19  ? 431.0637 431.0637 431.0637 0.0000 0.0000 0.0000 351 TYR I N   
140  C CA  . TYR A 19  ? 430.0682 430.0682 430.0682 0.0000 0.0000 0.0000 351 TYR I CA  
141  C C   . TYR A 19  ? 430.7917 430.7917 430.7917 0.0000 0.0000 0.0000 351 TYR I C   
142  O O   . TYR A 19  ? 431.9674 431.9674 431.9674 0.0000 0.0000 0.0000 351 TYR I O   
143  C CB  . TYR A 19  ? 430.3446 430.3446 430.3446 0.0000 0.0000 0.0000 351 TYR I CB  
144  C CG  . TYR A 19  ? 430.0453 430.0453 430.0453 0.0000 0.0000 0.0000 351 TYR I CG  
145  C CD1 . TYR A 19  ? 430.1276 430.1276 430.1276 0.0000 0.0000 0.0000 351 TYR I CD1 
146  C CD2 . TYR A 19  ? 431.5281 431.5281 431.5281 0.0000 0.0000 0.0000 351 TYR I CD2 
147  C CE1 . TYR A 19  ? 430.5843 430.5843 430.5843 0.0000 0.0000 0.0000 351 TYR I CE1 
148  C CE2 . TYR A 19  ? 431.2443 431.2443 431.2443 0.0000 0.0000 0.0000 351 TYR I CE2 
149  C CZ  . TYR A 19  ? 430.6287 430.6287 430.6287 0.0000 0.0000 0.0000 351 TYR I CZ  
150  O OH  . TYR A 19  ? 430.5220 430.5220 430.5220 0.0000 0.0000 0.0000 351 TYR I OH  
151  N N   . ALA A 20  ? 430.8565 430.8565 430.8565 0.0000 0.0000 0.0000 352 ALA I N   
152  C CA  . ALA A 20  ? 429.1488 429.1488 429.1488 0.0000 0.0000 0.0000 352 ALA I CA  
153  C C   . ALA A 20  ? 431.0087 431.0087 431.0087 0.0000 0.0000 0.0000 352 ALA I C   
154  O O   . ALA A 20  ? 432.1380 432.1380 432.1380 0.0000 0.0000 0.0000 352 ALA I O   
155  C CB  . ALA A 20  ? 430.0238 430.0238 430.0238 0.0000 0.0000 0.0000 352 ALA I CB  
156  N N   . TRP A 21  ? 431.5278 431.5278 431.5278 0.0000 0.0000 0.0000 353 TRP I N   
157  C CA  . TRP A 21  ? 429.5079 429.5079 429.5079 0.0000 0.0000 0.0000 353 TRP I CA  
158  C C   . TRP A 21  ? 430.4707 430.4707 430.4707 0.0000 0.0000 0.0000 353 TRP I C   
159  O O   . TRP A 21  ? 431.7124 431.7124 431.7124 0.0000 0.0000 0.0000 353 TRP I O   
160  C CB  . TRP A 21  ? 429.8956 429.8956 429.8956 0.0000 0.0000 0.0000 353 TRP I CB  
161  C CG  . TRP A 21  ? 429.4838 429.4838 429.4838 0.0000 0.0000 0.0000 353 TRP I CG  
162  C CD1 . TRP A 21  ? 430.2942 430.2942 430.2942 0.0000 0.0000 0.0000 353 TRP I CD1 
163  C CD2 . TRP A 21  ? 429.6319 429.6319 429.6319 0.0000 0.0000 0.0000 353 TRP I CD2 
164  N NE1 . TRP A 21  ? 430.1909 430.1909 430.1909 0.0000 0.0000 0.0000 353 TRP I NE1 
165  C CE2 . TRP A 21  ? 430.1546 430.1546 430.1546 0.0000 0.0000 0.0000 353 TRP I CE2 
166  C CE3 . TRP A 21  ? 430.3744 430.3744 430.3744 0.0000 0.0000 0.0000 353 TRP I CE3 
167  C CZ2 . TRP A 21  ? 430.8642 430.8642 430.8642 0.0000 0.0000 0.0000 353 TRP I CZ2 
168  C CZ3 . TRP A 21  ? 430.7651 430.7651 430.7651 0.0000 0.0000 0.0000 353 TRP I CZ3 
169  C CH2 . TRP A 21  ? 430.6347 430.6347 430.6347 0.0000 0.0000 0.0000 353 TRP I CH2 
170  N N   . ASN A 22  ? 430.1413 430.1413 430.1413 0.0000 0.0000 0.0000 354 ASN I N   
171  C CA  . ASN A 22  ? 429.8545 429.8545 429.8545 0.0000 0.0000 0.0000 354 ASN I CA  
172  C C   . ASN A 22  ? 430.3410 430.3410 430.3410 0.0000 0.0000 0.0000 354 ASN I C   
173  O O   . ASN A 22  ? 431.9960 431.9960 431.9960 0.0000 0.0000 0.0000 354 ASN I O   
174  C CB  . ASN A 22  ? 430.3896 430.3896 430.3896 0.0000 0.0000 0.0000 354 ASN I CB  
175  C CG  . ASN A 22  ? 431.5334 431.5334 431.5334 0.0000 0.0000 0.0000 354 ASN I CG  
176  O OD1 . ASN A 22  ? 431.4578 431.4578 431.4578 0.0000 0.0000 0.0000 354 ASN I OD1 
177  N ND2 . ASN A 22  ? 432.0974 432.0974 432.0974 0.0000 0.0000 0.0000 354 ASN I ND2 
178  N N   . ARG A 23  ? 430.3251 430.3251 430.3251 0.0000 0.0000 0.0000 355 ARG I N   
179  C CA  . ARG A 23  ? 430.3719 430.3719 430.3719 0.0000 0.0000 0.0000 355 ARG I CA  
180  C C   . ARG A 23  ? 431.3368 431.3368 431.3368 0.0000 0.0000 0.0000 355 ARG I C   
181  O O   . ARG A 23  ? 430.9854 430.9854 430.9854 0.0000 0.0000 0.0000 355 ARG I O   
182  C CB  . ARG A 23  ? 429.7633 429.7633 429.7633 0.0000 0.0000 0.0000 355 ARG I CB  
183  C CG  . ARG A 23  ? 430.3767 430.3767 430.3767 0.0000 0.0000 0.0000 355 ARG I CG  
184  C CD  . ARG A 23  ? 430.5317 430.5317 430.5317 0.0000 0.0000 0.0000 355 ARG I CD  
185  N NE  . ARG A 23  ? 431.5427 431.5427 431.5427 0.0000 0.0000 0.0000 355 ARG I NE  
186  C CZ  . ARG A 23  ? 431.0315 431.0315 431.0315 0.0000 0.0000 0.0000 355 ARG I CZ  
187  N NH1 . ARG A 23  ? 430.7694 430.7694 430.7694 0.0000 0.0000 0.0000 355 ARG I NH1 
188  N NH2 . ARG A 23  ? 431.6913 431.6913 431.6913 0.0000 0.0000 0.0000 355 ARG I NH2 
189  N N   . LYS A 24  ? 431.5283 431.5283 431.5283 0.0000 0.0000 0.0000 356 LYS I N   
190  C CA  . LYS A 24  ? 430.5846 430.5846 430.5846 0.0000 0.0000 0.0000 356 LYS I CA  
191  C C   . LYS A 24  ? 431.6979 431.6979 431.6979 0.0000 0.0000 0.0000 356 LYS I C   
192  O O   . LYS A 24  ? 433.3076 433.3076 433.3076 0.0000 0.0000 0.0000 356 LYS I O   
193  C CB  . LYS A 24  ? 430.6599 430.6599 430.6599 0.0000 0.0000 0.0000 356 LYS I CB  
194  C CG  . LYS A 24  ? 431.7429 431.7429 431.7429 0.0000 0.0000 0.0000 356 LYS I CG  
195  C CD  . LYS A 24  ? 431.5127 431.5127 431.5127 0.0000 0.0000 0.0000 356 LYS I CD  
196  C CE  . LYS A 24  ? 432.4952 432.4952 432.4952 0.0000 0.0000 0.0000 356 LYS I CE  
197  N NZ  . LYS A 24  ? 432.6120 432.6120 432.6120 0.0000 0.0000 0.0000 356 LYS I NZ  
198  N N   . ARG A 25  ? 460.9510 460.9510 460.9510 0.0000 0.0000 0.0000 357 ARG I N   
199  C CA  . ARG A 25  ? 462.1559 462.1559 462.1559 0.0000 0.0000 0.0000 357 ARG I CA  
200  C C   . ARG A 25  ? 463.5185 463.5185 463.5185 0.0000 0.0000 0.0000 357 ARG I C   
201  O O   . ARG A 25  ? 464.2658 464.2658 464.2658 0.0000 0.0000 0.0000 357 ARG I O   
202  C CB  . ARG A 25  ? 462.9688 462.9688 462.9688 0.0000 0.0000 0.0000 357 ARG I CB  
203  C CG  . ARG A 25  ? 464.2804 464.2804 464.2804 0.0000 0.0000 0.0000 357 ARG I CG  
204  C CD  . ARG A 25  ? 464.5784 464.5784 464.5784 0.0000 0.0000 0.0000 357 ARG I CD  
205  N NE  . ARG A 25  ? 465.7281 465.7281 465.7281 0.0000 0.0000 0.0000 357 ARG I NE  
206  C CZ  . ARG A 25  ? 465.7444 465.7444 465.7444 0.0000 0.0000 0.0000 357 ARG I CZ  
207  N NH1 . ARG A 25  ? 465.1823 465.1823 465.1823 0.0000 0.0000 0.0000 357 ARG I NH1 
208  N NH2 . ARG A 25  ? 465.4431 465.4431 465.4431 0.0000 0.0000 0.0000 357 ARG I NH2 
209  N N   . ILE A 26  ? 461.3658 461.3658 461.3658 0.0000 0.0000 0.0000 358 ILE I N   
210  C CA  . ILE A 26  ? 462.4016 462.4016 462.4016 0.0000 0.0000 0.0000 358 ILE I CA  
211  C C   . ILE A 26  ? 466.1536 466.1536 466.1536 0.0000 0.0000 0.0000 358 ILE I C   
212  O O   . ILE A 26  ? 466.5071 466.5071 466.5071 0.0000 0.0000 0.0000 358 ILE I O   
213  C CB  . ILE A 26  ? 461.2005 461.2005 461.2005 0.0000 0.0000 0.0000 358 ILE I CB  
214  C CG1 . ILE A 26  ? 460.4516 460.4516 460.4516 0.0000 0.0000 0.0000 358 ILE I CG1 
215  C CG2 . ILE A 26  ? 464.3158 464.3158 464.3158 0.0000 0.0000 0.0000 358 ILE I CG2 
216  C CD1 . ILE A 26  ? 460.9476 460.9476 460.9476 0.0000 0.0000 0.0000 358 ILE I CD1 
217  N N   . SER A 27  ? 532.7170 532.7170 532.7170 0.0000 0.0000 0.0000 359 SER I N   
218  C CA  . SER A 27  ? 536.0719 536.0719 536.0719 0.0000 0.0000 0.0000 359 SER I CA  
219  C C   . SER A 27  ? 538.7471 538.7471 538.7471 0.0000 0.0000 0.0000 359 SER I C   
220  O O   . SER A 27  ? 537.7478 537.7478 537.7478 0.0000 0.0000 0.0000 359 SER I O   
221  C CB  . SER A 27  ? 535.9989 535.9989 535.9989 0.0000 0.0000 0.0000 359 SER I CB  
222  O OG  . SER A 27  ? 535.9257 535.9257 535.9257 0.0000 0.0000 0.0000 359 SER I OG  
223  N N   . ASN A 28  ? 582.5201 582.5201 582.5201 0.0000 0.0000 0.0000 360 ASN I N   
224  C CA  . ASN A 28  ? 583.7513 583.7513 583.7513 0.0000 0.0000 0.0000 360 ASN I CA  
225  C C   . ASN A 28  ? 582.8646 582.8646 582.8646 0.0000 0.0000 0.0000 360 ASN I C   
226  O O   . ASN A 28  ? 584.0261 584.0261 584.0261 0.0000 0.0000 0.0000 360 ASN I O   
227  C CB  . ASN A 28  ? 583.7271 583.7271 583.7271 0.0000 0.0000 0.0000 360 ASN I CB  
228  C CG  . ASN A 28  ? 583.8926 583.8926 583.8926 0.0000 0.0000 0.0000 360 ASN I CG  
229  O OD1 . ASN A 28  ? 584.0627 584.0627 584.0627 0.0000 0.0000 0.0000 360 ASN I OD1 
230  N ND2 . ASN A 28  ? 584.0999 584.0999 584.0999 0.0000 0.0000 0.0000 360 ASN I ND2 
231  N N   . CYS A 29  ? 551.6119 551.6119 551.6119 0.0000 0.0000 0.0000 361 CYS I N   
232  C CA  . CYS A 29  ? 551.1270 551.1270 551.1270 0.0000 0.0000 0.0000 361 CYS I CA  
233  C C   . CYS A 29  ? 549.9916 549.9916 549.9916 0.0000 0.0000 0.0000 361 CYS I C   
234  O O   . CYS A 29  ? 551.6600 551.6600 551.6600 0.0000 0.0000 0.0000 361 CYS I O   
235  C CB  . CYS A 29  ? 551.9670 551.9670 551.9670 0.0000 0.0000 0.0000 361 CYS I CB  
236  S SG  . CYS A 29  ? 549.4412 549.4412 549.4412 0.0000 0.0000 0.0000 361 CYS I SG  
237  N N   . VAL A 30  ? 533.5223 533.5223 533.5223 0.0000 0.0000 0.0000 362 VAL I N   
238  C CA  . VAL A 30  ? 532.1946 532.1946 532.1946 0.0000 0.0000 0.0000 362 VAL I CA  
239  C C   . VAL A 30  ? 532.3242 532.3242 532.3242 0.0000 0.0000 0.0000 362 VAL I C   
240  O O   . VAL A 30  ? 534.0011 534.0011 534.0011 0.0000 0.0000 0.0000 362 VAL I O   
241  C CB  . VAL A 30  ? 531.9178 531.9178 531.9178 0.0000 0.0000 0.0000 362 VAL I CB  
242  C CG1 . VAL A 30  ? 532.5973 532.5973 532.5973 0.0000 0.0000 0.0000 362 VAL I CG1 
243  C CG2 . VAL A 30  ? 531.8985 531.8985 531.8985 0.0000 0.0000 0.0000 362 VAL I CG2 
244  N N   . ALA A 31  ? 529.9022 529.9022 529.9022 0.0000 0.0000 0.0000 363 ALA I N   
245  C CA  . ALA A 31  ? 529.9457 529.9457 529.9457 0.0000 0.0000 0.0000 363 ALA I CA  
246  C C   . ALA A 31  ? 531.2772 531.2772 531.2772 0.0000 0.0000 0.0000 363 ALA I C   
247  O O   . ALA A 31  ? 532.4326 532.4326 532.4326 0.0000 0.0000 0.0000 363 ALA I O   
248  C CB  . ALA A 31  ? 530.1995 530.1995 530.1995 0.0000 0.0000 0.0000 363 ALA I CB  
249  N N   . ASP A 32  ? 561.4914 561.4914 561.4914 0.0000 0.0000 0.0000 364 ASP I N   
250  C CA  . ASP A 32  ? 562.7291 562.7291 562.7291 0.0000 0.0000 0.0000 364 ASP I CA  
251  C C   . ASP A 32  ? 562.6875 562.6875 562.6875 0.0000 0.0000 0.0000 364 ASP I C   
252  O O   . ASP A 32  ? 562.2757 562.2757 562.2757 0.0000 0.0000 0.0000 364 ASP I O   
253  C CB  . ASP A 32  ? 563.2838 563.2838 563.2838 0.0000 0.0000 0.0000 364 ASP I CB  
254  C CG  . ASP A 32  ? 563.4309 563.4309 563.4309 0.0000 0.0000 0.0000 364 ASP I CG  
255  O OD1 . ASP A 32  ? 563.7870 563.7870 563.7870 0.0000 0.0000 0.0000 364 ASP I OD1 
256  O OD2 . ASP A 32  ? 563.5964 563.5964 563.5964 0.0000 0.0000 0.0000 364 ASP I OD2 
257  N N   . TYR A 33  ? 556.8489 556.8489 556.8489 0.0000 0.0000 0.0000 365 TYR I N   
258  C CA  . TYR A 33  ? 556.3084 556.3084 556.3084 0.0000 0.0000 0.0000 365 TYR I CA  
259  C C   . TYR A 33  ? 557.3785 557.3785 557.3785 0.0000 0.0000 0.0000 365 TYR I C   
260  O O   . TYR A 33  ? 556.5569 556.5569 556.5569 0.0000 0.0000 0.0000 365 TYR I O   
261  C CB  . TYR A 33  ? 556.7630 556.7630 556.7630 0.0000 0.0000 0.0000 365 TYR I CB  
262  C CG  . TYR A 33  ? 556.5263 556.5263 556.5263 0.0000 0.0000 0.0000 365 TYR I CG  
263  C CD1 . TYR A 33  ? 554.8210 554.8210 554.8210 0.0000 0.0000 0.0000 365 TYR I CD1 
264  C CD2 . TYR A 33  ? 557.5704 557.5704 557.5704 0.0000 0.0000 0.0000 365 TYR I CD2 
265  C CE1 . TYR A 33  ? 554.7644 554.7644 554.7644 0.0000 0.0000 0.0000 365 TYR I CE1 
266  C CE2 . TYR A 33  ? 557.5894 557.5894 557.5894 0.0000 0.0000 0.0000 365 TYR I CE2 
267  C CZ  . TYR A 33  ? 556.8926 556.8926 556.8926 0.0000 0.0000 0.0000 365 TYR I CZ  
268  O OH  . TYR A 33  ? 557.9783 557.9783 557.9783 0.0000 0.0000 0.0000 365 TYR I OH  
269  N N   . SER A 34  ? 582.4813 582.4813 582.4813 0.0000 0.0000 0.0000 366 SER I N   
270  C CA  . SER A 34  ? 582.9823 582.9823 582.9823 0.0000 0.0000 0.0000 366 SER I CA  
271  C C   . SER A 34  ? 582.6519 582.6519 582.6519 0.0000 0.0000 0.0000 366 SER I C   
272  O O   . SER A 34  ? 583.3432 583.3432 583.3432 0.0000 0.0000 0.0000 366 SER I O   
273  C CB  . SER A 34  ? 583.6965 583.6965 583.6965 0.0000 0.0000 0.0000 366 SER I CB  
274  O OG  . SER A 34  ? 583.7890 583.7890 583.7890 0.0000 0.0000 0.0000 366 SER I OG  
275  N N   . VAL A 35  ? 572.0682 572.0682 572.0682 0.0000 0.0000 0.0000 367 VAL I N   
276  C CA  . VAL A 35  ? 571.4629 571.4629 571.4629 0.0000 0.0000 0.0000 367 VAL I CA  
277  C C   . VAL A 35  ? 570.0564 570.0564 570.0564 0.0000 0.0000 0.0000 367 VAL I C   
278  O O   . VAL A 35  ? 571.8260 571.8260 571.8260 0.0000 0.0000 0.0000 367 VAL I O   
279  C CB  . VAL A 35  ? 571.5830 571.5830 571.5830 0.0000 0.0000 0.0000 367 VAL I CB  
280  C CG1 . VAL A 35  ? 571.4850 571.4850 571.4850 0.0000 0.0000 0.0000 367 VAL I CG1 
281  C CG2 . VAL A 35  ? 572.2485 572.2485 572.2485 0.0000 0.0000 0.0000 367 VAL I CG2 
282  N N   . LEU A 36  ? 510.7731 510.7731 510.7731 0.0000 0.0000 0.0000 368 LEU I N   
283  C CA  . LEU A 36  ? 508.8161 508.8161 508.8161 0.0000 0.0000 0.0000 368 LEU I CA  
284  C C   . LEU A 36  ? 509.8745 509.8745 509.8745 0.0000 0.0000 0.0000 368 LEU I C   
285  O O   . LEU A 36  ? 507.9736 507.9736 507.9736 0.0000 0.0000 0.0000 368 LEU I O   
286  C CB  . LEU A 36  ? 505.3482 505.3482 505.3482 0.0000 0.0000 0.0000 368 LEU I CB  
287  C CG  . LEU A 36  ? 503.3589 503.3589 503.3589 0.0000 0.0000 0.0000 368 LEU I CG  
288  C CD1 . LEU A 36  ? 503.1264 503.1264 503.1264 0.0000 0.0000 0.0000 368 LEU I CD1 
289  C CD2 . LEU A 36  ? 502.6384 502.6384 502.6384 0.0000 0.0000 0.0000 368 LEU I CD2 
290  N N   . TYR A 37  ? 564.1481 564.1481 564.1481 0.0000 0.0000 0.0000 369 TYR I N   
291  C CA  . TYR A 37  ? 565.1821 565.1821 565.1821 0.0000 0.0000 0.0000 369 TYR I CA  
292  C C   . TYR A 37  ? 567.6114 567.6114 567.6114 0.0000 0.0000 0.0000 369 TYR I C   
293  O O   . TYR A 37  ? 568.0297 568.0297 568.0297 0.0000 0.0000 0.0000 369 TYR I O   
294  C CB  . TYR A 37  ? 565.8243 565.8243 565.8243 0.0000 0.0000 0.0000 369 TYR I CB  
295  C CG  . TYR A 37  ? 565.3279 565.3279 565.3279 0.0000 0.0000 0.0000 369 TYR I CG  
296  C CD1 . TYR A 37  ? 564.1223 564.1223 564.1223 0.0000 0.0000 0.0000 369 TYR I CD1 
297  C CD2 . TYR A 37  ? 566.7462 566.7462 566.7462 0.0000 0.0000 0.0000 369 TYR I CD2 
298  C CE1 . TYR A 37  ? 564.0754 564.0754 564.0754 0.0000 0.0000 0.0000 369 TYR I CE1 
299  C CE2 . TYR A 37  ? 566.7565 566.7565 566.7565 0.0000 0.0000 0.0000 369 TYR I CE2 
300  C CZ  . TYR A 37  ? 566.2153 566.2153 566.2153 0.0000 0.0000 0.0000 369 TYR I CZ  
301  O OH  . TYR A 37  ? 566.3852 566.3852 566.3852 0.0000 0.0000 0.0000 369 TYR I OH  
302  N N   . ASN A 38  ? 593.2036 593.2036 593.2036 0.0000 0.0000 0.0000 370 ASN I N   
303  C CA  . ASN A 38  ? 594.3493 594.3493 594.3493 0.0000 0.0000 0.0000 370 ASN I CA  
304  C C   . ASN A 38  ? 594.0108 594.0108 594.0108 0.0000 0.0000 0.0000 370 ASN I C   
305  O O   . ASN A 38  ? 595.0225 595.0225 595.0225 0.0000 0.0000 0.0000 370 ASN I O   
306  C CB  . ASN A 38  ? 595.0685 595.0685 595.0685 0.0000 0.0000 0.0000 370 ASN I CB  
307  C CG  . ASN A 38  ? 595.2805 595.2805 595.2805 0.0000 0.0000 0.0000 370 ASN I CG  
308  O OD1 . ASN A 38  ? 595.5570 595.5570 595.5570 0.0000 0.0000 0.0000 370 ASN I OD1 
309  N ND2 . ASN A 38  ? 595.0917 595.0917 595.0917 0.0000 0.0000 0.0000 370 ASN I ND2 
310  N N   . SER A 39  ? 579.6433 579.6433 579.6433 0.0000 0.0000 0.0000 371 SER I N   
311  C CA  . SER A 39  ? 579.4261 579.4261 579.4261 0.0000 0.0000 0.0000 371 SER I CA  
312  C C   . SER A 39  ? 578.6655 578.6655 578.6655 0.0000 0.0000 0.0000 371 SER I C   
313  O O   . SER A 39  ? 578.7462 578.7462 578.7462 0.0000 0.0000 0.0000 371 SER I O   
314  C CB  . SER A 39  ? 578.3415 578.3415 578.3415 0.0000 0.0000 0.0000 371 SER I CB  
