data_9DAK
# 
_entry.id   9DAK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DAK         pdb_00009dak 10.2210/pdb9dak/pdb 
WWPDB D_1000287714 ?            ?                   
EMDB  EMD-46691    ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-02-19 ? 
2 'Structure model' 1 1 2025-04-02 ? 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'     
2 2 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation 
2 2 'Structure model' em_admin 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
4 2 'Structure model' '_em_admin.last_update'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DAK 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-22 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Merbecovirus PnNL2018B Spike glycoprotein RBD bound to the P. Nathusii ACE2' 
_pdbx_database_related.db_id          EMD-46691 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              dveesler@uw.edu 
_pdbx_contact_author.name_first         David 
_pdbx_contact_author.name_last          Veesler 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6019-8675 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Park, Y.J.'                                                         1 ? 
'Veesler, D.'                                                        2 ? 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 3 ? 
# 
_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            Cell 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1097-4172 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            188 
_citation.language                  ? 
_citation.page_first                1693 
_citation.page_last                 1710.e18 
_citation.title                     'Multiple independent acquisitions of ACE2 usage in MERS-related coronaviruses.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.cell.2024.12.031 
_citation.pdbx_database_id_PubMed   39922191 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ma, C.B.'        1  ? 
primary 'Liu, C.'         2  ? 
primary 'Park, Y.J.'      3  ? 
primary 'Tang, J.'        4  ? 
primary 'Chen, J.'        5  ? 
primary 'Xiong, Q.'       6  ? 
primary 'Lee, J.'         7  ? 
primary 'Stewart, C.'     8  ? 
primary 'Asarnow, D.'     9  ? 
primary 'Brown, J.'       10 ? 
primary 'Tortorici, M.A.' 11 ? 
primary 'Yang, X.'        12 ? 
primary 'Sun, Y.H.'       13 ? 
primary 'Chen, Y.M.'      14 ? 
primary 'Yu, X.'          15 ? 
primary 'Si, J.Y.'        16 ? 
primary 'Liu, P.'         17 ? 
primary 'Tong, F.'        18 ? 
primary 'Huang, M.L.'     19 ? 
primary 'Li, J.'          20 ? 
primary 'Shi, Z.L.'       21 ? 
primary 'Deng, Z.'        22 ? 
primary 'Veesler, D.'     23 ? 
primary 'Yan, H.'         24 ? 
# 
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 ACE2 102102.375 1   ? ? 
;GenBank CAK6450646.1 chimeric sequence with Bat30 (Pteronotus davyi) residues 407-432, 598; includes N-terminal signal sequence and C-terminal tag for protein expression
;
;N-terminal tag: MGGEGLRASPRRRPLLPLQPRGCPRGDGCLRGGRGRAGFGFWRVTGGSRASANHVHAFFFFLQLLGNVLVIVLSHHFGKEFATMPMGSLQPLATLYLLGMLVASVLA
C-terminal tag: PTLGPPYQPPVTGTGGGSWSHPQFEKGGGSGGGSGGSAWSHPQFEKGGGGSDYKDHDGDYKDHDIDYKDDDDKL
;
2 polymer     man 'Spike glycoprotein receptor binding domain' 34357.488  1   ? ? 
'GenBank WDE20340.1; includes N-terminal signal sequence and C-terminal tag for protein expression' 
;N-terminal tag: MGILPSPGMPALLSLVSLLSVLLMGCVAETGT
C-terminal tag: LVPRGSSSGGSGLNDIFEAQKIEWHEGGSHHHHHHHH
;
3 branched    man 
'2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose' 570.542    2 
? ? ? ? 
4 branched    man '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401    3   ? ? ? ? 
5 branched    man 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose'  586.542    2 
? ? ? ? 
6 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208    4   ? ? ? ? 
7 non-polymer syn 'ZINC ION' 65.409     1   ? ? ? ? 
8 water       nat water 18.015     144 ? ? ? ? 
# 
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 
;MGGEGLRASPRRRPLLPLQPRGCPRGDGCLRGGRGRAGFGFWRVTGGSRASANHVHAFFFFLQLLGNVLVIVLSHHFGKE
FATMPMGSLQPLATLYLLGMLVASVLAQSLTTEEKAREFLDKFNSEAENWSHESALASWDYNTNINDKNAQKMNEADSKW
SAFYKEHSKLAQGFPLQEIQNSTIKLQLQILQQNGSSVLTAEKSKRLSTILTTMSTIYSTGKVCNPNNPQQCFTLSGLED
IMEKSKDYHQRLWIWEGWRSEVGKQLRPLYEEYVALKNEMARGNNYKDYGDYWRGDYETEGGDGYNYSRNHLIEDVDRIF
LEIKPLYEQLHAYVRAKLMNAYPSRISPTGCLPAHLLGDMWGRFWTNLYNLTVPFEKKQNIDVTDTMKKQSWDAEKIFKE
AEKFYLSVGLHNMTPEFWNNSMLTEPSDGRQVVCHPTAWDLGKNDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYAKQPY
LLRNGANEGFHEAVGEIMSLSAATPKHLKDLGLLAQNYPEDYETEINFLLKQALNIVGTLPFTYMLEKWRWMVFEGKIPK
EQWMEKWWEMKREIVGVVEPLPHDETYCDPASLFHVANDYSFIRYFTRTILEFQFQEALCQIANHTGPLHKCDISNSTEA
GKQLKNMLELGKSKPWTFALEQIARTKEMDAKPLLNYFKPLFSWLKELNGNSVGWSADWSPYSEQSIKVRISLKSALGEK
AYEWNDNEMYLFRSSVAYAMRVYFLKVKNETIPFRAEDVWVSDEKIRVSFKFFVTSPTNVSDIIPRSEVEDAIRMSRGRI
NDAFRLDDKTLEFLGIQPTLGPPYQPPVTGTGGGSWSHPQFEKGGGSGGGSGGSAWSHPQFEKGGGGSDYKDHDGDYKDH
DIDYKDDDDKL
;
;MGGEGLRASPRRRPLLPLQPRGCPRGDGCLRGGRGRAGFGFWRVTGGSRASANHVHAFFFFLQLLGNVLVIVLSHHFGKE
FATMPMGSLQPLATLYLLGMLVASVLAQSLTTEEKAREFLDKFNSEAENWSHESALASWDYNTNINDKNAQKMNEADSKW
SAFYKEHSKLAQGFPLQEIQNSTIKLQLQILQQNGSSVLTAEKSKRLSTILTTMSTIYSTGKVCNPNNPQQCFTLSGLED
IMEKSKDYHQRLWIWEGWRSEVGKQLRPLYEEYVALKNEMARGNNYKDYGDYWRGDYETEGGDGYNYSRNHLIEDVDRIF
LEIKPLYEQLHAYVRAKLMNAYPSRISPTGCLPAHLLGDMWGRFWTNLYNLTVPFEKKQNIDVTDTMKKQSWDAEKIFKE
AEKFYLSVGLHNMTPEFWNNSMLTEPSDGRQVVCHPTAWDLGKNDFRIKMCTKVTMDDFLTAHHEMGHIQYDMAYAKQPY
LLRNGANEGFHEAVGEIMSLSAATPKHLKDLGLLAQNYPEDYETEINFLLKQALNIVGTLPFTYMLEKWRWMVFEGKIPK
EQWMEKWWEMKREIVGVVEPLPHDETYCDPASLFHVANDYSFIRYFTRTILEFQFQEALCQIANHTGPLHKCDISNSTEA
GKQLKNMLELGKSKPWTFALEQIARTKEMDAKPLLNYFKPLFSWLKELNGNSVGWSADWSPYSEQSIKVRISLKSALGEK
AYEWNDNEMYLFRSSVAYAMRVYFLKVKNETIPFRAEDVWVSDEKIRVSFKFFVTSPTNVSDIIPRSEVEDAIRMSRGRI
NDAFRLDDKTLEFLGIQPTLGPPYQPPVTGTGGGSWSHPQFEKGGGSGGGSGGSAWSHPQFEKGGGGSDYKDHDGDYKDH
DIDYKDDDDKL
;
A ? 
2 'polypeptide(L)' no no 
;MGILPSPGMPALLSLVSLLSVLLMGCVAETGTYSVSSFEARPQGSFVESVYEGNECDFTKLFRGPVPQPYEFGRLVFTNC
NYNFTKLLSYFQVDAFECKKVTPESIATGCYSSLTVDWFAYRVADKSDLLPGSSSDLQRFNYKPTYAHPTCLISAYTDLS
ALGGSNPTNYTLLTNCYGCVGQPPKRTCLEEFPSFVEAGYRPKPSCARIGMQGHASGNETYTAVVTNNELDSVGDPIWRM
GVAQTKEPSVTDKAELAFFVSVQIDSQSSSVCPLGSPKLVPRGSSSGGSGLNDIFEAQKIEWHEGGSHHHHHHHH
;
;MGILPSPGMPALLSLVSLLSVLLMGCVAETGTYSVSSFEARPQGSFVESVYEGNECDFTKLFRGPVPQPYEFGRLVFTNC
NYNFTKLLSYFQVDAFECKKVTPESIATGCYSSLTVDWFAYRVADKSDLLPGSSSDLQRFNYKPTYAHPTCLISAYTDLS
ALGGSNPTNYTLLTNCYGCVGQPPKRTCLEEFPSFVEAGYRPKPSCARIGMQGHASGNETYTAVVTNNELDSVGDPIWRM
GVAQTKEPSVTDKAELAFFVSVQIDSQSSSVCPLGSPKLVPRGSSSGGSGLNDIFEAQKIEWHEGGSHHHHHHHH
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
6 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
7 'ZINC ION'                               ZN  
8 water                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   GLY n 
1 4   GLU n 
1 5   GLY n 
1 6   LEU n 
1 7   ARG n 
1 8   ALA n 
1 9   SER n 
1 10  PRO n 
1 11  ARG n 
1 12  ARG n 
1 13  ARG n 
1 14  PRO n 
1 15  LEU n 
1 16  LEU n 
1 17  PRO n 
1 18  LEU n 
1 19  GLN n 
1 20  PRO n 
1 21  ARG n 
1 22  GLY n 
1 23  CYS n 
1 24  PRO n 
1 25  ARG n 
1 26  GLY n 
1 27  ASP n 
1 28  GLY n 
1 29  CYS n 
1 30  LEU n 
1 31  ARG n 
1 32  GLY n 
1 33  GLY n 
1 34  ARG n 
1 35  GLY n 
1 36  ARG n 
1 37  ALA n 
1 38  GLY n 
1 39  PHE n 
1 40  GLY n 
1 41  PHE n 
1 42  TRP n 
1 43  ARG n 
1 44  VAL n 
1 45  THR n 
1 46  GLY n 
1 47  GLY n 
1 48  SER n 
1 49  ARG n 
1 50  ALA n 
1 51  SER n 
1 52  ALA n 
1 53  ASN n 
1 54  HIS n 
1 55  VAL n 
1 56  HIS n 
1 57  ALA n 
1 58  PHE n 
1 59  PHE n 
1 60  PHE n 
1 61  PHE n 
1 62  LEU n 
1 63  GLN n 
1 64  LEU n 
1 65  LEU n 
1 66  GLY n 
1 67  ASN n 
1 68  VAL n 
1 69  LEU n 
1 70  VAL n 
1 71  ILE n 
1 72  VAL n 
1 73  LEU n 
1 74  SER n 
1 75  HIS n 
1 76  HIS n 
1 77  PHE n 
1 78  GLY n 
1 79  LYS n 
1 80  GLU n 
1 81  PHE n 
1 82  ALA n 
1 83  THR n 
1 84  MET n 
1 85  PRO n 
1 86  MET n 
1 87  GLY n 
1 88  SER n 
1 89  LEU n 
1 90  GLN n 
1 91  PRO n 
1 92  LEU n 
1 93  ALA n 
1 94  THR n 
1 95  LEU n 
1 96  TYR n 
1 97  LEU n 
1 98  LEU n 
1 99  GLY n 
1 100 MET n 
1 101 LEU n 
1 102 VAL n 
1 103 ALA n 
1 104 SER n 
1 105 VAL n 
1 106 LEU n 
1 107 ALA n 
1 108 GLN n 
1 109 SER n 
1 110 LEU n 
1 111 THR n 
1 112 THR n 
1 113 GLU n 
1 114 GLU n 
1 115 LYS n 
1 116 ALA n 
1 117 ARG n 
1 118 GLU n 
1 119 PHE n 
1 120 LEU n 
1 121 ASP n 
1 122 LYS n 
1 123 PHE n 
1 124 ASN n 
1 125 SER n 
1 126 GLU n 
1 127 ALA n 
1 128 GLU n 
1 129 ASN n 
1 130 TRP n 
1 131 SER n 
1 132 HIS n 
1 133 GLU n 
1 134 SER n 
1 135 ALA n 
1 136 LEU n 
1 137 ALA n 
1 138 SER n 
1 139 TRP n 
1 140 ASP n 
1 141 TYR n 
1 142 ASN n 
1 143 THR n 
1 144 ASN n 
1 145 ILE n 
1 146 ASN n 
1 147 ASP n 
1 148 LYS n 
1 149 ASN n 
1 150 ALA n 
1 151 GLN n 
1 152 LYS n 
1 153 MET n 
1 154 ASN n 
1 155 GLU n 
1 156 ALA n 
1 157 ASP n 
1 158 SER n 
1 159 LYS n 
1 160 TRP n 
1 161 SER n 
1 162 ALA n 
1 163 PHE n 
1 164 TYR n 
1 165 LYS n 
1 166 GLU n 
1 167 HIS n 
1 168 SER n 
1 169 LYS n 
1 170 LEU n 
1 171 ALA n 
1 172 GLN n 
1 173 GLY n 
1 174 PHE n 
1 175 PRO n 
1 176 LEU n 
1 177 GLN n 
1 178 GLU n 
1 179 ILE n 
1 180 GLN n 
1 181 ASN n 
1 182 SER n 
1 183 THR n 
1 184 ILE n 
1 185 LYS n 
1 186 LEU n 
1 187 GLN n 
1 188 LEU n 
1 189 GLN n 
1 190 ILE n 
1 191 LEU n 
1 192 GLN n 
1 193 GLN n 
1 194 ASN n 
1 195 GLY n 
1 196 SER n 
1 197 SER n 
1 198 VAL n 
1 199 LEU n 
1 200 THR n 
1 201 ALA n 
1 202 GLU n 
1 203 LYS n 
1 204 SER n 
1 205 LYS n 
1 206 ARG n 
1 207 LEU n 
1 208 SER n 
1 209 THR n 
1 210 ILE n 
1 211 LEU n 
1 212 THR n 
1 213 THR n 
1 214 MET n 
1 215 SER n 
1 216 THR n 
1 217 ILE n 
1 218 TYR n 
1 219 SER n 
1 220 THR n 
1 221 GLY n 
1 222 LYS n 
1 223 VAL n 
1 224 CYS n 
1 225 ASN n 
1 226 PRO n 
1 227 ASN n 
1 228 ASN n 
1 229 PRO n 
1 230 GLN n 
1 231 GLN n 
1 232 CYS n 
1 233 PHE n 
1 234 THR n 
1 235 LEU n 
1 236 SER n 
1 237 GLY n 
1 238 LEU n 
1 239 GLU n 
1 240 ASP n 
1 241 ILE n 
1 242 MET n 
1 243 GLU n 
1 244 LYS n 
1 245 SER n 
1 246 LYS n 
1 247 ASP n 
1 248 TYR n 
1 249 HIS n 
1 250 GLN n 
1 251 ARG n 
1 252 LEU n 
1 253 TRP n 
1 254 ILE n 
1 255 TRP n 
1 256 GLU n 
1 257 GLY n 
1 258 TRP n 
1 259 ARG n 
1 260 SER n 
1 261 GLU n 
1 262 VAL n 
1 263 GLY n 
1 264 LYS n 
1 265 GLN n 
1 266 LEU n 
1 267 ARG n 
1 268 PRO n 
1 269 LEU n 
1 270 TYR n 
1 271 GLU n 
1 272 GLU n 
1 273 TYR n 
1 274 VAL n 
1 275 ALA n 
1 276 LEU n 
1 277 LYS n 
1 278 ASN n 
1 279 GLU n 
1 280 MET n 
1 281 ALA n 
1 282 ARG n 
1 283 GLY n 
1 284 ASN n 
1 285 ASN n 
1 286 TYR n 
1 287 LYS n 
1 288 ASP n 
1 289 TYR n 
1 290 GLY n 
1 291 ASP n 
1 292 TYR n 
1 293 TRP n 
1 294 ARG n 
1 295 GLY n 
1 296 ASP n 
1 297 TYR n 
1 298 GLU n 
1 299 THR n 
1 300 GLU n 
1 301 GLY n 
1 302 GLY n 
1 303 ASP n 
1 304 GLY n 
1 305 TYR n 
1 306 ASN n 
1 307 TYR n 
1 308 SER n 
1 309 ARG n 
1 310 ASN n 
1 311 HIS n 
1 312 LEU n 
1 313 ILE n 
1 314 GLU n 
1 315 ASP n 
1 316 VAL n 
1 317 ASP n 
1 318 ARG n 
1 319 ILE n 
1 320 PHE n 
1 321 LEU n 
1 322 GLU n 
1 323 ILE n 
1 324 LYS n 
1 325 PRO n 
1 326 LEU n 
1 327 TYR n 
1 328 GLU n 
1 329 GLN n 
1 330 LEU n 
1 331 HIS n 
1 332 ALA n 
1 333 TYR n 
1 334 VAL n 
1 335 ARG n 
1 336 ALA n 
1 337 LYS n 
1 338 LEU n 
1 339 MET n 
1 340 ASN n 
1 341 ALA n 
1 342 TYR n 
1 343 PRO n 
1 344 SER n 
1 345 ARG n 
1 346 ILE n 
1 347 SER n 
1 348 PRO n 
1 349 THR n 
1 350 GLY n 
1 351 CYS n 
1 352 LEU n 
1 353 PRO n 
1 354 ALA n 
1 355 HIS n 
1 356 LEU n 
1 357 LEU n 
1 358 GLY n 
1 359 ASP n 
1 360 MET n 
1 361 TRP n 
1 362 GLY n 
1 363 ARG n 
1 364 PHE n 
1 365 TRP n 
1 366 THR n 
1 367 ASN n 
1 368 LEU n 
1 369 TYR n 
1 370 ASN n 
1 371 LEU n 
1 372 THR n 
1 373 VAL n 
1 374 PRO n 
1 375 PHE n 
1 376 GLU n 
1 377 LYS n 
1 378 LYS n 
1 379 GLN n 
1 380 ASN n 
1 381 ILE n 
1 382 ASP n 
1 383 VAL n 
1 384 THR n 
1 385 ASP n 
1 386 THR n 
1 387 MET n 
1 388 LYS n 
1 389 LYS n 
1 390 GLN n 
1 391 SER n 
1 392 TRP n 
1 393 ASP n 
1 394 ALA n 
1 395 GLU n 
1 396 LYS n 
1 397 ILE n 
1 398 PHE n 
1 399 LYS n 
1 400 GLU n 
1 401 ALA n 
1 402 GLU n 
1 403 LYS n 
1 404 PHE n 
1 405 TYR n 
1 406 LEU n 
1 407 SER n 
1 408 VAL n 
1 409 GLY n 
1 410 LEU n 
1 411 HIS n 
1 412 ASN n 
1 413 MET n 
1 414 THR n 
1 415 PRO n 
1 416 GLU n 
1 417 PHE n 
1 418 TRP n 
1 419 ASN n 
1 420 ASN n 
1 421 SER n 
1 422 MET n 
1 423 LEU n 
1 424 THR n 
1 425 GLU n 
1 426 PRO n 
1 427 SER n 
1 428 ASP n 
1 429 GLY n 
1 430 ARG n 
1 431 GLN n 
1 432 VAL n 
1 433 VAL n 
1 434 CYS n 
1 435 HIS n 
1 436 PRO n 
1 437 THR n 
1 438 ALA n 
1 439 TRP n 
1 440 ASP n 
1 441 LEU n 
1 442 GLY n 
1 443 LYS n 
1 444 ASN n 
1 445 ASP n 
1 446 PHE n 
1 447 ARG n 
1 448 ILE n 
1 449 LYS n 
1 450 MET n 
1 451 CYS n 
1 452 THR n 
1 453 LYS n 
1 454 VAL n 
1 455 THR n 
1 456 MET n 
1 457 ASP n 
1 458 ASP n 
1 459 PHE n 
1 460 LEU n 
1 461 THR n 
1 462 ALA n 
1 463 HIS n 
1 464 HIS n 
1 465 GLU n 
1 466 MET n 
1 467 GLY n 
1 468 HIS n 
1 469 ILE n 
1 470 GLN n 
1 471 TYR n 
1 472 ASP n 
1 473 MET n 
1 474 ALA n 
1 475 TYR n 
1 476 ALA n 
1 477 LYS n 
1 478 GLN n 
1 479 PRO n 
1 480 TYR n 
1 481 LEU n 
1 482 LEU n 
1 483 ARG n 
1 484 ASN n 
1 485 GLY n 
1 486 ALA n 
1 487 ASN n 
1 488 GLU n 
1 489 GLY n 
1 490 PHE n 
1 491 HIS n 
1 492 GLU n 
1 493 ALA n 
1 494 VAL n 
1 495 GLY n 
1 496 GLU n 
1 497 ILE n 
1 498 MET n 
1 499 SER n 
1 500 LEU n 
1 501 SER n 
1 502 ALA n 
1 503 ALA n 
1 504 THR n 
1 505 PRO n 
1 506 LYS n 
1 507 HIS n 
1 508 LEU n 
1 509 LYS n 
1 510 ASP n 
1 511 LEU n 
1 512 GLY n 
1 513 LEU n 
1 514 LEU n 
1 515 ALA n 
1 516 GLN n 
1 517 ASN n 
1 518 TYR n 
1 519 PRO n 
1 520 GLU n 
1 521 ASP n 
1 522 TYR n 
1 523 GLU n 
1 524 THR n 
1 525 GLU n 
1 526 ILE n 
1 527 ASN n 
1 528 PHE n 
1 529 LEU n 
1 530 LEU n 
1 531 LYS n 
1 532 GLN n 
1 533 ALA n 
1 534 LEU n 
1 535 ASN n 
1 536 ILE n 
1 537 VAL n 
1 538 GLY n 
1 539 THR n 
1 540 LEU n 
1 541 PRO n 
1 542 PHE n 
1 543 THR n 
1 544 TYR n 
1 545 MET n 
1 546 LEU n 
1 547 GLU n 
1 548 LYS n 
1 549 TRP n 
1 550 ARG n 
1 551 TRP n 
1 552 MET n 
1 553 VAL n 
1 554 PHE n 
1 555 GLU n 
1 556 GLY n 
1 557 LYS n 
1 558 ILE n 
1 559 PRO n 
1 560 LYS n 
1 561 GLU n 
1 562 GLN n 
1 563 TRP n 
1 564 MET n 
1 565 GLU n 
1 566 LYS n 
1 567 TRP n 
1 568 TRP n 
1 569 GLU n 
1 570 MET n 
1 571 LYS n 
1 572 ARG n 
1 573 GLU n 
1 574 ILE n 
1 575 VAL n 
1 576 GLY n 
1 577 VAL n 
1 578 VAL n 
1 579 GLU n 
1 580 PRO n 
1 581 LEU n 
1 582 PRO n 
1 583 HIS n 
1 584 ASP n 
1 585 GLU n 
1 586 THR n 
1 587 TYR n 
1 588 CYS n 
1 589 ASP n 
1 590 PRO n 
1 591 ALA n 
1 592 SER n 
1 593 LEU n 
1 594 PHE n 
1 595 HIS n 
1 596 VAL n 
1 597 ALA n 
1 598 ASN n 
1 599 ASP n 
1 600 TYR n 
1 601 SER n 
1 602 PHE n 
1 603 ILE n 
1 604 ARG n 
1 605 TYR n 
1 606 PHE n 
1 607 THR n 
1 608 ARG n 
1 609 THR n 
1 610 ILE n 
1 611 LEU n 
1 612 GLU n 
1 613 PHE n 
1 614 GLN n 
1 615 PHE n 
1 616 GLN n 
1 617 GLU n 
1 618 ALA n 
1 619 LEU n 
1 620 CYS n 
1 621 GLN n 
1 622 ILE n 
1 623 ALA n 
1 624 ASN n 
1 625 HIS n 
1 626 THR n 
1 627 GLY n 
1 628 PRO n 
1 629 LEU n 
1 630 HIS n 
1 631 LYS n 
1 632 CYS n 
1 633 ASP n 
1 634 ILE n 
1 635 SER n 
1 636 ASN n 
1 637 SER n 
1 638 THR n 
1 639 GLU n 
1 640 ALA n 
1 641 GLY n 
1 642 LYS n 
1 643 GLN n 
1 644 LEU n 
1 645 LYS n 
1 646 ASN n 
1 647 MET n 
1 648 LEU n 
1 649 GLU n 
1 650 LEU n 
1 651 GLY n 
1 652 LYS n 
1 653 SER n 
1 654 LYS n 
1 655 PRO n 
1 656 TRP n 
1 657 THR n 
1 658 PHE n 
1 659 ALA n 
1 660 LEU n 
1 661 GLU n 
1 662 GLN n 
1 663 ILE n 
1 664 ALA n 
1 665 ARG n 
1 666 THR n 
1 667 LYS n 
1 668 GLU n 
1 669 MET n 
1 670 ASP n 
1 671 ALA n 
1 672 LYS n 
1 673 PRO n 
1 674 LEU n 
1 675 LEU n 
1 676 ASN n 
1 677 TYR n 
1 678 PHE n 
1 679 LYS n 
1 680 PRO n 
1 681 LEU n 
1 682 PHE n 
1 683 SER n 
1 684 TRP n 
1 685 LEU n 
1 686 LYS n 
1 687 GLU n 
1 688 LEU n 
1 689 ASN n 
1 690 GLY n 
1 691 ASN n 
1 692 SER n 
1 693 VAL n 
1 694 GLY n 
1 695 TRP n 
1 696 SER n 
1 697 ALA n 
1 698 ASP n 
1 699 TRP n 
1 700 SER n 
1 701 PRO n 
1 702 TYR n 
1 703 SER n 
1 704 GLU n 
1 705 GLN n 
1 706 SER n 
1 707 ILE n 
1 708 LYS n 
1 709 VAL n 
1 710 ARG n 
1 711 ILE n 
1 712 SER n 
1 713 LEU n 
1 714 LYS n 
1 715 SER n 
1 716 ALA n 
1 717 LEU n 
1 718 GLY n 
1 719 GLU n 
1 720 LYS n 
1 721 ALA n 
1 722 TYR n 
1 723 GLU n 
1 724 TRP n 
1 725 ASN n 
1 726 ASP n 
1 727 ASN n 
1 728 GLU n 
1 729 MET n 
1 730 TYR n 
1 731 LEU n 
1 732 PHE n 
1 733 ARG n 
1 734 SER n 
1 735 SER n 
1 736 VAL n 
1 737 ALA n 
1 738 TYR n 
1 739 ALA n 
1 740 MET n 
1 741 ARG n 
1 742 VAL n 
1 743 TYR n 
1 744 PHE n 
1 745 LEU n 
1 746 LYS n 
1 747 VAL n 
1 748 LYS n 
1 749 ASN n 
1 750 GLU n 
1 751 THR n 
1 752 ILE n 
1 753 PRO n 
1 754 PHE n 
1 755 ARG n 
1 756 ALA n 
1 757 GLU n 
1 758 ASP n 
1 759 VAL n 
1 760 TRP n 
1 761 VAL n 
1 762 SER n 
1 763 ASP n 
1 764 GLU n 
1 765 LYS n 
1 766 ILE n 
1 767 ARG n 
1 768 VAL n 
1 769 SER n 
1 770 PHE n 
1 771 LYS n 
1 772 PHE n 
1 773 PHE n 
1 774 VAL n 
1 775 THR n 
1 776 SER n 
1 777 PRO n 
1 778 THR n 
1 779 ASN n 
1 780 VAL n 
1 781 SER n 
1 782 ASP n 
1 783 ILE n 
1 784 ILE n 
1 785 PRO n 
1 786 ARG n 
1 787 SER n 
1 788 GLU n 
1 789 VAL n 
1 790 GLU n 
1 791 ASP n 
1 792 ALA n 
1 793 ILE n 
1 794 ARG n 
1 795 MET n 
1 796 SER n 
1 797 ARG n 
1 798 GLY n 
1 799 ARG n 
1 800 ILE n 
1 801 ASN n 
1 802 ASP n 
1 803 ALA n 
1 804 PHE n 
1 805 ARG n 
1 806 LEU n 
1 807 ASP n 
1 808 ASP n 
1 809 LYS n 
1 810 THR n 
1 811 LEU n 
1 812 GLU n 
1 813 PHE n 
1 814 LEU n 
1 815 GLY n 
1 816 ILE n 
1 817 GLN n 
1 818 PRO n 
1 819 THR n 
1 820 LEU n 
1 821 GLY n 
1 822 PRO n 
1 823 PRO n 
1 824 TYR n 
1 825 GLN n 
1 826 PRO n 
1 827 PRO n 
1 828 VAL n 
1 829 THR n 
1 830 GLY n 
1 831 THR n 
1 832 GLY n 
1 833 GLY n 
1 834 GLY n 
1 835 SER n 
1 836 TRP n 
1 837 SER n 
1 838 HIS n 
1 839 PRO n 
1 840 GLN n 
1 841 PHE n 
1 842 GLU n 
1 843 LYS n 
1 844 GLY n 
1 845 GLY n 
1 846 GLY n 
1 847 SER n 
1 848 GLY n 
1 849 GLY n 
1 850 GLY n 
1 851 SER n 
1 852 GLY n 
1 853 GLY n 
1 854 SER n 
1 855 ALA n 
1 856 TRP n 
1 857 SER n 
1 858 HIS n 
1 859 PRO n 
1 860 GLN n 
1 861 PHE n 
1 862 GLU n 
1 863 LYS n 
1 864 GLY n 
1 865 GLY n 
1 866 GLY n 
1 867 GLY n 
1 868 SER n 
1 869 ASP n 
1 870 TYR n 
1 871 LYS n 
1 872 ASP n 
1 873 HIS n 
1 874 ASP n 
1 875 GLY n 
1 876 ASP n 
1 877 TYR n 
1 878 LYS n 
1 879 ASP n 
1 880 HIS n 
1 881 ASP n 
1 882 ILE n 
1 883 ASP n 
1 884 TYR n 
1 885 LYS n 
1 886 ASP n 
1 887 ASP n 
1 888 ASP n 
1 889 ASP n 
1 890 LYS n 
1 891 LEU n 
2 1   MET n 
2 2   GLY n 
2 3   ILE n 
2 4   LEU n 
2 5   PRO n 
2 6   SER n 
2 7   PRO n 
2 8   GLY n 
2 9   MET n 
2 10  PRO n 
2 11  ALA n 
2 12  LEU n 
2 13  LEU n 
2 14  SER n 
2 15  LEU n 
2 16  VAL n 
2 17  SER n 
2 18  LEU n 
2 19  LEU n 
2 20  SER n 
2 21  VAL n 
2 22  LEU n 
2 23  LEU n 
2 24  MET n 
2 25  GLY n 
2 26  CYS n 
2 27  VAL n 
2 28  ALA n 
2 29  GLU n 
2 30  THR n 
2 31  GLY n 
2 32  THR n 
2 33  TYR n 
2 34  SER n 
2 35  VAL n 
2 36  SER n 
2 37  SER n 
2 38  PHE n 
2 39  GLU n 
2 40  ALA n 
2 41  ARG n 
2 42  PRO n 
2 43  GLN n 
2 44  GLY n 
2 45  SER n 
2 46  PHE n 
2 47  VAL n 
2 48  GLU n 
2 49  SER n 
2 50  VAL n 
2 51  TYR n 
2 52  GLU n 
2 53  GLY n 
2 54  ASN n 
2 55  GLU n 
2 56  CYS n 
2 57  ASP n 
2 58  PHE n 
2 59  THR n 
2 60  LYS n 
2 61  LEU n 
2 62  PHE n 
2 63  ARG n 
2 64  GLY n 
2 65  PRO n 
2 66  VAL n 
2 67  PRO n 
2 68  GLN n 
2 69  PRO n 
2 70  TYR n 
2 71  GLU n 
2 72  PHE n 
2 73  GLY n 
2 74  ARG n 
2 75  LEU n 
2 76  VAL n 
2 77  PHE n 
2 78  THR n 
2 79  ASN n 
2 80  CYS n 
2 81  ASN n 
2 82  TYR n 
2 83  ASN n 
2 84  PHE n 
2 85  THR n 
2 86  LYS n 
2 87  LEU n 
2 88  LEU n 
2 89  SER n 
2 90  TYR n 
2 91  PHE n 
2 92  GLN n 
2 93  VAL n 
2 94  ASP n 
2 95  ALA n 
2 96  PHE n 
2 97  GLU n 
2 98  CYS n 
2 99  LYS n 
2 100 LYS n 
2 101 VAL n 
2 102 THR n 
2 103 PRO n 
2 104 GLU n 
2 105 SER n 
2 106 ILE n 
2 107 ALA n 
2 108 THR n 
2 109 GLY n 
2 110 CYS n 
2 111 TYR n 
2 112 SER n 
2 113 SER n 
2 114 LEU n 
2 115 THR n 
2 116 VAL n 
2 117 ASP n 
2 118 TRP n 
2 119 PHE n 
2 120 ALA n 
2 121 TYR n 
2 122 ARG n 
2 123 VAL n 
2 124 ALA n 
2 125 ASP n 
2 126 LYS n 
2 127 SER n 
2 128 ASP n 
2 129 LEU n 
2 130 LEU n 
2 131 PRO n 
2 132 GLY n 
2 133 SER n 
2 134 SER n 
2 135 SER n 
2 136 ASP n 
2 137 LEU n 
2 138 GLN n 
2 139 ARG n 
2 140 PHE n 
2 141 ASN n 
2 142 TYR n 
2 143 LYS n 
2 144 PRO n 
2 145 THR n 
2 146 TYR n 
2 147 ALA n 
2 148 HIS n 
2 149 PRO n 
2 150 THR n 
2 151 CYS n 
2 152 LEU n 
2 153 ILE n 
2 154 SER n 
2 155 ALA n 
2 156 TYR n 
2 157 THR n 
2 158 ASP n 
2 159 LEU n 
2 160 SER n 
2 161 ALA n 
2 162 LEU n 
2 163 GLY n 
2 164 GLY n 
2 165 SER n 
2 166 ASN n 
2 167 PRO n 
2 168 THR n 
2 169 ASN n 
2 170 TYR n 
2 171 THR n 
2 172 LEU n 
2 173 LEU n 
2 174 THR n 
2 175 ASN n 
2 176 CYS n 
2 177 TYR n 
2 178 GLY n 
2 179 CYS n 
2 180 VAL n 
2 181 GLY n 
2 182 GLN n 
2 183 PRO n 
2 184 PRO n 
2 185 LYS n 
2 186 ARG n 
2 187 THR n 
2 188 CYS n 
2 189 LEU n 
2 190 GLU n 
2 191 GLU n 
2 192 PHE n 
2 193 PRO n 
2 194 SER n 
2 195 PHE n 
2 196 VAL n 
2 197 GLU n 
2 198 ALA n 
2 199 GLY n 
2 200 TYR n 
2 201 ARG n 
2 202 PRO n 
2 203 LYS n 
2 204 PRO n 
2 205 SER n 
2 206 CYS n 
2 207 ALA n 
2 208 ARG n 
2 209 ILE n 
2 210 GLY n 
2 211 MET n 
2 212 GLN n 
2 213 GLY n 
2 214 HIS n 
2 215 ALA n 
2 216 SER n 
2 217 GLY n 
2 218 ASN n 
2 219 GLU n 
2 220 THR n 
2 221 TYR n 
2 222 THR n 
2 223 ALA n 
2 224 VAL n 
2 225 VAL n 
2 226 THR n 
2 227 ASN n 
2 228 ASN n 
2 229 GLU n 
2 230 LEU n 
2 231 ASP n 
2 232 SER n 
2 233 VAL n 
2 234 GLY n 
2 235 ASP n 
2 236 PRO n 
2 237 ILE n 
2 238 TRP n 
2 239 ARG n 
2 240 MET n 
2 241 GLY n 
2 242 VAL n 
2 243 ALA n 
2 244 GLN n 
2 245 THR n 
2 246 LYS n 
2 247 GLU n 
2 248 PRO n 
2 249 SER n 
2 250 VAL n 
2 251 THR n 
2 252 ASP n 
2 253 LYS n 
2 254 ALA n 
2 255 GLU n 
2 256 LEU n 
2 257 ALA n 
2 258 PHE n 
2 259 PHE n 
2 260 VAL n 
2 261 SER n 
2 262 VAL n 
2 263 GLN n 
2 264 ILE n 
2 265 ASP n 
2 266 SER n 
2 267 GLN n 
2 268 SER n 
2 269 SER n 
2 270 SER n 
2 271 VAL n 
2 272 CYS n 
2 273 PRO n 
2 274 LEU n 
2 275 GLY n 
2 276 SER n 
2 277 PRO n 
2 278 LYS n 
2 279 LEU n 
2 280 VAL n 
2 281 PRO n 
2 282 ARG n 
2 283 GLY n 
2 284 SER n 
2 285 SER n 
2 286 SER n 
2 287 GLY n 
2 288 GLY n 
2 289 SER n 
2 290 GLY n 
2 291 LEU n 
2 292 ASN n 
2 293 ASP n 
2 294 ILE n 
2 295 PHE n 
2 296 GLU n 
2 297 ALA n 
2 298 GLN n 
2 299 LYS n 
2 300 ILE n 
2 301 GLU n 
2 302 TRP n 
2 303 HIS n 
2 304 GLU n 
2 305 GLY n 
2 306 GLY n 
2 307 SER n 
2 308 HIS n 
2 309 HIS n 
2 310 HIS n 
2 311 HIS n 
2 312 HIS n 
2 313 HIS n 
2 314 HIS n 
2 315 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 891 ? ? ? ? ?         ? ? ? ? 'Pipistrellus nathusii' 59473   ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 315 ? ? ? ? PnNL2018B ? ? ? ? Merbecovirus            2509494 ? ? ? ? ? ? ? human 
'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
3 oligosaccharide 
4 oligosaccharide 
5 oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 3 'DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-'                                         'Glycam Condensed Sequence' GMML       1.0   
2 3 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1' WURCS                       PDB2Glycan 1.1.0 
3 3 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}}'        LINUCS                      PDB-CARE   ?     
4 4 DGlcpNAcb1-4DGlcpNAcb1-                                                      'Glycam Condensed Sequence' GMML       1.0   
5 4 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                        WURCS                       PDB2Glycan 1.1.0 
6 4 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}'                           LINUCS                      PDB-CARE   ?     
7 5 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-                                             'Glycam Condensed Sequence' GMML       1.0   
8 5 'WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1' WURCS                       PDB2Glycan 1.1.0 
9 5 '[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}'        LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 3 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
2 3 3 FUC C1 O1 1 NAG O6 HO6 sing ? 
3 4 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
4 5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
5 5 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
# 
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 
BMA 'D-saccharide, beta linking'  . beta-D-mannopyranose                     'beta-D-mannose; D-mannose; mannose' 'C6 H12 O6'      
180.156 
CYS 'L-peptide linking'           y CYSTEINE                                 ? 'C3 H7 N O2 S'   121.158 
FUC 'L-saccharide, alpha linking' . alpha-L-fucopyranose                     
'alpha-L-fucose; 6-deoxy-alpha-L-galactopyranose; L-fucose; fucose' 'C6 H12 O5'      164.156 
GLN 'L-peptide linking'           y GLUTAMINE                                ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'           y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'             y GLYCINE                                  ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking'           y HISTIDINE                                ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                   . WATER                                    ? 'H2 O'           18.015  
ILE 'L-peptide linking'           y ISOLEUCINE                               ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'           y LEUCINE                                  ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'           y LYSINE                                   ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'           y METHIONINE                               ? 'C5 H11 N O2 S'  149.211 
NAG 'D-saccharide, beta linking'  . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'    221.208 
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 
ZN  non-polymer                   . 'ZINC ION'                               ? 'Zn 2'           65.409  
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BMA 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DManpb                         
BMA 'COMMON NAME'                         GMML     1.0 b-D-mannopyranose              
BMA 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Manp                       
BMA 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Man                            
FUC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 LFucpa                         
FUC 'COMMON NAME'                         GMML     1.0 a-L-fucopyranose               
FUC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 a-L-Fucp                       
FUC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Fuc                            
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -89 ?   ?   ?   A . n 
A 1 2   GLY 2   -88 ?   ?   ?   A . n 
A 1 3   GLY 3   -87 ?   ?   ?   A . n 
A 1 4   GLU 4   -86 ?   ?   ?   A . n 
A 1 5   GLY 5   -85 ?   ?   ?   A . n 
A 1 6   LEU 6   -84 ?   ?   ?   A . n 
A 1 7   ARG 7   -83 ?   ?   ?   A . n 
A 1 8   ALA 8   -82 ?   ?   ?   A . n 
A 1 9   SER 9   -81 ?   ?   ?   A . n 
A 1 10  PRO 10  -80 ?   ?   ?   A . n 
A 1 11  ARG 11  -79 ?   ?   ?   A . n 
A 1 12  ARG 12  -78 ?   ?   ?   A . n 
A 1 13  ARG 13  -77 ?   ?   ?   A . n 
A 1 14  PRO 14  -76 ?   ?   ?   A . n 
A 1 15  LEU 15  -75 ?   ?   ?   A . n 
A 1 16  LEU 16  -74 ?   ?   ?   A . n 
A 1 17  PRO 17  -73 ?   ?   ?   A . n 
A 1 18  LEU 18  -72 ?   ?   ?   A . n 
A 1 19  GLN 19  -71 ?   ?   ?   A . n 
A 1 20  PRO 20  -70 ?   ?   ?   A . n 
A 1 21  ARG 21  -69 ?   ?   ?   A . n 
A 1 22  GLY 22  -68 ?   ?   ?   A . n 
A 1 23  CYS 23  -67 ?   ?   ?   A . n 
A 1 24  PRO 24  -66 ?   ?   ?   A . n 
A 1 25  ARG 25  -65 ?   ?   ?   A . n 
A 1 26  GLY 26  -64 ?   ?   ?   A . n 
A 1 27  ASP 27  -63 ?   ?   ?   A . n 
A 1 28  GLY 28  -62 ?   ?   ?   A . n 
A 1 29  CYS 29  -61 ?   ?   ?   A . n 
A 1 30  LEU 30  -60 ?   ?   ?   A . n 
A 1 31  ARG 31  -59 ?   ?   ?   A . n 
A 1 32  GLY 32  -58 ?   ?   ?   A . n 
A 1 33  GLY 33  -57 ?   ?   ?   A . n 
A 1 34  ARG 34  -56 ?   ?   ?   A . n 
A 1 35  GLY 35  -55 ?   ?   ?   A . n 
A 1 36  ARG 36  -54 ?   ?   ?   A . n 
A 1 37  ALA 37  -53 ?   ?   ?   A . n 
A 1 38  GLY 38  -52 ?   ?   ?   A . n 
A 1 39  PHE 39  -51 ?   ?   ?   A . n 
A 1 40  GLY 40  -50 ?   ?   ?   A . n 
A 1 41  PHE 41  -49 ?   ?   ?   A . n 
A 1 42  TRP 42  -48 ?   ?   ?   A . n 
A 1 43  ARG 43  -47 ?   ?   ?   A . n 
A 1 44  VAL 44  -46 ?   ?   ?   A . n 
A 1 45  THR 45  -45 ?   ?   ?   A . n 
A 1 46  GLY 46  -44 ?   ?   ?   A . n 
A 1 47  GLY 47  -43 ?   ?   ?   A . n 
A 1 48  SER 48  -42 ?   ?   ?   A . n 
A 1 49  ARG 49  -41 ?   ?   ?   A . n 
A 1 50  ALA 50  -40 ?   ?   ?   A . n 
A 1 51  SER 51  -39 ?   ?   ?   A . n 
A 1 52  ALA 52  -38 ?   ?   ?   A . n 
A 1 53  ASN 53  -37 ?   ?   ?   A . n 
A 1 54  HIS 54  -36 ?   ?   ?   A . n 
A 1 55  VAL 55  -35 ?   ?   ?   A . n 
A 1 56  HIS 56  -34 ?   ?   ?   A . n 
A 1 57  ALA 57  -33 ?   ?   ?   A . n 
A 1 58  PHE 58  -32 ?   ?   ?   A . n 
A 1 59  PHE 59  -31 ?   ?   ?   A . n 
A 1 60  PHE 60  -30 ?   ?   ?   A . n 
A 1 61  PHE 61  -29 ?   ?   ?   A . n 
A 1 62  LEU 62  -28 ?   ?   ?   A . n 
A 1 63  GLN 63  -27 ?   ?   ?   A . n 
A 1 64  LEU 64  -26 ?   ?   ?   A . n 
A 1 65  LEU 65  -25 ?   ?   ?   A . n 
A 1 66  GLY 66  -24 ?   ?   ?   A . n 
A 1 67  ASN 67  -23 ?   ?   ?   A . n 
A 1 68  VAL 68  -22 ?   ?   ?   A . n 
A 1 69  LEU 69  -21 ?   ?   ?   A . n 
A 1 70  VAL 70  -20 ?   ?   ?   A . n 
A 1 71  ILE 71  -19 ?   ?   ?   A . n 
A 1 72  VAL 72  -18 ?   ?   ?   A . n 
A 1 73  LEU 73  -17 ?   ?   ?   A . n 
A 1 74  SER 74  -16 ?   ?   ?   A . n 
A 1 75  HIS 75  -15 ?   ?   ?   A . n 
A 1 76  HIS 76  -14 ?   ?   ?   A . n 
A 1 77  PHE 77  -13 ?   ?   ?   A . n 
A 1 78  GLY 78  -12 ?   ?   ?   A . n 
A 1 79  LYS 79  -11 ?   ?   ?   A . n 
A 1 80  GLU 80  -10 ?   ?   ?   A . n 
A 1 81  PHE 81  -9  ?   ?   ?   A . n 
A 1 82  ALA 82  -8  ?   ?   ?   A . n 
A 1 83  THR 83  -7  ?   ?   ?   A . n 
A 1 84  MET 84  -6  ?   ?   ?   A . n 
A 1 85  PRO 85  -5  ?   ?   ?   A . n 
A 1 86  MET 86  -4  ?   ?   ?   A . n 
A 1 87  GLY 87  -3  ?   ?   ?   A . n 
A 1 88  SER 88  -2  ?   ?   ?   A . n 
A 1 89  LEU 89  -1  ?   ?   ?   A . n 
A 1 90  GLN 90  0   ?   ?   ?   A . n 
A 1 91  PRO 91  1   ?   ?   ?   A . n 
A 1 92  LEU 92  2   ?   ?   ?   A . n 
A 1 93  ALA 93  3   ?   ?   ?   A . n 
A 1 94  THR 94  4   ?   ?   ?   A . n 
A 1 95  LEU 95  5   ?   ?   ?   A . n 
A 1 96  TYR 96  6   ?   ?   ?   A . n 
A 1 97  LEU 97  7   ?   ?   ?   A . n 
A 1 98  LEU 98  8   ?   ?   ?   A . n 
A 1 99  GLY 99  9   ?   ?   ?   A . n 
A 1 100 MET 100 10  ?   ?   ?   A . n 
A 1 101 LEU 101 11  ?   ?   ?   A . n 
A 1 102 VAL 102 12  ?   ?   ?   A . n 
A 1 103 ALA 103 13  ?   ?   ?   A . n 
A 1 104 SER 104 14  ?   ?   ?   A . n 
A 1 105 VAL 105 15  ?   ?   ?   A . n 
A 1 106 LEU 106 16  ?   ?   ?   A . n 
A 1 107 ALA 107 17  ?   ?   ?   A . n 
A 1 108 GLN 108 18  ?   ?   ?   A . n 
A 1 109 SER 109 19  ?   ?   ?   A . n 
A 1 110 LEU 110 20  20  LEU LEU A . n 
A 1 111 THR 111 21  21  THR THR A . n 
A 1 112 THR 112 22  22  THR THR A . n 
A 1 113 GLU 113 23  23  GLU GLU A . n 
A 1 114 GLU 114 24  24  GLU GLU A . n 
A 1 115 LYS 115 25  25  LYS LYS A . n 
A 1 116 ALA 116 26  26  ALA ALA A . n 
A 1 117 ARG 117 27  27  ARG ARG A . n 
A 1 118 GLU 118 28  28  GLU GLU A . n 
A 1 119 PHE 119 29  29  PHE PHE A . n 
A 1 120 LEU 120 30  30  LEU LEU A . n 
A 1 121 ASP 121 31  31  ASP ASP A . n 
A 1 122 LYS 122 32  32  LYS LYS A . n 
A 1 123 PHE 123 33  33  PHE PHE A . n 
A 1 124 ASN 124 34  34  ASN ASN A . n 
A 1 125 SER 125 35  35  SER SER A . n 
A 1 126 GLU 126 36  36  GLU GLU A . n 
A 1 127 ALA 127 37  37  ALA ALA A . n 
A 1 128 GLU 128 38  38  GLU GLU A . n 
A 1 129 ASN 129 39  39  ASN ASN A . n 
A 1 130 TRP 130 40  40  TRP TRP A . n 
A 1 131 SER 131 41  41  SER SER A . n 
A 1 132 HIS 132 42  42  HIS HIS A . n 
A 1 133 GLU 133 43  43  GLU GLU A . n 
A 1 134 SER 134 44  44  SER SER A . n 
A 1 135 ALA 135 45  45  ALA ALA A . n 
A 1 136 LEU 136 46  46  LEU LEU A . n 
A 1 137 ALA 137 47  47  ALA ALA A . n 
A 1 138 SER 138 48  48  SER SER A . n 
A 1 139 TRP 139 49  49  TRP TRP A . n 
A 1 140 ASP 140 50  50  ASP ASP A . n 
A 1 141 TYR 141 51  51  TYR TYR A . n 
A 1 142 ASN 142 52  52  ASN ASN A . n 
A 1 143 THR 143 53  53  THR THR A . n 
A 1 144 ASN 144 54  54  ASN ASN A . n 
A 1 145 ILE 145 55  55  ILE ILE A . n 
A 1 146 ASN 146 56  56  ASN ASN A . n 
A 1 147 ASP 147 57  57  ASP ASP A . n 
A 1 148 LYS 148 58  58  LYS LYS A . n 
A 1 149 ASN 149 59  59  ASN ASN A . n 
A 1 150 ALA 150 60  60  ALA ALA A . n 
A 1 151 GLN 151 61  61  GLN GLN A . n 
A 1 152 LYS 152 62  62  LYS LYS A . n 
A 1 153 MET 153 63  63  MET MET A . n 
A 1 154 ASN 154 64  64  ASN ASN A . n 
A 1 155 GLU 155 65  65  GLU GLU A . n 
A 1 156 ALA 156 66  66  ALA ALA A . n 
A 1 157 ASP 157 67  67  ASP ASP A . n 
A 1 158 SER 158 68  68  SER SER A . n 
A 1 159 LYS 159 69  69  LYS LYS A . n 
A 1 160 TRP 160 70  70  TRP TRP A . n 
A 1 161 SER 161 71  71  SER SER A . n 
A 1 162 ALA 162 72  72  ALA ALA A . n 
A 1 163 PHE 163 73  73  PHE PHE A . n 
A 1 164 TYR 164 74  74  TYR TYR A . n 
A 1 165 LYS 165 75  75  LYS LYS A . n 
A 1 166 GLU 166 76  76  GLU GLU A . n 
A 1 167 HIS 167 77  77  HIS HIS A . n 
A 1 168 SER 168 78  78  SER SER A . n 
A 1 169 LYS 169 79  79  LYS LYS A . n 
A 1 170 LEU 170 80  80  LEU LEU A . n 
A 1 171 ALA 171 81  81  ALA ALA A . n 
A 1 172 GLN 172 82  82  GLN GLN A . n 
A 1 173 GLY 173 83  83  GLY GLY A . n 
A 1 174 PHE 174 84  84  PHE PHE A . n 
A 1 175 PRO 175 85  85  PRO PRO A . n 
A 1 176 LEU 176 86  86  LEU LEU A . n 
A 1 177 GLN 177 87  87  GLN GLN A . n 
A 1 178 GLU 178 88  88  GLU GLU A . n 
A 1 179 ILE 179 89  89  ILE ILE A . n 
A 1 180 GLN 180 90  90  GLN GLN A . n 
A 1 181 ASN 181 91  91  ASN ASN A . n 
A 1 182 SER 182 92  92  SER SER A . n 
A 1 183 THR 183 93  93  THR THR A . n 
A 1 184 ILE 184 94  94  ILE ILE A . n 
A 1 185 LYS 185 95  95  LYS LYS A . n 
A 1 186 LEU 186 96  96  LEU LEU A . n 
A 1 187 GLN 187 97  97  GLN GLN A . n 
A 1 188 LEU 188 98  98  LEU LEU A . n 
A 1 189 GLN 189 99  99  GLN GLN A . n 
A 1 190 ILE 190 100 100 ILE ILE A . n 
A 1 191 LEU 191 101 101 LEU LEU A . n 
A 1 192 GLN 192 102 102 GLN GLN A . n 
A 1 193 GLN 193 103 103 GLN GLN A . n 
A 1 194 ASN 194 104 104 ASN ASN A . n 
A 1 195 GLY 195 105 105 GLY GLY A . n 
A 1 196 SER 196 106 106 SER SER A . n 
A 1 197 SER 197 107 107 SER SER A . n 
A 1 198 VAL 198 108 108 VAL VAL A . n 
A 1 199 LEU 199 109 109 LEU LEU A . n 
A 1 200 THR 200 110 110 THR THR A . n 
A 1 201 ALA 201 111 111 ALA ALA A . n 
A 1 202 GLU 202 112 112 GLU GLU A . n 
A 1 203 LYS 203 113 113 LYS LYS A . n 
A 1 204 SER 204 114 114 SER SER A . n 
A 1 205 LYS 205 115 115 LYS LYS A . n 
A 1 206 ARG 206 116 116 ARG ARG A . n 
A 1 207 LEU 207 117 117 LEU LEU A . n 
A 1 208 SER 208 118 118 SER SER A . n 
A 1 209 THR 209 119 119 THR THR A . n 
A 1 210 ILE 210 120 120 ILE ILE A . n 
A 1 211 LEU 211 121 121 LEU LEU A . n 
A 1 212 THR 212 122 122 THR THR A . n 
A 1 213 THR 213 123 123 THR THR A . n 
A 1 214 MET 214 124 124 MET MET A . n 
A 1 215 SER 215 125 125 SER SER A . n 
A 1 216 THR 216 126 126 THR THR A . n 
A 1 217 ILE 217 127 127 ILE ILE A . n 
A 1 218 TYR 218 128 128 TYR TYR A . n 
A 1 219 SER 219 129 129 SER SER A . n 
A 1 220 THR 220 130 130 THR THR A . n 
A 1 221 GLY 221 131 131 GLY GLY A . n 
A 1 222 LYS 222 132 132 LYS LYS A . n 
A 1 223 VAL 223 133 133 VAL VAL A . n 
A 1 224 CYS 224 134 134 CYS CYS A . n 
A 1 225 ASN 225 135 135 ASN ASN A . n 
A 1 226 PRO 226 136 136 PRO PRO A . n 
A 1 227 ASN 227 137 137 ASN ASN A . n 
A 1 228 ASN 228 138 138 ASN ASN A . n 
A 1 229 PRO 229 139 139 PRO PRO A . n 
A 1 230 GLN 230 140 140 GLN GLN A . n 
A 1 231 GLN 231 141 141 GLN GLN A . n 
A 1 232 CYS 232 142 142 CYS CYS A . n 
A 1 233 PHE 233 143 143 PHE PHE A . n 
A 1 234 THR 234 144 144 THR THR A . n 
A 1 235 LEU 235 145 145 LEU LEU A . n 
A 1 236 SER 236 146 146 SER SER A . n 
A 1 237 GLY 237 147 147 GLY GLY A . n 
A 1 238 LEU 238 148 148 LEU LEU A . n 
A 1 239 GLU 239 149 149 GLU GLU A . n 
A 1 240 ASP 240 150 150 ASP ASP A . n 
A 1 241 ILE 241 151 151 ILE ILE A . n 
A 1 242 MET 242 152 152 MET MET A . n 
A 1 243 GLU 243 153 153 GLU GLU A . n 
A 1 244 LYS 244 154 154 LYS LYS A . n 
A 1 245 SER 245 155 155 SER SER A . n 
A 1 246 LYS 246 156 156 LYS LYS A . n 
A 1 247 ASP 247 157 157 ASP ASP A . n 
A 1 248 TYR 248 158 158 TYR TYR A . n 
A 1 249 HIS 249 159 159 HIS HIS A . n 
A 1 250 GLN 250 160 160 GLN GLN A . n 
A 1 251 ARG 251 161 161 ARG ARG A . n 
A 1 252 LEU 252 162 162 LEU LEU A . n 
A 1 253 TRP 253 163 163 TRP TRP A . n 
A 1 254 ILE 254 164 164 ILE ILE A . n 
A 1 255 TRP 255 165 165 TRP TRP A . n 
A 1 256 GLU 256 166 166 GLU GLU A . n 
A 1 257 GLY 257 167 167 GLY GLY A . n 
A 1 258 TRP 258 168 168 TRP TRP A . n 
A 1 259 ARG 259 169 169 ARG ARG A . n 
A 1 260 SER 260 170 170 SER SER A . n 
A 1 261 GLU 261 171 171 GLU GLU A . n 
A 1 262 VAL 262 172 172 VAL VAL A . n 
A 1 263 GLY 263 173 173 GLY GLY A . n 
A 1 264 LYS 264 174 174 LYS LYS A . n 
A 1 265 GLN 265 175 175 GLN GLN A . n 
A 1 266 LEU 266 176 176 LEU LEU A . n 
A 1 267 ARG 267 177 177 ARG ARG A . n 
A 1 268 PRO 268 178 178 PRO PRO A . n 
A 1 269 LEU 269 179 179 LEU LEU A . n 
A 1 270 TYR 270 180 180 TYR TYR A . n 
A 1 271 GLU 271 181 181 GLU GLU A . n 
A 1 272 GLU 272 182 182 GLU GLU A . n 
A 1 273 TYR 273 183 183 TYR TYR A . n 
A 1 274 VAL 274 184 184 VAL VAL A . n 
A 1 275 ALA 275 185 185 ALA ALA A . n 
A 1 276 LEU 276 186 186 LEU LEU A . n 
A 1 277 LYS 277 187 187 LYS LYS A . n 
A 1 278 ASN 278 188 188 ASN ASN A . n 
A 1 279 GLU 279 189 189 GLU GLU A . n 
A 1 280 MET 280 190 190 MET MET A . n 
A 1 281 ALA 281 191 191 ALA ALA A . n 
A 1 282 ARG 282 192 192 ARG ARG A . n 
A 1 283 GLY 283 193 193 GLY GLY A . n 
A 1 284 ASN 284 194 194 ASN ASN A . n 
A 1 285 ASN 285 195 195 ASN ASN A . n 
A 1 286 TYR 286 196 196 TYR TYR A . n 
A 1 287 LYS 287 197 197 LYS LYS A . n 
A 1 288 ASP 288 198 198 ASP ASP A . n 
A 1 289 TYR 289 199 199 TYR TYR A . n 
A 1 290 GLY 290 200 200 GLY GLY A . n 
A 1 291 ASP 291 201 201 ASP ASP A . n 
A 1 292 TYR 292 202 202 TYR TYR A . n 
A 1 293 TRP 293 203 203 TRP TRP A . n 
A 1 294 ARG 294 204 204 ARG ARG A . n 
A 1 295 GLY 295 205 205 GLY GLY A . n 
A 1 296 ASP 296 206 206 ASP ASP A . n 
A 1 297 TYR 297 207 207 TYR TYR A . n 
A 1 298 GLU 298 208 208 GLU GLU A . n 
A 1 299 THR 299 209 209 THR THR A . n 
A 1 300 GLU 300 210 210 GLU GLU A . n 
A 1 301 GLY 301 211 211 GLY GLY A . n 
A 1 302 GLY 302 212 212 GLY GLY A . n 
A 1 303 ASP 303 213 213 ASP ASP A . n 
A 1 304 GLY 304 214 214 GLY GLY A . n 
A 1 305 TYR 305 215 215 TYR TYR A . n 
A 1 306 ASN 306 216 216 ASN ASN A . n 
A 1 307 TYR 307 217 217 TYR TYR A . n 
A 1 308 SER 308 218 218 SER SER A . n 
A 1 309 ARG 309 219 219 ARG ARG A . n 
A 1 310 ASN 310 220 220 ASN ASN A . n 
A 1 311 HIS 311 221 221 HIS HIS A . n 
A 1 312 LEU 312 222 222 LEU LEU A . n 
A 1 313 ILE 313 223 223 ILE ILE A . n 
A 1 314 GLU 314 224 224 GLU GLU A . n 
A 1 315 ASP 315 225 225 ASP ASP A . n 
A 1 316 VAL 316 226 226 VAL VAL A . n 
A 1 317 ASP 317 227 227 ASP ASP A . n 
A 1 318 ARG 318 228 228 ARG ARG A . n 
A 1 319 ILE 319 229 229 ILE ILE A . n 
A 1 320 PHE 320 230 230 PHE PHE A . n 
A 1 321 LEU 321 231 231 LEU LEU A . n 
A 1 322 GLU 322 232 232 GLU GLU A . n 
A 1 323 ILE 323 233 233 ILE ILE A . n 
A 1 324 LYS 324 234 234 LYS LYS A . n 
A 1 325 PRO 325 235 235 PRO PRO A . n 
A 1 326 LEU 326 236 236 LEU LEU A . n 
A 1 327 TYR 327 237 237 TYR TYR A . n 
A 1 328 GLU 328 238 238 GLU GLU A . n 
A 1 329 GLN 329 239 239 GLN GLN A . n 
A 1 330 LEU 330 240 240 LEU LEU A . n 
A 1 331 HIS 331 241 241 HIS HIS A . n 
A 1 332 ALA 332 242 242 ALA ALA A . n 
A 1 333 TYR 333 243 243 TYR TYR A . n 
A 1 334 VAL 334 244 244 VAL VAL A . n 