315  O OG  . SER A 39  ? 575.9691 575.9691 575.9691 0.0000 0.0000 0.0000 371 SER I OG  
316  N N   . ALA A 40  ? 563.5682 563.5682 563.5682 0.0000 0.0000 0.0000 372 ALA I N   
317  C CA  . ALA A 40  ? 562.6508 562.6508 562.6508 0.0000 0.0000 0.0000 372 ALA I CA  
318  C C   . ALA A 40  ? 560.2225 560.2225 560.2225 0.0000 0.0000 0.0000 372 ALA I C   
319  O O   . ALA A 40  ? 561.0037 561.0037 561.0037 0.0000 0.0000 0.0000 372 ALA I O   
320  C CB  . ALA A 40  ? 563.8037 563.8037 563.8037 0.0000 0.0000 0.0000 372 ALA I CB  
321  N N   . SER A 41  ? 482.4503 482.4503 482.4503 0.0000 0.0000 0.0000 373 SER I N   
322  C CA  . SER A 41  ? 478.4238 478.4238 478.4238 0.0000 0.0000 0.0000 373 SER I CA  
323  C C   . SER A 41  ? 475.0579 475.0579 475.0579 0.0000 0.0000 0.0000 373 SER I C   
324  O O   . SER A 41  ? 474.7050 474.7050 474.7050 0.0000 0.0000 0.0000 373 SER I O   
325  C CB  . SER A 41  ? 478.4504 478.4504 478.4504 0.0000 0.0000 0.0000 373 SER I CB  
326  O OG  . SER A 41  ? 477.9410 477.9410 477.9410 0.0000 0.0000 0.0000 373 SER I OG  
327  N N   . PHE A 42  ? 435.4300 435.4300 435.4300 0.0000 0.0000 0.0000 374 PHE I N   
328  C CA  . PHE A 42  ? 432.4259 432.4259 432.4259 0.0000 0.0000 0.0000 374 PHE I CA  
329  C C   . PHE A 42  ? 430.4834 430.4834 430.4834 0.0000 0.0000 0.0000 374 PHE I C   
330  O O   . PHE A 42  ? 431.8200 431.8200 431.8200 0.0000 0.0000 0.0000 374 PHE I O   
331  C CB  . PHE A 42  ? 431.1031 431.1031 431.1031 0.0000 0.0000 0.0000 374 PHE I CB  
332  C CG  . PHE A 42  ? 431.5624 431.5624 431.5624 0.0000 0.0000 0.0000 374 PHE I CG  
333  C CD1 . PHE A 42  ? 432.4606 432.4606 432.4606 0.0000 0.0000 0.0000 374 PHE I CD1 
334  C CD2 . PHE A 42  ? 432.7598 432.7598 432.7598 0.0000 0.0000 0.0000 374 PHE I CD2 
335  C CE1 . PHE A 42  ? 431.5530 431.5530 431.5530 0.0000 0.0000 0.0000 374 PHE I CE1 
336  C CE2 . PHE A 42  ? 434.1567 434.1567 434.1567 0.0000 0.0000 0.0000 374 PHE I CE2 
337  C CZ  . PHE A 42  ? 432.1769 432.1769 432.1769 0.0000 0.0000 0.0000 374 PHE I CZ  
338  N N   . SER A 43  ? 431.1748 431.1748 431.1748 0.0000 0.0000 0.0000 375 SER I N   
339  C CA  . SER A 43  ? 430.4278 430.4278 430.4278 0.0000 0.0000 0.0000 375 SER I CA  
340  C C   . SER A 43  ? 430.5529 430.5529 430.5529 0.0000 0.0000 0.0000 375 SER I C   
341  O O   . SER A 43  ? 431.6941 431.6941 431.6941 0.0000 0.0000 0.0000 375 SER I O   
342  C CB  . SER A 43  ? 430.7077 430.7077 430.7077 0.0000 0.0000 0.0000 375 SER I CB  
343  O OG  . SER A 43  ? 431.1414 431.1414 431.1414 0.0000 0.0000 0.0000 375 SER I OG  
344  N N   . THR A 44  ? 430.6548 430.6548 430.6548 0.0000 0.0000 0.0000 376 THR I N   
345  C CA  . THR A 44  ? 430.2714 430.2714 430.2714 0.0000 0.0000 0.0000 376 THR I CA  
346  C C   . THR A 44  ? 430.6853 430.6853 430.6853 0.0000 0.0000 0.0000 376 THR I C   
347  O O   . THR A 44  ? 432.3449 432.3449 432.3449 0.0000 0.0000 0.0000 376 THR I O   
348  C CB  . THR A 44  ? 430.4684 430.4684 430.4684 0.0000 0.0000 0.0000 376 THR I CB  
349  O OG1 . THR A 44  ? 430.4312 430.4312 430.4312 0.0000 0.0000 0.0000 376 THR I OG1 
350  C CG2 . THR A 44  ? 430.5972 430.5972 430.5972 0.0000 0.0000 0.0000 376 THR I CG2 
351  N N   . PHE A 45  ? 430.6277 430.6277 430.6277 0.0000 0.0000 0.0000 377 PHE I N   
352  C CA  . PHE A 45  ? 430.8143 430.8143 430.8143 0.0000 0.0000 0.0000 377 PHE I CA  
353  C C   . PHE A 45  ? 430.7618 430.7618 430.7618 0.0000 0.0000 0.0000 377 PHE I C   
354  O O   . PHE A 45  ? 432.6161 432.6161 432.6161 0.0000 0.0000 0.0000 377 PHE I O   
355  C CB  . PHE A 45  ? 431.9907 431.9907 431.9907 0.0000 0.0000 0.0000 377 PHE I CB  
356  C CG  . PHE A 45  ? 432.1873 432.1873 432.1873 0.0000 0.0000 0.0000 377 PHE I CG  
357  C CD1 . PHE A 45  ? 433.2086 433.2086 433.2086 0.0000 0.0000 0.0000 377 PHE I CD1 
358  C CD2 . PHE A 45  ? 432.9433 432.9433 432.9433 0.0000 0.0000 0.0000 377 PHE I CD2 
359  C CE1 . PHE A 45  ? 432.6823 432.6823 432.6823 0.0000 0.0000 0.0000 377 PHE I CE1 
360  C CE2 . PHE A 45  ? 434.4128 434.4128 434.4128 0.0000 0.0000 0.0000 377 PHE I CE2 
361  C CZ  . PHE A 45  ? 433.1510 433.1510 433.1510 0.0000 0.0000 0.0000 377 PHE I CZ  
362  N N   . LYS A 46  ? 430.2738 430.2738 430.2738 0.0000 0.0000 0.0000 378 LYS I N   
363  C CA  . LYS A 46  ? 430.0731 430.0731 430.0731 0.0000 0.0000 0.0000 378 LYS I CA  
364  C C   . LYS A 46  ? 430.0497 430.0497 430.0497 0.0000 0.0000 0.0000 378 LYS I C   
365  O O   . LYS A 46  ? 431.7876 431.7876 431.7876 0.0000 0.0000 0.0000 378 LYS I O   
366  C CB  . LYS A 46  ? 430.7399 430.7399 430.7399 0.0000 0.0000 0.0000 378 LYS I CB  
367  C CG  . LYS A 46  ? 431.7646 431.7646 431.7646 0.0000 0.0000 0.0000 378 LYS I CG  
368  C CD  . LYS A 46  ? 431.9256 431.9256 431.9256 0.0000 0.0000 0.0000 378 LYS I CD  
369  C CE  . LYS A 46  ? 431.3552 431.3552 431.3552 0.0000 0.0000 0.0000 378 LYS I CE  
370  N NZ  . LYS A 46  ? 430.8844 430.8844 430.8844 0.0000 0.0000 0.0000 378 LYS I NZ  
371  N N   . CYS A 47  ? 430.5528 430.5528 430.5528 0.0000 0.0000 0.0000 379 CYS I N   
372  C CA  . CYS A 47  ? 430.7153 430.7153 430.7153 0.0000 0.0000 0.0000 379 CYS I CA  
373  C C   . CYS A 47  ? 430.6600 430.6600 430.6600 0.0000 0.0000 0.0000 379 CYS I C   
374  O O   . CYS A 47  ? 431.8962 431.8962 431.8962 0.0000 0.0000 0.0000 379 CYS I O   
375  C CB  . CYS A 47  ? 432.9021 432.9021 432.9021 0.0000 0.0000 0.0000 379 CYS I CB  
376  S SG  . CYS A 47  ? 434.5059 434.5059 434.5059 0.0000 0.0000 0.0000 379 CYS I SG  
377  N N   . TYR A 48  ? 429.6723 429.6723 429.6723 0.0000 0.0000 0.0000 380 TYR I N   
378  C CA  . TYR A 48  ? 430.1631 430.1631 430.1631 0.0000 0.0000 0.0000 380 TYR I CA  
379  C C   . TYR A 48  ? 430.1696 430.1696 430.1696 0.0000 0.0000 0.0000 380 TYR I C   
380  O O   . TYR A 48  ? 431.4355 431.4355 431.4355 0.0000 0.0000 0.0000 380 TYR I O   
381  C CB  . TYR A 48  ? 430.0424 430.0424 430.0424 0.0000 0.0000 0.0000 380 TYR I CB  
382  C CG  . TYR A 48  ? 430.0431 430.0431 430.0431 0.0000 0.0000 0.0000 380 TYR I CG  
383  C CD1 . TYR A 48  ? 430.6891 430.6891 430.6891 0.0000 0.0000 0.0000 380 TYR I CD1 
384  C CD2 . TYR A 48  ? 430.6721 430.6721 430.6721 0.0000 0.0000 0.0000 380 TYR I CD2 
385  C CE1 . TYR A 48  ? 431.4127 431.4127 431.4127 0.0000 0.0000 0.0000 380 TYR I CE1 
386  C CE2 . TYR A 48  ? 430.5938 430.5938 430.5938 0.0000 0.0000 0.0000 380 TYR I CE2 
387  C CZ  . TYR A 48  ? 431.0342 431.0342 431.0342 0.0000 0.0000 0.0000 380 TYR I CZ  
388  O OH  . TYR A 48  ? 430.7800 430.7800 430.7800 0.0000 0.0000 0.0000 380 TYR I OH  
389  N N   . GLY A 49  ? 430.3524 430.3524 430.3524 0.0000 0.0000 0.0000 381 GLY I N   
390  C CA  . GLY A 49  ? 430.2659 430.2659 430.2659 0.0000 0.0000 0.0000 381 GLY I CA  
391  C C   . GLY A 49  ? 430.6045 430.6045 430.6045 0.0000 0.0000 0.0000 381 GLY I C   
392  O O   . GLY A 49  ? 430.2335 430.2335 430.2335 0.0000 0.0000 0.0000 381 GLY I O   
393  N N   . VAL A 50  ? 431.2845 431.2845 431.2845 0.0000 0.0000 0.0000 382 VAL I N   
394  C CA  . VAL A 50  ? 431.3489 431.3489 431.3489 0.0000 0.0000 0.0000 382 VAL I CA  
395  C C   . VAL A 50  ? 432.8163 432.8163 432.8163 0.0000 0.0000 0.0000 382 VAL I C   
396  O O   . VAL A 50  ? 432.7990 432.7990 432.7990 0.0000 0.0000 0.0000 382 VAL I O   
397  C CB  . VAL A 50  ? 431.8213 431.8213 431.8213 0.0000 0.0000 0.0000 382 VAL I CB  
398  C CG1 . VAL A 50  ? 432.1725 432.1725 432.1725 0.0000 0.0000 0.0000 382 VAL I CG1 
399  C CG2 . VAL A 50  ? 435.1565 435.1565 435.1565 0.0000 0.0000 0.0000 382 VAL I CG2 
400  N N   . SER A 51  ? 467.3999 467.3999 467.3999 0.0000 0.0000 0.0000 383 SER I N   
401  C CA  . SER A 51  ? 470.4318 470.4318 470.4318 0.0000 0.0000 0.0000 383 SER I CA  
402  C C   . SER A 51  ? 474.0288 474.0288 474.0288 0.0000 0.0000 0.0000 383 SER I C   
403  O O   . SER A 51  ? 475.6692 475.6692 475.6692 0.0000 0.0000 0.0000 383 SER I O   
404  C CB  . SER A 51  ? 471.5749 471.5749 471.5749 0.0000 0.0000 0.0000 383 SER I CB  
405  O OG  . SER A 51  ? 469.7688 469.7688 469.7688 0.0000 0.0000 0.0000 383 SER I OG  
406  N N   . PRO A 52  ? 530.5706 530.5706 530.5706 0.0000 0.0000 0.0000 384 PRO I N   
407  C CA  . PRO A 52  ? 532.7020 532.7020 532.7020 0.0000 0.0000 0.0000 384 PRO I CA  
408  C C   . PRO A 52  ? 536.3449 536.3449 536.3449 0.0000 0.0000 0.0000 384 PRO I C   
409  O O   . PRO A 52  ? 535.7378 535.7378 535.7378 0.0000 0.0000 0.0000 384 PRO I O   
410  C CB  . PRO A 52  ? 532.9035 532.9035 532.9035 0.0000 0.0000 0.0000 384 PRO I CB  
411  C CG  . PRO A 52  ? 533.3018 533.3018 533.3018 0.0000 0.0000 0.0000 384 PRO I CG  
412  C CD  . PRO A 52  ? 531.2693 531.2693 531.2693 0.0000 0.0000 0.0000 384 PRO I CD  
413  N N   . THR A 53  ? 592.7587 592.7587 592.7587 0.0000 0.0000 0.0000 385 THR I N   
414  C CA  . THR A 53  ? 595.1446 595.1446 595.1446 0.0000 0.0000 0.0000 385 THR I CA  
415  C C   . THR A 53  ? 594.9417 594.9417 594.9417 0.0000 0.0000 0.0000 385 THR I C   
416  O O   . THR A 53  ? 594.4024 594.4024 594.4024 0.0000 0.0000 0.0000 385 THR I O   
417  C CB  . THR A 53  ? 596.3978 596.3978 596.3978 0.0000 0.0000 0.0000 385 THR I CB  
418  O OG1 . THR A 53  ? 596.3368 596.3368 596.3368 0.0000 0.0000 0.0000 385 THR I OG1 
419  C CG2 . THR A 53  ? 595.6645 595.6645 595.6645 0.0000 0.0000 0.0000 385 THR I CG2 
420  N N   . LYS A 54  ? 597.8824 597.8824 597.8824 0.0000 0.0000 0.0000 386 LYS I N   
421  C CA  . LYS A 54  ? 598.9493 598.9493 598.9493 0.0000 0.0000 0.0000 386 LYS I CA  
422  C C   . LYS A 54  ? 597.6444 597.6444 597.6444 0.0000 0.0000 0.0000 386 LYS I C   
423  O O   . LYS A 54  ? 598.5714 598.5714 598.5714 0.0000 0.0000 0.0000 386 LYS I O   
424  C CB  . LYS A 54  ? 599.4814 599.4814 599.4814 0.0000 0.0000 0.0000 386 LYS I CB  
425  C CG  . LYS A 54  ? 599.5009 599.5009 599.5009 0.0000 0.0000 0.0000 386 LYS I CG  
426  C CD  . LYS A 54  ? 599.2826 599.2826 599.2826 0.0000 0.0000 0.0000 386 LYS I CD  
427  C CE  . LYS A 54  ? 599.3852 599.3852 599.3852 0.0000 0.0000 0.0000 386 LYS I CE  
428  N NZ  . LYS A 54  ? 599.6151 599.6151 599.6151 0.0000 0.0000 0.0000 386 LYS I NZ  
429  N N   . LEU A 55  ? 569.7754 569.7754 569.7754 0.0000 0.0000 0.0000 387 LEU I N   
430  C CA  . LEU A 55  ? 569.1854 569.1854 569.1854 0.0000 0.0000 0.0000 387 LEU I CA  
431  C C   . LEU A 55  ? 569.9001 569.9001 569.9001 0.0000 0.0000 0.0000 387 LEU I C   
432  O O   . LEU A 55  ? 569.9346 569.9346 569.9346 0.0000 0.0000 0.0000 387 LEU I O   
433  C CB  . LEU A 55  ? 568.3537 568.3537 568.3537 0.0000 0.0000 0.0000 387 LEU I CB  
434  C CG  . LEU A 55  ? 568.1437 568.1437 568.1437 0.0000 0.0000 0.0000 387 LEU I CG  
435  C CD1 . LEU A 55  ? 565.8073 565.8073 565.8073 0.0000 0.0000 0.0000 387 LEU I CD1 
436  C CD2 . LEU A 55  ? 568.4012 568.4012 568.4012 0.0000 0.0000 0.0000 387 LEU I CD2 
437  N N   . ASN A 56  ? 581.2758 581.2758 581.2758 0.0000 0.0000 0.0000 388 ASN I N   
438  C CA  . ASN A 56  ? 581.7158 581.7158 581.7158 0.0000 0.0000 0.0000 388 ASN I CA  
439  C C   . ASN A 56  ? 582.3033 582.3033 582.3033 0.0000 0.0000 0.0000 388 ASN I C   
440  O O   . ASN A 56  ? 583.4117 583.4117 583.4117 0.0000 0.0000 0.0000 388 ASN I O   
441  C CB  . ASN A 56  ? 581.5798 581.5798 581.5798 0.0000 0.0000 0.0000 388 ASN I CB  
442  C CG  . ASN A 56  ? 581.2118 581.2118 581.2118 0.0000 0.0000 0.0000 388 ASN I CG  
443  O OD1 . ASN A 56  ? 581.2128 581.2128 581.2128 0.0000 0.0000 0.0000 388 ASN I OD1 
444  N ND2 . ASN A 56  ? 580.9955 580.9955 580.9955 0.0000 0.0000 0.0000 388 ASN I ND2 
445  N N   . ASP A 57  ? 591.4063 591.4063 591.4063 0.0000 0.0000 0.0000 389 ASP I N   
446  C CA  . ASP A 57  ? 591.8955 591.8955 591.8955 0.0000 0.0000 0.0000 389 ASP I CA  
447  C C   . ASP A 57  ? 592.4764 592.4764 592.4764 0.0000 0.0000 0.0000 389 ASP I C   
448  O O   . ASP A 57  ? 593.1659 593.1659 593.1659 0.0000 0.0000 0.0000 389 ASP I O   
449  C CB  . ASP A 57  ? 592.4815 592.4815 592.4815 0.0000 0.0000 0.0000 389 ASP I CB  
450  C CG  . ASP A 57  ? 592.3669 592.3669 592.3669 0.0000 0.0000 0.0000 389 ASP I CG  
451  O OD1 . ASP A 57  ? 592.4779 592.4779 592.4779 0.0000 0.0000 0.0000 389 ASP I OD1 
452  O OD2 . ASP A 57  ? 592.2095 592.2095 592.2095 0.0000 0.0000 0.0000 389 ASP I OD2 
453  N N   . LEU A 58  ? 583.5701 583.5701 583.5701 0.0000 0.0000 0.0000 390 LEU I N   
454  C CA  . LEU A 58  ? 583.3515 583.3515 583.3515 0.0000 0.0000 0.0000 390 LEU I CA  
455  C C   . LEU A 58  ? 584.4026 584.4026 584.4026 0.0000 0.0000 0.0000 390 LEU I C   
456  O O   . LEU A 58  ? 583.6950 583.6950 583.6950 0.0000 0.0000 0.0000 390 LEU I O   
457  C CB  . LEU A 58  ? 582.5566 582.5566 582.5566 0.0000 0.0000 0.0000 390 LEU I CB  
458  C CG  . LEU A 58  ? 582.6416 582.6416 582.6416 0.0000 0.0000 0.0000 390 LEU I CG  
459  C CD1 . LEU A 58  ? 582.5346 582.5346 582.5346 0.0000 0.0000 0.0000 390 LEU I CD1 
460  C CD2 . LEU A 58  ? 582.4147 582.4147 582.4147 0.0000 0.0000 0.0000 390 LEU I CD2 
461  N N   . CYS A 59  ? 625.0589 625.0589 625.0589 0.0000 0.0000 0.0000 391 CYS I N   
462  C CA  . CYS A 59  ? 625.2493 625.2493 625.2493 0.0000 0.0000 0.0000 391 CYS I CA  
463  C C   . CYS A 59  ? 623.6958 623.6958 623.6958 0.0000 0.0000 0.0000 391 CYS I C   
464  O O   . CYS A 59  ? 625.4025 625.4025 625.4025 0.0000 0.0000 0.0000 391 CYS I O   
465  C CB  . CYS A 59  ? 627.4120 627.4120 627.4120 0.0000 0.0000 0.0000 391 CYS I CB  
466  S SG  . CYS A 59  ? 627.5002 627.5002 627.5002 0.0000 0.0000 0.0000 391 CYS I SG  
467  N N   . PHE A 60  ? 554.9674 554.9674 554.9674 0.0000 0.0000 0.0000 392 PHE I N   
468  C CA  . PHE A 60  ? 551.8056 551.8056 551.8056 0.0000 0.0000 0.0000 392 PHE I CA  
469  C C   . PHE A 60  ? 553.6216 553.6216 553.6216 0.0000 0.0000 0.0000 392 PHE I C   
470  O O   . PHE A 60  ? 555.6848 555.6848 555.6848 0.0000 0.0000 0.0000 392 PHE I O   
471  C CB  . PHE A 60  ? 549.0607 549.0607 549.0607 0.0000 0.0000 0.0000 392 PHE I CB  
472  C CG  . PHE A 60  ? 548.8637 548.8637 548.8637 0.0000 0.0000 0.0000 392 PHE I CG  
473  C CD1 . PHE A 60  ? 550.1726 550.1726 550.1726 0.0000 0.0000 0.0000 392 PHE I CD1 
474  C CD2 . PHE A 60  ? 548.8567 548.8567 548.8567 0.0000 0.0000 0.0000 392 PHE I CD2 
475  C CE1 . PHE A 60  ? 550.0188 550.0188 550.0188 0.0000 0.0000 0.0000 392 PHE I CE1 
476  C CE2 . PHE A 60  ? 548.8578 548.8578 548.8578 0.0000 0.0000 0.0000 392 PHE I CE2 
477  C CZ  . PHE A 60  ? 549.0735 549.0735 549.0735 0.0000 0.0000 0.0000 392 PHE I CZ  
478  N N   . THR A 61  ? 582.9211 582.9211 582.9211 0.0000 0.0000 0.0000 393 THR I N   
479  C CA  . THR A 61  ? 583.5417 583.5417 583.5417 0.0000 0.0000 0.0000 393 THR I CA  
480  C C   . THR A 61  ? 581.4645 581.4645 581.4645 0.0000 0.0000 0.0000 393 THR I C   
481  O O   . THR A 61  ? 582.3486 582.3486 582.3486 0.0000 0.0000 0.0000 393 THR I O   
482  C CB  . THR A 61  ? 584.3642 584.3642 584.3642 0.0000 0.0000 0.0000 393 THR I CB  
483  O OG1 . THR A 61  ? 589.2170 589.2170 589.2170 0.0000 0.0000 0.0000 393 THR I OG1 
484  C CG2 . THR A 61  ? 585.7344 585.7344 585.7344 0.0000 0.0000 0.0000 393 THR I CG2 
485  N N   . ASN A 62  ? 539.0376 539.0376 539.0376 0.0000 0.0000 0.0000 394 ASN I N   
486  C CA  . ASN A 62  ? 536.0253 536.0253 536.0253 0.0000 0.0000 0.0000 394 ASN I CA  
487  C C   . ASN A 62  ? 531.7851 531.7851 531.7851 0.0000 0.0000 0.0000 394 ASN I C   
488  O O   . ASN A 62  ? 533.1229 533.1229 533.1229 0.0000 0.0000 0.0000 394 ASN I O   
489  C CB  . ASN A 62  ? 536.9922 536.9922 536.9922 0.0000 0.0000 0.0000 394 ASN I CB  
490  C CG  . ASN A 62  ? 533.6617 533.6617 533.6617 0.0000 0.0000 0.0000 394 ASN I CG  
491  O OD1 . ASN A 62  ? 531.6041 531.6041 531.6041 0.0000 0.0000 0.0000 394 ASN I OD1 
492  N ND2 . ASN A 62  ? 534.4091 534.4091 534.4091 0.0000 0.0000 0.0000 394 ASN I ND2 
493  N N   . VAL A 63  ? 437.7903 437.7903 437.7903 0.0000 0.0000 0.0000 395 VAL I N   
494  C CA  . VAL A 63  ? 433.8149 433.8149 433.8149 0.0000 0.0000 0.0000 395 VAL I CA  
495  C C   . VAL A 63  ? 433.0848 433.0848 433.0848 0.0000 0.0000 0.0000 395 VAL I C   
496  O O   . VAL A 63  ? 435.2294 435.2294 435.2294 0.0000 0.0000 0.0000 395 VAL I O   
497  C CB  . VAL A 63  ? 432.4149 432.4149 432.4149 0.0000 0.0000 0.0000 395 VAL I CB  
498  C CG1 . VAL A 63  ? 430.9193 430.9193 430.9193 0.0000 0.0000 0.0000 395 VAL I CG1 
499  C CG2 . VAL A 63  ? 435.9442 435.9442 435.9442 0.0000 0.0000 0.0000 395 VAL I CG2 
500  N N   . TYR A 64  ? 431.0933 431.0933 431.0933 0.0000 0.0000 0.0000 396 TYR I N   
501  C CA  . TYR A 64  ? 429.3009 429.3009 429.3009 0.0000 0.0000 0.0000 396 TYR I CA  
502  C C   . TYR A 64  ? 429.6652 429.6652 429.6652 0.0000 0.0000 0.0000 396 TYR I C   
503  O O   . TYR A 64  ? 432.2379 432.2379 432.2379 0.0000 0.0000 0.0000 396 TYR I O   
504  C CB  . TYR A 64  ? 430.4658 430.4658 430.4658 0.0000 0.0000 0.0000 396 TYR I CB  
505  C CG  . TYR A 64  ? 430.8062 430.8062 430.8062 0.0000 0.0000 0.0000 396 TYR I CG  
506  C CD1 . TYR A 64  ? 432.2815 432.2815 432.2815 0.0000 0.0000 0.0000 396 TYR I CD1 
507  C CD2 . TYR A 64  ? 431.7008 431.7008 431.7008 0.0000 0.0000 0.0000 396 TYR I CD2 
508  C CE1 . TYR A 64  ? 432.7193 432.7193 432.7193 0.0000 0.0000 0.0000 396 TYR I CE1 
509  C CE2 . TYR A 64  ? 432.7008 432.7008 432.7008 0.0000 0.0000 0.0000 396 TYR I CE2 
510  C CZ  . TYR A 64  ? 432.6374 432.6374 432.6374 0.0000 0.0000 0.0000 396 TYR I CZ  
511  O OH  . TYR A 64  ? 432.9418 432.9418 432.9418 0.0000 0.0000 0.0000 396 TYR I OH  
512  N N   . ALA A 65  ? 429.3297 429.3297 429.3297 0.0000 0.0000 0.0000 397 ALA I N   
513  C CA  . ALA A 65  ? 429.2417 429.2417 429.2417 0.0000 0.0000 0.0000 397 ALA I CA  
514  C C   . ALA A 65  ? 430.2507 430.2507 430.2507 0.0000 0.0000 0.0000 397 ALA I C   
515  O O   . ALA A 65  ? 431.8027 431.8027 431.8027 0.0000 0.0000 0.0000 397 ALA I O   
516  C CB  . ALA A 65  ? 430.2240 430.2240 430.2240 0.0000 0.0000 0.0000 397 ALA I CB  
517  N N   . ASP A 66  ? 430.9215 430.9215 430.9215 0.0000 0.0000 0.0000 398 ASP I N   
518  C CA  . ASP A 66  ? 429.3517 429.3517 429.3517 0.0000 0.0000 0.0000 398 ASP I CA  
519  C C   . ASP A 66  ? 429.2078 429.2078 429.2078 0.0000 0.0000 0.0000 398 ASP I C   
520  O O   . ASP A 66  ? 432.2116 432.2116 432.2116 0.0000 0.0000 0.0000 398 ASP I O   
521  C CB  . ASP A 66  ? 430.3289 430.3289 430.3289 0.0000 0.0000 0.0000 398 ASP I CB  
522  C CG  . ASP A 66  ? 430.3388 430.3388 430.3388 0.0000 0.0000 0.0000 398 ASP I CG  
523  O OD1 . ASP A 66  ? 430.2296 430.2296 430.2296 0.0000 0.0000 0.0000 398 ASP I OD1 
524  O OD2 . ASP A 66  ? 431.0819 431.0819 431.0819 0.0000 0.0000 0.0000 398 ASP I OD2 
525  N N   . SER A 67  ? 428.4829 428.4829 428.4829 0.0000 0.0000 0.0000 399 SER I N   
526  C CA  . SER A 67  ? 428.8679 428.8679 428.8679 0.0000 0.0000 0.0000 399 SER I CA  
527  C C   . SER A 67  ? 430.1789 430.1789 430.1789 0.0000 0.0000 0.0000 399 SER I C   
528  O O   . SER A 67  ? 432.3308 432.3308 432.3308 0.0000 0.0000 0.0000 399 SER I O   
529  C CB  . SER A 67  ? 430.4069 430.4069 430.4069 0.0000 0.0000 0.0000 399 SER I CB  
530  O OG  . SER A 67  ? 431.8275 431.8275 431.8275 0.0000 0.0000 0.0000 399 SER I OG  
531  N N   . PHE A 68  ? 430.1232 430.1232 430.1232 0.0000 0.0000 0.0000 400 PHE I N   
532  C CA  . PHE A 68  ? 429.2510 429.2510 429.2510 0.0000 0.0000 0.0000 400 PHE I CA  
533  C C   . PHE A 68  ? 429.1273 429.1273 429.1273 0.0000 0.0000 0.0000 400 PHE I C   
534  O O   . PHE A 68  ? 432.3759 432.3759 432.3759 0.0000 0.0000 0.0000 400 PHE I O   
535  C CB  . PHE A 68  ? 430.2526 430.2526 430.2526 0.0000 0.0000 0.0000 400 PHE I CB  
536  C CG  . PHE A 68  ? 429.9723 429.9723 429.9723 0.0000 0.0000 0.0000 400 PHE I CG  
537  C CD1 . PHE A 68  ? 430.4704 430.4704 430.4704 0.0000 0.0000 0.0000 400 PHE I CD1 
538  C CD2 . PHE A 68  ? 430.0485 430.0485 430.0485 0.0000 0.0000 0.0000 400 PHE I CD2 
539  C CE1 . PHE A 68  ? 431.0368 431.0368 431.0368 0.0000 0.0000 0.0000 400 PHE I CE1 
540  C CE2 . PHE A 68  ? 430.2622 430.2622 430.2622 0.0000 0.0000 0.0000 400 PHE I CE2 
541  C CZ  . PHE A 68  ? 431.0142 431.0142 431.0142 0.0000 0.0000 0.0000 400 PHE I CZ  
542  N N   . VAL A 69  ? 428.3384 428.3384 428.3384 0.0000 0.0000 0.0000 401 VAL I N   
543  C CA  . VAL A 69  ? 429.2953 429.2953 429.2953 0.0000 0.0000 0.0000 401 VAL I CA  
544  C C   . VAL A 69  ? 430.0037 430.0037 430.0037 0.0000 0.0000 0.0000 401 VAL I C   
545  O O   . VAL A 69  ? 431.2503 431.2503 431.2503 0.0000 0.0000 0.0000 401 VAL I O   
546  C CB  . VAL A 69  ? 429.2224 429.2224 429.2224 0.0000 0.0000 0.0000 401 VAL I CB  
547  C CG1 . VAL A 69  ? 430.6997 430.6997 430.6997 0.0000 0.0000 0.0000 401 VAL I CG1 
548  C CG2 . VAL A 69  ? 430.0893 430.0893 430.0893 0.0000 0.0000 0.0000 401 VAL I CG2 
549  N N   . ILE A 70  ? 430.2688 430.2688 430.2688 0.0000 0.0000 0.0000 402 ILE I N   
550  C CA  . ILE A 70  ? 429.4806 429.4806 429.4806 0.0000 0.0000 0.0000 402 ILE I CA  
551  C C   . ILE A 70  ? 430.3933 430.3933 430.3933 0.0000 0.0000 0.0000 402 ILE I C   
552  O O   . ILE A 70  ? 432.1991 432.1991 432.1991 0.0000 0.0000 0.0000 402 ILE I O   
553  C CB  . ILE A 70  ? 429.7376 429.7376 429.7376 0.0000 0.0000 0.0000 402 ILE I CB  
554  C CG1 . ILE A 70  ? 429.5865 429.5865 429.5865 0.0000 0.0000 0.0000 402 ILE I CG1 
555  C CG2 . ILE A 70  ? 431.3316 431.3316 431.3316 0.0000 0.0000 0.0000 402 ILE I CG2 
556  C CD1 . ILE A 70  ? 430.1401 430.1401 430.1401 0.0000 0.0000 0.0000 402 ILE I CD1 
557  N N   . ARG A 71  ? 430.5054 430.5054 430.5054 0.0000 0.0000 0.0000 403 ARG I N   
558  C CA  . ARG A 71  ? 429.8321 429.8321 429.8321 0.0000 0.0000 0.0000 403 ARG I CA  
559  C C   . ARG A 71  ? 430.8156 430.8156 430.8156 0.0000 0.0000 0.0000 403 ARG I C   
560  O O   . ARG A 71  ? 432.7066 432.7066 432.7066 0.0000 0.0000 0.0000 403 ARG I O   
561  C CB  . ARG A 71  ? 430.4325 430.4325 430.4325 0.0000 0.0000 0.0000 403 ARG I CB  
562  C CG  . ARG A 71  ? 431.7138 431.7138 431.7138 0.0000 0.0000 0.0000 403 ARG I CG  
563  C CD  . ARG A 71  ? 431.2661 431.2661 431.2661 0.0000 0.0000 0.0000 403 ARG I CD  
564  N NE  . ARG A 71  ? 431.9858 431.9858 431.9858 0.0000 0.0000 0.0000 403 ARG I NE  
565  C CZ  . ARG A 71  ? 432.1638 432.1638 432.1638 0.0000 0.0000 0.0000 403 ARG I CZ  
566  N NH1 . ARG A 71  ? 431.6067 431.6067 431.6067 0.0000 0.0000 0.0000 403 ARG I NH1 
567  N NH2 . ARG A 71  ? 432.8985 432.8985 432.8985 0.0000 0.0000 0.0000 403 ARG I NH2 
568  N N   . GLY A 72  ? 431.1134 431.1134 431.1134 0.0000 0.0000 0.0000 404 GLY I N   
569  C CA  . GLY A 72  ? 431.8227 431.8227 431.8227 0.0000 0.0000 0.0000 404 GLY I CA  
570  C C   . GLY A 72  ? 432.6149 432.6149 432.6149 0.0000 0.0000 0.0000 404 GLY I C   
571  O O   . GLY A 72  ? 431.4143 431.4143 431.4143 0.0000 0.0000 0.0000 404 GLY I O   
572  N N   . ASP A 73  ? 466.6458 466.6458 466.6458 0.0000 0.0000 0.0000 405 ASP I N   
573  C CA  . ASP A 73  ? 467.4532 467.4532 467.4532 0.0000 0.0000 0.0000 405 ASP I CA  
574  C C   . ASP A 73  ? 466.1065 466.1065 466.1065 0.0000 0.0000 0.0000 405 ASP I C   
575  O O   . ASP A 73  ? 466.7273 466.7273 466.7273 0.0000 0.0000 0.0000 405 ASP I O   
576  C CB  . ASP A 73  ? 468.6095 468.6095 468.6095 0.0000 0.0000 0.0000 405 ASP I CB  
577  C CG  . ASP A 73  ? 469.3352 469.3352 469.3352 0.0000 0.0000 0.0000 405 ASP I CG  
578  O OD1 . ASP A 73  ? 469.9230 469.9230 469.9230 0.0000 0.0000 0.0000 405 ASP I OD1 
579  O OD2 . ASP A 73  ? 468.4205 468.4205 468.4205 0.0000 0.0000 0.0000 405 ASP I OD2 
580  N N   . GLU A 74  ? 432.5735 432.5735 432.5735 0.0000 0.0000 0.0000 406 GLU I N   
581  C CA  . GLU A 74  ? 430.6556 430.6556 430.6556 0.0000 0.0000 0.0000 406 GLU I CA  
582  C C   . GLU A 74  ? 431.5525 431.5525 431.5525 0.0000 0.0000 0.0000 406 GLU I C   
583  O O   . GLU A 74  ? 432.2818 432.2818 432.2818 0.0000 0.0000 0.0000 406 GLU I O   
584  C CB  . GLU A 74  ? 431.1880 431.1880 431.1880 0.0000 0.0000 0.0000 406 GLU I CB  
585  C CG  . GLU A 74  ? 431.9748 431.9748 431.9748 0.0000 0.0000 0.0000 406 GLU I CG  
586  C CD  . GLU A 74  ? 432.2931 432.2931 432.2931 0.0000 0.0000 0.0000 406 GLU I CD  
587  O OE1 . GLU A 74  ? 432.3520 432.3520 432.3520 0.0000 0.0000 0.0000 406 GLU I OE1 
588  O OE2 . GLU A 74  ? 433.3187 433.3187 433.3187 0.0000 0.0000 0.0000 406 GLU I OE2 
589  N N   . VAL A 75  ? 431.9228 431.9228 431.9228 0.0000 0.0000 0.0000 407 VAL I N   
590  C CA  . VAL A 75  ? 430.7633 430.7633 430.7633 0.0000 0.0000 0.0000 407 VAL I CA  
591  C C   . VAL A 75  ? 430.8458 430.8458 430.8458 0.0000 0.0000 0.0000 407 VAL I C   
592  O O   . VAL A 75  ? 431.3741 431.3741 431.3741 0.0000 0.0000 0.0000 407 VAL I O   
593  C CB  . VAL A 75  ? 430.9828 430.9828 430.9828 0.0000 0.0000 0.0000 407 VAL I CB  
594  C CG1 . VAL A 75  ? 431.0487 431.0487 431.0487 0.0000 0.0000 0.0000 407 VAL I CG1 
595  C CG2 . VAL A 75  ? 431.0538 431.0538 431.0538 0.0000 0.0000 0.0000 407 VAL I CG2 
596  N N   . ARG A 76  ? 431.2433 431.2433 431.2433 0.0000 0.0000 0.0000 408 ARG I N   
597  C CA  . ARG A 76  ? 430.5529 430.5529 430.5529 0.0000 0.0000 0.0000 408 ARG I CA  
598  C C   . ARG A 76  ? 431.1699 431.1699 431.1699 0.0000 0.0000 0.0000 408 ARG I C   
599  O O   . ARG A 76  ? 432.5984 432.5984 432.5984 0.0000 0.0000 0.0000 408 ARG I O   
600  C CB  . ARG A 76  ? 430.7313 430.7313 430.7313 0.0000 0.0000 0.0000 408 ARG I CB  
601  C CG  . ARG A 76  ? 431.5080 431.5080 431.5080 0.0000 0.0000 0.0000 408 ARG I CG  
602  C CD  . ARG A 76  ? 431.4805 431.4805 431.4805 0.0000 0.0000 0.0000 408 ARG I CD  
603  N NE  . ARG A 76  ? 431.7133 431.7133 431.7133 0.0000 0.0000 0.0000 408 ARG I NE  
604  C CZ  . ARG A 76  ? 431.5022 431.5022 431.5022 0.0000 0.0000 0.0000 408 ARG I CZ  
605  N NH1 . ARG A 76  ? 431.3358 431.3358 431.3358 0.0000 0.0000 0.0000 408 ARG I NH1 
606  N NH2 . ARG A 76  ? 431.7651 431.7651 431.7651 0.0000 0.0000 0.0000 408 ARG I NH2 
607  N N   . GLN A 77  ? 431.2744 431.2744 431.2744 0.0000 0.0000 0.0000 409 GLN I N   
608  C CA  . GLN A 77  ? 430.6805 430.6805 430.6805 0.0000 0.0000 0.0000 409 GLN I CA  
609  C C   . GLN A 77  ? 431.3222 431.3222 431.3222 0.0000 0.0000 0.0000 409 GLN I C   
610  O O   . GLN A 77  ? 431.0153 431.0153 431.0153 0.0000 0.0000 0.0000 409 GLN I O   
611  C CB  . GLN A 77  ? 430.7526 430.7526 430.7526 0.0000 0.0000 0.0000 409 GLN I CB  
612  C CG  . GLN A 77  ? 432.2396 432.2396 432.2396 0.0000 0.0000 0.0000 409 GLN I CG  
613  C CD  . GLN A 77  ? 431.0141 431.0141 431.0141 0.0000 0.0000 0.0000 409 GLN I CD  
614  O OE1 . GLN A 77  ? 431.2328 431.2328 431.2328 0.0000 0.0000 0.0000 409 GLN I OE1 
615  N NE2 . GLN A 77  ? 431.2663 431.2663 431.2663 0.0000 0.0000 0.0000 409 GLN I NE2 
616  N N   . ILE A 78  ? 432.2564 432.2564 432.2564 0.0000 0.0000 0.0000 410 ILE I N   
617  C CA  . ILE A 78  ? 430.5091 430.5091 430.5091 0.0000 0.0000 0.0000 410 ILE I CA  
618  C C   . ILE A 78  ? 430.1709 430.1709 430.1709 0.0000 0.0000 0.0000 410 ILE I C   
619  O O   . ILE A 78  ? 431.1278 431.1278 431.1278 0.0000 0.0000 0.0000 410 ILE I O   
620  C CB  . ILE A 78  ? 429.9733 429.9733 429.9733 0.0000 0.0000 0.0000 410 ILE I CB  
621  C CG1 . ILE A 78  ? 430.0135 430.0135 430.0135 0.0000 0.0000 0.0000 410 ILE I CG1 
622  C CG2 . ILE A 78  ? 430.6738 430.6738 430.6738 0.0000 0.0000 0.0000 410 ILE I CG2 
623  C CD1 . ILE A 78  ? 430.3740 430.3740 430.3740 0.0000 0.0000 0.0000 410 ILE I CD1 
624  N N   . ALA A 79  ? 430.7079 430.7079 430.7079 0.0000 0.0000 0.0000 411 ALA I N   
625  C CA  . ALA A 79  ? 430.1178 430.1178 430.1178 0.0000 0.0000 0.0000 411 ALA I CA  
626  C C   . ALA A 79  ? 430.6732 430.6732 430.6732 0.0000 0.0000 0.0000 411 ALA I C   
627  O O   . ALA A 79  ? 432.3018 432.3018 432.3018 0.0000 0.0000 0.0000 411 ALA I O   
628  C CB  . ALA A 79  ? 430.9505 430.9505 430.9505 0.0000 0.0000 0.0000 411 ALA I CB  
629  N N   . PRO A 80  ? 430.0767 430.0767 430.0767 0.0000 0.0000 0.0000 412 PRO I N   
630  C CA  . PRO A 80  ? 430.6804 430.6804 430.6804 0.0000 0.0000 0.0000 412 PRO I CA  
631  C C   . PRO A 80  ? 432.4494 432.4494 432.4494 0.0000 0.0000 0.0000 412 PRO I C   
632  O O   . PRO A 80  ? 432.3974 432.3974 432.3974 0.0000 0.0000 0.0000 412 PRO I O   
633  C CB  . PRO A 80  ? 430.3945 430.3945 430.3945 0.0000 0.0000 0.0000 412 PRO I CB  
634  C CG  . PRO A 80  ? 430.9673 430.9673 430.9673 0.0000 0.0000 0.0000 412 PRO I CG  
635  C CD  . PRO A 80  ? 430.9155 430.9155 430.9155 0.0000 0.0000 0.0000 412 PRO I CD  
636  N N   . GLY A 81  ? 444.1305 444.1305 444.1305 0.0000 0.0000 0.0000 413 GLY I N   
637  C CA  . GLY A 81  ? 444.1143 444.1143 444.1143 0.0000 0.0000 0.0000 413 GLY I CA  
638  C C   . GLY A 81  ? 444.0303 444.0303 444.0303 0.0000 0.0000 0.0000 413 GLY I C   
639  O O   . GLY A 81  ? 443.9975 443.9975 443.9975 0.0000 0.0000 0.0000 413 GLY I O   
640  N N   . GLN A 82  ? 443.8559 443.8559 443.8559 0.0000 0.0000 0.0000 414 GLN I N   
641  C CA  . GLN A 82  ? 443.7732 443.7732 443.7732 0.0000 0.0000 0.0000 414 GLN I CA  
642  C C   . GLN A 82  ? 445.5935 445.5935 445.5935 0.0000 0.0000 0.0000 414 GLN I C   
643  O O   . GLN A 82  ? 445.0216 445.0216 445.0216 0.0000 0.0000 0.0000 414 GLN I O   
644  C CB  . GLN A 82  ? 442.9087 442.9087 442.9087 0.0000 0.0000 0.0000 414 GLN I CB  
645  C CG  . GLN A 82  ? 443.0925 443.0925 443.0925 0.0000 0.0000 0.0000 414 GLN I CG  
646  C CD  . GLN A 82  ? 443.6806 443.6806 443.6806 0.0000 0.0000 0.0000 414 GLN I CD  
647  O OE1 . GLN A 82  ? 444.1476 444.1476 444.1476 0.0000 0.0000 0.0000 414 GLN I OE1 
648  N NE2 . GLN A 82  ? 444.2942 444.2942 444.2942 0.0000 0.0000 0.0000 414 GLN I NE2 
649  N N   . THR A 83  ? 470.8244 470.8244 470.8244 0.0000 0.0000 0.0000 415 THR I N   
650  C CA  . THR A 83  ? 470.9130 470.9130 470.9130 0.0000 0.0000 0.0000 415 THR I CA  
651  C C   . THR A 83  ? 469.3455 469.3455 469.3455 0.0000 0.0000 0.0000 415 THR I C   
652  O O   . THR A 83  ? 469.8596 469.8596 469.8596 0.0000 0.0000 0.0000 415 THR I O   
653  C CB  . THR A 83  ? 472.3386 472.3386 472.3386 0.0000 0.0000 0.0000 415 THR I CB  
654  O OG1 . THR A 83  ? 472.4487 472.4487 472.4487 0.0000 0.0000 0.0000 415 THR I OG1 
655  C CG2 . THR A 83  ? 472.1997 472.1997 472.1997 0.0000 0.0000 0.0000 415 THR I CG2 
656  N N   . GLY A 84  ? 432.9047 432.9047 432.9047 0.0000 0.0000 0.0000 416 GLY I N   
657  C CA  . GLY A 84  ? 432.0043 432.0043 432.0043 0.0000 0.0000 0.0000 416 GLY I CA  
658  C C   . GLY A 84  ? 431.1882 431.1882 431.1882 0.0000 0.0000 0.0000 416 GLY I C   
659  O O   . GLY A 84  ? 432.6011 432.6011 432.6011 0.0000 0.0000 0.0000 416 GLY I O   
660  N N   . LYS A 85  ? 429.9816 429.9816 429.9816 0.0000 0.0000 0.0000 417 LYS I N   
661  C CA  . LYS A 85  ? 430.4986 430.4986 430.4986 0.0000 0.0000 0.0000 417 LYS I CA  
662  C C   . LYS A 85  ? 431.0913 431.0913 431.0913 0.0000 0.0000 0.0000 417 LYS I C   
663  O O   . LYS A 85  ? 431.6225 431.6225 431.6225 0.0000 0.0000 0.0000 417 LYS I O   
664  C CB  . LYS A 85  ? 430.6801 430.6801 430.6801 0.0000 0.0000 0.0000 417 LYS I CB  
665  C CG  . LYS A 85  ? 431.1370 431.1370 431.1370 0.0000 0.0000 0.0000 417 LYS I CG  