A 1 335 ARG 335 245 245 ARG ARG A . n 
A 1 336 ALA 336 246 246 ALA ALA A . n 
A 1 337 LYS 337 247 247 LYS LYS A . n 
A 1 338 LEU 338 248 248 LEU LEU A . n 
A 1 339 MET 339 249 249 MET MET A . n 
A 1 340 ASN 340 250 250 ASN ASN A . n 
A 1 341 ALA 341 251 251 ALA ALA A . n 
A 1 342 TYR 342 252 252 TYR TYR A . n 
A 1 343 PRO 343 253 253 PRO PRO A . n 
A 1 344 SER 344 254 254 SER SER A . n 
A 1 345 ARG 345 255 255 ARG ARG A . n 
A 1 346 ILE 346 256 256 ILE ILE A . n 
A 1 347 SER 347 257 257 SER SER A . n 
A 1 348 PRO 348 258 258 PRO PRO A . n 
A 1 349 THR 349 259 259 THR THR A . n 
A 1 350 GLY 350 260 260 GLY GLY A . n 
A 1 351 CYS 351 261 261 CYS CYS A . n 
A 1 352 LEU 352 262 262 LEU LEU A . n 
A 1 353 PRO 353 263 263 PRO PRO A . n 
A 1 354 ALA 354 264 264 ALA ALA A . n 
A 1 355 HIS 355 265 265 HIS HIS A . n 
A 1 356 LEU 356 266 266 LEU LEU A . n 
A 1 357 LEU 357 267 267 LEU LEU A . n 
A 1 358 GLY 358 268 268 GLY GLY A . n 
A 1 359 ASP 359 269 269 ASP ASP A . n 
A 1 360 MET 360 270 270 MET MET A . n 
A 1 361 TRP 361 271 271 TRP TRP A . n 
A 1 362 GLY 362 272 272 GLY GLY A . n 
A 1 363 ARG 363 273 273 ARG ARG A . n 
A 1 364 PHE 364 274 274 PHE PHE A . n 
A 1 365 TRP 365 275 275 TRP TRP A . n 
A 1 366 THR 366 276 276 THR THR A . n 
A 1 367 ASN 367 277 277 ASN ASN A . n 
A 1 368 LEU 368 278 278 LEU LEU A . n 
A 1 369 TYR 369 279 279 TYR TYR A . n 
A 1 370 ASN 370 280 280 ASN ASN A . n 
A 1 371 LEU 371 281 281 LEU LEU A . n 
A 1 372 THR 372 282 282 THR THR A . n 
A 1 373 VAL 373 283 283 VAL VAL A . n 
A 1 374 PRO 374 284 284 PRO PRO A . n 
A 1 375 PHE 375 285 285 PHE PHE A . n 
A 1 376 GLU 376 286 286 GLU GLU A . n 
A 1 377 LYS 377 287 287 LYS LYS A . n 
A 1 378 LYS 378 288 288 LYS LYS A . n 
A 1 379 GLN 379 289 289 GLN GLN A . n 
A 1 380 ASN 380 290 290 ASN ASN A . n 
A 1 381 ILE 381 291 291 ILE ILE A . n 
A 1 382 ASP 382 292 292 ASP ASP A . n 
A 1 383 VAL 383 293 293 VAL VAL A . n 
A 1 384 THR 384 294 294 THR THR A . n 
A 1 385 ASP 385 295 295 ASP ASP A . n 
A 1 386 THR 386 296 296 THR THR A . n 
A 1 387 MET 387 297 297 MET MET A . n 
A 1 388 LYS 388 298 298 LYS LYS A . n 
A 1 389 LYS 389 299 299 LYS LYS A . n 
A 1 390 GLN 390 300 300 GLN GLN A . n 
A 1 391 SER 391 301 301 SER SER A . n 
A 1 392 TRP 392 302 302 TRP TRP A . n 
A 1 393 ASP 393 303 303 ASP ASP A . n 
A 1 394 ALA 394 304 304 ALA ALA A . n 
A 1 395 GLU 395 305 305 GLU GLU A . n 
A 1 396 LYS 396 306 306 LYS LYS A . n 
A 1 397 ILE 397 307 307 ILE ILE A . n 
A 1 398 PHE 398 308 308 PHE PHE A . n 
A 1 399 LYS 399 309 309 LYS LYS A . n 
A 1 400 GLU 400 310 310 GLU GLU A . n 
A 1 401 ALA 401 311 311 ALA ALA A . n 
A 1 402 GLU 402 312 312 GLU GLU A . n 
A 1 403 LYS 403 313 313 LYS LYS A . n 
A 1 404 PHE 404 314 314 PHE PHE A . n 
A 1 405 TYR 405 315 315 TYR TYR A . n 
A 1 406 LEU 406 316 316 LEU LEU A . n 
A 1 407 SER 407 317 317 SER SER A . n 
A 1 408 VAL 408 318 318 VAL VAL A . n 
A 1 409 GLY 409 319 319 GLY GLY A . n 
A 1 410 LEU 410 320 320 LEU LEU A . n 
A 1 411 HIS 411 321 321 HIS HIS A . n 
A 1 412 ASN 412 322 322 ASN ASN A . n 
A 1 413 MET 413 323 323 MET MET A . n 
A 1 414 THR 414 324 324 THR THR A . n 
A 1 415 PRO 415 325 325 PRO PRO A . n 
A 1 416 GLU 416 326 326 GLU GLU A . n 
A 1 417 PHE 417 327 327 PHE PHE A . n 
A 1 418 TRP 418 328 328 TRP TRP A . n 
A 1 419 ASN 419 329 329 ASN ASN A . n 
A 1 420 ASN 420 330 330 ASN ASN A . n 
A 1 421 SER 421 331 331 SER SER A . n 
A 1 422 MET 422 332 332 MET MET A . n 
A 1 423 LEU 423 333 333 LEU LEU A . n 
A 1 424 THR 424 334 334 THR THR A . n 
A 1 425 GLU 425 335 335 GLU GLU A . n 
A 1 426 PRO 426 336 336 PRO PRO A . n 
A 1 427 SER 427 337 337 SER SER A . n 
A 1 428 ASP 428 338 338 ASP ASP A . n 
A 1 429 GLY 429 339 339 GLY GLY A . n 
A 1 430 ARG 430 340 340 ARG ARG A . n 
A 1 431 GLN 431 341 341 GLN GLN A . n 
A 1 432 VAL 432 342 342 VAL VAL A . n 
A 1 433 VAL 433 343 343 VAL VAL A . n 
A 1 434 CYS 434 344 344 CYS CYS A . n 
A 1 435 HIS 435 345 345 HIS HIS A . n 
A 1 436 PRO 436 346 346 PRO PRO A . n 
A 1 437 THR 437 347 347 THR THR A . n 
A 1 438 ALA 438 348 348 ALA ALA A . n 
A 1 439 TRP 439 349 349 TRP TRP A . n 
A 1 440 ASP 440 350 350 ASP ASP A . n 
A 1 441 LEU 441 351 351 LEU LEU A . n 
A 1 442 GLY 442 352 352 GLY GLY A . n 
A 1 443 LYS 443 353 353 LYS LYS A . n 
A 1 444 ASN 444 354 354 ASN ASN A . n 
A 1 445 ASP 445 355 355 ASP ASP A . n 
A 1 446 PHE 446 356 356 PHE PHE A . n 
A 1 447 ARG 447 357 357 ARG ARG A . n 
A 1 448 ILE 448 358 358 ILE ILE A . n 
A 1 449 LYS 449 359 359 LYS LYS A . n 
A 1 450 MET 450 360 360 MET MET A . n 
A 1 451 CYS 451 361 361 CYS CYS A . n 
A 1 452 THR 452 362 362 THR THR A . n 
A 1 453 LYS 453 363 363 LYS LYS A . n 
A 1 454 VAL 454 364 364 VAL VAL A . n 
A 1 455 THR 455 365 365 THR THR A . n 
A 1 456 MET 456 366 366 MET MET A . n 
A 1 457 ASP 457 367 367 ASP ASP A . n 
A 1 458 ASP 458 368 368 ASP ASP A . n 
A 1 459 PHE 459 369 369 PHE PHE A . n 
A 1 460 LEU 460 370 370 LEU LEU A . n 
A 1 461 THR 461 371 371 THR THR A . n 
A 1 462 ALA 462 372 372 ALA ALA A . n 
A 1 463 HIS 463 373 373 HIS HIS A . n 
A 1 464 HIS 464 374 374 HIS HIS A . n 
A 1 465 GLU 465 375 375 GLU GLU A . n 
A 1 466 MET 466 376 376 MET MET A . n 
A 1 467 GLY 467 377 377 GLY GLY A . n 
A 1 468 HIS 468 378 378 HIS HIS A . n 
A 1 469 ILE 469 379 379 ILE ILE A . n 
A 1 470 GLN 470 380 380 GLN GLN A . n 
A 1 471 TYR 471 381 381 TYR TYR A . n 
A 1 472 ASP 472 382 382 ASP ASP A . n 
A 1 473 MET 473 383 383 MET MET A . n 
A 1 474 ALA 474 384 384 ALA ALA A . n 
A 1 475 TYR 475 385 385 TYR TYR A . n 
A 1 476 ALA 476 386 386 ALA ALA A . n 
A 1 477 LYS 477 387 387 LYS LYS A . n 
A 1 478 GLN 478 388 388 GLN GLN A . n 
A 1 479 PRO 479 389 389 PRO PRO A . n 
A 1 480 TYR 480 390 390 TYR TYR A . n 
A 1 481 LEU 481 391 391 LEU LEU A . n 
A 1 482 LEU 482 392 392 LEU LEU A . n 
A 1 483 ARG 483 393 393 ARG ARG A . n 
A 1 484 ASN 484 394 394 ASN ASN A . n 
A 1 485 GLY 485 395 395 GLY GLY A . n 
A 1 486 ALA 486 396 396 ALA ALA A . n 
A 1 487 ASN 487 397 397 ASN ASN A . n 
A 1 488 GLU 488 398 398 GLU GLU A . n 
A 1 489 GLY 489 399 399 GLY GLY A . n 
A 1 490 PHE 490 400 400 PHE PHE A . n 
A 1 491 HIS 491 401 401 HIS HIS A . n 
A 1 492 GLU 492 402 402 GLU GLU A . n 
A 1 493 ALA 493 403 403 ALA ALA A . n 
A 1 494 VAL 494 404 404 VAL VAL A . n 
A 1 495 GLY 495 405 405 GLY GLY A . n 
A 1 496 GLU 496 406 406 GLU GLU A . n 
A 1 497 ILE 497 407 407 ILE ILE A . n 
A 1 498 MET 498 408 408 MET MET A . n 
A 1 499 SER 499 409 409 SER SER A . n 
A 1 500 LEU 500 410 410 LEU LEU A . n 
A 1 501 SER 501 411 411 SER SER A . n 
A 1 502 ALA 502 412 412 ALA ALA A . n 
A 1 503 ALA 503 413 413 ALA ALA A . n 
A 1 504 THR 504 414 414 THR THR A . n 
A 1 505 PRO 505 415 415 PRO PRO A . n 
A 1 506 LYS 506 416 416 LYS LYS A . n 
A 1 507 HIS 507 417 417 HIS HIS A . n 
A 1 508 LEU 508 418 418 LEU LEU A . n 
A 1 509 LYS 509 419 419 LYS LYS A . n 
A 1 510 ASP 510 420 420 ASP ASP A . n 
A 1 511 LEU 511 421 421 LEU LEU A . n 
A 1 512 GLY 512 422 422 GLY GLY A . n 
A 1 513 LEU 513 423 423 LEU LEU A . n 
A 1 514 LEU 514 424 424 LEU LEU A . n 
A 1 515 ALA 515 425 425 ALA ALA A . n 
A 1 516 GLN 516 426 426 GLN GLN A . n 
A 1 517 ASN 517 427 427 ASN ASN A . n 
A 1 518 TYR 518 428 428 TYR TYR A . n 
A 1 519 PRO 519 429 429 PRO PRO A . n 
A 1 520 GLU 520 430 430 GLU GLU A . n 
A 1 521 ASP 521 431 431 ASP ASP A . n 
A 1 522 TYR 522 432 432 TYR TYR A . n 
A 1 523 GLU 523 433 433 GLU GLU A . n 
A 1 524 THR 524 434 434 THR THR A . n 
A 1 525 GLU 525 435 435 GLU GLU A . n 
A 1 526 ILE 526 436 436 ILE ILE A . n 
A 1 527 ASN 527 437 437 ASN ASN A . n 
A 1 528 PHE 528 438 438 PHE PHE A . n 
A 1 529 LEU 529 439 439 LEU LEU A . n 
A 1 530 LEU 530 440 440 LEU LEU A . n 
A 1 531 LYS 531 441 441 LYS LYS A . n 
A 1 532 GLN 532 442 442 GLN GLN A . n 
A 1 533 ALA 533 443 443 ALA ALA A . n 
A 1 534 LEU 534 444 444 LEU LEU A . n 
A 1 535 ASN 535 445 445 ASN ASN A . n 
A 1 536 ILE 536 446 446 ILE ILE A . n 
A 1 537 VAL 537 447 447 VAL VAL A . n 
A 1 538 GLY 538 448 448 GLY GLY A . n 
A 1 539 THR 539 449 449 THR THR A . n 
A 1 540 LEU 540 450 450 LEU LEU A . n 
A 1 541 PRO 541 451 451 PRO PRO A . n 
A 1 542 PHE 542 452 452 PHE PHE A . n 
A 1 543 THR 543 453 453 THR THR A . n 
A 1 544 TYR 544 454 454 TYR TYR A . n 
A 1 545 MET 545 455 455 MET MET A . n 
A 1 546 LEU 546 456 456 LEU LEU A . n 
A 1 547 GLU 547 457 457 GLU GLU A . n 
A 1 548 LYS 548 458 458 LYS LYS A . n 
A 1 549 TRP 549 459 459 TRP TRP A . n 
A 1 550 ARG 550 460 460 ARG ARG A . n 
A 1 551 TRP 551 461 461 TRP TRP A . n 
A 1 552 MET 552 462 462 MET MET A . n 
A 1 553 VAL 553 463 463 VAL VAL A . n 
A 1 554 PHE 554 464 464 PHE PHE A . n 
A 1 555 GLU 555 465 465 GLU GLU A . n 
A 1 556 GLY 556 466 466 GLY GLY A . n 
A 1 557 LYS 557 467 467 LYS LYS A . n 
A 1 558 ILE 558 468 468 ILE ILE A . n 
A 1 559 PRO 559 469 469 PRO PRO A . n 
A 1 560 LYS 560 470 470 LYS LYS A . n 
A 1 561 GLU 561 471 471 GLU GLU A . n 
A 1 562 GLN 562 472 472 GLN GLN A . n 
A 1 563 TRP 563 473 473 TRP TRP A . n 
A 1 564 MET 564 474 474 MET MET A . n 
A 1 565 GLU 565 475 475 GLU GLU A . n 
A 1 566 LYS 566 476 476 LYS LYS A . n 
A 1 567 TRP 567 477 477 TRP TRP A . n 
A 1 568 TRP 568 478 478 TRP TRP A . n 
A 1 569 GLU 569 479 479 GLU GLU A . n 
A 1 570 MET 570 480 480 MET MET A . n 
A 1 571 LYS 571 481 481 LYS LYS A . n 
A 1 572 ARG 572 482 482 ARG ARG A . n 
A 1 573 GLU 573 483 483 GLU GLU A . n 
A 1 574 ILE 574 484 484 ILE ILE A . n 
A 1 575 VAL 575 485 485 VAL VAL A . n 
A 1 576 GLY 576 486 486 GLY GLY A . n 
A 1 577 VAL 577 487 487 VAL VAL A . n 
A 1 578 VAL 578 488 488 VAL VAL A . n 
A 1 579 GLU 579 489 489 GLU GLU A . n 
A 1 580 PRO 580 490 490 PRO PRO A . n 
A 1 581 LEU 581 491 491 LEU LEU A . n 
A 1 582 PRO 582 492 492 PRO PRO A . n 
A 1 583 HIS 583 493 493 HIS HIS A . n 
A 1 584 ASP 584 494 494 ASP ASP A . n 
A 1 585 GLU 585 495 495 GLU GLU A . n 
A 1 586 THR 586 496 496 THR THR A . n 
A 1 587 TYR 587 497 497 TYR TYR A . n 
A 1 588 CYS 588 498 498 CYS CYS A . n 
A 1 589 ASP 589 499 499 ASP ASP A . n 
A 1 590 PRO 590 500 500 PRO PRO A . n 
A 1 591 ALA 591 501 501 ALA ALA A . n 
A 1 592 SER 592 502 502 SER SER A . n 
A 1 593 LEU 593 503 503 LEU LEU A . n 
A 1 594 PHE 594 504 504 PHE PHE A . n 
A 1 595 HIS 595 505 505 HIS HIS A . n 
A 1 596 VAL 596 506 506 VAL VAL A . n 
A 1 597 ALA 597 507 507 ALA ALA A . n 
A 1 598 ASN 598 508 508 ASN ASN A . n 
A 1 599 ASP 599 509 509 ASP ASP A . n 
A 1 600 TYR 600 510 510 TYR TYR A . n 
A 1 601 SER 601 511 511 SER SER A . n 
A 1 602 PHE 602 512 512 PHE PHE A . n 
A 1 603 ILE 603 513 513 ILE ILE A . n 
A 1 604 ARG 604 514 514 ARG ARG A . n 
A 1 605 TYR 605 515 515 TYR TYR A . n 
A 1 606 PHE 606 516 516 PHE PHE A . n 
A 1 607 THR 607 517 517 THR THR A . n 
A 1 608 ARG 608 518 518 ARG ARG A . n 
A 1 609 THR 609 519 519 THR THR A . n 
A 1 610 ILE 610 520 520 ILE ILE A . n 
A 1 611 LEU 611 521 521 LEU LEU A . n 
A 1 612 GLU 612 522 522 GLU GLU A . n 
A 1 613 PHE 613 523 523 PHE PHE A . n 
A 1 614 GLN 614 524 524 GLN GLN A . n 
A 1 615 PHE 615 525 525 PHE PHE A . n 
A 1 616 GLN 616 526 526 GLN GLN A . n 
A 1 617 GLU 617 527 527 GLU GLU A . n 
A 1 618 ALA 618 528 528 ALA ALA A . n 
A 1 619 LEU 619 529 529 LEU LEU A . n 
A 1 620 CYS 620 530 530 CYS CYS A . n 
A 1 621 GLN 621 531 531 GLN GLN A . n 
A 1 622 ILE 622 532 532 ILE ILE A . n 
A 1 623 ALA 623 533 533 ALA ALA A . n 
A 1 624 ASN 624 534 534 ASN ASN A . n 
A 1 625 HIS 625 535 535 HIS HIS A . n 
A 1 626 THR 626 536 536 THR THR A . n 
A 1 627 GLY 627 537 537 GLY GLY A . n 
A 1 628 PRO 628 538 538 PRO PRO A . n 
A 1 629 LEU 629 539 539 LEU LEU A . n 
A 1 630 HIS 630 540 540 HIS HIS A . n 
A 1 631 LYS 631 541 541 LYS LYS A . n 
A 1 632 CYS 632 542 542 CYS CYS A . n 
A 1 633 ASP 633 543 543 ASP ASP A . n 
A 1 634 ILE 634 544 544 ILE ILE A . n 
A 1 635 SER 635 545 545 SER SER A . n 
A 1 636 ASN 636 546 546 ASN ASN A . n 
A 1 637 SER 637 547 547 SER SER A . n 
A 1 638 THR 638 548 548 THR THR A . n 
A 1 639 GLU 639 549 549 GLU GLU A . n 
A 1 640 ALA 640 550 550 ALA ALA A . n 
A 1 641 GLY 641 551 551 GLY GLY A . n 
A 1 642 LYS 642 552 552 LYS LYS A . n 
A 1 643 GLN 643 553 553 GLN GLN A . n 
A 1 644 LEU 644 554 554 LEU LEU A . n 
A 1 645 LYS 645 555 555 LYS LYS A . n 
A 1 646 ASN 646 556 556 ASN ASN A . n 
A 1 647 MET 647 557 557 MET MET A . n 
A 1 648 LEU 648 558 558 LEU LEU A . n 
A 1 649 GLU 649 559 559 GLU GLU A . n 
A 1 650 LEU 650 560 560 LEU LEU A . n 
A 1 651 GLY 651 561 561 GLY GLY A . n 
A 1 652 LYS 652 562 562 LYS LYS A . n 
A 1 653 SER 653 563 563 SER SER A . n 
A 1 654 LYS 654 564 564 LYS LYS A . n 
A 1 655 PRO 655 565 565 PRO PRO A . n 
A 1 656 TRP 656 566 566 TRP TRP A . n 
A 1 657 THR 657 567 567 THR THR A . n 
A 1 658 PHE 658 568 568 PHE PHE A . n 
A 1 659 ALA 659 569 569 ALA ALA A . n 
A 1 660 LEU 660 570 570 LEU LEU A . n 
A 1 661 GLU 661 571 571 GLU GLU A . n 
A 1 662 GLN 662 572 572 GLN GLN A . n 
A 1 663 ILE 663 573 573 ILE ILE A . n 
A 1 664 ALA 664 574 574 ALA ALA A . n 
A 1 665 ARG 665 575 575 ARG ARG A . n 
A 1 666 THR 666 576 576 THR THR A . n 
A 1 667 LYS 667 577 577 LYS LYS A . n 
A 1 668 GLU 668 578 578 GLU GLU A . n 
A 1 669 MET 669 579 579 MET MET A . n 
A 1 670 ASP 670 580 580 ASP ASP A . n 
A 1 671 ALA 671 581 581 ALA ALA A . n 
A 1 672 LYS 672 582 582 LYS LYS A . n 
A 1 673 PRO 673 583 583 PRO PRO A . n 
A 1 674 LEU 674 584 584 LEU LEU A . n 
A 1 675 LEU 675 585 585 LEU LEU A . n 
A 1 676 ASN 676 586 586 ASN ASN A . n 
A 1 677 TYR 677 587 587 TYR TYR A . n 
A 1 678 PHE 678 588 588 PHE PHE A . n 
A 1 679 LYS 679 589 589 LYS LYS A . n 
A 1 680 PRO 680 590 590 PRO PRO A . n 
A 1 681 LEU 681 591 591 LEU LEU A . n 
A 1 682 PHE 682 592 592 PHE PHE A . n 
A 1 683 SER 683 593 593 SER SER A . n 
A 1 684 TRP 684 594 594 TRP TRP A . n 
A 1 685 LEU 685 595 595 LEU LEU A . n 
A 1 686 LYS 686 596 596 LYS LYS A . n 
A 1 687 GLU 687 597 597 GLU GLU A . n 
A 1 688 LEU 688 598 598 LEU LEU A . n 
A 1 689 ASN 689 599 599 ASN ASN A . n 
A 1 690 GLY 690 600 600 GLY GLY A . n 
A 1 691 ASN 691 601 601 ASN ASN A . n 
A 1 692 SER 692 602 602 SER SER A . n 
A 1 693 VAL 693 603 603 VAL VAL A . n 
A 1 694 GLY 694 604 604 GLY GLY A . n 
A 1 695 TRP 695 605 605 TRP TRP A . n 
A 1 696 SER 696 606 606 SER SER A . n 
A 1 697 ALA 697 607 607 ALA ALA A . n 
A 1 698 ASP 698 608 608 ASP ASP A . n 
A 1 699 TRP 699 609 609 TRP TRP A . n 
A 1 700 SER 700 610 610 SER SER A . n 
A 1 701 PRO 701 611 611 PRO PRO A . n 
A 1 702 TYR 702 612 612 TYR TYR A . n 
A 1 703 SER 703 613 613 SER SER A . n 
A 1 704 GLU 704 614 614 GLU GLU A . n 
A 1 705 GLN 705 615 615 GLN GLN A . n 
A 1 706 SER 706 616 616 SER SER A . n 
A 1 707 ILE 707 617 617 ILE ILE A . n 
A 1 708 LYS 708 618 618 LYS LYS A . n 
A 1 709 VAL 709 619 619 VAL VAL A . n 
A 1 710 ARG 710 620 620 ARG ARG A . n 
A 1 711 ILE 711 621 621 ILE ILE A . n 
A 1 712 SER 712 622 622 SER SER A . n 
A 1 713 LEU 713 623 623 LEU LEU A . n 
A 1 714 LYS 714 624 624 LYS LYS A . n 
A 1 715 SER 715 625 625 SER SER A . n 
A 1 716 ALA 716 626 626 ALA ALA A . n 
A 1 717 LEU 717 627 627 LEU LEU A . n 
A 1 718 GLY 718 628 628 GLY GLY A . n 
A 1 719 GLU 719 629 629 GLU GLU A . n 
A 1 720 LYS 720 630 630 LYS LYS A . n 
A 1 721 ALA 721 631 631 ALA ALA A . n 
A 1 722 TYR 722 632 632 TYR TYR A . n 
A 1 723 GLU 723 633 633 GLU GLU A . n 
A 1 724 TRP 724 634 634 TRP TRP A . n 
A 1 725 ASN 725 635 635 ASN ASN A . n 
A 1 726 ASP 726 636 636 ASP ASP A . n 
A 1 727 ASN 727 637 637 ASN ASN A . n 
A 1 728 GLU 728 638 638 GLU GLU A . n 
A 1 729 MET 729 639 639 MET MET A . n 
A 1 730 TYR 730 640 640 TYR TYR A . n 
A 1 731 LEU 731 641 641 LEU LEU A . n 
A 1 732 PHE 732 642 642 PHE PHE A . n 
A 1 733 ARG 733 643 643 ARG ARG A . n 
A 1 734 SER 734 644 644 SER SER A . n 
A 1 735 SER 735 645 645 SER SER A . n 
A 1 736 VAL 736 646 646 VAL VAL A . n 
A 1 737 ALA 737 647 647 ALA ALA A . n 
A 1 738 TYR 738 648 648 TYR TYR A . n 
A 1 739 ALA 739 649 649 ALA ALA A . n 
A 1 740 MET 740 650 650 MET MET A . n 
A 1 741 ARG 741 651 651 ARG ARG A . n 
A 1 742 VAL 742 652 652 VAL VAL A . n 
A 1 743 TYR 743 653 653 TYR TYR A . n 
A 1 744 PHE 744 654 654 PHE PHE A . n 
A 1 745 LEU 745 655 655 LEU LEU A . n 
A 1 746 LYS 746 656 656 LYS LYS A . n 
A 1 747 VAL 747 657 657 VAL VAL A . n 
A 1 748 LYS 748 658 658 LYS LYS A . n 
A 1 749 ASN 749 659 659 ASN ASN A . n 
A 1 750 GLU 750 660 660 GLU GLU A . n 
A 1 751 THR 751 661 661 THR THR A . n 
A 1 752 ILE 752 662 662 ILE ILE A . n 
A 1 753 PRO 753 663 663 PRO PRO A . n 
A 1 754 PHE 754 664 664 PHE PHE A . n 
A 1 755 ARG 755 665 665 ARG ARG A . n 
A 1 756 ALA 756 666 666 ALA ALA A . n 
A 1 757 GLU 757 667 667 GLU GLU A . n 
A 1 758 ASP 758 668 668 ASP ASP A . n 
A 1 759 VAL 759 669 669 VAL VAL A . n 
A 1 760 TRP 760 670 670 TRP TRP A . n 
A 1 761 VAL 761 671 671 VAL VAL A . n 
A 1 762 SER 762 672 672 SER SER A . n 
A 1 763 ASP 763 673 673 ASP ASP A . n 
A 1 764 GLU 764 674 674 GLU GLU A . n 
A 1 765 LYS 765 675 675 LYS LYS A . n 
A 1 766 ILE 766 676 676 ILE ILE A . n 
A 1 767 ARG 767 677 677 ARG ARG A . n 
A 1 768 VAL 768 678 678 VAL VAL A . n 
A 1 769 SER 769 679 679 SER SER A . n 
A 1 770 PHE 770 680 680 PHE PHE A . n 
A 1 771 LYS 771 681 681 LYS LYS A . n 
A 1 772 PHE 772 682 682 PHE PHE A . n 
A 1 773 PHE 773 683 683 PHE PHE A . n 
A 1 774 VAL 774 684 684 VAL VAL A . n 
A 1 775 THR 775 685 685 THR THR A . n 
A 1 776 SER 776 686 686 SER SER A . n 
A 1 777 PRO 777 687 687 PRO PRO A . n 
A 1 778 THR 778 688 688 THR THR A . n 
A 1 779 ASN 779 689 689 ASN ASN A . n 
A 1 780 VAL 780 690 690 VAL VAL A . n 
A 1 781 SER 781 691 691 SER SER A . n 
A 1 782 ASP 782 692 692 ASP ASP A . n 
A 1 783 ILE 783 693 693 ILE ILE A . n 
A 1 784 ILE 784 694 694 ILE ILE A . n 
A 1 785 PRO 785 695 695 PRO PRO A . n 
A 1 786 ARG 786 696 696 ARG ARG A . n 
A 1 787 SER 787 697 697 SER SER A . n 
A 1 788 GLU 788 698 698 GLU GLU A . n 
A 1 789 VAL 789 699 699 VAL VAL A . n 
A 1 790 GLU 790 700 700 GLU GLU A . n 
A 1 791 ASP 791 701 701 ASP ASP A . n 
A 1 792 ALA 792 702 702 ALA ALA A . n 
A 1 793 ILE 793 703 703 ILE ILE A . n 
A 1 794 ARG 794 704 704 ARG ARG A . n 
A 1 795 MET 795 705 705 MET MET A . n 
A 1 796 SER 796 706 706 SER SER A . n 
A 1 797 ARG 797 707 707 ARG ARG A . n 
A 1 798 GLY 798 708 708 GLY GLY A . n 
A 1 799 ARG 799 709 709 ARG ARG A . n 
A 1 800 ILE 800 710 710 ILE ILE A . n 
A 1 801 ASN 801 711 711 ASN ASN A . n 
A 1 802 ASP 802 712 712 ASP ASP A . n 
A 1 803 ALA 803 713 713 ALA ALA A . n 
A 1 804 PHE 804 714 714 PHE PHE A . n 
A 1 805 ARG 805 715 715 ARG ARG A . n 
A 1 806 LEU 806 716 716 LEU LEU A . n 
A 1 807 ASP 807 717 717 ASP ASP A . n 
A 1 808 ASP 808 718 718 ASP ASP A . n 
A 1 809 LYS 809 719 719 LYS LYS A . n 
A 1 810 THR 810 720 720 THR THR A . n 
A 1 811 LEU 811 721 721 LEU LEU A . n 
A 1 812 GLU 812 722 722 GLU GLU A . n 
A 1 813 PHE 813 723 723 PHE PHE A . n 
A 1 814 LEU 814 724 724 LEU LEU A . n 
A 1 815 GLY 815 725 725 GLY GLY A . n 
A 1 816 ILE 816 726 726 ILE ILE A . n 
A 1 817 GLN 817 727 ?   ?   ?   A . n 
A 1 818 PRO 818 728 ?   ?   ?   A . n 
A 1 819 THR 819 729 ?   ?   ?   A . n 
A 1 820 LEU 820 730 ?   ?   ?   A . n 
A 1 821 GLY 821 731 ?   ?   ?   A . n 
A 1 822 PRO 822 732 ?   ?   ?   A . n 
A 1 823 PRO 823 733 ?   ?   ?   A . n 
A 1 824 TYR 824 734 ?   ?   ?   A . n 
A 1 825 GLN 825 735 ?   ?   ?   A . n 
A 1 826 PRO 826 736 ?   ?   ?   A . n 
A 1 827 PRO 827 737 ?   ?   ?   A . n 
A 1 828 VAL 828 738 ?   ?   ?   A . n 
A 1 829 THR 829 739 ?   ?   ?   A . n 
A 1 830 GLY 830 740 ?   ?   ?   A . n 
A 1 831 THR 831 741 ?   ?   ?   A . n 
A 1 832 GLY 832 742 ?   ?   ?   A . n 
A 1 833 GLY 833 743 ?   ?   ?   A . n 
A 1 834 GLY 834 744 ?   ?   ?   A . n 
A 1 835 SER 835 745 ?   ?   ?   A . n 
A 1 836 TRP 836 746 ?   ?   ?   A . n 
A 1 837 SER 837 747 ?   ?   ?   A . n 
A 1 838 HIS 838 748 ?   ?   ?   A . n 
A 1 839 PRO 839 749 ?   ?   ?   A . n 
A 1 840 GLN 840 750 ?   ?   ?   A . n 
A 1 841 PHE 841 751 ?   ?   ?   A . n 
A 1 842 GLU 842 752 ?   ?   ?   A . n 
A 1 843 LYS 843 753 ?   ?   ?   A . n 
A 1 844 GLY 844 754 ?   ?   ?   A . n 
A 1 845 GLY 845 755 ?   ?   ?   A . n 
A 1 846 GLY 846 756 ?   ?   ?   A . n 
A 1 847 SER 847 757 ?   ?   ?   A . n 
A 1 848 GLY 848 758 ?   ?   ?   A . n 
A 1 849 GLY 849 759 ?   ?   ?   A . n 
A 1 850 GLY 850 760 ?   ?   ?   A . n 
A 1 851 SER 851 761 ?   ?   ?   A . n 
A 1 852 GLY 852 762 ?   ?   ?   A . n 
A 1 853 GLY 853 763 ?   ?   ?   A . n 
A 1 854 SER 854 764 ?   ?   ?   A . n 
A 1 855 ALA 855 765 ?   ?   ?   A . n 
A 1 856 TRP 856 766 ?   ?   ?   A . n 
A 1 857 SER 857 767 ?   ?   ?   A . n 
A 1 858 HIS 858 768 ?   ?   ?   A . n 
A 1 859 PRO 859 769 ?   ?   ?   A . n 
A 1 860 GLN 860 770 ?   ?   ?   A . n 
A 1 861 PHE 861 771 ?   ?   ?   A . n 
A 1 862 GLU 862 772 ?   ?   ?   A . n 
A 1 863 LYS 863 773 ?   ?   ?   A . n 
A 1 864 GLY 864 774 ?   ?   ?   A . n 
A 1 865 GLY 865 775 ?   ?   ?   A . n 
A 1 866 GLY 866 776 ?   ?   ?   A . n 
A 1 867 GLY 867 777 ?   ?   ?   A . n 
A 1 868 SER 868 778 ?   ?   ?   A . n 
A 1 869 ASP 869 779 ?   ?   ?   A . n 
A 1 870 TYR 870 780 ?   ?   ?   A . n 
A 1 871 LYS 871 781 ?   ?   ?   A . n 
A 1 872 ASP 872 782 ?   ?   ?   A . n 
A 1 873 HIS 873 783 ?   ?   ?   A . n 
A 1 874 ASP 874 784 ?   ?   ?   A . n 
A 1 875 GLY 875 785 ?   ?   ?   A . n 
A 1 876 ASP 876 786 ?   ?   ?   A . n 
A 1 877 TYR 877 787 ?   ?   ?   A . n 
A 1 878 LYS 878 788 ?   ?   ?   A . n 
A 1 879 ASP 879 789 ?   ?   ?   A . n 
A 1 880 HIS 880 790 ?   ?   ?   A . n 
A 1 881 ASP 881 791 ?   ?   ?   A . n 
A 1 882 ILE 882 792 ?   ?   ?   A . n 
A 1 883 ASP 883 793 ?   ?   ?   A . n 
A 1 884 TYR 884 794 ?   ?   ?   A . n 
A 1 885 LYS 885 795 ?   ?   ?   A . n 
A 1 886 ASP 886 796 ?   ?   ?   A . n 
A 1 887 ASP 887 797 ?   ?   ?   A . n 
A 1 888 ASP 888 798 ?   ?   ?   A . n 
A 1 889 ASP 889 799 ?   ?   ?   A . n 
A 1 890 LYS 890 800 ?   ?   ?   A . n 
A 1 891 LEU 891 801 ?   ?   ?   A . n 
B 2 1   MET 1   329 ?   ?   ?   B . n 
B 2 2   GLY 2   330 ?   ?   ?   B . n 
B 2 3   ILE 3   331 ?   ?   ?   B . n 
B 2 4   LEU 4   332 ?   ?   ?   B . n 
B 2 5   PRO 5   333 ?   ?   ?   B . n 
B 2 6   SER 6   334 ?   ?   ?   B . n 
B 2 7   PRO 7   335 ?   ?   ?   B . n 
B 2 8   GLY 8   336 ?   ?   ?   B . n 
B 2 9   MET 9   337 ?   ?   ?   B . n 
B 2 10  PRO 10  338 ?   ?   ?   B . n 
B 2 11  ALA 11  339 ?   ?   ?   B . n 
B 2 12  LEU 12  340 ?   ?   ?   B . n 
B 2 13  LEU 13  341 ?   ?   ?   B . n 
B 2 14  SER 14  342 ?   ?   ?   B . n 
B 2 15  LEU 15  343 ?   ?   ?   B . n 
B 2 16  VAL 16  344 ?   ?   ?   B . n 
B 2 17  SER 17  345 ?   ?   ?   B . n 
B 2 18  LEU 18  346 ?   ?   ?   B . n 
B 2 19  LEU 19  347 ?   ?   ?   B . n 
B 2 20  SER 20  348 ?   ?   ?   B . n 
B 2 21  VAL 21  349 ?   ?   ?   B . n 
B 2 22  LEU 22  350 ?   ?   ?   B . n 
B 2 23  LEU 23  351 ?   ?   ?   B . n 
B 2 24  MET 24  352 ?   ?   ?   B . n 
B 2 25  GLY 25  353 ?   ?   ?   B . n 
B 2 26  CYS 26  354 ?   ?   ?   B . n 
B 2 27  VAL 27  355 ?   ?   ?   B . n 
B 2 28  ALA 28  356 ?   ?   ?   B . n 
B 2 29  GLU 29  357 ?   ?   ?   B . n 
B 2 30  THR 30  358 ?   ?   ?   B . n 
B 2 31  GLY 31  359 ?   ?   ?   B . n 
B 2 32  THR 32  360 ?   ?   ?   B . n 
B 2 33  TYR 33  361 ?   ?   ?   B . n 
B 2 34  SER 34  362 ?   ?   ?   B . n 
B 2 35  VAL 35  363 ?   ?   ?   B . n 
B 2 36  SER 36  364 ?   ?   ?   B . n 
B 2 37  SER 37  365 ?   ?   ?   B . n 
B 2 38  PHE 38  366 ?   ?   ?   B . n 
B 2 39  GLU 39  367 ?   ?   ?   B . n 
B 2 40  ALA 40  368 ?   ?   ?   B . n 
B 2 41  ARG 41  369 ?   ?   ?   B . n 
B 2 42  PRO 42  370 ?   ?   ?   B . n 
B 2 43  GLN 43  371 ?   ?   ?   B . n 
B 2 44  GLY 44  372 ?   ?   ?   B . n 
B 2 45  SER 45  373 ?   ?   ?   B . n 
B 2 46  PHE 46  374 ?   ?   ?   B . n 
B 2 47  VAL 47  375 ?   ?   ?   B . n 
B 2 48  GLU 48  376 ?   ?   ?   B . n 
B 2 49  SER 49  377 ?   ?   ?   B . n 
B 2 50  VAL 50  378 ?   ?   ?   B . n 
B 2 51  TYR 51  379 ?   ?   ?   B . n 
B 2 52  GLU 52  380 ?   ?   ?   B . n 
B 2 53  GLY 53  381 ?   ?   ?   B . n 
B 2 54  ASN 54  382 ?   ?   ?   B . n 
B 2 55  GLU 55  383 ?   ?   ?   B . n 
B 2 56  CYS 56  384 ?   ?   ?   B . n 
B 2 57  ASP 57  385 ?   ?   ?   B . n 
B 2 58  PHE 58  386 ?   ?   ?   B . n 
B 2 59  THR 59  387 ?   ?   ?   B . n 
B 2 60  LYS 60  388 ?   ?   ?   B . n 
B 2 61  LEU 61  389 389 LEU LEU B . n 
B 2 62  PHE 62  390 390 PHE PHE B . n 
B 2 63  ARG 63  391 391 ARG ARG B . n 
B 2 64  GLY 64  392 392 GLY GLY B . n 
B 2 65  PRO 65  393 393 PRO PRO B . n 
B 2 66  VAL 66  394 394 VAL VAL B . n 
B 2 67  PRO 67  395 395 PRO PRO B . n 
B 2 68  GLN 68  396 396 GLN GLN B . n 
B 2 69  PRO 69  397 397 PRO PRO B . n 
B 2 70  TYR 70  398 398 TYR TYR B . n 
B 2 71  GLU 71  399 399 GLU GLU B . n 
B 2 72  PHE 72  400 400 PHE PHE B . n 
B 2 73  GLY 73  401 401 GLY GLY B . n 
B 2 74  ARG 74  402 402 ARG ARG B . n 
B 2 75  LEU 75  403 403 LEU LEU B . n 
B 2 76  VAL 76  404 404 VAL VAL B . n 
B 2 77  PHE 77  405 ?   ?   ?   B . n 
B 2 78  THR 78  406 ?   ?   ?   B . n 
B 2 79  ASN 79  407 ?   ?   ?   B . n 
B 2 80  CYS 80  408 ?   ?   ?   B . n 
B 2 81  ASN 81  409 ?   ?   ?   B . n 
B 2 82  TYR 82  410 410 TYR TYR B . n 
B 2 83  ASN 83  411 411 ASN ASN B . n 
B 2 84  PHE 84  412 412 PHE PHE B . n 
B 2 85  THR 85  413 413 THR THR B . n 
B 2 86  LYS 86  414 414 LYS LYS B . n 
B 2 87  LEU 87  415 415 LEU LEU B . n 
B 2 88  LEU 88  416 416 LEU LEU B . n 
B 2 89  SER 89  417 417 SER SER B . n 
B 2 90  TYR 90  418 418 TYR TYR B . n 
B 2 91  PHE 91  419 419 PHE PHE B . n 
B 2 92  GLN 92  420 420 GLN GLN B . n 
B 2 93  VAL 93  421 421 VAL VAL B . n 
B 2 94  ASP 94  422 422 ASP ASP B . n 
B 2 95  ALA 95  423 423 ALA ALA B . n 
B 2 96  PHE 96  424 424 PHE PHE B . n 
B 2 97  GLU 97  425 425 GLU GLU B . n 
B 2 98  CYS 98  426 426 CYS CYS B . n 
B 2 99  LYS 99  427 427 LYS LYS B . n 
B 2 100 LYS 100 428 428 LYS LYS B . n 
B 2 101 VAL 101 429 429 VAL VAL B . n 
B 2 102 THR 102 430 430 THR THR B . n 
B 2 103 PRO 103 431 431 PRO PRO B . n 
B 2 104 GLU 104 432 432 GLU GLU B . n 
B 2 105 SER 105 433 433 SER SER B . n 
B 2 106 ILE 106 434 434 ILE ILE B . n 
B 2 107 ALA 107 435 435 ALA ALA B . n 
B 2 108 THR 108 436 436 THR THR B . n 
B 2 109 GLY 109 437 ?   ?   ?   B . n 
B 2 110 CYS 110 438 ?   ?   ?   B . n 
B 2 111 TYR 111 439 ?   ?   ?   B . n 
B 2 112 SER 112 440 ?   ?   ?   B . n 
B 2 113 SER 113 441 441 SER SER B . n 
B 2 114 LEU 114 442 442 LEU LEU B . n 
B 2 115 THR 115 443 443 THR THR B . n 
B 2 116 VAL 116 444 444 VAL VAL B . n 
B 2 117 ASP 117 445 445 ASP ASP B . n 
B 2 118 TRP 118 446 446 TRP TRP B . n 
B 2 119 PHE 119 447 447 PHE PHE B . n 
B 2 120 ALA 120 448 448 ALA ALA B . n 
B 2 121 TYR 121 449 449 TYR TYR B . n 
B 2 122 ARG 122 450 450 ARG ARG B . n 
B 2 123 VAL 123 451 451 VAL VAL B . n 
B 2 124 ALA 124 452 452 ALA ALA B . n 
B 2 125 ASP 125 453 453 ASP ASP B . n 
B 2 126 LYS 126 454 454 LYS LYS B . n 
B 2 127 SER 127 455 455 SER SER B . n 
B 2 128 ASP 128 456 456 ASP ASP B . n 
B 2 129 LEU 129 457 457 LEU LEU B . n 
B 2 130 LEU 130 458 458 LEU LEU B . n 
B 2 131 PRO 131 459 459 PRO PRO B . n 
B 2 132 GLY 132 460 460 GLY GLY B . n 
B 2 133 SER 133 461 461 SER SER B . n 
B 2 134 SER 134 462 462 SER SER B . n 
B 2 135 SER 135 463 463 SER SER B . n 
B 2 136 ASP 136 464 464 ASP ASP B . n 
B 2 137 LEU 137 465 465 LEU LEU B . n 
B 2 138 GLN 138 466 466 GLN GLN B . n 
B 2 139 ARG 139 467 467 ARG ARG B . n 
B 2 140 PHE 140 468 468 PHE PHE B . n 
B 2 141 ASN 141 469 469 ASN ASN B . n 
B 2 142 TYR 142 470 470 TYR TYR B . n 
B 2 143 LYS 143 471 471 LYS LYS B . n 
B 2 144 PRO 144 472 472 PRO PRO B . n 
B 2 145 THR 145 473 473 THR THR B . n 
B 2 146 TYR 146 474 474 TYR TYR B . n 
B 2 147 ALA 147 475 475 ALA ALA B . n 
B 2 148 HIS 148 476 476 HIS HIS B . n 
B 2 149 PRO 149 477 477 PRO PRO B . n 
B 2 150 THR 150 478 478 THR THR B . n 
B 2 151 CYS 151 479 479 CYS CYS B . n 
B 2 152 LEU 152 480 480 LEU LEU B . n 
B 2 153 ILE 153 481 481 ILE ILE B . n 
B 2 154 SER 154 482 482 SER SER B . n 
B 2 155 ALA 155 483 483 ALA ALA B . n 
B 2 156 TYR 156 484 484 TYR TYR B . n 
B 2 157 THR 157 485 485 THR THR B . n 
B 2 158 ASP 158 486 486 ASP ASP B . n 
B 2 159 LEU 159 487 487 LEU LEU B . n 
B 2 160 SER 160 488 488 SER SER B . n 
B 2 161 ALA 161 489 489 ALA ALA B . n 
B 2 162 LEU 162 490 490 LEU LEU B . n 
B 2 163 GLY 163 491 491 GLY GLY B . n 
B 2 164 GLY 164 492 492 GLY GLY B . n 
B 2 165 SER 165 493 493 SER SER B . n 
B 2 166 ASN 166 494 494 ASN ASN B . n 
B 2 167 PRO 167 495 495 PRO PRO B . n 
B 2 168 THR 168 496 496 THR THR B . n 
B 2 169 ASN 169 497 497 ASN ASN B . n 
B 2 170 TYR 170 498 498 TYR TYR B . n 
B 2 171 THR 171 499 499 THR THR B . n 
B 2 172 LEU 172 500 500 LEU LEU B . n 
B 2 173 LEU 173 501 501 LEU LEU B . n 
B 2 174 THR 174 502 502 THR THR B . n 
B 2 175 ASN 175 503 503 ASN ASN B . n 
B 2 176 CYS 176 504 504 CYS CYS B . n 
B 2 177 TYR 177 505 505 TYR TYR B . n 
B 2 178 GLY 178 506 506 GLY GLY B . n 
B 2 179 CYS 179 507 507 CYS CYS B . n 
B 2 180 VAL 180 508 508 VAL VAL B . n 
B 2 181 GLY 181 509 509 GLY GLY B . n 
B 2 182 GLN 182 510 510 GLN GLN B . n 
B 2 183 PRO 183 511 511 PRO PRO B . n 
B 2 184 PRO 184 512 512 PRO PRO B . n 
B 2 185 LYS 185 513 513 LYS LYS B . n 
B 2 186 ARG 186 514 514 ARG ARG B . n 
B 2 187 THR 187 515 515 THR THR B . n 
B 2 188 CYS 188 516 516 CYS CYS B . n 
B 2 189 LEU 189 517 517 LEU LEU B . n 
B 2 190 GLU 190 518 518 GLU GLU B . n 
B 2 191 GLU 191 519 519 GLU GLU B . n 
B 2 192 PHE 192 520 520 PHE PHE B . n 
B 2 193 PRO 193 521 521 PRO PRO B . n 
B 2 194 SER 194 522 522 SER SER B . n 
B 2 195 PHE 195 523 523 PHE PHE B . n 
B 2 196 VAL 196 524 524 VAL VAL B . n 
B 2 197 GLU 197 525 525 GLU GLU B . n 
B 2 198 ALA 198 526 526 ALA ALA B . n 
B 2 199 GLY 199 527 527 GLY GLY B . n 
B 2 200 TYR 200 528 528 TYR TYR B . n 
B 2 201 ARG 201 529 529 ARG ARG B . n 
B 2 202 PRO 202 530 530 PRO PRO B . n 
B 2 203 LYS 203 531 531 LYS LYS B . n 
B 2 204 PRO 204 532 532 PRO PRO B . n 
B 2 205 SER 205 533 533 SER SER B . n 
B 2 206 CYS 206 534 534 CYS CYS B . n 
B 2 207 ALA 207 535 535 ALA ALA B . n 
B 2 208 ARG 208 536 536 ARG ARG B . n 
B 2 209 ILE 209 537 537 ILE ILE B . n 
B 2 210 GLY 210 538 538 GLY GLY B . n 
B 2 211 MET 211 539 539 MET MET B . n 
B 2 212 GLN 212 540 540 GLN GLN B . n 
B 2 213 GLY 213 541 541 GLY GLY B . n 
B 2 214 HIS 214 542 542 HIS HIS B . n 
B 2 215 ALA 215 543 543 ALA ALA B . n 
B 2 216 SER 216 544 544 SER SER B . n 
B 2 217 GLY 217 545 545 GLY GLY B . n 
B 2 218 ASN 218 546 546 ASN ASN B . n 
B 2 219 GLU 219 547 547 GLU GLU B . n 
B 2 220 THR 220 548 548 THR THR B . n 
B 2 221 TYR 221 549 549 TYR TYR B . n 
B 2 222 THR 222 550 550 THR THR B . n 
B 2 223 ALA 223 551 551 ALA ALA B . n 
B 2 224 VAL 224 552 552 VAL VAL B . n 
B 2 225 VAL 225 553 553 VAL VAL B . n 
B 2 226 THR 226 554 554 THR THR B . n 
B 2 227 ASN 227 555 555 ASN ASN B . n 
B 2 228 ASN 228 556 556 ASN ASN B . n 
B 2 229 GLU 229 557 557 GLU GLU B . n 
B 2 230 LEU 230 558 558 LEU LEU B . n 
B 2 231 ASP 231 559 559 ASP ASP B . n 
B 2 232 SER 232 560 560 SER SER B . n 
B 2 233 VAL 233 561 561 VAL VAL B . n 
B 2 234 GLY 234 562 562 GLY GLY B . n 
B 2 235 ASP 235 563 563 ASP ASP B . n 
B 2 236 PRO 236 564 564 PRO PRO B . n 
B 2 237 ILE 237 565 565 ILE ILE B . n 
B 2 238 TRP 238 566 566 TRP TRP B . n 
B 2 239 ARG 239 567 567 ARG ARG B . n 
B 2 240 MET 240 568 568 MET MET B . n 
B 2 241 GLY 241 569 569 GLY GLY B . n 
B 2 242 VAL 242 570 570 VAL VAL B . n 
B 2 243 ALA 243 571 571 ALA ALA B . n 
B 2 244 GLN 244 572 572 GLN GLN B . n 
B 2 245 THR 245 573 573 THR THR B . n 
B 2 246 LYS 246 574 574 LYS LYS B . n 
B 2 247 GLU 247 575 575 GLU GLU B . n 
B 2 248 PRO 248 576 576 PRO PRO B . n 
B 2 249 SER 249 577 577 SER SER B . n 
B 2 250 VAL 250 578 578 VAL VAL B . n 
B 2 251 THR 251 579 579 THR THR B . n 
B 2 252 ASP 252 580 580 ASP ASP B . n 
B 2 253 LYS 253 581 581 LYS LYS B . n 
B 2 254 ALA 254 582 582 ALA ALA B . n 
B 2 255 GLU 255 583 583 GLU GLU B . n 
B 2 256 LEU 256 584 584 LEU LEU B . n 
B 2 257 ALA 257 585 585 ALA ALA B . n 
B 2 258 PHE 258 586 586 PHE PHE B . n 
B 2 259 PHE 259 587 587 PHE PHE B . n 
B 2 260 VAL 260 588 588 VAL VAL B . n 
B 2 261 SER 261 589 589 SER SER B . n 
B 2 262 VAL 262 590 ?   ?   ?   B . n 
B 2 263 GLN 263 591 ?   ?   ?   B . n 
B 2 264 ILE 264 592 ?   ?   ?   B . n 
B 2 265 ASP 265 593 ?   ?   ?   B . n 
B 2 266 SER 266 594 ?   ?   ?   B . n 
B 2 267 GLN 267 595 ?   ?   ?   B . n 
B 2 268 SER 268 596 ?   ?   ?   B . n 
B 2 269 SER 269 597 ?   ?   ?   B . n 
B 2 270 SER 270 598 ?   ?   ?   B . n 
B 2 271 VAL 271 599 ?   ?   ?   B . n 
B 2 272 CYS 272 600 ?   ?   ?   B . n 
B 2 273 PRO 273 601 ?   ?   ?   B . n 
B 2 274 LEU 274 602 ?   ?   ?   B . n 
B 2 275 GLY 275 603 ?   ?   ?   B . n 
B 2 276 SER 276 604 ?   ?   ?   B . n 
B 2 277 PRO 277 605 ?   ?   ?   B . n 
B 2 278 LYS 278 606 ?   ?   ?   B . n 
B 2 279 LEU 279 607 ?   ?   ?   B . n 
B 2 280 VAL 280 608 ?   ?   ?   B . n 
B 2 281 PRO 281 609 ?   ?   ?   B . n 
B 2 282 ARG 282 610 ?   ?   ?   B . n 
B 2 283 GLY 283 611 ?   ?   ?   B . n 
B 2 284 SER 284 612 ?   ?   ?   B . n 
B 2 285 SER 285 613 ?   ?   ?   B . n 
B 2 286 SER 286 614 ?   ?   ?   B . n 
B 2 287 GLY 287 615 ?   ?   ?   B . n 
B 2 288 GLY 288 616 ?   ?   ?   B . n 
B 2 289 SER 289 617 ?   ?   ?   B . n 
B 2 290 GLY 290 618 ?   ?   ?   B . n 
B 2 291 LEU 291 619 ?   ?   ?   B . n 
B 2 292 ASN 292 620 ?   ?   ?   B . n 
B 2 293 ASP 293 621 ?   ?   ?   B . n 
B 2 294 ILE 294 622 ?   ?   ?   B . n 
B 2 295 PHE 295 623 ?   ?   ?   B . n 
B 2 296 GLU 296 624 ?   ?   ?   B . n 
B 2 297 ALA 297 625 ?   ?   ?   B . n 
B 2 298 GLN 298 626 ?   ?   ?   B . n 
B 2 299 LYS 299 627 ?   ?   ?   B . n 
B 2 300 ILE 300 628 ?   ?   ?   B . n 
B 2 301 GLU 301 629 ?   ?   ?   B . n 
B 2 302 TRP 302 630 ?   ?   ?   B . n 
B 2 303 HIS 303 631 ?   ?   ?   B . n 
B 2 304 GLU 304 632 ?   ?   ?   B . n 
B 2 305 GLY 305 633 ?   ?   ?   B . n 
B 2 306 GLY 306 634 ?   ?   ?   B . n 
B 2 307 SER 307 635 ?   ?   ?   B . n 
B 2 308 HIS 308 636 ?   ?   ?   B . n 
B 2 309 HIS 309 637 ?   ?   ?   B . n 
B 2 310 HIS 310 638 ?   ?   ?   B . n 
B 2 311 HIS 311 639 ?   ?   ?   B . n 
B 2 312 HIS 312 640 ?   ?   ?   B . n 
B 2 313 HIS 313 641 ?   ?   ?   B . n 
B 2 314 HIS 314 642 ?   ?   ?   B . n 
B 2 315 HIS 315 643 ?   ?   ?   B . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
C 3 NAG 1 C NAG 1 A NAG 729 n 
C 3 NAG 2 C NAG 2 A NAG 730 n 
C 3 FUC 3 C FUC 3 A FUC 731 n 
D 4 NAG 1 D NAG 1 A NAG 733 n 
D 4 NAG 2 D NAG 2 A NAG 734 n 
E 4 NAG 1 E NAG 1 A NAG 735 n 
E 4 NAG 2 E NAG 2 A NAG 736 n 
F 3 NAG 1 F NAG 1 A NAG 739 n 
F 3 NAG 2 F NAG 2 A NAG 741 n 
F 3 FUC 3 F FUC 3 A FUC 740 n 
G 5 NAG 1 G NAG 1 A NAG 742 n 
G 5 NAG 2 G NAG 2 A NAG 743 n 
G 5 BMA 3 G BMA 3 A BMA 744 n 
H 4 NAG 1 H NAG 1 A NAG 745 n 
H 4 NAG 2 H NAG 2 A NAG 746 n 
I 5 NAG 1 I NAG 1 C NAG 696 n 
I 5 NAG 2 I NAG 2 C NAG 697 n 
I 5 BMA 3 I BMA 3 C BMA 698 n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
J 6 NAG 1   901  728 NAG NAG A . 
K 6 NAG 1   902  737 NAG NAG A . 
L 6 NAG 1   903  738 NAG NAG A . 
M 7 ZN  1   904  1   ZN  ZN  A . 
N 6 NAG 1   701  591 NAG NAG B . 
O 8 HOH 1   1001 124 HOH HOH A . 
O 8 HOH 2   1002 19  HOH HOH A . 
O 8 HOH 3   1003 89  HOH HOH A . 
O 8 HOH 4   1004 29  HOH HOH A . 
O 8 HOH 5   1005 30  HOH HOH A . 
O 8 HOH 6   1006 86  HOH HOH A . 
O 8 HOH 7   1007 118 HOH HOH A . 
O 8 HOH 8   1008 109 HOH HOH A . 
O 8 HOH 9   1009 84  HOH HOH A . 
O 8 HOH 10  1010 97  HOH HOH A . 
O 8 HOH 11  1011 28  HOH HOH A . 
O 8 HOH 12  1012 70  HOH HOH A . 
O 8 HOH 13  1013 78  HOH HOH A . 
O 8 HOH 14  1014 66  HOH HOH A . 
O 8 HOH 15  1015 47  HOH HOH A . 
O 8 HOH 16  1016 85  HOH HOH A . 
O 8 HOH 17  1017 24  HOH HOH A . 
O 8 HOH 18  1018 96  HOH HOH A . 
O 8 HOH 19  1019 44  HOH HOH A . 
O 8 HOH 20  1020 120 HOH HOH A . 
O 8 HOH 21  1021 98  HOH HOH A . 
O 8 HOH 22  1022 20  HOH HOH A . 
O 8 HOH 23  1023 23  HOH HOH A . 
O 8 HOH 24  1024 103 HOH HOH A . 
O 8 HOH 25  1025 119 HOH HOH A . 
O 8 HOH 26  1026 52  HOH HOH A . 
O 8 HOH 27  1027 14  HOH HOH A . 
O 8 HOH 28  1028 51  HOH HOH A . 
O 8 HOH 29  1029 121 HOH HOH A . 
O 8 HOH 30  1030 42  HOH HOH A . 
O 8 HOH 31  1031 56  HOH HOH A . 
O 8 HOH 32  1032 18  HOH HOH A . 
O 8 HOH 33  1033 141 HOH HOH A . 
O 8 HOH 34  1034 60  HOH HOH A . 
O 8 HOH 35  1035 32  HOH HOH A . 
O 8 HOH 36  1036 67  HOH HOH A . 
O 8 HOH 37  1037 59  HOH HOH A . 
O 8 HOH 38  1038 88  HOH HOH A . 
O 8 HOH 39  1039 25  HOH HOH A . 
O 8 HOH 40  1040 106 HOH HOH A . 
O 8 HOH 41  1041 69  HOH HOH A . 
O 8 HOH 42  1042 137 HOH HOH A . 
O 8 HOH 43  1043 62  HOH HOH A . 
O 8 HOH 44  1044 13  HOH HOH A . 
O 8 HOH 45  1045 77  HOH HOH A . 
O 8 HOH 46  1046 147 HOH HOH A . 
O 8 HOH 47  1047 57  HOH HOH A . 
O 8 HOH 48  1048 34  HOH HOH A . 
O 8 HOH 49  1049 73  HOH HOH A . 
O 8 HOH 50  1050 53  HOH HOH A . 
O 8 HOH 51  1051 71  HOH HOH A . 
O 8 HOH 52  1052 100 HOH HOH A . 
O 8 HOH 53  1053 143 HOH HOH A . 
O 8 HOH 54  1054 38  HOH HOH A . 
O 8 HOH 55  1055 15  HOH HOH A . 
O 8 HOH 56  1056 142 HOH HOH A . 
O 8 HOH 57  1057 126 HOH HOH A . 
O 8 HOH 58  1058 12  HOH HOH A . 
O 8 HOH 59  1059 63  HOH HOH A . 
O 8 HOH 60  1060 74  HOH HOH A . 
O 8 HOH 61  1061 27  HOH HOH A . 
O 8 HOH 62  1062 138 HOH HOH A . 
O 8 HOH 63  1063 80  HOH HOH A . 
O 8 HOH 64  1064 130 HOH HOH A . 
O 8 HOH 65  1065 91  HOH HOH A . 
O 8 HOH 66  1066 112 HOH HOH A . 
O 8 HOH 67  1067 48  HOH HOH A . 
O 8 HOH 68  1068 134 HOH HOH A . 
O 8 HOH 69  1069 41  HOH HOH A . 
O 8 HOH 70  1070 40  HOH HOH A . 
O 8 HOH 71  1071 95  HOH HOH A . 
O 8 HOH 72  1072 43  HOH HOH A . 
O 8 HOH 73  1073 101 HOH HOH A . 
O 8 HOH 74  1074 122 HOH HOH A . 
O 8 HOH 75  1075 144 HOH HOH A . 
O 8 HOH 76  1076 87  HOH HOH A . 
O 8 HOH 77  1077 128 HOH HOH A . 
O 8 HOH 78  1078 76  HOH HOH A . 
O 8 HOH 79  1079 72  HOH HOH A . 
O 8 HOH 80  1080 83  HOH HOH A . 
O 8 HOH 81  1081 75  HOH HOH A . 
O 8 HOH 82  1082 125 HOH HOH A . 
O 8 HOH 83  1083 58  HOH HOH A . 
O 8 HOH 84  1084 64  HOH HOH A . 
O 8 HOH 85  1085 157 HOH HOH A . 
O 8 HOH 86  1086 79  HOH HOH A . 
O 8 HOH 87  1087 115 HOH HOH A . 
O 8 HOH 88  1088 65  HOH HOH A . 
O 8 HOH 89  1089 135 HOH HOH A . 
O 8 HOH 90  1090 55  HOH HOH A . 
O 8 HOH 91  1091 45  HOH HOH A . 
O 8 HOH 92  1092 117 HOH HOH A . 
O 8 HOH 93  1093 37  HOH HOH A . 
O 8 HOH 94  1094 33  HOH HOH A . 
O 8 HOH 95  1095 99  HOH HOH A . 
O 8 HOH 96  1096 68  HOH HOH A . 
O 8 HOH 97  1097 108 HOH HOH A . 
O 8 HOH 98  1098 153 HOH HOH A . 
O 8 HOH 99  1099 54  HOH HOH A . 
O 8 HOH 100 1100 92  HOH HOH A . 
O 8 HOH 101 1101 61  HOH HOH A . 
O 8 HOH 102 1102 105 HOH HOH A . 
O 8 HOH 103 1103 104 HOH HOH A . 
O 8 HOH 104 1104 132 HOH HOH A . 
O 8 HOH 105 1105 113 HOH HOH A . 
O 8 HOH 106 1106 81  HOH HOH A . 
O 8 HOH 107 1107 16  HOH HOH A . 
O 8 HOH 108 1108 152 HOH HOH A . 
O 8 HOH 109 1109 50  HOH HOH A . 
O 8 HOH 110 1110 133 HOH HOH A . 
O 8 HOH 111 1111 111 HOH HOH A . 
O 8 HOH 112 1112 35  HOH HOH A . 
O 8 HOH 113 1113 21  HOH HOH A . 
O 8 HOH 114 1114 139 HOH HOH A . 
O 8 HOH 115 1115 155 HOH HOH A . 
O 8 HOH 116 1116 31  HOH HOH A . 
O 8 HOH 117 1117 123 HOH HOH A . 
O 8 HOH 118 1118 114 HOH HOH A . 
O 8 HOH 119 1119 107 HOH HOH A . 
O 8 HOH 120 1120 110 HOH HOH A . 
O 8 HOH 121 1121 156 HOH HOH A . 
O 8 HOH 122 1122 116 HOH HOH A . 
O 8 HOH 123 1123 26  HOH HOH A . 
O 8 HOH 124 1124 36  HOH HOH A . 
O 8 HOH 125 1125 4   HOH HOH A . 
O 8 HOH 126 1126 93  HOH HOH A . 
O 8 HOH 127 1127 17  HOH HOH A . 
O 8 HOH 128 1128 6   HOH HOH A . 
O 8 HOH 129 1129 1   HOH HOH A . 
O 8 HOH 130 1130 129 HOH HOH A . 
O 8 HOH 131 1131 22  HOH HOH A . 
O 8 HOH 132 1132 46  HOH HOH A . 
O 8 HOH 133 1133 131 HOH HOH A . 
O 8 HOH 134 1134 7   HOH HOH A . 
O 8 HOH 135 1135 159 HOH HOH A . 
O 8 HOH 136 1136 8   HOH HOH A . 
O 8 HOH 137 1137 3   HOH HOH A . 
O 8 HOH 138 1138 94  HOH HOH A . 
O 8 HOH 139 1139 2   HOH HOH A . 
P 8 HOH 1   801  146 HOH HOH B . 
P 8 HOH 2   802  102 HOH HOH B . 
P 8 HOH 3   803  82  HOH HOH B . 
P 8 HOH 4   804  49  HOH HOH B . 