666  C CD  . LYS A 85  ? 431.9443 431.9443 431.9443 0.0000 0.0000 0.0000 417 LYS I CD  
667  C CE  . LYS A 85  ? 431.1976 431.1976 431.1976 0.0000 0.0000 0.0000 417 LYS I CE  
668  N NZ  . LYS A 85  ? 431.1054 431.1054 431.1054 0.0000 0.0000 0.0000 417 LYS I NZ  
669  N N   . ILE A 86  ? 431.5848 431.5848 431.5848 0.0000 0.0000 0.0000 418 ILE I N   
670  C CA  . ILE A 86  ? 430.5294 430.5294 430.5294 0.0000 0.0000 0.0000 418 ILE I CA  
671  C C   . ILE A 86  ? 429.9397 429.9397 429.9397 0.0000 0.0000 0.0000 418 ILE I C   
672  O O   . ILE A 86  ? 431.2402 431.2402 431.2402 0.0000 0.0000 0.0000 418 ILE I O   
673  C CB  . ILE A 86  ? 429.7407 429.7407 429.7407 0.0000 0.0000 0.0000 418 ILE I CB  
674  C CG1 . ILE A 86  ? 429.7637 429.7637 429.7637 0.0000 0.0000 0.0000 418 ILE I CG1 
675  C CG2 . ILE A 86  ? 430.3764 430.3764 430.3764 0.0000 0.0000 0.0000 418 ILE I CG2 
676  C CD1 . ILE A 86  ? 430.7688 430.7688 430.7688 0.0000 0.0000 0.0000 418 ILE I CD1 
677  N N   . ALA A 87  ? 430.0819 430.0819 430.0819 0.0000 0.0000 0.0000 419 ALA I N   
678  C CA  . ALA A 87  ? 430.1632 430.1632 430.1632 0.0000 0.0000 0.0000 419 ALA I CA  
679  C C   . ALA A 87  ? 430.2908 430.2908 430.2908 0.0000 0.0000 0.0000 419 ALA I C   
680  O O   . ALA A 87  ? 430.3765 430.3765 430.3765 0.0000 0.0000 0.0000 419 ALA I O   
681  C CB  . ALA A 87  ? 430.9748 430.9748 430.9748 0.0000 0.0000 0.0000 419 ALA I CB  
682  N N   . ASP A 88  ? 431.3995 431.3995 431.3995 0.0000 0.0000 0.0000 420 ASP I N   
683  C CA  . ASP A 88  ? 430.3840 430.3840 430.3840 0.0000 0.0000 0.0000 420 ASP I CA  
684  C C   . ASP A 88  ? 430.3073 430.3073 430.3073 0.0000 0.0000 0.0000 420 ASP I C   
685  O O   . ASP A 88  ? 431.0184 431.0184 431.0184 0.0000 0.0000 0.0000 420 ASP I O   
686  C CB  . ASP A 88  ? 431.1866 431.1866 431.1866 0.0000 0.0000 0.0000 420 ASP I CB  
687  C CG  . ASP A 88  ? 431.4706 431.4706 431.4706 0.0000 0.0000 0.0000 420 ASP I CG  
688  O OD1 . ASP A 88  ? 432.2608 432.2608 432.2608 0.0000 0.0000 0.0000 420 ASP I OD1 
689  O OD2 . ASP A 88  ? 431.1485 431.1485 431.1485 0.0000 0.0000 0.0000 420 ASP I OD2 
690  N N   . TYR A 89  ? 430.9938 430.9938 430.9938 0.0000 0.0000 0.0000 421 TYR I N   
691  C CA  . TYR A 89  ? 430.8731 430.8731 430.8731 0.0000 0.0000 0.0000 421 TYR I CA  
692  C C   . TYR A 89  ? 430.2707 430.2707 430.2707 0.0000 0.0000 0.0000 421 TYR I C   
693  O O   . TYR A 89  ? 430.5799 430.5799 430.5799 0.0000 0.0000 0.0000 421 TYR I O   
694  C CB  . TYR A 89  ? 431.6046 431.6046 431.6046 0.0000 0.0000 0.0000 421 TYR I CB  
695  C CG  . TYR A 89  ? 431.3872 431.3872 431.3872 0.0000 0.0000 0.0000 421 TYR I CG  
696  C CD1 . TYR A 89  ? 431.7294 431.7294 431.7294 0.0000 0.0000 0.0000 421 TYR I CD1 
697  C CD2 . TYR A 89  ? 431.0118 431.0118 431.0118 0.0000 0.0000 0.0000 421 TYR I CD2 
698  C CE1 . TYR A 89  ? 431.3143 431.3143 431.3143 0.0000 0.0000 0.0000 421 TYR I CE1 
699  C CE2 . TYR A 89  ? 431.1728 431.1728 431.1728 0.0000 0.0000 0.0000 421 TYR I CE2 
700  C CZ  . TYR A 89  ? 430.9687 430.9687 430.9687 0.0000 0.0000 0.0000 421 TYR I CZ  
701  O OH  . TYR A 89  ? 431.0612 431.0612 431.0612 0.0000 0.0000 0.0000 421 TYR I OH  
702  N N   . ASN A 90  ? 430.6753 430.6753 430.6753 0.0000 0.0000 0.0000 422 ASN I N   
703  C CA  . ASN A 90  ? 430.3609 430.3609 430.3609 0.0000 0.0000 0.0000 422 ASN I CA  
704  C C   . ASN A 90  ? 430.3551 430.3551 430.3551 0.0000 0.0000 0.0000 422 ASN I C   
705  O O   . ASN A 90  ? 430.3258 430.3258 430.3258 0.0000 0.0000 0.0000 422 ASN I O   
706  C CB  . ASN A 90  ? 430.8750 430.8750 430.8750 0.0000 0.0000 0.0000 422 ASN I CB  
707  C CG  . ASN A 90  ? 430.3598 430.3598 430.3598 0.0000 0.0000 0.0000 422 ASN I CG  
708  O OD1 . ASN A 90  ? 431.2980 431.2980 431.2980 0.0000 0.0000 0.0000 422 ASN I OD1 
709  N ND2 . ASN A 90  ? 431.0393 431.0393 431.0393 0.0000 0.0000 0.0000 422 ASN I ND2 
710  N N   . TYR A 91  ? 431.2110 431.2110 431.2110 0.0000 0.0000 0.0000 423 TYR I N   
711  C CA  . TYR A 91  ? 430.1898 430.1898 430.1898 0.0000 0.0000 0.0000 423 TYR I CA  
712  C C   . TYR A 91  ? 430.1425 430.1425 430.1425 0.0000 0.0000 0.0000 423 TYR I C   
713  O O   . TYR A 91  ? 431.9761 431.9761 431.9761 0.0000 0.0000 0.0000 423 TYR I O   
714  C CB  . TYR A 91  ? 430.5209 430.5209 430.5209 0.0000 0.0000 0.0000 423 TYR I CB  
715  C CG  . TYR A 91  ? 429.8726 429.8726 429.8726 0.0000 0.0000 0.0000 423 TYR I CG  
716  C CD1 . TYR A 91  ? 430.0870 430.0870 430.0870 0.0000 0.0000 0.0000 423 TYR I CD1 
717  C CD2 . TYR A 91  ? 431.1512 431.1512 431.1512 0.0000 0.0000 0.0000 423 TYR I CD2 
718  C CE1 . TYR A 91  ? 429.7161 429.7161 429.7161 0.0000 0.0000 0.0000 423 TYR I CE1 
719  C CE2 . TYR A 91  ? 431.0436 431.0436 431.0436 0.0000 0.0000 0.0000 423 TYR I CE2 
720  C CZ  . TYR A 91  ? 429.9806 429.9806 429.9806 0.0000 0.0000 0.0000 423 TYR I CZ  
721  O OH  . TYR A 91  ? 431.5944 431.5944 431.5944 0.0000 0.0000 0.0000 423 TYR I OH  
722  N N   . LYS A 92  ? 429.8081 429.8081 429.8081 0.0000 0.0000 0.0000 424 LYS I N   
723  C CA  . LYS A 92  ? 430.2156 430.2156 430.2156 0.0000 0.0000 0.0000 424 LYS I CA  
724  C C   . LYS A 92  ? 430.9580 430.9580 430.9580 0.0000 0.0000 0.0000 424 LYS I C   
725  O O   . LYS A 92  ? 432.5209 432.5209 432.5209 0.0000 0.0000 0.0000 424 LYS I O   
726  C CB  . LYS A 92  ? 430.5247 430.5247 430.5247 0.0000 0.0000 0.0000 424 LYS I CB  
727  C CG  . LYS A 92  ? 431.1623 431.1623 431.1623 0.0000 0.0000 0.0000 424 LYS I CG  
728  C CD  . LYS A 92  ? 431.8044 431.8044 431.8044 0.0000 0.0000 0.0000 424 LYS I CD  
729  C CE  . LYS A 92  ? 431.2294 431.2294 431.2294 0.0000 0.0000 0.0000 424 LYS I CE  
730  N NZ  . LYS A 92  ? 432.3504 432.3504 432.3504 0.0000 0.0000 0.0000 424 LYS I NZ  
731  N N   . LEU A 93  ? 430.1589 430.1589 430.1589 0.0000 0.0000 0.0000 425 LEU I N   
732  C CA  . LEU A 93  ? 429.4581 429.4581 429.4581 0.0000 0.0000 0.0000 425 LEU I CA  
733  C C   . LEU A 93  ? 430.1437 430.1437 430.1437 0.0000 0.0000 0.0000 425 LEU I C   
734  O O   . LEU A 93  ? 432.3806 432.3806 432.3806 0.0000 0.0000 0.0000 425 LEU I O   
735  C CB  . LEU A 93  ? 429.9710 429.9710 429.9710 0.0000 0.0000 0.0000 425 LEU I CB  
736  C CG  . LEU A 93  ? 429.7124 429.7124 429.7124 0.0000 0.0000 0.0000 425 LEU I CG  
737  C CD1 . LEU A 93  ? 430.6970 430.6970 430.6970 0.0000 0.0000 0.0000 425 LEU I CD1 
738  C CD2 . LEU A 93  ? 431.8843 431.8843 431.8843 0.0000 0.0000 0.0000 425 LEU I CD2 
739  N N   . PRO A 94  ? 429.2259 429.2259 429.2259 0.0000 0.0000 0.0000 426 PRO I N   
740  C CA  . PRO A 94  ? 431.3743 431.3743 431.3743 0.0000 0.0000 0.0000 426 PRO I CA  
741  C C   . PRO A 94  ? 434.1786 434.1786 434.1786 0.0000 0.0000 0.0000 426 PRO I C   
742  O O   . PRO A 94  ? 434.5098 434.5098 434.5098 0.0000 0.0000 0.0000 426 PRO I O   
743  C CB  . PRO A 94  ? 431.6400 431.6400 431.6400 0.0000 0.0000 0.0000 426 PRO I CB  
744  C CG  . PRO A 94  ? 430.8801 430.8801 430.8801 0.0000 0.0000 0.0000 426 PRO I CG  
745  C CD  . PRO A 94  ? 430.4942 430.4942 430.4942 0.0000 0.0000 0.0000 426 PRO I CD  
746  N N   . ASP A 95  ? 460.0940 460.0940 460.0940 0.0000 0.0000 0.0000 427 ASP I N   
747  C CA  . ASP A 95  ? 460.5228 460.5228 460.5228 0.0000 0.0000 0.0000 427 ASP I CA  
748  C C   . ASP A 95  ? 460.6315 460.6315 460.6315 0.0000 0.0000 0.0000 427 ASP I C   
749  O O   . ASP A 95  ? 460.2434 460.2434 460.2434 0.0000 0.0000 0.0000 427 ASP I O   
750  C CB  . ASP A 95  ? 461.0885 461.0885 461.0885 0.0000 0.0000 0.0000 427 ASP I CB  
751  C CG  . ASP A 95  ? 460.9777 460.9777 460.9777 0.0000 0.0000 0.0000 427 ASP I CG  
752  O OD1 . ASP A 95  ? 460.7248 460.7248 460.7248 0.0000 0.0000 0.0000 427 ASP I OD1 
753  O OD2 . ASP A 95  ? 461.0139 461.0139 461.0139 0.0000 0.0000 0.0000 427 ASP I OD2 
754  N N   . ASP A 96  ? 478.1118 478.1118 478.1118 0.0000 0.0000 0.0000 428 ASP I N   
755  C CA  . ASP A 96  ? 478.4508 478.4508 478.4508 0.0000 0.0000 0.0000 428 ASP I CA  
756  C C   . ASP A 96  ? 477.2319 477.2319 477.2319 0.0000 0.0000 0.0000 428 ASP I C   
757  O O   . ASP A 96  ? 478.3469 478.3469 478.3469 0.0000 0.0000 0.0000 428 ASP I O   
758  C CB  . ASP A 96  ? 479.6840 479.6840 479.6840 0.0000 0.0000 0.0000 428 ASP I CB  
759  C CG  . ASP A 96  ? 480.6431 480.6431 480.6431 0.0000 0.0000 0.0000 428 ASP I CG  
760  O OD1 . ASP A 96  ? 480.4475 480.4475 480.4475 0.0000 0.0000 0.0000 428 ASP I OD1 
761  O OD2 . ASP A 96  ? 480.7028 480.7028 480.7028 0.0000 0.0000 0.0000 428 ASP I OD2 
762  N N   . PHE A 97  ? 434.3045 434.3045 434.3045 0.0000 0.0000 0.0000 429 PHE I N   
763  C CA  . PHE A 97  ? 431.8123 431.8123 431.8123 0.0000 0.0000 0.0000 429 PHE I CA  
764  C C   . PHE A 97  ? 431.4692 431.4692 431.4692 0.0000 0.0000 0.0000 429 PHE I C   
765  O O   . PHE A 97  ? 431.5342 431.5342 431.5342 0.0000 0.0000 0.0000 429 PHE I O   
766  C CB  . PHE A 97  ? 430.6751 430.6751 430.6751 0.0000 0.0000 0.0000 429 PHE I CB  
767  C CG  . PHE A 97  ? 429.6903 429.6903 429.6903 0.0000 0.0000 0.0000 429 PHE I CG  
768  C CD1 . PHE A 97  ? 430.8375 430.8375 430.8375 0.0000 0.0000 0.0000 429 PHE I CD1 
769  C CD2 . PHE A 97  ? 430.0746 430.0746 430.0746 0.0000 0.0000 0.0000 429 PHE I CD2 
770  C CE1 . PHE A 97  ? 431.4917 431.4917 431.4917 0.0000 0.0000 0.0000 429 PHE I CE1 
771  C CE2 . PHE A 97  ? 430.3172 430.3172 430.3172 0.0000 0.0000 0.0000 429 PHE I CE2 
772  C CZ  . PHE A 97  ? 431.2539 431.2539 431.2539 0.0000 0.0000 0.0000 429 PHE I CZ  
773  N N   . THR A 98  ? 431.4906 431.4906 431.4906 0.0000 0.0000 0.0000 430 THR I N   
774  C CA  . THR A 98  ? 431.0335 431.0335 431.0335 0.0000 0.0000 0.0000 430 THR I CA  
775  C C   . THR A 98  ? 429.8373 429.8373 429.8373 0.0000 0.0000 0.0000 430 THR I C   
776  O O   . THR A 98  ? 430.3898 430.3898 430.3898 0.0000 0.0000 0.0000 430 THR I O   
777  C CB  . THR A 98  ? 430.9357 430.9357 430.9357 0.0000 0.0000 0.0000 430 THR I CB  
778  O OG1 . THR A 98  ? 431.0080 431.0080 431.0080 0.0000 0.0000 0.0000 430 THR I OG1 
779  C CG2 . THR A 98  ? 431.3551 431.3551 431.3551 0.0000 0.0000 0.0000 430 THR I CG2 
780  N N   . GLY A 99  ? 429.6261 429.6261 429.6261 0.0000 0.0000 0.0000 431 GLY I N   
781  C CA  . GLY A 99  ? 429.1875 429.1875 429.1875 0.0000 0.0000 0.0000 431 GLY I CA  
782  C C   . GLY A 99  ? 430.1832 430.1832 430.1832 0.0000 0.0000 0.0000 431 GLY I C   
783  O O   . GLY A 99  ? 433.1066 433.1066 433.1066 0.0000 0.0000 0.0000 431 GLY I O   
784  N N   . CYS A 100 ? 428.9849 428.9849 428.9849 0.0000 0.0000 0.0000 432 CYS I N   
785  C CA  . CYS A 100 ? 429.7386 429.7386 429.7386 0.0000 0.0000 0.0000 432 CYS I CA  
786  C C   . CYS A 100 ? 430.1918 430.1918 430.1918 0.0000 0.0000 0.0000 432 CYS I C   
787  O O   . CYS A 100 ? 433.0291 433.0291 433.0291 0.0000 0.0000 0.0000 432 CYS I O   
788  C CB  . CYS A 100 ? 430.6840 430.6840 430.6840 0.0000 0.0000 0.0000 432 CYS I CB  
789  S SG  . CYS A 100 ? 433.0128 433.0128 433.0128 0.0000 0.0000 0.0000 432 CYS I SG  
790  N N   . VAL A 101 ? 429.5940 429.5940 429.5940 0.0000 0.0000 0.0000 433 VAL I N   
791  C CA  . VAL A 101 ? 429.5484 429.5484 429.5484 0.0000 0.0000 0.0000 433 VAL I CA  
792  C C   . VAL A 101 ? 429.9775 429.9775 429.9775 0.0000 0.0000 0.0000 433 VAL I C   
793  O O   . VAL A 101 ? 431.7096 431.7096 431.7096 0.0000 0.0000 0.0000 433 VAL I O   
794  C CB  . VAL A 101 ? 429.7452 429.7452 429.7452 0.0000 0.0000 0.0000 433 VAL I CB  
795  C CG1 . VAL A 101 ? 430.3259 430.3259 430.3259 0.0000 0.0000 0.0000 433 VAL I CG1 
796  C CG2 . VAL A 101 ? 430.5251 430.5251 430.5251 0.0000 0.0000 0.0000 433 VAL I CG2 
797  N N   . ILE A 102 ? 430.3425 430.3425 430.3425 0.0000 0.0000 0.0000 434 ILE I N   
798  C CA  . ILE A 102 ? 430.2468 430.2468 430.2468 0.0000 0.0000 0.0000 434 ILE I CA  
799  C C   . ILE A 102 ? 430.1267 430.1267 430.1267 0.0000 0.0000 0.0000 434 ILE I C   
800  O O   . ILE A 102 ? 432.3075 432.3075 432.3075 0.0000 0.0000 0.0000 434 ILE I O   
801  C CB  . ILE A 102 ? 429.9438 429.9438 429.9438 0.0000 0.0000 0.0000 434 ILE I CB  
802  C CG1 . ILE A 102 ? 429.7599 429.7599 429.7599 0.0000 0.0000 0.0000 434 ILE I CG1 
803  C CG2 . ILE A 102 ? 430.9355 430.9355 430.9355 0.0000 0.0000 0.0000 434 ILE I CG2 
804  C CD1 . ILE A 102 ? 430.4422 430.4422 430.4422 0.0000 0.0000 0.0000 434 ILE I CD1 
805  N N   . ALA A 103 ? 429.3743 429.3743 429.3743 0.0000 0.0000 0.0000 435 ALA I N   
806  C CA  . ALA A 103 ? 428.8608 428.8608 428.8608 0.0000 0.0000 0.0000 435 ALA I CA  
807  C C   . ALA A 103 ? 429.2234 429.2234 429.2234 0.0000 0.0000 0.0000 435 ALA I C   
808  O O   . ALA A 103 ? 432.2551 432.2551 432.2551 0.0000 0.0000 0.0000 435 ALA I O   
809  C CB  . ALA A 103 ? 430.2779 430.2779 430.2779 0.0000 0.0000 0.0000 435 ALA I CB  
810  N N   . TRP A 104 ? 429.9084 429.9084 429.9084 0.0000 0.0000 0.0000 436 TRP I N   
811  C CA  . TRP A 104 ? 430.0234 430.0234 430.0234 0.0000 0.0000 0.0000 436 TRP I CA  
812  C C   . TRP A 104 ? 430.3456 430.3456 430.3456 0.0000 0.0000 0.0000 436 TRP I C   
813  O O   . TRP A 104 ? 432.9262 432.9262 432.9262 0.0000 0.0000 0.0000 436 TRP I O   
814  C CB  . TRP A 104 ? 430.4863 430.4863 430.4863 0.0000 0.0000 0.0000 436 TRP I CB  
815  C CG  . TRP A 104 ? 430.4953 430.4953 430.4953 0.0000 0.0000 0.0000 436 TRP I CG  
816  C CD1 . TRP A 104 ? 430.3501 430.3501 430.3501 0.0000 0.0000 0.0000 436 TRP I CD1 
817  C CD2 . TRP A 104 ? 430.7657 430.7657 430.7657 0.0000 0.0000 0.0000 436 TRP I CD2 
818  N NE1 . TRP A 104 ? 429.7284 429.7284 429.7284 0.0000 0.0000 0.0000 436 TRP I NE1 
819  C CE2 . TRP A 104 ? 429.3254 429.3254 429.3254 0.0000 0.0000 0.0000 436 TRP I CE2 
820  C CE3 . TRP A 104 ? 431.6273 431.6273 431.6273 0.0000 0.0000 0.0000 436 TRP I CE3 
821  C CZ2 . TRP A 104 ? 429.2572 429.2572 429.2572 0.0000 0.0000 0.0000 436 TRP I CZ2 
822  C CZ3 . TRP A 104 ? 431.1393 431.1393 431.1393 0.0000 0.0000 0.0000 436 TRP I CZ3 
823  C CH2 . TRP A 104 ? 430.1994 430.1994 430.1994 0.0000 0.0000 0.0000 436 TRP I CH2 
824  N N   . ASN A 105 ? 429.8041 429.8041 429.8041 0.0000 0.0000 0.0000 437 ASN I N   
825  C CA  . ASN A 105 ? 430.6857 430.6857 430.6857 0.0000 0.0000 0.0000 437 ASN I CA  
826  C C   . ASN A 105 ? 431.4317 431.4317 431.4317 0.0000 0.0000 0.0000 437 ASN I C   
827  O O   . ASN A 105 ? 432.0418 432.0418 432.0418 0.0000 0.0000 0.0000 437 ASN I O   
828  C CB  . ASN A 105 ? 430.7868 430.7868 430.7868 0.0000 0.0000 0.0000 437 ASN I CB  
829  C CG  . ASN A 105 ? 429.8575 429.8575 429.8575 0.0000 0.0000 0.0000 437 ASN I CG  
830  O OD1 . ASN A 105 ? 429.5512 429.5512 429.5512 0.0000 0.0000 0.0000 437 ASN I OD1 
831  N ND2 . ASN A 105 ? 430.0633 430.0633 430.0633 0.0000 0.0000 0.0000 437 ASN I ND2 
832  N N   . SER A 106 ? 431.5090 431.5090 431.5090 0.0000 0.0000 0.0000 438 SER I N   
833  C CA  . SER A 106 ? 429.6413 429.6413 429.6413 0.0000 0.0000 0.0000 438 SER I CA  
834  C C   . SER A 106 ? 429.9230 429.9230 429.9230 0.0000 0.0000 0.0000 438 SER I C   
835  O O   . SER A 106 ? 430.8320 430.8320 430.8320 0.0000 0.0000 0.0000 438 SER I O   
836  C CB  . SER A 106 ? 429.7859 429.7859 429.7859 0.0000 0.0000 0.0000 438 SER I CB  
837  O OG  . SER A 106 ? 431.3682 431.3682 431.3682 0.0000 0.0000 0.0000 438 SER I OG  
838  N N   . ASN A 107 ? 430.6391 430.6391 430.6391 0.0000 0.0000 0.0000 439 ASN I N   
839  C CA  . ASN A 107 ? 429.2057 429.2057 429.2057 0.0000 0.0000 0.0000 439 ASN I CA  
840  C C   . ASN A 107 ? 427.3802 427.3802 427.3802 0.0000 0.0000 0.0000 439 ASN I C   
841  O O   . ASN A 107 ? 426.7739 426.7739 426.7739 0.0000 0.0000 0.0000 439 ASN I O   
842  C CB  . ASN A 107 ? 429.4140 429.4140 429.4140 0.0000 0.0000 0.0000 439 ASN I CB  
843  C CG  . ASN A 107 ? 427.5742 427.5742 427.5742 0.0000 0.0000 0.0000 439 ASN I CG  
844  O OD1 . ASN A 107 ? 427.1954 427.1954 427.1954 0.0000 0.0000 0.0000 439 ASN I OD1 
845  N ND2 . ASN A 107 ? 427.1274 427.1274 427.1274 0.0000 0.0000 0.0000 439 ASN I ND2 
846  N N   . ASN A 108 ? 428.1837 428.1837 428.1837 0.0000 0.0000 0.0000 440 ASN I N   
847  C CA  . ASN A 108 ? 423.6312 423.6312 423.6312 0.0000 0.0000 0.0000 440 ASN I CA  
848  C C   . ASN A 108 ? 426.1611 426.1611 426.1611 0.0000 0.0000 0.0000 440 ASN I C   
849  O O   . ASN A 108 ? 425.2003 425.2003 425.2003 0.0000 0.0000 0.0000 440 ASN I O   
850  C CB  . ASN A 108 ? 417.9723 417.9723 417.9723 0.0000 0.0000 0.0000 440 ASN I CB  
851  C CG  . ASN A 108 ? 426.1118 426.1118 426.1118 0.0000 0.0000 0.0000 440 ASN I CG  
852  O OD1 . ASN A 108 ? 431.1260 431.1260 431.1260 0.0000 0.0000 0.0000 440 ASN I OD1 
853  N ND2 . ASN A 108 ? 423.1920 423.1920 423.1920 0.0000 0.0000 0.0000 440 ASN I ND2 
854  N N   . LEU A 109 ? 429.6911 429.6911 429.6911 0.0000 0.0000 0.0000 441 LEU I N   
855  C CA  . LEU A 109 ? 428.6810 428.6810 428.6810 0.0000 0.0000 0.0000 441 LEU I CA  
856  C C   . LEU A 109 ? 426.7358 426.7358 426.7358 0.0000 0.0000 0.0000 441 LEU I C   
857  O O   . LEU A 109 ? 425.0828 425.0828 425.0828 0.0000 0.0000 0.0000 441 LEU I O   
858  C CB  . LEU A 109 ? 430.8430 430.8430 430.8430 0.0000 0.0000 0.0000 441 LEU I CB  
859  C CG  . LEU A 109 ? 423.5944 423.5944 423.5944 0.0000 0.0000 0.0000 441 LEU I CG  
860  C CD1 . LEU A 109 ? 424.8656 424.8656 424.8656 0.0000 0.0000 0.0000 441 LEU I CD1 
861  C CD2 . LEU A 109 ? 415.9168 415.9168 415.9168 0.0000 0.0000 0.0000 441 LEU I CD2 
862  N N   . ASP A 110 ? 428.9789 428.9789 428.9789 0.0000 0.0000 0.0000 442 ASP I N   
863  C CA  . ASP A 110 ? 426.4284 426.4284 426.4284 0.0000 0.0000 0.0000 442 ASP I CA  
864  C C   . ASP A 110 ? 428.8163 428.8163 428.8163 0.0000 0.0000 0.0000 442 ASP I C   
865  O O   . ASP A 110 ? 431.7152 431.7152 431.7152 0.0000 0.0000 0.0000 442 ASP I O   
866  C CB  . ASP A 110 ? 429.6578 429.6578 429.6578 0.0000 0.0000 0.0000 442 ASP I CB  
867  C CG  . ASP A 110 ? 428.0143 428.0143 428.0143 0.0000 0.0000 0.0000 442 ASP I CG  
868  O OD1 . ASP A 110 ? 426.7563 426.7563 426.7563 0.0000 0.0000 0.0000 442 ASP I OD1 
869  O OD2 . ASP A 110 ? 430.5150 430.5150 430.5150 0.0000 0.0000 0.0000 442 ASP I OD2 
870  N N   . SER A 111 ? 429.8317 429.8317 429.8317 0.0000 0.0000 0.0000 443 SER I N   
871  C CA  . SER A 111 ? 429.2474 429.2474 429.2474 0.0000 0.0000 0.0000 443 SER I CA  
872  C C   . SER A 111 ? 430.3074 430.3074 430.3074 0.0000 0.0000 0.0000 443 SER I C   
873  O O   . SER A 111 ? 428.5880 428.5880 428.5880 0.0000 0.0000 0.0000 443 SER I O   
874  C CB  . SER A 111 ? 428.3585 428.3585 428.3585 0.0000 0.0000 0.0000 443 SER I CB  
875  O OG  . SER A 111 ? 429.6552 429.6552 429.6552 0.0000 0.0000 0.0000 443 SER I OG  
876  N N   . LYS A 112 ? 430.7790 430.7790 430.7790 0.0000 0.0000 0.0000 444 LYS I N   
877  C CA  . LYS A 112 ? 431.0374 431.0374 431.0374 0.0000 0.0000 0.0000 444 LYS I CA  
878  C C   . LYS A 112 ? 431.7305 431.7305 431.7305 0.0000 0.0000 0.0000 444 LYS I C   
879  O O   . LYS A 112 ? 431.9048 431.9048 431.9048 0.0000 0.0000 0.0000 444 LYS I O   
880  C CB  . LYS A 112 ? 429.3583 429.3583 429.3583 0.0000 0.0000 0.0000 444 LYS I CB  
881  C CG  . LYS A 112 ? 424.8356 424.8356 424.8356 0.0000 0.0000 0.0000 444 LYS I CG  
882  C CD  . LYS A 112 ? 422.6936 422.6936 422.6936 0.0000 0.0000 0.0000 444 LYS I CD  
883  C CE  . LYS A 112 ? 416.0638 416.0638 416.0638 0.0000 0.0000 0.0000 444 LYS I CE  
884  N NZ  . LYS A 112 ? 415.4386 415.4386 415.4386 0.0000 0.0000 0.0000 444 LYS I NZ  
885  N N   . VAL A 113 ? 431.0962 431.0962 431.0962 0.0000 0.0000 0.0000 445 VAL I N   
886  C CA  . VAL A 113 ? 429.4401 429.4401 429.4401 0.0000 0.0000 0.0000 445 VAL I CA  
887  C C   . VAL A 113 ? 428.8743 428.8743 428.8743 0.0000 0.0000 0.0000 445 VAL I C   
888  O O   . VAL A 113 ? 426.6045 426.6045 426.6045 0.0000 0.0000 0.0000 445 VAL I O   
889  C CB  . VAL A 113 ? 425.1967 425.1967 425.1967 0.0000 0.0000 0.0000 445 VAL I CB  
890  C CG1 . VAL A 113 ? 421.6982 421.6982 421.6982 0.0000 0.0000 0.0000 445 VAL I CG1 
891  C CG2 . VAL A 113 ? 420.9203 420.9203 420.9203 0.0000 0.0000 0.0000 445 VAL I CG2 
892  N N   . GLY A 114 ? 430.1479 430.1479 430.1479 0.0000 0.0000 0.0000 446 GLY I N   
893  C CA  . GLY A 114 ? 427.9885 427.9885 427.9885 0.0000 0.0000 0.0000 446 GLY I CA  
894  C C   . GLY A 114 ? 428.2631 428.2631 428.2631 0.0000 0.0000 0.0000 446 GLY I C   
895  O O   . GLY A 114 ? 424.6379 424.6379 424.6379 0.0000 0.0000 0.0000 446 GLY I O   
896  N N   . GLY A 115 ? 429.8558 429.8558 429.8558 0.0000 0.0000 0.0000 447 GLY I N   
897  C CA  . GLY A 115 ? 429.4976 429.4976 429.4976 0.0000 0.0000 0.0000 447 GLY I CA  
898  C C   . GLY A 115 ? 429.1309 429.1309 429.1309 0.0000 0.0000 0.0000 447 GLY I C   
899  O O   . GLY A 115 ? 428.0364 428.0364 428.0364 0.0000 0.0000 0.0000 447 GLY I O   
900  N N   . ASN A 116 ? 429.5282 429.5282 429.5282 0.0000 0.0000 0.0000 448 ASN I N   
901  C CA  . ASN A 116 ? 429.5452 429.5452 429.5452 0.0000 0.0000 0.0000 448 ASN I CA  
902  C C   . ASN A 116 ? 428.2145 428.2145 428.2145 0.0000 0.0000 0.0000 448 ASN I C   
903  O O   . ASN A 116 ? 428.9598 428.9598 428.9598 0.0000 0.0000 0.0000 448 ASN I O   
904  C CB  . ASN A 116 ? 430.3070 430.3070 430.3070 0.0000 0.0000 0.0000 448 ASN I CB  
905  C CG  . ASN A 116 ? 429.9299 429.9299 429.9299 0.0000 0.0000 0.0000 448 ASN I CG  
906  O OD1 . ASN A 116 ? 431.1140 431.1140 431.1140 0.0000 0.0000 0.0000 448 ASN I OD1 
907  N ND2 . ASN A 116 ? 427.6002 427.6002 427.6002 0.0000 0.0000 0.0000 448 ASN I ND2 
908  N N   . TYR A 117 ? 425.7496 425.7496 425.7496 0.0000 0.0000 0.0000 449 TYR I N   
909  C CA  . TYR A 117 ? 423.6227 423.6227 423.6227 0.0000 0.0000 0.0000 449 TYR I CA  
910  C C   . TYR A 117 ? 430.5237 430.5237 430.5237 0.0000 0.0000 0.0000 449 TYR I C   
911  O O   . TYR A 117 ? 432.3638 432.3638 432.3638 0.0000 0.0000 0.0000 449 TYR I O   
912  C CB  . TYR A 117 ? 418.2981 418.2981 418.2981 0.0000 0.0000 0.0000 449 TYR I CB  
913  C CG  . TYR A 117 ? 420.9422 420.9422 420.9422 0.0000 0.0000 0.0000 449 TYR I CG  
914  C CD1 . TYR A 117 ? 425.3858 425.3858 425.3858 0.0000 0.0000 0.0000 449 TYR I CD1 
915  C CD2 . TYR A 117 ? 421.7456 421.7456 421.7456 0.0000 0.0000 0.0000 449 TYR I CD2 
916  C CE1 . TYR A 117 ? 428.8708 428.8708 428.8708 0.0000 0.0000 0.0000 449 TYR I CE1 
917  C CE2 . TYR A 117 ? 424.3201 424.3201 424.3201 0.0000 0.0000 0.0000 449 TYR I CE2 
918  C CZ  . TYR A 117 ? 428.5638 428.5638 428.5638 0.0000 0.0000 0.0000 449 TYR I CZ  
919  O OH  . TYR A 117 ? 431.0406 431.0406 431.0406 0.0000 0.0000 0.0000 449 TYR I OH  
920  N N   . ASN A 118 ? 430.1976 430.1976 430.1976 0.0000 0.0000 0.0000 450 ASN I N   
921  C CA  . ASN A 118 ? 429.9614 429.9614 429.9614 0.0000 0.0000 0.0000 450 ASN I CA  
922  C C   . ASN A 118 ? 430.3374 430.3374 430.3374 0.0000 0.0000 0.0000 450 ASN I C   
923  O O   . ASN A 118 ? 431.4576 431.4576 431.4576 0.0000 0.0000 0.0000 450 ASN I O   
924  C CB  . ASN A 118 ? 430.4174 430.4174 430.4174 0.0000 0.0000 0.0000 450 ASN I CB  
925  C CG  . ASN A 118 ? 426.8307 426.8307 426.8307 0.0000 0.0000 0.0000 450 ASN I CG  
926  O OD1 . ASN A 118 ? 423.0352 423.0352 423.0352 0.0000 0.0000 0.0000 450 ASN I OD1 
927  N ND2 . ASN A 118 ? 422.1315 422.1315 422.1315 0.0000 0.0000 0.0000 450 ASN I ND2 
928  N N   . TYR A 119 ? 429.8789 429.8789 429.8789 0.0000 0.0000 0.0000 451 TYR I N   
929  C CA  . TYR A 119 ? 431.2022 431.2022 431.2022 0.0000 0.0000 0.0000 451 TYR I CA  
930  C C   . TYR A 119 ? 432.3195 432.3195 432.3195 0.0000 0.0000 0.0000 451 TYR I C   
931  O O   . TYR A 119 ? 432.9088 432.9088 432.9088 0.0000 0.0000 0.0000 451 TYR I O   
932  C CB  . TYR A 119 ? 430.4853 430.4853 430.4853 0.0000 0.0000 0.0000 451 TYR I CB  
933  C CG  . TYR A 119 ? 429.4877 429.4877 429.4877 0.0000 0.0000 0.0000 451 TYR I CG  
934  C CD1 . TYR A 119 ? 430.6815 430.6815 430.6815 0.0000 0.0000 0.0000 451 TYR I CD1 
935  C CD2 . TYR A 119 ? 429.9992 429.9992 429.9992 0.0000 0.0000 0.0000 451 TYR I CD2 
936  C CE1 . TYR A 119 ? 430.5734 430.5734 430.5734 0.0000 0.0000 0.0000 451 TYR I CE1 
937  C CE2 . TYR A 119 ? 429.5617 429.5617 429.5617 0.0000 0.0000 0.0000 451 TYR I CE2 
938  C CZ  . TYR A 119 ? 428.6582 428.6582 428.6582 0.0000 0.0000 0.0000 451 TYR I CZ  
939  O OH  . TYR A 119 ? 426.4244 426.4244 426.4244 0.0000 0.0000 0.0000 451 TYR I OH  
940  N N   . LEU A 120 ? 430.7179 430.7179 430.7179 0.0000 0.0000 0.0000 452 LEU I N   
941  C CA  . LEU A 120 ? 430.6890 430.6890 430.6890 0.0000 0.0000 0.0000 452 LEU I CA  
942  C C   . LEU A 120 ? 430.2284 430.2284 430.2284 0.0000 0.0000 0.0000 452 LEU I C   
943  O O   . LEU A 120 ? 431.8546 431.8546 431.8546 0.0000 0.0000 0.0000 452 LEU I O   
944  C CB  . LEU A 120 ? 430.7910 430.7910 430.7910 0.0000 0.0000 0.0000 452 LEU I CB  
945  C CG  . LEU A 120 ? 430.1146 430.1146 430.1146 0.0000 0.0000 0.0000 452 LEU I CG  
946  C CD1 . LEU A 120 ? 430.6385 430.6385 430.6385 0.0000 0.0000 0.0000 452 LEU I CD1 
947  C CD2 . LEU A 120 ? 430.8711 430.8711 430.8711 0.0000 0.0000 0.0000 452 LEU I CD2 
948  N N   . TYR A 121 ? 429.2520 429.2520 429.2520 0.0000 0.0000 0.0000 453 TYR I N   
949  C CA  . TYR A 121 ? 429.5955 429.5955 429.5955 0.0000 0.0000 0.0000 453 TYR I CA  
950  C C   . TYR A 121 ? 430.0603 430.0603 430.0603 0.0000 0.0000 0.0000 453 TYR I C   
951  O O   . TYR A 121 ? 432.1260 432.1260 432.1260 0.0000 0.0000 0.0000 453 TYR I O   
952  C CB  . TYR A 121 ? 431.3097 431.3097 431.3097 0.0000 0.0000 0.0000 453 TYR I CB  
953  C CG  . TYR A 121 ? 430.5959 430.5959 430.5959 0.0000 0.0000 0.0000 453 TYR I CG  
954  C CD1 . TYR A 121 ? 431.2921 431.2921 431.2921 0.0000 0.0000 0.0000 453 TYR I CD1 
955  C CD2 . TYR A 121 ? 430.2427 430.2427 430.2427 0.0000 0.0000 0.0000 453 TYR I CD2 
956  C CE1 . TYR A 121 ? 430.6304 430.6304 430.6304 0.0000 0.0000 0.0000 453 TYR I CE1 
957  C CE2 . TYR A 121 ? 430.4758 430.4758 430.4758 0.0000 0.0000 0.0000 453 TYR I CE2 
958  C CZ  . TYR A 121 ? 431.0280 431.0280 431.0280 0.0000 0.0000 0.0000 453 TYR I CZ  
959  O OH  . TYR A 121 ? 432.1809 432.1809 432.1809 0.0000 0.0000 0.0000 453 TYR I OH  
960  N N   . ARG A 122 ? 430.4165 430.4165 430.4165 0.0000 0.0000 0.0000 454 ARG I N   
961  C CA  . ARG A 122 ? 430.3736 430.3736 430.3736 0.0000 0.0000 0.0000 454 ARG I CA  
962  C C   . ARG A 122 ? 430.9106 430.9106 430.9106 0.0000 0.0000 0.0000 454 ARG I C   
963  O O   . ARG A 122 ? 431.6868 431.6868 431.6868 0.0000 0.0000 0.0000 454 ARG I O   
964  C CB  . ARG A 122 ? 429.9255 429.9255 429.9255 0.0000 0.0000 0.0000 454 ARG I CB  
965  C CG  . ARG A 122 ? 429.6254 429.6254 429.6254 0.0000 0.0000 0.0000 454 ARG I CG  
966  C CD  . ARG A 122 ? 430.4792 430.4792 430.4792 0.0000 0.0000 0.0000 454 ARG I CD  
967  N NE  . ARG A 122 ? 430.2558 430.2558 430.2558 0.0000 0.0000 0.0000 454 ARG I NE  
968  C CZ  . ARG A 122 ? 431.6478 431.6478 431.6478 0.0000 0.0000 0.0000 454 ARG I CZ  
969  N NH1 . ARG A 122 ? 431.8756 431.8756 431.8756 0.0000 0.0000 0.0000 454 ARG I NH1 
970  N NH2 . ARG A 122 ? 433.1495 433.1495 433.1495 0.0000 0.0000 0.0000 454 ARG I NH2 
971  N N   . LEU A 123 ? 431.3065 431.3065 431.3065 0.0000 0.0000 0.0000 455 LEU I N   
972  C CA  . LEU A 123 ? 430.4793 430.4793 430.4793 0.0000 0.0000 0.0000 455 LEU I CA  
973  C C   . LEU A 123 ? 431.7990 431.7990 431.7990 0.0000 0.0000 0.0000 455 LEU I C   
974  O O   . LEU A 123 ? 432.3387 432.3387 432.3387 0.0000 0.0000 0.0000 455 LEU I O   
975  C CB  . LEU A 123 ? 430.6121 430.6121 430.6121 0.0000 0.0000 0.0000 455 LEU I CB  
976  C CG  . LEU A 123 ? 431.4483 431.4483 431.4483 0.0000 0.0000 0.0000 455 LEU I CG  
977  C CD1 . LEU A 123 ? 431.9140 431.9140 431.9140 0.0000 0.0000 0.0000 455 LEU I CD1 
978  C CD2 . LEU A 123 ? 430.9393 430.9393 430.9393 0.0000 0.0000 0.0000 455 LEU I CD2 
979  N N   . PHE A 124 ? 439.6634 439.6634 439.6634 0.0000 0.0000 0.0000 456 PHE I N   
980  C CA  . PHE A 124 ? 440.0036 440.0036 440.0036 0.0000 0.0000 0.0000 456 PHE I CA  
981  C C   . PHE A 124 ? 440.9111 440.9111 440.9111 0.0000 0.0000 0.0000 456 PHE I C   
982  O O   . PHE A 124 ? 442.2976 442.2976 442.2976 0.0000 0.0000 0.0000 456 PHE I O   
983  C CB  . PHE A 124 ? 442.4095 442.4095 442.4095 0.0000 0.0000 0.0000 456 PHE I CB  
984  C CG  . PHE A 124 ? 441.8310 441.8310 441.8310 0.0000 0.0000 0.0000 456 PHE I CG  
985  C CD1 . PHE A 124 ? 441.2920 441.2920 441.2920 0.0000 0.0000 0.0000 456 PHE I CD1 
986  C CD2 . PHE A 124 ? 442.5762 442.5762 442.5762 0.0000 0.0000 0.0000 456 PHE I CD2 
987  C CE1 . PHE A 124 ? 440.6790 440.6790 440.6790 0.0000 0.0000 0.0000 456 PHE I CE1 
988  C CE2 . PHE A 124 ? 442.2226 442.2226 442.2226 0.0000 0.0000 0.0000 456 PHE I CE2 
989  C CZ  . PHE A 124 ? 441.0981 441.0981 441.0981 0.0000 0.0000 0.0000 456 PHE I CZ  
990  N N   . ARG A 125 ? 447.8574 447.8574 447.8574 0.0000 0.0000 0.0000 457 ARG I N   
991  C CA  . ARG A 125 ? 449.5430 449.5430 449.5430 0.0000 0.0000 0.0000 457 ARG I CA  
992  C C   . ARG A 125 ? 452.0060 452.0060 452.0060 0.0000 0.0000 0.0000 457 ARG I C   
993  O O   . ARG A 125 ? 450.9238 450.9238 450.9238 0.0000 0.0000 0.0000 457 ARG I O   
994  C CB  . ARG A 125 ? 448.4691 448.4691 448.4691 0.0000 0.0000 0.0000 457 ARG I CB  
995  C CG  . ARG A 125 ? 447.8898 447.8898 447.8898 0.0000 0.0000 0.0000 457 ARG I CG  
996  C CD  . ARG A 125 ? 447.3684 447.3684 447.3684 0.0000 0.0000 0.0000 457 ARG I CD  
997  N NE  . ARG A 125 ? 447.5298 447.5298 447.5298 0.0000 0.0000 0.0000 457 ARG I NE  
998  C CZ  . ARG A 125 ? 447.7947 447.7947 447.7947 0.0000 0.0000 0.0000 457 ARG I CZ  
999  N NH1 . ARG A 125 ? 448.1045 448.1045 448.1045 0.0000 0.0000 0.0000 457 ARG I NH1 
1000 N NH2 . ARG A 125 ? 448.0049 448.0049 448.0049 0.0000 0.0000 0.0000 457 ARG I NH2 
1001 N N   . LYS A 126 ? 497.8485 497.8485 497.8485 0.0000 0.0000 0.0000 458 LYS I N   
1002 C CA  . LYS A 126 ? 499.1345 499.1345 499.1345 0.0000 0.0000 0.0000 458 LYS I CA  
1003 C C   . LYS A 126 ? 497.7762 497.7762 497.7762 0.0000 0.0000 0.0000 458 LYS I C   
1004 O O   . LYS A 126 ? 498.4187 498.4187 498.4187 0.0000 0.0000 0.0000 458 LYS I O   
1005 C CB  . LYS A 126 ? 499.7041 499.7041 499.7041 0.0000 0.0000 0.0000 458 LYS I CB  
1006 C CG  . LYS A 126 ? 501.0756 501.0756 501.0756 0.0000 0.0000 0.0000 458 LYS I CG  
1007 C CD  . LYS A 126 ? 501.4476 501.4476 501.4476 0.0000 0.0000 0.0000 458 LYS I CD  
1008 C CE  . LYS A 126 ? 501.4807 501.4807 501.4807 0.0000 0.0000 0.0000 458 LYS I CE  
1009 N NZ  . LYS A 126 ? 501.1736 501.1736 501.1736 0.0000 0.0000 0.0000 458 LYS I NZ  
1010 N N   . SER A 127 ? 463.0619 463.0619 463.0619 0.0000 0.0000 0.0000 459 SER I N   
1011 C CA  . SER A 127 ? 461.2704 461.2704 461.2704 0.0000 0.0000 0.0000 459 SER I CA  
1012 C C   . SER A 127 ? 459.3396 459.3396 459.3396 0.0000 0.0000 0.0000 459 SER I C   
1013 O O   . SER A 127 ? 459.5893 459.5893 459.5893 0.0000 0.0000 0.0000 459 SER I O   
1014 C CB  . SER A 127 ? 461.2035 461.2035 461.2035 0.0000 0.0000 0.0000 459 SER I CB  
1015 O OG  . SER A 127 ? 461.2253 461.2253 461.2253 0.0000 0.0000 0.0000 459 SER I OG  
1016 N N   . ASN A 128 ? 433.0347 433.0347 433.0347 0.0000 0.0000 0.0000 460 ASN I N   