P 8 HOH 5   805  136 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ASP 57  ? CG  ? A ASP 147 CG  
2   1 Y 1 A ASP 57  ? OD1 ? A ASP 147 OD1 
3   1 Y 1 A ASP 57  ? OD2 ? A ASP 147 OD2 
4   1 Y 1 A LYS 58  ? CG  ? A LYS 148 CG  
5   1 Y 1 A LYS 58  ? CD  ? A LYS 148 CD  
6   1 Y 1 A LYS 58  ? CE  ? A LYS 148 CE  
7   1 Y 1 A LYS 58  ? NZ  ? A LYS 148 NZ  
8   1 Y 1 A GLN 61  ? CG  ? A GLN 151 CG  
9   1 Y 1 A GLN 61  ? CD  ? A GLN 151 CD  
10  1 Y 1 A GLN 61  ? OE1 ? A GLN 151 OE1 
11  1 Y 1 A GLN 61  ? NE2 ? A GLN 151 NE2 
12  1 Y 1 A GLU 65  ? CG  ? A GLU 155 CG  
13  1 Y 1 A GLU 65  ? CD  ? A GLU 155 CD  
14  1 Y 1 A GLU 65  ? OE1 ? A GLU 155 OE1 
15  1 Y 1 A GLU 65  ? OE2 ? A GLU 155 OE2 
16  1 Y 1 A ASP 67  ? CG  ? A ASP 157 CG  
17  1 Y 1 A ASP 67  ? OD1 ? A ASP 157 OD1 
18  1 Y 1 A ASP 67  ? OD2 ? A ASP 157 OD2 
19  1 Y 1 A SER 68  ? OG  ? A SER 158 OG  
20  1 Y 1 A LYS 75  ? CG  ? A LYS 165 CG  
21  1 Y 1 A LYS 75  ? CD  ? A LYS 165 CD  
22  1 Y 1 A LYS 75  ? CE  ? A LYS 165 CE  
23  1 Y 1 A LYS 75  ? NZ  ? A LYS 165 NZ  
24  1 Y 1 A SER 78  ? OG  ? A SER 168 OG  
25  1 Y 1 A LYS 79  ? CG  ? A LYS 169 CG  
26  1 Y 1 A LYS 79  ? CD  ? A LYS 169 CD  
27  1 Y 1 A LYS 79  ? CE  ? A LYS 169 CE  
28  1 Y 1 A LYS 79  ? NZ  ? A LYS 169 NZ  
29  1 Y 1 A GLN 87  ? CG  ? A GLN 177 CG  
30  1 Y 1 A GLN 87  ? CD  ? A GLN 177 CD  
31  1 Y 1 A GLN 87  ? OE1 ? A GLN 177 OE1 
32  1 Y 1 A GLN 87  ? NE2 ? A GLN 177 NE2 
33  1 Y 1 A SER 92  ? OG  ? A SER 182 OG  
34  1 Y 1 A SER 107 ? OG  ? A SER 197 OG  
35  1 Y 1 A GLU 112 ? CG  ? A GLU 202 CG  
36  1 Y 1 A GLU 112 ? CD  ? A GLU 202 CD  
37  1 Y 1 A GLU 112 ? OE1 ? A GLU 202 OE1 
38  1 Y 1 A GLU 112 ? OE2 ? A GLU 202 OE2 
39  1 Y 1 A SER 118 ? OG  ? A SER 208 OG  
40  1 Y 1 A SER 146 ? OG  ? A SER 236 OG  
41  1 Y 1 A ASP 150 ? CG  ? A ASP 240 CG  
42  1 Y 1 A ASP 150 ? OD1 ? A ASP 240 OD1 
43  1 Y 1 A ASP 150 ? OD2 ? A ASP 240 OD2 
44  1 Y 1 A SER 170 ? OG  ? A SER 260 OG  
45  1 Y 1 A GLU 171 ? CG  ? A GLU 261 CG  
46  1 Y 1 A GLU 171 ? CD  ? A GLU 261 CD  
47  1 Y 1 A GLU 171 ? OE1 ? A GLU 261 OE1 
48  1 Y 1 A GLU 171 ? OE2 ? A GLU 261 OE2 
49  1 Y 1 A ASP 206 ? CG  ? A ASP 296 CG  
50  1 Y 1 A ASP 206 ? OD1 ? A ASP 296 OD1 
51  1 Y 1 A ASP 206 ? OD2 ? A ASP 296 OD2 
52  1 Y 1 A ASP 213 ? CG  ? A ASP 303 CG  
53  1 Y 1 A ASP 213 ? OD1 ? A ASP 303 OD1 
54  1 Y 1 A ASP 213 ? OD2 ? A ASP 303 OD2 
55  1 Y 1 A GLU 224 ? CG  ? A GLU 314 CG  
56  1 Y 1 A GLU 224 ? CD  ? A GLU 314 CD  
57  1 Y 1 A GLU 224 ? OE1 ? A GLU 314 OE1 
58  1 Y 1 A GLU 224 ? OE2 ? A GLU 314 OE2 
59  1 Y 1 A ASP 225 ? CG  ? A ASP 315 CG  
60  1 Y 1 A ASP 225 ? OD1 ? A ASP 315 OD1 
61  1 Y 1 A ASP 225 ? OD2 ? A ASP 315 OD2 
62  1 Y 1 A SER 254 ? OG  ? A SER 344 OG  
63  1 Y 1 A ASN 290 ? CG  ? A ASN 380 CG  
64  1 Y 1 A ASN 290 ? OD1 ? A ASN 380 OD1 
65  1 Y 1 A ASN 290 ? ND2 ? A ASN 380 ND2 
66  1 Y 1 A ASP 295 ? CG  ? A ASP 385 CG  
67  1 Y 1 A ASP 295 ? OD1 ? A ASP 385 OD1 
68  1 Y 1 A ASP 295 ? OD2 ? A ASP 385 OD2 
69  1 Y 1 A LYS 299 ? CG  ? A LYS 389 CG  
70  1 Y 1 A LYS 299 ? CD  ? A LYS 389 CD  
71  1 Y 1 A LYS 299 ? CE  ? A LYS 389 CE  
72  1 Y 1 A LYS 299 ? NZ  ? A LYS 389 NZ  
73  1 Y 1 A SER 301 ? OG  ? A SER 391 OG  
74  1 Y 1 A SER 337 ? OG  ? A SER 427 OG  
75  1 Y 1 A ASP 338 ? CG  ? A ASP 428 CG  
76  1 Y 1 A ASP 338 ? OD1 ? A ASP 428 OD1 
77  1 Y 1 A ASP 338 ? OD2 ? A ASP 428 OD2 
78  1 Y 1 A GLN 341 ? CG  ? A GLN 431 CG  
79  1 Y 1 A GLN 341 ? CD  ? A GLN 431 CD  
80  1 Y 1 A GLN 341 ? OE1 ? A GLN 431 OE1 
81  1 Y 1 A GLN 341 ? NE2 ? A GLN 431 NE2 
82  1 Y 1 A VAL 343 ? CG1 ? A VAL 433 CG1 
83  1 Y 1 A VAL 343 ? CG2 ? A VAL 433 CG2 
84  1 Y 1 A ASP 367 ? CG  ? A ASP 457 CG  
85  1 Y 1 A ASP 367 ? OD1 ? A ASP 457 OD1 
86  1 Y 1 A ASP 367 ? OD2 ? A ASP 457 OD2 
87  1 Y 1 A ASN 394 ? CG  ? A ASN 484 CG  
88  1 Y 1 A ASN 394 ? OD1 ? A ASN 484 OD1 
89  1 Y 1 A ASN 394 ? ND2 ? A ASN 484 ND2 
90  1 Y 1 A SER 409 ? OG  ? A SER 499 OG  
91  1 Y 1 A SER 411 ? OG  ? A SER 501 OG  
92  1 Y 1 A ASN 427 ? CG  ? A ASN 517 CG  
93  1 Y 1 A ASN 427 ? OD1 ? A ASN 517 OD1 
94  1 Y 1 A ASN 427 ? ND2 ? A ASN 517 ND2 
95  1 Y 1 A GLU 430 ? CG  ? A GLU 520 CG  
96  1 Y 1 A GLU 430 ? CD  ? A GLU 520 CD  
97  1 Y 1 A GLU 430 ? OE1 ? A GLU 520 OE1 
98  1 Y 1 A GLU 430 ? OE2 ? A GLU 520 OE2 
99  1 Y 1 A GLU 465 ? CG  ? A GLU 555 CG  
100 1 Y 1 A GLU 465 ? CD  ? A GLU 555 CD  
101 1 Y 1 A GLU 465 ? OE1 ? A GLU 555 OE1 
102 1 Y 1 A GLU 465 ? OE2 ? A GLU 555 OE2 
103 1 Y 1 A LYS 467 ? CG  ? A LYS 557 CG  
104 1 Y 1 A LYS 467 ? CD  ? A LYS 557 CD  
105 1 Y 1 A LYS 467 ? CE  ? A LYS 557 CE  
106 1 Y 1 A LYS 467 ? NZ  ? A LYS 557 NZ  
107 1 Y 1 A LYS 470 ? CG  ? A LYS 560 CG  
108 1 Y 1 A LYS 470 ? CD  ? A LYS 560 CD  
109 1 Y 1 A LYS 470 ? CE  ? A LYS 560 CE  
110 1 Y 1 A LYS 470 ? NZ  ? A LYS 560 NZ  
111 1 Y 1 A GLU 475 ? CG  ? A GLU 565 CG  
112 1 Y 1 A GLU 475 ? CD  ? A GLU 565 CD  
113 1 Y 1 A GLU 475 ? OE1 ? A GLU 565 OE1 
114 1 Y 1 A GLU 475 ? OE2 ? A GLU 565 OE2 
115 1 Y 1 A GLU 479 ? CG  ? A GLU 569 CG  
116 1 Y 1 A GLU 479 ? CD  ? A GLU 569 CD  
117 1 Y 1 A GLU 479 ? OE1 ? A GLU 569 OE1 
118 1 Y 1 A GLU 479 ? OE2 ? A GLU 569 OE2 
119 1 Y 1 A GLU 483 ? CG  ? A GLU 573 CG  
120 1 Y 1 A GLU 483 ? CD  ? A GLU 573 CD  
121 1 Y 1 A GLU 483 ? OE1 ? A GLU 573 OE1 
122 1 Y 1 A GLU 483 ? OE2 ? A GLU 573 OE2 
123 1 Y 1 A SER 511 ? OG  ? A SER 601 OG  
124 1 Y 1 A GLN 531 ? CG  ? A GLN 621 CG  
125 1 Y 1 A GLN 531 ? CD  ? A GLN 621 CD  
126 1 Y 1 A GLN 531 ? OE1 ? A GLN 621 OE1 
127 1 Y 1 A GLN 531 ? NE2 ? A GLN 621 NE2 
128 1 Y 1 A SER 545 ? OG  ? A SER 635 OG  
129 1 Y 1 A GLU 549 ? CG  ? A GLU 639 CG  
130 1 Y 1 A GLU 549 ? CD  ? A GLU 639 CD  
131 1 Y 1 A GLU 549 ? OE1 ? A GLU 639 OE1 
132 1 Y 1 A GLU 549 ? OE2 ? A GLU 639 OE2 
133 1 Y 1 A THR 576 ? OG1 ? A THR 666 OG1 
134 1 Y 1 A THR 576 ? CG2 ? A THR 666 CG2 
135 1 Y 1 A GLU 578 ? CG  ? A GLU 668 CG  
136 1 Y 1 A GLU 578 ? CD  ? A GLU 668 CD  
137 1 Y 1 A GLU 578 ? OE1 ? A GLU 668 OE1 
138 1 Y 1 A GLU 578 ? OE2 ? A GLU 668 OE2 
139 1 Y 1 A ASP 580 ? CG  ? A ASP 670 CG  
140 1 Y 1 A ASP 580 ? OD1 ? A ASP 670 OD1 
141 1 Y 1 A ASP 580 ? OD2 ? A ASP 670 OD2 
142 1 Y 1 A GLU 597 ? CG  ? A GLU 687 CG  
143 1 Y 1 A GLU 597 ? CD  ? A GLU 687 CD  
144 1 Y 1 A GLU 597 ? OE1 ? A GLU 687 OE1 
145 1 Y 1 A GLU 597 ? OE2 ? A GLU 687 OE2 
146 1 Y 1 A ASN 601 ? CG  ? A ASN 691 CG  
147 1 Y 1 A ASN 601 ? OD1 ? A ASN 691 OD1 
148 1 Y 1 A ASN 601 ? ND2 ? A ASN 691 ND2 
149 1 Y 1 A SER 606 ? OG  ? A SER 696 OG  
150 1 Y 1 A ASP 608 ? CG  ? A ASP 698 CG  
151 1 Y 1 A ASP 608 ? OD1 ? A ASP 698 OD1 
152 1 Y 1 A ASP 608 ? OD2 ? A ASP 698 OD2 
153 1 Y 1 A GLU 614 ? CG  ? A GLU 704 CG  
154 1 Y 1 A GLU 614 ? CD  ? A GLU 704 CD  
155 1 Y 1 A GLU 614 ? OE1 ? A GLU 704 OE1 
156 1 Y 1 A GLU 614 ? OE2 ? A GLU 704 OE2 
157 1 Y 1 A ARG 620 ? CG  ? A ARG 710 CG  
158 1 Y 1 A ARG 620 ? CD  ? A ARG 710 CD  
159 1 Y 1 A ARG 620 ? NE  ? A ARG 710 NE  
160 1 Y 1 A ARG 620 ? CZ  ? A ARG 710 CZ  
161 1 Y 1 A ARG 620 ? NH1 ? A ARG 710 NH1 
162 1 Y 1 A ARG 620 ? NH2 ? A ARG 710 NH2 
163 1 Y 1 A SER 622 ? OG  ? A SER 712 OG  
164 1 Y 1 A LEU 623 ? CG  ? A LEU 713 CG  
165 1 Y 1 A LEU 623 ? CD1 ? A LEU 713 CD1 
166 1 Y 1 A LEU 623 ? CD2 ? A LEU 713 CD2 
167 1 Y 1 A LYS 624 ? CG  ? A LYS 714 CG  
168 1 Y 1 A LYS 624 ? CD  ? A LYS 714 CD  
169 1 Y 1 A LYS 624 ? CE  ? A LYS 714 CE  
170 1 Y 1 A LYS 624 ? NZ  ? A LYS 714 NZ  
171 1 Y 1 A SER 625 ? OG  ? A SER 715 OG  
172 1 Y 1 A LEU 627 ? CG  ? A LEU 717 CG  
173 1 Y 1 A LEU 627 ? CD1 ? A LEU 717 CD1 
174 1 Y 1 A LEU 627 ? CD2 ? A LEU 717 CD2 
175 1 Y 1 A GLU 629 ? CG  ? A GLU 719 CG  
176 1 Y 1 A GLU 629 ? CD  ? A GLU 719 CD  
177 1 Y 1 A GLU 629 ? OE1 ? A GLU 719 OE1 
178 1 Y 1 A GLU 629 ? OE2 ? A GLU 719 OE2 
179 1 Y 1 A LYS 630 ? CG  ? A LYS 720 CG  
180 1 Y 1 A LYS 630 ? CD  ? A LYS 720 CD  
181 1 Y 1 A LYS 630 ? CE  ? A LYS 720 CE  
182 1 Y 1 A LYS 630 ? NZ  ? A LYS 720 NZ  
183 1 Y 1 A GLU 633 ? CG  ? A GLU 723 CG  
184 1 Y 1 A GLU 633 ? CD  ? A GLU 723 CD  
185 1 Y 1 A GLU 633 ? OE1 ? A GLU 723 OE1 
186 1 Y 1 A GLU 633 ? OE2 ? A GLU 723 OE2 
187 1 Y 1 A ASP 636 ? CG  ? A ASP 726 CG  
188 1 Y 1 A ASP 636 ? OD1 ? A ASP 726 OD1 
189 1 Y 1 A ASP 636 ? OD2 ? A ASP 726 OD2 
190 1 Y 1 A GLU 638 ? CG  ? A GLU 728 CG  
191 1 Y 1 A GLU 638 ? CD  ? A GLU 728 CD  
192 1 Y 1 A GLU 638 ? OE1 ? A GLU 728 OE1 
193 1 Y 1 A GLU 638 ? OE2 ? A GLU 728 OE2 
194 1 Y 1 A SER 644 ? OG  ? A SER 734 OG  
195 1 Y 1 A SER 645 ? OG  ? A SER 735 OG  
196 1 Y 1 A LYS 656 ? CG  ? A LYS 746 CG  
197 1 Y 1 A LYS 656 ? CD  ? A LYS 746 CD  
198 1 Y 1 A LYS 656 ? CE  ? A LYS 746 CE  
199 1 Y 1 A LYS 656 ? NZ  ? A LYS 746 NZ  
200 1 Y 1 A LYS 658 ? CG  ? A LYS 748 CG  
201 1 Y 1 A LYS 658 ? CD  ? A LYS 748 CD  
202 1 Y 1 A LYS 658 ? CE  ? A LYS 748 CE  
203 1 Y 1 A LYS 658 ? NZ  ? A LYS 748 NZ  
204 1 Y 1 A ASN 659 ? CG  ? A ASN 749 CG  
205 1 Y 1 A ASN 659 ? OD1 ? A ASN 749 OD1 
206 1 Y 1 A ASN 659 ? ND2 ? A ASN 749 ND2 
207 1 Y 1 A GLU 660 ? CG  ? A GLU 750 CG  
208 1 Y 1 A GLU 660 ? CD  ? A GLU 750 CD  
209 1 Y 1 A GLU 660 ? OE1 ? A GLU 750 OE1 
210 1 Y 1 A GLU 660 ? OE2 ? A GLU 750 OE2 
211 1 Y 1 A THR 661 ? OG1 ? A THR 751 OG1 
212 1 Y 1 A THR 661 ? CG2 ? A THR 751 CG2 
213 1 Y 1 A GLU 667 ? CG  ? A GLU 757 CG  
214 1 Y 1 A GLU 667 ? CD  ? A GLU 757 CD  
215 1 Y 1 A GLU 667 ? OE1 ? A GLU 757 OE1 
216 1 Y 1 A GLU 667 ? OE2 ? A GLU 757 OE2 
217 1 Y 1 A SER 672 ? OG  ? A SER 762 OG  
218 1 Y 1 A ASP 673 ? CG  ? A ASP 763 CG  
219 1 Y 1 A ASP 673 ? OD1 ? A ASP 763 OD1 
220 1 Y 1 A ASP 673 ? OD2 ? A ASP 763 OD2 
221 1 Y 1 A GLU 674 ? CG  ? A GLU 764 CG  
222 1 Y 1 A GLU 674 ? CD  ? A GLU 764 CD  
223 1 Y 1 A GLU 674 ? OE1 ? A GLU 764 OE1 
224 1 Y 1 A GLU 674 ? OE2 ? A GLU 764 OE2 
225 1 Y 1 A LYS 675 ? CG  ? A LYS 765 CG  
226 1 Y 1 A LYS 675 ? CD  ? A LYS 765 CD  
227 1 Y 1 A LYS 675 ? CE  ? A LYS 765 CE  
228 1 Y 1 A LYS 675 ? NZ  ? A LYS 765 NZ  
229 1 Y 1 A ILE 676 ? CG1 ? A ILE 766 CG1 
230 1 Y 1 A ILE 676 ? CG2 ? A ILE 766 CG2 
231 1 Y 1 A ILE 676 ? CD1 ? A ILE 766 CD1 
232 1 Y 1 A ARG 677 ? CG  ? A ARG 767 CG  
233 1 Y 1 A ARG 677 ? CD  ? A ARG 767 CD  
234 1 Y 1 A ARG 677 ? NE  ? A ARG 767 NE  
235 1 Y 1 A ARG 677 ? CZ  ? A ARG 767 CZ  
236 1 Y 1 A ARG 677 ? NH1 ? A ARG 767 NH1 
237 1 Y 1 A ARG 677 ? NH2 ? A ARG 767 NH2 
238 1 Y 1 A VAL 678 ? CG1 ? A VAL 768 CG1 
239 1 Y 1 A VAL 678 ? CG2 ? A VAL 768 CG2 
240 1 Y 1 A SER 679 ? OG  ? A SER 769 OG  
241 1 Y 1 A THR 688 ? OG1 ? A THR 778 OG1 
242 1 Y 1 A THR 688 ? CG2 ? A THR 778 CG2 
243 1 Y 1 A SER 691 ? OG  ? A SER 781 OG  
244 1 Y 1 A SER 697 ? OG  ? A SER 787 OG  
245 1 Y 1 A GLU 698 ? CG  ? A GLU 788 CG  
246 1 Y 1 A GLU 698 ? CD  ? A GLU 788 CD  
247 1 Y 1 A GLU 698 ? OE1 ? A GLU 788 OE1 
248 1 Y 1 A GLU 698 ? OE2 ? A GLU 788 OE2 
249 1 Y 1 A SER 706 ? OG  ? A SER 796 OG  
250 1 Y 1 A ASP 712 ? CG  ? A ASP 802 CG  
251 1 Y 1 A ASP 712 ? OD1 ? A ASP 802 OD1 
252 1 Y 1 A ASP 712 ? OD2 ? A ASP 802 OD2 
253 1 Y 1 A ASP 717 ? CG  ? A ASP 807 CG  
254 1 Y 1 A ASP 717 ? OD1 ? A ASP 807 OD1 
255 1 Y 1 A ASP 717 ? OD2 ? A ASP 807 OD2 
256 1 Y 1 A ASP 718 ? CG  ? A ASP 808 CG  
257 1 Y 1 A ASP 718 ? OD1 ? A ASP 808 OD1 
258 1 Y 1 A ASP 718 ? OD2 ? A ASP 808 OD2 
259 1 Y 1 A LYS 719 ? CG  ? A LYS 809 CG  
260 1 Y 1 A LYS 719 ? CD  ? A LYS 809 CD  
261 1 Y 1 A LYS 719 ? CE  ? A LYS 809 CE  
262 1 Y 1 A LYS 719 ? NZ  ? A LYS 809 NZ  
263 1 Y 1 A THR 720 ? OG1 ? A THR 810 OG1 
264 1 Y 1 A THR 720 ? CG2 ? A THR 810 CG2 
265 1 Y 1 A GLU 722 ? CG  ? A GLU 812 CG  
266 1 Y 1 A GLU 722 ? CD  ? A GLU 812 CD  
267 1 Y 1 A GLU 722 ? OE1 ? A GLU 812 OE1 
268 1 Y 1 A GLU 722 ? OE2 ? A GLU 812 OE2 
269 1 Y 1 A ILE 726 ? CG1 ? A ILE 816 CG1 
270 1 Y 1 A ILE 726 ? CG2 ? A ILE 816 CG2 
271 1 Y 1 A ILE 726 ? CD1 ? A ILE 816 CD1 
272 1 Y 1 B PHE 390 ? CG  ? B PHE 62  CG  
273 1 Y 1 B PHE 390 ? CD1 ? B PHE 62  CD1 
274 1 Y 1 B PHE 390 ? CD2 ? B PHE 62  CD2 
275 1 Y 1 B PHE 390 ? CE1 ? B PHE 62  CE1 
276 1 Y 1 B PHE 390 ? CE2 ? B PHE 62  CE2 
277 1 Y 1 B PHE 390 ? CZ  ? B PHE 62  CZ  
278 1 Y 1 B ARG 391 ? CG  ? B ARG 63  CG  
279 1 Y 1 B ARG 391 ? CD  ? B ARG 63  CD  
280 1 Y 1 B ARG 391 ? NE  ? B ARG 63  NE  
281 1 Y 1 B ARG 391 ? CZ  ? B ARG 63  CZ  
282 1 Y 1 B ARG 391 ? NH1 ? B ARG 63  NH1 
283 1 Y 1 B ARG 391 ? NH2 ? B ARG 63  NH2 
284 1 Y 1 B LEU 403 ? CG  ? B LEU 75  CG  
285 1 Y 1 B LEU 403 ? CD1 ? B LEU 75  CD1 
286 1 Y 1 B LEU 403 ? CD2 ? B LEU 75  CD2 
287 1 Y 1 B VAL 404 ? CG1 ? B VAL 76  CG1 
288 1 Y 1 B VAL 404 ? CG2 ? B VAL 76  CG2 
289 1 Y 1 B TYR 410 ? CG  ? B TYR 82  CG  
290 1 Y 1 B TYR 410 ? CD1 ? B TYR 82  CD1 
291 1 Y 1 B TYR 410 ? CD2 ? B TYR 82  CD2 
292 1 Y 1 B TYR 410 ? CE1 ? B TYR 82  CE1 
293 1 Y 1 B TYR 410 ? CE2 ? B TYR 82  CE2 
294 1 Y 1 B TYR 410 ? CZ  ? B TYR 82  CZ  
295 1 Y 1 B TYR 410 ? OH  ? B TYR 82  OH  
296 1 Y 1 B ASN 411 ? CG  ? B ASN 83  CG  
297 1 Y 1 B ASN 411 ? OD1 ? B ASN 83  OD1 
298 1 Y 1 B ASN 411 ? ND2 ? B ASN 83  ND2 
299 1 Y 1 B PHE 412 ? CG  ? B PHE 84  CG  
300 1 Y 1 B PHE 412 ? CD1 ? B PHE 84  CD1 
301 1 Y 1 B PHE 412 ? CD2 ? B PHE 84  CD2 
302 1 Y 1 B PHE 412 ? CE1 ? B PHE 84  CE1 
303 1 Y 1 B PHE 412 ? CE2 ? B PHE 84  CE2 
304 1 Y 1 B PHE 412 ? CZ  ? B PHE 84  CZ  
305 1 Y 1 B THR 413 ? OG1 ? B THR 85  OG1 
306 1 Y 1 B THR 413 ? CG2 ? B THR 85  CG2 
307 1 Y 1 B LYS 414 ? CG  ? B LYS 86  CG  
308 1 Y 1 B LYS 414 ? CD  ? B LYS 86  CD  
309 1 Y 1 B LYS 414 ? CE  ? B LYS 86  CE  
310 1 Y 1 B LYS 414 ? NZ  ? B LYS 86  NZ  
311 1 Y 1 B LEU 415 ? CG  ? B LEU 87  CG  
312 1 Y 1 B LEU 415 ? CD1 ? B LEU 87  CD1 
313 1 Y 1 B LEU 415 ? CD2 ? B LEU 87  CD2 
314 1 Y 1 B SER 417 ? OG  ? B SER 89  OG  
315 1 Y 1 B TYR 418 ? CG  ? B TYR 90  CG  
316 1 Y 1 B TYR 418 ? CD1 ? B TYR 90  CD1 
317 1 Y 1 B TYR 418 ? CD2 ? B TYR 90  CD2 
318 1 Y 1 B TYR 418 ? CE1 ? B TYR 90  CE1 
319 1 Y 1 B TYR 418 ? CE2 ? B TYR 90  CE2 
320 1 Y 1 B TYR 418 ? CZ  ? B TYR 90  CZ  
321 1 Y 1 B TYR 418 ? OH  ? B TYR 90  OH  
322 1 Y 1 B PHE 419 ? CG  ? B PHE 91  CG  
323 1 Y 1 B PHE 419 ? CD1 ? B PHE 91  CD1 
324 1 Y 1 B PHE 419 ? CD2 ? B PHE 91  CD2 
325 1 Y 1 B PHE 419 ? CE1 ? B PHE 91  CE1 
326 1 Y 1 B PHE 419 ? CE2 ? B PHE 91  CE2 
327 1 Y 1 B PHE 419 ? CZ  ? B PHE 91  CZ  
328 1 Y 1 B GLN 420 ? CG  ? B GLN 92  CG  
329 1 Y 1 B GLN 420 ? CD  ? B GLN 92  CD  
330 1 Y 1 B GLN 420 ? OE1 ? B GLN 92  OE1 
331 1 Y 1 B GLN 420 ? NE2 ? B GLN 92  NE2 
332 1 Y 1 B ASP 422 ? CG  ? B ASP 94  CG  
333 1 Y 1 B ASP 422 ? OD1 ? B ASP 94  OD1 
334 1 Y 1 B ASP 422 ? OD2 ? B ASP 94  OD2 
335 1 Y 1 B GLU 425 ? CG  ? B GLU 97  CG  
336 1 Y 1 B GLU 425 ? CD  ? B GLU 97  CD  
337 1 Y 1 B GLU 425 ? OE1 ? B GLU 97  OE1 
338 1 Y 1 B GLU 425 ? OE2 ? B GLU 97  OE2 
339 1 Y 1 B VAL 429 ? CG1 ? B VAL 101 CG1 
340 1 Y 1 B VAL 429 ? CG2 ? B VAL 101 CG2 
341 1 Y 1 B THR 430 ? OG1 ? B THR 102 OG1 
342 1 Y 1 B THR 430 ? CG2 ? B THR 102 CG2 
343 1 Y 1 B GLU 432 ? CG  ? B GLU 104 CG  
344 1 Y 1 B GLU 432 ? CD  ? B GLU 104 CD  
345 1 Y 1 B GLU 432 ? OE1 ? B GLU 104 OE1 
346 1 Y 1 B GLU 432 ? OE2 ? B GLU 104 OE2 
347 1 Y 1 B SER 433 ? OG  ? B SER 105 OG  
348 1 Y 1 B ILE 434 ? CG1 ? B ILE 106 CG1 
349 1 Y 1 B ILE 434 ? CG2 ? B ILE 106 CG2 
350 1 Y 1 B ILE 434 ? CD1 ? B ILE 106 CD1 
351 1 Y 1 B THR 436 ? OG1 ? B THR 108 OG1 
352 1 Y 1 B THR 436 ? CG2 ? B THR 108 CG2 
353 1 Y 1 B SER 441 ? OG  ? B SER 113 OG  
354 1 Y 1 B LEU 442 ? CG  ? B LEU 114 CG  
355 1 Y 1 B LEU 442 ? CD1 ? B LEU 114 CD1 
356 1 Y 1 B LEU 442 ? CD2 ? B LEU 114 CD2 
357 1 Y 1 B THR 443 ? OG1 ? B THR 115 OG1 
358 1 Y 1 B THR 443 ? CG2 ? B THR 115 CG2 
359 1 Y 1 B VAL 451 ? CG1 ? B VAL 123 CG1 
360 1 Y 1 B VAL 451 ? CG2 ? B VAL 123 CG2 
361 1 Y 1 B LYS 454 ? CG  ? B LYS 126 CG  
362 1 Y 1 B LYS 454 ? CD  ? B LYS 126 CD  
363 1 Y 1 B LYS 454 ? CE  ? B LYS 126 CE  
364 1 Y 1 B LYS 454 ? NZ  ? B LYS 126 NZ  
365 1 Y 1 B SER 455 ? OG  ? B SER 127 OG  
366 1 Y 1 B LEU 458 ? CG  ? B LEU 130 CG  
367 1 Y 1 B LEU 458 ? CD1 ? B LEU 130 CD1 
368 1 Y 1 B LEU 458 ? CD2 ? B LEU 130 CD2 
369 1 Y 1 B SER 461 ? OG  ? B SER 133 OG  
370 1 Y 1 B SER 462 ? OG  ? B SER 134 OG  
371 1 Y 1 B SER 463 ? OG  ? B SER 135 OG  
372 1 Y 1 B THR 473 ? OG1 ? B THR 145 OG1 
373 1 Y 1 B THR 473 ? CG2 ? B THR 145 CG2 
374 1 Y 1 B THR 478 ? OG1 ? B THR 150 OG1 
375 1 Y 1 B THR 478 ? CG2 ? B THR 150 CG2 
376 1 Y 1 B LEU 480 ? CG  ? B LEU 152 CG  
377 1 Y 1 B LEU 480 ? CD1 ? B LEU 152 CD1 
378 1 Y 1 B LEU 480 ? CD2 ? B LEU 152 CD2 
379 1 Y 1 B ILE 481 ? CG1 ? B ILE 153 CG1 
380 1 Y 1 B ILE 481 ? CG2 ? B ILE 153 CG2 
381 1 Y 1 B ILE 481 ? CD1 ? B ILE 153 CD1 
382 1 Y 1 B SER 482 ? OG  ? B SER 154 OG  
383 1 Y 1 B TYR 484 ? CG  ? B TYR 156 CG  
384 1 Y 1 B TYR 484 ? CD1 ? B TYR 156 CD1 
385 1 Y 1 B TYR 484 ? CD2 ? B TYR 156 CD2 
386 1 Y 1 B TYR 484 ? CE1 ? B TYR 156 CE1 
387 1 Y 1 B TYR 484 ? CE2 ? B TYR 156 CE2 
388 1 Y 1 B TYR 484 ? CZ  ? B TYR 156 CZ  
389 1 Y 1 B TYR 484 ? OH  ? B TYR 156 OH  
390 1 Y 1 B THR 485 ? OG1 ? B THR 157 OG1 
391 1 Y 1 B THR 485 ? CG2 ? B THR 157 CG2 
392 1 Y 1 B ASP 486 ? CG  ? B ASP 158 CG  
393 1 Y 1 B ASP 486 ? OD1 ? B ASP 158 OD1 
394 1 Y 1 B ASP 486 ? OD2 ? B ASP 158 OD2 
395 1 Y 1 B LEU 487 ? CG  ? B LEU 159 CG  
396 1 Y 1 B LEU 487 ? CD1 ? B LEU 159 CD1 
397 1 Y 1 B LEU 487 ? CD2 ? B LEU 159 CD2 
398 1 Y 1 B SER 488 ? OG  ? B SER 160 OG  
399 1 Y 1 B LEU 490 ? CG  ? B LEU 162 CG  
400 1 Y 1 B LEU 490 ? CD1 ? B LEU 162 CD1 
401 1 Y 1 B LEU 490 ? CD2 ? B LEU 162 CD2 
402 1 Y 1 B SER 493 ? OG  ? B SER 165 OG  
403 1 Y 1 B THR 496 ? OG1 ? B THR 168 OG1 
404 1 Y 1 B THR 496 ? CG2 ? B THR 168 CG2 
405 1 Y 1 B GLU 525 ? CG  ? B GLU 197 CG  
406 1 Y 1 B GLU 525 ? CD  ? B GLU 197 CD  
407 1 Y 1 B GLU 525 ? OE1 ? B GLU 197 OE1 
408 1 Y 1 B GLU 525 ? OE2 ? B GLU 197 OE2 
409 1 Y 1 B GLU 547 ? CG  ? B GLU 219 CG  
410 1 Y 1 B GLU 547 ? CD  ? B GLU 219 CD  
411 1 Y 1 B GLU 547 ? OE1 ? B GLU 219 OE1 
412 1 Y 1 B GLU 547 ? OE2 ? B GLU 219 OE2 
413 1 Y 1 B THR 548 ? OG1 ? B THR 220 OG1 
414 1 Y 1 B THR 548 ? CG2 ? B THR 220 CG2 
415 1 Y 1 B ASN 556 ? CG  ? B ASN 228 CG  
416 1 Y 1 B ASN 556 ? OD1 ? B ASN 228 OD1 
417 1 Y 1 B ASN 556 ? ND2 ? B ASN 228 ND2 
418 1 Y 1 B GLU 557 ? CG  ? B GLU 229 CG  
419 1 Y 1 B GLU 557 ? CD  ? B GLU 229 CD  
420 1 Y 1 B GLU 557 ? OE1 ? B GLU 229 OE1 
421 1 Y 1 B GLU 557 ? OE2 ? B GLU 229 OE2 
422 1 Y 1 B SER 560 ? OG  ? B SER 232 OG  
423 1 Y 1 B VAL 561 ? CG1 ? B VAL 233 CG1 
424 1 Y 1 B VAL 561 ? CG2 ? B VAL 233 CG2 
425 1 Y 1 B GLU 575 ? CG  ? B GLU 247 CG  
426 1 Y 1 B GLU 575 ? CD  ? B GLU 247 CD  
427 1 Y 1 B GLU 575 ? OE1 ? B GLU 247 OE1 
428 1 Y 1 B GLU 575 ? OE2 ? B GLU 247 OE2 
429 1 Y 1 B SER 577 ? OG  ? B SER 249 OG  
430 1 Y 1 B VAL 578 ? CG1 ? B VAL 250 CG1 
431 1 Y 1 B VAL 578 ? CG2 ? B VAL 250 CG2 
432 1 Y 1 B THR 579 ? OG1 ? B THR 251 OG1 
433 1 Y 1 B THR 579 ? CG2 ? B THR 251 CG2 
434 1 Y 1 B ASP 580 ? CG  ? B ASP 252 CG  
435 1 Y 1 B ASP 580 ? OD1 ? B ASP 252 OD1 
436 1 Y 1 B ASP 580 ? OD2 ? B ASP 252 OD2 
437 1 Y 1 B LYS 581 ? CG  ? B LYS 253 CG  
438 1 Y 1 B LYS 581 ? CD  ? B LYS 253 CD  
439 1 Y 1 B LYS 581 ? CE  ? B LYS 253 CE  
440 1 Y 1 B LYS 581 ? NZ  ? B LYS 253 NZ  
441 1 Y 1 B LEU 584 ? CG  ? B LEU 256 CG  
442 1 Y 1 B LEU 584 ? CD1 ? B LEU 256 CD1 
443 1 Y 1 B LEU 584 ? CD2 ? B LEU 256 CD2 
444 1 Y 1 B VAL 588 ? CG1 ? B VAL 260 CG1 
445 1 Y 1 B VAL 588 ? CG2 ? B VAL 260 CG2 
446 1 Y 1 B SER 589 ? OG  ? B SER 261 OG  
# 
_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                     9DAK 
_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                         9DAK 
_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                   9DAK 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9DAK 
_struct.title                        'Merbecovirus PnNL2018B Spike glycoprotein RBD bound to the P. Nathusii ACE2' 
_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        9DAK 
_struct_keywords.text            
;Merbecovirus, Spike glycoprotein, fusion protein, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, SSGCID, inhibitor, 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 ? 
D N N 4 ? 
E N N 4 ? 
F N N 3 ? 
G N N 5 ? 
H N N 4 ? 
I N N 5 ? 
J N N 6 ? 
K N N 6 ? 
L N N 6 ? 
M N N 7 ? 
N N N 6 ? 
O N N 8 ? 
P N N 8 ? 
# 
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 PDB 9DAK 9DAK ? 1 ? 1 
2 PDB 9DAK 9DAK ? 2 ? 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 9DAK A 1 ? 891 ? 9DAK -89 ? 801 ? -89 801 
2 2 9DAK B 1 ? 315 ? 9DAK 329 ? 643 ? 329 643 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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 THR A 111 ? THR A 143 ? THR A 21  THR A 53  1 ? 33 
HELX_P HELX_P2  AA2 ASN A 146 ? ALA A 171 ? ASN A 56  ALA A 81  1 ? 26 
HELX_P HELX_P3  AA3 GLN A 172 ? PHE A 174 ? GLN A 82  PHE A 84  5 ? 3  
HELX_P HELX_P4  AA4 PRO A 175 ? ILE A 179 ? PRO A 85  ILE A 89  5 ? 5  
HELX_P HELX_P5  AA5 ASN A 181 ? GLN A 192 ? ASN A 91  GLN A 102 1 ? 12 
HELX_P HELX_P6  AA6 ASN A 194 ? LEU A 199 ? ASN A 104 LEU A 109 5 ? 6  
HELX_P HELX_P7  AA7 THR A 200 ? THR A 220 ? THR A 110 THR A 130 1 ? 21 
HELX_P HELX_P8  AA8 LEU A 235 ? GLU A 243 ? LEU A 145 GLU A 153 1 ? 9  
HELX_P HELX_P9  AA9 ASP A 247 ? VAL A 262 ? ASP A 157 VAL A 172 1 ? 16 
HELX_P HELX_P10 AB1 VAL A 262 ? ASN A 284 ? VAL A 172 ASN A 194 1 ? 23 
HELX_P HELX_P11 AB2 ASP A 288 ? ARG A 294 ? ASP A 198 ARG A 204 1 ? 7  
HELX_P HELX_P12 AB3 GLY A 295 ? GLU A 298 ? GLY A 205 GLU A 208 5 ? 4  
HELX_P HELX_P13 AB4 SER A 308 ? TYR A 342 ? SER A 218 TYR A 252 1 ? 35 
HELX_P HELX_P14 AB5 HIS A 355 ? LEU A 357 ? HIS A 265 LEU A 267 5 ? 3  
HELX_P HELX_P15 AB6 TRP A 365 ? ASN A 367 ? TRP A 275 ASN A 277 5 ? 3  
HELX_P HELX_P16 AB7 LEU A 368 ? VAL A 373 ? LEU A 278 VAL A 283 1 ? 6  
HELX_P HELX_P17 AB8 VAL A 383 ? GLN A 390 ? VAL A 293 GLN A 300 1 ? 8  
HELX_P HELX_P18 AB9 ASP A 393 ? SER A 407 ? ASP A 303 SER A 317 1 ? 15 
HELX_P HELX_P19 AC1 GLU A 416 ? SER A 421 ? GLU A 326 SER A 331 1 ? 6  
HELX_P HELX_P20 AC2 THR A 455 ? TYR A 475 ? THR A 365 TYR A 385 1 ? 21 
HELX_P HELX_P21 AC3 PRO A 479 ? ARG A 483 ? PRO A 389 ARG A 393 5 ? 5  
HELX_P HELX_P22 AC4 GLY A 489 ? ALA A 503 ? GLY A 399 ALA A 413 1 ? 15 
HELX_P HELX_P23 AC5 THR A 504 ? LEU A 511 ? THR A 414 LEU A 421 1 ? 8  
HELX_P HELX_P24 AC6 ASP A 521 ? VAL A 537 ? ASP A 431 VAL A 447 1 ? 17 
HELX_P HELX_P25 AC7 THR A 539 ? GLY A 556 ? THR A 449 GLY A 466 1 ? 18 
HELX_P HELX_P26 AC8 PRO A 559 ? GLU A 561 ? PRO A 469 GLU A 471 5 ? 3  
HELX_P HELX_P27 AC9 GLN A 562 ? ILE A 574 ? GLN A 472 ILE A 484 1 ? 13 
HELX_P HELX_P28 AD1 CYS A 588 ? SER A 592 ? CYS A 498 SER A 502 5 ? 5  
HELX_P HELX_P29 AD2 LEU A 593 ? ASN A 598 ? LEU A 503 ASN A 508 1 ? 6  
HELX_P HELX_P30 AD3 ILE A 603 ? ALA A 623 ? ILE A 513 ALA A 533 1 ? 21 
HELX_P HELX_P31 AD4 PRO A 628 ? CYS A 632 ? PRO A 538 CYS A 542 5 ? 5  
HELX_P HELX_P32 AD5 SER A 637 ? GLU A 649 ? SER A 547 GLU A 559 1 ? 13 
HELX_P HELX_P33 AD6 PRO A 655 ? ARG A 665 ? PRO A 565 ARG A 575 1 ? 11 
HELX_P HELX_P34 AD7 ALA A 671 ? PHE A 678 ? ALA A 581 PHE A 588 1 ? 8  
HELX_P HELX_P35 AD8 PHE A 678 ? GLY A 690 ? PHE A 588 GLY A 600 1 ? 13 
HELX_P HELX_P36 AD9 LEU A 713 ? GLY A 718 ? LEU A 623 GLY A 628 1 ? 6  
HELX_P HELX_P37 AE1 GLU A 719 ? ALA A 721 ? GLU A 629 ALA A 631 5 ? 3  
HELX_P HELX_P38 AE2 ASN A 725 ? LYS A 748 ? ASN A 635 LYS A 658 1 ? 24 
HELX_P HELX_P39 AE3 ARG A 755 ? GLU A 757 ? ARG A 665 GLU A 667 5 ? 3  
HELX_P HELX_P40 AE4 PRO A 785 ? SER A 796 ? PRO A 695 SER A 706 1 ? 12 
HELX_P HELX_P41 AE5 SER A 796 ? PHE A 804 ? SER A 706 PHE A 714 1 ? 9  
HELX_P HELX_P42 AE6 GLN B 68  ? PHE B 72  ? GLN B 396 PHE B 400 5 ? 5  
HELX_P HELX_P43 AE7 ASN B 83  ? LEU B 88  ? ASN B 411 LEU B 416 1 ? 6  
HELX_P HELX_P44 AE8 THR B 102 ? THR B 108 ? THR B 430 THR B 436 1 ? 7  
HELX_P HELX_P45 AE9 ARG B 122 ? LEU B 130 ? ARG B 450 LEU B 458 5 ? 9  
HELX_P HELX_P46 AF1 ASP B 136 ? ASN B 141 ? ASP B 464 ASN B 469 1 ? 6  
HELX_P HELX_P47 AF2 LEU B 159 ? GLY B 163 ? LEU B 487 GLY B 491 5 ? 5  
HELX_P HELX_P48 AF3 LYS B 203 ? ALA B 215 ? LYS B 531 ALA B 543 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 224 SG  ? ? ? 1_555 A CYS 232 SG ? ? A CYS 134 A CYS 142 1_555 ? ? ? ? ? ? ? 2.099 ? ?               
disulf2  disulf ?    ? A CYS 434 SG  ? ? ? 1_555 A CYS 451 SG ? ? A CYS 344 A CYS 361 1_555 ? ? ? ? ? ? ? 2.027 ? ?               
disulf3  disulf ?    ? A CYS 620 SG  ? ? ? 1_555 A CYS 632 SG ? ? A CYS 530 A CYS 542 1_555 ? ? ? ? ? ? ? 2.022 ? ?               
disulf4  disulf ?    ? B CYS 98  SG  ? ? ? 1_555 B CYS 151 SG ? ? B CYS 426 B CYS 479 1_555 ? ? ? ? ? ? ? 2.155 ? ?               
disulf5  disulf ?    ? B CYS 176 SG  ? ? ? 1_555 B CYS 206 SG ? ? B CYS 504 B CYS 534 1_555 ? ? ? ? ? ? ? 2.280 ? ?               
disulf6  disulf ?    ? B CYS 179 SG  ? ? ? 1_555 B CYS 188 SG ? ? B CYS 507 B CYS 516 1_555 ? ? ? ? ? ? ? 2.086 ? ?               
covale1  covale one  ? A ASN 181 ND2 ? ? ? 1_555 J NAG .   C1 ? ? A ASN 91  A NAG 901 1_555 ? ? ? ? ? ? ? 1.483 ? N-Glycosylation 
covale2  covale one  ? A ASN 194 ND2 ? ? ? 1_555 C NAG .   C1 ? ? A ASN 104 C NAG 1   1_555 ? ? ? ? ? ? ? 1.500 ? N-Glycosylation 
covale3  covale one  ? A ASN 306 ND2 ? ? ? 1_555 D NAG .   C1 ? ? A ASN 216 D NAG 1   1_555 ? ? ? ? ? ? ? 1.497 ? N-Glycosylation 
covale4  covale one  ? A ASN 370 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 280 E NAG 1   1_555 ? ? ? ? ? ? ? 1.486 ? N-Glycosylation 
covale5  covale one  ? A ASN 412 ND2 ? ? ? 1_555 K NAG .   C1 ? ? A ASN 322 A NAG 902 1_555 ? ? ? ? ? ? ? 1.500 ? N-Glycosylation 
covale6  covale one  ? A ASN 419 ND2 ? ? ? 1_555 L NAG .   C1 ? ? A ASN 329 A NAG 903 1_555 ? ? ? ? ? ? ? 1.495 ? N-Glycosylation 
covale7  covale one  ? A ASN 624 ND2 ? ? ? 1_555 F NAG .   C1 ? ? A ASN 534 F NAG 1   1_555 ? ? ? ? ? ? ? 1.505 ? N-Glycosylation 
covale8  covale one  ? A ASN 636 ND2 ? ? ? 1_555 G NAG .   C1 ? ? A ASN 546 G NAG 1   1_555 ? ? ? ? ? ? ? 1.490 ? N-Glycosylation 
covale9  covale one  ? A ASN 779 ND2 ? ? ? 1_555 H NAG .   C1 ? ? A ASN 689 H NAG 1   1_555 ? ? ? ? ? ? ? 1.466 ? N-Glycosylation 
covale10 covale one  ? B ASN 169 ND2 ? ? ? 1_555 I NAG .   C1 ? ? B ASN 497 I NAG 1   1_555 ? ? ? ? ? ? ? 1.493 ? N-Glycosylation 
covale11 covale one  ? B ASN 218 ND2 ? ? ? 1_555 N NAG .   C1 ? ? B ASN 546 B NAG 701 1_555 ? ? ? ? ? ? ? 1.496 ? N-Glycosylation 
covale12 covale both ? C NAG .   O4  ? ? ? 1_555 C NAG .   C1 ? ? C NAG 1   C NAG 2   1_555 ? ? ? ? ? ? ? 1.487 ? ?               
covale13 covale both ? C NAG .   O6  ? ? ? 1_555 C FUC .   C1 ? ? C NAG 1   C FUC 3   1_555 ? ? ? ? ? ? ? 1.475 ? ?               
covale14 covale both ? D NAG .   O4  ? ? ? 1_555 D NAG .   C1 ? ? D NAG 1   D NAG 2   1_555 ? ? ? ? ? ? ? 1.502 ? ?               
covale15 covale both ? E NAG .   O4  ? ? ? 1_555 E NAG .   C1 ? ? E NAG 1   E NAG 2   1_555 ? ? ? ? ? ? ? 1.500 ? ?               
covale16 covale both ? F NAG .   O4  ? ? ? 1_555 F NAG .   C1 ? ? F NAG 1   F NAG 2   1_555 ? ? ? ? ? ? ? 1.501 ? ?               
covale17 covale both ? F NAG .   O6  ? ? ? 1_555 F FUC .   C1 ? ? F NAG 1   F FUC 3   1_555 ? ? ? ? ? ? ? 1.497 ? ?               
covale18 covale both ? G NAG .   O4  ? ? ? 1_555 G NAG .   C1 ? ? G NAG 1   G NAG 2   1_555 ? ? ? ? ? ? ? 1.401 ? ?               
covale19 covale both ? G NAG .   O4  ? ? ? 1_555 G BMA .   C1 ? ? G NAG 2   G BMA 3   1_555 ? ? ? ? ? ? ? 1.406 ? ?               
covale20 covale both ? H NAG .   O4  ? ? ? 1_555 H NAG .   C1 ? ? H NAG 1   H NAG 2   1_555 ? ? ? ? ? ? ? 1.396 ? ?               
covale21 covale both ? I NAG .   O4  ? ? ? 1_555 I NAG .   C1 ? ? I NAG 1   I NAG 2   1_555 ? ? ? ? ? ? ? 1.509 ? ?               
covale22 covale both ? I NAG .   O4  ? ? ? 1_555 I BMA .   C1 ? ? I NAG 2   I BMA 3   1_555 ? ? ? ? ? ? ? 1.497 ? ?               
metalc1  metalc ?    ? A HIS 468 NE2 ? ? ? 1_555 M ZN  .   ZN ? ? A HIS 378 A ZN  904 1_555 ? ? ? ? ? ? ? 2.445 ? ?               
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG C .   ? ASN A 194 ? NAG C 1   ? 1_555 ASN A 104 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG D .   ? ASN A 306 ? NAG D 1   ? 1_555 ASN A 216 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG E .   ? ASN A 370 ? NAG E 1   ? 1_555 ASN A 280 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG F .   ? ASN A 624 ? NAG F 1   ? 1_555 ASN A 534 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG G .   ? ASN A 636 ? NAG G 1   ? 1_555 ASN A 546 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG H .   ? ASN A 779 ? NAG H 1   ? 1_555 ASN A 689 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG I .   ? ASN B 169 ? NAG I 1   ? 1_555 ASN B 497 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG J .   ? ASN A 181 ? NAG A 901 ? 1_555 ASN A 91  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG K .   ? ASN A 412 ? NAG A 902 ? 1_555 ASN A 322 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG L .   ? ASN A 419 ? NAG A 903 ? 1_555 ASN A 329 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 NAG N .   ? ASN B 218 ? NAG B 701 ? 1_555 ASN B 546 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
12 CYS A 224 ? CYS A 232 ? CYS A 134 ? 1_555 CYS A 142 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
13 CYS A 434 ? CYS A 451 ? CYS A 344 ? 1_555 CYS A 361 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
14 CYS A 620 ? CYS A 632 ? CYS A 530 ? 1_555 CYS A 542 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
15 CYS B 98  ? CYS B 151 ? CYS B 426 ? 1_555 CYS B 479 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
16 CYS B 176 ? CYS B 206 ? CYS B 504 ? 1_555 CYS B 534 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
17 CYS B 179 ? CYS B 188 ? CYS B 507 ? 1_555 CYS B 516 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           183 
_struct_mon_prot_cis.label_asym_id          B 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PRO 
_struct_mon_prot_cis.auth_seq_id            511 
_struct_mon_prot_cis.auth_asym_id           B 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    184 
_struct_mon_prot_cis.pdbx_label_asym_id_2   B 
_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     512 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    B 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -0.07 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 2 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 4 ? 
AA6 ? 5 ? 
AA7 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 222 ? CYS A 224 ? LYS A 132 CYS A 134 
AA1 2 CYS A 232 ? THR A 234 ? CYS A 142 THR A 144 
AA2 1 LEU A 352 ? PRO A 353 ? LEU A 262 PRO A 263 
AA2 2 VAL A 577 ? VAL A 578 ? VAL A 487 VAL A 488 
AA3 1 THR A 437 ? GLY A 442 ? THR A 347 GLY A 352 
AA3 2 ASP A 445 ? LYS A 449 ? ASP A 355 LYS A 359 
AA4 1 VAL A 759 ? SER A 762 ? VAL A 669 SER A 672 
AA4 2 SER A 769 ? SER A 776 ? SER A 679 SER A 686 
AA4 3 ASN A 779 ? ILE A 783 ? ASN A 689 ILE A 693 
AA5 1 VAL A 759 ? SER A 762 ? VAL A 669 SER A 672 
AA5 2 SER A 769 ? SER A 776 ? SER A 679 SER A 686 
AA5 3 ILE A 707 ? ILE A 711 ? ILE A 617 ILE A 621 
AA5 4 LEU A 811 ? PHE A 813 ? LEU A 721 PHE A 723 
AA6 1 GLY B 73  ? LEU B 75  ? GLY B 401 LEU B 403 
AA6 2 THR B 115 ? ALA B 120 ? THR B 443 ALA B 448 
AA6 3 ALA B 254 ? SER B 261 ? ALA B 582 SER B 589 
AA6 4 THR B 150 ? THR B 157 ? THR B 478 THR B 485 
AA6 5 GLN B 92  ? LYS B 99  ? GLN B 420 LYS B 427 
AA7 1 THR B 187 ? PRO B 193 ? THR B 515 PRO B 521 
AA7 2 TYR B 170 ? VAL B 180 ? TYR B 498 VAL B 508 
AA7 3 ARG B 239 ? LYS B 246 ? ARG B 567 LYS B 574 
AA7 4 THR B 220 ? VAL B 225 ? THR B 548 VAL B 553 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 223 ? N VAL A 133 O PHE A 233 ? O PHE A 143 
AA2 1 2 N LEU A 352 ? N LEU A 262 O VAL A 578 ? O VAL A 488 
AA3 1 2 N TRP A 439 ? N TRP A 349 O ARG A 447 ? O ARG A 357 
AA4 1 2 N TRP A 760 ? N TRP A 670 O PHE A 773 ? O PHE A 683 
AA4 2 3 N SER A 776 ? N SER A 686 O ASN A 779 ? O ASN A 689 
AA5 1 2 N TRP A 760 ? N TRP A 670 O PHE A 773 ? O PHE A 683 
AA5 2 3 O PHE A 770 ? O PHE A 680 N VAL A 709 ? N VAL A 619 
AA5 3 4 N ARG A 710 ? N ARG A 620 O GLU A 812 ? O GLU A 722 
AA6 1 2 N LEU B 75  ? N LEU B 403 O VAL B 116 ? O VAL B 444 
AA6 2 3 N ASP B 117 ? N ASP B 445 O PHE B 259 ? O PHE B 587 
AA6 3 4 O ALA B 254 ? O ALA B 582 N THR B 157 ? N THR B 485 
AA6 4 5 O LEU B 152 ? O LEU B 480 N GLU B 97  ? N GLU B 425 
AA7 1 2 O PHE B 192 ? O PHE B 520 N GLY B 178 ? N GLY B 506 
AA7 2 3 N TYR B 177 ? N TYR B 505 O MET B 240 ? O MET B 568 
AA7 3 4 O ALA B 243 ? O ALA B 571 N TYR B 221 ? N TYR B 549 
# 
_pdbx_entry_details.entry_id                   9DAK 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 A ASP 350 ? ? O  A HOH 1001 ? ? 1.93 
2 1 O   B PHE 523 ? ? O  B HOH 801  ? ? 2.10 
3 1 O   A ASP 269 ? ? O  A HOH 1002 ? ? 2.11 
4 1 O   A ASP 608 ? ? O  A HOH 1003 ? ? 2.12 
5 1 ND2 A ASN 322 ? ? O5 A NAG 902  ? ? 2.13 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CD1 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_1              517 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_2              517 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CD2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LEU 
_pdbx_validate_rmsd_angle.auth_seq_id_3              517 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                132.70 
_pdbx_validate_rmsd_angle.angle_target_value         110.50 
_pdbx_validate_rmsd_angle.angle_deviation            22.20 
_pdbx_validate_rmsd_angle.angle_standard_deviation   3.00 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 54  ? ? -165.11 81.88   
2 1 ASN A 138 ? ? -161.68 80.86   
3 1 ASP A 213 ? ? 50.47   -132.58 
4 1 HIS A 345 ? ? -39.57  118.80  
5 1 GLU B 399 ? ? -143.51 46.56   
6 1 SER B 417 ? ? -150.55 -4.78   
7 1 PHE B 520 ? ? -118.60 71.04   
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9DAK 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9DAK 
_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                  2.4 
_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               1555546 
_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            8.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               'MULTIPLE SOURCES' 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Merbecovirus PnNL2018B Spike glycoprotein RBD bound to the P. Nathusii ACE2' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1,2 
# 
_em_imaging.entry_id                        9DAK 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_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                      ? 
_em_imaging.nominal_defocus_min             200 
_em_imaging.nominal_defocus_max             3500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_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             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9DAK 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9DAK 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -89 ? A MET 1   
2   1 Y 1 A GLY -88 ? A GLY 2   
3   1 Y 1 A GLY -87 ? A GLY 3   
4   1 Y 1 A GLU -86 ? A GLU 4   
5   1 Y 1 A GLY -85 ? A GLY 5   
6   1 Y 1 A LEU -84 ? A LEU 6   
7   1 Y 1 A ARG -83 ? A ARG 7   
8   1 Y 1 A ALA -82 ? A ALA 8   
9   1 Y 1 A SER -81 ? A SER 9   
10  1 Y 1 A PRO -80 ? A PRO 10  
11  1 Y 1 A ARG -79 ? A ARG 11  
12  1 Y 1 A ARG -78 ? A ARG 12  
13  1 Y 1 A ARG -77 ? A ARG 13  
14  1 Y 1 A PRO -76 ? A PRO 14  
15  1 Y 1 A LEU -75 ? A LEU 15  
16  1 Y 1 A LEU -74 ? A LEU 16  
17  1 Y 1 A PRO -73 ? A PRO 17  
18  1 Y 1 A LEU -72 ? A LEU 18  
19  1 Y 1 A GLN -71 ? A GLN 19  
20  1 Y 1 A PRO -70 ? A PRO 20  
21  1 Y 1 A ARG -69 ? A ARG 21  
22  1 Y 1 A GLY -68 ? A GLY 22  
23  1 Y 1 A CYS -67 ? A CYS 23  
24  1 Y 1 A PRO -66 ? A PRO 24  
25  1 Y 1 A ARG -65 ? A ARG 25  
26  1 Y 1 A GLY -64 ? A GLY 26  
27  1 Y 1 A ASP -63 ? A ASP 27  
28  1 Y 1 A GLY -62 ? A GLY 28  
29  1 Y 1 A CYS -61 ? A CYS 29  
30  1 Y 1 A LEU -60 ? A LEU 30  
31  1 Y 1 A ARG -59 ? A ARG 31  
32  1 Y 1 A GLY -58 ? A GLY 32  
33  1 Y 1 A GLY -57 ? A GLY 33  
34  1 Y 1 A ARG -56 ? A ARG 34  
35  1 Y 1 A GLY -55 ? A GLY 35  
36  1 Y 1 A ARG -54 ? A ARG 36  
37  1 Y 1 A ALA -53 ? A ALA 37  
38  1 Y 1 A GLY -52 ? A GLY 38  
39  1 Y 1 A PHE -51 ? A PHE 39  
40  1 Y 1 A GLY -50 ? A GLY 40  
41  1 Y 1 A PHE -49 ? A PHE 41  
42  1 Y 1 A TRP -48 ? A TRP 42  
43  1 Y 1 A ARG -47 ? A ARG 43  
44  1 Y 1 A VAL -46 ? A VAL 44  
45  1 Y 1 A THR -45 ? A THR 45  
46  1 Y 1 A GLY -44 ? A GLY 46  
47  1 Y 1 A GLY -43 ? A GLY 47  
48  1 Y 1 A SER -42 ? A SER 48  
49  1 Y 1 A ARG -41 ? A ARG 49  
50  1 Y 1 A ALA -40 ? A ALA 50  
51  1 Y 1 A SER -39 ? A SER 51  
52  1 Y 1 A ALA -38 ? A ALA 52  
53  1 Y 1 A ASN -37 ? A ASN 53  
54  1 Y 1 A HIS -36 ? A HIS 54  
55  1 Y 1 A VAL -35 ? A VAL 55  
56  1 Y 1 A HIS -34 ? A HIS 56  
57  1 Y 1 A ALA -33 ? A ALA 57  
58  1 Y 1 A PHE -32 ? A PHE 58  
59  1 Y 1 A PHE -31 ? A PHE 59  
60  1 Y 1 A PHE -30 ? A PHE 60  
61  1 Y 1 A PHE -29 ? A PHE 61  
62  1 Y 1 A LEU -28 ? A LEU 62  
63  1 Y 1 A GLN -27 ? A GLN 63  
64  1 Y 1 A LEU -26 ? A LEU 64  
65  1 Y 1 A LEU -25 ? A LEU 65  
66  1 Y 1 A GLY -24 ? A GLY 66  
67  1 Y 1 A ASN -23 ? A ASN 67  
68  1 Y 1 A VAL -22 ? A VAL 68  
69  1 Y 1 A LEU -21 ? A LEU 69  
70  1 Y 1 A VAL -20 ? A VAL 70  
71  1 Y 1 A ILE -19 ? A ILE 71  
72  1 Y 1 A VAL -18 ? A VAL 72  
73  1 Y 1 A LEU -17 ? A LEU 73  
74  1 Y 1 A SER -16 ? A SER 74  
75  1 Y 1 A HIS -15 ? A HIS 75  
76  1 Y 1 A HIS -14 ? A HIS 76  
77  1 Y 1 A PHE -13 ? A PHE 77  
78  1 Y 1 A GLY -12 ? A GLY 78  
79  1 Y 1 A LYS -11 ? A LYS 79  
80  1 Y 1 A GLU -10 ? A GLU 80  
81  1 Y 1 A PHE -9  ? A PHE 81  
82  1 Y 1 A ALA -8  ? A ALA 82  
83  1 Y 1 A THR -7  ? A THR 83  
84  1 Y 1 A MET -6  ? A MET 84  
85  1 Y 1 A PRO -5  ? A PRO 85  
86  1 Y 1 A MET -4  ? A MET 86  
87  1 Y 1 A GLY -3  ? A GLY 87  
88  1 Y 1 A SER -2  ? A SER 88  
89  1 Y 1 A LEU -1  ? A LEU 89  
90  1 Y 1 A GLN 0   ? A GLN 90  
91  1 Y 1 A PRO 1   ? A PRO 91  
92  1 Y 1 A LEU 2   ? A LEU 92  
93  1 Y 1 A ALA 3   ? A ALA 93  
94  1 Y 1 A THR 4   ? A THR 94  
95  1 Y 1 A LEU 5   ? A LEU 95  
96  1 Y 1 A TYR 6   ? A TYR 96  
97  1 Y 1 A LEU 7   ? A LEU 97  
98  1 Y 1 A LEU 8   ? A LEU 98  
99  1 Y 1 A GLY 9   ? A GLY 99  
100 1 Y 1 A MET 10  ? A MET 100 
101 1 Y 1 A LEU 11  ? A LEU 101 
102 1 Y 1 A VAL 12  ? A VAL 102 
103 1 Y 1 A ALA 13  ? A ALA 103 
104 1 Y 1 A SER 14  ? A SER 104 
105 1 Y 1 A VAL 15  ? A VAL 105 
106 1 Y 1 A LEU 16  ? A LEU 106 
107 1 Y 1 A ALA 17  ? A ALA 107 
108 1 Y 1 A GLN 18  ? A GLN 108 
109 1 Y 1 A SER 19  ? A SER 109 
110 1 Y 1 A GLN 727 ? A GLN 817 
111 1 Y 1 A PRO 728 ? A PRO 818 
112 1 Y 1 A THR 729 ? A THR 819 
113 1 Y 1 A LEU 730 ? A LEU 820 
114 1 Y 1 A GLY 731 ? A GLY 821 
115 1 Y 1 A PRO 732 ? A PRO 822 
116 1 Y 1 A PRO 733 ? A PRO 823 
117 1 Y 1 A TYR 734 ? A TYR 824 
118 1 Y 1 A GLN 735 ? A GLN 825 
119 1 Y 1 A PRO 736 ? A PRO 826 
120 1 Y 1 A PRO 737 ? A PRO 827 
121 1 Y 1 A VAL 738 ? A VAL 828 
122 1 Y 1 A THR 739 ? A THR 829 
123 1 Y 1 A GLY 740 ? A GLY 830 
124 1 Y 1 A THR 741 ? A THR 831 
125 1 Y 1 A GLY 742 ? A GLY 832 
126 1 Y 1 A GLY 743 ? A GLY 833 
127 1 Y 1 A GLY 744 ? A GLY 834 
128 1 Y 1 A SER 745 ? A SER 835 
129 1 Y 1 A TRP 746 ? A TRP 836 
130 1 Y 1 A SER 747 ? A SER 837 
131 1 Y 1 A HIS 748 ? A HIS 838 
132 1 Y 1 A PRO 749 ? A PRO 839 
133 1 Y 1 A GLN 750 ? A GLN 840 
134 1 Y 1 A PHE 751 ? A PHE 841 
135 1 Y 1 A GLU 752 ? A GLU 842 
136 1 Y 1 A LYS 753 ? A LYS 843 
137 1 Y 1 A GLY 754 ? A GLY 844 
138 1 Y 1 A GLY 755 ? A GLY 845 
139 1 Y 1 A GLY 756 ? A GLY 846 
140 1 Y 1 A SER 757 ? A SER 847 
141 1 Y 1 A GLY 758 ? A GLY 848 
142 1 Y 1 A GLY 759 ? A GLY 849 
143 1 Y 1 A GLY 760 ? A GLY 850 
144 1 Y 1 A SER 761 ? A SER 851 
145 1 Y 1 A GLY 762 ? A GLY 852 
146 1 Y 1 A GLY 763 ? A GLY 853 
147 1 Y 1 A SER 764 ? A SER 854 
148 1 Y 1 A ALA 765 ? A ALA 855 
149 1 Y 1 A TRP 766 ? A TRP 856 
150 1 Y 1 A SER 767 ? A SER 857 
151 1 Y 1 A HIS 768 ? A HIS 858 
152 1 Y 1 A PRO 769 ? A PRO 859 
153 1 Y 1 A GLN 770 ? A GLN 860 
154 1 Y 1 A PHE 771 ? A PHE 861 
155 1 Y 1 A GLU 772 ? A GLU 862 
156 1 Y 1 A LYS 773 ? A LYS 863 
157 1 Y 1 A GLY 774 ? A GLY 864 
158 1 Y 1 A GLY 775 ? A GLY 865 
159 1 Y 1 A GLY 776 ? A GLY 866 
160 1 Y 1 A GLY 777 ? A GLY 867 
161 1 Y 1 A SER 778 ? A SER 868 
162 1 Y 1 A ASP 779 ? A ASP 869 
163 1 Y 1 A TYR 780 ? A TYR 870 
164 1 Y 1 A LYS 781 ? A LYS 871 
165 1 Y 1 A ASP 782 ? A ASP 872 
166 1 Y 1 A HIS 783 ? A HIS 873 
167 1 Y 1 A ASP 784 ? A ASP 874 
168 1 Y 1 A GLY 785 ? A GLY 875 
169 1 Y 1 A ASP 786 ? A ASP 876 
170 1 Y 1 A TYR 787 ? A TYR 877 
171 1 Y 1 A LYS 788 ? A LYS 878 
172 1 Y 1 A ASP 789 ? A ASP 879 
173 1 Y 1 A HIS 790 ? A HIS 880 
174 1 Y 1 A ASP 791 ? A ASP 881 
175 1 Y 1 A ILE 792 ? A ILE 882 
176 1 Y 1 A ASP 793 ? A ASP 883 
177 1 Y 1 A TYR 794 ? A TYR 884 
178 1 Y 1 A LYS 795 ? A LYS 885 
179 1 Y 1 A ASP 796 ? A ASP 886 
180 1 Y 1 A ASP 797 ? A ASP 887 
181 1 Y 1 A ASP 798 ? A ASP 888 
182 1 Y 1 A ASP 799 ? A ASP 889 
183 1 Y 1 A LYS 800 ? A LYS 890 
184 1 Y 1 A LEU 801 ? A LEU 891 
185 1 Y 1 B MET 329 ? B MET 1   
186 1 Y 1 B GLY 330 ? B GLY 2   
187 1 Y 1 B ILE 331 ? B ILE 3   
188 1 Y 1 B LEU 332 ? B LEU 4   
189 1 Y 1 B PRO 333 ? B PRO 5   
190 1 Y 1 B SER 334 ? B SER 6   
191 1 Y 1 B PRO 335 ? B PRO 7   
192 1 Y 1 B GLY 336 ? B GLY 8   
193 1 Y 1 B MET 337 ? B MET 9   
194 1 Y 1 B PRO 338 ? B PRO 10  
195 1 Y 1 B ALA 339 ? B ALA 11  
196 1 Y 1 B LEU 340 ? B LEU 12  
197 1 Y 1 B LEU 341 ? B LEU 13  
198 1 Y 1 B SER 342 ? B SER 14  
199 1 Y 1 B LEU 343 ? B LEU 15  
200 1 Y 1 B VAL 344 ? B VAL 16  
201 1 Y 1 B SER 345 ? B SER 17  
202 1 Y 1 B LEU 346 ? B LEU 18  
203 1 Y 1 B LEU 347 ? B LEU 19  
204 1 Y 1 B SER 348 ? B SER 20  
205 1 Y 1 B VAL 349 ? B VAL 21  
206 1 Y 1 B LEU 350 ? B LEU 22  
207 1 Y 1 B LEU 351 ? B LEU 23  
208 1 Y 1 B MET 352 ? B MET 24  
209 1 Y 1 B GLY 353 ? B GLY 25  
210 1 Y 1 B CYS 354 ? B CYS 26  
211 1 Y 1 B VAL 355 ? B VAL 27  
212 1 Y 1 B ALA 356 ? B ALA 28  
213 1 Y 1 B GLU 357 ? B GLU 29  
214 1 Y 1 B THR 358 ? B THR 30  
215 1 Y 1 B GLY 359 ? B GLY 31  
216 1 Y 1 B THR 360 ? B THR 32  
217 1 Y 1 B TYR 361 ? B TYR 33  
218 1 Y 1 B SER 362 ? B SER 34  
219 1 Y 1 B VAL 363 ? B VAL 35  
220 1 Y 1 B SER 364 ? B SER 36  
221 1 Y 1 B SER 365 ? B SER 37  
222 1 Y 1 B PHE 366 ? B PHE 38  
223 1 Y 1 B GLU 367 ? B GLU 39  
224 1 Y 1 B ALA 368 ? B ALA 40  
225 1 Y 1 B ARG 369 ? B ARG 41  
226 1 Y 1 B PRO 370 ? B PRO 42  
227 1 Y 1 B GLN 371 ? B GLN 43  
228 1 Y 1 B GLY 372 ? B GLY 44  
229 1 Y 1 B SER 373 ? B SER 45  
230 1 Y 1 B PHE 374 ? B PHE 46  
231 1 Y 1 B VAL 375 ? B VAL 47  
232 1 Y 1 B GLU 376 ? B GLU 48  
233 1 Y 1 B SER 377 ? B SER 49  
234 1 Y 1 B VAL 378 ? B VAL 50  
235 1 Y 1 B TYR 379 ? B TYR 51  
236 1 Y 1 B GLU 380 ? B GLU 52  
237 1 Y 1 B GLY 381 ? B GLY 53  
238 1 Y 1 B ASN 382 ? B ASN 54  
239 1 Y 1 B GLU 383 ? B GLU 55  
240 1 Y 1 B CYS 384 ? B CYS 56  
241 1 Y 1 B ASP 385 ? B ASP 57  
242 1 Y 1 B PHE 386 ? B PHE 58  
243 1 Y 1 B THR 387 ? B THR 59  
244 1 Y 1 B LYS 388 ? B LYS 60  
245 1 Y 1 B PHE 405 ? B PHE 77  
246 1 Y 1 B THR 406 ? B THR 78  
247 1 Y 1 B ASN 407 ? B ASN 79  
248 1 Y 1 B CYS 408 ? B CYS 80  
249 1 Y 1 B ASN 409 ? B ASN 81  
250 1 Y 1 B GLY 437 ? B GLY 109 
251 1 Y 1 B CYS 438 ? B CYS 110 
252 1 Y 1 B TYR 439 ? B TYR 111 
253 1 Y 1 B SER 440 ? B SER 112 
254 1 Y 1 B VAL 590 ? B VAL 262 
255 1 Y 1 B GLN 591 ? B GLN 263 
256 1 Y 1 B ILE 592 ? B ILE 264 
257 1 Y 1 B ASP 593 ? B ASP 265 
258 1 Y 1 B SER 594 ? B SER 266 
259 1 Y 1 B GLN 595 ? B GLN 267 
260 1 Y 1 B SER 596 ? B SER 268 
261 1 Y 1 B SER 597 ? B SER 269 
262 1 Y 1 B SER 598 ? B SER 270 
263 1 Y 1 B VAL 599 ? B VAL 271 
264 1 Y 1 B CYS 600 ? B CYS 272 
265 1 Y 1 B PRO 601 ? B PRO 273 
266 1 Y 1 B LEU 602 ? B LEU 274 
267 1 Y 1 B GLY 603 ? B GLY 275 
268 1 Y 1 B SER 604 ? B SER 276 
269 1 Y 1 B PRO 605 ? B PRO 277 
270 1 Y 1 B LYS 606 ? B LYS 278 
271 1 Y 1 B LEU 607 ? B LEU 279 
272 1 Y 1 B VAL 608 ? B VAL 280 
273 1 Y 1 B PRO 609 ? B PRO 281 
274 1 Y 1 B ARG 610 ? B ARG 282 
275 1 Y 1 B GLY 611 ? B GLY 283 
276 1 Y 1 B SER 612 ? B SER 284 
277 1 Y 1 B SER 613 ? B SER 285 
278 1 Y 1 B SER 614 ? B SER 286 
279 1 Y 1 B GLY 615 ? B GLY 287 
280 1 Y 1 B GLY 616 ? B GLY 288 
281 1 Y 1 B SER 617 ? B SER 289 
282 1 Y 1 B GLY 618 ? B GLY 290 
283 1 Y 1 B LEU 619 ? B LEU 291 
284 1 Y 1 B ASN 620 ? B ASN 292 
285 1 Y 1 B ASP 621 ? B ASP 293 
286 1 Y 1 B ILE 622 ? B ILE 294 
287 1 Y 1 B PHE 623 ? B PHE 295 
288 1 Y 1 B GLU 624 ? B GLU 296 
289 1 Y 1 B ALA 625 ? B ALA 297 
290 1 Y 1 B GLN 626 ? B GLN 298 
291 1 Y 1 B LYS 627 ? B LYS 299 
292 1 Y 1 B ILE 628 ? B ILE 300 
293 1 Y 1 B GLU 629 ? B GLU 301 
294 1 Y 1 B TRP 630 ? B TRP 302 
295 1 Y 1 B HIS 631 ? B HIS 303 
296 1 Y 1 B GLU 632 ? B GLU 304 
297 1 Y 1 B GLY 633 ? B GLY 305 
298 1 Y 1 B GLY 634 ? B GLY 306 
299 1 Y 1 B SER 635 ? B SER 307 
300 1 Y 1 B HIS 636 ? B HIS 308 
301 1 Y 1 B HIS 637 ? B HIS 309 
302 1 Y 1 B HIS 638 ? B HIS 310 
303 1 Y 1 B HIS 639 ? B HIS 311 
304 1 Y 1 B HIS 640 ? B HIS 312 
305 1 Y 1 B HIS 641 ? B HIS 313 
306 1 Y 1 B HIS 642 ? B HIS 314 
307 1 Y 1 B HIS 643 ? B HIS 315 
# 
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  
BMA C1   C  N R 74  
BMA C2   C  N S 75  
BMA C3   C  N S 76  
BMA C4   C  N S 77  
BMA C5   C  N R 78  
BMA C6   C  N N 79  
BMA O1   O  N N 80  
BMA O2   O  N N 81  
BMA O3   O  N N 82  
BMA O4   O  N N 83  
BMA O5   O  N N 84  
BMA O6   O  N N 85  
BMA H1   H  N N 86  
BMA H2   H  N N 87  
BMA H3   H  N N 88  
BMA H4   H  N N 89  
BMA H5   H  N N 90  
BMA H61  H  N N 91  
BMA H62  H  N N 92  
BMA HO1  H  N N 93  
BMA HO2  H  N N 94  
BMA HO3  H  N N 95  
BMA HO4  H  N N 96  
BMA HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
FUC C1   C  N R 112 
FUC C2   C  N S 113 
FUC C3   C  N R 114 
FUC C4   C  N S 115 
FUC C5   C  N S 116 
FUC C6   C  N N 117 
FUC O1   O  N N 118 
FUC O2   O  N N 119 
FUC O3   O  N N 120 
FUC O4   O  N N 121 
FUC O5   O  N N 122 
FUC H1   H  N N 123 
FUC H2   H  N N 124 
FUC H3   H  N N 125 
FUC H4   H  N N 126 
FUC H5   H  N N 127 
FUC H61  H  N N 128 
FUC H62  H  N N 129 
FUC H63  H  N N 130 
FUC HO1  H  N N 131 
FUC HO2  H  N N 132 
FUC HO3  H  N N 133 
FUC HO4  H  N N 134 
GLN N    N  N N 135 
GLN CA   C  N S 136 
GLN C    C  N N 137 
GLN O    O  N N 138 
GLN CB   C  N N 139 
GLN CG   C  N N 140 
GLN CD   C  N N 141 
GLN OE1  O  N N 142 
GLN NE2  N  N N 143 
GLN OXT  O  N N 144 
GLN H    H  N N 145 
GLN H2   H  N N 146 
GLN HA   H  N N 147 
GLN HB2  H  N N 148 
GLN HB3  H  N N 149 
GLN HG2  H  N N 150 
GLN HG3  H  N N 151 
GLN HE21 H  N N 152 
GLN HE22 H  N N 153 
GLN HXT  H  N N 154 
GLU N    N  N N 155 
GLU CA   C  N S 156 
GLU C    C  N N 157 
GLU O    O  N N 158 
GLU CB   C  N N 159 
GLU CG   C  N N 160 
GLU CD   C  N N 161 
GLU OE1  O  N N 162 
GLU OE2  O  N N 163 
GLU OXT  O  N N 164 
GLU H    H  N N 165 
GLU H2   H  N N 166 
GLU HA   H  N N 167 
GLU HB2  H  N N 168 
GLU HB3  H  N N 169 
GLU HG2  H  N N 170 
GLU HG3  H  N N 171 
GLU HE2  H  N N 172 
GLU HXT  H  N N 173 
GLY N    N  N N 174 
GLY CA   C  N N 175 
GLY C    C  N N 176 
GLY O    O  N N 177 
GLY OXT  O  N N 178 
GLY H    H  N N 179 
GLY H2   H  N N 180 
GLY HA2  H  N N 181 
GLY HA3  H  N N 182 
GLY HXT  H  N N 183 
HIS N    N  N N 184 
HIS CA   C  N S 185 
HIS C    C  N N 186 
HIS O    O  N N 187 
HIS CB   C  N N 188 
HIS CG   C  Y N 189 
HIS ND1  N  Y N 190 
HIS CD2  C  Y N 191 
HIS CE1  C  Y N 192 
HIS NE2  N  Y N 193 
HIS OXT  O  N N 194 
HIS H    H  N N 195 
HIS H2   H  N N 196 
HIS HA   H  N N 197 
HIS HB2  H  N N 198 
HIS HB3  H  N N 199 
HIS HD1  H  N N 200 
HIS HD2  H  N N 201 
HIS HE1  H  N N 202 
HIS HE2  H  N N 203 
HIS HXT  H  N N 204 
HOH O    O  N N 205 
HOH H1   H  N N 206 
HOH H2   H  N N 207 
ILE N    N  N N 208 
ILE CA   C  N S 209 
ILE C    C  N N 210 
ILE O    O  N N 211 
ILE CB   C  N S 212 
ILE CG1  C  N N 213 
ILE CG2  C  N N 214 
ILE CD1  C  N N 215 
ILE OXT  O  N N 216 
ILE H    H  N N 217 
ILE H2   H  N N 218 
ILE HA   H  N N 219 
ILE HB   H  N N 220 
ILE HG12 H  N N 221 
ILE HG13 H  N N 222 
ILE HG21 H  N N 223 
ILE HG22 H  N N 224 
ILE HG23 H  N N 225 
ILE HD11 H  N N 226 
ILE HD12 H  N N 227 
ILE HD13 H  N N 228 
ILE HXT  H  N N 229 
LEU N    N  N N 230 
LEU CA   C  N S 231 
LEU C    C  N N 232 
LEU O    O  N N 233 
LEU CB   C  N N 234 
LEU CG   C  N N 235 
LEU CD1  C  N N 236 
LEU CD2  C  N N 237 
LEU OXT  O  N N 238 
LEU H    H  N N 239 
LEU H2   H  N N 240 
LEU HA   H  N N 241 
LEU HB2  H  N N 242 
LEU HB3  H  N N 243 
LEU HG   H  N N 244 
LEU HD11 H  N N 245 
LEU HD12 H  N N 246 
LEU HD13 H  N N 247 
LEU HD21 H  N N 248 
LEU HD22 H  N N 249 
LEU HD23 H  N N 250 
LEU HXT  H  N N 251 
LYS N    N  N N 252 
LYS CA   C  N S 253 
LYS C    C  N N 254 
LYS O    O  N N 255 
LYS CB   C  N N 256 
LYS CG   C  N N 257 
LYS CD   C  N N 258 
LYS CE   C  N N 259 
LYS NZ   N  N N 260 
LYS OXT  O  N N 261 
LYS H    H  N N 262 
LYS H2   H  N N 263 
LYS HA   H  N N 264 
LYS HB2  H  N N 265 
LYS HB3  H  N N 266 
LYS HG2  H  N N 267 
LYS HG3  H  N N 268 
LYS HD2  H  N N 269 
LYS HD3  H  N N 270 
LYS HE2  H  N N 271 
LYS HE3  H  N N 272 
LYS HZ1  H  N N 273 
LYS HZ2  H  N N 274 
LYS HZ3  H  N N 275 
LYS HXT  H  N N 276 
MET N    N  N N 277 
MET CA   C  N S 278 
MET C    C  N N 279 
MET O    O  N N 280 
MET CB   C  N N 281 
MET CG   C  N N 282 
MET SD   S  N N 283 
MET CE   C  N N 284 
MET OXT  O  N N 285 
MET H    H  N N 286 
MET H2   H  N N 287 
MET HA   H  N N 288 
MET HB2  H  N N 289 
MET HB3  H  N N 290 
MET HG2  H  N N 291 
MET HG3  H  N N 292 
MET HE1  H  N N 293 
MET HE2  H  N N 294 
MET HE3  H  N N 295 
MET HXT  H  N N 296 
NAG C1   C  N R 297 
NAG C2   C  N R 298 
NAG C3   C  N R 299 
NAG C4   C  N S 300 
NAG C5   C  N R 301 
NAG C6   C  N N 302 
NAG C7   C  N N 303 
NAG C8   C  N N 304 
NAG N2   N  N N 305 
NAG O1   O  N N 306 
NAG O3   O  N N 307 
NAG O4   O  N N 308 
NAG O5   O  N N 309 
NAG O6   O  N N 310 
NAG O7   O  N N 311 
NAG H1   H  N N 312 
NAG H2   H  N N 313 
NAG H3   H  N N 314 
NAG H4   H  N N 315 
NAG H5   H  N N 316 
NAG H61  H  N N 317 
NAG H62  H  N N 318 
NAG H81  H  N N 319 
NAG H82  H  N N 320 
NAG H83  H  N N 321 
NAG HN2  H  N N 322 
NAG HO1  H  N N 323 
NAG HO3  H  N N 324 
NAG HO4  H  N N 325 
NAG HO6  H  N N 326 
PHE N    N  N N 327 
PHE CA   C  N S 328 
PHE C    C  N N 329 
PHE O    O  N N 330 
PHE CB   C  N N 331 
PHE CG   C  Y N 332 
PHE CD1  C  Y N 333 
PHE CD2  C  Y N 334 
PHE CE1  C  Y N 335 
PHE CE2  C  Y N 336 
PHE CZ   C  Y N 337 
PHE OXT  O  N N 338 
PHE H    H  N N 339 
PHE H2   H  N N 340 
PHE HA   H  N N 341 
PHE HB2  H  N N 342 
PHE HB3  H  N N 343 
PHE HD1  H  N N 344 
PHE HD2  H  N N 345 
PHE HE1  H  N N 346 
PHE HE2  H  N N 347 
PHE HZ   H  N N 348 
PHE HXT  H  N N 349 
PRO N    N  N N 350 
PRO CA   C  N S 351 
PRO C    C  N N 352 
PRO O    O  N N 353 
PRO CB   C  N N 354 
PRO CG   C  N N 355 
PRO CD   C  N N 356 
PRO OXT  O  N N 357 
PRO H    H  N N 358 
PRO HA   H  N N 359 
PRO HB2  H  N N 360 
PRO HB3  H  N N 361 
PRO HG2  H  N N 362 
PRO HG3  H  N N 363 
PRO HD2  H  N N 364 
PRO HD3  H  N N 365 
PRO HXT  H  N N 366 
SER N    N  N N 367 
SER CA   C  N S 368 
SER C    C  N N 369 
SER O    O  N N 370 
SER CB   C  N N 371 
SER OG   O  N N 372 
SER OXT  O  N N 373 
SER H    H  N N 374 
SER H2   H  N N 375 
SER HA   H  N N 376 
SER HB2  H  N N 377 
SER HB3  H  N N 378 
SER HG   H  N N 379 
SER HXT  H  N N 380 
THR N    N  N N 381 
THR CA   C  N S 382 
THR C    C  N N 383 
THR O    O  N N 384 
THR CB   C  N R 385 
THR OG1  O  N N 386 
THR CG2  C  N N 387 
THR OXT  O  N N 388 
THR H    H  N N 389 
THR H2   H  N N 390 
THR HA   H  N N 391 
THR HB   H  N N 392 
THR HG1  H  N N 393 
THR HG21 H  N N 394 
THR HG22 H  N N 395 
THR HG23 H  N N 396 
THR HXT  H  N N 397 
TRP N    N  N N 398 
TRP CA   C  N S 399 
TRP C    C  N N 400 
TRP O    O  N N 401 
TRP CB   C  N N 402 
TRP CG   C  Y N 403 
TRP CD1  C  Y N 404 
TRP CD2  C  Y N 405 
TRP NE1  N  Y N 406 
TRP CE2  C  Y N 407 
TRP CE3  C  Y N 408 
TRP CZ2  C  Y N 409 
TRP CZ3  C  Y N 410 
TRP CH2  C  Y N 411 
TRP OXT  O  N N 412 
TRP H    H  N N 413 
TRP H2   H  N N 414 
TRP HA   H  N N 415 
TRP HB2  H  N N 416 
TRP HB3  H  N N 417 
TRP HD1  H  N N 418 
TRP HE1  H  N N 419 
TRP HE3  H  N N 420 
TRP HZ2  H  N N 421 
TRP HZ3  H  N N 422 
TRP HH2  H  N N 423 
TRP HXT  H  N N 424 
TYR N    N  N N 425 
TYR CA   C  N S 426 
TYR C    C  N N 427 
TYR O    O  N N 428 
TYR CB   C  N N 429 
TYR CG   C  Y N 430 
TYR CD1  C  Y N 431 
TYR CD2  C  Y N 432 
TYR CE1  C  Y N 433 
TYR CE2  C  Y N 434 
TYR CZ   C  Y N 435 
TYR OH   O  N N 436 
TYR OXT  O  N N 437 
TYR H    H  N N 438 
TYR H2   H  N N 439 
TYR HA   H  N N 440 
TYR HB2  H  N N 441 
TYR HB3  H  N N 442 
TYR HD1  H  N N 443 
TYR HD2  H  N N 444 
TYR HE1  H  N N 445 
TYR HE2  H  N N 446 
TYR HH   H  N N 447 
TYR HXT  H  N N 448 
VAL N    N  N N 449 
VAL CA   C  N S 450 
VAL C    C  N N 451 
VAL O    O  N N 452 
VAL CB   C  N N 453 
VAL CG1  C  N N 454 
VAL CG2  C  N N 455 
VAL OXT  O  N N 456 
VAL H    H  N N 457 
VAL H2   H  N N 458 
VAL HA   H  N N 459 
VAL HB   H  N N 460 
VAL HG11 H  N N 461 
VAL HG12 H  N N 462 
VAL HG13 H  N N 463 
VAL HG21 H  N N 464 
VAL HG22 H  N N 465 
VAL HG23 H  N N 466 
VAL HXT  H  N N 467 
ZN  ZN   ZN N N 468 
# 
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  
BMA C1  C2   sing N N 70  
BMA C1  O1   sing N N 71  
BMA C1  O5   sing N N 72  
BMA C1  H1   sing N N 73  
BMA C2  C3   sing N N 74  
BMA C2  O2   sing N N 75  
BMA C2  H2   sing N N 76  
BMA C3  C4   sing N N 77  
BMA C3  O3   sing N N 78  
BMA C3  H3   sing N N 79  
BMA C4  C5   sing N N 80  
BMA C4  O4   sing N N 81  
BMA C4  H4   sing N N 82  
BMA C5  C6   sing N N 83  
BMA C5  O5   sing N N 84  
BMA C5  H5   sing N N 85  
BMA C6  O6   sing N N 86  
BMA C6  H61  sing N N 87  
BMA C6  H62  sing N N 88  
BMA O1  HO1  sing N N 89  
BMA O2  HO2  sing N N 90  
BMA O3  HO3  sing N N 91  
BMA O4  HO4  sing N N 92  
BMA O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
FUC C1  C2   sing N N 107 
FUC C1  O1   sing N N 108 
FUC C1  O5   sing N N 109 
FUC C1  H1   sing N N 110 
FUC C2  C3   sing N N 111 
FUC C2  O2   sing N N 112 
FUC C2  H2   sing N N 113 
FUC C3  C4   sing N N 114 
FUC C3  O3   sing N N 115 
FUC C3  H3   sing N N 116 
FUC C4  C5   sing N N 117 
FUC C4  O4   sing N N 118 
FUC C4  H4   sing N N 119 
FUC C5  C6   sing N N 120 
FUC C5  O5   sing N N 121 
FUC C5  H5   sing N N 122 
FUC C6  H61  sing N N 123 
FUC C6  H62  sing N N 124 
FUC C6  H63  sing N N 125 
FUC O1  HO1  sing N N 126 
FUC O2  HO2  sing N N 127 
FUC O3  HO3  sing N N 128 
FUC O4  HO4  sing N N 129 
GLN N   CA   sing N N 130 
GLN N   H    sing N N 131 
GLN N   H2   sing N N 132 
GLN CA  C    sing N N 133 
GLN CA  CB   sing N N 134 
GLN CA  HA   sing N N 135 
GLN C   O    doub N N 136 
GLN C   OXT  sing N N 137 
GLN CB  CG   sing N N 138 
GLN CB  HB2  sing N N 139 
GLN CB  HB3  sing N N 140 
GLN CG  CD   sing N N 141 
GLN CG  HG2  sing N N 142 
GLN CG  HG3  sing N N 143 
GLN CD  OE1  doub N N 144 
GLN CD  NE2  sing N N 145 
GLN NE2 HE21 sing N N 146 
GLN NE2 HE22 sing N N 147 
GLN OXT HXT  sing N N 148 
GLU N   CA   sing N N 149 
GLU N   H    sing N N 150 
GLU N   H2   sing N N 151 
GLU CA  C    sing N N 152 
GLU CA  CB   sing N N 153 
GLU CA  HA   sing N N 154 
GLU C   O    doub N N 155 
GLU C   OXT  sing N N 156 
GLU CB  CG   sing N N 157 
GLU CB  HB2  sing N N 158 
GLU CB  HB3  sing N N 159 
GLU CG  CD   sing N N 160 
GLU CG  HG2  sing N N 161 
GLU CG  HG3  sing N N 162 
GLU CD  OE1  doub N N 163 
GLU CD  OE2  sing N N 164 
GLU OE2 HE2  sing N N 165 
GLU OXT HXT  sing N N 166 
GLY N   CA   sing N N 167 
GLY N   H    sing N N 168 
GLY N   H2   sing N N 169 
GLY CA  C    sing N N 170 
GLY CA  HA2  sing N N 171 
GLY CA  HA3  sing N N 172 
GLY C   O    doub N N 173 
GLY C   OXT  sing N N 174 
GLY OXT HXT  sing N N 175 
HIS N   CA   sing N N 176 
HIS N   H    sing N N 177 
HIS N   H2   sing N N 178 
HIS CA  C    sing N N 179 
HIS CA  CB   sing N N 180 
HIS CA  HA   sing N N 181 
HIS C   O    doub N N 182 
HIS C   OXT  sing N N 183 
HIS CB  CG   sing N N 184 
HIS CB  HB2  sing N N 185 
HIS CB  HB3  sing N N 186 
HIS CG  ND1  sing Y N 187 
HIS CG  CD2  doub Y N 188 
HIS ND1 CE1  doub Y N 189 
HIS ND1 HD1  sing N N 190 
HIS CD2 NE2  sing Y N 191 
HIS CD2 HD2  sing N N 192 
HIS CE1 NE2  sing Y N 193 
HIS CE1 HE1  sing N N 194 
HIS NE2 HE2  sing N N 195 
HIS OXT HXT  sing N N 196 
HOH O   H1   sing N N 197 
HOH O   H2   sing N N 198 
ILE N   CA   sing N N 199 
ILE N   H    sing N N 200 
ILE N   H2   sing N N 201 
ILE CA  C    sing N N 202 
ILE CA  CB   sing N N 203 
ILE CA  HA   sing N N 204 
ILE C   O    doub N N 205 
ILE C   OXT  sing N N 206 
ILE CB  CG1  sing N N 207 
ILE CB  CG2  sing N N 208 
ILE CB  HB   sing N N 209 
ILE CG1 CD1  sing N N 210 
ILE CG1 HG12 sing N N 211 
ILE CG1 HG13 sing N N 212 
ILE CG2 HG21 sing N N 213 
ILE CG2 HG22 sing N N 214 
ILE CG2 HG23 sing N N 215 
ILE CD1 HD11 sing N N 216 
ILE CD1 HD12 sing N N 217 
ILE CD1 HD13 sing N N 218 
ILE OXT HXT  sing N N 219 
LEU N   CA   sing N N 220 
LEU N   H    sing N N 221 
LEU N   H2   sing N N 222 
LEU CA  C    sing N N 223 
LEU CA  CB   sing N N 224 
LEU CA  HA   sing N N 225 
LEU C   O    doub N N 226 
LEU C   OXT  sing N N 227 
LEU CB  CG   sing N N 228 
LEU CB  HB2  sing N N 229 
LEU CB  HB3  sing N N 230 
LEU CG  CD1  sing N N 231 
LEU CG  CD2  sing N N 232 
LEU CG  HG   sing N N 233 
LEU CD1 HD11 sing N N 234 
LEU CD1 HD12 sing N N 235 
LEU CD1 HD13 sing N N 236 
LEU CD2 HD21 sing N N 237 
LEU CD2 HD22 sing N N 238 
LEU CD2 HD23 sing N N 239 
LEU OXT HXT  sing N N 240 
LYS N   CA   sing N N 241 
LYS N   H    sing N N 242 
LYS N   H2   sing N N 243 
LYS CA  C    sing N N 244 
LYS CA  CB   sing N N 245 
LYS CA  HA   sing N N 246 
LYS C   O    doub N N 247 
LYS C   OXT  sing N N 248 
LYS CB  CG   sing N N 249 
LYS CB  HB2  sing N N 250 
LYS CB  HB3  sing N N 251 
LYS CG  CD   sing N N 252 
LYS CG  HG2  sing N N 253 
LYS CG  HG3  sing N N 254 
LYS CD  CE   sing N N 255 
LYS CD  HD2  sing N N 256 
LYS CD  HD3  sing N N 257 
LYS CE  NZ   sing N N 258 
LYS CE  HE2  sing N N 259 
LYS CE  HE3  sing N N 260 
LYS NZ  HZ1  sing N N 261 
LYS NZ  HZ2  sing N N 262 
LYS NZ  HZ3  sing N N 263 
LYS OXT HXT  sing N N 264 
MET N   CA   sing N N 265 
MET N   H    sing N N 266 
MET N   H2   sing N N 267 
MET CA  C    sing N N 268 
MET CA  CB   sing N N 269 
MET CA  HA   sing N N 270 
MET C   O    doub N N 271 
MET C   OXT  sing N N 272 
MET CB  CG   sing N N 273 
MET CB  HB2  sing N N 274 
MET CB  HB3  sing N N 275 
MET CG  SD   sing N N 276 
MET CG  HG2  sing N N 277 
MET CG  HG3  sing N N 278 
MET SD  CE   sing N N 279 
MET CE  HE1  sing N N 280 
MET CE  HE2  sing N N 281 
MET CE  HE3  sing N N 282 
MET OXT HXT  sing N N 283 
NAG C1  C2   sing N N 284 
NAG C1  O1   sing N N 285 
NAG C1  O5   sing N N 286 
NAG C1  H1   sing N N 287 
NAG C2  C3   sing N N 288 
NAG C2  N2   sing N N 289 
NAG C2  H2   sing N N 290 
NAG C3  C4   sing N N 291 
NAG C3  O3   sing N N 292 
NAG C3  H3   sing N N 293 
NAG C4  C5   sing N N 294 
NAG C4  O4   sing N N 295 
NAG C4  H4   sing N N 296 
NAG C5  C6   sing N N 297 
NAG C5  O5   sing N N 298 
NAG C5  H5   sing N N 299 
NAG C6  O6   sing N N 300 
NAG C6  H61  sing N N 301 
NAG C6  H62  sing N N 302 
NAG C7  C8   sing N N 303 
NAG C7  N2   sing N N 304 
NAG C7  O7   doub N N 305 
NAG C8  H81  sing N N 306 
NAG C8  H82  sing N N 307 
NAG C8  H83  sing N N 308 
NAG N2  HN2  sing N N 309 
NAG O1  HO1  sing N N 310 
NAG O3  HO3  sing N N 311 
NAG O4  HO4  sing N N 312 
NAG O6  HO6  sing N N 313 
PHE N   CA   sing N N 314 
PHE N   H    sing N N 315 
PHE N   H2   sing N N 316 
PHE CA  C    sing N N 317 
PHE CA  CB   sing N N 318 
PHE CA  HA   sing N N 319 
PHE C   O    doub N N 320 
PHE C   OXT  sing N N 321 
PHE CB  CG   sing N N 322 
PHE CB  HB2  sing N N 323 
PHE CB  HB3  sing N N 324 
PHE CG  CD1  doub Y N 325 
PHE CG  CD2  sing Y N 326 
PHE CD1 CE1  sing Y N 327 
PHE CD1 HD1  sing N N 328 
PHE CD2 CE2  doub Y N 329 
PHE CD2 HD2  sing N N 330 
PHE CE1 CZ   doub Y N 331 
PHE CE1 HE1  sing N N 332 
PHE CE2 CZ   sing Y N 333 
PHE CE2 HE2  sing N N 334 
PHE CZ  HZ   sing N N 335 
PHE OXT HXT  sing N N 336 
PRO N   CA   sing N N 337 
PRO N   CD   sing N N 338 
PRO N   H    sing N N 339 
PRO CA  C    sing N N 340 
PRO CA  CB   sing N N 341 
PRO CA  HA   sing N N 342 
PRO C   O    doub N N 343 
PRO C   OXT  sing N N 344 
PRO CB  CG   sing N N 345 
PRO CB  HB2  sing N N 346 
PRO CB  HB3  sing N N 347 
PRO CG  CD   sing N N 348 
PRO CG  HG2  sing N N 349 
PRO CG  HG3  sing N N 350 
PRO CD  HD2  sing N N 351 
PRO CD  HD3  sing N N 352 
PRO OXT HXT  sing N N 353 
SER N   CA   sing N N 354 
SER N   H    sing N N 355 
SER N   H2   sing N N 356 
SER CA  C    sing N N 357 
SER CA  CB   sing N N 358 
SER CA  HA   sing N N 359 
SER C   O    doub N N 360 
SER C   OXT  sing N N 361 
SER CB  OG   sing N N 362 
SER CB  HB2  sing N N 363 
SER CB  HB3  sing N N 364 
SER OG  HG   sing N N 365 
SER OXT HXT  sing N N 366 
THR N   CA   sing N N 367 
THR N   H    sing N N 368 
THR N   H2   sing N N 369 
THR CA  C    sing N N 370 
THR CA  CB   sing N N 371 
THR CA  HA   sing N N 372 
THR C   O    doub N N 373 
THR C   OXT  sing N N 374 
THR CB  OG1  sing N N 375 
THR CB  CG2  sing N N 376 
THR CB  HB   sing N N 377 
THR OG1 HG1  sing N N 378 
THR CG2 HG21 sing N N 379 
THR CG2 HG22 sing N N 380 
THR CG2 HG23 sing N N 381 
THR OXT HXT  sing N N 382 
TRP N   CA   sing N N 383 
TRP N   H    sing N N 384 
TRP N   H2   sing N N 385 
TRP CA  C    sing N N 386 
TRP CA  CB   sing N N 387 
TRP CA  HA   sing N N 388 
TRP C   O    doub N N 389 
TRP C   OXT  sing N N 390 
TRP CB  CG   sing N N 391 
TRP CB  HB2  sing N N 392 
TRP CB  HB3  sing N N 393 
TRP CG  CD1  doub Y N 394 
TRP CG  CD2  sing Y N 395 
TRP CD1 NE1  sing Y N 396 
TRP CD1 HD1  sing N N 397 
TRP CD2 CE2  doub Y N 398 
TRP CD2 CE3  sing Y N 399 
TRP NE1 CE2  sing Y N 400 
TRP NE1 HE1  sing N N 401 
TRP CE2 CZ2  sing Y N 402 
TRP CE3 CZ3  doub Y N 403 
TRP CE3 HE3  sing N N 404 
TRP CZ2 CH2  doub Y N 405 
TRP CZ2 HZ2  sing N N 406 
TRP CZ3 CH2  sing Y N 407 
TRP CZ3 HZ3  sing N N 408 
TRP CH2 HH2  sing N N 409 
TRP OXT HXT  sing N N 410 
TYR N   CA   sing N N 411 
TYR N   H    sing N N 412 
TYR N   H2   sing N N 413 
TYR CA  C    sing N N 414 
TYR CA  CB   sing N N 415 
TYR CA  HA   sing N N 416 
TYR C   O    doub N N 417 
TYR C   OXT  sing N N 418 
TYR CB  CG   sing N N 419 
TYR CB  HB2  sing N N 420 
TYR CB  HB3  sing N N 421 
TYR CG  CD1  doub Y N 422 
TYR CG  CD2  sing Y N 423 
TYR CD1 CE1  sing Y N 424 
TYR CD1 HD1  sing N N 425 
TYR CD2 CE2  doub Y N 426 
TYR CD2 HD2  sing N N 427 
TYR CE1 CZ   doub Y N 428 
TYR CE1 HE1  sing N N 429 
TYR CE2 CZ   sing Y N 430 
TYR CE2 HE2  sing N N 431 
TYR CZ  OH   sing N N 432 
TYR OH  HH   sing N N 433 
TYR OXT HXT  sing N N 434 
VAL N   CA   sing N N 435 
VAL N   H    sing N N 436 
VAL N   H2   sing N N 437 
VAL CA  C    sing N N 438 
VAL CA  CB   sing N N 439 
VAL CA  HA   sing N N 440 
VAL C   O    doub N N 441 
VAL C   OXT  sing N N 442 
VAL CB  CG1  sing N N 443 
VAL CB  CG2  sing N N 444 
VAL CB  HB   sing N N 445 
VAL CG1 HG11 sing N N 446 
VAL CG1 HG12 sing N N 447 
VAL CG1 HG13 sing N N 448 
VAL CG2 HG21 sing N N 449 
VAL CG2 HG22 sing N N 450 
VAL CG2 HG23 sing N N 451 
VAL OXT HXT  sing N N 452 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-08-22 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9DAK 
_em_admin.last_update        2025-04-02 
_em_admin.map_release_date   2025-02-19 
_em_admin.title              'Merbecovirus PnNL2018B Spike glycoprotein RBD bound to the P. Nathusii ACE2' 
# 
_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' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                ? 
_em_entity_assembly_molwt.value                ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          2509494 
_em_entity_assembly_naturalsource.organism             Merbecovirus 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   1 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         60 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 (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                     ? 
# 
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 ? ? ?         ? 
'IMAGE ACQUISITION'        ? 2  ? ? 1 Leginon   ? 
MASKING                    ? 3  ? ? ? ?         ? 
'CTF CORRECTION'           ? 4  1 ? ? ?         ? 
'LAYERLINE INDEXING'       ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'     ? 6  ? ? ? ?         ? 
'MODEL FITTING'            ? 7  ? ? ? ?         ? 
'MODEL REFINEMENT'         ? 8  ? ? ? ?         ? 
OTHER                      ? 9  ? ? ? ?         ? 
'INITIAL EULER ASSIGNMENT' ? 10 1 ? ? ?         ? 
'FINAL EULER ASSIGNMENT'   ? 11 1 ? ? ?         ? 
CLASSIFICATION             ? 12 1 ? ? ?         ? 
RECONSTRUCTION             ? 13 1 ? ? cryoSPARC ? 
# 
_em_specimen.concentration           ? 
_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   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           AI158186 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
3 NAG 1 n 
3 NAG 2 n 
3 FUC 3 n 
4 NAG 1 n 
4 NAG 2 n 
5 NAG 1 n 
5 NAG 2 n 
5 BMA 3 n 
# 
_atom_sites.entry_id                    9DAK 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   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  
ZN 
# 
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   . LEU A 1 110 ? 163.195 226.801 167.186 1.00 13.86  ? 20   LEU A N   1 
ATOM   2    C  CA  . LEU A 1 110 ? 164.268 225.858 166.888 1.00 13.70  ? 20   LEU A CA  1 
ATOM   3    C  C   . LEU A 1 110 ? 164.397 225.635 165.385 1.00 13.57  ? 20   LEU A C   1 
ATOM   4    O  O   . LEU A 1 110 ? 163.425 225.790 164.638 1.00 13.74  ? 20   LEU A O   1 
ATOM   5    C  CB  . LEU A 1 110 ? 164.011 224.495 167.578 1.00 13.72  ? 20   LEU A CB  1 
ATOM   6    C  CG  . LEU A 1 110 ? 163.946 224.472 169.149 1.00 13.72  ? 20   LEU A CG  1 
ATOM   7    C  CD1 . LEU A 1 110 ? 163.561 223.043 169.617 1.00 13.23  ? 20   LEU A CD1 1 
ATOM   8    C  CD2 . LEU A 1 110 ? 165.312 224.891 169.741 1.00 13.75  ? 20   LEU A CD2 1 
ATOM   9    N  N   . THR A 1 111 ? 165.597 225.233 164.954 1.00 13.61  ? 21   THR A N   1 
ATOM   10   C  CA  . THR A 1 111 ? 165.877 224.879 163.563 1.00 13.28  ? 21   THR A CA  1 
ATOM   11   C  C   . THR A 1 111 ? 165.620 223.396 163.347 1.00 13.39  ? 21   THR A C   1 
ATOM   12   O  O   . THR A 1 111 ? 165.406 222.653 164.304 1.00 12.80  ? 21   THR A O   1 
ATOM   13   C  CB  . THR A 1 111 ? 167.327 225.219 163.183 1.00 13.43  ? 21   THR A CB  1 
ATOM   14   O  OG1 . THR A 1 111 ? 168.228 224.389 163.924 1.00 13.35  ? 21   THR A OG1 1 
ATOM   15   C  CG2 . THR A 1 111 ? 167.610 226.677 163.505 1.00 13.86  ? 21   THR A CG2 1 
ATOM   16   N  N   . THR A 1 112 ? 165.646 222.962 162.094 1.00 13.07  ? 22   THR A N   1 
ATOM   17   C  CA  . THR A 1 112 ? 165.390 221.562 161.782 1.00 12.75  ? 22   THR A CA  1 
ATOM   18   C  C   . THR A 1 112 ? 166.381 220.636 162.469 1.00 12.58  ? 22   THR A C   1 
ATOM   19   O  O   . THR A 1 112 ? 166.002 219.588 162.990 1.00 12.35  ? 22   THR A O   1 
ATOM   20   C  CB  . THR A 1 112 ? 165.421 221.315 160.266 1.00 12.84  ? 22   THR A CB  1 
ATOM   21   O  OG1 . THR A 1 112 ? 164.372 222.063 159.646 1.00 13.07  ? 22   THR A OG1 1 
ATOM   22   C  CG2 . THR A 1 112 ? 165.231 219.825 159.967 1.00 12.27  ? 22   THR A CG2 1 
ATOM   23   N  N   . GLU A 1 113 ? 167.653 221.013 162.460 1.00 12.72  ? 23   GLU A N   1 
ATOM   24   C  CA  . GLU A 1 113 ? 168.684 220.186 163.067 1.00 12.62  ? 23   GLU A CA  1 
ATOM   25   C  C   . GLU A 1 113 ? 168.464 220.021 164.565 1.00 12.65  ? 23   GLU A C   1 
ATOM   26   O  O   . GLU A 1 113 ? 168.640 218.930 165.109 1.00 12.28  ? 23   GLU A O   1 
ATOM   27   C  CB  . GLU A 1 113 ? 170.062 220.779 162.805 1.00 12.61  ? 23   GLU A CB  1 
ATOM   28   C  CG  . GLU A 1 113 ? 171.207 219.912 163.270 1.00 12.60  ? 23   GLU A CG  1 
ATOM   29   C  CD  . GLU A 1 113 ? 172.531 220.459 162.865 1.00 12.82  ? 23   GLU A CD  1 
ATOM   30   O  OE1 . GLU A 1 113 ? 172.990 221.380 163.494 1.00 13.59  ? 23   GLU A OE1 1 
ATOM   31   O  OE2 . GLU A 1 113 ? 173.084 219.973 161.901 1.00 12.78  ? 23   GLU A OE2 1 
ATOM   32   N  N   . GLU A 1 114 ? 168.072 221.102 165.229 1.00 12.55  ? 24   GLU A N   1 
ATOM   33   C  CA  . GLU A 1 114 ? 167.818 221.068 166.662 1.00 12.77  ? 24   GLU A CA  1 
ATOM   34   C  C   . GLU A 1 114 ? 166.617 220.189 166.990 1.00 12.34  ? 24   GLU A C   1 
ATOM   35   O  O   . GLU A 1 114 ? 166.643 219.426 167.956 1.00 12.19  ? 24   GLU A O   1 
ATOM   36   C  CB  . GLU A 1 114 ? 167.597 222.484 167.186 1.00 12.95  ? 24   GLU A CB  1 
ATOM   37   C  CG  . GLU A 1 114 ? 168.849 223.338 167.197 1.00 13.35  ? 24   GLU A CG  1 
ATOM   38   C  CD  . GLU A 1 114 ? 168.588 224.770 167.550 1.00 13.83  ? 24   GLU A CD  1 
ATOM   39   O  OE1 . GLU A 1 114 ? 167.555 225.281 167.179 1.00 13.78  ? 24   GLU A OE1 1 
ATOM   40   O  OE2 . GLU A 1 114 ? 169.424 225.359 168.193 1.00 14.28  ? 24   GLU A OE2 1 
ATOM   41   N  N   . LYS A 1 115 ? 165.580 220.270 166.163 1.00 12.37  ? 25   LYS A N   1 
ATOM   42   C  CA  . LYS A 1 115 ? 164.399 219.440 166.356 1.00 12.10  ? 25   LYS A CA  1 
ATOM   43   C  C   . LYS A 1 115 ? 164.730 217.973 166.118 1.00 11.95  ? 25   LYS A C   1 
ATOM   44   O  O   . LYS A 1 115 ? 164.255 217.095 166.840 1.00 11.60  ? 25   LYS A O   1 
ATOM   45   C  CB  . LYS A 1 115 ? 163.275 219.884 165.425 1.00 12.23  ? 25   LYS A CB  1 
ATOM   46   C  CG  . LYS A 1 115 ? 162.671 221.232 165.769 1.00 12.65  ? 25   LYS A CG  1 
ATOM   47   C  CD  . LYS A 1 115 ? 161.614 221.630 164.754 1.00 13.15  ? 25   LYS A CD  1 
ATOM   48   C  CE  . LYS A 1 115 ? 161.055 223.012 165.045 1.00 13.80  ? 25   LYS A CE  1 
ATOM   49   N  NZ  . LYS A 1 115 ? 160.052 223.427 164.027 1.00 13.95  ? 25   LYS A NZ  1 
ATOM   50   N  N   . ALA A 1 116 ? 165.558 217.710 165.110 1.00 11.81  ? 26   ALA A N   1 
ATOM   51   C  CA  . ALA A 1 116 ? 165.985 216.351 164.804 1.00 11.55  ? 26   ALA A CA  1 
ATOM   52   C  C   . ALA A 1 116 ? 166.794 215.824 165.976 1.00 11.55  ? 26   ALA A C   1 
ATOM   53   O  O   . ALA A 1 116 ? 166.720 214.642 166.310 1.00 11.19  ? 26   ALA A O   1 
ATOM   54   C  CB  . ALA A 1 116 ? 166.820 216.327 163.537 1.00 11.50  ? 26   ALA A CB  1 
ATOM   55   N  N   . ARG A 1 117 ? 167.555 216.710 166.609 1.00 11.75  ? 27   ARG A N   1 
ATOM   56   C  CA  . ARG A 1 117 ? 168.365 216.339 167.759 1.00 11.74  ? 27   ARG A CA  1 
ATOM   57   C  C   . ARG A 1 117 ? 167.486 215.818 168.888 1.00 11.53  ? 27   ARG A C   1 
ATOM   58   O  O   . ARG A 1 117 ? 167.719 214.729 169.411 1.00 11.29  ? 27   ARG A O   1 
ATOM   59   C  CB  . ARG A 1 117 ? 169.191 217.524 168.223 1.00 12.13  ? 27   ARG A CB  1 
ATOM   60   C  CG  . ARG A 1 117 ? 170.177 217.235 169.334 1.00 12.32  ? 27   ARG A CG  1 
ATOM   61   C  CD  . ARG A 1 117 ? 170.894 218.465 169.742 1.00 12.63  ? 27   ARG A CD  1 
ATOM   62   N  NE  . ARG A 1 117 ? 171.732 218.980 168.667 1.00 13.02  ? 27   ARG A NE  1 
ATOM   63   C  CZ  . ARG A 1 117 ? 172.985 218.560 168.386 1.00 13.43  ? 27   ARG A CZ  1 
ATOM   64   N  NH1 . ARG A 1 117 ? 173.550 217.611 169.105 1.00 13.32  ? 27   ARG A NH1 1 
ATOM   65   N  NH2 . ARG A 1 117 ? 173.649 219.106 167.382 1.00 13.11  ? 27   ARG A NH2 1 
ATOM   66   N  N   . GLU A 1 118 ? 166.442 216.574 169.228 1.00 11.58  ? 28   GLU A N   1 
ATOM   67   C  CA  . GLU A 1 118 ? 165.516 216.150 170.273 1.00 11.52  ? 28   GLU A CA  1 
ATOM   68   C  C   . GLU A 1 118 ? 164.782 214.858 169.937 1.00 11.17  ? 28   GLU A C   1 
ATOM   69   O  O   . GLU A 1 118 ? 164.589 213.999 170.799 1.00 11.05  ? 28   GLU A O   1 
ATOM   70   C  CB  . GLU A 1 118 ? 164.498 217.264 170.513 1.00 11.73  ? 28   GLU A CB  1 
ATOM   71   C  CG  . GLU A 1 118 ? 165.065 218.514 171.157 1.00 12.05  ? 28   GLU A CG  1 
ATOM   72   C  CD  . GLU A 1 118 ? 164.022 219.572 171.387 1.00 12.82  ? 28   GLU A CD  1 
ATOM   73   O  OE1 . GLU A 1 118 ? 162.940 219.434 170.868 1.00 12.54  ? 28   GLU A OE1 1 
ATOM   74   O  OE2 . GLU A 1 118 ? 164.305 220.516 172.088 1.00 13.28  ? 28   GLU A OE2 1 
ATOM   75   N  N   . PHE A 1 119 ? 164.403 214.716 168.673 1.00 11.08  ? 29   PHE A N   1 
ATOM   76   C  CA  . PHE A 1 119 ? 163.721 213.521 168.199 1.00 10.88  ? 29   PHE A CA  1 
ATOM   77   C  C   . PHE A 1 119 ? 164.565 212.277 168.425 1.00 10.88  ? 29   PHE A C   1 
ATOM   78   O  O   . PHE A 1 119 ? 164.086 211.284 168.974 1.00 10.52  ? 29   PHE A O   1 
ATOM   79   C  CB  . PHE A 1 119 ? 163.380 213.668 166.715 1.00 10.86  ? 29   PHE A CB  1 
ATOM   80   C  CG  . PHE A 1 119 ? 162.872 212.422 166.061 1.00 10.74  ? 29   PHE A CG  1 
ATOM   81   C  CD1 . PHE A 1 119 ? 163.698 211.684 165.230 1.00 10.57  ? 29   PHE A CD1 1 
ATOM   82   C  CD2 . PHE A 1 119 ? 161.579 211.984 166.267 1.00 10.47  ? 29   PHE A CD2 1 
ATOM   83   C  CE1 . PHE A 1 119 ? 163.241 210.539 164.622 1.00 10.39  ? 29   PHE A CE1 1 
ATOM   84   C  CE2 . PHE A 1 119 ? 161.121 210.838 165.660 1.00 10.43  ? 29   PHE A CE2 1 
ATOM   85   C  CZ  . PHE A 1 119 ? 161.953 210.115 164.838 1.00 10.34  ? 29   PHE A CZ  1 
ATOM   86   N  N   . LEU A 1 120 ? 165.826 212.330 168.006 1.00 10.76  ? 30   LEU A N   1 
ATOM   87   C  CA  . LEU A 1 120 ? 166.709 211.183 168.140 1.00 10.65  ? 30   LEU A CA  1 
ATOM   88   C  C   . LEU A 1 120 ? 167.013 210.854 169.595 1.00 10.62  ? 30   LEU A C   1 
ATOM   89   O  O   . LEU A 1 120 ? 167.091 209.684 169.959 1.00 10.21  ? 30   LEU A O   1 
ATOM   90   C  CB  . LEU A 1 120 ? 168.016 211.418 167.379 1.00 10.56  ? 30   LEU A CB  1 
ATOM   91   C  CG  . LEU A 1 120 ? 167.920 211.423 165.840 1.00 10.39  ? 30   LEU A CG  1 
ATOM   92   C  CD1 . LEU A 1 120 ? 169.248 211.871 165.269 1.00 10.34  ? 30   LEU A CD1 1 
ATOM   93   C  CD2 . LEU A 1 120 ? 167.562 210.026 165.333 1.00 9.98   ? 30   LEU A CD2 1 
ATOM   94   N  N   . ASP A 1 121 ? 167.171 211.873 170.436 1.00 10.67  ? 31   ASP A N   1 
ATOM   95   C  CA  . ASP A 1 121 ? 167.462 211.617 171.841 1.00 10.60  ? 31   ASP A CA  1 
ATOM   96   C  C   . ASP A 1 121 ? 166.333 210.839 172.504 1.00 10.61  ? 31   ASP A C   1 
ATOM   97   O  O   . ASP A 1 121 ? 166.577 209.885 173.246 1.00 10.36  ? 31   ASP A O   1 
ATOM   98   C  CB  . ASP A 1 121 ? 167.697 212.922 172.602 1.00 11.02  ? 31   ASP A CB  1 
ATOM   99   C  CG  . ASP A 1 121 ? 169.047 213.567 172.306 1.00 11.45  ? 31   ASP A CG  1 
ATOM   100  O  OD1 . ASP A 1 121 ? 169.892 212.915 171.740 1.00 11.28  ? 31   ASP A OD1 1 
ATOM   101  O  OD2 . ASP A 1 121 ? 169.224 214.707 172.663 1.00 11.86  ? 31   ASP A OD2 1 
ATOM   102  N  N   . LYS A 1 122 ? 165.095 211.224 172.211 1.00 10.64  ? 32   LYS A N   1 
ATOM   103  C  CA  . LYS A 1 122 ? 163.942 210.530 172.768 1.00 10.26  ? 32   LYS A CA  1 
ATOM   104  C  C   . LYS A 1 122 ? 163.829 209.119 172.206 1.00 10.57  ? 32   LYS A C   1 
ATOM   105  O  O   . LYS A 1 122 ? 163.582 208.166 172.946 1.00 10.32  ? 32   LYS A O   1 
ATOM   106  C  CB  . LYS A 1 122 ? 162.660 211.312 172.497 1.00 10.47  ? 32   LYS A CB  1 
ATOM   107  C  CG  . LYS A 1 122 ? 161.416 210.703 173.122 1.00 10.59  ? 32   LYS A CG  1 
ATOM   108  C  CD  . LYS A 1 122 ? 160.203 211.593 172.923 1.00 10.62  ? 32   LYS A CD  1 
ATOM   109  C  CE  . LYS A 1 122 ? 158.959 210.972 173.541 1.00 10.84  ? 32   LYS A CE  1 
ATOM   110  N  NZ  . LYS A 1 122 ? 157.761 211.836 173.367 1.00 11.00  ? 32   LYS A NZ  1 
ATOM   111  N  N   . PHE A 1 123 ? 164.030 208.983 170.898 1.00 10.20  ? 33   PHE A N   1 
ATOM   112  C  CA  . PHE A 1 123 ? 163.956 207.682 170.253 1.00 10.26  ? 33   PHE A CA  1 
ATOM   113  C  C   . PHE A 1 123 ? 164.962 206.707 170.839 1.00 10.17  ? 33   PHE A C   1 
ATOM   114  O  O   . PHE A 1 123 ? 164.615 205.573 171.155 1.00 9.46   ? 33   PHE A O   1 
ATOM   115  C  CB  . PHE A 1 123 ? 164.199 207.798 168.749 1.00 10.09  ? 33   PHE A CB  1 
ATOM   116  C  CG  . PHE A 1 123 ? 164.350 206.465 168.079 1.00 9.84   ? 33   PHE A CG  1 
ATOM   117  C  CD1 . PHE A 1 123 ? 163.246 205.705 167.754 1.00 9.96   ? 33   PHE A CD1 1 
ATOM   118  C  CD2 . PHE A 1 123 ? 165.604 205.963 167.789 1.00 9.62   ? 33   PHE A CD2 1 
ATOM   119  C  CE1 . PHE A 1 123 ? 163.388 204.475 167.153 1.00 9.86   ? 33   PHE A CE1 1 
ATOM   120  C  CE2 . PHE A 1 123 ? 165.749 204.734 167.196 1.00 9.48   ? 33   PHE A CE2 1 
ATOM   121  C  CZ  . PHE A 1 123 ? 164.640 203.988 166.876 1.00 9.56   ? 33   PHE A CZ  1 
ATOM   122  N  N   . ASN A 1 124 ? 166.213 207.138 170.958 1.00 9.63   ? 34   ASN A N   1 
ATOM   123  C  CA  . ASN A 1 124 ? 167.277 206.257 171.414 1.00 9.84   ? 34   ASN A CA  1 
ATOM   124  C  C   . ASN A 1 124 ? 167.032 205.759 172.832 1.00 9.83   ? 34   ASN A C   1 
ATOM   125  O  O   . ASN A 1 124 ? 167.328 204.607 173.149 1.00 9.65   ? 34   ASN A O   1 
ATOM   126  C  CB  . ASN A 1 124 ? 168.619 206.958 171.313 1.00 9.68   ? 34   ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 124 ? 169.128 207.047 169.892 1.00 9.22   ? 34   ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 124 ? 168.853 206.175 169.062 1.00 9.04   ? 34   ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 124 ? 169.860 208.090 169.598 1.00 9.32   ? 34   ASN A ND2 1 
ATOM   130  N  N   . SER A 1 125 ? 166.469 206.612 173.681 1.00 9.94   ? 35   SER A N   1 
ATOM   131  C  CA  . SER A 1 125 ? 166.176 206.206 175.049 1.00 9.94   ? 35   SER A CA  1 
ATOM   132  C  C   . SER A 1 125 ? 165.124 205.104 175.081 1.00 10.15  ? 35   SER A C   1 
ATOM   133  O  O   . SER A 1 125 ? 165.305 204.076 175.738 1.00 9.98   ? 35   SER A O   1 
ATOM   134  C  CB  . SER A 1 125 ? 165.702 207.397 175.855 1.00 10.05  ? 35   SER A CB  1 
ATOM   135  O  OG  . SER A 1 125 ? 165.422 207.029 177.178 1.00 10.28  ? 35   SER A OG  1 
ATOM   136  N  N   . GLU A 1 126 ? 164.032 205.310 174.352 1.00 9.86   ? 36   GLU A N   1 
ATOM   137  C  CA  . GLU A 1 126 ? 162.955 204.330 174.309 1.00 10.18  ? 36   GLU A CA  1 
ATOM   138  C  C   . GLU A 1 126 ? 163.378 203.066 173.574 1.00 10.26  ? 36   GLU A C   1 
ATOM   139  O  O   . GLU A 1 126 ? 163.003 201.959 173.960 1.00 9.59   ? 36   GLU A O   1 
ATOM   140  C  CB  . GLU A 1 126 ? 161.716 204.930 173.646 1.00 10.12  ? 36   GLU A CB  1 
ATOM   141  C  CG  . GLU A 1 126 ? 161.025 206.004 174.476 1.00 10.36  ? 36   GLU A CG  1 
ATOM   142  C  CD  . GLU A 1 126 ? 159.836 206.615 173.786 1.00 10.80  ? 36   GLU A CD  1 
ATOM   143  O  OE1 . GLU A 1 126 ? 159.756 206.520 172.586 1.00 10.73  ? 36   GLU A OE1 1 
ATOM   144  O  OE2 . GLU A 1 126 ? 159.004 207.172 174.461 1.00 10.96  ? 36   GLU A OE2 1 
ATOM   145  N  N   . ALA A 1 127 ? 164.164 203.230 172.517 1.00 9.79   ? 37   ALA A N   1 
ATOM   146  C  CA  . ALA A 1 127 ? 164.597 202.101 171.709 1.00 9.88   ? 37   ALA A CA  1 
ATOM   147  C  C   . ALA A 1 127 ? 165.411 201.121 172.536 1.00 9.79   ? 37   ALA A C   1 
ATOM   148  O  O   . ALA A 1 127 ? 165.287 199.909 172.368 1.00 9.63   ? 37   ALA A O   1 
ATOM   149  C  CB  . ALA A 1 127 ? 165.398 202.587 170.513 1.00 9.54   ? 37   ALA A CB  1 
ATOM   150  N  N   . GLU A 1 128 ? 166.222 201.641 173.454 1.00 9.71   ? 38   GLU A N   1 
ATOM   151  C  CA  . GLU A 1 128 ? 167.024 200.789 174.325 1.00 9.79   ? 38   GLU A CA  1 
ATOM   152  C  C   . GLU A 1 128 ? 166.128 199.958 175.233 1.00 9.94   ? 38   GLU A C   1 
ATOM   153  O  O   . GLU A 1 128 ? 166.351 198.762 175.421 1.00 9.83   ? 38   GLU A O   1 
ATOM   154  C  CB  . GLU A 1 128 ? 167.969 201.649 175.172 1.00 9.68   ? 38   GLU A CB  1 
ATOM   155  C  CG  . GLU A 1 128 ? 168.906 200.884 176.125 1.00 9.74   ? 38   GLU A CG  1 
ATOM   156  C  CD  . GLU A 1 128 ? 170.012 200.128 175.437 1.00 9.19   ? 38   GLU A CD  1 
ATOM   157  O  OE1 . GLU A 1 128 ? 169.856 199.778 174.294 1.00 9.19   ? 38   GLU A OE1 1 
ATOM   158  O  OE2 . GLU A 1 128 ? 171.038 199.932 176.056 1.00 8.97   ? 38   GLU A OE2 1 
ATOM   159  N  N   . ASN A 1 129 ? 165.092 200.588 175.784 1.00 9.67   ? 39   ASN A N   1 
ATOM   160  C  CA  . ASN A 1 129 ? 164.174 199.892 176.674 1.00 9.70   ? 39   ASN A CA  1 
ATOM   161  C  C   . ASN A 1 129 ? 163.445 198.757 175.963 1.00 10.04  ? 39   ASN A C   1 
ATOM   162  O  O   . ASN A 1 129 ? 163.358 197.641 176.482 1.00 10.01  ? 39   ASN A O   1 
ATOM   163  C  CB  . ASN A 1 129 ? 163.161 200.860 177.260 1.00 9.86   ? 39   ASN A CB  1 
ATOM   164  C  CG  . ASN A 1 129 ? 163.750 201.826 178.252 1.00 10.02  ? 39   ASN A CG  1 
ATOM   165  O  OD1 . ASN A 1 129 ? 163.041 202.708 178.754 1.00 10.20  ? 39   ASN A OD1 1 
ATOM   166  N  ND2 . ASN A 1 129 ? 165.018 201.690 178.544 1.00 10.18  ? 39   ASN A ND2 1 
ATOM   167  N  N   . TRP A 1 130 ? 162.909 199.047 174.783 1.00 9.80   ? 40   TRP A N   1 
ATOM   168  C  CA  . TRP A 1 130 ? 162.132 198.063 174.040 1.00 10.21  ? 40   TRP A CA  1 
ATOM   169  C  C   . TRP A 1 130 ? 163.005 196.937 173.507 1.00 10.30  ? 40   TRP A C   1 
ATOM   170  O  O   . TRP A 1 130 ? 162.617 195.769 173.540 1.00 10.13  ? 40   TRP A O   1 
ATOM   171  C  CB  . TRP A 1 130 ? 161.405 198.725 172.872 1.00 10.12  ? 40   TRP A CB  1 
ATOM   172  C  CG  . TRP A 1 130 ? 160.279 199.606 173.281 1.00 10.27  ? 40   TRP A CG  1 
ATOM   173  C  CD1 . TRP A 1 130 ? 160.209 200.957 173.153 1.00 10.27  ? 40   TRP A CD1 1 
ATOM   174  C  CD2 . TRP A 1 130 ? 159.042 199.198 173.894 1.00 10.55  ? 40   TRP A CD2 1 
ATOM   175  N  NE1 . TRP A 1 130 ? 159.019 201.416 173.646 1.00 10.44  ? 40   TRP A NE1 1 
ATOM   176  C  CE2 . TRP A 1 130 ? 158.292 200.354 174.104 1.00 10.63  ? 40   TRP A CE2 1 
ATOM   177  C  CE3 . TRP A 1 130 ? 158.516 197.962 174.277 1.00 10.92  ? 40   TRP A CE3 1 
ATOM   178  C  CZ2 . TRP A 1 130 ? 157.040 200.317 174.684 1.00 10.84  ? 40   TRP A CZ2 1 
ATOM   179  C  CZ3 . TRP A 1 130 ? 157.262 197.924 174.858 1.00 11.41  ? 40   TRP A CZ3 1 
ATOM   180  C  CH2 . TRP A 1 130 ? 156.542 199.071 175.057 1.00 11.60  ? 40   TRP A CH2 1 
ATOM   181  N  N   . SER A 1 131 ? 164.191 197.289 173.026 1.00 9.77   ? 41   SER A N   1 
ATOM   182  C  CA  . SER A 1 131 ? 165.119 196.308 172.486 1.00 10.00  ? 41   SER A CA  1 
ATOM   183  C  C   . SER A 1 131 ? 165.541 195.320 173.565 1.00 10.03  ? 41   SER A C   1 
ATOM   184  O  O   . SER A 1 131 ? 165.673 194.125 173.308 1.00 10.14  ? 41   SER A O   1 
ATOM   185  C  CB  . SER A 1 131 ? 166.331 196.999 171.902 1.00 9.88   ? 41   SER A CB  1 
ATOM   186  O  OG  . SER A 1 131 ? 167.219 196.069 171.349 1.00 10.43  ? 41   SER A OG  1 
ATOM   187  N  N   . HIS A 1 132 ? 165.745 195.824 174.778 1.00 9.86   ? 42   HIS A N   1 
ATOM   188  C  CA  . HIS A 1 132 ? 166.135 194.985 175.902 1.00 9.82   ? 42   HIS A CA  1 
ATOM   189  C  C   . HIS A 1 132 ? 165.088 193.915 176.191 1.00 10.29  ? 42   HIS A C   1 
ATOM   190  O  O   . HIS A 1 132 ? 165.423 192.745 176.373 1.00 10.04  ? 42   HIS A O   1 
ATOM   191  C  CB  . HIS A 1 132 ? 166.356 195.838 177.153 1.00 9.81   ? 42   HIS A CB  1 
ATOM   192  C  CG  . HIS A 1 132 ? 166.916 195.084 178.315 1.00 9.69   ? 42   HIS A CG  1 
ATOM   193  N  ND1 . HIS A 1 132 ? 168.225 194.673 178.363 1.00 9.40   ? 42   HIS A ND1 1 
ATOM   194  C  CD2 . HIS A 1 132 ? 166.352 194.675 179.470 1.00 9.88   ? 42   HIS A CD2 1 
ATOM   195  C  CE1 . HIS A 1 132 ? 168.446 194.041 179.496 1.00 9.49   ? 42   HIS A CE1 1 
ATOM   196  N  NE2 . HIS A 1 132 ? 167.327 194.030 180.189 1.00 9.72   ? 42   HIS A NE2 1 
ATOM   197  N  N   . GLU A 1 133 ? 163.814 194.309 176.223 1.00 10.03  ? 43   GLU A N   1 
ATOM   198  C  CA  . GLU A 1 133 ? 162.746 193.361 176.524 1.00 10.24  ? 43   GLU A CA  1 
ATOM   199  C  C   . GLU A 1 133 ? 162.651 192.271 175.463 1.00 10.52  ? 43   GLU A C   1 
ATOM   200  O  O   . GLU A 1 133 ? 162.447 191.097 175.782 1.00 10.76  ? 43   GLU A O   1 
ATOM   201  C  CB  . GLU A 1 133 ? 161.409 194.087 176.647 1.00 10.25  ? 43   GLU A CB  1 
ATOM   202  C  CG  . GLU A 1 133 ? 161.317 195.008 177.845 1.00 10.29  ? 43   GLU A CG  1 
ATOM   203  C  CD  . GLU A 1 133 ? 161.502 194.286 179.144 1.00 10.71  ? 43   GLU A CD  1 
ATOM   204  O  OE1 . GLU A 1 133 ? 160.855 193.289 179.347 1.00 11.14  ? 43   GLU A OE1 1 
ATOM   205  O  OE2 . GLU A 1 133 ? 162.299 194.730 179.935 1.00 10.70  ? 43   GLU A OE2 1 
ATOM   206  N  N   . SER A 1 134 ? 162.848 192.651 174.206 1.00 10.36  ? 44   SER A N   1 
ATOM   207  C  CA  . SER A 1 134 ? 162.872 191.685 173.115 1.00 10.81  ? 44   SER A CA  1 
ATOM   208  C  C   . SER A 1 134 ? 164.022 190.704 173.278 1.00 10.92  ? 44   SER A C   1 
ATOM   209  O  O   . SER A 1 134 ? 163.839 189.491 173.151 1.00 11.14  ? 44   SER A O   1 
ATOM   210  C  CB  . SER A 1 134 ? 162.988 192.408 171.787 1.00 11.01  ? 44   SER A CB  1 
ATOM   211  O  OG  . SER A 1 134 ? 163.191 191.503 170.731 1.00 11.77  ? 44   SER A OG  1 
ATOM   212  N  N   . ALA A 1 135 ? 165.207 191.228 173.582 1.00 10.81  ? 45   ALA A N   1 
ATOM   213  C  CA  . ALA A 1 135 ? 166.391 190.394 173.735 1.00 10.61  ? 45   ALA A CA  1 
ATOM   214  C  C   . ALA A 1 135 ? 166.229 189.394 174.870 1.00 10.76  ? 45   ALA A C   1 
ATOM   215  O  O   . ALA A 1 135 ? 166.638 188.238 174.742 1.00 10.80  ? 45   ALA A O   1 
ATOM   216  C  CB  . ALA A 1 135 ? 167.612 191.262 173.975 1.00 10.17  ? 45   ALA A CB  1 
ATOM   217  N  N   . LEU A 1 136 ? 165.618 189.820 175.973 1.00 10.60  ? 46   LEU A N   1 
ATOM   218  C  CA  . LEU A 1 136 ? 165.417 188.919 177.101 1.00 10.68  ? 46   LEU A CA  1 
ATOM   219  C  C   . LEU A 1 136 ? 164.484 187.779 176.741 1.00 11.21  ? 46   LEU A C   1 
ATOM   220  O  O   . LEU A 1 136 ? 164.756 186.624 177.068 1.00 11.15  ? 46   LEU A O   1 
ATOM   221  C  CB  . LEU A 1 136 ? 164.826 189.666 178.300 1.00 10.59  ? 46   LEU A CB  1 
ATOM   222  C  CG  . LEU A 1 136 ? 165.749 190.626 179.045 1.00 10.35  ? 46   LEU A CG  1 
ATOM   223  C  CD1 . LEU A 1 136 ? 164.914 191.437 180.017 1.00 10.40  ? 46   LEU A CD1 1 
ATOM   224  C  CD2 . LEU A 1 136 ? 166.820 189.840 179.790 1.00 10.33  ? 46   LEU A CD2 1 
ATOM   225  N  N   . ALA A 1 137 ? 163.391 188.093 176.055 1.00 11.10  ? 47   ALA A N   1 
ATOM   226  C  CA  . ALA A 1 137 ? 162.431 187.065 175.685 1.00 11.28  ? 47   ALA A CA  1 
ATOM   227  C  C   . ALA A 1 137 ? 163.059 186.052 174.742 1.00 11.47  ? 47   ALA A C   1 
ATOM   228  O  O   . ALA A 1 137 ? 162.844 184.846 174.881 1.00 11.79  ? 47   ALA A O   1 
ATOM   229  C  CB  . ALA A 1 137 ? 161.208 187.696 175.046 1.00 11.71  ? 47   ALA A CB  1 
ATOM   230  N  N   . SER A 1 138 ? 163.867 186.537 173.806 1.00 11.35  ? 48   SER A N   1 
ATOM   231  C  CA  . SER A 1 138 ? 164.538 185.662 172.859 1.00 11.38  ? 48   SER A CA  1 
ATOM   232  C  C   . SER A 1 138 ? 165.528 184.753 173.576 1.00 11.48  ? 48   SER A C   1 
ATOM   233  O  O   . SER A 1 138 ? 165.593 183.554 173.303 1.00 11.59  ? 48   SER A O   1 
ATOM   234  C  CB  . SER A 1 138 ? 165.237 186.479 171.794 1.00 11.45  ? 48   SER A CB  1 
ATOM   235  O  OG  . SER A 1 138 ? 165.857 185.649 170.851 1.00 11.58  ? 48   SER A OG  1 
ATOM   236  N  N   . TRP A 1 139 ? 166.287 185.320 174.509 1.00 11.06  ? 49   TRP A N   1 
ATOM   237  C  CA  . TRP A 1 139 ? 167.236 184.540 175.292 1.00 11.18  ? 49   TRP A CA  1 
ATOM   238  C  C   . TRP A 1 139 ? 166.540 183.401 176.017 1.00 12.86  ? 49   TRP A C   1 
ATOM   239  O  O   . TRP A 1 139 ? 166.966 182.249 175.928 1.00 11.36  ? 49   TRP A O   1 
ATOM   240  C  CB  . TRP A 1 139 ? 167.950 185.423 176.315 1.00 10.84  ? 49   TRP A CB  1 
ATOM   241  C  CG  . TRP A 1 139 ? 168.876 184.663 177.228 1.00 10.79  ? 49   TRP A CG  1 
ATOM   242  C  CD1 . TRP A 1 139 ? 168.575 184.181 178.463 1.00 10.75  ? 49   TRP A CD1 1 
ATOM   243  C  CD2 . TRP A 1 139 ? 170.256 184.303 176.986 1.00 10.39  ? 49   TRP A CD2 1 
ATOM   244  N  NE1 . TRP A 1 139 ? 169.666 183.552 179.003 1.00 10.61  ? 49   TRP A NE1 1 
ATOM   245  C  CE2 . TRP A 1 139 ? 170.702 183.617 178.114 1.00 10.37  ? 49   TRP A CE2 1 
ATOM   246  C  CE3 . TRP A 1 139 ? 171.130 184.504 175.923 1.00 10.04  ? 49   TRP A CE3 1 
ATOM   247  C  CZ2 . TRP A 1 139 ? 171.997 183.131 178.213 1.00 9.95   ? 49   TRP A CZ2 1 
ATOM   248  C  CZ3 . TRP A 1 139 ? 172.425 184.019 176.021 1.00 9.85   ? 49   TRP A CZ3 1 
ATOM   249  C  CH2 . TRP A 1 139 ? 172.847 183.350 177.137 1.00 9.84   ? 49   TRP A CH2 1 
ATOM   250  N  N   . ASP A 1 140 ? 165.463 183.721 176.734 1.00 11.45  ? 50   ASP A N   1 
ATOM   251  C  CA  . ASP A 1 140 ? 164.758 182.719 177.522 1.00 11.95  ? 50   ASP A CA  1 
ATOM   252  C  C   . ASP A 1 140 ? 164.293 181.560 176.658 1.00 12.46  ? 50   ASP A C   1 
ATOM   253  O  O   . ASP A 1 140 ? 164.376 180.405 177.069 1.00 12.46  ? 50   ASP A O   1 
ATOM   254  C  CB  . ASP A 1 140 ? 163.551 183.333 178.233 1.00 12.04  ? 50   ASP A CB  1 
ATOM   255  C  CG  . ASP A 1 140 ? 163.924 184.219 179.414 1.00 11.84  ? 50   ASP A CG  1 
ATOM   256  O  OD1 . ASP A 1 140 ? 165.053 184.182 179.840 1.00 11.88  ? 50   ASP A OD1 1 
ATOM   257  O  OD2 . ASP A 1 140 ? 163.063 184.919 179.889 1.00 12.14  ? 50   ASP A OD2 1 
ATOM   258  N  N   . TYR A 1 141 ? 163.827 181.861 175.453 1.00 12.16  ? 51   TYR A N   1 
ATOM   259  C  CA  . TYR A 1 141 ? 163.408 180.819 174.530 1.00 12.74  ? 51   TYR A CA  1 
ATOM   260  C  C   . TYR A 1 141 ? 164.569 179.926 174.109 1.00 12.87  ? 51   TYR A C   1 
ATOM   261  O  O   . TYR A 1 141 ? 164.471 178.702 174.161 1.00 12.74  ? 51   TYR A O   1 
ATOM   262  C  CB  . TYR A 1 141 ? 162.743 181.430 173.299 1.00 12.73  ? 51   TYR A CB  1 
ATOM   263  C  CG  . TYR A 1 141 ? 162.394 180.413 172.258 1.00 13.01  ? 51   TYR A CG  1 
ATOM   264  C  CD1 . TYR A 1 141 ? 161.316 179.574 172.450 1.00 13.36  ? 51   TYR A CD1 1 
ATOM   265  C  CD2 . TYR A 1 141 ? 163.155 180.312 171.111 1.00 12.98  ? 51   TYR A CD2 1 
ATOM   266  C  CE1 . TYR A 1 141 ? 161.001 178.636 171.499 1.00 13.45  ? 51   TYR A CE1 1 
ATOM   267  C  CE2 . TYR A 1 141 ? 162.840 179.375 170.158 1.00 13.32  ? 51   TYR A CE2 1 
ATOM   268  C  CZ  . TYR A 1 141 ? 161.766 178.538 170.349 1.00 13.69  ? 51   TYR A CZ  1 