1017 C CA  . ASN A 128 ? 432.1819 432.1819 432.1819 0.0000 0.0000 0.0000 460 ASN I CA  
1018 C C   . ASN A 128 ? 432.1476 432.1476 432.1476 0.0000 0.0000 0.0000 460 ASN I C   
1019 O O   . ASN A 128 ? 431.8493 431.8493 431.8493 0.0000 0.0000 0.0000 460 ASN I O   
1020 C CB  . ASN A 128 ? 431.1925 431.1925 431.1925 0.0000 0.0000 0.0000 460 ASN I CB  
1021 C CG  . ASN A 128 ? 430.9509 430.9509 430.9509 0.0000 0.0000 0.0000 460 ASN I CG  
1022 O OD1 . ASN A 128 ? 431.6675 431.6675 431.6675 0.0000 0.0000 0.0000 460 ASN I OD1 
1023 N ND2 . ASN A 128 ? 430.4635 430.4635 430.4635 0.0000 0.0000 0.0000 460 ASN I ND2 
1024 N N   . LEU A 129 ? 432.3587 432.3587 432.3587 0.0000 0.0000 0.0000 461 LEU I N   
1025 C CA  . LEU A 129 ? 431.5929 431.5929 431.5929 0.0000 0.0000 0.0000 461 LEU I CA  
1026 C C   . LEU A 129 ? 432.1192 432.1192 432.1192 0.0000 0.0000 0.0000 461 LEU I C   
1027 O O   . LEU A 129 ? 432.4729 432.4729 432.4729 0.0000 0.0000 0.0000 461 LEU I O   
1028 C CB  . LEU A 129 ? 430.5751 430.5751 430.5751 0.0000 0.0000 0.0000 461 LEU I CB  
1029 C CG  . LEU A 129 ? 430.8126 430.8126 430.8126 0.0000 0.0000 0.0000 461 LEU I CG  
1030 C CD1 . LEU A 129 ? 430.8682 430.8682 430.8682 0.0000 0.0000 0.0000 461 LEU I CD1 
1031 C CD2 . LEU A 129 ? 432.6972 432.6972 432.6972 0.0000 0.0000 0.0000 461 LEU I CD2 
1032 N N   . LYS A 130 ? 444.8218 444.8218 444.8218 0.0000 0.0000 0.0000 462 LYS I N   
1033 C CA  . LYS A 130 ? 445.1356 445.1356 445.1356 0.0000 0.0000 0.0000 462 LYS I CA  
1034 C C   . LYS A 130 ? 446.3669 446.3669 446.3669 0.0000 0.0000 0.0000 462 LYS I C   
1035 O O   . LYS A 130 ? 447.1605 447.1605 447.1605 0.0000 0.0000 0.0000 462 LYS I O   
1036 C CB  . LYS A 130 ? 445.4562 445.4562 445.4562 0.0000 0.0000 0.0000 462 LYS I CB  
1037 C CG  . LYS A 130 ? 446.6240 446.6240 446.6240 0.0000 0.0000 0.0000 462 LYS I CG  
1038 C CD  . LYS A 130 ? 446.5796 446.5796 446.5796 0.0000 0.0000 0.0000 462 LYS I CD  
1039 C CE  . LYS A 130 ? 447.2823 447.2823 447.2823 0.0000 0.0000 0.0000 462 LYS I CE  
1040 N NZ  . LYS A 130 ? 447.5537 447.5537 447.5537 0.0000 0.0000 0.0000 462 LYS I NZ  
1041 N N   . PRO A 131 ? 432.1419 432.1419 432.1419 0.0000 0.0000 0.0000 463 PRO I N   
1042 C CA  . PRO A 131 ? 431.2654 431.2654 431.2654 0.0000 0.0000 0.0000 463 PRO I CA  
1043 C C   . PRO A 131 ? 431.5603 431.5603 431.5603 0.0000 0.0000 0.0000 463 PRO I C   
1044 O O   . PRO A 131 ? 432.3689 432.3689 432.3689 0.0000 0.0000 0.0000 463 PRO I O   
1045 C CB  . PRO A 131 ? 430.5605 430.5605 430.5605 0.0000 0.0000 0.0000 463 PRO I CB  
1046 C CG  . PRO A 131 ? 430.7427 430.7427 430.7427 0.0000 0.0000 0.0000 463 PRO I CG  
1047 C CD  . PRO A 131 ? 431.2136 431.2136 431.2136 0.0000 0.0000 0.0000 463 PRO I CD  
1048 N N   . PHE A 132 ? 430.8982 430.8982 430.8982 0.0000 0.0000 0.0000 464 PHE I N   
1049 C CA  . PHE A 132 ? 430.6128 430.6128 430.6128 0.0000 0.0000 0.0000 464 PHE I CA  
1050 C C   . PHE A 132 ? 432.2946 432.2946 432.2946 0.0000 0.0000 0.0000 464 PHE I C   
1051 O O   . PHE A 132 ? 432.7881 432.7881 432.7881 0.0000 0.0000 0.0000 464 PHE I O   
1052 C CB  . PHE A 132 ? 431.0327 431.0327 431.0327 0.0000 0.0000 0.0000 464 PHE I CB  
1053 C CG  . PHE A 132 ? 430.6381 430.6381 430.6381 0.0000 0.0000 0.0000 464 PHE I CG  
1054 C CD1 . PHE A 132 ? 430.4216 430.4216 430.4216 0.0000 0.0000 0.0000 464 PHE I CD1 
1055 C CD2 . PHE A 132 ? 431.1626 431.1626 431.1626 0.0000 0.0000 0.0000 464 PHE I CD2 
1056 C CE1 . PHE A 132 ? 430.6585 430.6585 430.6585 0.0000 0.0000 0.0000 464 PHE I CE1 
1057 C CE2 . PHE A 132 ? 430.8169 430.8169 430.8169 0.0000 0.0000 0.0000 464 PHE I CE2 
1058 C CZ  . PHE A 132 ? 430.4167 430.4167 430.4167 0.0000 0.0000 0.0000 464 PHE I CZ  
1059 N N   . GLU A 133 ? 443.4528 443.4528 443.4528 0.0000 0.0000 0.0000 465 GLU I N   
1060 C CA  . GLU A 133 ? 443.7601 443.7601 443.7601 0.0000 0.0000 0.0000 465 GLU I CA  
1061 C C   . GLU A 133 ? 443.9066 443.9066 443.9066 0.0000 0.0000 0.0000 465 GLU I C   
1062 O O   . GLU A 133 ? 444.8903 444.8903 444.8903 0.0000 0.0000 0.0000 465 GLU I O   
1063 C CB  . GLU A 133 ? 444.5575 444.5575 444.5575 0.0000 0.0000 0.0000 465 GLU I CB  
1064 C CG  . GLU A 133 ? 445.4161 445.4161 445.4161 0.0000 0.0000 0.0000 465 GLU I CG  
1065 C CD  . GLU A 133 ? 445.3712 445.3712 445.3712 0.0000 0.0000 0.0000 465 GLU I CD  
1066 O OE1 . GLU A 133 ? 445.8732 445.8732 445.8732 0.0000 0.0000 0.0000 465 GLU I OE1 
1067 O OE2 . GLU A 133 ? 444.3917 444.3917 444.3917 0.0000 0.0000 0.0000 465 GLU I OE2 
1068 N N   . ARG A 134 ? 431.8866 431.8866 431.8866 0.0000 0.0000 0.0000 466 ARG I N   
1069 C CA  . ARG A 134 ? 431.1755 431.1755 431.1755 0.0000 0.0000 0.0000 466 ARG I CA  
1070 C C   . ARG A 134 ? 431.7743 431.7743 431.7743 0.0000 0.0000 0.0000 466 ARG I C   
1071 O O   . ARG A 134 ? 432.1808 432.1808 432.1808 0.0000 0.0000 0.0000 466 ARG I O   
1072 C CB  . ARG A 134 ? 430.5312 430.5312 430.5312 0.0000 0.0000 0.0000 466 ARG I CB  
1073 C CG  . ARG A 134 ? 431.0761 431.0761 431.0761 0.0000 0.0000 0.0000 466 ARG I CG  
1074 C CD  . ARG A 134 ? 430.7031 430.7031 430.7031 0.0000 0.0000 0.0000 466 ARG I CD  
1075 N NE  . ARG A 134 ? 431.0446 431.0446 431.0446 0.0000 0.0000 0.0000 466 ARG I NE  
1076 C CZ  . ARG A 134 ? 430.9217 430.9217 430.9217 0.0000 0.0000 0.0000 466 ARG I CZ  
1077 N NH1 . ARG A 134 ? 430.4294 430.4294 430.4294 0.0000 0.0000 0.0000 466 ARG I NH1 
1078 N NH2 . ARG A 134 ? 431.7224 431.7224 431.7224 0.0000 0.0000 0.0000 466 ARG I NH2 
1079 N N   . ASP A 135 ? 438.2640 438.2640 438.2640 0.0000 0.0000 0.0000 467 ASP I N   
1080 C CA  . ASP A 135 ? 438.8082 438.8082 438.8082 0.0000 0.0000 0.0000 467 ASP I CA  
1081 C C   . ASP A 135 ? 439.9319 439.9319 439.9319 0.0000 0.0000 0.0000 467 ASP I C   
1082 O O   . ASP A 135 ? 440.3479 440.3479 440.3479 0.0000 0.0000 0.0000 467 ASP I O   
1083 C CB  . ASP A 135 ? 439.0605 439.0605 439.0605 0.0000 0.0000 0.0000 467 ASP I CB  
1084 C CG  . ASP A 135 ? 440.2129 440.2129 440.2129 0.0000 0.0000 0.0000 467 ASP I CG  
1085 O OD1 . ASP A 135 ? 440.1328 440.1328 440.1328 0.0000 0.0000 0.0000 467 ASP I OD1 
1086 O OD2 . ASP A 135 ? 440.7880 440.7880 440.7880 0.0000 0.0000 0.0000 467 ASP I OD2 
1087 N N   . ILE A 136 ? 453.6057 453.6057 453.6057 0.0000 0.0000 0.0000 468 ILE I N   
1088 C CA  . ILE A 136 ? 454.2089 454.2089 454.2089 0.0000 0.0000 0.0000 468 ILE I CA  
1089 C C   . ILE A 136 ? 456.0990 456.0990 456.0990 0.0000 0.0000 0.0000 468 ILE I C   
1090 O O   . ILE A 136 ? 456.6444 456.6444 456.6444 0.0000 0.0000 0.0000 468 ILE I O   
1091 C CB  . ILE A 136 ? 453.9321 453.9321 453.9321 0.0000 0.0000 0.0000 468 ILE I CB  
1092 C CG1 . ILE A 136 ? 454.3992 454.3992 454.3992 0.0000 0.0000 0.0000 468 ILE I CG1 
1093 C CG2 . ILE A 136 ? 453.8280 453.8280 453.8280 0.0000 0.0000 0.0000 468 ILE I CG2 
1094 C CD1 . ILE A 136 ? 454.6386 454.6386 454.6386 0.0000 0.0000 0.0000 468 ILE I CD1 
1095 N N   . SER A 137 ? 471.7820 471.7820 471.7820 0.0000 0.0000 0.0000 469 SER I N   
1096 C CA  . SER A 137 ? 472.9293 472.9293 472.9293 0.0000 0.0000 0.0000 469 SER I CA  
1097 C C   . SER A 137 ? 475.7315 475.7315 475.7315 0.0000 0.0000 0.0000 469 SER I C   
1098 O O   . SER A 137 ? 473.6647 473.6647 473.6647 0.0000 0.0000 0.0000 469 SER I O   
1099 C CB  . SER A 137 ? 473.6662 473.6662 473.6662 0.0000 0.0000 0.0000 469 SER I CB  
1100 O OG  . SER A 137 ? 473.4691 473.4691 473.4691 0.0000 0.0000 0.0000 469 SER I OG  
1101 N N   . THR A 138 ? 532.0197 532.0197 532.0197 0.0000 0.0000 0.0000 470 THR I N   
1102 C CA  . THR A 138 ? 533.1817 533.1817 533.1817 0.0000 0.0000 0.0000 470 THR I CA  
1103 C C   . THR A 138 ? 535.3680 535.3680 535.3680 0.0000 0.0000 0.0000 470 THR I C   
1104 O O   . THR A 138 ? 535.6425 535.6425 535.6425 0.0000 0.0000 0.0000 470 THR I O   
1105 C CB  . THR A 138 ? 534.1717 534.1717 534.1717 0.0000 0.0000 0.0000 470 THR I CB  
1106 O OG1 . THR A 138 ? 535.0189 535.0189 535.0189 0.0000 0.0000 0.0000 470 THR I OG1 
1107 C CG2 . THR A 138 ? 533.0231 533.0231 533.0231 0.0000 0.0000 0.0000 470 THR I CG2 
1108 N N   . GLU A 139 ? 576.3598 576.3598 576.3598 0.0000 0.0000 0.0000 471 GLU I N   
1109 C CA  . GLU A 139 ? 579.1458 579.1458 579.1458 0.0000 0.0000 0.0000 471 GLU I CA  
1110 C C   . GLU A 139 ? 579.9064 579.9064 579.9064 0.0000 0.0000 0.0000 471 GLU I C   
1111 O O   . GLU A 139 ? 578.7524 578.7524 578.7524 0.0000 0.0000 0.0000 471 GLU I O   
1112 C CB  . GLU A 139 ? 579.9154 579.9154 579.9154 0.0000 0.0000 0.0000 471 GLU I CB  
1113 C CG  . GLU A 139 ? 580.4841 580.4841 580.4841 0.0000 0.0000 0.0000 471 GLU I CG  
1114 C CD  . GLU A 139 ? 580.9453 580.9453 580.9453 0.0000 0.0000 0.0000 471 GLU I CD  
1115 O OE1 . GLU A 139 ? 581.1986 581.1986 581.1986 0.0000 0.0000 0.0000 471 GLU I OE1 
1116 O OE2 . GLU A 139 ? 580.8263 580.8263 580.8263 0.0000 0.0000 0.0000 471 GLU I OE2 
1117 N N   . ILE A 140 ? 602.5395 602.5395 602.5395 0.0000 0.0000 0.0000 472 ILE I N   
1118 C CA  . ILE A 140 ? 602.7795 602.7795 602.7795 0.0000 0.0000 0.0000 472 ILE I CA  
1119 C C   . ILE A 140 ? 602.9159 602.9159 602.9159 0.0000 0.0000 0.0000 472 ILE I C   
1120 O O   . ILE A 140 ? 604.5198 604.5198 604.5198 0.0000 0.0000 0.0000 472 ILE I O   
1121 C CB  . ILE A 140 ? 605.6406 605.6406 605.6406 0.0000 0.0000 0.0000 472 ILE I CB  
1122 C CG1 . ILE A 140 ? 606.8720 606.8720 606.8720 0.0000 0.0000 0.0000 472 ILE I CG1 
1123 C CG2 . ILE A 140 ? 606.2149 606.2149 606.2149 0.0000 0.0000 0.0000 472 ILE I CG2 
1124 C CD1 . ILE A 140 ? 606.7258 606.7258 606.7258 0.0000 0.0000 0.0000 472 ILE I CD1 
1125 N N   . TYR A 141 ? 561.0365 561.0365 561.0365 0.0000 0.0000 0.0000 473 TYR I N   
1126 C CA  . TYR A 141 ? 560.9833 560.9833 560.9833 0.0000 0.0000 0.0000 473 TYR I CA  
1127 C C   . TYR A 141 ? 564.5515 564.5515 564.5515 0.0000 0.0000 0.0000 473 TYR I C   
1128 O O   . TYR A 141 ? 564.2161 564.2161 564.2161 0.0000 0.0000 0.0000 473 TYR I O   
1129 C CB  . TYR A 141 ? 558.4693 558.4693 558.4693 0.0000 0.0000 0.0000 473 TYR I CB  
1130 C CG  . TYR A 141 ? 557.4972 557.4972 557.4972 0.0000 0.0000 0.0000 473 TYR I CG  
1131 C CD1 . TYR A 141 ? 555.9451 555.9451 555.9451 0.0000 0.0000 0.0000 473 TYR I CD1 
1132 C CD2 . TYR A 141 ? 558.6349 558.6349 558.6349 0.0000 0.0000 0.0000 473 TYR I CD2 
1133 C CE1 . TYR A 141 ? 555.7299 555.7299 555.7299 0.0000 0.0000 0.0000 473 TYR I CE1 
1134 C CE2 . TYR A 141 ? 558.9541 558.9541 558.9541 0.0000 0.0000 0.0000 473 TYR I CE2 
1135 C CZ  . TYR A 141 ? 557.3196 557.3196 557.3196 0.0000 0.0000 0.0000 473 TYR I CZ  
1136 O OH  . TYR A 141 ? 556.8879 556.8879 556.8879 0.0000 0.0000 0.0000 473 TYR I OH  
1137 N N   . GLN A 142 ? 649.3564 649.3564 649.3564 0.0000 0.0000 0.0000 474 GLN I N   
1138 C CA  . GLN A 142 ? 651.7466 651.7466 651.7466 0.0000 0.0000 0.0000 474 GLN I CA  
1139 C C   . GLN A 142 ? 652.1416 652.1416 652.1416 0.0000 0.0000 0.0000 474 GLN I C   
1140 O O   . GLN A 142 ? 652.2430 652.2430 652.2430 0.0000 0.0000 0.0000 474 GLN I O   
1141 C CB  . GLN A 142 ? 653.4001 653.4001 653.4001 0.0000 0.0000 0.0000 474 GLN I CB  
1142 C CG  . GLN A 142 ? 655.6117 655.6117 655.6117 0.0000 0.0000 0.0000 474 GLN I CG  
1143 C CD  . GLN A 142 ? 655.8758 655.8758 655.8758 0.0000 0.0000 0.0000 474 GLN I CD  
1144 O OE1 . GLN A 142 ? 654.3704 654.3704 654.3704 0.0000 0.0000 0.0000 474 GLN I OE1 
1145 N NE2 . GLN A 142 ? 657.9139 657.9139 657.9139 0.0000 0.0000 0.0000 474 GLN I NE2 
1146 N N   . ALA A 143 ? 640.0185 640.0185 640.0185 0.0000 0.0000 0.0000 475 ALA I N   
1147 C CA  . ALA A 143 ? 640.6407 640.6407 640.6407 0.0000 0.0000 0.0000 475 ALA I CA  
1148 C C   . ALA A 143 ? 642.9847 642.9847 642.9847 0.0000 0.0000 0.0000 475 ALA I C   
1149 O O   . ALA A 143 ? 642.2228 642.2228 642.2228 0.0000 0.0000 0.0000 475 ALA I O   
1150 C CB  . ALA A 143 ? 640.1545 640.1545 640.1545 0.0000 0.0000 0.0000 475 ALA I CB  
1151 N N   . GLY A 144 ? 697.4247 697.4247 697.4247 0.0000 0.0000 0.0000 476 GLY I N   
1152 C CA  . GLY A 144 ? 699.2674 699.2674 699.2674 0.0000 0.0000 0.0000 476 GLY I CA  
1153 C C   . GLY A 144 ? 701.3911 701.3911 701.3911 0.0000 0.0000 0.0000 476 GLY I C   
1154 O O   . GLY A 144 ? 700.3654 700.3654 700.3654 0.0000 0.0000 0.0000 476 GLY I O   
1155 N N   . SER A 145 ? 757.3779 757.3779 757.3779 0.0000 0.0000 0.0000 477 SER I N   
1156 C CA  . SER A 145 ? 758.6968 758.6968 758.6968 0.0000 0.0000 0.0000 477 SER I CA  
1157 C C   . SER A 145 ? 758.7592 758.7592 758.7592 0.0000 0.0000 0.0000 477 SER I C   
1158 O O   . SER A 145 ? 758.6098 758.6098 758.6098 0.0000 0.0000 0.0000 477 SER I O   
1159 C CB  . SER A 145 ? 759.2763 759.2763 759.2763 0.0000 0.0000 0.0000 477 SER I CB  
1160 O OG  . SER A 145 ? 759.2741 759.2741 759.2741 0.0000 0.0000 0.0000 477 SER I OG  
1161 N N   . THR A 146 ? 757.1948 757.1948 757.1948 0.0000 0.0000 0.0000 478 THR I N   
1162 C CA  . THR A 146 ? 757.2763 757.2763 757.2763 0.0000 0.0000 0.0000 478 THR I CA  
1163 C C   . THR A 146 ? 756.7651 756.7651 756.7651 0.0000 0.0000 0.0000 478 THR I C   
1164 O O   . THR A 146 ? 755.7955 755.7955 755.7955 0.0000 0.0000 0.0000 478 THR I O   
1165 C CB  . THR A 146 ? 757.6888 757.6888 757.6888 0.0000 0.0000 0.0000 478 THR I CB  
1166 O OG1 . THR A 146 ? 757.6535 757.6535 757.6535 0.0000 0.0000 0.0000 478 THR I OG1 
1167 C CG2 . THR A 146 ? 757.2902 757.2902 757.2902 0.0000 0.0000 0.0000 478 THR I CG2 
1168 N N   . PRO A 147 ? 757.4743 757.4743 757.4743 0.0000 0.0000 0.0000 479 PRO I N   
1169 C CA  . PRO A 147 ? 757.2251 757.2251 757.2251 0.0000 0.0000 0.0000 479 PRO I CA  
1170 C C   . PRO A 147 ? 757.1828 757.1828 757.1828 0.0000 0.0000 0.0000 479 PRO I C   
1171 O O   . PRO A 147 ? 757.8257 757.8257 757.8257 0.0000 0.0000 0.0000 479 PRO I O   
1172 C CB  . PRO A 147 ? 757.4607 757.4607 757.4607 0.0000 0.0000 0.0000 479 PRO I CB  
1173 C CG  . PRO A 147 ? 757.8134 757.8134 757.8134 0.0000 0.0000 0.0000 479 PRO I CG  
1174 C CD  . PRO A 147 ? 757.8294 757.8294 757.8294 0.0000 0.0000 0.0000 479 PRO I CD  
1175 N N   . CYS A 148 ? 747.5936 747.5936 747.5936 0.0000 0.0000 0.0000 480 CYS I N   
1176 C CA  . CYS A 148 ? 747.3694 747.3694 747.3694 0.0000 0.0000 0.0000 480 CYS I CA  
1177 C C   . CYS A 148 ? 747.2424 747.2424 747.2424 0.0000 0.0000 0.0000 480 CYS I C   
1178 O O   . CYS A 148 ? 747.0647 747.0647 747.0647 0.0000 0.0000 0.0000 480 CYS I O   
1179 C CB  . CYS A 148 ? 746.0286 746.0286 746.0286 0.0000 0.0000 0.0000 480 CYS I CB  
1180 S SG  . CYS A 148 ? 742.8290 742.8290 742.8290 0.0000 0.0000 0.0000 480 CYS I SG  
1181 N N   . ASN A 149 ? 745.1299 745.1299 745.1299 0.0000 0.0000 0.0000 481 ASN I N   
1182 C CA  . ASN A 149 ? 744.8850 744.8850 744.8850 0.0000 0.0000 0.0000 481 ASN I CA  
1183 C C   . ASN A 149 ? 743.9096 743.9096 743.9096 0.0000 0.0000 0.0000 481 ASN I C   
1184 O O   . ASN A 149 ? 744.1611 744.1611 744.1611 0.0000 0.0000 0.0000 481 ASN I O   
1185 C CB  . ASN A 149 ? 745.1581 745.1581 745.1581 0.0000 0.0000 0.0000 481 ASN I CB  
1186 C CG  . ASN A 149 ? 745.4656 745.4656 745.4656 0.0000 0.0000 0.0000 481 ASN I CG  
1187 O OD1 . ASN A 149 ? 745.5139 745.5139 745.5139 0.0000 0.0000 0.0000 481 ASN I OD1 
1188 N ND2 . ASN A 149 ? 745.5074 745.5074 745.5074 0.0000 0.0000 0.0000 481 ASN I ND2 
1189 N N   . GLY A 150 ? 706.5881 706.5881 706.5881 0.0000 0.0000 0.0000 482 GLY I N   
1190 C CA  . GLY A 150 ? 705.1718 705.1718 705.1718 0.0000 0.0000 0.0000 482 GLY I CA  
1191 C C   . GLY A 150 ? 704.7220 704.7220 704.7220 0.0000 0.0000 0.0000 482 GLY I C   
1192 O O   . GLY A 150 ? 704.5874 704.5874 704.5874 0.0000 0.0000 0.0000 482 GLY I O   