ATOM   269  O  OH  . TYR A 1 141 ? 161.450 177.598 169.398 1.00 13.95  ? 51   TYR A OH  1 
ATOM   270  N  N   . ASN A 1 142 ? 165.674 180.534 173.694 1.00 12.21  ? 52   ASN A N   1 
ATOM   271  C  CA  . ASN A 1 142 ? 166.809 179.783 173.162 1.00 12.35  ? 52   ASN A CA  1 
ATOM   272  C  C   . ASN A 1 142 ? 167.478 178.889 174.202 1.00 12.39  ? 52   ASN A C   1 
ATOM   273  O  O   . ASN A 1 142 ? 168.080 177.869 173.856 1.00 12.69  ? 52   ASN A O   1 
ATOM   274  C  CB  . ASN A 1 142 ? 167.817 180.728 172.544 1.00 11.96  ? 52   ASN A CB  1 
ATOM   275  C  CG  . ASN A 1 142 ? 167.382 181.225 171.199 1.00 12.07  ? 52   ASN A CG  1 
ATOM   276  O  OD1 . ASN A 1 142 ? 167.559 180.543 170.186 1.00 12.58  ? 52   ASN A OD1 1 
ATOM   277  N  ND2 . ASN A 1 142 ? 166.805 182.393 171.166 1.00 11.78  ? 52   ASN A ND2 1 
ATOM   278  N  N   . THR A 1 143 ? 167.367 179.258 175.475 1.00 12.36  ? 53   THR A N   1 
ATOM   279  C  CA  . THR A 1 143 ? 167.955 178.466 176.548 1.00 12.68  ? 53   THR A CA  1 
ATOM   280  C  C   . THR A 1 143 ? 166.917 177.610 177.273 1.00 13.07  ? 53   THR A C   1 
ATOM   281  O  O   . THR A 1 143 ? 167.226 176.979 178.285 1.00 13.37  ? 53   THR A O   1 
ATOM   282  C  CB  . THR A 1 143 ? 168.683 179.361 177.563 1.00 12.07  ? 53   THR A CB  1 
ATOM   283  O  OG1 . THR A 1 143 ? 167.756 180.281 178.148 1.00 12.06  ? 53   THR A OG1 1 
ATOM   284  C  CG2 . THR A 1 143 ? 169.795 180.139 176.867 1.00 11.31  ? 53   THR A CG2 1 
ATOM   285  N  N   . ASN A 1 144 ? 165.685 177.610 176.772 1.00 12.96  ? 54   ASN A N   1 
ATOM   286  C  CA  . ASN A 1 144 ? 164.600 176.817 177.345 1.00 13.43  ? 54   ASN A CA  1 
ATOM   287  C  C   . ASN A 1 144 ? 163.438 176.736 176.359 1.00 13.34  ? 54   ASN A C   1 
ATOM   288  O  O   . ASN A 1 144 ? 162.485 177.512 176.441 1.00 13.49  ? 54   ASN A O   1 
ATOM   289  C  CB  . ASN A 1 144 ? 164.146 177.401 178.671 1.00 13.58  ? 54   ASN A CB  1 
ATOM   290  C  CG  . ASN A 1 144 ? 163.164 176.525 179.396 1.00 14.01  ? 54   ASN A CG  1 
ATOM   291  O  OD1 . ASN A 1 144 ? 162.854 175.411 178.959 1.00 14.03  ? 54   ASN A OD1 1 
ATOM   292  N  ND2 . ASN A 1 144 ? 162.669 177.006 180.509 1.00 14.35  ? 54   ASN A ND2 1 
ATOM   293  N  N   . ILE A 1 145 ? 163.534 175.826 175.398 1.00 13.61  ? 55   ILE A N   1 
ATOM   294  C  CA  . ILE A 1 145 ? 162.588 175.817 174.292 1.00 13.61  ? 55   ILE A CA  1 
ATOM   295  C  C   . ILE A 1 145 ? 161.268 175.139 174.638 1.00 13.91  ? 55   ILE A C   1 
ATOM   296  O  O   . ILE A 1 145 ? 161.219 173.938 174.905 1.00 13.94  ? 55   ILE A O   1 
ATOM   297  C  CB  . ILE A 1 145 ? 163.214 175.132 173.064 1.00 13.65  ? 55   ILE A CB  1 
ATOM   298  C  CG1 . ILE A 1 145 ? 164.439 175.937 172.606 1.00 13.42  ? 55   ILE A CG1 1 
ATOM   299  C  CG2 . ILE A 1 145 ? 162.187 175.002 171.946 1.00 13.96  ? 55   ILE A CG2 1 
ATOM   300  C  CD1 . ILE A 1 145 ? 165.324 175.219 171.620 1.00 13.23  ? 55   ILE A CD1 1 
ATOM   301  N  N   . ASN A 1 146 ? 160.192 175.920 174.590 1.00 14.01  ? 56   ASN A N   1 
ATOM   302  C  CA  . ASN A 1 146 ? 158.839 175.432 174.825 1.00 14.15  ? 56   ASN A CA  1 
ATOM   303  C  C   . ASN A 1 146 ? 157.821 176.410 174.236 1.00 14.34  ? 56   ASN A C   1 
ATOM   304  O  O   . ASN A 1 146 ? 158.195 177.449 173.689 1.00 14.10  ? 56   ASN A O   1 
ATOM   305  C  CB  . ASN A 1 146 ? 158.595 175.175 176.304 1.00 14.24  ? 56   ASN A CB  1 
ATOM   306  C  CG  . ASN A 1 146 ? 158.781 176.385 177.165 1.00 14.14  ? 56   ASN A CG  1 
ATOM   307  O  OD1 . ASN A 1 146 ? 158.301 177.474 176.838 1.00 14.13  ? 56   ASN A OD1 1 
ATOM   308  N  ND2 . ASN A 1 146 ? 159.462 176.215 178.271 1.00 14.00  ? 56   ASN A ND2 1 
ATOM   309  N  N   . ASP A 1 147 ? 156.537 176.081 174.352 1.00 14.51  ? 57   ASP A N   1 
ATOM   310  C  CA  . ASP A 1 147 ? 155.486 176.900 173.753 1.00 14.44  ? 57   ASP A CA  1 
ATOM   311  C  C   . ASP A 1 147 ? 155.276 178.222 174.477 1.00 14.29  ? 57   ASP A C   1 
ATOM   312  O  O   . ASP A 1 147 ? 154.957 179.235 173.852 1.00 14.27  ? 57   ASP A O   1 
ATOM   313  C  CB  . ASP A 1 147 ? 154.166 176.132 173.724 1.00 14.79  ? 57   ASP A CB  1 
ATOM   314  N  N   . LYS A 1 148 ? 155.428 178.216 175.795 1.00 14.29  ? 58   LYS A N   1 
ATOM   315  C  CA  . LYS A 1 148 ? 155.193 179.427 176.569 1.00 14.33  ? 58   LYS A CA  1 
ATOM   316  C  C   . LYS A 1 148 ? 156.222 180.496 176.238 1.00 14.03  ? 58   LYS A C   1 
ATOM   317  O  O   . LYS A 1 148 ? 155.884 181.671 176.084 1.00 14.39  ? 58   LYS A O   1 
ATOM   318  C  CB  . LYS A 1 148 ? 155.221 179.125 178.066 1.00 14.78  ? 58   LYS A CB  1 
ATOM   319  N  N   . ASN A 1 149 ? 157.477 180.085 176.108 1.00 14.25  ? 59   ASN A N   1 
ATOM   320  C  CA  . ASN A 1 149 ? 158.543 181.021 175.803 1.00 13.93  ? 59   ASN A CA  1 
ATOM   321  C  C   . ASN A 1 149 ? 158.466 181.496 174.362 1.00 13.90  ? 59   ASN A C   1 
ATOM   322  O  O   . ASN A 1 149 ? 158.781 182.650 174.071 1.00 13.21  ? 59   ASN A O   1 
ATOM   323  C  CB  . ASN A 1 149 ? 159.894 180.415 176.114 1.00 13.57  ? 59   ASN A CB  1 
ATOM   324  C  CG  . ASN A 1 149 ? 160.160 180.367 177.588 1.00 13.47  ? 59   ASN A CG  1 
ATOM   325  O  OD1 . ASN A 1 149 ? 159.526 181.094 178.363 1.00 14.05  ? 59   ASN A OD1 1 
ATOM   326  N  ND2 . ASN A 1 149 ? 161.081 179.539 177.996 1.00 13.62  ? 59   ASN A ND2 1 
ATOM   327  N  N   . ALA A 1 150 ? 158.022 180.624 173.462 1.00 14.60  ? 60   ALA A N   1 
ATOM   328  C  CA  . ALA A 1 150 ? 157.870 181.017 172.068 1.00 13.58  ? 60   ALA A CA  1 
ATOM   329  C  C   . ALA A 1 150 ? 156.838 182.128 171.948 1.00 13.75  ? 60   ALA A C   1 
ATOM   330  O  O   . ALA A 1 150 ? 157.015 183.075 171.180 1.00 13.68  ? 60   ALA A O   1 
ATOM   331  C  CB  . ALA A 1 150 ? 157.460 179.826 171.223 1.00 13.72  ? 60   ALA A CB  1 
ATOM   332  N  N   . GLN A 1 151 ? 155.771 182.028 172.737 1.00 13.98  ? 61   GLN A N   1 
ATOM   333  C  CA  . GLN A 1 151 ? 154.716 183.030 172.715 1.00 13.90  ? 61   GLN A CA  1 
ATOM   334  C  C   . GLN A 1 151 ? 155.208 184.370 173.241 1.00 14.72  ? 61   GLN A C   1 
ATOM   335  O  O   . GLN A 1 151 ? 154.941 185.411 172.641 1.00 13.43  ? 61   GLN A O   1 
ATOM   336  C  CB  . GLN A 1 151 ? 153.519 182.555 173.543 1.00 14.19  ? 61   GLN A CB  1 
ATOM   337  N  N   . LYS A 1 152 ? 155.957 184.346 174.340 1.00 13.57  ? 62   LYS A N   1 
ATOM   338  C  CA  . LYS A 1 152 ? 156.474 185.582 174.916 1.00 13.64  ? 62   LYS A CA  1 
ATOM   339  C  C   . LYS A 1 152 ? 157.430 186.271 173.956 1.00 13.45  ? 62   LYS A C   1 
ATOM   340  O  O   . LYS A 1 152 ? 157.415 187.496 173.819 1.00 13.16  ? 62   LYS A O   1 
ATOM   341  C  CB  . LYS A 1 152 ? 157.174 185.309 176.245 1.00 13.75  ? 62   LYS A CB  1 
ATOM   342  C  CG  . LYS A 1 152 ? 156.238 184.939 177.382 1.00 14.16  ? 62   LYS A CG  1 
ATOM   343  C  CD  . LYS A 1 152 ? 157.007 184.687 178.670 1.00 14.90  ? 62   LYS A CD  1 
ATOM   344  C  CE  . LYS A 1 152 ? 156.073 184.320 179.813 1.00 15.68  ? 62   LYS A CE  1 
ATOM   345  N  NZ  . LYS A 1 152 ? 156.813 184.091 181.085 1.00 15.43  ? 62   LYS A NZ  1 
ATOM   346  N  N   . MET A 1 153 ? 158.250 185.476 173.279 1.00 13.27  ? 63   MET A N   1 
ATOM   347  C  CA  . MET A 1 153 ? 159.200 185.993 172.307 1.00 12.99  ? 63   MET A CA  1 
ATOM   348  C  C   . MET A 1 153 ? 158.488 186.704 171.168 1.00 14.87  ? 63   MET A C   1 
ATOM   349  O  O   . MET A 1 153 ? 158.850 187.824 170.807 1.00 12.88  ? 63   MET A O   1 
ATOM   350  C  CB  . MET A 1 153 ? 160.063 184.852 171.783 1.00 13.04  ? 63   MET A CB  1 
ATOM   351  C  CG  . MET A 1 153 ? 161.076 185.247 170.729 1.00 13.07  ? 63   MET A CG  1 
ATOM   352  S  SD  . MET A 1 153 ? 162.041 183.842 170.141 1.00 13.27  ? 63   MET A SD  1 
ATOM   353  C  CE  . MET A 1 153 ? 160.805 182.906 169.236 1.00 13.86  ? 63   MET A CE  1 
ATOM   354  N  N   . ASN A 1 154 ? 157.458 186.068 170.620 1.00 13.00  ? 64   ASN A N   1 
ATOM   355  C  CA  . ASN A 1 154 ? 156.730 186.644 169.499 1.00 13.36  ? 64   ASN A CA  1 
ATOM   356  C  C   . ASN A 1 154 ? 156.031 187.944 169.884 1.00 13.14  ? 64   ASN A C   1 
ATOM   357  O  O   . ASN A 1 154 ? 155.991 188.891 169.097 1.00 13.10  ? 64   ASN A O   1 
ATOM   358  C  CB  . ASN A 1 154 ? 155.732 185.641 168.958 1.00 13.52  ? 64   ASN A CB  1 
ATOM   359  C  CG  . ASN A 1 154 ? 156.394 184.518 168.207 1.00 13.93  ? 64   ASN A CG  1 
ATOM   360  O  OD1 . ASN A 1 154 ? 157.511 184.657 167.697 1.00 14.04  ? 64   ASN A OD1 1 
ATOM   361  N  ND2 . ASN A 1 154 ? 155.723 183.399 168.130 1.00 14.87  ? 64   ASN A ND2 1 
ATOM   362  N  N   . GLU A 1 155 ? 155.500 188.001 171.102 1.00 13.19  ? 65   GLU A N   1 
ATOM   363  C  CA  . GLU A 1 155 ? 154.819 189.203 171.565 1.00 13.10  ? 65   GLU A CA  1 
ATOM   364  C  C   . GLU A 1 155 ? 155.789 190.362 171.747 1.00 12.81  ? 65   GLU A C   1 
ATOM   365  O  O   . GLU A 1 155 ? 155.490 191.498 171.374 1.00 12.82  ? 65   GLU A O   1 
ATOM   366  C  CB  . GLU A 1 155 ? 154.092 188.929 172.881 1.00 13.40  ? 65   GLU A CB  1 
ATOM   367  N  N   . ALA A 1 156 ? 156.959 190.076 172.312 1.00 12.91  ? 66   ALA A N   1 
ATOM   368  C  CA  . ALA A 1 156 ? 157.958 191.110 172.544 1.00 12.50  ? 66   ALA A CA  1 
ATOM   369  C  C   . ALA A 1 156 ? 158.458 191.693 171.228 1.00 12.36  ? 66   ALA A C   1 
ATOM   370  O  O   . ALA A 1 156 ? 158.678 192.901 171.120 1.00 12.14  ? 66   ALA A O   1 
ATOM   371  C  CB  . ALA A 1 156 ? 159.117 190.547 173.348 1.00 11.87  ? 66   ALA A CB  1 
ATOM   372  N  N   . ASP A 1 157 ? 158.607 190.839 170.220 1.00 12.62  ? 67   ASP A N   1 
ATOM   373  C  CA  . ASP A 1 157 ? 159.070 191.285 168.912 1.00 12.49  ? 67   ASP A CA  1 
ATOM   374  C  C   . ASP A 1 157 ? 158.024 192.137 168.215 1.00 12.40  ? 67   ASP A C   1 
ATOM   375  O  O   . ASP A 1 157 ? 158.358 193.095 167.517 1.00 12.16  ? 67   ASP A O   1 
ATOM   376  C  CB  . ASP A 1 157 ? 159.430 190.092 168.031 1.00 12.80  ? 67   ASP A CB  1 
ATOM   377  N  N   . SER A 1 158 ? 156.754 191.799 168.414 1.00 12.51  ? 68   SER A N   1 
ATOM   378  C  CA  . SER A 1 158 ? 155.673 192.569 167.817 1.00 12.39  ? 68   SER A CA  1 
ATOM   379  C  C   . SER A 1 158 ? 155.680 194.000 168.339 1.00 12.04  ? 68   SER A C   1 
ATOM   380  O  O   . SER A 1 158 ? 155.547 194.951 167.566 1.00 11.97  ? 68   SER A O   1 
ATOM   381  C  CB  . SER A 1 158 ? 154.340 191.914 168.112 1.00 12.46  ? 68   SER A CB  1 
ATOM   382  N  N   . LYS A 1 159 ? 155.864 194.152 169.649 1.00 12.07  ? 69   LYS A N   1 
ATOM   383  C  CA  . LYS A 1 159 ? 155.910 195.474 170.262 1.00 11.93  ? 69   LYS A CA  1 
ATOM   384  C  C   . LYS A 1 159 ? 157.080 196.294 169.728 1.00 11.72  ? 69   LYS A C   1 
ATOM   385  O  O   . LYS A 1 159 ? 156.929 197.476 169.420 1.00 11.66  ? 69   LYS A O   1 
ATOM   386  C  CB  . LYS A 1 159 ? 156.005 195.355 171.782 1.00 12.06  ? 69   LYS A CB  1 
ATOM   387  C  CG  . LYS A 1 159 ? 154.735 194.850 172.445 1.00 12.40  ? 69   LYS A CG  1 
ATOM   388  C  CD  . LYS A 1 159 ? 154.907 194.707 173.949 1.00 12.92  ? 69   LYS A CD  1 
ATOM   389  C  CE  . LYS A 1 159 ? 153.657 194.130 174.595 1.00 14.09  ? 69   LYS A CE  1 
ATOM   390  N  NZ  . LYS A 1 159 ? 153.829 193.931 176.060 1.00 14.78  ? 69   LYS A NZ  1 
ATOM   391  N  N   . TRP A 1 160 ? 158.238 195.653 169.585 1.00 11.58  ? 70   TRP A N   1 
ATOM   392  C  CA  . TRP A 1 160 ? 159.410 196.321 169.035 1.00 11.39  ? 70   TRP A CA  1 
ATOM   393  C  C   . TRP A 1 160 ? 159.160 196.824 167.622 1.00 11.49  ? 70   TRP A C   1 
ATOM   394  O  O   . TRP A 1 160 ? 159.488 197.963 167.290 1.00 10.80  ? 70   TRP A O   1 
ATOM   395  C  CB  . TRP A 1 160 ? 160.619 195.386 169.035 1.00 11.35  ? 70   TRP A CB  1 
ATOM   396  C  CG  . TRP A 1 160 ? 161.769 195.912 168.232 1.00 11.24  ? 70   TRP A CG  1 
ATOM   397  C  CD1 . TRP A 1 160 ? 162.258 195.382 167.079 1.00 11.35  ? 70   TRP A CD1 1 
ATOM   398  C  CD2 . TRP A 1 160 ? 162.567 197.085 168.502 1.00 10.84  ? 70   TRP A CD2 1 
ATOM   399  N  NE1 . TRP A 1 160 ? 163.301 196.139 166.618 1.00 11.17  ? 70   TRP A NE1 1 
ATOM   400  C  CE2 . TRP A 1 160 ? 163.501 197.187 167.476 1.00 10.87  ? 70   TRP A CE2 1 
ATOM   401  C  CE3 . TRP A 1 160 ? 162.557 198.039 169.506 1.00 10.50  ? 70   TRP A CE3 1 
ATOM   402  C  CZ2 . TRP A 1 160 ? 164.426 198.214 167.430 1.00 10.50  ? 70   TRP A CZ2 1 
ATOM   403  C  CZ3 . TRP A 1 160 ? 163.479 199.066 169.462 1.00 10.28  ? 70   TRP A CZ3 1 
ATOM   404  C  CH2 . TRP A 1 160 ? 164.390 199.153 168.451 1.00 10.18  ? 70   TRP A CH2 1 
ATOM   405  N  N   . SER A 1 161 ? 158.581 195.972 166.784 1.00 11.58  ? 71   SER A N   1 
ATOM   406  C  CA  . SER A 1 161 ? 158.332 196.329 165.398 1.00 11.46  ? 71   SER A CA  1 
ATOM   407  C  C   . SER A 1 161 ? 157.361 197.499 165.284 1.00 11.38  ? 71   SER A C   1 
ATOM   408  O  O   . SER A 1 161 ? 157.563 198.402 164.475 1.00 11.31  ? 71   SER A O   1 
ATOM   409  C  CB  . SER A 1 161 ? 157.791 195.137 164.640 1.00 11.56  ? 71   SER A CB  1 
ATOM   410  O  OG  . SER A 1 161 ? 158.756 194.125 164.535 1.00 11.88  ? 71   SER A OG  1 
ATOM   411  N  N   . ALA A 1 162 ? 156.315 197.490 166.107 1.00 11.35  ? 72   ALA A N   1 
ATOM   412  C  CA  . ALA A 1 162 ? 155.335 198.573 166.078 1.00 11.19  ? 72   ALA A CA  1 
ATOM   413  C  C   . ALA A 1 162 ? 155.986 199.894 166.464 1.00 11.13  ? 72   ALA A C   1 
ATOM   414  O  O   . ALA A 1 162 ? 155.739 200.924 165.830 1.00 11.29  ? 72   ALA A O   1 
ATOM   415  C  CB  . ALA A 1 162 ? 154.190 198.258 167.023 1.00 11.59  ? 72   ALA A CB  1 
ATOM   416  N  N   . PHE A 1 163 ? 156.841 199.858 167.480 1.00 11.04  ? 73   PHE A N   1 
ATOM   417  C  CA  . PHE A 1 163 ? 157.570 201.035 167.929 1.00 10.83  ? 73   PHE A CA  1 
ATOM   418  C  C   . PHE A 1 163 ? 158.448 201.600 166.827 1.00 10.76  ? 73   PHE A C   1 
ATOM   419  O  O   . PHE A 1 163 ? 158.395 202.788 166.513 1.00 10.63  ? 73   PHE A O   1 
ATOM   420  C  CB  . PHE A 1 163 ? 158.434 200.683 169.144 1.00 10.62  ? 73   PHE A CB  1 
ATOM   421  C  CG  . PHE A 1 163 ? 159.463 201.714 169.492 1.00 10.53  ? 73   PHE A CG  1 
ATOM   422  C  CD1 . PHE A 1 163 ? 160.784 201.531 169.116 1.00 10.46  ? 73   PHE A CD1 1 
ATOM   423  C  CD2 . PHE A 1 163 ? 159.129 202.856 170.191 1.00 10.51  ? 73   PHE A CD2 1 
ATOM   424  C  CE1 . PHE A 1 163 ? 161.740 202.464 169.427 1.00 10.29  ? 73   PHE A CE1 1 
ATOM   425  C  CE2 . PHE A 1 163 ? 160.091 203.794 170.506 1.00 10.25  ? 73   PHE A CE2 1 
ATOM   426  C  CZ  . PHE A 1 163 ? 161.396 203.597 170.122 1.00 10.09  ? 73   PHE A CZ  1 
ATOM   427  N  N   . TYR A 1 164 ? 159.277 200.740 166.248 1.00 10.78  ? 74   TYR A N   1 
ATOM   428  C  CA  . TYR A 1 164 ? 160.236 201.175 165.254 1.00 10.74  ? 74   TYR A CA  1 
ATOM   429  C  C   . TYR A 1 164 ? 159.539 201.800 164.052 1.00 10.81  ? 74   TYR A C   1 
ATOM   430  O  O   . TYR A 1 164 ? 159.969 202.838 163.550 1.00 10.46  ? 74   TYR A O   1 
ATOM   431  C  CB  . TYR A 1 164 ? 161.112 200.002 164.821 1.00 10.64  ? 74   TYR A CB  1 
ATOM   432  C  CG  . TYR A 1 164 ? 162.321 200.410 164.033 1.00 10.43  ? 74   TYR A CG  1 
ATOM   433  C  CD1 . TYR A 1 164 ? 162.299 200.381 162.653 1.00 10.33  ? 74   TYR A CD1 1 
ATOM   434  C  CD2 . TYR A 1 164 ? 163.465 200.810 164.702 1.00 10.22  ? 74   TYR A CD2 1 
ATOM   435  C  CE1 . TYR A 1 164 ? 163.420 200.753 161.942 1.00 10.22  ? 74   TYR A CE1 1 
ATOM   436  C  CE2 . TYR A 1 164 ? 164.583 201.179 163.993 1.00 10.08  ? 74   TYR A CE2 1 
ATOM   437  C  CZ  . TYR A 1 164 ? 164.564 201.151 162.618 1.00 10.19  ? 74   TYR A CZ  1 
ATOM   438  O  OH  . TYR A 1 164 ? 165.681 201.516 161.909 1.00 9.99   ? 74   TYR A OH  1 
ATOM   439  N  N   . LYS A 1 165 ? 158.466 201.167 163.583 1.00 10.77  ? 75   LYS A N   1 
ATOM   440  C  CA  . LYS A 1 165 ? 157.745 201.654 162.415 1.00 10.79  ? 75   LYS A CA  1 
ATOM   441  C  C   . LYS A 1 165 ? 157.135 203.035 162.639 1.00 10.64  ? 75   LYS A C   1 
ATOM   442  O  O   . LYS A 1 165 ? 157.157 203.878 161.740 1.00 10.61  ? 75   LYS A O   1 
ATOM   443  C  CB  . LYS A 1 165 ? 156.659 200.666 161.995 1.00 11.11  ? 75   LYS A CB  1 
ATOM   444  N  N   . GLU A 1 166 ? 156.599 203.281 163.830 1.00 10.58  ? 76   GLU A N   1 
ATOM   445  C  CA  . GLU A 1 166 ? 156.011 204.584 164.114 1.00 10.71  ? 76   GLU A CA  1 
ATOM   446  C  C   . GLU A 1 166 ? 157.049 205.688 163.997 1.00 10.69  ? 76   GLU A C   1 
ATOM   447  O  O   . GLU A 1 166 ? 156.805 206.718 163.363 1.00 10.50  ? 76   GLU A O   1 
ATOM   448  C  CB  . GLU A 1 166 ? 155.390 204.613 165.511 1.00 10.83  ? 76   GLU A CB  1 
ATOM   449  C  CG  . GLU A 1 166 ? 154.734 205.943 165.869 1.00 10.87  ? 76   GLU A CG  1 
ATOM   450  C  CD  . GLU A 1 166 ? 154.092 205.943 167.225 1.00 11.43  ? 76   GLU A CD  1 
ATOM   451  O  OE1 . GLU A 1 166 ? 154.044 204.907 167.843 1.00 11.70  ? 76   GLU A OE1 1 
ATOM   452  O  OE2 . GLU A 1 166 ? 153.651 206.984 167.648 1.00 11.84  ? 76   GLU A OE2 1 
ATOM   453  N  N   . HIS A 1 167 ? 158.216 205.465 164.591 1.00 10.40  ? 77   HIS A N   1 
ATOM   454  C  CA  . HIS A 1 167 ? 159.274 206.465 164.582 1.00 10.50  ? 77   HIS A CA  1 
ATOM   455  C  C   . HIS A 1 167 ? 159.944 206.584 163.224 1.00 10.48  ? 77   HIS A C   1 
ATOM   456  O  O   . HIS A 1 167 ? 160.416 207.657 162.856 1.00 10.22  ? 77   HIS A O   1 
ATOM   457  C  CB  . HIS A 1 167 ? 160.292 206.171 165.677 1.00 10.40  ? 77   HIS A CB  1 
ATOM   458  C  CG  . HIS A 1 167 ? 159.786 206.551 167.021 1.00 10.41  ? 77   HIS A CG  1 
ATOM   459  N  ND1 . HIS A 1 167 ? 158.886 205.782 167.715 1.00 10.47  ? 77   HIS A ND1 1 
ATOM   460  C  CD2 . HIS A 1 167 ? 160.040 207.626 167.796 1.00 10.43  ? 77   HIS A CD2 1 
ATOM   461  C  CE1 . HIS A 1 167 ? 158.605 206.368 168.861 1.00 10.62  ? 77   HIS A CE1 1 
ATOM   462  N  NE2 . HIS A 1 167 ? 159.294 207.487 168.936 1.00 10.64  ? 77   HIS A NE2 1 
ATOM   463  N  N   . SER A 1 168 ? 159.949 205.500 162.460 1.00 10.39  ? 78   SER A N   1 
ATOM   464  C  CA  . SER A 1 168 ? 160.469 205.553 161.103 1.00 10.30  ? 78   SER A CA  1 
ATOM   465  C  C   . SER A 1 168 ? 159.663 206.550 160.277 1.00 10.47  ? 78   SER A C   1 
ATOM   466  O  O   . SER A 1 168 ? 160.225 207.386 159.570 1.00 10.26  ? 78   SER A O   1 
ATOM   467  C  CB  . SER A 1 168 ? 160.413 204.179 160.465 1.00 10.45  ? 78   SER A CB  1 
ATOM   468  N  N   . LYS A 1 169 ? 158.341 206.493 160.409 1.00 10.42  ? 79   LYS A N   1 
ATOM   469  C  CA  . LYS A 1 169 ? 157.468 207.432 159.717 1.00 10.37  ? 79   LYS A CA  1 
ATOM   470  C  C   . LYS A 1 169 ? 157.701 208.870 160.179 1.00 10.32  ? 79   LYS A C   1 
ATOM   471  O  O   . LYS A 1 169 ? 157.745 209.790 159.365 1.00 10.41  ? 79   LYS A O   1 
ATOM   472  C  CB  . LYS A 1 169 ? 156.004 207.048 159.915 1.00 10.58  ? 79   LYS A CB  1 
ATOM   473  N  N   . LEU A 1 170 ? 157.871 209.063 161.482 1.00 10.23  ? 80   LEU A N   1 
ATOM   474  C  CA  . LEU A 1 170 ? 158.099 210.400 162.024 1.00 10.21  ? 80   LEU A CA  1 
ATOM   475  C  C   . LEU A 1 170 ? 159.406 210.997 161.511 1.00 10.31  ? 80   LEU A C   1 
ATOM   476  O  O   . LEU A 1 170 ? 159.499 212.203 161.277 1.00 10.25  ? 80   LEU A O   1 
ATOM   477  C  CB  . LEU A 1 170 ? 158.132 210.359 163.557 1.00 10.23  ? 80   LEU A CB  1 
ATOM   478  C  CG  . LEU A 1 170 ? 156.806 210.025 164.263 1.00 10.31  ? 80   LEU A CG  1 
ATOM   479  C  CD1 . LEU A 1 170 ? 157.069 209.840 165.754 1.00 10.58  ? 80   LEU A CD1 1 
ATOM   480  C  CD2 . LEU A 1 170 ? 155.802 211.143 164.035 1.00 10.26  ? 80   LEU A CD2 1 
ATOM   481  N  N   . ALA A 1 171 ? 160.406 210.144 161.311 1.00 10.14  ? 81   ALA A N   1 
ATOM   482  C  CA  . ALA A 1 171 ? 161.729 210.568 160.867 1.00 10.20  ? 81   ALA A CA  1 
ATOM   483  C  C   . ALA A 1 171 ? 161.685 211.217 159.487 1.00 10.32  ? 81   ALA A C   1 
ATOM   484  O  O   . ALA A 1 171 ? 162.629 211.895 159.081 1.00 10.40  ? 81   ALA A O   1 
ATOM   485  C  CB  . ALA A 1 171 ? 162.681 209.382 160.848 1.00 9.95   ? 81   ALA A CB  1 
ATOM   486  N  N   . GLN A 1 172 ? 160.593 211.011 158.758 1.00 10.15  ? 82   GLN A N   1 
ATOM   487  C  CA  . GLN A 1 172 ? 160.463 211.538 157.404 1.00 10.21  ? 82   GLN A CA  1 
ATOM   488  C  C   . GLN A 1 172 ? 160.257 213.047 157.426 1.00 10.32  ? 82   GLN A C   1 
ATOM   489  O  O   . GLN A 1 172 ? 160.311 213.705 156.388 1.00 10.71  ? 82   GLN A O   1 
ATOM   490  C  CB  . GLN A 1 172 ? 159.283 210.881 156.684 1.00 10.30  ? 82   GLN A CB  1 
ATOM   491  C  CG  . GLN A 1 172 ? 159.370 209.371 156.548 1.00 10.44  ? 82   GLN A CG  1 
ATOM   492  C  CD  . GLN A 1 172 ? 160.459 208.903 155.610 1.00 10.28  ? 82   GLN A CD  1 
ATOM   493  O  OE1 . GLN A 1 172 ? 160.926 209.640 154.739 1.00 10.41  ? 82   GLN A OE1 1 
ATOM   494  N  NE2 . GLN A 1 172 ? 160.864 207.657 155.777 1.00 10.20  ? 82   GLN A NE2 1 
ATOM   495  N  N   . GLY A 1 173 ? 160.011 213.592 158.613 1.00 10.47  ? 83   GLY A N   1 
ATOM   496  C  CA  . GLY A 1 173 ? 159.745 215.014 158.775 1.00 10.56  ? 83   GLY A CA  1 
ATOM   497  C  C   . GLY A 1 173 ? 161.019 215.829 158.967 1.00 10.79  ? 83   GLY A C   1 
ATOM   498  O  O   . GLY A 1 173 ? 160.955 217.028 159.242 1.00 11.13  ? 83   GLY A O   1 
ATOM   499  N  N   . PHE A 1 174 ? 162.175 215.184 158.820 1.00 10.81  ? 84   PHE A N   1 
ATOM   500  C  CA  . PHE A 1 174 ? 163.459 215.858 158.990 1.00 11.05  ? 84   PHE A CA  1 
ATOM   501  C  C   . PHE A 1 174 ? 164.355 215.694 157.761 1.00 11.20  ? 84   PHE A C   1 
ATOM   502  O  O   . PHE A 1 174 ? 165.144 214.751 157.699 1.00 11.08  ? 84   PHE A O   1 
ATOM   503  C  CB  . PHE A 1 174 ? 164.199 215.302 160.205 1.00 10.92  ? 84   PHE A CB  1 
ATOM   504  C  CG  . PHE A 1 174 ? 163.434 215.403 161.473 1.00 10.77  ? 84   PHE A CG  1 
ATOM   505  C  CD1 . PHE A 1 174 ? 162.816 214.289 161.997 1.00 10.64  ? 84   PHE A CD1 1 
ATOM   506  C  CD2 . PHE A 1 174 ? 163.320 216.602 162.141 1.00 11.25  ? 84   PHE A CD2 1 
ATOM   507  C  CE1 . PHE A 1 174 ? 162.100 214.365 163.165 1.00 10.71  ? 84   PHE A CE1 1 
ATOM   508  C  CE2 . PHE A 1 174 ? 162.603 216.684 163.311 1.00 11.24  ? 84   PHE A CE2 1 
ATOM   509  C  CZ  . PHE A 1 174 ? 161.993 215.563 163.824 1.00 11.01  ? 84   PHE A CZ  1 
ATOM   510  N  N   . PRO A 1 175 ? 164.235 216.581 156.766 1.00 11.41  ? 85   PRO A N   1 
ATOM   511  C  CA  . PRO A 1 175 ? 164.974 216.580 155.517 1.00 11.61  ? 85   PRO A CA  1 
ATOM   512  C  C   . PRO A 1 175 ? 166.467 216.542 155.786 1.00 11.89  ? 85   PRO A C   1 
ATOM   513  O  O   . PRO A 1 175 ? 166.972 217.288 156.621 1.00 11.80  ? 85   PRO A O   1 
ATOM   514  C  CB  . PRO A 1 175 ? 164.550 217.913 154.891 1.00 12.02  ? 85   PRO A CB  1 
ATOM   515  C  CG  . PRO A 1 175 ? 163.181 218.174 155.467 1.00 11.84  ? 85   PRO A CG  1 
ATOM   516  C  CD  . PRO A 1 175 ? 163.264 217.666 156.889 1.00 11.49  ? 85   PRO A CD  1 
ATOM   517  N  N   . LEU A 1 176 ? 167.176 215.688 155.062 1.00 11.85  ? 86   LEU A N   1 
ATOM   518  C  CA  . LEU A 1 176 ? 168.603 215.501 155.285 1.00 11.82  ? 86   LEU A CA  1 
ATOM   519  C  C   . LEU A 1 176 ? 169.404 216.656 154.715 1.00 12.10  ? 86   LEU A C   1 
ATOM   520  O  O   . LEU A 1 176 ? 170.550 216.883 155.100 1.00 12.01  ? 86   LEU A O   1 
ATOM   521  C  CB  . LEU A 1 176 ? 169.057 214.189 154.643 1.00 11.54  ? 86   LEU A CB  1 
ATOM   522  C  CG  . LEU A 1 176 ? 168.421 212.908 155.210 1.00 11.01  ? 86   LEU A CG  1 
ATOM   523  C  CD1 . LEU A 1 176 ? 168.815 211.738 154.339 1.00 10.85  ? 86   LEU A CD1 1 
ATOM   524  C  CD2 . LEU A 1 176 ? 168.882 212.681 156.646 1.00 10.62  ? 86   LEU A CD2 1 
ATOM   525  N  N   . GLN A 1 177 ? 168.783 217.401 153.815 1.00 12.32  ? 87   GLN A N   1 
ATOM   526  C  CA  . GLN A 1 177 ? 169.428 218.526 153.157 1.00 12.51  ? 87   GLN A CA  1 
ATOM   527  C  C   . GLN A 1 177 ? 169.635 219.681 154.124 1.00 12.49  ? 87   GLN A C   1 
ATOM   528  O  O   . GLN A 1 177 ? 170.413 220.595 153.856 1.00 12.46  ? 87   GLN A O   1 
ATOM   529  C  CB  . GLN A 1 177 ? 168.595 218.994 151.960 1.00 12.85  ? 87   GLN A CB  1 
ATOM   530  N  N   . GLU A 1 178 ? 168.906 219.655 155.234 1.00 12.36  ? 88   GLU A N   1 
ATOM   531  C  CA  . GLU A 1 178 ? 168.969 220.726 156.215 1.00 12.46  ? 88   GLU A CA  1 
ATOM   532  C  C   . GLU A 1 178 ? 169.791 220.329 157.437 1.00 12.19  ? 88   GLU A C   1 
ATOM   533  O  O   . GLU A 1 178 ? 169.843 221.067 158.420 1.00 12.45  ? 88   GLU A O   1 
ATOM   534  C  CB  . GLU A 1 178 ? 167.555 221.140 156.617 1.00 12.66  ? 88   GLU A CB  1 
ATOM   535  C  CG  . GLU A 1 178 ? 166.753 221.737 155.463 1.00 12.82  ? 88   GLU A CG  1 
ATOM   536  C  CD  . GLU A 1 178 ? 165.322 222.031 155.804 1.00 13.00  ? 88   GLU A CD  1 
ATOM   537  O  OE1 . GLU A 1 178 ? 164.853 221.543 156.799 1.00 12.91  ? 88   GLU A OE1 1 
ATOM   538  O  OE2 . GLU A 1 178 ? 164.695 222.749 155.060 1.00 13.24  ? 88   GLU A OE2 1 
ATOM   539  N  N   . ILE A 1 179 ? 170.433 219.165 157.373 1.00 12.23  ? 89   ILE A N   1 
ATOM   540  C  CA  . ILE A 1 179 ? 171.249 218.693 158.485 1.00 12.29  ? 89   ILE A CA  1 
ATOM   541  C  C   . ILE A 1 179 ? 172.731 218.823 158.149 1.00 12.42  ? 89   ILE A C   1 
ATOM   542  O  O   . ILE A 1 179 ? 173.184 218.364 157.102 1.00 12.27  ? 89   ILE A O   1 
ATOM   543  C  CB  . ILE A 1 179 ? 170.931 217.222 158.831 1.00 11.99  ? 89   ILE A CB  1 
ATOM   544  C  CG1 . ILE A 1 179 ? 169.412 217.019 159.050 1.00 11.87  ? 89   ILE A CG1 1 
ATOM   545  C  CG2 . ILE A 1 179 ? 171.711 216.796 160.074 1.00 11.81  ? 89   ILE A CG2 1 
ATOM   546  C  CD1 . ILE A 1 179 ? 168.808 217.816 160.188 1.00 12.04  ? 89   ILE A CD1 1 
ATOM   547  N  N   . GLN A 1 180 ? 173.484 219.468 159.034 1.00 12.40  ? 90   GLN A N   1 
ATOM   548  C  CA  . GLN A 1 180 ? 174.925 219.641 158.835 1.00 12.37  ? 90   GLN A CA  1 
ATOM   549  C  C   . GLN A 1 180 ? 175.754 218.714 159.729 1.00 12.14  ? 90   GLN A C   1 
ATOM   550  O  O   . GLN A 1 180 ? 176.887 218.361 159.393 1.00 12.37  ? 90   GLN A O   1 
ATOM   551  C  CB  . GLN A 1 180 ? 175.322 221.094 159.077 1.00 12.86  ? 90   GLN A CB  1 
ATOM   552  C  CG  . GLN A 1 180 ? 174.652 222.068 158.135 1.00 12.84  ? 90   GLN A CG  1 
ATOM   553  C  CD  . GLN A 1 180 ? 174.997 221.776 156.690 1.00 13.07  ? 90   GLN A CD  1 
ATOM   554  O  OE1 . GLN A 1 180 ? 176.173 221.709 156.324 1.00 13.11  ? 90   GLN A OE1 1 
ATOM   555  N  NE2 . GLN A 1 180 ? 173.978 221.596 155.860 1.00 12.94  ? 90   GLN A NE2 1 
ATOM   556  N  N   . ASN A 1 181 ? 175.179 218.319 160.868 1.00 12.31  ? 91   ASN A N   1 
ATOM   557  C  CA  . ASN A 1 181 ? 175.778 217.408 161.825 1.00 12.00  ? 91   ASN A CA  1 
ATOM   558  C  C   . ASN A 1 181 ? 175.728 215.978 161.311 1.00 11.65  ? 91   ASN A C   1 
ATOM   559  O  O   . ASN A 1 181 ? 174.641 215.407 161.139 1.00 11.18  ? 91   ASN A O   1 
ATOM   560  C  CB  . ASN A 1 181 ? 175.073 217.539 163.173 1.00 12.24  ? 91   ASN A CB  1 
ATOM   561  C  CG  . ASN A 1 181 ? 175.681 216.703 164.278 1.00 12.37  ? 91   ASN A CG  1 
ATOM   562  O  OD1 . ASN A 1 181 ? 175.656 215.461 164.227 1.00 11.89  ? 91   ASN A OD1 1 
ATOM   563  N  ND2 . ASN A 1 181 ? 176.225 217.351 165.285 1.00 13.01  ? 91   ASN A ND2 1 
ATOM   564  N  N   . SER A 1 182 ? 176.900 215.382 161.039 1.00 11.56  ? 92   SER A N   1 
ATOM   565  C  CA  . SER A 1 182 ? 176.996 214.066 160.410 1.00 11.26  ? 92   SER A CA  1 
ATOM   566  C  C   . SER A 1 182 ? 176.483 212.937 161.301 1.00 10.93  ? 92   SER A C   1 
ATOM   567  O  O   . SER A 1 182 ? 175.976 211.936 160.799 1.00 10.65  ? 92   SER A O   1 
ATOM   568  C  CB  . SER A 1 182 ? 178.429 213.788 160.016 1.00 11.28  ? 92   SER A CB  1 
ATOM   569  N  N   . THR A 1 183 ? 176.576 213.111 162.617 1.00 11.13  ? 93   THR A N   1 
ATOM   570  C  CA  . THR A 1 183 ? 176.058 212.098 163.532 1.00 11.01  ? 93   THR A CA  1 
ATOM   571  C  C   . THR A 1 183 ? 174.539 212.015 163.413 1.00 10.69  ? 93   THR A C   1 
ATOM   572  O  O   . THR A 1 183 ? 173.971 210.923 163.341 1.00 10.12  ? 93   THR A O   1 
ATOM   573  C  CB  . THR A 1 183 ? 176.453 212.392 164.993 1.00 11.17  ? 93   THR A CB  1 
ATOM   574  O  OG1 . THR A 1 183 ? 177.878 212.400 165.112 1.00 11.77  ? 93   THR A OG1 1 
ATOM   575  C  CG2 . THR A 1 183 ? 175.876 211.327 165.925 1.00 10.58  ? 93   THR A CG2 1 
ATOM   576  N  N   . ILE A 1 184 ? 173.889 213.176 163.387 1.00 10.77  ? 94   ILE A N   1 
ATOM   577  C  CA  . ILE A 1 184 ? 172.437 213.237 163.258 1.00 10.65  ? 94   ILE A CA  1 
ATOM   578  C  C   . ILE A 1 184 ? 171.980 212.769 161.888 1.00 10.58  ? 94   ILE A C   1 
ATOM   579  O  O   . ILE A 1 184 ? 171.020 212.007 161.773 1.00 10.08  ? 94   ILE A O   1 
ATOM   580  C  CB  . ILE A 1 184 ? 171.914 214.661 163.528 1.00 10.86  ? 94   ILE A CB  1 
ATOM   581  C  CG1 . ILE A 1 184 ? 172.094 214.994 165.013 1.00 11.21  ? 94   ILE A CG1 1 
ATOM   582  C  CG2 . ILE A 1 184 ? 170.448 214.787 163.102 1.00 10.90  ? 94   ILE A CG2 1 
ATOM   583  C  CD1 . ILE A 1 184 ? 171.863 216.448 165.360 1.00 11.97  ? 94   ILE A CD1 1 
ATOM   584  N  N   . LYS A 1 185 ? 172.660 213.236 160.850 1.00 10.47  ? 95   LYS A N   1 
ATOM   585  C  CA  . LYS A 1 185 ? 172.308 212.873 159.487 1.00 10.43  ? 95   LYS A CA  1 
ATOM   586  C  C   . LYS A 1 185 ? 172.353 211.369 159.296 1.00 10.29  ? 95   LYS A C   1 
ATOM   587  O  O   . LYS A 1 185 ? 171.448 210.782 158.707 1.00 9.83   ? 95   LYS A O   1 
ATOM   588  C  CB  . LYS A 1 185 ? 173.244 213.579 158.511 1.00 10.64  ? 95   LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 185 ? 172.970 213.328 157.047 1.00 10.56  ? 95   LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 185 ? 173.788 214.272 156.186 1.00 10.65  ? 95   LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 185 ? 173.559 214.028 154.705 1.00 10.67  ? 95   LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 185 ? 174.276 215.025 153.870 1.00 10.83  ? 95   LYS A NZ  1 
ATOM   593  N  N   . LEU A 1 186 ? 173.391 210.733 159.826 1.00 9.97   ? 96   LEU A N   1 
ATOM   594  C  CA  . LEU A 1 186 ? 173.562 209.296 159.681 1.00 9.75   ? 96   LEU A CA  1 
ATOM   595  C  C   . LEU A 1 186 ? 172.436 208.515 160.356 1.00 9.75   ? 96   LEU A C   1 
ATOM   596  O  O   . LEU A 1 186 ? 171.906 207.566 159.783 1.00 9.49   ? 96   LEU A O   1 
ATOM   597  C  CB  . LEU A 1 186 ? 174.923 208.885 160.260 1.00 9.68   ? 96   LEU A CB  1 
ATOM   598  C  CG  . LEU A 1 186 ? 175.303 207.398 160.175 1.00 9.28   ? 96   LEU A CG  1 
ATOM   599  C  CD1 . LEU A 1 186 ? 175.339 206.951 158.720 1.00 9.27   ? 96   LEU A CD1 1 
ATOM   600  C  CD2 . LEU A 1 186 ? 176.663 207.204 160.830 1.00 8.17   ? 96   LEU A CD2 1 
ATOM   601  N  N   . GLN A 1 187 ? 172.045 208.930 161.561 1.00 9.51   ? 97   GLN A N   1 
ATOM   602  C  CA  . GLN A 1 187 ? 170.963 208.245 162.260 1.00 9.55   ? 97   GLN A CA  1 
ATOM   603  C  C   . GLN A 1 187 ? 169.625 208.405 161.541 1.00 9.71   ? 97   GLN A C   1 
ATOM   604  O  O   . GLN A 1 187 ? 168.839 207.458 161.466 1.00 9.46   ? 97   GLN A O   1 
ATOM   605  C  CB  . GLN A 1 187 ? 170.848 208.745 163.699 1.00 9.45   ? 97   GLN A CB  1 
ATOM   606  C  CG  . GLN A 1 187 ? 171.981 208.299 164.601 1.00 9.10   ? 97   GLN A CG  1 
ATOM   607  C  CD  . GLN A 1 187 ? 171.811 208.768 166.027 1.00 9.07   ? 97   GLN A CD  1 
ATOM   608  O  OE1 . GLN A 1 187 ? 170.849 208.397 166.708 1.00 9.14   ? 97   GLN A OE1 1 
ATOM   609  N  NE2 . GLN A 1 187 ? 172.739 209.589 166.487 1.00 9.05   ? 97   GLN A NE2 1 
ATOM   610  N  N   . LEU A 1 188 ? 169.377 209.587 160.986 1.00 9.68   ? 98   LEU A N   1 
ATOM   611  C  CA  . LEU A 1 188 ? 168.141 209.819 160.247 1.00 9.75   ? 98   LEU A CA  1 
ATOM   612  C  C   . LEU A 1 188 ? 168.089 208.983 158.978 1.00 9.82   ? 98   LEU A C   1 
ATOM   613  O  O   . LEU A 1 188 ? 167.031 208.467 158.614 1.00 9.50   ? 98   LEU A O   1 
ATOM   614  C  CB  . LEU A 1 188 ? 167.991 211.296 159.886 1.00 9.91   ? 98   LEU A CB  1 
ATOM   615  C  CG  . LEU A 1 188 ? 167.697 212.263 161.035 1.00 10.13  ? 98   LEU A CG  1 
ATOM   616  C  CD1 . LEU A 1 188 ? 167.813 213.680 160.511 1.00 10.60  ? 98   LEU A CD1 1 
ATOM   617  C  CD2 . LEU A 1 188 ? 166.296 212.005 161.590 1.00 10.20  ? 98   LEU A CD2 1 
ATOM   618  N  N   . GLN A 1 189 ? 169.229 208.820 158.317 1.00 9.62   ? 99   GLN A N   1 
ATOM   619  C  CA  . GLN A 1 189 ? 169.281 208.019 157.099 1.00 9.67   ? 99   GLN A CA  1 
ATOM   620  C  C   . GLN A 1 189 ? 168.887 206.578 157.383 1.00 9.50   ? 99   GLN A C   1 
ATOM   621  O  O   . GLN A 1 189 ? 168.239 205.930 156.565 1.00 9.48   ? 99   GLN A O   1 
ATOM   622  C  CB  . GLN A 1 189 ? 170.679 208.048 156.485 1.00 9.68   ? 99   GLN A CB  1 
ATOM   623  C  CG  . GLN A 1 189 ? 171.065 209.364 155.865 1.00 9.88   ? 99   GLN A CG  1 
ATOM   624  C  CD  . GLN A 1 189 ? 172.502 209.381 155.404 1.00 10.00  ? 99   GLN A CD  1 
ATOM   625  O  OE1 . GLN A 1 189 ? 173.314 208.555 155.831 1.00 9.96   ? 99   GLN A OE1 1 
ATOM   626  N  NE2 . GLN A 1 189 ? 172.828 210.319 154.523 1.00 10.12  ? 99   GLN A NE2 1 
ATOM   627  N  N   . ILE A 1 190 ? 169.269 206.088 158.555 1.00 9.49   ? 100  ILE A N   1 
ATOM   628  C  CA  . ILE A 1 190 ? 168.940 204.730 158.963 1.00 9.44   ? 100  ILE A CA  1 
ATOM   629  C  C   . ILE A 1 190 ? 167.436 204.563 159.166 1.00 9.51   ? 100  ILE A C   1 
ATOM   630  O  O   . ILE A 1 190 ? 166.850 203.579 158.713 1.00 9.50   ? 100  ILE A O   1 
ATOM   631  C  CB  . ILE A 1 190 ? 169.689 204.358 160.259 1.00 9.39   ? 100  ILE A CB  1 
ATOM   632  C  CG1 . ILE A 1 190 ? 171.198 204.280 159.976 1.00 9.30   ? 100  ILE A CG1 1 
ATOM   633  C  CG2 . ILE A 1 190 ? 169.169 203.037 160.817 1.00 9.35   ? 100  ILE A CG2 1 
ATOM   634  C  CD1 . ILE A 1 190 ? 172.067 204.248 161.222 1.00 8.91   ? 100  ILE A CD1 1 
ATOM   635  N  N   . LEU A 1 191 ? 166.823 205.523 159.854 1.00 9.48   ? 101  LEU A N   1 
ATOM   636  C  CA  . LEU A 1 191 ? 165.397 205.466 160.160 1.00 9.54   ? 101  LEU A CA  1 
ATOM   637  C  C   . LEU A 1 191 ? 164.493 205.739 158.961 1.00 9.76   ? 101  LEU A C   1 
ATOM   638  O  O   . LEU A 1 191 ? 163.376 205.231 158.904 1.00 9.82   ? 101  LEU A O   1 
ATOM   639  C  CB  . LEU A 1 191 ? 165.051 206.477 161.263 1.00 9.63   ? 101  LEU A CB  1 
ATOM   640  C  CG  . LEU A 1 191 ? 165.605 206.181 162.663 1.00 9.52   ? 101  LEU A CG  1 
ATOM   641  C  CD1 . LEU A 1 191 ? 165.312 207.366 163.571 1.00 9.69   ? 101  LEU A CD1 1 
ATOM   642  C  CD2 . LEU A 1 191 ? 164.964 204.916 163.218 1.00 9.54   ? 101  LEU A CD2 1 
ATOM   643  N  N   . GLN A 1 192 ? 164.953 206.549 158.016 1.00 9.50   ? 102  GLN A N   1 
ATOM   644  C  CA  . GLN A 1 192 ? 164.095 206.984 156.915 1.00 9.67   ? 102  GLN A CA  1 
ATOM   645  C  C   . GLN A 1 192 ? 163.942 205.967 155.784 1.00 9.42   ? 102  GLN A C   1 
ATOM   646  O  O   . GLN A 1 192 ? 163.163 206.195 154.860 1.00 9.84   ? 102  GLN A O   1 
ATOM   647  C  CB  . GLN A 1 192 ? 164.588 208.313 156.337 1.00 9.68   ? 102  GLN A CB  1 
ATOM   648  C  CG  . GLN A 1 192 ? 164.400 209.505 157.257 1.00 9.82   ? 102  GLN A CG  1 
ATOM   649  C  CD  . GLN A 1 192 ? 164.988 210.785 156.695 1.00 10.04  ? 102  GLN A CD  1 
ATOM   650  O  OE1 . GLN A 1 192 ? 165.625 210.786 155.637 1.00 10.13  ? 102  GLN A OE1 1 
ATOM   651  N  NE2 . GLN A 1 192 ? 164.775 211.885 157.408 1.00 10.17  ? 102  GLN A NE2 1 
ATOM   652  N  N   . GLN A 1 193 ? 164.648 204.847 155.853 1.00 9.27   ? 103  GLN A N   1 
ATOM   653  C  CA  . GLN A 1 193 ? 164.555 203.841 154.792 1.00 9.01   ? 103  GLN A CA  1 
ATOM   654  C  C   . GLN A 1 193 ? 163.130 203.294 154.670 1.00 8.76   ? 103  GLN A C   1 
ATOM   655  O  O   . GLN A 1 193 ? 162.527 202.919 155.680 1.00 8.95   ? 103  GLN A O   1 
ATOM   656  C  CB  . GLN A 1 193 ? 165.512 202.685 155.063 1.00 9.05   ? 103  GLN A CB  1 
ATOM   657  C  CG  . GLN A 1 193 ? 166.966 203.069 155.017 1.00 9.23   ? 103  GLN A CG  1 
ATOM   658  C  CD  . GLN A 1 193 ? 167.889 201.915 155.348 1.00 9.43   ? 103  GLN A CD  1 
ATOM   659  O  OE1 . GLN A 1 193 ? 168.379 201.215 154.456 1.00 9.28   ? 103  GLN A OE1 1 
ATOM   660  N  NE2 . GLN A 1 193 ? 168.131 201.708 156.637 1.00 9.44   ? 103  GLN A NE2 1 
ATOM   661  N  N   . ASN A 1 194 ? 162.597 203.218 153.443 1.00 8.39   ? 104  ASN A N   1 
ATOM   662  C  CA  . ASN A 1 194 ? 161.243 202.724 153.187 1.00 8.17   ? 104  ASN A CA  1 
ATOM   663  C  C   . ASN A 1 194 ? 161.205 201.214 152.974 1.00 7.53   ? 104  ASN A C   1 
ATOM   664  O  O   . ASN A 1 194 ? 160.372 200.516 153.561 1.00 7.36   ? 104  ASN A O   1 
ATOM   665  C  CB  . ASN A 1 194 ? 160.616 203.452 152.009 1.00 8.35   ? 104  ASN A CB  1 
ATOM   666  C  CG  . ASN A 1 194 ? 159.858 204.703 152.404 1.00 9.38   ? 104  ASN A CG  1 
ATOM   667  O  OD1 . ASN A 1 194 ? 159.087 204.702 153.378 1.00 10.02  ? 104  ASN A OD1 1 
ATOM   668  N  ND2 . ASN A 1 194 ? 160.052 205.772 151.677 1.00 10.13  ? 104  ASN A ND2 1 
ATOM   669  N  N   . GLY A 1 195 ? 162.116 200.696 152.141 1.00 7.22   ? 105  GLY A N   1 
ATOM   670  C  CA  . GLY A 1 195 ? 162.182 199.267 151.845 1.00 6.53   ? 105  GLY A CA  1 
ATOM   671  C  C   . GLY A 1 195 ? 160.961 198.761 151.083 1.00 6.43   ? 105  GLY A C   1 
ATOM   672  O  O   . GLY A 1 195 ? 160.555 199.346 150.081 1.00 6.32   ? 105  GLY A O   1 
ATOM   673  N  N   . SER A 1 196 ? 160.372 197.675 151.568 1.00 6.38   ? 106  SER A N   1 
ATOM   674  C  CA  . SER A 1 196 ? 159.263 197.011 150.892 1.00 6.22   ? 106  SER A CA  1 
ATOM   675  C  C   . SER A 1 196 ? 157.995 197.855 150.831 1.00 6.28   ? 106  SER A C   1 
ATOM   676  O  O   . SER A 1 196 ? 157.101 197.583 150.032 1.00 6.24   ? 106  SER A O   1 
ATOM   677  C  CB  . SER A 1 196 ? 158.968 195.689 151.569 1.00 6.21   ? 106  SER A CB  1 
ATOM   678  O  OG  . SER A 1 196 ? 157.924 195.015 150.921 1.00 6.16   ? 106  SER A OG  1 
ATOM   679  N  N   . SER A 1 197 ? 157.907 198.876 151.678 1.00 6.50   ? 107  SER A N   1 
ATOM   680  C  CA  . SER A 1 197 ? 156.697 199.688 151.766 1.00 6.60   ? 107  SER A CA  1 
ATOM   681  C  C   . SER A 1 197 ? 156.437 200.506 150.505 1.00 6.54   ? 107  SER A C   1 
ATOM   682  O  O   . SER A 1 197 ? 155.375 201.107 150.359 1.00 6.84   ? 107  SER A O   1 
ATOM   683  C  CB  . SER A 1 197 ? 156.761 200.613 152.965 1.00 7.39   ? 107  SER A CB  1 
ATOM   684  N  N   . VAL A 1 198 ? 157.407 200.532 149.595 1.00 6.40   ? 108  VAL A N   1 
ATOM   685  C  CA  . VAL A 1 198 ? 157.249 201.253 148.336 1.00 6.24   ? 108  VAL A CA  1 
ATOM   686  C  C   . VAL A 1 198 ? 156.354 200.486 147.364 1.00 6.08   ? 108  VAL A C   1 
ATOM   687  O  O   . VAL A 1 198 ? 155.903 201.036 146.360 1.00 6.10   ? 108  VAL A O   1 
ATOM   688  C  CB  . VAL A 1 198 ? 158.616 201.505 147.682 1.00 5.87   ? 108  VAL A CB  1 
ATOM   689  C  CG1 . VAL A 1 198 ? 159.514 202.267 148.643 1.00 6.28   ? 108  VAL A CG1 1 
ATOM   690  C  CG2 . VAL A 1 198 ? 159.246 200.178 147.271 1.00 5.54   ? 108  VAL A CG2 1 
ATOM   691  N  N   . LEU A 1 199 ? 156.131 199.206 147.647 1.00 6.02   ? 109  LEU A N   1 
ATOM   692  C  CA  . LEU A 1 199 ? 155.310 198.354 146.796 1.00 5.93   ? 109  LEU A CA  1 
ATOM   693  C  C   . LEU A 1 199 ? 153.845 198.452 147.188 1.00 5.94   ? 109  LEU A C   1 
ATOM   694  O  O   . LEU A 1 199 ? 153.519 198.788 148.326 1.00 6.04   ? 109  LEU A O   1 
ATOM   695  C  CB  . LEU A 1 199 ? 155.754 196.888 146.896 1.00 5.67   ? 109  LEU A CB  1 
ATOM   696  C  CG  . LEU A 1 199 ? 157.187 196.556 146.451 1.00 5.47   ? 109  LEU A CG  1 
ATOM   697  C  CD1 . LEU A 1 199 ? 157.463 195.086 146.744 1.00 5.14   ? 109  LEU A CD1 1 
ATOM   698  C  CD2 . LEU A 1 199 ? 157.346 196.844 144.964 1.00 5.02   ? 109  LEU A CD2 1 
ATOM   699  N  N   . THR A 1 200 ? 152.962 198.120 146.255 1.00 5.88   ? 110  THR A N   1 
ATOM   700  C  CA  . THR A 1 200 ? 151.539 198.076 146.553 1.00 5.84   ? 110  THR A CA  1 
ATOM   701  C  C   . THR A 1 200 ? 151.243 196.866 147.420 1.00 5.73   ? 110  THR A C   1 
ATOM   702  O  O   . THR A 1 200 ? 152.079 195.971 147.551 1.00 5.45   ? 110  THR A O   1 
ATOM   703  C  CB  . THR A 1 200 ? 150.699 198.028 145.263 1.00 5.93   ? 110  THR A CB  1 
ATOM   704  O  OG1 . THR A 1 200 ? 150.990 196.825 144.543 1.00 5.70   ? 110  THR A OG1 1 
ATOM   705  C  CG2 . THR A 1 200 ? 151.027 199.225 144.391 1.00 6.36   ? 110  THR A CG2 1 
ATOM   706  N  N   . ALA A 1 201 ? 150.064 196.835 148.025 1.00 5.74   ? 111  ALA A N   1 
ATOM   707  C  CA  . ALA A 1 201 ? 149.728 195.765 148.957 1.00 5.66   ? 111  ALA A CA  1 
ATOM   708  C  C   . ALA A 1 201 ? 149.818 194.392 148.307 1.00 5.51   ? 111  ALA A C   1 
ATOM   709  O  O   . ALA A 1 201 ? 150.267 193.431 148.933 1.00 5.39   ? 111  ALA A O   1 
ATOM   710  C  CB  . ALA A 1 201 ? 148.329 195.981 149.507 1.00 5.75   ? 111  ALA A CB  1 
ATOM   711  N  N   . GLU A 1 202 ? 149.406 194.298 147.050 1.00 5.55   ? 112  GLU A N   1 
ATOM   712  C  CA  . GLU A 1 202 ? 149.399 193.023 146.351 1.00 5.42   ? 112  GLU A CA  1 
ATOM   713  C  C   . GLU A 1 202 ? 150.809 192.516 146.085 1.00 5.29   ? 112  GLU A C   1 
ATOM   714  O  O   . GLU A 1 202 ? 151.090 191.329 146.258 1.00 5.11   ? 112  GLU A O   1 
ATOM   715  C  CB  . GLU A 1 202 ? 148.639 193.160 145.033 1.00 5.56   ? 112  GLU A CB  1 
ATOM   716  N  N   . LYS A 1 203 ? 151.691 193.411 145.663 1.00 5.25   ? 113  LYS A N   1 
ATOM   717  C  CA  . LYS A 1 203 ? 153.067 193.047 145.357 1.00 5.04   ? 113  LYS A CA  1 
ATOM   718  C  C   . LYS A 1 203 ? 153.874 192.775 146.613 1.00 5.25   ? 113  LYS A C   1 
ATOM   719  O  O   . LYS A 1 203 ? 154.743 191.907 146.627 1.00 4.61   ? 113  LYS A O   1 
ATOM   720  C  CB  . LYS A 1 203 ? 153.728 194.119 144.501 1.00 5.17   ? 113  LYS A CB  1 
ATOM   721  C  CG  . LYS A 1 203 ? 153.217 194.150 143.079 1.00 5.07   ? 113  LYS A CG  1 
ATOM   722  C  CD  . LYS A 1 203 ? 153.930 195.184 142.244 1.00 5.03   ? 113  LYS A CD  1 
ATOM   723  C  CE  . LYS A 1 203 ? 153.445 195.134 140.805 1.00 5.10   ? 113  LYS A CE  1 
ATOM   724  N  NZ  . LYS A 1 203 ? 154.103 196.157 139.958 1.00 5.33   ? 113  LYS A NZ  1 
ATOM   725  N  N   . SER A 1 204 ? 153.590 193.520 147.677 1.00 5.11   ? 114  SER A N   1 
ATOM   726  C  CA  . SER A 1 204 ? 154.288 193.317 148.934 1.00 5.12   ? 114  SER A CA  1 
ATOM   727  C  C   . SER A 1 204 ? 153.935 191.947 149.506 1.00 4.88   ? 114  SER A C   1 
ATOM   728  O  O   . SER A 1 204 ? 154.808 191.192 149.937 1.00 4.61   ? 114  SER A O   1 
ATOM   729  C  CB  . SER A 1 204 ? 153.932 194.414 149.916 1.00 5.47   ? 114  SER A CB  1 
ATOM   730  O  OG  . SER A 1 204 ? 154.648 194.269 151.116 1.00 5.95   ? 114  SER A OG  1 
ATOM   731  N  N   . LYS A 1 205 ? 152.644 191.614 149.465 1.00 4.93   ? 115  LYS A N   1 
ATOM   732  C  CA  . LYS A 1 205 ? 152.166 190.325 149.942 1.00 4.80   ? 115  LYS A CA  1 
ATOM   733  C  C   . LYS A 1 205 ? 152.711 189.182 149.099 1.00 4.52   ? 115  LYS A C   1 
ATOM   734  O  O   . LYS A 1 205 ? 153.086 188.132 149.629 1.00 4.37   ? 115  LYS A O   1 
ATOM   735  C  CB  . LYS A 1 205 ? 150.635 190.293 149.930 1.00 4.95   ? 115  LYS A CB  1 
ATOM   736  C  CG  . LYS A 1 205 ? 150.014 188.990 150.426 1.00 4.92   ? 115  LYS A CG  1 
ATOM   737  C  CD  . LYS A 1 205 ? 150.324 188.742 151.895 1.00 5.03   ? 115  LYS A CD  1 
ATOM   738  C  CE  . LYS A 1 205 ? 149.382 187.703 152.496 1.00 5.07   ? 115  LYS A CE  1 
ATOM   739  N  NZ  . LYS A 1 205 ? 149.589 186.349 151.906 1.00 5.07   ? 115  LYS A NZ  1 
ATOM   740  N  N   . ARG A 1 206 ? 152.761 189.382 147.786 1.00 4.55   ? 116  ARG A N   1 
ATOM   741  C  CA  . ARG A 1 206 ? 153.235 188.342 146.885 1.00 4.32   ? 116  ARG A CA  1 
ATOM   742  C  C   . ARG A 1 206 ? 154.716 188.065 147.091 1.00 4.26   ? 116  ARG A C   1 
ATOM   743  O  O   . ARG A 1 206 ? 155.135 186.907 147.092 1.00 3.92   ? 116  ARG A O   1 
ATOM   744  C  CB  . ARG A 1 206 ? 152.976 188.727 145.437 1.00 4.31   ? 116  ARG A CB  1 
ATOM   745  C  CG  . ARG A 1 206 ? 153.494 187.737 144.399 1.00 3.97   ? 116  ARG A CG  1 
ATOM   746  C  CD  . ARG A 1 206 ? 152.844 186.404 144.510 1.00 3.85   ? 116  ARG A CD  1 
ATOM   747  N  NE  . ARG A 1 206 ? 153.363 185.474 143.522 1.00 3.73   ? 116  ARG A NE  1 
ATOM   748  C  CZ  . ARG A 1 206 ? 153.250 184.132 143.589 1.00 3.69   ? 116  ARG A CZ  1 
ATOM   749  N  NH1 . ARG A 1 206 ? 152.622 183.567 144.598 1.00 3.79   ? 116  ARG A NH1 1 
ATOM   750  N  NH2 . ARG A 1 206 ? 153.776 183.385 142.636 1.00 3.53   ? 116  ARG A NH2 1 
ATOM   751  N  N   . LEU A 1 207 ? 155.506 189.111 147.292 1.00 4.04   ? 117  LEU A N   1 
ATOM   752  C  CA  . LEU A 1 207 ? 156.933 188.924 147.507 1.00 4.02   ? 117  LEU A CA  1 
ATOM   753  C  C   . LEU A 1 207 ? 157.192 188.138 148.783 1.00 4.13   ? 117  LEU A C   1 
ATOM   754  O  O   . LEU A 1 207 ? 158.036 187.241 148.806 1.00 3.66   ? 117  LEU A O   1 
ATOM   755  C  CB  . LEU A 1 207 ? 157.650 190.276 147.566 1.00 4.04   ? 117  LEU A CB  1 
ATOM   756  C  CG  . LEU A 1 207 ? 159.170 190.225 147.802 1.00 3.86   ? 117  LEU A CG  1 
ATOM   757  C  CD1 . LEU A 1 207 ? 159.846 189.383 146.713 1.00 3.61   ? 117  LEU A CD1 1 
ATOM   758  C  CD2 . LEU A 1 207 ? 159.707 191.644 147.795 1.00 3.76   ? 117  LEU A CD2 1 
ATOM   759  N  N   . SER A 1 208 ? 156.451 188.455 149.840 1.00 3.95   ? 118  SER A N   1 
ATOM   760  C  CA  . SER A 1 208 ? 156.595 187.748 151.105 1.00 3.88   ? 118  SER A CA  1 
ATOM   761  C  C   . SER A 1 208 ? 156.287 186.266 150.930 1.00 3.89   ? 118  SER A C   1 
ATOM   762  O  O   . SER A 1 208 ? 157.002 185.404 151.449 1.00 3.66   ? 118  SER A O   1 
ATOM   763  C  CB  . SER A 1 208 ? 155.676 188.352 152.145 1.00 3.95   ? 118  SER A CB  1 
ATOM   764  N  N   . THR A 1 209 ? 155.234 185.975 150.171 1.00 3.87   ? 119  THR A N   1 
ATOM   765  C  CA  . THR A 1 209 ? 154.825 184.603 149.904 1.00 3.81   ? 119  THR A CA  1 
ATOM   766  C  C   . THR A 1 209 ? 155.913 183.826 149.168 1.00 3.68   ? 119  THR A C   1 
ATOM   767  O  O   . THR A 1 209 ? 156.217 182.685 149.520 1.00 3.60   ? 119  THR A O   1 
ATOM   768  C  CB  . THR A 1 209 ? 153.525 184.576 149.078 1.00 3.90   ? 119  THR A CB  1 
ATOM   769  O  OG1 . THR A 1 209 ? 152.481 185.223 149.811 1.00 4.16   ? 119  THR A OG1 1 
ATOM   770  C  CG2 . THR A 1 209 ? 153.112 183.142 148.781 1.00 3.83   ? 119  THR A CG2 1 
ATOM   771  N  N   . ILE A 1 210 ? 156.508 184.451 148.157 1.00 3.62   ? 120  ILE A N   1 
ATOM   772  C  CA  . ILE A 1 210 ? 157.553 183.809 147.368 1.00 3.60   ? 120  ILE A CA  1 
ATOM   773  C  C   . ILE A 1 210 ? 158.767 183.476 148.218 1.00 3.55   ? 120  ILE A C   1 
ATOM   774  O  O   . ILE A 1 210 ? 159.331 182.388 148.102 1.00 3.35   ? 120  ILE A O   1 
ATOM   775  C  CB  . ILE A 1 210 ? 157.978 184.703 146.192 1.00 3.58   ? 120  ILE A CB  1 
ATOM   776  C  CG1 . ILE A 1 210 ? 156.840 184.798 145.186 1.00 3.61   ? 120  ILE A CG1 1 
ATOM   777  C  CG2 . ILE A 1 210 ? 159.242 184.152 145.534 1.00 3.28   ? 120  ILE A CG2 1 
ATOM   778  C  CD1 . ILE A 1 210 ? 157.011 185.902 144.186 1.00 3.53   ? 120  ILE A CD1 1 
ATOM   779  N  N   . LEU A 1 211 ? 159.177 184.411 149.064 1.00 3.56   ? 121  LEU A N   1 
ATOM   780  C  CA  . LEU A 1 211 ? 160.342 184.197 149.908 1.00 3.48   ? 121  LEU A CA  1 
ATOM   781  C  C   . LEU A 1 211 ? 160.121 183.036 150.868 1.00 3.48   ? 121  LEU A C   1 
ATOM   782  O  O   . LEU A 1 211 ? 161.010 182.206 151.066 1.00 3.29   ? 121  LEU A O   1 
ATOM   783  C  CB  . LEU A 1 211 ? 160.653 185.475 150.691 1.00 3.47   ? 121  LEU A CB  1 
ATOM   784  C  CG  . LEU A 1 211 ? 161.159 186.665 149.861 1.00 3.46   ? 121  LEU A CG  1 
ATOM   785  C  CD1 . LEU A 1 211 ? 161.146 187.913 150.718 1.00 3.58   ? 121  LEU A CD1 1 
ATOM   786  C  CD2 . LEU A 1 211 ? 162.559 186.378 149.363 1.00 3.35   ? 121  LEU A CD2 1 
ATOM   787  N  N   . THR A 1 212 ? 158.919 182.951 151.429 1.00 3.45   ? 122  THR A N   1 
ATOM   788  C  CA  . THR A 1 212 ? 158.578 181.852 152.321 1.00 3.44   ? 122  THR A CA  1 
ATOM   789  C  C   . THR A 1 212 ? 158.613 180.528 151.572 1.00 3.43   ? 122  THR A C   1 
ATOM   790  O  O   . THR A 1 212 ? 159.129 179.527 152.077 1.00 3.29   ? 122  THR A O   1 
ATOM   791  C  CB  . THR A 1 212 ? 157.187 182.057 152.951 1.00 3.55   ? 122  THR A CB  1 
ATOM   792  O  OG1 . THR A 1 212 ? 157.187 183.258 153.724 1.00 3.77   ? 122  THR A OG1 1 
ATOM   793  C  CG2 . THR A 1 212 ? 156.836 180.881 153.852 1.00 3.46   ? 122  THR A CG2 1 
ATOM   794  N  N   . THR A 1 213 ? 158.066 180.529 150.363 1.00 3.36   ? 123  THR A N   1 
ATOM   795  C  CA  . THR A 1 213 ? 157.991 179.325 149.554 1.00 3.35   ? 123  THR A CA  1 
ATOM   796  C  C   . THR A 1 213 ? 159.373 178.790 149.194 1.00 3.28   ? 123  THR A C   1 
ATOM   797  O  O   . THR A 1 213 ? 159.621 177.589 149.302 1.00 3.11   ? 123  THR A O   1 
ATOM   798  C  CB  . THR A 1 213 ? 157.192 179.585 148.267 1.00 3.33   ? 123  THR A CB  1 
ATOM   799  O  OG1 . THR A 1 213 ? 155.865 179.996 148.605 1.00 3.49   ? 123  THR A OG1 1 
ATOM   800  C  CG2 . THR A 1 213 ? 157.122 178.321 147.434 1.00 3.22   ? 123  THR A CG2 1 
ATOM   801  N  N   . MET A 1 214 ? 160.276 179.672 148.765 1.00 3.12   ? 124  MET A N   1 
ATOM   802  C  CA  . MET A 1 214 ? 161.607 179.228 148.374 1.00 3.13   ? 124  MET A CA  1 
ATOM   803  C  C   . MET A 1 214 ? 162.351 178.616 149.551 1.00 3.15   ? 124  MET A C   1 
ATOM   804  O  O   . MET A 1 214 ? 163.014 177.587 149.408 1.00 3.01   ? 124  MET A O   1 
ATOM   805  C  CB  . MET A 1 214 ? 162.422 180.378 147.785 1.00 3.05   ? 124  MET A CB  1 
ATOM   806  C  CG  . MET A 1 214 ? 161.965 180.847 146.407 1.00 3.04   ? 124  MET A CG  1 
ATOM   807  S  SD  . MET A 1 214 ? 163.155 181.954 145.607 1.00 3.09   ? 124  MET A SD  1 
ATOM   808  C  CE  . MET A 1 214 ? 163.129 183.390 146.670 1.00 3.11   ? 124  MET A CE  1 
ATOM   809  N  N   . SER A 1 215 ? 162.213 179.229 150.723 1.00 3.08   ? 125  SER A N   1 
ATOM   810  C  CA  . SER A 1 215 ? 162.860 178.722 151.925 1.00 3.11   ? 125  SER A CA  1 
ATOM   811  C  C   . SER A 1 215 ? 162.356 177.333 152.275 1.00 3.20   ? 125  SER A C   1 
ATOM   812  O  O   . SER A 1 215 ? 163.143 176.441 152.600 1.00 3.09   ? 125  SER A O   1 
ATOM   813  C  CB  . SER A 1 215 ? 162.621 179.665 153.083 1.00 3.09   ? 125  SER A CB  1 
ATOM   814  O  OG  . SER A 1 215 ? 163.191 179.165 154.262 1.00 3.40   ? 125  SER A OG  1 
ATOM   815  N  N   . THR A 1 216 ? 161.043 177.145 152.192 1.00 3.11   ? 126  THR A N   1 
ATOM   816  C  CA  . THR A 1 216 ? 160.433 175.862 152.509 1.00 3.18   ? 126  THR A CA  1 
ATOM   817  C  C   . THR A 1 216 ? 160.891 174.766 151.553 1.00 3.32   ? 126  THR A C   1 
ATOM   818  O  O   . THR A 1 216 ? 161.207 173.658 151.983 1.00 3.12   ? 126  THR A O   1 
ATOM   819  C  CB  . THR A 1 216 ? 158.897 175.965 152.490 1.00 3.19   ? 126  THR A CB  1 
ATOM   820  O  OG1 . THR A 1 216 ? 158.472 176.921 153.467 1.00 3.26   ? 126  THR A OG1 1 
ATOM   821  C  CG2 . THR A 1 216 ? 158.275 174.610 152.813 1.00 3.14   ? 126  THR A CG2 1 
ATOM   822  N  N   . ILE A 1 217 ? 160.936 175.071 150.258 1.00 3.08   ? 127  ILE A N   1 
ATOM   823  C  CA  . ILE A 1 217 ? 161.346 174.077 149.273 1.00 3.10   ? 127  ILE A CA  1 
ATOM   824  C  C   . ILE A 1 217 ? 162.769 173.613 149.536 1.00 3.19   ? 127  ILE A C   1 
ATOM   825  O  O   . ILE A 1 217 ? 163.061 172.420 149.475 1.00 3.16   ? 127  ILE A O   1 
ATOM   826  C  CB  . ILE A 1 217 ? 161.231 174.627 147.838 1.00 3.05   ? 127  ILE A CB  1 
ATOM   827  C  CG1 . ILE A 1 217 ? 159.758 174.815 147.468 1.00 3.02   ? 127  ILE A CG1 1 
ATOM   828  C  CG2 . ILE A 1 217 ? 161.927 173.688 146.850 1.00 3.00   ? 127  ILE A CG2 1 
ATOM   829  C  CD1 . ILE A 1 217 ? 159.538 175.628 146.215 1.00 2.97   ? 127  ILE A CD1 1 
ATOM   830  N  N   . TYR A 1 218 ? 163.654 174.559 149.822 1.00 3.10   ? 128  TYR A N   1 
ATOM   831  C  CA  . TYR A 1 218 ? 165.044 174.240 150.107 1.00 3.13   ? 128  TYR A CA  1 
ATOM   832  C  C   . TYR A 1 218 ? 165.169 173.295 151.301 1.00 3.18   ? 128  TYR A C   1 
ATOM   833  O  O   . TYR A 1 218 ? 165.830 172.259 151.218 1.00 3.15   ? 128  TYR A O   1 
ATOM   834  C  CB  . TYR A 1 218 ? 165.824 175.533 150.369 1.00 3.04   ? 128  TYR A CB  1 
ATOM   835  C  CG  . TYR A 1 218 ? 167.290 175.336 150.690 1.00 3.00   ? 128  TYR A CG  1 
ATOM   836  C  CD1 . TYR A 1 218 ? 168.218 175.281 149.670 1.00 2.94   ? 128  TYR A CD1 1 
ATOM   837  C  CD2 . TYR A 1 218 ? 167.704 175.214 152.006 1.00 3.05   ? 128  TYR A CD2 1 
ATOM   838  C  CE1 . TYR A 1 218 ? 169.550 175.109 149.963 1.00 2.94   ? 128  TYR A CE1 1 
ATOM   839  C  CE2 . TYR A 1 218 ? 169.038 175.037 152.294 1.00 3.06   ? 128  TYR A CE2 1 
ATOM   840  C  CZ  . TYR A 1 218 ? 169.959 174.986 151.275 1.00 2.99   ? 128  TYR A CZ  1 
ATOM   841  O  OH  . TYR A 1 218 ? 171.295 174.815 151.555 1.00 3.06   ? 128  TYR A OH  1 
ATOM   842  N  N   . SER A 1 219 ? 164.537 173.654 152.417 1.00 3.13   ? 129  SER A N   1 
ATOM   843  C  CA  . SER A 1 219 ? 164.729 172.926 153.669 1.00 3.18   ? 129  SER A CA  1 
ATOM   844  C  C   . SER A 1 219 ? 164.053 171.556 153.708 1.00 3.24   ? 129  SER A C   1 
ATOM   845  O  O   . SER A 1 219 ? 164.445 170.699 154.500 1.00 3.23   ? 129  SER A O   1 
ATOM   846  C  CB  . SER A 1 219 ? 164.230 173.757 154.834 1.00 3.16   ? 129  SER A CB  1 
ATOM   847  O  OG  . SER A 1 219 ? 162.832 173.775 154.885 1.00 3.21   ? 129  SER A OG  1 
ATOM   848  N  N   . THR A 1 220 ? 163.051 171.332 152.863 1.00 3.25   ? 130  THR A N   1 
ATOM   849  C  CA  . THR A 1 220 ? 162.337 170.061 152.881 1.00 3.33   ? 130  THR A CA  1 
ATOM   850  C  C   . THR A 1 220 ? 162.636 169.205 151.655 1.00 3.41   ? 130  THR A C   1 
ATOM   851  O  O   . THR A 1 220 ? 161.910 168.252 151.371 1.00 3.57   ? 130  THR A O   1 
ATOM   852  C  CB  . THR A 1 220 ? 160.812 170.269 152.986 1.00 3.27   ? 130  THR A CB  1 
ATOM   853  O  OG1 . THR A 1 220 ? 160.333 170.955 151.824 1.00 3.30   ? 130  THR A OG1 1 
ATOM   854  C  CG2 . THR A 1 220 ? 160.487 171.102 154.219 1.00 3.21   ? 130  THR A CG2 1 
ATOM   855  N  N   . GLY A 1 221 ? 163.676 169.558 150.909 1.00 3.38   ? 131  GLY A N   1 
ATOM   856  C  CA  . GLY A 1 221 ? 164.012 168.819 149.697 1.00 3.51   ? 131  GLY A CA  1 
ATOM   857  C  C   . GLY A 1 221 ? 164.619 167.455 149.992 1.00 3.73   ? 131  GLY A C   1 
ATOM   858  O  O   . GLY A 1 221 ? 165.411 167.307 150.926 1.00 3.82   ? 131  GLY A O   1 
ATOM   859  N  N   . LYS A 1 222 ? 164.284 166.470 149.164 1.00 3.83   ? 132  LYS A N   1 
ATOM   860  C  CA  . LYS A 1 222 ? 164.872 165.143 149.266 1.00 3.95   ? 132  LYS A CA  1 
ATOM   861  C  C   . LYS A 1 222 ? 165.394 164.650 147.933 1.00 3.95   ? 132  LYS A C   1 
ATOM   862  O  O   . LYS A 1 222 ? 164.873 165.003 146.875 1.00 3.86   ? 132  LYS A O   1 
ATOM   863  C  CB  . LYS A 1 222 ? 163.869 164.122 149.798 1.00 4.09   ? 132  LYS A CB  1 
ATOM   864  C  CG  . LYS A 1 222 ? 163.359 164.402 151.183 1.00 4.14   ? 132  LYS A CG  1 
ATOM   865  C  CD  . LYS A 1 222 ? 162.430 163.301 151.650 1.00 4.36   ? 132  LYS A CD  1 
ATOM   866  C  CE  . LYS A 1 222 ? 163.194 162.031 151.935 1.00 4.56   ? 132  LYS A CE  1 
ATOM   867  N  NZ  . LYS A 1 222 ? 164.078 162.170 153.109 1.00 4.70   ? 132  LYS A NZ  1 
ATOM   868  N  N   . VAL A 1 223 ? 166.401 163.797 148.005 1.00 4.03   ? 133  VAL A N   1 
ATOM   869  C  CA  . VAL A 1 223 ? 166.935 163.110 146.837 1.00 4.13   ? 133  VAL A CA  1 
ATOM   870  C  C   . VAL A 1 223 ? 166.938 161.606 147.105 1.00 4.38   ? 133  VAL A C   1 
ATOM   871  O  O   . VAL A 1 223 ? 167.424 161.164 148.154 1.00 4.37   ? 133  VAL A O   1 
ATOM   872  C  CB  . VAL A 1 223 ? 168.361 163.605 146.524 1.00 3.85   ? 133  VAL A CB  1 
ATOM   873  C  CG1 . VAL A 1 223 ? 168.950 162.871 145.328 1.00 3.83   ? 133  VAL A CG1 1 
ATOM   874  C  CG2 . VAL A 1 223 ? 168.317 165.092 146.250 1.00 3.61   ? 133  VAL A CG2 1 
ATOM   875  N  N   . CYS A 1 224 ? 166.365 160.830 146.188 1.00 4.45   ? 134  CYS A N   1 
ATOM   876  C  CA  . CYS A 1 224 ? 166.227 159.378 146.348 1.00 4.62   ? 134  CYS A CA  1 
ATOM   877  C  C   . CYS A 1 224 ? 167.200 158.633 145.479 1.00 4.70   ? 134  CYS A C   1 
ATOM   878  O  O   . CYS A 1 224 ? 167.323 158.933 144.267 1.00 4.72   ? 134  CYS A O   1 
ATOM   879  C  CB  . CYS A 1 224 ? 164.789 158.944 146.084 1.00 4.75   ? 134  CYS A CB  1 
ATOM   880  S  SG  . CYS A 1 224 ? 163.559 159.696 147.194 1.00 5.86   ? 134  CYS A SG  1 
ATOM   881  N  N   . ASN A 1 225 ? 167.870 157.639 146.035 1.00 4.71   ? 135  ASN A N   1 
ATOM   882  C  CA  . ASN A 1 225 ? 168.825 156.815 145.322 1.00 4.83   ? 135  ASN A CA  1 
ATOM   883  C  C   . ASN A 1 225 ? 168.159 156.195 144.096 1.00 5.10   ? 135  ASN A C   1 
ATOM   884  O  O   . ASN A 1 225 ? 167.177 155.467 144.234 1.00 5.02   ? 135  ASN A O   1 
ATOM   885  C  CB  . ASN A 1 225 ? 169.382 155.751 146.256 1.00 4.82   ? 135  ASN A CB  1 
ATOM   886  C  CG  . ASN A 1 225 ? 170.471 154.911 145.646 1.00 4.94   ? 135  ASN A CG  1 
ATOM   887  O  OD1 . ASN A 1 225 ? 170.535 154.717 144.427 1.00 5.10   ? 135  ASN A OD1 1 
ATOM   888  N  ND2 . ASN A 1 225 ? 171.327 154.398 146.482 1.00 4.86   ? 135  ASN A ND2 1 
ATOM   889  N  N   . PRO A 1 226 ? 168.664 156.470 142.885 1.00 5.00   ? 136  PRO A N   1 
ATOM   890  C  CA  . PRO A 1 226 ? 168.084 156.077 141.615 1.00 5.27   ? 136  PRO A CA  1 
ATOM   891  C  C   . PRO A 1 226 ? 168.029 154.565 141.443 1.00 5.53   ? 136  PRO A C   1 
ATOM   892  O  O   . PRO A 1 226 ? 167.310 154.062 140.582 1.00 5.70   ? 136  PRO A O   1 
ATOM   893  C  CB  . PRO A 1 226 ? 169.019 156.738 140.598 1.00 5.21   ? 136  PRO A CB  1 
ATOM   894  C  CG  . PRO A 1 226 ? 170.326 156.934 141.328 1.00 4.99   ? 136  PRO A CG  1 
ATOM   895  C  CD  . PRO A 1 226 ? 169.933 157.213 142.764 1.00 4.78   ? 136  PRO A CD  1 
ATOM   896  N  N   . ASN A 1 227 ? 168.794 153.840 142.251 1.00 5.47   ? 137  ASN A N   1 
ATOM   897  C  CA  . ASN A 1 227 ? 168.791 152.386 142.182 1.00 5.62   ? 137  ASN A CA  1 
ATOM   898  C  C   . ASN A 1 227 ? 168.264 151.755 143.466 1.00 5.56   ? 137  ASN A C   1 
ATOM   899  O  O   . ASN A 1 227 ? 168.427 150.556 143.694 1.00 5.61   ? 137  ASN A O   1 
ATOM   900  C  CB  . ASN A 1 227 ? 170.170 151.870 141.831 1.00 6.02   ? 137  ASN A CB  1 
ATOM   901  C  CG  . ASN A 1 227 ? 170.483 152.071 140.367 1.00 6.85   ? 137  ASN A CG  1 
ATOM   902  O  OD1 . ASN A 1 227 ? 169.916 151.379 139.514 1.00 7.56   ? 137  ASN A OD1 1 
ATOM   903  N  ND2 . ASN A 1 227 ? 171.353 152.997 140.059 1.00 7.28   ? 137  ASN A ND2 1 
ATOM   904  N  N   . ASN A 1 228 ? 167.613 152.569 144.288 1.00 5.27   ? 138  ASN A N   1 
ATOM   905  C  CA  . ASN A 1 228 ? 167.016 152.127 145.541 1.00 5.21   ? 138  ASN A CA  1 
ATOM   906  C  C   . ASN A 1 228 ? 165.986 153.149 146.010 1.00 6.06   ? 138  ASN A C   1 
ATOM   907  O  O   . ASN A 1 228 ? 166.287 153.976 146.868 1.00 4.83   ? 138  ASN A O   1 
ATOM   908  C  CB  . ASN A 1 228 ? 168.079 151.917 146.603 1.00 5.25   ? 138  ASN A CB  1 
ATOM   909  C  CG  . ASN A 1 228 ? 167.522 151.305 147.852 1.00 5.33   ? 138  ASN A CG  1 
ATOM   910  O  OD1 . ASN A 1 228 ? 166.308 151.105 147.968 1.00 5.34   ? 138  ASN A OD1 1 
ATOM   911  N  ND2 . ASN A 1 228 ? 168.382 151.003 148.788 1.00 5.52   ? 138  ASN A ND2 1 
ATOM   912  N  N   . PRO A 1 229 ? 164.771 153.107 145.455 1.00 5.10   ? 139  PRO A N   1 
ATOM   913  C  CA  . PRO A 1 229 ? 163.696 154.075 145.603 1.00 5.14   ? 139  PRO A CA  1 
ATOM   914  C  C   . PRO A 1 229 ? 163.269 154.281 147.053 1.00 5.16   ? 139  PRO A C   1 
ATOM   915  O  O   . PRO A 1 229 ? 162.608 155.266 147.374 1.00 5.21   ? 139  PRO A O   1 
ATOM   916  C  CB  . PRO A 1 229 ? 162.564 153.437 144.788 1.00 5.04   ? 139  PRO A CB  1 
ATOM   917  C  CG  . PRO A 1 229 ? 163.258 152.528 143.808 1.00 5.07   ? 139  PRO A CG  1 
ATOM   918  C  CD  . PRO A 1 229 ? 164.451 151.994 144.556 1.00 5.20   ? 139  PRO A CD  1 
ATOM   919  N  N   . GLN A 1 230 ? 163.616 153.339 147.923 1.00 5.16   ? 140  GLN A N   1 
ATOM   920  C  CA  . GLN A 1 230 ? 163.237 153.428 149.326 1.00 5.19   ? 140  GLN A CA  1 
ATOM   921  C  C   . GLN A 1 230 ? 164.313 154.089 150.181 1.00 5.13   ? 140  GLN A C   1 
ATOM   922  O  O   . GLN A 1 230 ? 164.146 154.231 151.393 1.00 5.30   ? 140  GLN A O   1 
ATOM   923  C  CB  . GLN A 1 230 ? 162.921 152.040 149.881 1.00 5.26   ? 140  GLN A CB  1 
ATOM   924  C  CG  . GLN A 1 230 ? 161.590 151.467 149.422 1.00 5.28   ? 140  GLN A CG  1 
ATOM   925  C  CD  . GLN A 1 230 ? 161.620 150.983 147.991 1.00 5.29   ? 140  GLN A CD  1 
ATOM   926  O  OE1 . GLN A 1 230 ? 162.579 150.340 147.556 1.00 5.30   ? 140  GLN A OE1 1 
ATOM   927  N  NE2 . GLN A 1 230 ? 160.563 151.283 147.249 1.00 5.39   ? 140  GLN A NE2 1 
ATOM   928  N  N   . GLN A 1 231 ? 165.416 154.488 149.558 1.00 5.09   ? 141  GLN A N   1 
ATOM   929  C  CA  . GLN A 1 231 ? 166.504 155.139 150.277 1.00 4.98   ? 141  GLN A CA  1 
ATOM   930  C  C   . GLN A 1 231 ? 166.596 156.617 149.903 1.00 4.95   ? 141  GLN A C   1 
ATOM   931  O  O   . GLN A 1 231 ? 167.230 156.971 148.906 1.00 4.76   ? 141  GLN A O   1 
ATOM   932  C  CB  . GLN A 1 231 ? 167.831 154.438 149.980 1.00 5.02   ? 141  GLN A CB  1 
ATOM   933  C  CG  . GLN A 1 231 ? 169.014 155.002 150.736 1.00 5.00   ? 141  GLN A CG  1 
ATOM   934  C  CD  . GLN A 1 231 ? 170.306 154.287 150.412 1.00 5.12   ? 141  GLN A CD  1 
ATOM   935  O  OE1 . GLN A 1 231 ? 170.800 154.345 149.284 1.00 5.17   ? 141  GLN A OE1 1 
ATOM   936  N  NE2 . GLN A 1 231 ? 170.867 153.604 151.400 1.00 5.29   ? 141  GLN A NE2 1 
ATOM   937  N  N   . CYS A 1 232 ? 165.956 157.472 150.706 1.00 4.68   ? 142  CYS A N   1 
ATOM   938  C  CA  . CYS A 1 232 ? 165.865 158.907 150.444 1.00 4.57   ? 142  CYS A CA  1 
ATOM   939  C  C   . CYS A 1 232 ? 166.537 159.683 151.561 1.00 4.47   ? 142  CYS A C   1 
ATOM   940  O  O   . CYS A 1 232 ? 166.422 159.326 152.736 1.00 4.47   ? 142  CYS A O   1 
ATOM   941  C  CB  . CYS A 1 232 ? 164.397 159.343 150.311 1.00 4.57   ? 142  CYS A CB  1 
ATOM   942  S  SG  . CYS A 1 232 ? 163.497 158.534 148.941 1.00 5.19   ? 142  CYS A SG  1 
ATOM   943  N  N   . PHE A 1 233 ? 167.229 160.754 151.198 1.00 4.43   ? 143  PHE A N   1 
ATOM   944  C  CA  . PHE A 1 233 ? 167.914 161.568 152.188 1.00 4.37   ? 143  PHE A CA  1 
ATOM   945  C  C   . PHE A 1 233 ? 167.469 163.017 152.131 1.00 4.35   ? 143  PHE A C   1 
ATOM   946  O  O   . PHE A 1 233 ? 167.211 163.563 151.057 1.00 4.19   ? 143  PHE A O   1 
ATOM   947  C  CB  . PHE A 1 233 ? 169.425 161.533 151.967 1.00 4.36   ? 143  PHE A CB  1 
ATOM   948  C  CG  . PHE A 1 233 ? 170.039 160.176 151.994 1.00 4.45   ? 143  PHE A CG  1 
ATOM   949  C  CD1 . PHE A 1 233 ? 170.499 159.622 153.172 1.00 4.55   ? 143  PHE A CD1 1 
ATOM   950  C  CD2 . PHE A 1 233 ? 170.168 159.452 150.825 1.00 4.50   ? 143  PHE A CD2 1 
ATOM   951  C  CE1 . PHE A 1 233 ? 171.073 158.369 153.178 1.00 4.81   ? 143  PHE A CE1 1 
ATOM   952  C  CE2 . PHE A 1 233 ? 170.741 158.206 150.828 1.00 4.66   ? 143  PHE A CE2 1 
ATOM   953  C  CZ  . PHE A 1 233 ? 171.192 157.661 152.005 1.00 4.97   ? 143  PHE A CZ  1 
ATOM   954  N  N   . THR A 1 234 ? 167.453 163.652 153.292 1.00 4.29   ? 144  THR A N   1 
ATOM   955  C  CA  . THR A 1 234 ? 167.233 165.085 153.403 1.00 4.26   ? 144  THR A CA  1 
ATOM   956  C  C   . THR A 1 234 ? 168.547 165.804 153.177 1.00 4.29   ? 144  THR A C   1 
ATOM   957  O  O   . THR A 1 234 ? 169.600 165.168 153.139 1.00 4.18   ? 144  THR A O   1 
ATOM   958  C  CB  . THR A 1 234 ? 166.662 165.441 154.783 1.00 4.45   ? 144  THR A CB  1 
ATOM   959  O  OG1 . THR A 1 234 ? 167.599 165.054 155.797 1.00 4.44   ? 144  THR A OG1 1 
ATOM   960  C  CG2 . THR A 1 234 ? 165.356 164.714 155.002 1.00 4.63   ? 144  THR A CG2 1 
ATOM   961  N  N   . LEU A 1 235 ? 168.510 167.122 153.047 1.00 4.12   ? 145  LEU A N   1 
ATOM   962  C  CA  . LEU A 1 235 ? 169.741 167.851 152.770 1.00 4.05   ? 145  LEU A CA  1 
ATOM   963  C  C   . LEU A 1 235 ? 170.830 167.559 153.793 1.00 4.44   ? 145  LEU A C   1 
ATOM   964  O  O   . LEU A 1 235 ? 171.998 167.432 153.434 1.00 3.86   ? 145  LEU A O   1 
ATOM   965  C  CB  . LEU A 1 235 ? 169.481 169.356 152.706 1.00 3.79   ? 145  LEU A CB  1 
ATOM   966  C  CG  . LEU A 1 235 ? 170.721 170.241 152.436 1.00 3.74   ? 145  LEU A CG  1 
ATOM   967  C  CD1 . LEU A 1 235 ? 171.386 169.838 151.112 1.00 3.61   ? 145  LEU A CD1 1 
ATOM   968  C  CD2 . LEU A 1 235 ? 170.286 171.688 152.392 1.00 3.45   ? 145  LEU A CD2 1 
ATOM   969  N  N   . SER A 1 236 ? 170.459 167.435 155.062 1.00 4.24   ? 146  SER A N   1 
ATOM   970  C  CA  . SER A 1 236 ? 171.447 167.167 156.102 1.00 4.24   ? 146  SER A CA  1 
ATOM   971  C  C   . SER A 1 236 ? 172.149 165.832 155.864 1.00 4.22   ? 146  SER A C   1 
ATOM   972  O  O   . SER A 1 236 ? 173.351 165.701 156.101 1.00 4.28   ? 146  SER A O   1 
ATOM   973  C  CB  . SER A 1 236 ? 170.783 167.158 157.463 1.00 4.23   ? 146  SER A CB  1 
ATOM   974  N  N   . GLY A 1 237 ? 171.391 164.841 155.402 1.00 4.29   ? 147  GLY A N   1 
ATOM   975  C  CA  . GLY A 1 237 ? 171.940 163.524 155.111 1.00 4.23   ? 147  GLY A CA  1 
ATOM   976  C  C   . GLY A 1 237 ? 172.836 163.579 153.883 1.00 4.36   ? 147  GLY A C   1 
ATOM   977  O  O   . GLY A 1 237 ? 173.905 162.969 153.849 1.00 4.31   ? 147  GLY A O   1 
ATOM   978  N  N   . LEU A 1 238 ? 172.392 164.316 152.872 1.00 4.16   ? 148  LEU A N   1 
ATOM   979  C  CA  . LEU A 1 238 ? 173.132 164.418 151.624 1.00 4.21   ? 148  LEU A CA  1 
ATOM   980  C  C   . LEU A 1 238 ? 174.454 165.137 151.845 1.00 4.25   ? 148  LEU A C   1 
ATOM   981  O  O   . LEU A 1 238 ? 175.481 164.744 151.290 1.00 4.06   ? 148  LEU A O   1 
ATOM   982  C  CB  . LEU A 1 238 ? 172.299 165.172 150.583 1.00 4.13   ? 148  LEU A CB  1 
ATOM   983  C  CG  . LEU A 1 238 ? 170.986 164.495 150.144 1.00 4.14   ? 148  LEU A CG  1 
ATOM   984  C  CD1 . LEU A 1 238 ? 170.177 165.472 149.311 1.00 3.98   ? 148  LEU A CD1 1 
ATOM   985  C  CD2 . LEU A 1 238 ? 171.285 163.224 149.353 1.00 4.14   ? 148  LEU A CD2 1 
ATOM   986  N  N   . GLU A 1 239 ? 174.439 166.170 152.683 1.00 4.16   ? 149  GLU A N   1 
ATOM   987  C  CA  . GLU A 1 239 ? 175.657 166.903 153.005 1.00 4.15   ? 149  GLU A CA  1 
ATOM   988  C  C   . GLU A 1 239 ? 176.641 166.009 153.739 1.00 4.68   ? 149  GLU A C   1 
ATOM   989  O  O   . GLU A 1 239 ? 177.835 166.019 153.447 1.00 4.23   ? 149  GLU A O   1 
ATOM   990  C  CB  . GLU A 1 239 ? 175.347 168.127 153.868 1.00 4.24   ? 149  GLU A CB  1 
ATOM   991  C  CG  . GLU A 1 239 ? 174.665 169.276 153.143 1.00 4.09   ? 149  GLU A CG  1 
ATOM   992  C  CD  . GLU A 1 239 ? 174.209 170.357 154.088 1.00 4.16   ? 149  GLU A CD  1 
ATOM   993  O  OE1 . GLU A 1 239 ? 174.263 170.140 155.275 1.00 4.65   ? 149  GLU A OE1 1 
ATOM   994  O  OE2 . GLU A 1 239 ? 173.815 171.400 153.627 1.00 3.94   ? 149  GLU A OE2 1 
ATOM   995  N  N   . ASP A 1 240 ? 176.132 165.202 154.665 1.00 4.23   ? 150  ASP A N   1 
ATOM   996  C  CA  . ASP A 1 240 ? 176.983 164.308 155.432 1.00 4.42   ? 150  ASP A CA  1 
ATOM   997  C  C   . ASP A 1 240 ? 177.716 163.330 154.522 1.00 4.43   ? 150  ASP A C   1 
ATOM   998  O  O   . ASP A 1 240 ? 178.889 163.029 154.741 1.00 4.42   ? 150  ASP A O   1 
ATOM   999  C  CB  . ASP A 1 240 ? 176.149 163.540 156.462 1.00 4.46   ? 150  ASP A CB  1 
ATOM   1000 N  N   . ILE A 1 241 ? 177.032 162.864 153.479 1.00 4.27   ? 151  ILE A N   1 
ATOM   1001 C  CA  . ILE A 1 241 ? 177.640 161.947 152.522 1.00 4.24   ? 151  ILE A CA  1 
ATOM   1002 C  C   . ILE A 1 241 ? 178.671 162.660 151.652 1.00 4.27   ? 151  ILE A C   1 
ATOM   1003 O  O   . ILE A 1 241 ? 179.768 162.150 151.438 1.00 4.16   ? 151  ILE A O   1 
ATOM   1004 C  CB  . ILE A 1 241 ? 176.580 161.288 151.618 1.00 4.24   ? 151  ILE A CB  1 
ATOM   1005 C  CG1 . ILE A 1 241 ? 175.660 160.390 152.455 1.00 4.29   ? 151  ILE A CG1 1 
ATOM   1006 C  CG2 . ILE A 1 241 ? 177.272 160.469 150.526 1.00 4.19   ? 151  ILE A CG2 1 
ATOM   1007 C  CD1 . ILE A 1 241 ? 174.405 159.944 151.727 1.00 4.48   ? 151  ILE A CD1 1 
ATOM   1008 N  N   . MET A 1 242 ? 178.320 163.837 151.141 1.00 4.14   ? 152  MET A N   1 
ATOM   1009 C  CA  . MET A 1 242 ? 179.215 164.573 150.250 1.00 4.01   ? 152  MET A CA  1 
ATOM   1010 C  C   . MET A 1 242 ? 180.524 164.944 150.937 1.00 4.11   ? 152  MET A C   1 
ATOM   1011 O  O   . MET A 1 242 ? 181.576 164.991 150.303 1.00 3.95   ? 152  MET A O   1 
ATOM   1012 C  CB  . MET A 1 242 ? 178.521 165.823 149.714 1.00 3.78   ? 152  MET A CB  1 
ATOM   1013 C  CG  . MET A 1 242 ? 177.404 165.545 148.714 1.00 3.73   ? 152  MET A CG  1 
ATOM   1014 S  SD  . MET A 1 242 ? 177.977 164.738 147.197 1.00 3.72   ? 152  MET A SD  1 
ATOM   1015 C  CE  . MET A 1 242 ? 178.669 166.112 146.281 1.00 3.29   ? 152  MET A CE  1 
ATOM   1016 N  N   . GLU A 1 243 ? 180.472 165.182 152.236 1.00 4.04   ? 153  GLU A N   1 
ATOM   1017 C  CA  . GLU A 1 243 ? 181.665 165.554 152.982 1.00 4.41   ? 153  GLU A CA  1 
ATOM   1018 C  C   . GLU A 1 243 ? 182.654 164.402 153.179 1.00 4.38   ? 153  GLU A C   1 
ATOM   1019 O  O   . GLU A 1 243 ? 183.811 164.644 153.524 1.00 4.56   ? 153  GLU A O   1 
ATOM   1020 C  CB  . GLU A 1 243 ? 181.275 166.132 154.342 1.00 4.42   ? 153  GLU A CB  1 
ATOM   1021 C  CG  . GLU A 1 243 ? 180.587 167.493 154.271 1.00 4.42   ? 153  GLU A CG  1 
ATOM   1022 C  CD  . GLU A 1 243 ? 180.188 168.019 155.619 1.00 4.79   ? 153  GLU A CD  1 
ATOM   1023 O  OE1 . GLU A 1 243 ? 180.331 167.304 156.582 1.00 4.94   ? 153  GLU A OE1 1 
ATOM   1024 O  OE2 . GLU A 1 243 ? 179.742 169.140 155.688 1.00 4.64   ? 153  GLU A OE2 1 
ATOM   1025 N  N   . LYS A 1 244 ? 182.204 163.157 153.019 1.00 4.44   ? 154  LYS A N   1 
ATOM   1026 C  CA  . LYS A 1 244 ? 183.061 162.010 153.315 1.00 4.57   ? 154  LYS A CA  1 
ATOM   1027 C  C   . LYS A 1 244 ? 183.256 161.025 152.158 1.00 4.32   ? 154  LYS A C   1 
ATOM   1028 O  O   . LYS A 1 244 ? 184.283 160.352 152.084 1.00 4.53   ? 154  LYS A O   1 
ATOM   1029 C  CB  . LYS A 1 244 ? 182.530 161.268 154.540 1.00 4.66   ? 154  LYS A CB  1 
ATOM   1030 C  CG  . LYS A 1 244 ? 182.701 162.029 155.852 1.00 5.03   ? 154  LYS A CG  1 
ATOM   1031 C  CD  . LYS A 1 244 ? 182.266 161.191 157.051 1.00 5.22   ? 154  LYS A CD  1 
ATOM   1032 C  CE  . LYS A 1 244 ? 180.767 161.312 157.318 1.00 4.95   ? 154  LYS A CE  1 
ATOM   1033 N  NZ  . LYS A 1 244 ? 180.420 162.626 157.930 1.00 4.84   ? 154  LYS A NZ  1 
ATOM   1034 N  N   . SER A 1 245 ? 182.257 160.888 151.292 1.00 4.24   ? 155  SER A N   1 
ATOM   1035 C  CA  . SER A 1 245 ? 182.288 159.863 150.250 1.00 4.12   ? 155  SER A CA  1 
ATOM   1036 C  C   . SER A 1 245 ? 183.423 160.070 149.260 1.00 4.02   ? 155  SER A C   1 
ATOM   1037 O  O   . SER A 1 245 ? 183.679 161.189 148.817 1.00 3.93   ? 155  SER A O   1 
ATOM   1038 C  CB  . SER A 1 245 ? 180.978 159.845 149.491 1.00 4.03   ? 155  SER A CB  1 
ATOM   1039 O  OG  . SER A 1 245 ? 181.020 158.912 148.445 1.00 3.97   ? 155  SER A OG  1 
ATOM   1040 N  N   . LYS A 1 246 ? 184.069 158.974 148.877 1.00 4.01   ? 156  LYS A N   1 
ATOM   1041 C  CA  . LYS A 1 246 ? 185.107 158.995 147.853 1.00 3.94   ? 156  LYS A CA  1 
ATOM   1042 C  C   . LYS A 1 246 ? 184.684 158.193 146.627 1.00 3.87   ? 156  LYS A C   1 
ATOM   1043 O  O   . LYS A 1 246 ? 185.515 157.824 145.799 1.00 3.75   ? 156  LYS A O   1 
ATOM   1044 C  CB  . LYS A 1 246 ? 186.426 158.453 148.407 1.00 4.03   ? 156  LYS A CB  1 
ATOM   1045 C  CG  . LYS A 1 246 ? 187.056 159.324 149.493 1.00 4.19   ? 156  LYS A CG  1 
ATOM   1046 C  CD  . LYS A 1 246 ? 188.476 158.868 149.852 1.00 4.46   ? 156  LYS A CD  1 
ATOM   1047 C  CE  . LYS A 1 246 ? 188.486 157.544 150.616 1.00 4.45   ? 156  LYS A CE  1 
ATOM   1048 N  NZ  . LYS A 1 246 ? 187.805 157.656 151.936 1.00 4.71   ? 156  LYS A NZ  1 
ATOM   1049 N  N   . ASP A 1 247 ? 183.392 157.888 146.539 1.00 3.90   ? 157  ASP A N   1 
ATOM   1050 C  CA  . ASP A 1 247 ? 182.854 157.110 145.431 1.00 4.05   ? 157  ASP A CA  1 
ATOM   1051 C  C   . ASP A 1 247 ? 182.344 158.022 144.319 1.00 4.10   ? 157  ASP A C   1 
ATOM   1052 O  O   . ASP A 1 247 ? 181.420 158.807 144.528 1.00 3.92   ? 157  ASP A O   1 
ATOM   1053 C  CB  . ASP A 1 247 ? 181.735 156.188 145.919 1.00 4.08   ? 157  ASP A CB  1 
ATOM   1054 C  CG  . ASP A 1 247 ? 181.244 155.226 144.850 1.00 4.30   ? 157  ASP A CG  1 
ATOM   1055 O  OD1 . ASP A 1 247 ? 181.832 154.180 144.710 1.00 4.42   ? 157  ASP A OD1 1 
ATOM   1056 O  OD2 . ASP A 1 247 ? 180.295 155.546 144.174 1.00 4.51   ? 157  ASP A OD2 1 
ATOM   1057 N  N   . TYR A 1 248 ? 182.958 157.931 143.147 1.00 4.09   ? 158  TYR A N   1 
ATOM   1058 C  CA  . TYR A 1 248 ? 182.628 158.819 142.037 1.00 4.09   ? 158  TYR A CA  1 
ATOM   1059 C  C   . TYR A 1 248 ? 181.139 158.777 141.698 1.00 4.28   ? 158  TYR A C   1 
ATOM   1060 O  O   . TYR A 1 248 ? 180.505 159.815 141.509 1.00 4.10   ? 158  TYR A O   1 
ATOM   1061 C  CB  . TYR A 1 248 ? 183.453 158.444 140.803 1.00 4.19   ? 158  TYR A CB  1 
ATOM   1062 C  CG  . TYR A 1 248 ? 183.281 159.381 139.632 1.00 4.18   ? 158  TYR A CG  1 
ATOM   1063 C  CD1 . TYR A 1 248 ? 182.269 159.170 138.709 1.00 4.47   ? 158  TYR A CD1 1 
ATOM   1064 C  CD2 . TYR A 1 248 ? 184.149 160.446 139.473 1.00 3.80   ? 158  TYR A CD2 1 
ATOM   1065 C  CE1 . TYR A 1 248 ? 182.125 160.025 137.638 1.00 4.37   ? 158  TYR A CE1 1 
ATOM   1066 C  CE2 . TYR A 1 248 ? 184.005 161.296 138.401 1.00 3.85   ? 158  TYR A CE2 1 
ATOM   1067 C  CZ  . TYR A 1 248 ? 183.000 161.090 137.487 1.00 3.99   ? 158  TYR A CZ  1 
ATOM   1068 O  OH  . TYR A 1 248 ? 182.866 161.940 136.415 1.00 4.13   ? 158  TYR A OH  1 
ATOM   1069 N  N   . HIS A 1 249 ? 180.588 157.570 141.596 1.00 4.57   ? 159  HIS A N   1 
ATOM   1070 C  CA  . HIS A 1 249 ? 179.191 157.402 141.214 1.00 5.12   ? 159  HIS A CA  1 
ATOM   1071 C  C   . HIS A 1 249 ? 178.242 157.964 142.261 1.00 4.79   ? 159  HIS A C   1 
ATOM   1072 O  O   . HIS A 1 249 ? 177.305 158.692 141.927 1.00 4.54   ? 159  HIS A O   1 
ATOM   1073 C  CB  . HIS A 1 249 ? 178.856 155.930 140.975 1.00 5.98   ? 159  HIS A CB  1 
ATOM   1074 C  CG  . HIS A 1 249 ? 177.426 155.701 140.563 1.00 6.93   ? 159  HIS A CG  1 
ATOM   1075 N  ND1 . HIS A 1 249 ? 176.758 154.525 140.821 1.00 7.53   ? 159  HIS A ND1 1 
ATOM   1076 C  CD2 . HIS A 1 249 ? 176.542 156.500 139.917 1.00 7.04   ? 159  HIS A CD2 1 
ATOM   1077 C  CE1 . HIS A 1 249 ? 175.526 154.611 140.349 1.00 8.00   ? 159  HIS A CE1 1 
ATOM   1078 N  NE2 . HIS A 1 249 ? 175.373 155.796 139.799 1.00 7.70   ? 159  HIS A NE2 1 
ATOM   1079 N  N   . GLN A 1 250 ? 178.464 157.611 143.524 1.00 4.44   ? 160  GLN A N   1 
ATOM   1080 C  CA  . GLN A 1 250 ? 177.569 158.056 144.582 1.00 4.23   ? 160  GLN A CA  1 
ATOM   1081 C  C   . GLN A 1 250 ? 177.521 159.568 144.649 1.00 4.06   ? 160  GLN A C   1 
ATOM   1082 O  O   . GLN A 1 250 ? 176.453 160.163 144.788 1.00 3.90   ? 160  GLN A O   1 
ATOM   1083 C  CB  . GLN A 1 250 ? 177.995 157.499 145.937 1.00 4.08   ? 160  GLN A CB  1 
ATOM   1084 C  CG  . GLN A 1 250 ? 177.047 157.856 147.067 1.00 3.97   ? 160  GLN A CG  1 
ATOM   1085 C  CD  . GLN A 1 250 ? 177.464 157.265 148.383 1.00 3.82   ? 160  GLN A CD  1 
ATOM   1086 O  OE1 . GLN A 1 250 ? 178.650 157.036 148.634 1.00 3.97   ? 160  GLN A OE1 1 
ATOM   1087 N  NE2 . GLN A 1 250 ? 176.489 157.007 149.243 1.00 4.02   ? 160  GLN A NE2 1 
ATOM   1088 N  N   . ARG A 1 251 ? 178.682 160.192 144.533 1.00 3.88   ? 161  ARG A N   1 
ATOM   1089 C  CA  . ARG A 1 251 ? 178.767 161.635 144.607 1.00 3.78   ? 161  ARG A CA  1 
ATOM   1090 C  C   . ARG A 1 251 ? 178.024 162.284 143.448 1.00 3.75   ? 161  ARG A C   1 
ATOM   1091 O  O   . ARG A 1 251 ? 177.446 163.361 143.597 1.00 3.56   ? 161  ARG A O   1 
ATOM   1092 C  CB  . ARG A 1 251 ? 180.216 162.080 144.601 1.00 3.61   ? 161  ARG A CB  1 
ATOM   1093 C  CG  . ARG A 1 251 ? 181.008 161.706 145.845 1.00 3.65   ? 161  ARG A CG  1 
ATOM   1094 C  CD  . ARG A 1 251 ? 182.371 162.255 145.780 1.00 3.59   ? 161  ARG A CD  1 
ATOM   1095 N  NE  . ARG A 1 251 ? 182.323 163.686 145.869 1.00 3.35   ? 161  ARG A NE  1 
ATOM   1096 C  CZ  . ARG A 1 251 ? 182.356 164.383 147.009 1.00 3.48   ? 161  ARG A CZ  1 
ATOM   1097 N  NH1 . ARG A 1 251 ? 182.507 163.775 148.158 1.00 3.69   ? 161  ARG A NH1 1 
ATOM   1098 N  NH2 . ARG A 1 251 ? 182.221 165.689 146.963 1.00 3.43   ? 161  ARG A NH2 1 
ATOM   1099 N  N   . LEU A 1 252 ? 178.050 161.636 142.285 1.00 3.76   ? 162  LEU A N   1 
ATOM   1100 C  CA  . LEU A 1 252 ? 177.429 162.208 141.104 1.00 3.79   ? 162  LEU A CA  1 
ATOM   1101 C  C   . LEU A 1 252 ? 175.905 162.196 141.158 1.00 3.86   ? 162  LEU A C   1 
ATOM   1102 O  O   . LEU A 1 252 ? 175.278 163.194 140.806 1.00 3.55   ? 162  LEU A O   1 
ATOM   1103 C  CB  . LEU A 1 252 ? 177.910 161.482 139.842 1.00 3.98   ? 162  LEU A CB  1 
ATOM   1104 C  CG  . LEU A 1 252 ? 177.364 162.021 138.498 1.00 4.30   ? 162  LEU A CG  1 
ATOM   1105 C  CD1 . LEU A 1 252 ? 177.713 163.493 138.344 1.00 3.77   ? 162  LEU A CD1 1 
ATOM   1106 C  CD2 . LEU A 1 252 ? 177.970 161.219 137.366 1.00 5.46   ? 162  LEU A CD2 1 
ATOM   1107 N  N   . TRP A 1 253 ? 175.287 161.088 141.589 1.00 3.88   ? 163  TRP A N   1 
ATOM   1108 C  CA  . TRP A 1 253 ? 173.824 161.095 141.602 1.00 3.90   ? 163  TRP A CA  1 
ATOM   1109 C  C   . TRP A 1 253 ? 173.279 161.989 142.705 1.00 3.75   ? 163  TRP A C   1 
ATOM   1110 O  O   . TRP A 1 253 ? 172.185 162.535 142.576 1.00 3.47   ? 163  TRP A O   1 
ATOM   1111 C  CB  . TRP A 1 253 ? 173.191 159.690 141.674 1.00 4.25   ? 163  TRP A CB  1 
ATOM   1112 C  CG  . TRP A 1 253 ? 173.371 158.885 142.944 1.00 4.18   ? 163  TRP A CG  1 
ATOM   1113 C  CD1 . TRP A 1 253 ? 174.255 157.879 143.133 1.00 4.57   ? 163  TRP A CD1 1 
ATOM   1114 C  CD2 . TRP A 1 253 ? 172.626 158.995 144.191 1.00 4.11   ? 163  TRP A CD2 1 
ATOM   1115 N  NE1 . TRP A 1 253 ? 174.115 157.352 144.393 1.00 4.23   ? 163  TRP A NE1 1 
ATOM   1116 C  CE2 . TRP A 1 253 ? 173.132 158.024 145.051 1.00 4.23   ? 163  TRP A CE2 1 
ATOM   1117 C  CE3 . TRP A 1 253 ? 171.585 159.821 144.635 1.00 4.18   ? 163  TRP A CE3 1 
ATOM   1118 C  CZ2 . TRP A 1 253 ? 172.644 157.853 146.331 1.00 4.31   ? 163  TRP A CZ2 1 
ATOM   1119 C  CZ3 . TRP A 1 253 ? 171.101 159.647 145.923 1.00 4.24   ? 163  TRP A CZ3 1 
ATOM   1120 C  CH2 . TRP A 1 253 ? 171.618 158.690 146.746 1.00 4.36   ? 163  TRP A CH2 1 
ATOM   1121 N  N   . ILE A 1 254 ? 174.064 162.207 143.753 1.00 3.72   ? 164  ILE A N   1 
ATOM   1122 C  CA  . ILE A 1 254 ? 173.677 163.163 144.779 1.00 3.60   ? 164  ILE A CA  1 
ATOM   1123 C  C   . ILE A 1 254 ? 173.771 164.594 144.265 1.00 3.40   ? 164  ILE A C   1 
ATOM   1124 O  O   . ILE A 1 254 ? 172.856 165.394 144.465 1.00 3.30   ? 164  ILE A O   1 
ATOM   1125 C  CB  . ILE A 1 254 ? 174.527 162.996 146.047 1.00 3.66   ? 164  ILE A CB  1 
ATOM   1126 C  CG1 . ILE A 1 254 ? 174.160 161.674 146.730 1.00 3.84   ? 164  ILE A CG1 1 
ATOM   1127 C  CG2 . ILE A 1 254 ? 174.333 164.187 146.974 1.00 3.73   ? 164  ILE A CG2 1 
ATOM   1128 C  CD1 . ILE A 1 254 ? 175.098 161.265 147.832 1.00 3.99   ? 164  ILE A CD1 1 
ATOM   1129 N  N   . TRP A 1 255 ? 174.872 164.912 143.591 1.00 3.25   ? 165  TRP A N   1 
ATOM   1130 C  CA  . TRP A 1 255 ? 175.081 166.248 143.051 1.00 3.25   ? 165  TRP A CA  1 
ATOM   1131 C  C   . TRP A 1 255 ? 173.992 166.606 142.043 1.00 3.17   ? 165  TRP A C   1 
ATOM   1132 O  O   . TRP A 1 255 ? 173.367 167.664 142.140 1.00 3.03   ? 165  TRP A O   1 
ATOM   1133 C  CB  . TRP A 1 255 ? 176.457 166.319 142.380 1.00 3.06   ? 165  TRP A CB  1 
ATOM   1134 C  CG  . TRP A 1 255 ? 176.857 167.686 141.923 1.00 2.95   ? 165  TRP A CG  1 
ATOM   1135 C  CD1 . TRP A 1 255 ? 177.547 168.604 142.645 1.00 2.91   ? 165  TRP A CD1 1 
ATOM   1136 C  CD2 . TRP A 1 255 ? 176.600 168.300 140.641 1.00 2.93   ? 165  TRP A CD2 1 
ATOM   1137 N  NE1 . TRP A 1 255 ? 177.734 169.737 141.909 1.00 2.87   ? 165  TRP A NE1 1 
ATOM   1138 C  CE2 . TRP A 1 255 ? 177.158 169.571 140.683 1.00 2.94   ? 165  TRP A CE2 1 
ATOM   1139 C  CE3 . TRP A 1 255 ? 175.949 167.877 139.479 1.00 3.07   ? 165  TRP A CE3 1 
ATOM   1140 C  CZ2 . TRP A 1 255 ? 177.083 170.436 139.613 1.00 2.85   ? 165  TRP A CZ2 1 
ATOM   1141 C  CZ3 . TRP A 1 255 ? 175.874 168.743 138.407 1.00 3.09   ? 165  TRP A CZ3 1 
ATOM   1142 C  CH2 . TRP A 1 255 ? 176.425 169.993 138.473 1.00 2.97   ? 165  TRP A CH2 1 
ATOM   1143 N  N   . GLU A 1 256 ? 173.758 165.708 141.088 1.00 3.25   ? 166  GLU A N   1 
ATOM   1144 C  CA  . GLU A 1 256 ? 172.759 165.920 140.047 1.00 3.28   ? 166  GLU A CA  1 
ATOM   1145 C  C   . GLU A 1 256 ? 171.349 165.881 140.613 1.00 3.22   ? 166  GLU A C   1 
ATOM   1146 O  O   . GLU A 1 256 ? 170.493 166.668 140.212 1.00 3.07   ? 166  GLU A O   1 
ATOM   1147 C  CB  . GLU A 1 256 ? 172.913 164.867 138.943 1.00 3.37   ? 166  GLU A CB  1 
ATOM   1148 C  CG  . GLU A 1 256 ? 171.848 164.913 137.833 1.00 3.58   ? 166  GLU A CG  1 
ATOM   1149 C  CD  . GLU A 1 256 ? 171.880 166.165 136.991 1.00 3.69   ? 166  GLU A CD  1 
ATOM   1150 O  OE1 . GLU A 1 256 ? 172.872 166.853 137.011 1.00 3.65   ? 166  GLU A OE1 1 
ATOM   1151 O  OE2 . GLU A 1 256 ? 170.912 166.417 136.308 1.00 3.76   ? 166  GLU A OE2 1 
ATOM   1152 N  N   . GLY A 1 257 ? 171.111 164.972 141.551 1.00 3.18   ? 167  GLY A N   1 
ATOM   1153 C  CA  . GLY A 1 257 ? 169.794 164.815 142.143 1.00 3.21   ? 167  GLY A CA  1 
ATOM   1154 C  C   . GLY A 1 257 ? 169.331 166.099 142.806 1.00 3.21   ? 167  GLY A C   1 
ATOM   1155 O  O   . GLY A 1 257 ? 168.210 166.547 142.587 1.00 3.04   ? 167  GLY A O   1 
ATOM   1156 N  N   . TRP A 1 258 ? 170.190 166.702 143.617 1.00 3.04   ? 168  TRP A N   1 
ATOM   1157 C  CA  . TRP A 1 258 ? 169.822 167.931 144.305 1.00 3.05   ? 168  TRP A CA  1 
ATOM   1158 C  C   . TRP A 1 258 ? 169.457 169.032 143.306 1.00 3.05   ? 168  TRP A C   1 
ATOM   1159 O  O   . TRP A 1 258 ? 168.447 169.721 143.469 1.00 2.90   ? 168  TRP A O   1 
ATOM   1160 C  CB  . TRP A 1 258 ? 170.960 168.384 145.225 1.00 3.03   ? 168  TRP A CB  1 
ATOM   1161 C  CG  . TRP A 1 258 ? 170.625 169.576 146.076 1.00 2.96   ? 168  TRP A CG  1 
ATOM   1162 C  CD1 . TRP A 1 258 ? 171.145 170.822 145.963 1.00 2.97   ? 168  TRP A CD1 1 
ATOM   1163 C  CD2 . TRP A 1 258 ? 169.691 169.634 147.181 1.00 3.06   ? 168  TRP A CD2 1 
ATOM   1164 N  NE1 . TRP A 1 258 ? 170.599 171.652 146.911 1.00 2.93   ? 168  TRP A NE1 1 
ATOM   1165 C  CE2 . TRP A 1 258 ? 169.706 170.944 147.658 1.00 2.98   ? 168  TRP A CE2 1 
ATOM   1166 C  CE3 . TRP A 1 258 ? 168.856 168.696 147.791 1.00 3.16   ? 168  TRP A CE3 1 
ATOM   1167 C  CZ2 . TRP A 1 258 ? 168.913 171.347 148.714 1.00 3.06   ? 168  TRP A CZ2 1 
ATOM   1168 C  CZ3 . TRP A 1 258 ? 168.065 169.098 148.854 1.00 3.33   ? 168  TRP A CZ3 1 
ATOM   1169 C  CH2 . TRP A 1 258 ? 168.091 170.392 149.301 1.00 3.24   ? 168  TRP A CH2 1 
ATOM   1170 N  N   . ARG A 1 259 ? 170.265 169.177 142.256 1.00 2.88   ? 169  ARG A N   1 
ATOM   1171 C  CA  . ARG A 1 259 ? 170.028 170.209 141.252 1.00 2.97   ? 169  ARG A CA  1 
ATOM   1172 C  C   . ARG A 1 259 ? 168.725 169.997 140.487 1.00 3.01   ? 169  ARG A C   1 
ATOM   1173 O  O   . ARG A 1 259 ? 168.059 170.966 140.121 1.00 2.85   ? 169  ARG A O   1 
ATOM   1174 C  CB  . ARG A 1 259 ? 171.178 170.276 140.257 1.00 2.91   ? 169  ARG A CB  1 
ATOM   1175 C  CG  . ARG A 1 259 ? 172.295 171.237 140.626 1.00 2.89   ? 169  ARG A CG  1 
ATOM   1176 C  CD  . ARG A 1 259 ? 173.227 170.651 141.597 1.00 2.79   ? 169  ARG A CD  1 
ATOM   1177 N  NE  . ARG A 1 259 ? 174.198 171.613 142.057 1.00 2.85   ? 169  ARG A NE  1 
ATOM   1178 C  CZ  . ARG A 1 259 ? 175.021 171.420 143.099 1.00 2.87   ? 169  ARG A CZ  1 
ATOM   1179 N  NH1 . ARG A 1 259 ? 174.983 170.296 143.771 1.00 2.84   ? 169  ARG A NH1 1 
ATOM   1180 N  NH2 . ARG A 1 259 ? 175.872 172.356 143.455 1.00 2.87   ? 169  ARG A NH2 1 
ATOM   1181 N  N   . SER A 1 260 ? 168.367 168.742 140.235 1.00 2.93   ? 170  SER A N   1 
ATOM   1182 C  CA  . SER A 1 260 ? 167.150 168.438 139.490 1.00 2.97   ? 170  SER A CA  1 
ATOM   1183 C  C   . SER A 1 260 ? 165.896 168.466 140.357 1.00 2.99   ? 170  SER A C   1 
ATOM   1184 O  O   . SER A 1 260 ? 164.844 168.931 139.920 1.00 2.89   ? 170  SER A O   1 
ATOM   1185 C  CB  . SER A 1 260 ? 167.263 167.075 138.841 1.00 3.06   ? 170  SER A CB  1 
ATOM   1186 N  N   . GLU A 1 261 ? 165.996 167.943 141.574 1.00 2.97   ? 171  GLU A N   1 
ATOM   1187 C  CA  . GLU A 1 261 ? 164.832 167.812 142.440 1.00 3.01   ? 171  GLU A CA  1 
ATOM   1188 C  C   . GLU A 1 261 ? 164.423 169.126 143.083 1.00 3.02   ? 171  GLU A C   1 
ATOM   1189 O  O   . GLU A 1 261 ? 163.234 169.392 143.248 1.00 2.97   ? 171  GLU A O   1 
ATOM   1190 C  CB  . GLU A 1 261 ? 165.096 166.769 143.527 1.00 3.13   ? 171  GLU A CB  1 
ATOM   1191 N  N   . VAL A 1 262 ? 165.400 169.942 143.457 1.00 2.94   ? 172  VAL A N   1 
ATOM   1192 C  CA  . VAL A 1 262 ? 165.120 171.201 144.132 1.00 2.89   ? 172  VAL A CA  1 
ATOM   1193 C  C   . VAL A 1 262 ? 165.311 172.391 143.204 1.00 2.92   ? 172  VAL A C   1 
ATOM   1194 O  O   . VAL A 1 262 ? 164.481 173.299 143.160 1.00 2.75   ? 172  VAL A O   1 
ATOM   1195 C  CB  . VAL A 1 262 ? 166.019 171.338 145.375 1.00 2.93   ? 172  VAL A CB  1 
ATOM   1196 C  CG1 . VAL A 1 262 ? 165.830 172.695 146.034 1.00 2.94   ? 172  VAL A CG1 1 
ATOM   1197 C  CG2 . VAL A 1 262 ? 165.675 170.231 146.345 1.00 3.07   ? 172  VAL A CG2 1 
ATOM   1198 N  N   . GLY A 1 263 ? 166.409 172.387 142.464 1.00 2.83   ? 173  GLY A N   1 
ATOM   1199 C  CA  . GLY A 1 263 ? 166.744 173.511 141.596 1.00 2.72   ? 173  GLY A CA  1 
ATOM   1200 C  C   . GLY A 1 263 ? 165.645 173.819 140.580 1.00 2.77   ? 173  GLY A C   1 
ATOM   1201 O  O   . GLY A 1 263 ? 165.409 174.984 140.254 1.00 2.67   ? 173  GLY A O   1 
ATOM   1202 N  N   . LYS A 1 264 ? 164.959 172.786 140.096 1.00 2.76   ? 174  LYS A N   1 
ATOM   1203 C  CA  . LYS A 1 264 ? 163.923 172.972 139.085 1.00 2.78   ? 174  LYS A CA  1 
ATOM   1204 C  C   . LYS A 1 264 ? 162.605 173.465 139.670 1.00 2.76   ? 174  LYS A C   1 
ATOM   1205 O  O   . LYS A 1 264 ? 161.710 173.871 138.932 1.00 2.75   ? 174  LYS A O   1 
ATOM   1206 C  CB  . LYS A 1 264 ? 163.684 171.682 138.303 1.00 2.77   ? 174  LYS A CB  1 
ATOM   1207 C  CG  . LYS A 1 264 ? 164.825 171.272 137.380 1.00 2.81   ? 174  LYS A CG  1 
ATOM   1208 C  CD  . LYS A 1 264 ? 164.448 170.041 136.573 1.00 2.90   ? 174  LYS A CD  1 
ATOM   1209 C  CE  . LYS A 1 264 ? 165.540 169.644 135.599 1.00 2.87   ? 174  LYS A CE  1 
ATOM   1210 N  NZ  . LYS A 1 264 ? 165.124 168.493 134.750 1.00 3.04   ? 174  LYS A NZ  1 
ATOM   1211 N  N   . GLN A 1 265 ? 162.479 173.438 140.993 1.00 2.73   ? 175  GLN A N   1 
ATOM   1212 C  CA  . GLN A 1 265 ? 161.277 173.953 141.632 1.00 2.78   ? 175  GLN A CA  1 
ATOM   1213 C  C   . GLN A 1 265 ? 161.442 175.432 141.917 1.00 2.77   ? 175  GLN A C   1 
ATOM   1214 O  O   . GLN A 1 265 ? 160.474 176.190 141.925 1.00 2.75   ? 175  GLN A O   1 
ATOM   1215 C  CB  . GLN A 1 265 ? 160.979 173.223 142.941 1.00 2.82   ? 175  GLN A CB  1 
ATOM   1216 C  CG  . GLN A 1 265 ? 160.592 171.780 142.791 1.00 2.85   ? 175  GLN A CG  1 
ATOM   1217 C  CD  . GLN A 1 265 ? 160.160 171.183 144.111 1.00 2.79   ? 175  GLN A CD  1 
ATOM   1218 O  OE1 . GLN A 1 265 ? 159.139 171.583 144.676 1.00 2.96   ? 175  GLN A OE1 1 
ATOM   1219 N  NE2 . GLN A 1 265 ? 160.930 170.234 144.615 1.00 2.96   ? 175  GLN A NE2 1 
ATOM   1220 N  N   . LEU A 1 266 ? 162.684 175.836 142.149 1.00 2.74   ? 176  LEU A N   1 
ATOM   1221 C  CA  . LEU A 1 266 ? 162.991 177.209 142.501 1.00 2.74   ? 176  LEU A CA  1 
ATOM   1222 C  C   . LEU A 1 266 ? 163.120 178.103 141.274 1.00 2.81   ? 176  LEU A C   1 
ATOM   1223 O  O   . LEU A 1 266 ? 162.890 179.307 141.356 1.00 2.55   ? 176  LEU A O   1 
ATOM   1224 C  CB  . LEU A 1 266 ? 164.287 177.250 143.315 1.00 2.69   ? 176  LEU A CB  1 
ATOM   1225 C  CG  . LEU A 1 266 ? 164.253 176.511 144.669 1.00 2.74   ? 176  LEU A CG  1 
ATOM   1226 C  CD1 . LEU A 1 266 ? 165.652 176.453 145.242 1.00 2.69   ? 176  LEU A CD1 1 
ATOM   1227 C  CD2 . LEU A 1 266 ? 163.319 177.232 145.629 1.00 2.83   ? 176  LEU A CD2 1 
ATOM   1228 N  N   . ARG A 1 267 ? 163.474 177.522 140.132 1.00 2.64   ? 177  ARG A N   1 
ATOM   1229 C  CA  . ARG A 1 267 ? 163.653 178.311 138.918 1.00 2.63   ? 177  ARG A CA  1 
ATOM   1230 C  C   . ARG A 1 267 ? 162.568 179.388 138.694 1.00 2.63   ? 177  ARG A C   1 
ATOM   1231 O  O   . ARG A 1 267 ? 162.914 180.568 138.638 1.00 2.54   ? 177  ARG A O   1 
ATOM   1232 C  CB  . ARG A 1 267 ? 163.779 177.409 137.691 1.00 2.57   ? 177  ARG A CB  1 
ATOM   1233 C  CG  . ARG A 1 267 ? 163.826 178.145 136.349 1.00 2.55   ? 177  ARG A CG  1 
ATOM   1234 C  CD  . ARG A 1 267 ? 165.141 178.786 136.101 1.00 2.55   ? 177  ARG A CD  1 
ATOM   1235 N  NE  . ARG A 1 267 ? 165.074 179.753 135.019 1.00 2.48   ? 177  ARG A NE  1 
ATOM   1236 C  CZ  . ARG A 1 267 ? 166.050 180.002 134.124 1.00 2.48   ? 177  ARG A CZ  1 
ATOM   1237 N  NH1 . ARG A 1 267 ? 167.184 179.328 134.143 1.00 2.48   ? 177  ARG A NH1 1 
ATOM   1238 N  NH2 . ARG A 1 267 ? 165.849 180.934 133.214 1.00 2.42   ? 177  ARG A NH2 1 
ATOM   1239 N  N   . PRO A 1 268 ? 161.269 179.040 138.560 1.00 2.56   ? 178  PRO A N   1 
ATOM   1240 C  CA  . PRO A 1 268 ? 160.182 179.968 138.283 1.00 2.59   ? 178  PRO A CA  1 
ATOM   1241 C  C   . PRO A 1 268 ? 159.926 180.953 139.418 1.00 2.65   ? 178  PRO A C   1 
ATOM   1242 O  O   . PRO A 1 268 ? 159.430 182.058 139.187 1.00 2.69   ? 178  PRO A O   1 
ATOM   1243 C  CB  . PRO A 1 268 ? 158.985 179.031 138.082 1.00 2.61   ? 178  PRO A CB  1 
ATOM   1244 C  CG  . PRO A 1 268 ? 159.353 177.764 138.818 1.00 2.66   ? 178  PRO A CG  1 
ATOM   1245 C  CD  . PRO A 1 268 ? 160.840 177.633 138.648 1.00 2.62   ? 178  PRO A CD  1 
ATOM   1246 N  N   . LEU A 1 269 ? 160.289 180.572 140.639 1.00 2.60   ? 179  LEU A N   1 
ATOM   1247 C  CA  . LEU A 1 269 ? 160.103 181.452 141.782 1.00 2.74   ? 179  LEU A CA  1 
ATOM   1248 C  C   . LEU A 1 269 ? 161.194 182.497 141.816 1.00 2.89   ? 179  LEU A C   1 
ATOM   1249 O  O   . LEU A 1 269 ? 160.965 183.636 142.224 1.00 2.72   ? 179  LEU A O   1 
ATOM   1250 C  CB  . LEU A 1 269 ? 160.124 180.649 143.087 1.00 2.78   ? 179  LEU A CB  1 
ATOM   1251 C  CG  . LEU A 1 269 ? 158.950 179.690 143.316 1.00 2.77   ? 179  LEU A CG  1 