1193 N N   . VAL A 151 ? 698.2416 698.2416 698.2416 0.0000 0.0000 0.0000 483 VAL I N   
1194 C CA  . VAL A 151 ? 697.6843 697.6843 697.6843 0.0000 0.0000 0.0000 483 VAL I CA  
1195 C C   . VAL A 151 ? 697.1247 697.1247 697.1247 0.0000 0.0000 0.0000 483 VAL I C   
1196 O O   . VAL A 151 ? 697.3686 697.3686 697.3686 0.0000 0.0000 0.0000 483 VAL I O   
1197 C CB  . VAL A 151 ? 697.5248 697.5248 697.5248 0.0000 0.0000 0.0000 483 VAL I CB  
1198 C CG1 . VAL A 151 ? 697.9303 697.9303 697.9303 0.0000 0.0000 0.0000 483 VAL I CG1 
1199 C CG2 . VAL A 151 ? 697.2779 697.2779 697.2779 0.0000 0.0000 0.0000 483 VAL I CG2 
1200 N N   . GLU A 152 ? 684.9651 684.9651 684.9651 0.0000 0.0000 0.0000 484 GLU I N   
1201 C CA  . GLU A 152 ? 684.6298 684.6298 684.6298 0.0000 0.0000 0.0000 484 GLU I CA  
1202 C C   . GLU A 152 ? 684.7594 684.7594 684.7594 0.0000 0.0000 0.0000 484 GLU I C   
1203 O O   . GLU A 152 ? 685.1464 685.1464 685.1464 0.0000 0.0000 0.0000 484 GLU I O   
1204 C CB  . GLU A 152 ? 684.9090 684.9090 684.9090 0.0000 0.0000 0.0000 484 GLU I CB  
1205 C CG  . GLU A 152 ? 684.7009 684.7009 684.7009 0.0000 0.0000 0.0000 484 GLU I CG  
1206 C CD  . GLU A 152 ? 681.9448 681.9448 681.9448 0.0000 0.0000 0.0000 484 GLU I CD  
1207 O OE1 . GLU A 152 ? 681.0209 681.0209 681.0209 0.0000 0.0000 0.0000 484 GLU I OE1 
1208 O OE2 . GLU A 152 ? 680.6361 680.6361 680.6361 0.0000 0.0000 0.0000 484 GLU I OE2 
1209 N N   . GLY A 153 ? 676.5281 676.5281 676.5281 0.0000 0.0000 0.0000 485 GLY I N   
1210 C CA  . GLY A 153 ? 676.8876 676.8876 676.8876 0.0000 0.0000 0.0000 485 GLY I CA  
1211 C C   . GLY A 153 ? 676.8713 676.8713 676.8713 0.0000 0.0000 0.0000 485 GLY I C   
1212 O O   . GLY A 153 ? 676.0456 676.0456 676.0456 0.0000 0.0000 0.0000 485 GLY I O   
1213 N N   . PHE A 154 ? 708.2846 708.2846 708.2846 0.0000 0.0000 0.0000 486 PHE I N   
1214 C CA  . PHE A 154 ? 708.5536 708.5536 708.5536 0.0000 0.0000 0.0000 486 PHE I CA  
1215 C C   . PHE A 154 ? 707.0574 707.0574 707.0574 0.0000 0.0000 0.0000 486 PHE I C   
1216 O O   . PHE A 154 ? 707.7967 707.7967 707.7967 0.0000 0.0000 0.0000 486 PHE I O   
1217 C CB  . PHE A 154 ? 709.4842 709.4842 709.4842 0.0000 0.0000 0.0000 486 PHE I CB  
1218 C CG  . PHE A 154 ? 709.4732 709.4732 709.4732 0.0000 0.0000 0.0000 486 PHE I CG  
1219 C CD1 . PHE A 154 ? 709.4670 709.4670 709.4670 0.0000 0.0000 0.0000 486 PHE I CD1 
1220 C CD2 . PHE A 154 ? 709.2572 709.2572 709.2572 0.0000 0.0000 0.0000 486 PHE I CD2 
1221 C CE1 . PHE A 154 ? 709.3008 709.3008 709.3008 0.0000 0.0000 0.0000 486 PHE I CE1 
1222 C CE2 . PHE A 154 ? 709.1066 709.1066 709.1066 0.0000 0.0000 0.0000 486 PHE I CE2 
1223 C CZ  . PHE A 154 ? 709.1853 709.1853 709.1853 0.0000 0.0000 0.0000 486 PHE I CZ  
1224 N N   . ASN A 155 ? 654.0751 654.0751 654.0751 0.0000 0.0000 0.0000 487 ASN I N   
1225 C CA  . ASN A 155 ? 652.2205 652.2205 652.2205 0.0000 0.0000 0.0000 487 ASN I CA  
1226 C C   . ASN A 155 ? 650.5777 650.5777 650.5777 0.0000 0.0000 0.0000 487 ASN I C   
1227 O O   . ASN A 155 ? 650.9293 650.9293 650.9293 0.0000 0.0000 0.0000 487 ASN I O   
1228 C CB  . ASN A 155 ? 653.1761 653.1761 653.1761 0.0000 0.0000 0.0000 487 ASN I CB  
1229 C CG  . ASN A 155 ? 653.3405 653.3405 653.3405 0.0000 0.0000 0.0000 487 ASN I CG  
1230 O OD1 . ASN A 155 ? 653.9150 653.9150 653.9150 0.0000 0.0000 0.0000 487 ASN I OD1 
1231 N ND2 . ASN A 155 ? 652.1846 652.1846 652.1846 0.0000 0.0000 0.0000 487 ASN I ND2 
1232 N N   . CYS A 156 ? 631.7309 631.7309 631.7309 0.0000 0.0000 0.0000 488 CYS I N   
1233 C CA  . CYS A 156 ? 629.8645 629.8645 629.8645 0.0000 0.0000 0.0000 488 CYS I CA  
1234 C C   . CYS A 156 ? 627.2963 627.2963 627.2963 0.0000 0.0000 0.0000 488 CYS I C   
1235 O O   . CYS A 156 ? 629.5365 629.5365 629.5365 0.0000 0.0000 0.0000 488 CYS I O   
1236 C CB  . CYS A 156 ? 632.2639 632.2639 632.2639 0.0000 0.0000 0.0000 488 CYS I CB  
1237 S SG  . CYS A 156 ? 634.2022 634.2022 634.2022 0.0000 0.0000 0.0000 488 CYS I SG  
1238 N N   . TYR A 157 ? 549.4259 549.4259 549.4259 0.0000 0.0000 0.0000 489 TYR I N   
1239 C CA  . TYR A 157 ? 545.7208 545.7208 545.7208 0.0000 0.0000 0.0000 489 TYR I CA  
1240 C C   . TYR A 157 ? 543.1288 543.1288 543.1288 0.0000 0.0000 0.0000 489 TYR I C   
1241 O O   . TYR A 157 ? 544.1599 544.1599 544.1599 0.0000 0.0000 0.0000 489 TYR I O   
1242 C CB  . TYR A 157 ? 543.7218 543.7218 543.7218 0.0000 0.0000 0.0000 489 TYR I CB  
1243 C CG  . TYR A 157 ? 544.6863 544.6863 544.6863 0.0000 0.0000 0.0000 489 TYR I CG  
1244 C CD1 . TYR A 157 ? 544.7831 544.7831 544.7831 0.0000 0.0000 0.0000 489 TYR I CD1 
1245 C CD2 . TYR A 157 ? 545.5659 545.5659 545.5659 0.0000 0.0000 0.0000 489 TYR I CD2 
1246 C CE1 . TYR A 157 ? 545.2976 545.2976 545.2976 0.0000 0.0000 0.0000 489 TYR I CE1 
1247 C CE2 . TYR A 157 ? 547.1474 547.1474 547.1474 0.0000 0.0000 0.0000 489 TYR I CE2 
1248 C CZ  . TYR A 157 ? 546.2591 546.2591 546.2591 0.0000 0.0000 0.0000 489 TYR I CZ  
1249 O OH  . TYR A 157 ? 546.0487 546.0487 546.0487 0.0000 0.0000 0.0000 489 TYR I OH  
1250 N N   . PHE A 158 ? 495.7158 495.7158 495.7158 0.0000 0.0000 0.0000 490 PHE I N   
1251 C CA  . PHE A 158 ? 492.5652 492.5652 492.5652 0.0000 0.0000 0.0000 490 PHE I CA  
1252 C C   . PHE A 158 ? 487.8920 487.8920 487.8920 0.0000 0.0000 0.0000 490 PHE I C   
1253 O O   . PHE A 158 ? 488.7106 488.7106 488.7106 0.0000 0.0000 0.0000 490 PHE I O   
1254 C CB  . PHE A 158 ? 492.5015 492.5015 492.5015 0.0000 0.0000 0.0000 490 PHE I CB  
1255 C CG  . PHE A 158 ? 491.4516 491.4516 491.4516 0.0000 0.0000 0.0000 490 PHE I CG  
1256 C CD1 . PHE A 158 ? 492.3888 492.3888 492.3888 0.0000 0.0000 0.0000 490 PHE I CD1 
1257 C CD2 . PHE A 158 ? 489.3386 489.3386 489.3386 0.0000 0.0000 0.0000 490 PHE I CD2 
1258 C CE1 . PHE A 158 ? 491.6282 491.6282 491.6282 0.0000 0.0000 0.0000 490 PHE I CE1 
1259 C CE2 . PHE A 158 ? 489.0358 489.0358 489.0358 0.0000 0.0000 0.0000 490 PHE I CE2 
1260 C CZ  . PHE A 158 ? 490.3569 490.3569 490.3569 0.0000 0.0000 0.0000 490 PHE I CZ  
1261 N N   . PRO A 159 ? 435.3698 435.3698 435.3698 0.0000 0.0000 0.0000 491 PRO I N   
1262 C CA  . PRO A 159 ? 432.3389 432.3389 432.3389 0.0000 0.0000 0.0000 491 PRO I CA  
1263 C C   . PRO A 159 ? 431.6930 431.6930 431.6930 0.0000 0.0000 0.0000 491 PRO I C   
1264 O O   . PRO A 159 ? 432.6609 432.6609 432.6609 0.0000 0.0000 0.0000 491 PRO I O   
1265 C CB  . PRO A 159 ? 431.4746 431.4746 431.4746 0.0000 0.0000 0.0000 491 PRO I CB  
1266 C CG  . PRO A 159 ? 435.8392 435.8392 435.8392 0.0000 0.0000 0.0000 491 PRO I CG  
1267 C CD  . PRO A 159 ? 438.5895 438.5895 438.5895 0.0000 0.0000 0.0000 491 PRO I CD  
1268 N N   . LEU A 160 ? 432.1785 432.1785 432.1785 0.0000 0.0000 0.0000 492 LEU I N   
1269 C CA  . LEU A 160 ? 430.4942 430.4942 430.4942 0.0000 0.0000 0.0000 492 LEU I CA  
1270 C C   . LEU A 160 ? 429.9616 429.9616 429.9616 0.0000 0.0000 0.0000 492 LEU I C   
1271 O O   . LEU A 160 ? 432.7610 432.7610 432.7610 0.0000 0.0000 0.0000 492 LEU I O   
1272 C CB  . LEU A 160 ? 430.9933 430.9933 430.9933 0.0000 0.0000 0.0000 492 LEU I CB  
1273 C CG  . LEU A 160 ? 431.3885 431.3885 431.3885 0.0000 0.0000 0.0000 492 LEU I CG  
1274 C CD1 . LEU A 160 ? 432.0668 432.0668 432.0668 0.0000 0.0000 0.0000 492 LEU I CD1 
1275 C CD2 . LEU A 160 ? 431.2128 431.2128 431.2128 0.0000 0.0000 0.0000 492 LEU I CD2 
1276 N N   . GLN A 161 ? 428.6164 428.6164 428.6164 0.0000 0.0000 0.0000 493 GLN I N   
1277 C CA  . GLN A 161 ? 429.8173 429.8173 429.8173 0.0000 0.0000 0.0000 493 GLN I CA  
1278 C C   . GLN A 161 ? 431.1430 431.1430 431.1430 0.0000 0.0000 0.0000 493 GLN I C   
1279 O O   . GLN A 161 ? 432.7392 432.7392 432.7392 0.0000 0.0000 0.0000 493 GLN I O   
1280 C CB  . GLN A 161 ? 430.6118 430.6118 430.6118 0.0000 0.0000 0.0000 493 GLN I CB  
1281 C CG  . GLN A 161 ? 431.3625 431.3625 431.3625 0.0000 0.0000 0.0000 493 GLN I CG  
1282 C CD  . GLN A 161 ? 431.3918 431.3918 431.3918 0.0000 0.0000 0.0000 493 GLN I CD  
1283 O OE1 . GLN A 161 ? 430.4375 430.4375 430.4375 0.0000 0.0000 0.0000 493 GLN I OE1 
1284 N NE2 . GLN A 161 ? 431.4258 431.4258 431.4258 0.0000 0.0000 0.0000 493 GLN I NE2 
1285 N N   . SER A 162 ? 430.6264 430.6264 430.6264 0.0000 0.0000 0.0000 494 SER I N   
1286 C CA  . SER A 162 ? 429.9996 429.9996 429.9996 0.0000 0.0000 0.0000 494 SER I CA  
1287 C C   . SER A 162 ? 431.0602 431.0602 431.0602 0.0000 0.0000 0.0000 494 SER I C   
1288 O O   . SER A 162 ? 431.7402 431.7402 431.7402 0.0000 0.0000 0.0000 494 SER I O   
1289 C CB  . SER A 162 ? 428.5571 428.5571 428.5571 0.0000 0.0000 0.0000 494 SER I CB  
1290 O OG  . SER A 162 ? 428.0778 428.0778 428.0778 0.0000 0.0000 0.0000 494 SER I OG  
1291 N N   . TYR A 163 ? 430.9060 430.9060 430.9060 0.0000 0.0000 0.0000 495 TYR I N   
1292 C CA  . TYR A 163 ? 430.4925 430.4925 430.4925 0.0000 0.0000 0.0000 495 TYR I CA  
1293 C C   . TYR A 163 ? 430.7542 430.7542 430.7542 0.0000 0.0000 0.0000 495 TYR I C   
1294 O O   . TYR A 163 ? 429.7927 429.7927 429.7927 0.0000 0.0000 0.0000 495 TYR I O   
1295 C CB  . TYR A 163 ? 430.8511 430.8511 430.8511 0.0000 0.0000 0.0000 495 TYR I CB  
1296 C CG  . TYR A 163 ? 430.5461 430.5461 430.5461 0.0000 0.0000 0.0000 495 TYR I CG  
1297 C CD1 . TYR A 163 ? 431.8902 431.8902 431.8902 0.0000 0.0000 0.0000 495 TYR I CD1 
1298 C CD2 . TYR A 163 ? 429.8492 429.8492 429.8492 0.0000 0.0000 0.0000 495 TYR I CD2 
1299 C CE1 . TYR A 163 ? 431.9085 431.9085 431.9085 0.0000 0.0000 0.0000 495 TYR I CE1 
1300 C CE2 . TYR A 163 ? 429.7721 429.7721 429.7721 0.0000 0.0000 0.0000 495 TYR I CE2 
1301 C CZ  . TYR A 163 ? 430.0056 430.0056 430.0056 0.0000 0.0000 0.0000 495 TYR I CZ  
1302 O OH  . TYR A 163 ? 429.9410 429.9410 429.9410 0.0000 0.0000 0.0000 495 TYR I OH  
1303 N N   . GLY A 164 ? 433.5974 433.5974 433.5974 0.0000 0.0000 0.0000 496 GLY I N   
1304 C CA  . GLY A 164 ? 432.0917 432.0917 432.0917 0.0000 0.0000 0.0000 496 GLY I CA  
1305 C C   . GLY A 164 ? 433.5668 433.5668 433.5668 0.0000 0.0000 0.0000 496 GLY I C   
1306 O O   . GLY A 164 ? 434.3996 434.3996 434.3996 0.0000 0.0000 0.0000 496 GLY I O   
1307 N N   . PHE A 165 ? 431.5028 431.5028 431.5028 0.0000 0.0000 0.0000 497 PHE I N   
1308 C CA  . PHE A 165 ? 430.7657 430.7657 430.7657 0.0000 0.0000 0.0000 497 PHE I CA  
1309 C C   . PHE A 165 ? 431.4850 431.4850 431.4850 0.0000 0.0000 0.0000 497 PHE I C   
1310 O O   . PHE A 165 ? 432.3489 432.3489 432.3489 0.0000 0.0000 0.0000 497 PHE I O   
1311 C CB  . PHE A 165 ? 430.4602 430.4602 430.4602 0.0000 0.0000 0.0000 497 PHE I CB  
1312 C CG  . PHE A 165 ? 429.4133 429.4133 429.4133 0.0000 0.0000 0.0000 497 PHE I CG  
1313 C CD1 . PHE A 165 ? 430.4396 430.4396 430.4396 0.0000 0.0000 0.0000 497 PHE I CD1 
1314 C CD2 . PHE A 165 ? 430.0922 430.0922 430.0922 0.0000 0.0000 0.0000 497 PHE I CD2 
1315 C CE1 . PHE A 165 ? 430.3559 430.3559 430.3559 0.0000 0.0000 0.0000 497 PHE I CE1 
1316 C CE2 . PHE A 165 ? 430.1257 430.1257 430.1257 0.0000 0.0000 0.0000 497 PHE I CE2 
1317 C CZ  . PHE A 165 ? 429.7754 429.7754 429.7754 0.0000 0.0000 0.0000 497 PHE I CZ  
1318 N N   . GLN A 166 ? 431.1895 431.1895 431.1895 0.0000 0.0000 0.0000 498 GLN I N   
1319 C CA  . GLN A 166 ? 430.8420 430.8420 430.8420 0.0000 0.0000 0.0000 498 GLN I CA  
1320 C C   . GLN A 166 ? 431.9077 431.9077 431.9077 0.0000 0.0000 0.0000 498 GLN I C   
1321 O O   . GLN A 166 ? 432.1735 432.1735 432.1735 0.0000 0.0000 0.0000 498 GLN I O   
1322 C CB  . GLN A 166 ? 431.6774 431.6774 431.6774 0.0000 0.0000 0.0000 498 GLN I CB  
1323 C CG  . GLN A 166 ? 430.5259 430.5259 430.5259 0.0000 0.0000 0.0000 498 GLN I CG  
1324 C CD  . GLN A 166 ? 430.9564 430.9564 430.9564 0.0000 0.0000 0.0000 498 GLN I CD  
1325 O OE1 . GLN A 166 ? 432.3951 432.3951 432.3951 0.0000 0.0000 0.0000 498 GLN I OE1 
1326 N NE2 . GLN A 166 ? 430.5890 430.5890 430.5890 0.0000 0.0000 0.0000 498 GLN I NE2 
1327 N N   . PRO A 167 ? 430.5705 430.5705 430.5705 0.0000 0.0000 0.0000 499 PRO I N   
1328 C CA  . PRO A 167 ? 425.5097 425.5097 425.5097 0.0000 0.0000 0.0000 499 PRO I CA  
1329 C C   . PRO A 167 ? 428.9138 428.9138 428.9138 0.0000 0.0000 0.0000 499 PRO I C   
1330 O O   . PRO A 167 ? 427.8381 427.8381 427.8381 0.0000 0.0000 0.0000 499 PRO I O   
1331 C CB  . PRO A 167 ? 417.0275 417.0275 417.0275 0.0000 0.0000 0.0000 499 PRO I CB  
1332 C CG  . PRO A 167 ? 419.2644 419.2644 419.2644 0.0000 0.0000 0.0000 499 PRO I CG  
1333 C CD  . PRO A 167 ? 428.1173 428.1173 428.1173 0.0000 0.0000 0.0000 499 PRO I CD  
1334 N N   . THR A 168 ? 445.1263 445.1263 445.1263 0.0000 0.0000 0.0000 500 THR I N   
1335 C CA  . THR A 168 ? 445.6619 445.6619 445.6619 0.0000 0.0000 0.0000 500 THR I CA  
1336 C C   . THR A 168 ? 447.5192 447.5192 447.5192 0.0000 0.0000 0.0000 500 THR I C   
1337 O O   . THR A 168 ? 448.9340 448.9340 448.9340 0.0000 0.0000 0.0000 500 THR I O   
1338 C CB  . THR A 168 ? 448.7929 448.7929 448.7929 0.0000 0.0000 0.0000 500 THR I CB  
1339 O OG1 . THR A 168 ? 448.9152 448.9152 448.9152 0.0000 0.0000 0.0000 500 THR I OG1 
1340 C CG2 . THR A 168 ? 444.6718 444.6718 444.6718 0.0000 0.0000 0.0000 500 THR I CG2 
1341 N N   . ASN A 169 ? 432.6432 432.6432 432.6432 0.0000 0.0000 0.0000 501 ASN I N   
1342 C CA  . ASN A 169 ? 432.8499 432.8499 432.8499 0.0000 0.0000 0.0000 501 ASN I CA  
1343 C C   . ASN A 169 ? 433.5306 433.5306 433.5306 0.0000 0.0000 0.0000 501 ASN I C   
1344 O O   . ASN A 169 ? 433.4876 433.4876 433.4876 0.0000 0.0000 0.0000 501 ASN I O   
1345 C CB  . ASN A 169 ? 432.3449 432.3449 432.3449 0.0000 0.0000 0.0000 501 ASN I CB  
1346 C CG  . ASN A 169 ? 432.8836 432.8836 432.8836 0.0000 0.0000 0.0000 501 ASN I CG  
1347 O OD1 . ASN A 169 ? 434.0859 434.0859 434.0859 0.0000 0.0000 0.0000 501 ASN I OD1 
1348 N ND2 . ASN A 169 ? 432.5415 432.5415 432.5415 0.0000 0.0000 0.0000 501 ASN I ND2 
1349 N N   . GLY A 170 ? 438.7298 438.7298 438.7298 0.0000 0.0000 0.0000 502 GLY I N   
1350 C CA  . GLY A 170 ? 438.8573 438.8573 438.8573 0.0000 0.0000 0.0000 502 GLY I CA  
1351 C C   . GLY A 170 ? 439.2687 439.2687 439.2687 0.0000 0.0000 0.0000 502 GLY I C   
1352 O O   . GLY A 170 ? 440.7146 440.7146 440.7146 0.0000 0.0000 0.0000 502 GLY I O   
1353 N N   . VAL A 171 ? 431.2824 431.2824 431.2824 0.0000 0.0000 0.0000 503 VAL I N   
1354 C CA  . VAL A 171 ? 431.3660 431.3660 431.3660 0.0000 0.0000 0.0000 503 VAL I CA  
1355 C C   . VAL A 171 ? 431.4817 431.4817 431.4817 0.0000 0.0000 0.0000 503 VAL I C   
1356 O O   . VAL A 171 ? 431.9797 431.9797 431.9797 0.0000 0.0000 0.0000 503 VAL I O   
1357 C CB  . VAL A 171 ? 431.1831 431.1831 431.1831 0.0000 0.0000 0.0000 503 VAL I CB  
1358 C CG1 . VAL A 171 ? 431.3879 431.3879 431.3879 0.0000 0.0000 0.0000 503 VAL I CG1 
1359 C CG2 . VAL A 171 ? 430.8598 430.8598 430.8598 0.0000 0.0000 0.0000 503 VAL I CG2 
1360 N N   . GLY A 172 ? 431.0229 431.0229 431.0229 0.0000 0.0000 0.0000 504 GLY I N   
1361 C CA  . GLY A 172 ? 431.4508 431.4508 431.4508 0.0000 0.0000 0.0000 504 GLY I CA  
1362 C C   . GLY A 172 ? 431.5622 431.5622 431.5622 0.0000 0.0000 0.0000 504 GLY I C   
1363 O O   . GLY A 172 ? 433.2397 433.2397 433.2397 0.0000 0.0000 0.0000 504 GLY I O   
1364 N N   . TYR A 173 ? 430.5735 430.5735 430.5735 0.0000 0.0000 0.0000 505 TYR I N   
1365 C CA  . TYR A 173 ? 430.9903 430.9903 430.9903 0.0000 0.0000 0.0000 505 TYR I CA  
1366 C C   . TYR A 173 ? 430.9824 430.9824 430.9824 0.0000 0.0000 0.0000 505 TYR I C   
1367 O O   . TYR A 173 ? 431.5774 431.5774 431.5774 0.0000 0.0000 0.0000 505 TYR I O   