ATOM   1252 C  CD1 . LEU A 1 269 ? 159.266 178.802 144.503 1.00 2.84   ? 179  LEU A CD1 1 
ATOM   1253 C  CD2 . LEU A 1 269 ? 157.676 180.489 143.576 1.00 2.79   ? 179  LEU A CD2 1 
ATOM   1254 N  N   . TYR A 1 270 ? 162.386 182.108 141.378 1.00 2.60   ? 180  TYR A N   1 
ATOM   1255 C  CA  . TYR A 1 270 ? 163.512 183.019 141.376 1.00 2.66   ? 180  TYR A CA  1 
ATOM   1256 C  C   . TYR A 1 270 ? 163.301 184.090 140.316 1.00 2.98   ? 180  TYR A C   1 
ATOM   1257 O  O   . TYR A 1 270 ? 163.658 185.249 140.519 1.00 2.62   ? 180  TYR A O   1 
ATOM   1258 C  CB  . TYR A 1 270 ? 164.822 182.263 141.152 1.00 2.58   ? 180  TYR A CB  1 
ATOM   1259 C  CG  . TYR A 1 270 ? 166.026 183.035 141.631 1.00 2.55   ? 180  TYR A CG  1 
ATOM   1260 C  CD1 . TYR A 1 270 ? 166.887 183.621 140.729 1.00 2.52   ? 180  TYR A CD1 1 
ATOM   1261 C  CD2 . TYR A 1 270 ? 166.257 183.162 142.989 1.00 2.64   ? 180  TYR A CD2 1 
ATOM   1262 C  CE1 . TYR A 1 270 ? 167.973 184.333 141.177 1.00 2.50   ? 180  TYR A CE1 1 
ATOM   1263 C  CE2 . TYR A 1 270 ? 167.341 183.874 143.439 1.00 2.61   ? 180  TYR A CE2 1 
ATOM   1264 C  CZ  . TYR A 1 270 ? 168.197 184.459 142.537 1.00 2.49   ? 180  TYR A CZ  1 
ATOM   1265 O  OH  . TYR A 1 270 ? 169.280 185.172 142.980 1.00 2.68   ? 180  TYR A OH  1 
ATOM   1266 N  N   . GLU A 1 271 ? 162.700 183.711 139.192 1.00 2.60   ? 181  GLU A N   1 
ATOM   1267 C  CA  . GLU A 1 271 ? 162.432 184.671 138.127 1.00 2.68   ? 181  GLU A CA  1 
ATOM   1268 C  C   . GLU A 1 271 ? 161.470 185.769 138.577 1.00 2.73   ? 181  GLU A C   1 
ATOM   1269 O  O   . GLU A 1 271 ? 161.697 186.948 138.299 1.00 2.72   ? 181  GLU A O   1 
ATOM   1270 C  CB  . GLU A 1 271 ? 161.865 183.961 136.897 1.00 2.57   ? 181  GLU A CB  1 
ATOM   1271 C  CG  . GLU A 1 271 ? 162.871 183.106 136.131 1.00 2.53   ? 181  GLU A CG  1 
ATOM   1272 C  CD  . GLU A 1 271 ? 162.252 182.407 134.953 1.00 2.47   ? 181  GLU A CD  1 
ATOM   1273 O  OE1 . GLU A 1 271 ? 161.057 182.496 134.806 1.00 2.57   ? 181  GLU A OE1 1 
ATOM   1274 O  OE2 . GLU A 1 271 ? 162.967 181.790 134.195 1.00 2.53   ? 181  GLU A OE2 1 
ATOM   1275 N  N   . GLU A 1 272 ? 160.412 185.388 139.294 1.00 2.75   ? 182  GLU A N   1 
ATOM   1276 C  CA  . GLU A 1 272 ? 159.457 186.367 139.800 1.00 2.87   ? 182  GLU A CA  1 
ATOM   1277 C  C   . GLU A 1 272 ? 160.068 187.186 140.931 1.00 3.01   ? 182  GLU A C   1 
ATOM   1278 O  O   . GLU A 1 272 ? 159.835 188.390 141.039 1.00 3.01   ? 182  GLU A O   1 
ATOM   1279 C  CB  . GLU A 1 272 ? 158.175 185.686 140.270 1.00 2.96   ? 182  GLU A CB  1 
ATOM   1280 C  CG  . GLU A 1 272 ? 157.046 186.655 140.578 1.00 3.18   ? 182  GLU A CG  1 
ATOM   1281 C  CD  . GLU A 1 272 ? 155.753 185.971 140.879 1.00 3.38   ? 182  GLU A CD  1 
ATOM   1282 O  OE1 . GLU A 1 272 ? 155.718 184.767 140.845 1.00 3.34   ? 182  GLU A OE1 1 
ATOM   1283 O  OE2 . GLU A 1 272 ? 154.793 186.650 141.152 1.00 3.49   ? 182  GLU A OE2 1 
ATOM   1284 N  N   . TYR A 1 273 ? 160.865 186.523 141.757 1.00 2.85   ? 183  TYR A N   1 
ATOM   1285 C  CA  . TYR A 1 273 ? 161.592 187.159 142.847 1.00 3.01   ? 183  TYR A CA  1 
ATOM   1286 C  C   . TYR A 1 273 ? 162.451 188.313 142.347 1.00 3.06   ? 183  TYR A C   1 
ATOM   1287 O  O   . TYR A 1 273 ? 162.379 189.418 142.881 1.00 3.04   ? 183  TYR A O   1 
ATOM   1288 C  CB  . TYR A 1 273 ? 162.438 186.102 143.555 1.00 2.85   ? 183  TYR A CB  1 
ATOM   1289 C  CG  . TYR A 1 273 ? 163.592 186.605 144.366 1.00 2.85   ? 183  TYR A CG  1 
ATOM   1290 C  CD1 . TYR A 1 273 ? 163.418 187.080 145.650 1.00 3.00   ? 183  TYR A CD1 1 
ATOM   1291 C  CD2 . TYR A 1 273 ? 164.857 186.558 143.811 1.00 2.80   ? 183  TYR A CD2 1 
ATOM   1292 C  CE1 . TYR A 1 273 ? 164.518 187.506 146.369 1.00 3.06   ? 183  TYR A CE1 1 
ATOM   1293 C  CE2 . TYR A 1 273 ? 165.942 186.982 144.524 1.00 2.84   ? 183  TYR A CE2 1 
ATOM   1294 C  CZ  . TYR A 1 273 ? 165.780 187.452 145.795 1.00 3.02   ? 183  TYR A CZ  1 
ATOM   1295 O  OH  . TYR A 1 273 ? 166.870 187.868 146.506 1.00 3.03   ? 183  TYR A OH  1 
ATOM   1296 N  N   . VAL A 1 274 ? 163.238 188.070 141.304 1.00 2.84   ? 184  VAL A N   1 
ATOM   1297 C  CA  . VAL A 1 274 ? 164.116 189.101 140.765 1.00 3.00   ? 184  VAL A CA  1 
ATOM   1298 C  C   . VAL A 1 274 ? 163.328 190.318 140.300 1.00 3.15   ? 184  VAL A C   1 
ATOM   1299 O  O   . VAL A 1 274 ? 163.717 191.455 140.573 1.00 3.13   ? 184  VAL A O   1 
ATOM   1300 C  CB  . VAL A 1 274 ? 164.952 188.540 139.592 1.00 2.84   ? 184  VAL A CB  1 
ATOM   1301 C  CG1 . VAL A 1 274 ? 165.683 189.665 138.865 1.00 2.89   ? 184  VAL A CG1 1 
ATOM   1302 C  CG2 . VAL A 1 274 ? 165.963 187.531 140.123 1.00 2.80   ? 184  VAL A CG2 1 
ATOM   1303 N  N   . ALA A 1 275 ? 162.225 190.090 139.595 1.00 3.00   ? 185  ALA A N   1 
ATOM   1304 C  CA  . ALA A 1 275 ? 161.420 191.197 139.094 1.00 3.15   ? 185  ALA A CA  1 
ATOM   1305 C  C   . ALA A 1 275 ? 160.867 192.060 140.228 1.00 3.31   ? 185  ALA A C   1 
ATOM   1306 O  O   . ALA A 1 275 ? 160.880 193.289 140.140 1.00 3.41   ? 185  ALA A O   1 
ATOM   1307 C  CB  . ALA A 1 275 ? 160.278 190.661 138.250 1.00 3.01   ? 185  ALA A CB  1 
ATOM   1308 N  N   . LEU A 1 276 ? 160.388 191.418 141.292 1.00 3.20   ? 186  LEU A N   1 
ATOM   1309 C  CA  . LEU A 1 276 ? 159.809 192.140 142.422 1.00 3.34   ? 186  LEU A CA  1 
ATOM   1310 C  C   . LEU A 1 276 ? 160.845 192.899 143.241 1.00 3.54   ? 186  LEU A C   1 
ATOM   1311 O  O   . LEU A 1 276 ? 160.590 194.020 143.682 1.00 3.65   ? 186  LEU A O   1 
ATOM   1312 C  CB  . LEU A 1 276 ? 159.048 191.169 143.332 1.00 3.35   ? 186  LEU A CB  1 
ATOM   1313 C  CG  . LEU A 1 276 ? 157.712 190.634 142.789 1.00 3.33   ? 186  LEU A CG  1 
ATOM   1314 C  CD1 . LEU A 1 276 ? 157.280 189.440 143.615 1.00 3.54   ? 186  LEU A CD1 1 
ATOM   1315 C  CD2 . LEU A 1 276 ? 156.654 191.730 142.865 1.00 3.73   ? 186  LEU A CD2 1 
ATOM   1316 N  N   . LYS A 1 277 ? 162.017 192.303 143.440 1.00 3.31   ? 187  LYS A N   1 
ATOM   1317 C  CA  . LYS A 1 277 ? 163.050 192.956 144.233 1.00 3.46   ? 187  LYS A CA  1 
ATOM   1318 C  C   . LYS A 1 277 ? 163.597 194.175 143.503 1.00 3.79   ? 187  LYS A C   1 
ATOM   1319 O  O   . LYS A 1 277 ? 163.913 195.186 144.130 1.00 3.68   ? 187  LYS A O   1 
ATOM   1320 C  CB  . LYS A 1 277 ? 164.184 191.989 144.573 1.00 3.24   ? 187  LYS A CB  1 
ATOM   1321 C  CG  . LYS A 1 277 ? 163.784 190.778 145.424 1.00 3.21   ? 187  LYS A CG  1 
ATOM   1322 C  CD  . LYS A 1 277 ? 163.313 191.140 146.831 1.00 3.33   ? 187  LYS A CD  1 
ATOM   1323 C  CE  . LYS A 1 277 ? 164.453 191.420 147.755 1.00 3.25   ? 187  LYS A CE  1 
ATOM   1324 N  NZ  . LYS A 1 277 ? 164.024 191.425 149.180 1.00 3.35   ? 187  LYS A NZ  1 
ATOM   1325 N  N   . ASN A 1 278 ? 163.686 194.097 142.177 1.00 3.45   ? 188  ASN A N   1 
ATOM   1326 C  CA  . ASN A 1 278 ? 164.149 195.243 141.405 1.00 3.56   ? 188  ASN A CA  1 
ATOM   1327 C  C   . ASN A 1 278 ? 163.167 196.402 141.470 1.00 4.09   ? 188  ASN A C   1 
ATOM   1328 O  O   . ASN A 1 278 ? 163.581 197.556 141.574 1.00 3.89   ? 188  ASN A O   1 
ATOM   1329 C  CB  . ASN A 1 278 ? 164.419 194.870 139.962 1.00 3.48   ? 188  ASN A CB  1 
ATOM   1330 C  CG  . ASN A 1 278 ? 165.759 194.233 139.745 1.00 3.41   ? 188  ASN A CG  1 
ATOM   1331 O  OD1 . ASN A 1 278 ? 166.673 194.332 140.576 1.00 3.28   ? 188  ASN A OD1 1 
ATOM   1332 N  ND2 . ASN A 1 278 ? 165.909 193.600 138.615 1.00 3.20   ? 188  ASN A ND2 1 
ATOM   1333 N  N   . GLU A 1 279 ? 161.869 196.109 141.433 1.00 3.80   ? 189  GLU A N   1 
ATOM   1334 C  CA  . GLU A 1 279 ? 160.881 197.174 141.539 1.00 4.08   ? 189  GLU A CA  1 
ATOM   1335 C  C   . GLU A 1 279 ? 160.971 197.861 142.892 1.00 4.13   ? 189  GLU A C   1 
ATOM   1336 O  O   . GLU A 1 279 ? 160.891 199.086 142.983 1.00 4.30   ? 189  GLU A O   1 
ATOM   1337 C  CB  . GLU A 1 279 ? 159.466 196.651 141.307 1.00 4.05   ? 189  GLU A CB  1 
ATOM   1338 C  CG  . GLU A 1 279 ? 158.410 197.743 141.360 1.00 4.30   ? 189  GLU A CG  1 
ATOM   1339 C  CD  . GLU A 1 279 ? 157.065 197.309 140.870 1.00 4.61   ? 189  GLU A CD  1 
ATOM   1340 O  OE1 . GLU A 1 279 ? 156.953 196.224 140.356 1.00 4.86   ? 189  GLU A OE1 1 
ATOM   1341 O  OE2 . GLU A 1 279 ? 156.137 198.070 141.009 1.00 4.92   ? 189  GLU A OE2 1 
ATOM   1342 N  N   . MET A 1 280 ? 161.166 197.070 143.941 1.00 4.14   ? 190  MET A N   1 
ATOM   1343 C  CA  . MET A 1 280 ? 161.338 197.618 145.277 1.00 4.34   ? 190  MET A CA  1 
ATOM   1344 C  C   . MET A 1 280 ? 162.539 198.556 145.305 1.00 4.48   ? 190  MET A C   1 
ATOM   1345 O  O   . MET A 1 280 ? 162.436 199.700 145.752 1.00 4.64   ? 190  MET A O   1 
ATOM   1346 C  CB  . MET A 1 280 ? 161.511 196.479 146.283 1.00 4.39   ? 190  MET A CB  1 
ATOM   1347 C  CG  . MET A 1 280 ? 161.696 196.908 147.740 1.00 4.94   ? 190  MET A CG  1 
ATOM   1348 S  SD  . MET A 1 280 ? 163.404 197.375 148.155 1.00 4.92   ? 190  MET A SD  1 
ATOM   1349 C  CE  . MET A 1 280 ? 164.287 195.823 148.048 1.00 4.01   ? 190  MET A CE  1 
ATOM   1350 N  N   . ALA A 1 281 ? 163.671 198.085 144.793 1.00 4.20   ? 191  ALA A N   1 
ATOM   1351 C  CA  . ALA A 1 281 ? 164.896 198.871 144.809 1.00 4.28   ? 191  ALA A CA  1 
ATOM   1352 C  C   . ALA A 1 281 ? 164.715 200.196 144.084 1.00 4.50   ? 191  ALA A C   1 
ATOM   1353 O  O   . ALA A 1 281 ? 165.173 201.233 144.566 1.00 4.43   ? 191  ALA A O   1 
ATOM   1354 C  CB  . ALA A 1 281 ? 166.026 198.082 144.177 1.00 3.97   ? 191  ALA A CB  1 
ATOM   1355 N  N   . ARG A 1 282 ? 164.006 200.177 142.960 1.00 4.29   ? 192  ARG A N   1 
ATOM   1356 C  CA  . ARG A 1 282 ? 163.751 201.403 142.211 1.00 4.43   ? 192  ARG A CA  1 
ATOM   1357 C  C   . ARG A 1 282 ? 162.887 202.369 143.015 1.00 4.51   ? 192  ARG A C   1 
ATOM   1358 O  O   . ARG A 1 282 ? 163.076 203.585 142.955 1.00 4.63   ? 192  ARG A O   1 
ATOM   1359 C  CB  . ARG A 1 282 ? 163.090 201.108 140.875 1.00 4.28   ? 192  ARG A CB  1 
ATOM   1360 C  CG  . ARG A 1 282 ? 163.998 200.445 139.844 1.00 4.16   ? 192  ARG A CG  1 
ATOM   1361 C  CD  . ARG A 1 282 ? 163.424 200.515 138.473 1.00 4.06   ? 192  ARG A CD  1 
ATOM   1362 N  NE  . ARG A 1 282 ? 162.140 199.830 138.370 1.00 4.24   ? 192  ARG A NE  1 
ATOM   1363 C  CZ  . ARG A 1 282 ? 161.973 198.528 138.055 1.00 4.02   ? 192  ARG A CZ  1 
ATOM   1364 N  NH1 . ARG A 1 282 ? 163.012 197.762 137.811 1.00 3.98   ? 192  ARG A NH1 1 
ATOM   1365 N  NH2 . ARG A 1 282 ? 160.756 198.021 137.989 1.00 4.06   ? 192  ARG A NH2 1 
ATOM   1366 N  N   . GLY A 1 283 ? 161.952 201.827 143.793 1.00 4.55   ? 193  GLY A N   1 
ATOM   1367 C  CA  . GLY A 1 283 ? 161.082 202.641 144.635 1.00 4.80   ? 193  GLY A CA  1 
ATOM   1368 C  C   . GLY A 1 283 ? 161.878 203.341 145.733 1.00 4.91   ? 193  GLY A C   1 
ATOM   1369 O  O   . GLY A 1 283 ? 161.448 204.359 146.275 1.00 5.08   ? 193  GLY A O   1 
ATOM   1370 N  N   . ASN A 1 284 ? 163.056 202.802 146.033 1.00 4.79   ? 194  ASN A N   1 
ATOM   1371 C  CA  . ASN A 1 284 ? 163.961 203.370 147.025 1.00 4.86   ? 194  ASN A CA  1 
ATOM   1372 C  C   . ASN A 1 284 ? 165.099 204.148 146.365 1.00 4.81   ? 194  ASN A C   1 
ATOM   1373 O  O   . ASN A 1 284 ? 166.120 204.421 146.995 1.00 4.69   ? 194  ASN A O   1 
ATOM   1374 C  CB  . ASN A 1 284 ? 164.514 202.283 147.927 1.00 4.81   ? 194  ASN A CB  1 
ATOM   1375 C  CG  . ASN A 1 284 ? 163.517 201.776 148.935 1.00 5.63   ? 194  ASN A CG  1 
ATOM   1376 O  OD1 . ASN A 1 284 ? 163.445 202.283 150.065 1.00 6.23   ? 194  ASN A OD1 1 
ATOM   1377 N  ND2 . ASN A 1 284 ? 162.746 200.796 148.552 1.00 5.37   ? 194  ASN A ND2 1 
ATOM   1378 N  N   . ASN A 1 285 ? 164.900 204.524 145.103 1.00 4.63   ? 195  ASN A N   1 
ATOM   1379 C  CA  . ASN A 1 285 ? 165.859 205.309 144.329 1.00 4.60   ? 195  ASN A CA  1 
ATOM   1380 C  C   . ASN A 1 285 ? 167.200 204.618 144.089 1.00 4.48   ? 195  ASN A C   1 
ATOM   1381 O  O   . ASN A 1 285 ? 168.244 205.269 144.064 1.00 4.49   ? 195  ASN A O   1 
ATOM   1382 C  CB  . ASN A 1 285 ? 166.073 206.664 144.974 1.00 4.65   ? 195  ASN A CB  1 
ATOM   1383 C  CG  . ASN A 1 285 ? 164.818 207.478 144.998 1.00 4.83   ? 195  ASN A CG  1 
ATOM   1384 O  OD1 . ASN A 1 285 ? 164.073 207.511 144.012 1.00 5.10   ? 195  ASN A OD1 1 
ATOM   1385 N  ND2 . ASN A 1 285 ? 164.563 208.134 146.101 1.00 5.19   ? 195  ASN A ND2 1 
ATOM   1386 N  N   . TYR A 1 286 ? 167.160 203.314 143.840 1.00 4.35   ? 196  TYR A N   1 
ATOM   1387 C  CA  . TYR A 1 286 ? 168.342 202.567 143.423 1.00 4.16   ? 196  TYR A CA  1 
ATOM   1388 C  C   . TYR A 1 286 ? 168.175 202.105 141.983 1.00 4.03   ? 196  TYR A C   1 
ATOM   1389 O  O   . TYR A 1 286 ? 167.056 202.012 141.482 1.00 4.06   ? 196  TYR A O   1 
ATOM   1390 C  CB  . TYR A 1 286 ? 168.588 201.371 144.340 1.00 4.04   ? 196  TYR A CB  1 
ATOM   1391 C  CG  . TYR A 1 286 ? 169.058 201.748 145.710 1.00 4.11   ? 196  TYR A CG  1 
ATOM   1392 C  CD1 . TYR A 1 286 ? 168.144 201.967 146.717 1.00 4.18   ? 196  TYR A CD1 1 
ATOM   1393 C  CD2 . TYR A 1 286 ? 170.409 201.871 145.962 1.00 4.02   ? 196  TYR A CD2 1 
ATOM   1394 C  CE1 . TYR A 1 286 ? 168.579 202.305 147.978 1.00 4.20   ? 196  TYR A CE1 1 
ATOM   1395 C  CE2 . TYR A 1 286 ? 170.846 202.208 147.219 1.00 4.03   ? 196  TYR A CE2 1 
ATOM   1396 C  CZ  . TYR A 1 286 ? 169.937 202.424 148.226 1.00 4.10   ? 196  TYR A CZ  1 
ATOM   1397 O  OH  . TYR A 1 286 ? 170.374 202.760 149.484 1.00 4.15   ? 196  TYR A OH  1 
ATOM   1398 N  N   . LYS A 1 287 ? 169.282 201.839 141.300 1.00 3.88   ? 197  LYS A N   1 
ATOM   1399 C  CA  . LYS A 1 287 ? 169.200 201.366 139.921 1.00 3.81   ? 197  LYS A CA  1 
ATOM   1400 C  C   . LYS A 1 287 ? 168.535 199.997 139.850 1.00 3.77   ? 197  LYS A C   1 
ATOM   1401 O  O   . LYS A 1 287 ? 167.705 199.736 138.980 1.00 3.75   ? 197  LYS A O   1 
ATOM   1402 C  CB  . LYS A 1 287 ? 170.589 201.296 139.295 1.00 3.83   ? 197  LYS A CB  1 
ATOM   1403 C  CG  . LYS A 1 287 ? 171.229 202.648 139.030 1.00 3.92   ? 197  LYS A CG  1 
ATOM   1404 C  CD  . LYS A 1 287 ? 172.489 202.512 138.184 1.00 4.13   ? 197  LYS A CD  1 
ATOM   1405 C  CE  . LYS A 1 287 ? 173.597 201.790 138.941 1.00 4.11   ? 197  LYS A CE  1 
ATOM   1406 N  NZ  . LYS A 1 287 ? 174.902 201.877 138.231 1.00 4.50   ? 197  LYS A NZ  1 
ATOM   1407 N  N   . ASP A 1 288 ? 168.918 199.127 140.774 1.00 3.67   ? 198  ASP A N   1 
ATOM   1408 C  CA  . ASP A 1 288 ? 168.404 197.767 140.846 1.00 3.62   ? 198  ASP A CA  1 
ATOM   1409 C  C   . ASP A 1 288 ? 168.700 197.180 142.222 1.00 3.64   ? 198  ASP A C   1 
ATOM   1410 O  O   . ASP A 1 288 ? 169.258 197.861 143.082 1.00 3.59   ? 198  ASP A O   1 
ATOM   1411 C  CB  . ASP A 1 288 ? 169.011 196.904 139.736 1.00 3.40   ? 198  ASP A CB  1 
ATOM   1412 C  CG  . ASP A 1 288 ? 170.518 196.814 139.812 1.00 3.41   ? 198  ASP A CG  1 
ATOM   1413 O  OD1 . ASP A 1 288 ? 171.012 196.392 140.833 1.00 3.28   ? 198  ASP A OD1 1 
ATOM   1414 O  OD2 . ASP A 1 288 ? 171.170 197.174 138.864 1.00 3.40   ? 198  ASP A OD2 1 
ATOM   1415 N  N   . TYR A 1 289 ? 168.313 195.930 142.439 1.00 3.41   ? 199  TYR A N   1 
ATOM   1416 C  CA  . TYR A 1 289 ? 168.519 195.294 143.734 1.00 3.42   ? 199  TYR A CA  1 
ATOM   1417 C  C   . TYR A 1 289 ? 169.994 195.028 144.042 1.00 3.45   ? 199  TYR A C   1 
ATOM   1418 O  O   . TYR A 1 289 ? 170.381 194.941 145.207 1.00 3.42   ? 199  TYR A O   1 
ATOM   1419 C  CB  . TYR A 1 289 ? 167.699 194.015 143.836 1.00 3.35   ? 199  TYR A CB  1 
ATOM   1420 C  CG  . TYR A 1 289 ? 167.665 193.432 145.222 1.00 3.24   ? 199  TYR A CG  1 
ATOM   1421 C  CD1 . TYR A 1 289 ? 167.242 194.201 146.295 1.00 3.36   ? 199  TYR A CD1 1 
ATOM   1422 C  CD2 . TYR A 1 289 ? 168.037 192.125 145.419 1.00 3.19   ? 199  TYR A CD2 1 
ATOM   1423 C  CE1 . TYR A 1 289 ? 167.207 193.652 147.555 1.00 3.33   ? 199  TYR A CE1 1 
ATOM   1424 C  CE2 . TYR A 1 289 ? 167.993 191.575 146.670 1.00 3.20   ? 199  TYR A CE2 1 
ATOM   1425 C  CZ  . TYR A 1 289 ? 167.582 192.331 147.738 1.00 3.25   ? 199  TYR A CZ  1 
ATOM   1426 O  OH  . TYR A 1 289 ? 167.528 191.773 148.995 1.00 3.18   ? 199  TYR A OH  1 
ATOM   1427 N  N   . GLY A 1 290 ? 170.818 194.886 143.009 1.00 3.37   ? 200  GLY A N   1 
ATOM   1428 C  CA  . GLY A 1 290 ? 172.248 194.691 143.218 1.00 3.35   ? 200  GLY A CA  1 
ATOM   1429 C  C   . GLY A 1 290 ? 172.849 195.978 143.762 1.00 3.67   ? 200  GLY A C   1 
ATOM   1430 O  O   . GLY A 1 290 ? 173.639 195.965 144.706 1.00 3.50   ? 200  GLY A O   1 
ATOM   1431 N  N   . ASP A 1 291 ? 172.416 197.091 143.178 1.00 3.51   ? 201  ASP A N   1 
ATOM   1432 C  CA  . ASP A 1 291 ? 172.817 198.431 143.590 1.00 3.71   ? 201  ASP A CA  1 
ATOM   1433 C  C   . ASP A 1 291 ? 172.355 198.702 145.017 1.00 3.92   ? 201  ASP A C   1 
ATOM   1434 O  O   . ASP A 1 291 ? 173.051 199.350 145.797 1.00 3.80   ? 201  ASP A O   1 
ATOM   1435 C  CB  . ASP A 1 291 ? 172.215 199.456 142.617 1.00 3.73   ? 201  ASP A CB  1 
ATOM   1436 C  CG  . ASP A 1 291 ? 172.783 200.859 142.734 1.00 3.95   ? 201  ASP A CG  1 
ATOM   1437 O  OD1 . ASP A 1 291 ? 173.974 200.989 142.862 1.00 3.97   ? 201  ASP A OD1 1 
ATOM   1438 O  OD2 . ASP A 1 291 ? 172.021 201.802 142.654 1.00 3.93   ? 201  ASP A OD2 1 
ATOM   1439 N  N   . TYR A 1 292 ? 171.188 198.168 145.361 1.00 3.53   ? 202  TYR A N   1 
ATOM   1440 C  CA  . TYR A 1 292 ? 170.636 198.278 146.704 1.00 3.91   ? 202  TYR A CA  1 
ATOM   1441 C  C   . TYR A 1 292 ? 171.567 197.628 147.727 1.00 3.75   ? 202  TYR A C   1 
ATOM   1442 O  O   . TYR A 1 292 ? 171.955 198.250 148.713 1.00 3.79   ? 202  TYR A O   1 
ATOM   1443 C  CB  . TYR A 1 292 ? 169.251 197.625 146.734 1.00 3.69   ? 202  TYR A CB  1 
ATOM   1444 C  CG  . TYR A 1 292 ? 168.519 197.698 148.040 1.00 3.83   ? 202  TYR A CG  1 
ATOM   1445 C  CD1 . TYR A 1 292 ? 167.687 198.767 148.301 1.00 4.02   ? 202  TYR A CD1 1 
ATOM   1446 C  CD2 . TYR A 1 292 ? 168.663 196.687 148.971 1.00 3.72   ? 202  TYR A CD2 1 
ATOM   1447 C  CE1 . TYR A 1 292 ? 167.000 198.831 149.490 1.00 4.29   ? 202  TYR A CE1 1 
ATOM   1448 C  CE2 . TYR A 1 292 ? 167.979 196.750 150.162 1.00 3.83   ? 202  TYR A CE2 1 
ATOM   1449 C  CZ  . TYR A 1 292 ? 167.148 197.817 150.422 1.00 4.14   ? 202  TYR A CZ  1 
ATOM   1450 O  OH  . TYR A 1 292 ? 166.462 197.880 151.611 1.00 4.52   ? 202  TYR A OH  1 
ATOM   1451 N  N   . TRP A 1 293 ? 171.953 196.380 147.470 1.00 3.59   ? 203  TRP A N   1 
ATOM   1452 C  CA  . TRP A 1 293 ? 172.843 195.648 148.369 1.00 3.68   ? 203  TRP A CA  1 
ATOM   1453 C  C   . TRP A 1 293 ? 174.216 196.294 148.510 1.00 3.85   ? 203  TRP A C   1 
ATOM   1454 O  O   . TRP A 1 293 ? 174.793 196.309 149.597 1.00 3.92   ? 203  TRP A O   1 
ATOM   1455 C  CB  . TRP A 1 293 ? 173.025 194.206 147.895 1.00 3.47   ? 203  TRP A CB  1 
ATOM   1456 C  CG  . TRP A 1 293 ? 172.044 193.217 148.468 1.00 3.34   ? 203  TRP A CG  1 
ATOM   1457 C  CD1 . TRP A 1 293 ? 171.236 193.375 149.555 1.00 3.35   ? 203  TRP A CD1 1 
ATOM   1458 C  CD2 . TRP A 1 293 ? 171.796 191.884 147.982 1.00 3.18   ? 203  TRP A CD2 1 
ATOM   1459 N  NE1 . TRP A 1 293 ? 170.515 192.238 149.772 1.00 3.20   ? 203  TRP A NE1 1 
ATOM   1460 C  CE2 . TRP A 1 293 ? 170.846 191.315 148.823 1.00 3.13   ? 203  TRP A CE2 1 
ATOM   1461 C  CE3 . TRP A 1 293 ? 172.302 191.137 146.920 1.00 3.10   ? 203  TRP A CE3 1 
ATOM   1462 C  CZ2 . TRP A 1 293 ? 170.387 190.027 148.640 1.00 3.07   ? 203  TRP A CZ2 1 
ATOM   1463 C  CZ3 . TRP A 1 293 ? 171.839 189.848 146.735 1.00 3.00   ? 203  TRP A CZ3 1 
ATOM   1464 C  CH2 . TRP A 1 293 ? 170.906 189.308 147.575 1.00 3.03   ? 203  TRP A CH2 1 
ATOM   1465 N  N   . ARG A 1 294 ? 174.740 196.835 147.420 1.00 3.72   ? 204  ARG A N   1 
ATOM   1466 C  CA  . ARG A 1 294 ? 176.071 197.432 147.434 1.00 3.90   ? 204  ARG A CA  1 
ATOM   1467 C  C   . ARG A 1 294 ? 176.110 198.717 148.258 1.00 4.07   ? 204  ARG A C   1 
ATOM   1468 O  O   . ARG A 1 294 ? 177.181 199.270 148.509 1.00 4.30   ? 204  ARG A O   1 
ATOM   1469 C  CB  . ARG A 1 294 ? 176.559 197.710 146.021 1.00 3.88   ? 204  ARG A CB  1 
ATOM   1470 C  CG  . ARG A 1 294 ? 176.901 196.465 145.204 1.00 3.65   ? 204  ARG A CG  1 
ATOM   1471 C  CD  . ARG A 1 294 ? 177.685 196.794 143.987 1.00 3.65   ? 204  ARG A CD  1 
ATOM   1472 N  NE  . ARG A 1 294 ? 176.921 197.577 143.031 1.00 3.66   ? 204  ARG A NE  1 
ATOM   1473 C  CZ  . ARG A 1 294 ? 176.136 197.069 142.062 1.00 3.42   ? 204  ARG A CZ  1 
ATOM   1474 N  NH1 . ARG A 1 294 ? 176.003 195.774 141.920 1.00 3.27   ? 204  ARG A NH1 1 
ATOM   1475 N  NH2 . ARG A 1 294 ? 175.498 197.885 141.246 1.00 3.54   ? 204  ARG A NH2 1 
ATOM   1476 N  N   . GLY A 1 295 ? 174.942 199.192 148.681 1.00 4.00   ? 205  GLY A N   1 
ATOM   1477 C  CA  . GLY A 1 295 ? 174.845 200.409 149.473 1.00 4.27   ? 205  GLY A CA  1 
ATOM   1478 C  C   . GLY A 1 295 ? 175.370 200.194 150.884 1.00 4.37   ? 205  GLY A C   1 
ATOM   1479 O  O   . GLY A 1 295 ? 175.621 201.151 151.613 1.00 4.55   ? 205  GLY A O   1 
ATOM   1480 N  N   . ASP A 1 296 ? 175.567 198.937 151.260 1.00 4.29   ? 206  ASP A N   1 
ATOM   1481 C  CA  . ASP A 1 296 ? 176.042 198.604 152.596 1.00 4.41   ? 206  ASP A CA  1 
ATOM   1482 C  C   . ASP A 1 296 ? 177.499 198.994 152.804 1.00 4.56   ? 206  ASP A C   1 
ATOM   1483 O  O   . ASP A 1 296 ? 177.989 199.005 153.934 1.00 4.72   ? 206  ASP A O   1 
ATOM   1484 C  CB  . ASP A 1 296 ? 175.846 197.114 152.870 1.00 4.32   ? 206  ASP A CB  1 
ATOM   1485 N  N   . TYR A 1 297 ? 178.197 199.312 151.718 1.00 4.62   ? 207  TYR A N   1 
ATOM   1486 C  CA  . TYR A 1 297 ? 179.587 199.739 151.797 1.00 4.80   ? 207  TYR A CA  1 
ATOM   1487 C  C   . TYR A 1 297 ? 179.745 201.216 151.468 1.00 5.00   ? 207  TYR A C   1 
ATOM   1488 O  O   . TYR A 1 297 ? 180.862 201.723 151.386 1.00 5.23   ? 207  TYR A O   1 
ATOM   1489 C  CB  . TYR A 1 297 ? 180.451 198.905 150.856 1.00 4.75   ? 207  TYR A CB  1 
ATOM   1490 C  CG  . TYR A 1 297 ? 180.611 197.488 151.294 1.00 4.77   ? 207  TYR A CG  1 
ATOM   1491 C  CD1 . TYR A 1 297 ? 181.727 197.120 152.022 1.00 4.93   ? 207  TYR A CD1 1 
ATOM   1492 C  CD2 . TYR A 1 297 ? 179.639 196.556 150.990 1.00 4.57   ? 207  TYR A CD2 1 
ATOM   1493 C  CE1 . TYR A 1 297 ? 181.873 195.818 152.437 1.00 4.88   ? 207  TYR A CE1 1 
ATOM   1494 C  CE2 . TYR A 1 297 ? 179.784 195.258 151.409 1.00 4.61   ? 207  TYR A CE2 1 
ATOM   1495 C  CZ  . TYR A 1 297 ? 180.897 194.889 152.128 1.00 4.70   ? 207  TYR A CZ  1 
ATOM   1496 O  OH  . TYR A 1 297 ? 181.034 193.597 152.550 1.00 4.48   ? 207  TYR A OH  1 
ATOM   1497 N  N   . GLU A 1 298 ? 178.624 201.901 151.265 1.00 4.95   ? 208  GLU A N   1 
ATOM   1498 C  CA  . GLU A 1 298 ? 178.660 203.293 150.853 1.00 5.20   ? 208  GLU A CA  1 
ATOM   1499 C  C   . GLU A 1 298 ? 178.865 204.235 152.024 1.00 5.53   ? 208  GLU A C   1 
ATOM   1500 O  O   . GLU A 1 298 ? 178.185 204.125 153.047 1.00 5.65   ? 208  GLU A O   1 
ATOM   1501 C  CB  . GLU A 1 298 ? 177.369 203.670 150.137 1.00 4.96   ? 208  GLU A CB  1 
ATOM   1502 C  CG  . GLU A 1 298 ? 177.373 205.062 149.548 1.00 5.15   ? 208  GLU A CG  1 
ATOM   1503 C  CD  . GLU A 1 298 ? 176.118 205.384 148.820 1.00 4.99   ? 208  GLU A CD  1 
ATOM   1504 O  OE1 . GLU A 1 298 ? 175.255 204.539 148.762 1.00 4.82   ? 208  GLU A OE1 1 
ATOM   1505 O  OE2 . GLU A 1 298 ? 176.008 206.477 148.320 1.00 5.04   ? 208  GLU A OE2 1 
ATOM   1506 N  N   . THR A 1 299 ? 179.790 205.169 151.863 1.00 5.77   ? 209  THR A N   1 
ATOM   1507 C  CA  . THR A 1 299 ? 180.027 206.196 152.869 1.00 6.08   ? 209  THR A CA  1 
ATOM   1508 C  C   . THR A 1 299 ? 180.271 207.548 152.220 1.00 6.43   ? 209  THR A C   1 
ATOM   1509 O  O   . THR A 1 299 ? 180.610 207.633 151.038 1.00 6.46   ? 209  THR A O   1 
ATOM   1510 C  CB  . THR A 1 299 ? 181.215 205.827 153.783 1.00 6.22   ? 209  THR A CB  1 
ATOM   1511 O  OG1 . THR A 1 299 ? 182.434 205.843 153.031 1.00 6.21   ? 209  THR A OG1 1 
ATOM   1512 C  CG2 . THR A 1 299 ? 181.006 204.434 154.376 1.00 6.04   ? 209  THR A CG2 1 
ATOM   1513 N  N   . GLU A 1 300 ? 180.148 208.611 153.006 1.00 6.92   ? 210  GLU A N   1 
ATOM   1514 C  CA  . GLU A 1 300 ? 180.436 209.951 152.516 1.00 7.25   ? 210  GLU A CA  1 
ATOM   1515 C  C   . GLU A 1 300 ? 181.279 210.720 153.519 1.00 7.31   ? 210  GLU A C   1 
ATOM   1516 O  O   . GLU A 1 300 ? 181.221 210.460 154.721 1.00 7.31   ? 210  GLU A O   1 
ATOM   1517 C  CB  . GLU A 1 300 ? 179.137 210.714 152.235 1.00 7.46   ? 210  GLU A CB  1 
ATOM   1518 C  CG  . GLU A 1 300 ? 178.274 210.986 153.465 1.00 7.84   ? 210  GLU A CG  1 
ATOM   1519 C  CD  . GLU A 1 300 ? 176.996 211.727 153.136 1.00 8.81   ? 210  GLU A CD  1 
ATOM   1520 O  OE1 . GLU A 1 300 ? 176.919 212.900 153.428 1.00 9.14   ? 210  GLU A OE1 1 
ATOM   1521 O  OE2 . GLU A 1 300 ? 176.101 211.122 152.597 1.00 9.21   ? 210  GLU A OE2 1 
ATOM   1522 N  N   . GLY A 1 301 ? 182.052 211.680 153.023 1.00 7.41   ? 211  GLY A N   1 
ATOM   1523 C  CA  . GLY A 1 301 ? 182.881 212.516 153.881 1.00 7.58   ? 211  GLY A CA  1 
ATOM   1524 C  C   . GLY A 1 301 ? 183.954 213.228 153.073 1.00 7.66   ? 211  GLY A C   1 
ATOM   1525 O  O   . GLY A 1 301 ? 183.946 213.187 151.840 1.00 7.71   ? 211  GLY A O   1 
ATOM   1526 N  N   . GLY A 1 302 ? 184.860 213.910 153.771 1.00 7.68   ? 212  GLY A N   1 
ATOM   1527 C  CA  . GLY A 1 302 ? 185.909 214.679 153.112 1.00 7.75   ? 212  GLY A CA  1 
ATOM   1528 C  C   . GLY A 1 302 ? 187.110 213.807 152.782 1.00 7.54   ? 212  GLY A C   1 
ATOM   1529 O  O   . GLY A 1 302 ? 187.069 212.586 152.954 1.00 7.78   ? 212  GLY A O   1 
ATOM   1530 N  N   . ASP A 1 303 ? 188.179 214.442 152.316 1.00 7.82   ? 213  ASP A N   1 
ATOM   1531 C  CA  . ASP A 1 303 ? 189.403 213.733 151.973 1.00 7.79   ? 213  ASP A CA  1 
ATOM   1532 C  C   . ASP A 1 303 ? 189.109 212.545 151.058 1.00 7.68   ? 213  ASP A C   1 
ATOM   1533 O  O   . ASP A 1 303 ? 188.362 212.669 150.088 1.00 7.78   ? 213  ASP A O   1 
ATOM   1534 C  CB  . ASP A 1 303 ? 190.115 213.264 153.244 1.00 7.74   ? 213  ASP A CB  1 
ATOM   1535 N  N   . GLY A 1 304 ? 189.679 211.391 151.389 1.00 7.62   ? 214  GLY A N   1 
ATOM   1536 C  CA  . GLY A 1 304 ? 189.446 210.165 150.640 1.00 7.52   ? 214  GLY A CA  1 
ATOM   1537 C  C   . GLY A 1 304 ? 188.533 209.221 151.408 1.00 7.25   ? 214  GLY A C   1 
ATOM   1538 O  O   . GLY A 1 304 ? 188.560 208.009 151.186 1.00 7.11   ? 214  GLY A O   1 
ATOM   1539 N  N   . TYR A 1 305 ? 187.743 209.764 152.333 1.00 7.44   ? 215  TYR A N   1 
ATOM   1540 C  CA  . TYR A 1 305 ? 186.900 208.933 153.187 1.00 7.05   ? 215  TYR A CA  1 
ATOM   1541 C  C   . TYR A 1 305 ? 185.534 208.575 152.563 1.00 7.17   ? 215  TYR A C   1 
ATOM   1542 O  O   . TYR A 1 305 ? 184.737 207.887 153.192 1.00 6.91   ? 215  TYR A O   1 
ATOM   1543 C  CB  . TYR A 1 305 ? 186.684 209.607 154.552 1.00 7.18   ? 215  TYR A CB  1 
ATOM   1544 C  CG  . TYR A 1 305 ? 187.942 209.765 155.373 1.00 7.16   ? 215  TYR A CG  1 
ATOM   1545 C  CD1 . TYR A 1 305 ? 188.387 211.030 155.692 1.00 7.38   ? 215  TYR A CD1 1 
ATOM   1546 C  CD2 . TYR A 1 305 ? 188.647 208.654 155.801 1.00 6.86   ? 215  TYR A CD2 1 
ATOM   1547 C  CE1 . TYR A 1 305 ? 189.534 211.193 156.431 1.00 7.23   ? 215  TYR A CE1 1 
ATOM   1548 C  CE2 . TYR A 1 305 ? 189.799 208.815 156.542 1.00 6.93   ? 215  TYR A CE2 1 
ATOM   1549 C  CZ  . TYR A 1 305 ? 190.243 210.085 156.855 1.00 7.10   ? 215  TYR A CZ  1 
ATOM   1550 O  OH  . TYR A 1 305 ? 191.394 210.262 157.591 1.00 7.28   ? 215  TYR A OH  1 
ATOM   1551 N  N   . ASN A 1 306 ? 185.272 209.061 151.350 1.00 7.18   ? 216  ASN A N   1 
ATOM   1552 C  CA  . ASN A 1 306 ? 184.044 208.743 150.612 1.00 6.99   ? 216  ASN A CA  1 
ATOM   1553 C  C   . ASN A 1 306 ? 184.218 207.487 149.799 1.00 6.91   ? 216  ASN A C   1 
ATOM   1554 O  O   . ASN A 1 306 ? 185.317 207.251 149.233 1.00 7.04   ? 216  ASN A O   1 
ATOM   1555 C  CB  . ASN A 1 306 ? 183.596 209.926 149.766 1.00 7.37   ? 216  ASN A CB  1 
ATOM   1556 C  CG  . ASN A 1 306 ? 184.610 210.332 148.711 1.00 7.79   ? 216  ASN A CG  1 
ATOM   1557 O  OD1 . ASN A 1 306 ? 185.539 211.109 148.994 1.00 8.04   ? 216  ASN A OD1 1 
ATOM   1558 N  ND2 . ASN A 1 306 ? 184.443 209.839 147.503 1.00 8.40   ? 216  ASN A ND2 1 
ATOM   1559 N  N   . TYR A 1 307 ? 183.166 206.694 149.663 1.00 6.36   ? 217  TYR A N   1 
ATOM   1560 C  CA  . TYR A 1 307 ? 183.176 205.439 148.925 1.00 6.07   ? 217  TYR A CA  1 
ATOM   1561 C  C   . TYR A 1 307 ? 181.863 205.226 148.195 1.00 5.76   ? 217  TYR A C   1 
ATOM   1562 O  O   . TYR A 1 307 ? 180.831 204.995 148.832 1.00 5.50   ? 217  TYR A O   1 
ATOM   1563 C  CB  . TYR A 1 307 ? 183.416 204.303 149.910 1.00 5.72   ? 217  TYR A CB  1 
ATOM   1564 C  CG  . TYR A 1 307 ? 183.873 203.019 149.293 1.00 5.45   ? 217  TYR A CG  1 
ATOM   1565 C  CD1 . TYR A 1 307 ? 182.952 202.058 148.907 1.00 5.22   ? 217  TYR A CD1 1 
ATOM   1566 C  CD2 . TYR A 1 307 ? 185.223 202.788 149.132 1.00 5.43   ? 217  TYR A CD2 1 
ATOM   1567 C  CE1 . TYR A 1 307 ? 183.387 200.872 148.357 1.00 5.05   ? 217  TYR A CE1 1 
ATOM   1568 C  CE2 . TYR A 1 307 ? 185.654 201.607 148.585 1.00 5.10   ? 217  TYR A CE2 1 
ATOM   1569 C  CZ  . TYR A 1 307 ? 184.744 200.651 148.199 1.00 4.98   ? 217  TYR A CZ  1 
ATOM   1570 O  OH  . TYR A 1 307 ? 185.184 199.473 147.651 1.00 4.90   ? 217  TYR A OH  1 
ATOM   1571 N  N   . SER A 1 308 ? 181.889 205.311 146.867 1.00 5.61   ? 218  SER A N   1 
ATOM   1572 C  CA  . SER A 1 308 ? 180.671 205.144 146.085 1.00 5.36   ? 218  SER A CA  1 
ATOM   1573 C  C   . SER A 1 308 ? 180.326 203.674 145.928 1.00 5.09   ? 218  SER A C   1 
ATOM   1574 O  O   . SER A 1 308 ? 181.178 202.804 146.109 1.00 4.97   ? 218  SER A O   1 
ATOM   1575 C  CB  . SER A 1 308 ? 180.823 205.791 144.724 1.00 5.28   ? 218  SER A CB  1 
ATOM   1576 O  OG  . SER A 1 308 ? 181.722 205.085 143.923 1.00 5.28   ? 218  SER A OG  1 
ATOM   1577 N  N   . ARG A 1 309 ? 179.083 203.399 145.558 1.00 4.90   ? 219  ARG A N   1 
ATOM   1578 C  CA  . ARG A 1 309 ? 178.629 202.025 145.382 1.00 4.76   ? 219  ARG A CA  1 
ATOM   1579 C  C   . ARG A 1 309 ? 179.344 201.343 144.218 1.00 4.66   ? 219  ARG A C   1 
ATOM   1580 O  O   . ARG A 1 309 ? 179.685 200.165 144.289 1.00 4.48   ? 219  ARG A O   1 
ATOM   1581 C  CB  . ARG A 1 309 ? 177.123 201.990 145.166 1.00 4.54   ? 219  ARG A CB  1 
ATOM   1582 C  CG  . ARG A 1 309 ? 176.322 202.439 146.380 1.00 4.53   ? 219  ARG A CG  1 
ATOM   1583 C  CD  . ARG A 1 309 ? 174.885 202.069 146.305 1.00 4.32   ? 219  ARG A CD  1 
ATOM   1584 N  NE  . ARG A 1 309 ? 174.183 202.694 145.200 1.00 4.25   ? 219  ARG A NE  1 
ATOM   1585 C  CZ  . ARG A 1 309 ? 173.607 203.917 145.223 1.00 4.32   ? 219  ARG A CZ  1 
ATOM   1586 N  NH1 . ARG A 1 309 ? 173.675 204.679 146.294 1.00 4.35   ? 219  ARG A NH1 1 
ATOM   1587 N  NH2 . ARG A 1 309 ? 172.961 204.345 144.154 1.00 4.51   ? 219  ARG A NH2 1 
ATOM   1588 N  N   . ASN A 1 310 ? 179.620 202.107 143.167 1.00 4.75   ? 220  ASN A N   1 
ATOM   1589 C  CA  . ASN A 1 310 ? 180.279 201.584 141.974 1.00 4.68   ? 220  ASN A CA  1 
ATOM   1590 C  C   . ASN A 1 310 ? 181.718 201.166 142.255 1.00 4.69   ? 220  ASN A C   1 
ATOM   1591 O  O   . ASN A 1 310 ? 182.293 200.352 141.531 1.00 4.54   ? 220  ASN A O   1 
ATOM   1592 C  CB  . ASN A 1 310 ? 180.271 202.618 140.872 1.00 4.69   ? 220  ASN A CB  1 
ATOM   1593 C  CG  . ASN A 1 310 ? 178.913 202.859 140.307 1.00 4.69   ? 220  ASN A CG  1 
ATOM   1594 O  OD1 . ASN A 1 310 ? 178.014 202.019 140.416 1.00 4.74   ? 220  ASN A OD1 1 
ATOM   1595 N  ND2 . ASN A 1 310 ? 178.738 204.003 139.702 1.00 4.69   ? 220  ASN A ND2 1 
ATOM   1596 N  N   . HIS A 1 311 ? 182.307 201.761 143.282 1.00 4.73   ? 221  HIS A N   1 
ATOM   1597 C  CA  . HIS A 1 311 ? 183.705 201.521 143.597 1.00 4.79   ? 221  HIS A CA  1 
ATOM   1598 C  C   . HIS A 1 311 ? 183.898 200.123 144.149 1.00 5.31   ? 221  HIS A C   1 
ATOM   1599 O  O   . HIS A 1 311 ? 184.985 199.557 144.065 1.00 4.45   ? 221  HIS A O   1 
ATOM   1600 C  CB  . HIS A 1 311 ? 184.235 202.550 144.594 1.00 5.08   ? 221  HIS A CB  1 
ATOM   1601 C  CG  . HIS A 1 311 ? 185.718 202.700 144.542 1.00 5.17   ? 221  HIS A CG  1 
ATOM   1602 N  ND1 . HIS A 1 311 ? 186.350 203.482 143.601 1.00 5.30   ? 221  HIS A ND1 1 
ATOM   1603 C  CD2 . HIS A 1 311 ? 186.697 202.146 145.285 1.00 5.19   ? 221  HIS A CD2 1 
ATOM   1604 C  CE1 . HIS A 1 311 ? 187.655 203.409 143.779 1.00 5.39   ? 221  HIS A CE1 1 
ATOM   1605 N  NE2 . HIS A 1 311 ? 187.891 202.606 144.795 1.00 5.21   ? 221  HIS A NE2 1 
ATOM   1606 N  N   . LEU A 1 312 ? 182.839 199.560 144.727 1.00 4.60   ? 222  LEU A N   1 
ATOM   1607 C  CA  . LEU A 1 312 ? 182.933 198.237 145.319 1.00 4.55   ? 222  LEU A CA  1 
ATOM   1608 C  C   . LEU A 1 312 ? 183.232 197.212 144.242 1.00 4.50   ? 222  LEU A C   1 
ATOM   1609 O  O   . LEU A 1 312 ? 183.975 196.259 144.470 1.00 4.38   ? 222  LEU A O   1 
ATOM   1610 C  CB  . LEU A 1 312 ? 181.630 197.869 146.042 1.00 4.52   ? 222  LEU A CB  1 
ATOM   1611 C  CG  . LEU A 1 312 ? 181.624 196.527 146.825 1.00 4.45   ? 222  LEU A CG  1 
ATOM   1612 C  CD1 . LEU A 1 312 ? 182.670 196.561 147.939 1.00 4.59   ? 222  LEU A CD1 1 
ATOM   1613 C  CD2 . LEU A 1 312 ? 180.239 196.298 147.399 1.00 4.34   ? 222  LEU A CD2 1 
ATOM   1614 N  N   . ILE A 1 313 ? 182.647 197.411 143.066 1.00 4.39   ? 223  ILE A N   1 
ATOM   1615 C  CA  . ILE A 1 313 ? 182.852 196.494 141.958 1.00 4.28   ? 223  ILE A CA  1 
ATOM   1616 C  C   . ILE A 1 313 ? 184.300 196.545 141.501 1.00 4.41   ? 223  ILE A C   1 
ATOM   1617 O  O   . ILE A 1 313 ? 184.930 195.509 141.288 1.00 4.22   ? 223  ILE A O   1 
ATOM   1618 C  CB  . ILE A 1 313 ? 181.926 196.835 140.779 1.00 4.26   ? 223  ILE A CB  1 
ATOM   1619 C  CG1 . ILE A 1 313 ? 180.468 196.588 141.177 1.00 4.03   ? 223  ILE A CG1 1 
ATOM   1620 C  CG2 . ILE A 1 313 ? 182.303 195.990 139.565 1.00 4.20   ? 223  ILE A CG2 1 
ATOM   1621 C  CD1 . ILE A 1 313 ? 179.464 197.176 140.216 1.00 3.87   ? 223  ILE A CD1 1 
ATOM   1622 N  N   . GLU A 1 314 ? 184.832 197.753 141.367 1.00 4.37   ? 224  GLU A N   1 
ATOM   1623 C  CA  . GLU A 1 314 ? 186.214 197.908 140.935 1.00 4.45   ? 224  GLU A CA  1 
ATOM   1624 C  C   . GLU A 1 314 ? 187.186 197.285 141.928 1.00 4.39   ? 224  GLU A C   1 
ATOM   1625 O  O   . GLU A 1 314 ? 188.167 196.649 141.525 1.00 4.33   ? 224  GLU A O   1 
ATOM   1626 C  CB  . GLU A 1 314 ? 186.546 199.388 140.744 1.00 4.59   ? 224  GLU A CB  1 
ATOM   1627 N  N   . ASP A 1 315 ? 186.918 197.437 143.227 1.00 4.42   ? 225  ASP A N   1 
ATOM   1628 C  CA  . ASP A 1 315 ? 187.801 196.883 144.242 1.00 4.55   ? 225  ASP A CA  1 
ATOM   1629 C  C   . ASP A 1 315 ? 187.778 195.361 144.322 1.00 4.57   ? 225  ASP A C   1 
ATOM   1630 O  O   . ASP A 1 315 ? 188.825 194.745 144.497 1.00 4.20   ? 225  ASP A O   1 
ATOM   1631 C  CB  . ASP A 1 315 ? 187.503 197.473 145.624 1.00 4.69   ? 225  ASP A CB  1 
ATOM   1632 N  N   . VAL A 1 316 ? 186.608 194.740 144.175 1.00 4.26   ? 226  VAL A N   1 
ATOM   1633 C  CA  . VAL A 1 316 ? 186.593 193.277 144.246 1.00 4.19   ? 226  VAL A CA  1 
ATOM   1634 C  C   . VAL A 1 316 ? 187.261 192.658 143.026 1.00 4.25   ? 226  VAL A C   1 
ATOM   1635 O  O   . VAL A 1 316 ? 187.889 191.607 143.135 1.00 3.83   ? 226  VAL A O   1 
ATOM   1636 C  CB  . VAL A 1 316 ? 185.162 192.716 144.420 1.00 4.09   ? 226  VAL A CB  1 
ATOM   1637 C  CG1 . VAL A 1 316 ? 184.572 193.211 145.728 1.00 4.19   ? 226  VAL A CG1 1 
ATOM   1638 C  CG2 . VAL A 1 316 ? 184.281 193.115 143.254 1.00 4.06   ? 226  VAL A CG2 1 
ATOM   1639 N  N   . ASP A 1 317 ? 187.163 193.323 141.879 1.00 3.97   ? 227  ASP A N   1 
ATOM   1640 C  CA  . ASP A 1 317 ? 187.815 192.819 140.680 1.00 3.99   ? 227  ASP A CA  1 
ATOM   1641 C  C   . ASP A 1 317 ? 189.327 192.952 140.801 1.00 4.14   ? 227  ASP A C   1 
ATOM   1642 O  O   . ASP A 1 317 ? 190.071 192.027 140.466 1.00 3.91   ? 227  ASP A O   1 
ATOM   1643 C  CB  . ASP A 1 317 ? 187.336 193.580 139.444 1.00 3.94   ? 227  ASP A CB  1 
ATOM   1644 C  CG  . ASP A 1 317 ? 185.897 193.271 139.057 1.00 3.89   ? 227  ASP A CG  1 
ATOM   1645 O  OD1 . ASP A 1 317 ? 185.320 192.378 139.624 1.00 3.75   ? 227  ASP A OD1 1 
ATOM   1646 O  OD2 . ASP A 1 317 ? 185.393 193.924 138.175 1.00 4.00   ? 227  ASP A OD2 1 
ATOM   1647 N  N   . ARG A 1 318 ? 189.775 194.086 141.326 1.00 4.12   ? 228  ARG A N   1 
ATOM   1648 C  CA  . ARG A 1 318 ? 191.192 194.337 141.532 1.00 4.15   ? 228  ARG A CA  1 
ATOM   1649 C  C   . ARG A 1 318 ? 191.792 193.333 142.509 1.00 4.28   ? 228  ARG A C   1 
ATOM   1650 O  O   . ARG A 1 318 ? 192.842 192.748 142.245 1.00 4.09   ? 228  ARG A O   1 
ATOM   1651 C  CB  . ARG A 1 318 ? 191.390 195.754 142.048 1.00 4.34   ? 228  ARG A CB  1 
ATOM   1652 C  CG  . ARG A 1 318 ? 192.807 196.137 142.393 1.00 4.44   ? 228  ARG A CG  1 
ATOM   1653 C  CD  . ARG A 1 318 ? 192.883 197.548 142.866 1.00 4.56   ? 228  ARG A CD  1 
ATOM   1654 N  NE  . ARG A 1 318 ? 192.126 197.761 144.101 1.00 4.71   ? 228  ARG A NE  1 
ATOM   1655 C  CZ  . ARG A 1 318 ? 192.541 197.397 145.330 1.00 4.86   ? 228  ARG A CZ  1 
ATOM   1656 N  NH1 . ARG A 1 318 ? 193.699 196.792 145.490 1.00 4.79   ? 228  ARG A NH1 1 
ATOM   1657 N  NH2 . ARG A 1 318 ? 191.775 197.656 146.372 1.00 5.05   ? 228  ARG A NH2 1 
ATOM   1658 N  N   . ILE A 1 319 ? 191.101 193.112 143.622 1.00 4.04   ? 229  ILE A N   1 
ATOM   1659 C  CA  . ILE A 1 319 ? 191.561 192.174 144.632 1.00 4.17   ? 229  ILE A CA  1 
ATOM   1660 C  C   . ILE A 1 319 ? 191.592 190.754 144.095 1.00 4.14   ? 229  ILE A C   1 
ATOM   1661 O  O   . ILE A 1 319 ? 192.542 190.016 144.345 1.00 3.96   ? 229  ILE A O   1 
ATOM   1662 C  CB  . ILE A 1 319 ? 190.686 192.255 145.893 1.00 4.20   ? 229  ILE A CB  1 
ATOM   1663 C  CG1 . ILE A 1 319 ? 190.928 193.605 146.585 1.00 4.47   ? 229  ILE A CG1 1 
ATOM   1664 C  CG2 . ILE A 1 319 ? 190.985 191.089 146.833 1.00 4.26   ? 229  ILE A CG2 1 
ATOM   1665 C  CD1 . ILE A 1 319 ? 189.922 193.947 147.654 1.00 4.75   ? 229  ILE A CD1 1 
ATOM   1666 N  N   . PHE A 1 320 ? 190.554 190.361 143.365 1.00 3.84   ? 230  PHE A N   1 
ATOM   1667 C  CA  . PHE A 1 320 ? 190.506 189.015 142.818 1.00 3.78   ? 230  PHE A CA  1 
ATOM   1668 C  C   . PHE A 1 320 ? 191.736 188.719 141.972 1.00 3.91   ? 230  PHE A C   1 
ATOM   1669 O  O   . PHE A 1 320 ? 192.354 187.664 142.118 1.00 3.61   ? 230  PHE A O   1 
ATOM   1670 C  CB  . PHE A 1 320 ? 189.246 188.795 141.987 1.00 3.56   ? 230  PHE A CB  1 
ATOM   1671 C  CG  . PHE A 1 320 ? 189.218 187.444 141.357 1.00 3.36   ? 230  PHE A CG  1 
ATOM   1672 C  CD1 . PHE A 1 320 ? 188.989 186.322 142.128 1.00 3.26   ? 230  PHE A CD1 1 
ATOM   1673 C  CD2 . PHE A 1 320 ? 189.437 187.285 140.000 1.00 3.38   ? 230  PHE A CD2 1 
ATOM   1674 C  CE1 . PHE A 1 320 ? 188.988 185.070 141.561 1.00 3.17   ? 230  PHE A CE1 1 
ATOM   1675 C  CE2 . PHE A 1 320 ? 189.432 186.034 139.431 1.00 3.23   ? 230  PHE A CE2 1 
ATOM   1676 C  CZ  . PHE A 1 320 ? 189.211 184.924 140.215 1.00 3.10   ? 230  PHE A CZ  1 
ATOM   1677 N  N   . LEU A 1 321 ? 192.096 189.644 141.089 1.00 3.79   ? 231  LEU A N   1 
ATOM   1678 C  CA  . LEU A 1 321 ? 193.239 189.438 140.209 1.00 3.85   ? 231  LEU A CA  1 
ATOM   1679 C  C   . LEU A 1 321 ? 194.554 189.311 140.976 1.00 3.82   ? 231  LEU A C   1 
ATOM   1680 O  O   . LEU A 1 321 ? 195.455 188.594 140.545 1.00 3.70   ? 231  LEU A O   1 
ATOM   1681 C  CB  . LEU A 1 321 ? 193.335 190.579 139.189 1.00 3.96   ? 231  LEU A CB  1 
ATOM   1682 C  CG  . LEU A 1 321 ? 192.220 190.629 138.119 1.00 4.08   ? 231  LEU A CG  1 
ATOM   1683 C  CD1 . LEU A 1 321 ? 192.356 191.913 137.316 1.00 4.08   ? 231  LEU A CD1 1 
ATOM   1684 C  CD2 . LEU A 1 321 ? 192.321 189.410 137.203 1.00 3.91   ? 231  LEU A CD2 1 
ATOM   1685 N  N   . GLU A 1 322 ? 194.668 190.002 142.109 1.00 3.84   ? 232  GLU A N   1 
ATOM   1686 C  CA  . GLU A 1 322 ? 195.863 189.898 142.947 1.00 3.92   ? 232  GLU A CA  1 
ATOM   1687 C  C   . GLU A 1 322 ? 195.960 188.524 143.614 1.00 3.85   ? 232  GLU A C   1 
ATOM   1688 O  O   . GLU A 1 322 ? 197.052 187.988 143.787 1.00 3.85   ? 232  GLU A O   1 
ATOM   1689 C  CB  . GLU A 1 322 ? 195.869 190.988 144.018 1.00 4.09   ? 232  GLU A CB  1 
ATOM   1690 C  CG  . GLU A 1 322 ? 196.077 192.397 143.488 1.00 4.20   ? 232  GLU A CG  1 
ATOM   1691 C  CD  . GLU A 1 322 ? 195.927 193.448 144.554 1.00 4.61   ? 232  GLU A CD  1 
ATOM   1692 O  OE1 . GLU A 1 322 ? 195.452 193.123 145.611 1.00 4.73   ? 232  GLU A OE1 1 
ATOM   1693 O  OE2 . GLU A 1 322 ? 196.289 194.576 144.309 1.00 4.86   ? 232  GLU A OE2 1 
ATOM   1694 N  N   . ILE A 1 323 ? 194.809 187.973 143.989 1.00 3.75   ? 233  ILE A N   1 
ATOM   1695 C  CA  . ILE A 1 323 ? 194.731 186.668 144.638 1.00 3.75   ? 233  ILE A CA  1 
ATOM   1696 C  C   . ILE A 1 323 ? 194.960 185.523 143.654 1.00 3.84   ? 233  ILE A C   1 
ATOM   1697 O  O   . ILE A 1 323 ? 195.560 184.506 143.997 1.00 3.54   ? 233  ILE A O   1 
ATOM   1698 C  CB  . ILE A 1 323 ? 193.359 186.468 145.324 1.00 3.78   ? 233  ILE A CB  1 
ATOM   1699 C  CG1 . ILE A 1 323 ? 193.145 187.499 146.464 1.00 3.93   ? 233  ILE A CG1 1 
ATOM   1700 C  CG2 . ILE A 1 323 ? 193.223 185.035 145.851 1.00 3.96   ? 233  ILE A CG2 1 
ATOM   1701 C  CD1 . ILE A 1 323 ? 194.157 187.440 147.588 1.00 4.39   ? 233  ILE A CD1 1 
ATOM   1702 N  N   . LYS A 1 324 ? 194.420 185.677 142.447 1.00 3.54   ? 234  LYS A N   1 
ATOM   1703 C  CA  . LYS A 1 324 ? 194.388 184.609 141.450 1.00 3.49   ? 234  LYS A CA  1 
ATOM   1704 C  C   . LYS A 1 324 ? 195.670 183.760 141.329 1.00 3.40   ? 234  LYS A C   1 
ATOM   1705 O  O   . LYS A 1 324 ? 195.560 182.534 141.331 1.00 3.27   ? 234  LYS A O   1 
ATOM   1706 C  CB  . LYS A 1 324 ? 193.935 185.169 140.091 1.00 3.41   ? 234  LYS A CB  1 
ATOM   1707 C  CG  . LYS A 1 324 ? 193.876 184.155 138.970 1.00 3.28   ? 234  LYS A CG  1 
ATOM   1708 C  CD  . LYS A 1 324 ? 193.279 184.779 137.714 1.00 3.07   ? 234  LYS A CD  1 
ATOM   1709 C  CE  . LYS A 1 324 ? 193.350 183.831 136.524 1.00 2.97   ? 234  LYS A CE  1 
ATOM   1710 N  NZ  . LYS A 1 324 ? 192.404 182.689 136.661 1.00 2.79   ? 234  LYS A NZ  1 
ATOM   1711 N  N   . PRO A 1 325 ? 196.885 184.333 141.221 1.00 3.41   ? 235  PRO A N   1 
ATOM   1712 C  CA  . PRO A 1 325 ? 198.140 183.610 141.073 1.00 3.43   ? 235  PRO A CA  1 
ATOM   1713 C  C   . PRO A 1 325 ? 198.373 182.589 142.191 1.00 3.51   ? 235  PRO A C   1 
ATOM   1714 O  O   . PRO A 1 325 ? 199.051 181.585 141.987 1.00 3.54   ? 235  PRO A O   1 
ATOM   1715 C  CB  . PRO A 1 325 ? 199.180 184.731 141.116 1.00 3.51   ? 235  PRO A CB  1 
ATOM   1716 C  CG  . PRO A 1 325 ? 198.431 185.955 140.654 1.00 3.44   ? 235  PRO A CG  1 
ATOM   1717 C  CD  . PRO A 1 325 ? 197.042 185.789 141.226 1.00 3.50   ? 235  PRO A CD  1 
ATOM   1718 N  N   . LEU A 1 326 ? 197.805 182.844 143.370 1.00 3.46   ? 236  LEU A N   1 
ATOM   1719 C  CA  . LEU A 1 326 ? 197.926 181.920 144.490 1.00 3.60   ? 236  LEU A CA  1 
ATOM   1720 C  C   . LEU A 1 326 ? 196.938 180.783 144.324 1.00 3.46   ? 236  LEU A C   1 
ATOM   1721 O  O   . LEU A 1 326 ? 197.258 179.618 144.562 1.00 3.34   ? 236  LEU A O   1 
ATOM   1722 C  CB  . LEU A 1 326 ? 197.672 182.653 145.818 1.00 3.62   ? 236  LEU A CB  1 
ATOM   1723 C  CG  . LEU A 1 326 ? 197.666 181.785 147.106 1.00 3.68   ? 236  LEU A CG  1 
ATOM   1724 C  CD1 . LEU A 1 326 ? 198.999 181.088 147.274 1.00 4.32   ? 236  LEU A CD1 1 
ATOM   1725 C  CD2 . LEU A 1 326 ? 197.375 182.676 148.305 1.00 4.05   ? 236  LEU A CD2 1 
ATOM   1726 N  N   . TYR A 1 327 ? 195.730 181.136 143.905 1.00 3.27   ? 237  TYR A N   1 
ATOM   1727 C  CA  . TYR A 1 327 ? 194.676 180.158 143.692 1.00 3.25   ? 237  TYR A CA  1 
ATOM   1728 C  C   . TYR A 1 327 ? 195.067 179.146 142.626 1.00 3.27   ? 237  TYR A C   1 
ATOM   1729 O  O   . TYR A 1 327 ? 194.785 177.959 142.761 1.00 3.03   ? 237  TYR A O   1 
ATOM   1730 C  CB  . TYR A 1 327 ? 193.362 180.839 143.331 1.00 3.15   ? 237  TYR A CB  1 
ATOM   1731 C  CG  . TYR A 1 327 ? 192.255 179.864 143.059 1.00 2.97   ? 237  TYR A CG  1 
ATOM   1732 C  CD1 . TYR A 1 327 ? 191.711 179.123 144.096 1.00 3.05   ? 237  TYR A CD1 1 
ATOM   1733 C  CD2 . TYR A 1 327 ? 191.782 179.709 141.774 1.00 2.87   ? 237  TYR A CD2 1 
ATOM   1734 C  CE1 . TYR A 1 327 ? 190.696 178.231 143.837 1.00 2.98   ? 237  TYR A CE1 1 
ATOM   1735 C  CE2 . TYR A 1 327 ? 190.769 178.824 141.520 1.00 2.80   ? 237  TYR A CE2 1 
ATOM   1736 C  CZ  . TYR A 1 327 ? 190.226 178.087 142.544 1.00 2.86   ? 237  TYR A CZ  1 
ATOM   1737 O  OH  . TYR A 1 327 ? 189.208 177.211 142.285 1.00 2.83   ? 237  TYR A OH  1 
ATOM   1738 N  N   . GLU A 1 328 ? 195.702 179.619 141.556 1.00 3.19   ? 238  GLU A N   1 
ATOM   1739 C  CA  . GLU A 1 328 ? 196.115 178.737 140.470 1.00 3.19   ? 238  GLU A CA  1 
ATOM   1740 C  C   . GLU A 1 328 ? 197.118 177.682 140.935 1.00 3.26   ? 238  GLU A C   1 
ATOM   1741 O  O   . GLU A 1 328 ? 197.122 176.559 140.428 1.00 3.13   ? 238  GLU A O   1 
ATOM   1742 C  CB  . GLU A 1 328 ? 196.706 179.535 139.310 1.00 3.12   ? 238  GLU A CB  1 
ATOM   1743 C  CG  . GLU A 1 328 ? 195.687 180.294 138.484 1.00 3.03   ? 238  GLU A CG  1 