1368 C CB  . TYR A 173 ? 431.4671 431.4671 431.4671 0.0000 0.0000 0.0000 505 TYR I CB  
1369 C CG  . TYR A 173 ? 431.1515 431.1515 431.1515 0.0000 0.0000 0.0000 505 TYR I CG  
1370 C CD1 . TYR A 173 ? 430.9739 430.9739 430.9739 0.0000 0.0000 0.0000 505 TYR I CD1 
1371 C CD2 . TYR A 173 ? 430.8218 430.8218 430.8218 0.0000 0.0000 0.0000 505 TYR I CD2 
1372 C CE1 . TYR A 173 ? 431.5754 431.5754 431.5754 0.0000 0.0000 0.0000 505 TYR I CE1 
1373 C CE2 . TYR A 173 ? 430.7909 430.7909 430.7909 0.0000 0.0000 0.0000 505 TYR I CE2 
1374 C CZ  . TYR A 173 ? 431.8675 431.8675 431.8675 0.0000 0.0000 0.0000 505 TYR I CZ  
1375 O OH  . TYR A 173 ? 432.1541 432.1541 432.1541 0.0000 0.0000 0.0000 505 TYR I OH  
1376 N N   . GLN A 174 ? 430.5803 430.5803 430.5803 0.0000 0.0000 0.0000 506 GLN I N   
1377 C CA  . GLN A 174 ? 429.7936 429.7936 429.7936 0.0000 0.0000 0.0000 506 GLN I CA  
1378 C C   . GLN A 174 ? 430.1704 430.1704 430.1704 0.0000 0.0000 0.0000 506 GLN I C   
1379 O O   . GLN A 174 ? 430.7760 430.7760 430.7760 0.0000 0.0000 0.0000 506 GLN I O   
1380 C CB  . GLN A 174 ? 430.3902 430.3902 430.3902 0.0000 0.0000 0.0000 506 GLN I CB  
1381 C CG  . GLN A 174 ? 431.1065 431.1065 431.1065 0.0000 0.0000 0.0000 506 GLN I CG  
1382 C CD  . GLN A 174 ? 431.1523 431.1523 431.1523 0.0000 0.0000 0.0000 506 GLN I CD  
1383 O OE1 . GLN A 174 ? 431.8243 431.8243 431.8243 0.0000 0.0000 0.0000 506 GLN I OE1 
1384 N NE2 . GLN A 174 ? 431.0313 431.0313 431.0313 0.0000 0.0000 0.0000 506 GLN I NE2 
1385 N N   . PRO A 175 ? 430.4778 430.4778 430.4778 0.0000 0.0000 0.0000 507 PRO I N   
1386 C CA  . PRO A 175 ? 429.9565 429.9565 429.9565 0.0000 0.0000 0.0000 507 PRO I CA  
1387 C C   . PRO A 175 ? 429.4535 429.4535 429.4535 0.0000 0.0000 0.0000 507 PRO I C   
1388 O O   . PRO A 175 ? 431.4632 431.4632 431.4632 0.0000 0.0000 0.0000 507 PRO I O   
1389 C CB  . PRO A 175 ? 429.9485 429.9485 429.9485 0.0000 0.0000 0.0000 507 PRO I CB  
1390 C CG  . PRO A 175 ? 430.6304 430.6304 430.6304 0.0000 0.0000 0.0000 507 PRO I CG  
1391 C CD  . PRO A 175 ? 431.2196 431.2196 431.2196 0.0000 0.0000 0.0000 507 PRO I CD  
1392 N N   . TYR A 176 ? 429.4646 429.4646 429.4646 0.0000 0.0000 0.0000 508 TYR I N   
1393 C CA  . TYR A 176 ? 429.5749 429.5749 429.5749 0.0000 0.0000 0.0000 508 TYR I CA  
1394 C C   . TYR A 176 ? 429.7608 429.7608 429.7608 0.0000 0.0000 0.0000 508 TYR I C   
1395 O O   . TYR A 176 ? 431.5408 431.5408 431.5408 0.0000 0.0000 0.0000 508 TYR I O   
1396 C CB  . TYR A 176 ? 430.0854 430.0854 430.0854 0.0000 0.0000 0.0000 508 TYR I CB  
1397 C CG  . TYR A 176 ? 430.0804 430.0804 430.0804 0.0000 0.0000 0.0000 508 TYR I CG  
1398 C CD1 . TYR A 176 ? 431.2276 431.2276 431.2276 0.0000 0.0000 0.0000 508 TYR I CD1 
1399 C CD2 . TYR A 176 ? 430.2621 430.2621 430.2621 0.0000 0.0000 0.0000 508 TYR I CD2 
1400 C CE1 . TYR A 176 ? 430.7629 430.7629 430.7629 0.0000 0.0000 0.0000 508 TYR I CE1 
1401 C CE2 . TYR A 176 ? 431.0571 431.0571 431.0571 0.0000 0.0000 0.0000 508 TYR I CE2 
1402 C CZ  . TYR A 176 ? 430.9713 430.9713 430.9713 0.0000 0.0000 0.0000 508 TYR I CZ  
1403 O OH  . TYR A 176 ? 431.5131 431.5131 431.5131 0.0000 0.0000 0.0000 508 TYR I OH  
1404 N N   . ARG A 177 ? 429.3986 429.3986 429.3986 0.0000 0.0000 0.0000 509 ARG I N   
1405 C CA  . ARG A 177 ? 428.6821 428.6821 428.6821 0.0000 0.0000 0.0000 509 ARG I CA  
1406 C C   . ARG A 177 ? 429.3010 429.3010 429.3010 0.0000 0.0000 0.0000 509 ARG I C   
1407 O O   . ARG A 177 ? 432.0349 432.0349 432.0349 0.0000 0.0000 0.0000 509 ARG I O   
1408 C CB  . ARG A 177 ? 430.4174 430.4174 430.4174 0.0000 0.0000 0.0000 509 ARG I CB  
1409 C CG  . ARG A 177 ? 430.4200 430.4200 430.4200 0.0000 0.0000 0.0000 509 ARG I CG  
1410 C CD  . ARG A 177 ? 430.6161 430.6161 430.6161 0.0000 0.0000 0.0000 509 ARG I CD  
1411 N NE  . ARG A 177 ? 429.1489 429.1489 429.1489 0.0000 0.0000 0.0000 509 ARG I NE  
1412 C CZ  . ARG A 177 ? 427.8064 427.8064 427.8064 0.0000 0.0000 0.0000 509 ARG I CZ  
1413 N NH1 . ARG A 177 ? 428.8501 428.8501 428.8501 0.0000 0.0000 0.0000 509 ARG I NH1 
1414 N NH2 . ARG A 177 ? 426.9782 426.9782 426.9782 0.0000 0.0000 0.0000 509 ARG I NH2 
1415 N N   . VAL A 178 ? 429.0393 429.0393 429.0393 0.0000 0.0000 0.0000 510 VAL I N   
1416 C CA  . VAL A 178 ? 429.3059 429.3059 429.3059 0.0000 0.0000 0.0000 510 VAL I CA  
1417 C C   . VAL A 178 ? 429.9067 429.9067 429.9067 0.0000 0.0000 0.0000 510 VAL I C   
1418 O O   . VAL A 178 ? 432.5123 432.5123 432.5123 0.0000 0.0000 0.0000 510 VAL I O   
1419 C CB  . VAL A 178 ? 428.9991 428.9991 428.9991 0.0000 0.0000 0.0000 510 VAL I CB  
1420 C CG1 . VAL A 178 ? 430.3378 430.3378 430.3378 0.0000 0.0000 0.0000 510 VAL I CG1 
1421 C CG2 . VAL A 178 ? 430.9735 430.9735 430.9735 0.0000 0.0000 0.0000 510 VAL I CG2 
1422 N N   . VAL A 179 ? 429.9793 429.9793 429.9793 0.0000 0.0000 0.0000 511 VAL I N   
1423 C CA  . VAL A 179 ? 429.4078 429.4078 429.4078 0.0000 0.0000 0.0000 511 VAL I CA  
1424 C C   . VAL A 179 ? 429.6486 429.6486 429.6486 0.0000 0.0000 0.0000 511 VAL I C   
1425 O O   . VAL A 179 ? 431.1573 431.1573 431.1573 0.0000 0.0000 0.0000 511 VAL I O   
1426 C CB  . VAL A 179 ? 429.6119 429.6119 429.6119 0.0000 0.0000 0.0000 511 VAL I CB  
1427 C CG1 . VAL A 179 ? 429.9416 429.9416 429.9416 0.0000 0.0000 0.0000 511 VAL I CG1 
1428 C CG2 . VAL A 179 ? 430.4423 430.4423 430.4423 0.0000 0.0000 0.0000 511 VAL I CG2 
1429 N N   . VAL A 180 ? 429.8628 429.8628 429.8628 0.0000 0.0000 0.0000 512 VAL I N   
1430 C CA  . VAL A 180 ? 429.0186 429.0186 429.0186 0.0000 0.0000 0.0000 512 VAL I CA  
1431 C C   . VAL A 180 ? 429.4896 429.4896 429.4896 0.0000 0.0000 0.0000 512 VAL I C   
1432 O O   . VAL A 180 ? 431.6314 431.6314 431.6314 0.0000 0.0000 0.0000 512 VAL I O   
1433 C CB  . VAL A 180 ? 429.2888 429.2888 429.2888 0.0000 0.0000 0.0000 512 VAL I CB  
1434 C CG1 . VAL A 180 ? 430.2353 430.2353 430.2353 0.0000 0.0000 0.0000 512 VAL I CG1 
1435 C CG2 . VAL A 180 ? 430.4549 430.4549 430.4549 0.0000 0.0000 0.0000 512 VAL I CG2 
1436 N N   . LEU A 181 ? 429.3454 429.3454 429.3454 0.0000 0.0000 0.0000 513 LEU I N   
1437 C CA  . LEU A 181 ? 429.2748 429.2748 429.2748 0.0000 0.0000 0.0000 513 LEU I CA  
1438 C C   . LEU A 181 ? 429.4506 429.4506 429.4506 0.0000 0.0000 0.0000 513 LEU I C   
1439 O O   . LEU A 181 ? 431.3717 431.3717 431.3717 0.0000 0.0000 0.0000 513 LEU I O   
1440 C CB  . LEU A 181 ? 430.6450 430.6450 430.6450 0.0000 0.0000 0.0000 513 LEU I CB  
1441 C CG  . LEU A 181 ? 430.3107 430.3107 430.3107 0.0000 0.0000 0.0000 513 LEU I CG  
1442 C CD1 . LEU A 181 ? 431.2796 431.2796 431.2796 0.0000 0.0000 0.0000 513 LEU I CD1 
1443 C CD2 . LEU A 181 ? 431.1830 431.1830 431.1830 0.0000 0.0000 0.0000 513 LEU I CD2 
1444 N N   . SER A 182 ? 429.3923 429.3923 429.3923 0.0000 0.0000 0.0000 514 SER I N   
1445 C CA  . SER A 182 ? 429.6504 429.6504 429.6504 0.0000 0.0000 0.0000 514 SER I CA  
1446 C C   . SER A 182 ? 430.8610 430.8610 430.8610 0.0000 0.0000 0.0000 514 SER I C   
1447 O O   . SER A 182 ? 433.4286 433.4286 433.4286 0.0000 0.0000 0.0000 514 SER I O   
1448 C CB  . SER A 182 ? 430.6211 430.6211 430.6211 0.0000 0.0000 0.0000 514 SER I CB  
1449 O OG  . SER A 182 ? 430.4394 430.4394 430.4394 0.0000 0.0000 0.0000 514 SER I OG  
1450 N N   . PHE A 183 ? 431.2095 431.2095 431.2095 0.0000 0.0000 0.0000 515 PHE I N   
1451 C CA  . PHE A 183 ? 434.2489 434.2489 434.2489 0.0000 0.0000 0.0000 515 PHE I CA  
1452 C C   . PHE A 183 ? 439.0665 439.0665 439.0665 0.0000 0.0000 0.0000 515 PHE I C   
1453 O O   . PHE A 183 ? 437.6875 437.6875 437.6875 0.0000 0.0000 0.0000 515 PHE I O   
1454 C CB  . PHE A 183 ? 436.1094 436.1094 436.1094 0.0000 0.0000 0.0000 515 PHE I CB  
1455 C CG  . PHE A 183 ? 433.6844 433.6844 433.6844 0.0000 0.0000 0.0000 515 PHE I CG  
1456 C CD1 . PHE A 183 ? 433.9133 433.9133 433.9133 0.0000 0.0000 0.0000 515 PHE I CD1 
1457 C CD2 . PHE A 183 ? 432.8012 432.8012 432.8012 0.0000 0.0000 0.0000 515 PHE I CD2 
1458 C CE1 . PHE A 183 ? 432.3183 432.3183 432.3183 0.0000 0.0000 0.0000 515 PHE I CE1 
1459 C CE2 . PHE A 183 ? 431.3510 431.3510 431.3510 0.0000 0.0000 0.0000 515 PHE I CE2 
1460 C CZ  . PHE A 183 ? 431.5819 431.5819 431.5819 0.0000 0.0000 0.0000 515 PHE I CZ  
1461 N N   . GLU A 184 ? 581.0015 581.0015 581.0015 0.0000 0.0000 0.0000 516 GLU I N   
1462 C CA  . GLU A 184 ? 586.5677 586.5677 586.5677 0.0000 0.0000 0.0000 516 GLU I CA  
1463 C C   . GLU A 184 ? 589.6036 589.6036 589.6036 0.0000 0.0000 0.0000 516 GLU I C   
1464 O O   . GLU A 184 ? 589.3634 589.3634 589.3634 0.0000 0.0000 0.0000 516 GLU I O   
1465 C CB  . GLU A 184 ? 588.0305 588.0305 588.0305 0.0000 0.0000 0.0000 516 GLU I CB  
1466 C CG  . GLU A 184 ? 590.2064 590.2064 590.2064 0.0000 0.0000 0.0000 516 GLU I CG  
1467 C CD  . GLU A 184 ? 590.3187 590.3187 590.3187 0.0000 0.0000 0.0000 516 GLU I CD  
1468 O OE1 . GLU A 184 ? 589.0352 589.0352 589.0352 0.0000 0.0000 0.0000 516 GLU I OE1 
1469 O OE2 . GLU A 184 ? 590.7274 590.7274 590.7274 0.0000 0.0000 0.0000 516 GLU I OE2 
1470 N N   . LEU A 185 ? 643.1149 643.1149 643.1149 0.0000 0.0000 0.0000 517 LEU I N   
1471 C CA  . LEU A 185 ? 646.1565 646.1565 646.1565 0.0000 0.0000 0.0000 517 LEU I CA  
1472 C C   . LEU A 185 ? 649.6466 649.6466 649.6466 0.0000 0.0000 0.0000 517 LEU I C   
1473 O O   . LEU A 185 ? 648.2749 648.2749 648.2749 0.0000 0.0000 0.0000 517 LEU I O   
1474 C CB  . LEU A 185 ? 645.9455 645.9455 645.9455 0.0000 0.0000 0.0000 517 LEU I CB  
1475 C CG  . LEU A 185 ? 645.0185 645.0185 645.0185 0.0000 0.0000 0.0000 517 LEU I CG  
1476 C CD1 . LEU A 185 ? 642.3553 642.3553 642.3553 0.0000 0.0000 0.0000 517 LEU I CD1 
1477 C CD2 . LEU A 185 ? 645.0884 645.0884 645.0884 0.0000 0.0000 0.0000 517 LEU I CD2 
1478 N N   . LEU A 186 ? 756.7763 756.7763 756.7763 0.0000 0.0000 0.0000 518 LEU I N   
1479 C CA  . LEU A 186 ? 760.7955 760.7955 760.7955 0.0000 0.0000 0.0000 518 LEU I CA  
1480 C C   . LEU A 186 ? 762.7712 762.7712 762.7712 0.0000 0.0000 0.0000 518 LEU I C   
1481 O O   . LEU A 186 ? 761.6507 761.6507 761.6507 0.0000 0.0000 0.0000 518 LEU I O   
1482 C CB  . LEU A 186 ? 760.4170 760.4170 760.4170 0.0000 0.0000 0.0000 518 LEU I CB  
1483 C CG  . LEU A 186 ? 761.6302 761.6302 761.6302 0.0000 0.0000 0.0000 518 LEU I CG  
1484 C CD1 . LEU A 186 ? 761.2915 761.2915 761.2915 0.0000 0.0000 0.0000 518 LEU I CD1 
1485 C CD2 . LEU A 186 ? 761.2593 761.2593 761.2593 0.0000 0.0000 0.0000 518 LEU I CD2 
1486 N N   . HIS A 187 ? 831.6498 831.6498 831.6498 0.0000 0.0000 0.0000 519 HIS I N   
1487 C CA  . HIS A 187 ? 832.9225 832.9225 832.9225 0.0000 0.0000 0.0000 519 HIS I CA  
1488 C C   . HIS A 187 ? 832.2289 832.2289 832.2289 0.0000 0.0000 0.0000 519 HIS I C   
1489 O O   . HIS A 187 ? 833.1489 833.1489 833.1489 0.0000 0.0000 0.0000 519 HIS I O   
1490 C CB  . HIS A 187 ? 834.0457 834.0457 834.0457 0.0000 0.0000 0.0000 519 HIS I CB  
1491 C CG  . HIS A 187 ? 834.3548 834.3548 834.3548 0.0000 0.0000 0.0000 519 HIS I CG  
1492 N ND1 . HIS A 187 ? 833.9089 833.9089 833.9089 0.0000 0.0000 0.0000 519 HIS I ND1 
1493 C CD2 . HIS A 187 ? 834.5315 834.5315 834.5315 0.0000 0.0000 0.0000 519 HIS I CD2 
1494 C CE1 . HIS A 187 ? 834.2166 834.2166 834.2166 0.0000 0.0000 0.0000 519 HIS I CE1 
1495 N NE2 . HIS A 187 ? 834.5905 834.5905 834.5905 0.0000 0.0000 0.0000 519 HIS I NE2 
1496 N N   . ALA A 188 ? 771.0953 771.0953 771.0953 0.0000 0.0000 0.0000 520 ALA I N   
1497 C CA  . ALA A 188 ? 769.2513 769.2513 769.2513 0.0000 0.0000 0.0000 520 ALA I CA  
1498 C C   . ALA A 188 ? 767.9825 767.9825 767.9825 0.0000 0.0000 0.0000 520 ALA I C   
1499 O O   . ALA A 188 ? 768.6042 768.6042 768.6042 0.0000 0.0000 0.0000 520 ALA I O   
1500 C CB  . ALA A 188 ? 768.5663 768.5663 768.5663 0.0000 0.0000 0.0000 520 ALA I CB  
1501 N N   . PRO A 189 ? 739.7620 739.7620 739.7620 0.0000 0.0000 0.0000 521 PRO I N   
1502 C CA  . PRO A 189 ? 739.2199 739.2199 739.2199 0.0000 0.0000 0.0000 521 PRO I CA  
1503 C C   . PRO A 189 ? 737.3191 737.3191 737.3191 0.0000 0.0000 0.0000 521 PRO I C   
1504 O O   . PRO A 189 ? 737.7433 737.7433 737.7433 0.0000 0.0000 0.0000 521 PRO I O   
1505 C CB  . PRO A 189 ? 738.8651 738.8651 738.8651 0.0000 0.0000 0.0000 521 PRO I CB  
1506 C CG  . PRO A 189 ? 739.1298 739.1298 739.1298 0.0000 0.0000 0.0000 521 PRO I CG  
1507 C CD  . PRO A 189 ? 739.5847 739.5847 739.5847 0.0000 0.0000 0.0000 521 PRO I CD  
1508 N N   . ALA A 190 ? 685.3851 685.3851 685.3851 0.0000 0.0000 0.0000 522 ALA I N   
1509 C CA  . ALA A 190 ? 682.4970 682.4970 682.4970 0.0000 0.0000 0.0000 522 ALA I CA  
1510 C C   . ALA A 190 ? 681.6694 681.6694 681.6694 0.0000 0.0000 0.0000 522 ALA I C   
1511 O O   . ALA A 190 ? 681.7620 681.7620 681.7620 0.0000 0.0000 0.0000 522 ALA I O   
1512 C CB  . ALA A 190 ? 682.7453 682.7453 682.7453 0.0000 0.0000 0.0000 522 ALA I CB  
1513 N N   . THR A 191 ? 650.8941 650.8941 650.8941 0.0000 0.0000 0.0000 523 THR I N   
1514 C CA  . THR A 191 ? 649.5813 649.5813 649.5813 0.0000 0.0000 0.0000 523 THR I CA  
1515 C C   . THR A 191 ? 647.1852 647.1852 647.1852 0.0000 0.0000 0.0000 523 THR I C   
1516 O O   . THR A 191 ? 648.2263 648.2263 648.2263 0.0000 0.0000 0.0000 523 THR I O   
1517 C CB  . THR A 191 ? 649.2553 649.2553 649.2553 0.0000 0.0000 0.0000 523 THR I CB  
1518 O OG1 . THR A 191 ? 647.8023 647.8023 647.8023 0.0000 0.0000 0.0000 523 THR I OG1 
1519 C CG2 . THR A 191 ? 650.4440 650.4440 650.4440 0.0000 0.0000 0.0000 523 THR I CG2 
1520 N N   . VAL A 192 ? 583.7538 583.7538 583.7538 0.0000 0.0000 0.0000 524 VAL I N   
1521 C CA  . VAL A 192 ? 582.0757 582.0757 582.0757 0.0000 0.0000 0.0000 524 VAL I CA  
1522 C C   . VAL A 192 ? 583.5126 583.5126 583.5126 0.0000 0.0000 0.0000 524 VAL I C   
1523 O O   . VAL A 192 ? 581.8825 581.8825 581.8825 0.0000 0.0000 0.0000 524 VAL I O   
1524 C CB  . VAL A 192 ? 578.4982 578.4982 578.4982 0.0000 0.0000 0.0000 524 VAL I CB  
1525 C CG1 . VAL A 192 ? 577.6578 577.6578 577.6578 0.0000 0.0000 0.0000 524 VAL I CG1 
1526 C CG2 . VAL A 192 ? 577.5815 577.5815 577.5815 0.0000 0.0000 0.0000 524 VAL I CG2 
1527 N N   . CYS A 193 ? 662.9377 662.9377 662.9377 0.0000 0.0000 0.0000 525 CYS I N   
1528 C CA  . CYS A 193 ? 664.6537 664.6537 664.6537 0.0000 0.0000 0.0000 525 CYS I CA  
1529 C C   . CYS A 193 ? 663.1463 663.1463 663.1463 0.0000 0.0000 0.0000 525 CYS I C   
1530 O O   . CYS A 193 ? 663.4219 663.4219 663.4219 0.0000 0.0000 0.0000 525 CYS I O   
1531 C CB  . CYS A 193 ? 666.1670 666.1670 666.1670 0.0000 0.0000 0.0000 525 CYS I CB  
1532 S SG  . CYS A 193 ? 666.7073 666.7073 666.7073 0.0000 0.0000 0.0000 525 CYS I SG  
1533 N N   . GLY A 194 ? 587.5302 587.5302 587.5302 0.0000 0.0000 0.0000 526 GLY I N   
1534 C CA  . GLY A 194 ? 585.5846 585.5846 585.5846 0.0000 0.0000 0.0000 526 GLY I CA  
1535 C C   . GLY A 194 ? 585.7334 585.7334 585.7334 0.0000 0.0000 0.0000 526 GLY I C   
1536 O O   . GLY A 194 ? 585.2223 585.2223 585.2223 0.0000 0.0000 0.0000 526 GLY I O   
1537 N N   . PRO A 195 ? 608.4686 608.4686 608.4686 0.0000 0.0000 0.0000 527 PRO I N   
1538 C CA  . PRO A 195 ? 609.3111 609.3111 609.3111 0.0000 0.0000 0.0000 527 PRO I CA  
1539 C C   . PRO A 195 ? 608.7009 608.7009 608.7009 0.0000 0.0000 0.0000 527 PRO I C   
1540 O O   . PRO A 195 ? 608.1034 608.1034 608.1034 0.0000 0.0000 0.0000 527 PRO I O   
1541 C CB  . PRO A 195 ? 609.2996 609.2996 609.2996 0.0000 0.0000 0.0000 527 PRO I CB  
1542 C CG  . PRO A 195 ? 609.7101 609.7101 609.7101 0.0000 0.0000 0.0000 527 PRO I CG  
1543 C CD  . PRO A 195 ? 609.2276 609.2276 609.2276 0.0000 0.0000 0.0000 527 PRO I CD  
# 