ATOM   1744 C  CD  . GLU A 1 328 ? 196.298 180.993 137.308 1.00 3.13   ? 238  GLU A CD  1 
ATOM   1745 O  OE1 . GLU A 1 328 ? 197.462 181.307 137.365 1.00 3.49   ? 238  GLU A OE1 1 
ATOM   1746 O  OE2 . GLU A 1 328 ? 195.605 181.193 136.337 1.00 3.15   ? 238  GLU A OE2 1 
ATOM   1747 N  N   . GLN A 1 329 ? 197.979 178.039 141.885 1.00 3.22   ? 239  GLN A N   1 
ATOM   1748 C  CA  . GLN A 1 329 ? 198.953 177.087 142.404 1.00 3.47   ? 239  GLN A CA  1 
ATOM   1749 C  C   . GLN A 1 329 ? 198.268 176.035 143.266 1.00 3.53   ? 239  GLN A C   1 
ATOM   1750 O  O   . GLN A 1 329 ? 198.604 174.851 143.203 1.00 3.43   ? 239  GLN A O   1 
ATOM   1751 C  CB  . GLN A 1 329 ? 200.025 177.802 143.230 1.00 3.67   ? 239  GLN A CB  1 
ATOM   1752 C  CG  . GLN A 1 329 ? 200.961 178.688 142.436 1.00 3.94   ? 239  GLN A CG  1 
ATOM   1753 C  CD  . GLN A 1 329 ? 201.903 177.915 141.549 1.00 4.11   ? 239  GLN A CD  1 
ATOM   1754 O  OE1 . GLN A 1 329 ? 202.077 176.703 141.700 1.00 4.21   ? 239  GLN A OE1 1 
ATOM   1755 N  NE2 . GLN A 1 329 ? 202.533 178.614 140.616 1.00 4.20   ? 239  GLN A NE2 1 
ATOM   1756 N  N   . LEU A 1 330 ? 197.288 176.468 144.053 1.00 3.29   ? 240  LEU A N   1 
ATOM   1757 C  CA  . LEU A 1 330 ? 196.525 175.557 144.896 1.00 3.31   ? 240  LEU A CA  1 
ATOM   1758 C  C   . LEU A 1 330 ? 195.668 174.642 144.033 1.00 3.19   ? 240  LEU A C   1 
ATOM   1759 O  O   . LEU A 1 330 ? 195.545 173.449 144.304 1.00 3.07   ? 240  LEU A O   1 
ATOM   1760 C  CB  . LEU A 1 330 ? 195.633 176.349 145.866 1.00 3.26   ? 240  LEU A CB  1 
ATOM   1761 C  CG  . LEU A 1 330 ? 194.811 175.526 146.896 1.00 3.29   ? 240  LEU A CG  1 
ATOM   1762 C  CD1 . LEU A 1 330 ? 195.751 174.749 147.816 1.00 3.46   ? 240  LEU A CD1 1 
ATOM   1763 C  CD2 . LEU A 1 330 ? 193.920 176.475 147.699 1.00 3.50   ? 240  LEU A CD2 1 
ATOM   1764 N  N   . HIS A 1 331 ? 195.086 175.214 142.986 1.00 2.93   ? 241  HIS A N   1 
ATOM   1765 C  CA  . HIS A 1 331 ? 194.226 174.486 142.065 1.00 3.03   ? 241  HIS A CA  1 
ATOM   1766 C  C   . HIS A 1 331 ? 194.995 173.369 141.371 1.00 3.03   ? 241  HIS A C   1 
ATOM   1767 O  O   . HIS A 1 331 ? 194.539 172.226 141.332 1.00 2.87   ? 241  HIS A O   1 
ATOM   1768 C  CB  . HIS A 1 331 ? 193.637 175.459 141.030 1.00 2.89   ? 241  HIS A CB  1 
ATOM   1769 C  CG  . HIS A 1 331 ? 192.705 174.841 140.032 1.00 2.74   ? 241  HIS A CG  1 
ATOM   1770 N  ND1 . HIS A 1 331 ? 193.144 174.294 138.847 1.00 2.74   ? 241  HIS A ND1 1 
ATOM   1771 C  CD2 . HIS A 1 331 ? 191.362 174.706 140.032 1.00 2.69   ? 241  HIS A CD2 1 
ATOM   1772 C  CE1 . HIS A 1 331 ? 192.110 173.831 138.171 1.00 2.72   ? 241  HIS A CE1 1 
ATOM   1773 N  NE2 . HIS A 1 331 ? 191.020 174.074 138.867 1.00 2.60   ? 241  HIS A NE2 1 
ATOM   1774 N  N   . ALA A 1 332 ? 196.176 173.691 140.846 1.00 2.98   ? 242  ALA A N   1 
ATOM   1775 C  CA  . ALA A 1 332 ? 196.998 172.704 140.155 1.00 3.14   ? 242  ALA A CA  1 
ATOM   1776 C  C   . ALA A 1 332 ? 197.416 171.576 141.088 1.00 3.14   ? 242  ALA A C   1 
ATOM   1777 O  O   . ALA A 1 332 ? 197.420 170.408 140.698 1.00 2.91   ? 242  ALA A O   1 
ATOM   1778 C  CB  . ALA A 1 332 ? 198.225 173.374 139.567 1.00 3.38   ? 242  ALA A CB  1 
ATOM   1779 N  N   . TYR A 1 333 ? 197.748 171.924 142.327 1.00 3.07   ? 243  TYR A N   1 
ATOM   1780 C  CA  . TYR A 1 333 ? 198.153 170.940 143.321 1.00 3.29   ? 243  TYR A CA  1 
ATOM   1781 C  C   . TYR A 1 333 ? 197.026 169.967 143.635 1.00 3.21   ? 243  TYR A C   1 
ATOM   1782 O  O   . TYR A 1 333 ? 197.223 168.751 143.644 1.00 3.16   ? 243  TYR A O   1 
ATOM   1783 C  CB  . TYR A 1 333 ? 198.624 171.644 144.590 1.00 3.43   ? 243  TYR A CB  1 
ATOM   1784 C  CG  . TYR A 1 333 ? 199.045 170.713 145.694 1.00 3.58   ? 243  TYR A CG  1 
ATOM   1785 C  CD1 . TYR A 1 333 ? 200.243 170.036 145.598 1.00 3.98   ? 243  TYR A CD1 1 
ATOM   1786 C  CD2 . TYR A 1 333 ? 198.241 170.543 146.809 1.00 3.79   ? 243  TYR A CD2 1 
ATOM   1787 C  CE1 . TYR A 1 333 ? 200.635 169.190 146.606 1.00 4.23   ? 243  TYR A CE1 1 
ATOM   1788 C  CE2 . TYR A 1 333 ? 198.639 169.695 147.816 1.00 4.29   ? 243  TYR A CE2 1 
ATOM   1789 C  CZ  . TYR A 1 333 ? 199.832 169.023 147.713 1.00 4.61   ? 243  TYR A CZ  1 
ATOM   1790 O  OH  . TYR A 1 333 ? 200.233 168.177 148.710 1.00 5.34   ? 243  TYR A OH  1 
ATOM   1791 N  N   . VAL A 1 334 ? 195.839 170.507 143.882 1.00 3.03   ? 244  VAL A N   1 
ATOM   1792 C  CA  . VAL A 1 334 ? 194.680 169.683 144.183 1.00 3.09   ? 244  VAL A CA  1 
ATOM   1793 C  C   . VAL A 1 334 ? 194.332 168.786 143.004 1.00 3.07   ? 244  VAL A C   1 
ATOM   1794 O  O   . VAL A 1 334 ? 194.008 167.615 143.189 1.00 2.92   ? 244  VAL A O   1 
ATOM   1795 C  CB  . VAL A 1 334 ? 193.477 170.564 144.567 1.00 2.97   ? 244  VAL A CB  1 
ATOM   1796 C  CG1 . VAL A 1 334 ? 192.210 169.728 144.659 1.00 2.95   ? 244  VAL A CG1 1 
ATOM   1797 C  CG2 . VAL A 1 334 ? 193.759 171.234 145.904 1.00 3.15   ? 244  VAL A CG2 1 
ATOM   1798 N  N   . ARG A 1 335 ? 194.404 169.331 141.794 1.00 2.88   ? 245  ARG A N   1 
ATOM   1799 C  CA  . ARG A 1 335 ? 194.118 168.554 140.595 1.00 2.91   ? 245  ARG A CA  1 
ATOM   1800 C  C   . ARG A 1 335 ? 195.024 167.337 140.494 1.00 2.96   ? 245  ARG A C   1 
ATOM   1801 O  O   . ARG A 1 335 ? 194.559 166.232 140.218 1.00 2.89   ? 245  ARG A O   1 
ATOM   1802 C  CB  . ARG A 1 335 ? 194.286 169.418 139.353 1.00 2.77   ? 245  ARG A CB  1 
ATOM   1803 C  CG  . ARG A 1 335 ? 193.995 168.725 138.030 1.00 2.82   ? 245  ARG A CG  1 
ATOM   1804 C  CD  . ARG A 1 335 ? 193.994 169.687 136.902 1.00 2.78   ? 245  ARG A CD  1 
ATOM   1805 N  NE  . ARG A 1 335 ? 195.274 170.359 136.766 1.00 2.73   ? 245  ARG A NE  1 
ATOM   1806 C  CZ  . ARG A 1 335 ? 195.479 171.502 136.080 1.00 2.81   ? 245  ARG A CZ  1 
ATOM   1807 N  NH1 . ARG A 1 335 ? 194.490 172.097 135.457 1.00 2.77   ? 245  ARG A NH1 1 
ATOM   1808 N  NH2 . ARG A 1 335 ? 196.684 172.033 136.030 1.00 2.99   ? 245  ARG A NH2 1 
ATOM   1809 N  N   . ALA A 1 336 ? 196.314 167.535 140.742 1.00 2.85   ? 246  ALA A N   1 
ATOM   1810 C  CA  . ALA A 1 336 ? 197.281 166.448 140.669 1.00 2.95   ? 246  ALA A CA  1 
ATOM   1811 C  C   . ALA A 1 336 ? 196.957 165.339 141.663 1.00 3.02   ? 246  ALA A C   1 
ATOM   1812 O  O   . ALA A 1 336 ? 197.174 164.161 141.377 1.00 2.99   ? 246  ALA A O   1 
ATOM   1813 C  CB  . ALA A 1 336 ? 198.679 166.982 140.926 1.00 2.79   ? 246  ALA A CB  1 
ATOM   1814 N  N   . LYS A 1 337 ? 196.451 165.713 142.835 1.00 2.94   ? 247  LYS A N   1 
ATOM   1815 C  CA  . LYS A 1 337 ? 196.114 164.739 143.868 1.00 3.14   ? 247  LYS A CA  1 
ATOM   1816 C  C   . LYS A 1 337 ? 194.813 164.002 143.557 1.00 3.07   ? 247  LYS A C   1 
ATOM   1817 O  O   . LYS A 1 337 ? 194.711 162.791 143.761 1.00 3.02   ? 247  LYS A O   1 
ATOM   1818 C  CB  . LYS A 1 337 ? 196.007 165.431 145.226 1.00 3.43   ? 247  LYS A CB  1 
ATOM   1819 C  CG  . LYS A 1 337 ? 197.325 165.970 145.774 1.00 3.81   ? 247  LYS A CG  1 
ATOM   1820 C  CD  . LYS A 1 337 ? 198.235 164.844 146.234 1.00 3.92   ? 247  LYS A CD  1 
ATOM   1821 C  CE  . LYS A 1 337 ? 199.446 165.378 146.971 1.00 4.35   ? 247  LYS A CE  1 
ATOM   1822 N  NZ  . LYS A 1 337 ? 200.350 164.284 147.417 1.00 4.51   ? 247  LYS A NZ  1 
ATOM   1823 N  N   . LEU A 1 338 ? 193.825 164.724 143.041 1.00 2.91   ? 248  LEU A N   1 
ATOM   1824 C  CA  . LEU A 1 338 ? 192.546 164.111 142.716 1.00 3.02   ? 248  LEU A CA  1 
ATOM   1825 C  C   . LEU A 1 338 ? 192.683 163.116 141.575 1.00 3.14   ? 248  LEU A C   1 
ATOM   1826 O  O   . LEU A 1 338 ? 191.951 162.131 141.520 1.00 2.97   ? 248  LEU A O   1 
ATOM   1827 C  CB  . LEU A 1 338 ? 191.500 165.173 142.366 1.00 2.93   ? 248  LEU A CB  1 
ATOM   1828 C  CG  . LEU A 1 338 ? 190.991 166.043 143.528 1.00 2.96   ? 248  LEU A CG  1 
ATOM   1829 C  CD1 . LEU A 1 338 ? 190.151 167.173 142.970 1.00 2.94   ? 248  LEU A CD1 1 
ATOM   1830 C  CD2 . LEU A 1 338 ? 190.161 165.197 144.478 1.00 3.06   ? 248  LEU A CD2 1 
ATOM   1831 N  N   . MET A 1 339 ? 193.650 163.339 140.690 1.00 2.92   ? 249  MET A N   1 
ATOM   1832 C  CA  . MET A 1 339 ? 193.895 162.410 139.593 1.00 3.03   ? 249  MET A CA  1 
ATOM   1833 C  C   . MET A 1 339 ? 194.295 161.025 140.086 1.00 3.13   ? 249  MET A C   1 
ATOM   1834 O  O   . MET A 1 339 ? 194.168 160.045 139.354 1.00 3.12   ? 249  MET A O   1 
ATOM   1835 C  CB  . MET A 1 339 ? 194.963 162.947 138.651 1.00 2.94   ? 249  MET A CB  1 
ATOM   1836 C  CG  . MET A 1 339 ? 194.500 164.074 137.751 1.00 2.96   ? 249  MET A CG  1 
ATOM   1837 S  SD  . MET A 1 339 ? 195.804 164.688 136.691 1.00 2.98   ? 249  MET A SD  1 
ATOM   1838 C  CE  . MET A 1 339 ? 195.899 163.365 135.488 1.00 2.90   ? 249  MET A CE  1 
ATOM   1839 N  N   . ASN A 1 340 ? 194.808 160.942 141.309 1.00 2.98   ? 250  ASN A N   1 
ATOM   1840 C  CA  . ASN A 1 340 ? 195.182 159.654 141.875 1.00 3.07   ? 250  ASN A CA  1 
ATOM   1841 C  C   . ASN A 1 340 ? 193.990 159.036 142.587 1.00 3.15   ? 250  ASN A C   1 
ATOM   1842 O  O   . ASN A 1 340 ? 193.808 157.819 142.578 1.00 3.12   ? 250  ASN A O   1 
ATOM   1843 C  CB  . ASN A 1 340 ? 196.358 159.804 142.817 1.00 3.08   ? 250  ASN A CB  1 
ATOM   1844 C  CG  . ASN A 1 340 ? 197.628 160.133 142.098 1.00 3.20   ? 250  ASN A CG  1 
ATOM   1845 O  OD1 . ASN A 1 340 ? 197.835 159.723 140.949 1.00 3.17   ? 250  ASN A OD1 1 
ATOM   1846 N  ND2 . ASN A 1 340 ? 198.487 160.870 142.748 1.00 3.17   ? 250  ASN A ND2 1 
ATOM   1847 N  N   . ALA A 1 341 ? 193.174 159.890 143.200 1.00 3.08   ? 251  ALA A N   1 
ATOM   1848 C  CA  . ALA A 1 341 ? 191.969 159.453 143.894 1.00 3.12   ? 251  ALA A CA  1 
ATOM   1849 C  C   . ALA A 1 341 ? 190.922 158.946 142.907 1.00 3.15   ? 251  ALA A C   1 
ATOM   1850 O  O   . ALA A 1 341 ? 190.184 158.006 143.201 1.00 3.23   ? 251  ALA A O   1 
ATOM   1851 C  CB  . ALA A 1 341 ? 191.398 160.592 144.723 1.00 3.22   ? 251  ALA A CB  1 
ATOM   1852 N  N   . TYR A 1 342 ? 190.862 159.572 141.733 1.00 3.06   ? 252  TYR A N   1 
ATOM   1853 C  CA  . TYR A 1 342 ? 189.887 159.214 140.707 1.00 3.24   ? 252  TYR A CA  1 
ATOM   1854 C  C   . TYR A 1 342 ? 190.539 159.027 139.335 1.00 3.32   ? 252  TYR A C   1 
ATOM   1855 O  O   . TYR A 1 342 ? 190.408 159.894 138.469 1.00 3.24   ? 252  TYR A O   1 
ATOM   1856 C  CB  . TYR A 1 342 ? 188.809 160.297 140.611 1.00 3.16   ? 252  TYR A CB  1 
ATOM   1857 C  CG  . TYR A 1 342 ? 188.122 160.603 141.916 1.00 3.12   ? 252  TYR A CG  1 
ATOM   1858 C  CD1 . TYR A 1 342 ? 187.080 159.810 142.358 1.00 3.28   ? 252  TYR A CD1 1 
ATOM   1859 C  CD2 . TYR A 1 342 ? 188.538 161.683 142.671 1.00 3.09   ? 252  TYR A CD2 1 
ATOM   1860 C  CE1 . TYR A 1 342 ? 186.457 160.096 143.552 1.00 3.35   ? 252  TYR A CE1 1 
ATOM   1861 C  CE2 . TYR A 1 342 ? 187.916 161.968 143.865 1.00 3.14   ? 252  TYR A CE2 1 
ATOM   1862 C  CZ  . TYR A 1 342 ? 186.881 161.179 144.305 1.00 3.22   ? 252  TYR A CZ  1 
ATOM   1863 O  OH  . TYR A 1 342 ? 186.262 161.466 145.497 1.00 3.47   ? 252  TYR A OH  1 
ATOM   1864 N  N   . PRO A 1 343 ? 191.239 157.912 139.112 1.00 3.26   ? 253  PRO A N   1 
ATOM   1865 C  CA  . PRO A 1 343 ? 192.025 157.617 137.931 1.00 3.31   ? 253  PRO A CA  1 
ATOM   1866 C  C   . PRO A 1 343 ? 191.182 157.699 136.666 1.00 3.40   ? 253  PRO A C   1 
ATOM   1867 O  O   . PRO A 1 343 ? 190.069 157.179 136.619 1.00 3.48   ? 253  PRO A O   1 
ATOM   1868 C  CB  . PRO A 1 343 ? 192.479 156.175 138.194 1.00 3.30   ? 253  PRO A CB  1 
ATOM   1869 C  CG  . PRO A 1 343 ? 192.442 156.033 139.694 1.00 3.26   ? 253  PRO A CG  1 
ATOM   1870 C  CD  . PRO A 1 343 ? 191.256 156.857 140.125 1.00 3.26   ? 253  PRO A CD  1 
ATOM   1871 N  N   . SER A 1 344 ? 191.735 158.337 135.640 1.00 3.41   ? 254  SER A N   1 
ATOM   1872 C  CA  . SER A 1 344 ? 191.110 158.459 134.322 1.00 3.50   ? 254  SER A CA  1 
ATOM   1873 C  C   . SER A 1 344 ? 189.834 159.301 134.311 1.00 3.56   ? 254  SER A C   1 
ATOM   1874 O  O   . SER A 1 344 ? 189.147 159.366 133.292 1.00 3.72   ? 254  SER A O   1 
ATOM   1875 C  CB  . SER A 1 344 ? 190.809 157.085 133.756 1.00 3.47   ? 254  SER A CB  1 
ATOM   1876 N  N   . ARG A 1 345 ? 189.534 159.979 135.415 1.00 3.52   ? 255  ARG A N   1 
ATOM   1877 C  CA  . ARG A 1 345 ? 188.356 160.841 135.462 1.00 3.54   ? 255  ARG A CA  1 
ATOM   1878 C  C   . ARG A 1 345 ? 188.703 162.307 135.272 1.00 3.54   ? 255  ARG A C   1 
ATOM   1879 O  O   . ARG A 1 345 ? 187.856 163.106 134.876 1.00 3.56   ? 255  ARG A O   1 
ATOM   1880 C  CB  . ARG A 1 345 ? 187.624 160.683 136.782 1.00 3.60   ? 255  ARG A CB  1 
ATOM   1881 C  CG  . ARG A 1 345 ? 187.051 159.308 137.040 1.00 3.85   ? 255  ARG A CG  1 
ATOM   1882 C  CD  . ARG A 1 345 ? 185.921 159.005 136.136 1.00 4.19   ? 255  ARG A CD  1 
ATOM   1883 N  NE  . ARG A 1 345 ? 185.259 157.780 136.513 1.00 4.67   ? 255  ARG A NE  1 
ATOM   1884 C  CZ  . ARG A 1 345 ? 184.112 157.326 135.979 1.00 5.27   ? 255  ARG A CZ  1 
ATOM   1885 N  NH1 . ARG A 1 345 ? 183.495 158.013 135.043 1.00 5.18   ? 255  ARG A NH1 1 
ATOM   1886 N  NH2 . ARG A 1 345 ? 183.609 156.183 136.405 1.00 7.46   ? 255  ARG A NH2 1 
ATOM   1887 N  N   . ILE A 1 346 ? 189.932 162.671 135.604 1.00 3.41   ? 256  ILE A N   1 
ATOM   1888 C  CA  . ILE A 1 346 ? 190.336 164.066 135.587 1.00 3.43   ? 256  ILE A CA  1 
ATOM   1889 C  C   . ILE A 1 346 ? 191.470 164.311 134.606 1.00 3.40   ? 256  ILE A C   1 
ATOM   1890 O  O   . ILE A 1 346 ? 192.474 163.600 134.610 1.00 3.22   ? 256  ILE A O   1 
ATOM   1891 C  CB  . ILE A 1 346 ? 190.736 164.517 137.003 1.00 3.21   ? 256  ILE A CB  1 
ATOM   1892 C  CG1 . ILE A 1 346 ? 189.524 164.375 137.936 1.00 3.16   ? 256  ILE A CG1 1 
ATOM   1893 C  CG2 . ILE A 1 346 ? 191.256 165.953 136.988 1.00 3.19   ? 256  ILE A CG2 1 
ATOM   1894 C  CD1 . ILE A 1 346 ? 189.851 164.490 139.395 1.00 3.01   ? 256  ILE A CD1 1 
ATOM   1895 N  N   . SER A 1 347 ? 191.293 165.320 133.763 1.00 3.52   ? 257  SER A N   1 
ATOM   1896 C  CA  . SER A 1 347 ? 192.301 165.713 132.789 1.00 3.37   ? 257  SER A CA  1 
ATOM   1897 C  C   . SER A 1 347 ? 193.319 166.662 133.424 1.00 3.02   ? 257  SER A C   1 
ATOM   1898 O  O   . SER A 1 347 ? 192.929 167.634 134.066 1.00 2.94   ? 257  SER A O   1 
ATOM   1899 C  CB  . SER A 1 347 ? 191.630 166.378 131.603 1.00 3.66   ? 257  SER A CB  1 
ATOM   1900 O  OG  . SER A 1 347 ? 192.567 166.952 130.741 1.00 3.41   ? 257  SER A OG  1 
ATOM   1901 N  N   . PRO A 1 348 ? 194.620 166.418 133.223 1.00 2.98   ? 258  PRO A N   1 
ATOM   1902 C  CA  . PRO A 1 348 ? 195.748 167.100 133.838 1.00 2.86   ? 258  PRO A CA  1 
ATOM   1903 C  C   . PRO A 1 348 ? 195.842 168.582 133.496 1.00 2.84   ? 258  PRO A C   1 
ATOM   1904 O  O   . PRO A 1 348 ? 196.541 169.329 134.178 1.00 2.79   ? 258  PRO A O   1 
ATOM   1905 C  CB  . PRO A 1 348 ? 196.949 166.332 133.271 1.00 2.79   ? 258  PRO A CB  1 
ATOM   1906 C  CG  . PRO A 1 348 ? 196.446 165.699 131.999 1.00 2.86   ? 258  PRO A CG  1 
ATOM   1907 C  CD  . PRO A 1 348 ? 194.999 165.377 132.268 1.00 3.02   ? 258  PRO A CD  1 
ATOM   1908 N  N   . THR A 1 349 ? 195.170 169.004 132.433 1.00 2.83   ? 259  THR A N   1 
ATOM   1909 C  CA  . THR A 1 349 ? 195.222 170.400 132.018 1.00 2.80   ? 259  THR A CA  1 
ATOM   1910 C  C   . THR A 1 349 ? 193.845 171.055 132.027 1.00 2.84   ? 259  THR A C   1 
ATOM   1911 O  O   . THR A 1 349 ? 193.663 172.128 131.447 1.00 2.79   ? 259  THR A O   1 
ATOM   1912 C  CB  . THR A 1 349 ? 195.824 170.528 130.608 1.00 2.65   ? 259  THR A CB  1 
ATOM   1913 O  OG1 . THR A 1 349 ? 194.986 169.849 129.669 1.00 2.75   ? 259  THR A OG1 1 
ATOM   1914 C  CG2 . THR A 1 349 ? 197.211 169.902 130.578 1.00 2.69   ? 259  THR A CG2 1 
ATOM   1915 N  N   . GLY A 1 350 ? 192.860 170.390 132.623 1.00 2.83   ? 260  GLY A N   1 
ATOM   1916 C  CA  . GLY A 1 350 ? 191.491 170.890 132.570 1.00 2.95   ? 260  GLY A CA  1 
ATOM   1917 C  C   . GLY A 1 350 ? 190.947 171.316 133.927 1.00 2.80   ? 260  GLY A C   1 
ATOM   1918 O  O   . GLY A 1 350 ? 191.677 171.392 134.916 1.00 2.60   ? 260  GLY A O   1 
ATOM   1919 N  N   . CYS A 1 351 ? 189.646 171.585 133.955 1.00 2.81   ? 261  CYS A N   1 
ATOM   1920 C  CA  . CYS A 1 351 ? 188.935 172.003 135.156 1.00 2.67   ? 261  CYS A CA  1 
ATOM   1921 C  C   . CYS A 1 351 ? 188.604 170.814 136.045 1.00 2.79   ? 261  CYS A C   1 
ATOM   1922 O  O   . CYS A 1 351 ? 188.582 169.673 135.587 1.00 2.78   ? 261  CYS A O   1 
ATOM   1923 C  CB  . CYS A 1 351 ? 187.633 172.705 134.780 1.00 2.59   ? 261  CYS A CB  1 
ATOM   1924 S  SG  . CYS A 1 351 ? 187.840 174.289 133.953 1.00 2.78   ? 261  CYS A SG  1 
ATOM   1925 N  N   . LEU A 1 352 ? 188.332 171.086 137.315 1.00 2.60   ? 262  LEU A N   1 
ATOM   1926 C  CA  . LEU A 1 352 ? 187.923 170.041 138.242 1.00 2.66   ? 262  LEU A CA  1 
ATOM   1927 C  C   . LEU A 1 352 ? 186.420 169.812 138.129 1.00 2.79   ? 262  LEU A C   1 
ATOM   1928 O  O   . LEU A 1 352 ? 185.667 170.778 138.038 1.00 2.65   ? 262  LEU A O   1 
ATOM   1929 C  CB  . LEU A 1 352 ? 188.267 170.447 139.680 1.00 2.63   ? 262  LEU A CB  1 
ATOM   1930 C  CG  . LEU A 1 352 ? 189.749 170.713 139.973 1.00 2.60   ? 262  LEU A CG  1 
ATOM   1931 C  CD1 . LEU A 1 352 ? 189.903 171.202 141.409 1.00 2.70   ? 262  LEU A CD1 1 
ATOM   1932 C  CD2 . LEU A 1 352 ? 190.544 169.449 139.749 1.00 2.64   ? 262  LEU A CD2 1 
ATOM   1933 N  N   . PRO A 1 353 ? 185.961 168.557 138.112 1.00 2.72   ? 263  PRO A N   1 
ATOM   1934 C  CA  . PRO A 1 353 ? 184.568 168.159 138.189 1.00 2.79   ? 263  PRO A CA  1 
ATOM   1935 C  C   . PRO A 1 353 ? 183.902 168.732 139.433 1.00 2.91   ? 263  PRO A C   1 
ATOM   1936 O  O   . PRO A 1 353 ? 184.421 168.614 140.542 1.00 2.83   ? 263  PRO A O   1 
ATOM   1937 C  CB  . PRO A 1 353 ? 184.671 166.634 138.235 1.00 2.86   ? 263  PRO A CB  1 
ATOM   1938 C  CG  . PRO A 1 353 ? 185.962 166.324 137.512 1.00 2.97   ? 263  PRO A CG  1 
ATOM   1939 C  CD  . PRO A 1 353 ? 186.896 167.449 137.891 1.00 2.84   ? 263  PRO A CD  1 
ATOM   1940 N  N   . ALA A 1 354 ? 182.735 169.331 139.244 1.00 2.84   ? 264  ALA A N   1 
ATOM   1941 C  CA  . ALA A 1 354 ? 182.024 170.025 140.314 1.00 2.88   ? 264  ALA A CA  1 
ATOM   1942 C  C   . ALA A 1 354 ? 181.661 169.128 141.493 1.00 2.91   ? 264  ALA A C   1 
ATOM   1943 O  O   . ALA A 1 354 ? 181.589 169.601 142.626 1.00 2.89   ? 264  ALA A O   1 
ATOM   1944 C  CB  . ALA A 1 354 ? 180.760 170.661 139.761 1.00 2.80   ? 264  ALA A CB  1 
ATOM   1945 N  N   . HIS A 1 355 ? 181.393 167.853 141.241 1.00 2.93   ? 265  HIS A N   1 
ATOM   1946 C  CA  . HIS A 1 355 ? 180.897 166.979 142.299 1.00 3.00   ? 265  HIS A CA  1 
ATOM   1947 C  C   . HIS A 1 355 ? 181.994 166.378 143.174 1.00 3.11   ? 265  HIS A C   1 
ATOM   1948 O  O   . HIS A 1 355 ? 181.692 165.669 144.131 1.00 3.08   ? 265  HIS A O   1 
ATOM   1949 C  CB  . HIS A 1 355 ? 180.028 165.861 141.712 1.00 3.08   ? 265  HIS A CB  1 
ATOM   1950 C  CG  . HIS A 1 355 ? 180.752 164.898 140.839 1.00 3.17   ? 265  HIS A CG  1 
ATOM   1951 N  ND1 . HIS A 1 355 ? 181.345 165.269 139.662 1.00 3.18   ? 265  HIS A ND1 1 
ATOM   1952 C  CD2 . HIS A 1 355 ? 180.954 163.569 140.958 1.00 3.39   ? 265  HIS A CD2 1 
ATOM   1953 C  CE1 . HIS A 1 355 ? 181.888 164.210 139.097 1.00 3.32   ? 265  HIS A CE1 1 
ATOM   1954 N  NE2 . HIS A 1 355 ? 181.661 163.169 139.863 1.00 3.58   ? 265  HIS A NE2 1 
ATOM   1955 N  N   . LEU A 1 356 ? 183.258 166.640 142.850 1.00 2.98   ? 266  LEU A N   1 
ATOM   1956 C  CA  . LEU A 1 356 ? 184.374 166.034 143.578 1.00 3.06   ? 266  LEU A CA  1 
ATOM   1957 C  C   . LEU A 1 356 ? 185.127 167.018 144.477 1.00 3.13   ? 266  LEU A C   1 
ATOM   1958 O  O   . LEU A 1 356 ? 186.289 166.787 144.807 1.00 3.11   ? 266  LEU A O   1 
ATOM   1959 C  CB  . LEU A 1 356 ? 185.376 165.426 142.588 1.00 3.01   ? 266  LEU A CB  1 
ATOM   1960 C  CG  . LEU A 1 356 ? 184.838 164.355 141.628 1.00 3.09   ? 266  LEU A CG  1 
ATOM   1961 C  CD1 . LEU A 1 356 ? 185.966 163.903 140.724 1.00 3.00   ? 266  LEU A CD1 1 
ATOM   1962 C  CD2 . LEU A 1 356 ? 184.267 163.186 142.411 1.00 3.20   ? 266  LEU A CD2 1 
ATOM   1963 N  N   . LEU A 1 357 ? 184.494 168.129 144.841 1.00 3.05   ? 267  LEU A N   1 
ATOM   1964 C  CA  . LEU A 1 357 ? 185.198 169.207 145.536 1.00 3.17   ? 267  LEU A CA  1 
ATOM   1965 C  C   . LEU A 1 357 ? 185.075 169.214 147.065 1.00 3.28   ? 267  LEU A C   1 
ATOM   1966 O  O   . LEU A 1 357 ? 185.546 170.145 147.711 1.00 3.27   ? 267  LEU A O   1 
ATOM   1967 C  CB  . LEU A 1 357 ? 184.723 170.553 144.987 1.00 3.04   ? 267  LEU A CB  1 
ATOM   1968 C  CG  . LEU A 1 357 ? 184.998 170.800 143.491 1.00 2.97   ? 267  LEU A CG  1 
ATOM   1969 C  CD1 . LEU A 1 357 ? 184.308 172.074 143.065 1.00 2.94   ? 267  LEU A CD1 1 
ATOM   1970 C  CD2 . LEU A 1 357 ? 186.502 170.902 143.247 1.00 3.00   ? 267  LEU A CD2 1 
ATOM   1971 N  N   . GLY A 1 358 ? 184.478 168.182 147.648 1.00 3.30   ? 268  GLY A N   1 
ATOM   1972 C  CA  . GLY A 1 358 ? 184.437 168.078 149.109 1.00 3.45   ? 268  GLY A CA  1 
ATOM   1973 C  C   . GLY A 1 358 ? 183.086 168.409 149.750 1.00 3.59   ? 268  GLY A C   1 
ATOM   1974 O  O   . GLY A 1 358 ? 182.879 168.132 150.930 1.00 3.77   ? 268  GLY A O   1 
ATOM   1975 N  N   . ASP A 1 359 ? 182.176 169.017 148.999 1.00 3.39   ? 269  ASP A N   1 
ATOM   1976 C  CA  . ASP A 1 359 ? 180.845 169.300 149.532 1.00 3.43   ? 269  ASP A CA  1 
ATOM   1977 C  C   . ASP A 1 359 ? 179.832 169.477 148.406 1.00 3.34   ? 269  ASP A C   1 
ATOM   1978 O  O   . ASP A 1 359 ? 180.149 169.265 147.236 1.00 3.24   ? 269  ASP A O   1 
ATOM   1979 C  CB  . ASP A 1 359 ? 180.852 170.499 150.503 1.00 3.44   ? 269  ASP A CB  1 
ATOM   1980 C  CG  . ASP A 1 359 ? 181.175 171.869 149.880 1.00 3.32   ? 269  ASP A CG  1 
ATOM   1981 O  OD1 . ASP A 1 359 ? 180.546 172.239 148.913 1.00 3.14   ? 269  ASP A OD1 1 
ATOM   1982 O  OD2 . ASP A 1 359 ? 182.030 172.551 150.404 1.00 3.35   ? 269  ASP A OD2 1 
ATOM   1983 N  N   . MET A 1 360 ? 178.600 169.819 148.768 1.00 3.23   ? 270  MET A N   1 
ATOM   1984 C  CA  . MET A 1 360 ? 177.499 169.894 147.811 1.00 3.22   ? 270  MET A CA  1 
ATOM   1985 C  C   . MET A 1 360 ? 177.660 171.002 146.767 1.00 3.16   ? 270  MET A C   1 
ATOM   1986 O  O   . MET A 1 360 ? 177.075 170.919 145.688 1.00 2.98   ? 270  MET A O   1 
ATOM   1987 C  CB  . MET A 1 360 ? 176.176 170.059 148.562 1.00 3.15   ? 270  MET A CB  1 
ATOM   1988 C  CG  . MET A 1 360 ? 174.922 170.030 147.685 1.00 3.04   ? 270  MET A CG  1 
ATOM   1989 S  SD  . MET A 1 360 ? 174.641 168.447 146.878 1.00 3.19   ? 270  MET A SD  1 
ATOM   1990 C  CE  . MET A 1 360 ? 173.643 167.629 148.114 1.00 3.60   ? 270  MET A CE  1 
ATOM   1991 N  N   . TRP A 1 361 ? 178.398 172.063 147.094 1.00 3.07   ? 271  TRP A N   1 
ATOM   1992 C  CA  . TRP A 1 361 ? 178.480 173.210 146.189 1.00 3.09   ? 271  TRP A CA  1 
ATOM   1993 C  C   . TRP A 1 361 ? 179.902 173.542 145.751 1.00 3.13   ? 271  TRP A C   1 
ATOM   1994 O  O   . TRP A 1 361 ? 180.099 174.316 144.816 1.00 3.11   ? 271  TRP A O   1 
ATOM   1995 C  CB  . TRP A 1 361 ? 177.859 174.441 146.841 1.00 3.06   ? 271  TRP A CB  1 
ATOM   1996 C  CG  . TRP A 1 361 ? 176.463 174.219 147.310 1.00 3.03   ? 271  TRP A CG  1 
ATOM   1997 C  CD1 . TRP A 1 361 ? 175.317 174.371 146.595 1.00 2.95   ? 271  TRP A CD1 1 
ATOM   1998 C  CD2 . TRP A 1 361 ? 176.059 173.804 148.626 1.00 3.03   ? 271  TRP A CD2 1 
ATOM   1999 N  NE1 . TRP A 1 361 ? 174.235 174.074 147.379 1.00 2.91   ? 271  TRP A NE1 1 
ATOM   2000 C  CE2 . TRP A 1 361 ? 174.669 173.724 148.617 1.00 2.98   ? 271  TRP A CE2 1 
ATOM   2001 C  CE3 . TRP A 1 361 ? 176.755 173.499 149.797 1.00 3.08   ? 271  TRP A CE3 1 
ATOM   2002 C  CZ2 . TRP A 1 361 ? 173.952 173.346 149.733 1.00 3.05   ? 271  TRP A CZ2 1 
ATOM   2003 C  CZ3 . TRP A 1 361 ? 176.034 173.119 150.917 1.00 3.22   ? 271  TRP A CZ3 1 
ATOM   2004 C  CH2 . TRP A 1 361 ? 174.668 173.046 150.883 1.00 3.28   ? 271  TRP A CH2 1 
ATOM   2005 N  N   . GLY A 1 362 ? 180.890 172.979 146.434 1.00 3.18   ? 272  GLY A N   1 
ATOM   2006 C  CA  . GLY A 1 362 ? 182.283 173.297 146.156 1.00 3.19   ? 272  GLY A CA  1 
ATOM   2007 C  C   . GLY A 1 362 ? 182.664 174.618 146.803 1.00 3.24   ? 272  GLY A C   1 
ATOM   2008 O  O   . GLY A 1 362 ? 183.516 175.347 146.294 1.00 3.14   ? 272  GLY A O   1 
ATOM   2009 N  N   . ARG A 1 363 ? 182.008 174.931 147.914 1.00 3.18   ? 273  ARG A N   1 
ATOM   2010 C  CA  . ARG A 1 363 ? 182.247 176.190 148.606 1.00 3.28   ? 273  ARG A CA  1 
ATOM   2011 C  C   . ARG A 1 363 ? 183.570 176.171 149.364 1.00 3.34   ? 273  ARG A C   1 
ATOM   2012 O  O   . ARG A 1 363 ? 184.284 177.174 149.406 1.00 3.29   ? 273  ARG A O   1 
ATOM   2013 C  CB  . ARG A 1 363 ? 181.112 176.509 149.561 1.00 3.21   ? 273  ARG A CB  1 
ATOM   2014 C  CG  . ARG A 1 363 ? 181.237 177.855 150.238 1.00 3.25   ? 273  ARG A CG  1 
ATOM   2015 C  CD  . ARG A 1 363 ? 180.071 178.172 151.080 1.00 3.26   ? 273  ARG A CD  1 
ATOM   2016 N  NE  . ARG A 1 363 ? 180.289 179.394 151.828 1.00 3.35   ? 273  ARG A NE  1 
ATOM   2017 C  CZ  . ARG A 1 363 ? 179.528 179.823 152.850 1.00 3.30   ? 273  ARG A CZ  1 
ATOM   2018 N  NH1 . ARG A 1 363 ? 178.490 179.122 153.241 1.00 3.49   ? 273  ARG A NH1 1 
ATOM   2019 N  NH2 . ARG A 1 363 ? 179.833 180.950 153.461 1.00 3.37   ? 273  ARG A NH2 1 
ATOM   2020 N  N   . PHE A 1 364 ? 183.897 175.031 149.972 1.00 3.31   ? 274  PHE A N   1 
ATOM   2021 C  CA  . PHE A 1 364 ? 185.160 174.891 150.692 1.00 3.41   ? 274  PHE A CA  1 
ATOM   2022 C  C   . PHE A 1 364 ? 185.888 173.636 150.237 1.00 3.48   ? 274  PHE A C   1 
ATOM   2023 O  O   . PHE A 1 364 ? 185.255 172.648 149.883 1.00 3.37   ? 274  PHE A O   1 
ATOM   2024 C  CB  . PHE A 1 364 ? 184.930 174.815 152.202 1.00 3.46   ? 274  PHE A CB  1 
ATOM   2025 C  CG  . PHE A 1 364 ? 184.263 176.017 152.796 1.00 3.46   ? 274  PHE A CG  1 
ATOM   2026 C  CD1 . PHE A 1 364 ? 182.926 175.975 153.149 1.00 3.42   ? 274  PHE A CD1 1 
ATOM   2027 C  CD2 . PHE A 1 364 ? 184.965 177.191 153.004 1.00 3.55   ? 274  PHE A CD2 1 
ATOM   2028 C  CE1 . PHE A 1 364 ? 182.308 177.075 153.702 1.00 3.35   ? 274  PHE A CE1 1 
ATOM   2029 C  CE2 . PHE A 1 364 ? 184.349 178.293 153.552 1.00 3.50   ? 274  PHE A CE2 1 
ATOM   2030 C  CZ  . PHE A 1 364 ? 183.019 178.234 153.903 1.00 3.36   ? 274  PHE A CZ  1 
ATOM   2031 N  N   . TRP A 1 365 ? 187.218 173.656 150.278 1.00 3.53   ? 275  TRP A N   1 
ATOM   2032 C  CA  . TRP A 1 365 ? 187.996 172.482 149.895 1.00 3.68   ? 275  TRP A CA  1 
ATOM   2033 C  C   . TRP A 1 365 ? 188.563 171.772 151.119 1.00 4.04   ? 275  TRP A C   1 
ATOM   2034 O  O   . TRP A 1 365 ? 189.455 170.935 151.010 1.00 3.91   ? 275  TRP A O   1 
ATOM   2035 C  CB  . TRP A 1 365 ? 189.136 172.877 148.957 1.00 3.57   ? 275  TRP A CB  1 
ATOM   2036 C  CG  . TRP A 1 365 ? 188.690 173.352 147.596 1.00 3.37   ? 275  TRP A CG  1 
ATOM   2037 C  CD1 . TRP A 1 365 ? 187.411 173.480 147.140 1.00 3.27   ? 275  TRP A CD1 1 
ATOM   2038 C  CD2 . TRP A 1 365 ? 189.543 173.754 146.500 1.00 3.23   ? 275  TRP A CD2 1 
ATOM   2039 N  NE1 . TRP A 1 365 ? 187.414 173.935 145.852 1.00 3.20   ? 275  TRP A NE1 1 
ATOM   2040 C  CE2 . TRP A 1 365 ? 188.706 174.105 145.442 1.00 3.16   ? 275  TRP A CE2 1 
ATOM   2041 C  CE3 . TRP A 1 365 ? 190.928 173.842 146.333 1.00 3.19   ? 275  TRP A CE3 1 
ATOM   2042 C  CZ2 . TRP A 1 365 ? 189.205 174.537 144.229 1.00 3.06   ? 275  TRP A CZ2 1 
ATOM   2043 C  CZ3 . TRP A 1 365 ? 191.427 174.275 145.112 1.00 3.13   ? 275  TRP A CZ3 1 
ATOM   2044 C  CH2 . TRP A 1 365 ? 190.588 174.612 144.091 1.00 2.98   ? 275  TRP A CH2 1 
ATOM   2045 N  N   . THR A 1 366 ? 188.035 172.113 152.287 1.00 3.87   ? 276  THR A N   1 
ATOM   2046 C  CA  . THR A 1 366 ? 188.529 171.594 153.556 1.00 3.98   ? 276  THR A CA  1 
ATOM   2047 C  C   . THR A 1 366 ? 188.551 170.072 153.610 1.00 4.20   ? 276  THR A C   1 
ATOM   2048 O  O   . THR A 1 366 ? 189.482 169.476 154.156 1.00 4.28   ? 276  THR A O   1 
ATOM   2049 C  CB  . THR A 1 366 ? 187.681 172.128 154.730 1.00 3.92   ? 276  THR A CB  1 
ATOM   2050 O  OG1 . THR A 1 366 ? 187.801 173.552 154.801 1.00 3.85   ? 276  THR A OG1 1 
ATOM   2051 C  CG2 . THR A 1 366 ? 188.155 171.523 156.043 1.00 4.10   ? 276  THR A CG2 1 
ATOM   2052 N  N   . ASN A 1 367 ? 187.525 169.436 153.067 1.00 4.16   ? 277  ASN A N   1 
ATOM   2053 C  CA  . ASN A 1 367 ? 187.373 167.994 153.194 1.00 4.35   ? 277  ASN A CA  1 
ATOM   2054 C  C   . ASN A 1 367 ? 188.273 167.226 152.240 1.00 4.45   ? 277  ASN A C   1 
ATOM   2055 O  O   . ASN A 1 367 ? 188.264 165.994 152.225 1.00 4.71   ? 277  ASN A O   1 
ATOM   2056 C  CB  . ASN A 1 367 ? 185.929 167.607 152.994 1.00 4.31   ? 277  ASN A CB  1 
ATOM   2057 C  CG  . ASN A 1 367 ? 185.068 168.107 154.097 1.00 4.36   ? 277  ASN A CG  1 
ATOM   2058 O  OD1 . ASN A 1 367 ? 185.490 168.188 155.255 1.00 4.53   ? 277  ASN A OD1 1 
ATOM   2059 N  ND2 . ASN A 1 367 ? 183.866 168.460 153.766 1.00 4.29   ? 277  ASN A ND2 1 
ATOM   2060 N  N   . LEU A 1 368 ? 189.066 167.940 151.453 1.00 4.33   ? 278  LEU A N   1 
ATOM   2061 C  CA  . LEU A 1 368 ? 190.007 167.288 150.558 1.00 4.45   ? 278  LEU A CA  1 
ATOM   2062 C  C   . LEU A 1 368 ? 191.350 167.086 151.244 1.00 4.92   ? 278  LEU A C   1 
ATOM   2063 O  O   . LEU A 1 368 ? 192.227 166.411 150.712 1.00 4.77   ? 278  LEU A O   1 
ATOM   2064 C  CB  . LEU A 1 368 ? 190.201 168.116 149.281 1.00 4.29   ? 278  LEU A CB  1 
ATOM   2065 C  CG  . LEU A 1 368 ? 188.944 168.355 148.414 1.00 3.94   ? 278  LEU A CG  1 
ATOM   2066 C  CD1 . LEU A 1 368 ? 189.316 169.239 147.234 1.00 3.63   ? 278  LEU A CD1 1 
ATOM   2067 C  CD2 . LEU A 1 368 ? 188.383 167.026 147.937 1.00 3.87   ? 278  LEU A CD2 1 
ATOM   2068 N  N   . TYR A 1 369 ? 191.498 167.643 152.445 1.00 4.79   ? 279  TYR A N   1 
ATOM   2069 C  CA  . TYR A 1 369 ? 192.771 167.589 153.164 1.00 5.05   ? 279  TYR A CA  1 
ATOM   2070 C  C   . TYR A 1 369 ? 193.363 166.182 153.254 1.00 5.48   ? 279  TYR A C   1 
ATOM   2071 O  O   . TYR A 1 369 ? 194.576 166.015 153.092 1.00 5.41   ? 279  TYR A O   1 
ATOM   2072 C  CB  . TYR A 1 369 ? 192.630 168.189 154.563 1.00 5.15   ? 279  TYR A CB  1 
ATOM   2073 C  CG  . TYR A 1 369 ? 193.918 168.163 155.347 1.00 5.44   ? 279  TYR A CG  1 
ATOM   2074 C  CD1 . TYR A 1 369 ? 194.890 169.123 155.117 1.00 5.54   ? 279  TYR A CD1 1 
ATOM   2075 C  CD2 . TYR A 1 369 ? 194.130 167.177 156.291 1.00 5.71   ? 279  TYR A CD2 1 
ATOM   2076 C  CE1 . TYR A 1 369 ? 196.069 169.093 155.828 1.00 5.88   ? 279  TYR A CE1 1 
ATOM   2077 C  CE2 . TYR A 1 369 ? 195.308 167.149 157.002 1.00 5.83   ? 279  TYR A CE2 1 
ATOM   2078 C  CZ  . TYR A 1 369 ? 196.274 168.102 156.773 1.00 5.95   ? 279  TYR A CZ  1 
ATOM   2079 O  OH  . TYR A 1 369 ? 197.445 168.073 157.487 1.00 6.81   ? 279  TYR A OH  1 
ATOM   2080 N  N   . ASN A 1 370 ? 192.539 165.164 153.512 1.00 5.40   ? 280  ASN A N   1 
ATOM   2081 C  CA  . ASN A 1 370 ? 192.981 163.786 153.658 1.00 5.75   ? 280  ASN A CA  1 
ATOM   2082 C  C   . ASN A 1 370 ? 193.602 163.227 152.367 1.00 5.47   ? 280  ASN A C   1 
ATOM   2083 O  O   . ASN A 1 370 ? 194.323 162.234 152.397 1.00 5.57   ? 280  ASN A O   1 
ATOM   2084 C  CB  . ASN A 1 370 ? 191.854 162.884 154.130 1.00 6.71   ? 280  ASN A CB  1 
ATOM   2085 C  CG  . ASN A 1 370 ? 191.605 162.947 155.633 1.00 7.55   ? 280  ASN A CG  1 
ATOM   2086 O  OD1 . ASN A 1 370 ? 192.356 163.600 156.381 1.00 7.33   ? 280  ASN A OD1 1 
ATOM   2087 N  ND2 . ASN A 1 370 ? 190.570 162.279 156.090 1.00 8.74   ? 280  ASN A ND2 1 
ATOM   2088 N  N   . LEU A 1 371 ? 193.276 163.850 151.224 1.00 5.15   ? 281  LEU A N   1 
ATOM   2089 C  CA  . LEU A 1 371 ? 193.807 163.460 149.920 1.00 5.05   ? 281  LEU A CA  1 
ATOM   2090 C  C   . LEU A 1 371 ? 194.995 164.339 149.530 1.00 4.92   ? 281  LEU A C   1 
ATOM   2091 O  O   . LEU A 1 371 ? 195.861 163.917 148.764 1.00 4.74   ? 281  LEU A O   1 
ATOM   2092 C  CB  . LEU A 1 371 ? 192.721 163.584 148.838 1.00 4.84   ? 281  LEU A CB  1 
ATOM   2093 C  CG  . LEU A 1 371 ? 191.451 162.722 149.016 1.00 4.77   ? 281  LEU A CG  1 
ATOM   2094 C  CD1 . LEU A 1 371 ? 190.449 163.081 147.921 1.00 4.50   ? 281  LEU A CD1 1 
ATOM   2095 C  CD2 . LEU A 1 371 ? 191.811 161.244 148.939 1.00 4.75   ? 281  LEU A CD2 1 
ATOM   2096 N  N   . THR A 1 372 ? 195.013 165.574 150.035 1.00 5.03   ? 282  THR A N   1 
ATOM   2097 C  CA  . THR A 1 372 ? 195.999 166.562 149.608 1.00 4.97   ? 282  THR A CA  1 
ATOM   2098 C  C   . THR A 1 372 ? 197.129 166.813 150.608 1.00 5.46   ? 282  THR A C   1 
ATOM   2099 O  O   . THR A 1 372 ? 198.118 167.457 150.267 1.00 5.25   ? 282  THR A O   1 
ATOM   2100 C  CB  . THR A 1 372 ? 195.315 167.908 149.293 1.00 4.77   ? 282  THR A CB  1 
ATOM   2101 O  OG1 . THR A 1 372 ? 194.680 168.414 150.468 1.00 4.90   ? 282  THR A OG1 1 
ATOM   2102 C  CG2 . THR A 1 372 ? 194.276 167.735 148.202 1.00 4.44   ? 282  THR A CG2 1 
ATOM   2103 N  N   . VAL A 1 373 ? 196.998 166.321 151.836 1.00 5.60   ? 283  VAL A N   1 
ATOM   2104 C  CA  . VAL A 1 373 ? 198.014 166.582 152.857 1.00 6.08   ? 283  VAL A CA  1 
ATOM   2105 C  C   . VAL A 1 373 ? 199.435 166.359 152.312 1.00 6.74   ? 283  VAL A C   1 
ATOM   2106 O  O   . VAL A 1 373 ? 199.760 165.262 151.862 1.00 6.78   ? 283  VAL A O   1 
ATOM   2107 C  CB  . VAL A 1 373 ? 197.767 165.692 154.099 1.00 6.15   ? 283  VAL A CB  1 
ATOM   2108 C  CG1 . VAL A 1 373 ? 197.857 164.212 153.750 1.00 6.42   ? 283  VAL A CG1 1 
ATOM   2109 C  CG2 . VAL A 1 373 ? 198.785 166.031 155.175 1.00 6.94   ? 283  VAL A CG2 1 
ATOM   2110 N  N   . PRO A 1 374 ? 200.281 167.404 152.311 1.00 6.83   ? 284  PRO A N   1 
ATOM   2111 C  CA  . PRO A 1 374 ? 201.673 167.412 151.883 1.00 7.25   ? 284  PRO A CA  1 
ATOM   2112 C  C   . PRO A 1 374 ? 202.506 166.293 152.497 1.00 8.22   ? 284  PRO A C   1 
ATOM   2113 O  O   . PRO A 1 374 ? 203.096 165.489 151.776 1.00 8.45   ? 284  PRO A O   1 
ATOM   2114 C  CB  . PRO A 1 374 ? 202.133 168.791 152.364 1.00 7.57   ? 284  PRO A CB  1 
ATOM   2115 C  CG  . PRO A 1 374 ? 200.895 169.636 152.271 1.00 6.80   ? 284  PRO A CG  1 
ATOM   2116 C  CD  . PRO A 1 374 ? 199.779 168.724 152.713 1.00 6.64   ? 284  PRO A CD  1 
ATOM   2117 N  N   . PHE A 1 375 ? 202.568 166.250 153.826 1.00 8.34   ? 285  PHE A N   1 
ATOM   2118 C  CA  . PHE A 1 375 ? 203.384 165.259 154.515 1.00 8.83   ? 285  PHE A CA  1 
ATOM   2119 C  C   . PHE A 1 375 ? 202.534 164.401 155.442 1.00 9.59   ? 285  PHE A C   1 
ATOM   2120 O  O   . PHE A 1 375 ? 202.192 164.817 156.549 1.00 9.53   ? 285  PHE A O   1 
ATOM   2121 C  CB  . PHE A 1 375 ? 204.495 165.963 155.294 1.00 9.59   ? 285  PHE A CB  1 
ATOM   2122 C  CG  . PHE A 1 375 ? 205.355 166.825 154.415 1.00 9.70   ? 285  PHE A CG  1 
ATOM   2123 C  CD1 . PHE A 1 375 ? 205.125 168.189 154.320 1.00 9.39   ? 285  PHE A CD1 1 
ATOM   2124 C  CD2 . PHE A 1 375 ? 206.374 166.276 153.663 1.00 10.53  ? 285  PHE A CD2 1 
ATOM   2125 C  CE1 . PHE A 1 375 ? 205.896 168.978 153.496 1.00 9.68   ? 285  PHE A CE1 1 
ATOM   2126 C  CE2 . PHE A 1 375 ? 207.145 167.066 152.839 1.00 11.04  ? 285  PHE A CE2 1 
ATOM   2127 C  CZ  . PHE A 1 375 ? 206.903 168.416 152.755 1.00 10.88  ? 285  PHE A CZ  1 
ATOM   2128 N  N   . GLU A 1 376 ? 202.169 163.209 154.977 1.00 9.33   ? 286  GLU A N   1 
ATOM   2129 C  CA  . GLU A 1 376 ? 201.189 162.372 155.668 1.00 9.65   ? 286  GLU A CA  1 
ATOM   2130 C  C   . GLU A 1 376 ? 201.747 161.692 156.918 1.00 10.39  ? 286  GLU A C   1 
ATOM   2131 O  O   . GLU A 1 376 ? 200.989 161.136 157.714 1.00 10.57  ? 286  GLU A O   1 
ATOM   2132 C  CB  . GLU A 1 376 ? 200.627 161.315 154.708 1.00 9.60   ? 286  GLU A CB  1 
ATOM   2133 C  CG  . GLU A 1 376 ? 201.541 160.110 154.441 1.00 10.16  ? 286  GLU A CG  1 
ATOM   2134 C  CD  . GLU A 1 376 ? 202.569 160.350 153.368 1.00 10.36  ? 286  GLU A CD  1 
ATOM   2135 O  OE1 . GLU A 1 376 ? 202.849 161.487 153.083 1.00 10.06  ? 286  GLU A OE1 1 
ATOM   2136 O  OE2 . GLU A 1 376 ? 203.077 159.391 152.838 1.00 10.32  ? 286  GLU A OE2 1 
ATOM   2137 N  N   . LYS A 1 377 ? 203.062 161.737 157.092 1.00 10.81  ? 287  LYS A N   1 
ATOM   2138 C  CA  . LYS A 1 377 ? 203.691 161.105 158.250 1.00 11.03  ? 287  LYS A CA  1 
ATOM   2139 C  C   . LYS A 1 377 ? 203.736 162.044 159.448 1.00 11.56  ? 287  LYS A C   1 
ATOM   2140 O  O   . LYS A 1 377 ? 204.159 161.652 160.534 1.00 11.93  ? 287  LYS A O   1 
ATOM   2141 C  CB  . LYS A 1 377 ? 205.113 160.645 157.924 1.00 12.21  ? 287  LYS A CB  1 
ATOM   2142 C  CG  . LYS A 1 377 ? 205.210 159.541 156.880 1.00 12.26  ? 287  LYS A CG  1 
ATOM   2143 C  CD  . LYS A 1 377 ? 206.619 158.927 156.843 1.00 13.93  ? 287  LYS A CD  1 
ATOM   2144 C  CE  . LYS A 1 377 ? 207.642 159.876 156.211 1.00 16.27  ? 287  LYS A CE  1 
ATOM   2145 N  NZ  . LYS A 1 377 ? 208.973 159.222 156.011 1.00 18.67  ? 287  LYS A NZ  1 
ATOM   2146 N  N   . LYS A 1 378 ? 203.328 163.292 159.243 1.00 11.25  ? 288  LYS A N   1 
ATOM   2147 C  CA  . LYS A 1 378 ? 203.367 164.282 160.306 1.00 10.87  ? 288  LYS A CA  1 
ATOM   2148 C  C   . LYS A 1 378 ? 201.958 164.712 160.682 1.00 10.80  ? 288  LYS A C   1 
ATOM   2149 O  O   . LYS A 1 378 ? 201.093 164.861 159.820 1.00 10.98  ? 288  LYS A O   1 
ATOM   2150 C  CB  . LYS A 1 378 ? 204.204 165.490 159.873 1.00 11.35  ? 288  LYS A CB  1 
ATOM   2151 C  CG  . LYS A 1 378 ? 205.660 165.160 159.518 1.00 12.04  ? 288  LYS A CG  1 
ATOM   2152 C  CD  . LYS A 1 378 ? 206.492 164.887 160.766 1.00 13.84  ? 288  LYS A CD  1 
ATOM   2153 C  CE  . LYS A 1 378 ? 207.896 164.393 160.427 1.00 16.52  ? 288  LYS A CE  1 
ATOM   2154 N  NZ  . LYS A 1 378 ? 208.721 165.428 159.737 1.00 16.00  ? 288  LYS A NZ  1 
ATOM   2155 N  N   . GLN A 1 379 ? 201.726 164.901 161.974 1.00 11.24  ? 289  GLN A N   1 
ATOM   2156 C  CA  . GLN A 1 379 ? 200.414 165.307 162.456 1.00 10.98  ? 289  GLN A CA  1 
ATOM   2157 C  C   . GLN A 1 379 ? 200.404 166.758 162.900 1.00 10.48  ? 289  GLN A C   1 
ATOM   2158 O  O   . GLN A 1 379 ? 201.445 167.326 163.226 1.00 10.70  ? 289  GLN A O   1 
ATOM   2159 C  CB  . GLN A 1 379 ? 199.961 164.408 163.608 1.00 10.97  ? 289  GLN A CB  1 
ATOM   2160 C  CG  . GLN A 1 379 ? 199.857 162.942 163.239 1.00 11.27  ? 289  GLN A CG  1 
ATOM   2161 C  CD  . GLN A 1 379 ? 198.834 162.701 162.151 1.00 11.66  ? 289  GLN A CD  1 
ATOM   2162 O  OE1 . GLN A 1 379 ? 197.680 163.120 162.266 1.00 11.77  ? 289  GLN A OE1 1 
ATOM   2163 N  NE2 . GLN A 1 379 ? 199.251 162.028 161.085 1.00 11.60  ? 289  GLN A NE2 1 
ATOM   2164 N  N   . ASN A 1 380 ? 199.218 167.346 162.935 1.00 10.54  ? 290  ASN A N   1 
ATOM   2165 C  CA  . ASN A 1 380 ? 199.055 168.707 163.418 1.00 10.42  ? 290  ASN A CA  1 
ATOM   2166 C  C   . ASN A 1 380 ? 198.929 168.709 164.929 1.00 10.45  ? 290  ASN A C   1 
ATOM   2167 O  O   . ASN A 1 380 ? 198.605 167.687 165.533 1.00 10.74  ? 290  ASN A O   1 
ATOM   2168 C  CB  . ASN A 1 380 ? 197.857 169.369 162.770 1.00 10.16  ? 290  ASN A CB  1 
ATOM   2169 N  N   . ILE A 1 381 ? 199.196 169.853 165.542 1.00 10.75  ? 291  ILE A N   1 
ATOM   2170 C  CA  . ILE A 1 381 ? 199.127 169.957 166.990 1.00 11.05  ? 291  ILE A CA  1 
ATOM   2171 C  C   . ILE A 1 381 ? 197.695 169.891 167.490 1.00 11.10  ? 291  ILE A C   1 
ATOM   2172 O  O   . ILE A 1 381 ? 196.824 170.622 167.021 1.00 11.14  ? 291  ILE A O   1 
ATOM   2173 C  CB  . ILE A 1 381 ? 199.787 171.256 167.478 1.00 11.06  ? 291  ILE A CB  1 
ATOM   2174 C  CG1 . ILE A 1 381 ? 201.285 171.215 167.154 1.00 11.47  ? 291  ILE A CG1 1 
ATOM   2175 C  CG2 . ILE A 1 381 ? 199.551 171.442 168.979 1.00 11.28  ? 291  ILE A CG2 1 
ATOM   2176 C  CD1 . ILE A 1 381 ? 201.980 172.540 167.306 1.00 11.61  ? 291  ILE A CD1 1 
ATOM   2177 N  N   . ASP A 1 382 ? 197.472 169.014 168.459 1.00 11.28  ? 292  ASP A N   1 
ATOM   2178 C  CA  . ASP A 1 382 ? 196.171 168.838 169.083 1.00 11.24  ? 292  ASP A CA  1 
ATOM   2179 C  C   . ASP A 1 382 ? 196.353 168.613 170.575 1.00 11.30  ? 292  ASP A C   1 
ATOM   2180 O  O   . ASP A 1 382 ? 196.961 167.629 170.996 1.00 11.60  ? 292  ASP A O   1 
ATOM   2181 C  CB  . ASP A 1 382 ? 195.409 167.675 168.452 1.00 11.48  ? 292  ASP A CB  1 
ATOM   2182 C  CG  . ASP A 1 382 ? 193.991 167.557 168.982 1.00 11.57  ? 292  ASP A CG  1 
ATOM   2183 O  OD1 . ASP A 1 382 ? 193.725 168.115 170.025 1.00 11.63  ? 292  ASP A OD1 1 
ATOM   2184 O  OD2 . ASP A 1 382 ? 193.182 166.923 168.347 1.00 12.00  ? 292  ASP A OD2 1 
ATOM   2185 N  N   . VAL A 1 383 ? 195.884 169.562 171.372 1.00 11.29  ? 293  VAL A N   1 
ATOM   2186 C  CA  . VAL A 1 383 ? 196.139 169.549 172.804 1.00 11.53  ? 293  VAL A CA  1 
ATOM   2187 C  C   . VAL A 1 383 ? 194.938 169.042 173.591 1.00 11.50  ? 293  VAL A C   1 
ATOM   2188 O  O   . VAL A 1 383 ? 194.897 169.174 174.813 1.00 11.34  ? 293  VAL A O   1 
ATOM   2189 C  CB  . VAL A 1 383 ? 196.521 170.961 173.294 1.00 11.50  ? 293  VAL A CB  1 
ATOM   2190 C  CG1 . VAL A 1 383 ? 197.780 171.440 172.579 1.00 11.37  ? 293  VAL A CG1 1 
ATOM   2191 C  CG2 . VAL A 1 383 ? 195.370 171.927 173.054 1.00 11.19  ? 293  VAL A CG2 1 
ATOM   2192 N  N   . THR A 1 384 ? 193.969 168.456 172.892 1.00 11.31  ? 294  THR A N   1 
ATOM   2193 C  CA  . THR A 1 384 ? 192.762 167.950 173.537 1.00 11.33  ? 294  THR A CA  1 
ATOM   2194 C  C   . THR A 1 384 ? 193.085 166.962 174.657 1.00 11.51  ? 294  THR A C   1 
ATOM   2195 O  O   . THR A 1 384 ? 192.518 167.039 175.748 1.00 11.35  ? 294  THR A O   1 
ATOM   2196 C  CB  . THR A 1 384 ? 191.827 167.267 172.515 1.00 11.17  ? 294  THR A CB  1 
ATOM   2197 O  OG1 . THR A 1 384 ? 191.405 168.220 171.530 1.00 11.10  ? 294  THR A OG1 1 
ATOM   2198 C  CG2 . THR A 1 384 ? 190.608 166.690 173.223 1.00 11.18  ? 294  THR A CG2 1 
ATOM   2199 N  N   . ASP A 1 385 ? 194.002 166.039 174.390 1.00 11.64  ? 295  ASP A N   1 
ATOM   2200 C  CA  . ASP A 1 385 ? 194.359 165.025 175.375 1.00 11.60  ? 295  ASP A CA  1 
ATOM   2201 C  C   . ASP A 1 385 ? 195.006 165.643 176.605 1.00 11.69  ? 295  ASP A C   1 
ATOM   2202 O  O   . ASP A 1 385 ? 194.828 165.152 177.721 1.00 11.67  ? 295  ASP A O   1 
ATOM   2203 C  CB  . ASP A 1 385 ? 195.311 163.997 174.767 1.00 11.85  ? 295  ASP A CB  1 
ATOM   2204 N  N   . THR A 1 386 ? 195.773 166.708 176.401 1.00 11.55  ? 296  THR A N   1 
ATOM   2205 C  CA  . THR A 1 386 ? 196.438 167.382 177.505 1.00 11.42  ? 296  THR A CA  1 
ATOM   2206 C  C   . THR A 1 386 ? 195.424 168.114 178.371 1.00 11.59  ? 296  THR A C   1 
ATOM   2207 O  O   . THR A 1 386 ? 195.511 168.086 179.598 1.00 11.44  ? 296  THR A O   1 
ATOM   2208 C  CB  . THR A 1 386 ? 197.511 168.361 177.000 1.00 11.68  ? 296  THR A CB  1 
ATOM   2209 O  OG1 . THR A 1 386 ? 198.497 167.642 176.251 1.00 12.02  ? 296  THR A OG1 1 
ATOM   2210 C  CG2 . THR A 1 386 ? 198.181 169.047 178.178 1.00 11.68  ? 296  THR A CG2 1 
ATOM   2211 N  N   . MET A 1 387 ? 194.455 168.761 177.730 1.00 11.34  ? 297  MET A N   1 
ATOM   2212 C  CA  . MET A 1 387 ? 193.419 169.483 178.455 1.00 11.39  ? 297  MET A CA  1 
ATOM   2213 C  C   . MET A 1 387 ? 192.648 168.549 179.370 1.00 11.95  ? 297  MET A C   1 
ATOM   2214 O  O   . MET A 1 387 ? 192.331 168.897 180.508 1.00 11.15  ? 297  MET A O   1 
ATOM   2215 C  CB  . MET A 1 387 ? 192.457 170.158 177.482 1.00 11.11  ? 297  MET A CB  1 
ATOM   2216 C  CG  . MET A 1 387 ? 193.048 171.312 176.706 1.00 11.02  ? 297  MET A CG  1 
ATOM   2217 S  SD  . MET A 1 387 ? 191.941 171.940 175.434 1.00 10.66  ? 297  MET A SD  1 
ATOM   2218 C  CE  . MET A 1 387 ? 190.724 172.803 176.417 1.00 10.51  ? 297  MET A CE  1 
ATOM   2219 N  N   . LYS A 1 388 ? 192.357 167.349 178.880 1.00 11.37  ? 298  LYS A N   1 
ATOM   2220 C  CA  . LYS A 1 388 ? 191.641 166.368 179.678 1.00 11.62  ? 298  LYS A CA  1 
ATOM   2221 C  C   . LYS A 1 388 ? 192.514 165.857 180.816 1.00 11.66  ? 298  LYS A C   1 
ATOM   2222 O  O   . LYS A 1 388 ? 192.062 165.733 181.952 1.00 11.80  ? 298  LYS A O   1 
ATOM   2223 C  CB  . LYS A 1 388 ? 191.175 165.214 178.798 1.00 11.45  ? 298  LYS A CB  1 
ATOM   2224 C  CG  . LYS A 1 388 ? 190.092 165.600 177.807 1.00 11.56  ? 298  LYS A CG  1 
ATOM   2225 C  CD  . LYS A 1 388 ? 189.713 164.433 176.917 1.00 11.80  ? 298  LYS A CD  1 
ATOM   2226 C  CE  . LYS A 1 388 ? 188.627 164.825 175.927 1.00 12.08  ? 298  LYS A CE  1 
ATOM   2227 N  NZ  . LYS A 1 388 ? 187.293 164.929 176.577 1.00 11.84  ? 298  LYS A NZ  1 
ATOM   2228 N  N   . LYS A 1 389 ? 193.783 165.599 180.516 1.00 11.67  ? 299  LYS A N   1 
ATOM   2229 C  CA  . LYS A 1 389 ? 194.723 165.102 181.513 1.00 11.56  ? 299  LYS A CA  1 
ATOM   2230 C  C   . LYS A 1 389 ? 194.909 166.095 182.656 1.00 11.66  ? 299  LYS A C   1 
ATOM   2231 O  O   . LYS A 1 389 ? 195.066 165.704 183.813 1.00 11.87  ? 299  LYS A O   1 
ATOM   2232 C  CB  . LYS A 1 389 ? 196.072 164.790 180.866 1.00 12.01  ? 299  LYS A CB  1 
ATOM   2233 N  N   . GLN A 1 390 ? 194.883 167.383 182.327 1.00 11.61  ? 300  GLN A N   1 
ATOM   2234 C  CA  . GLN A 1 390 ? 195.075 168.444 183.309 1.00 11.56  ? 300  GLN A CA  1 
ATOM   2235 C  C   . GLN A 1 390 ? 193.761 168.879 183.956 1.00 11.50  ? 300  GLN A C   1 
ATOM   2236 O  O   . GLN A 1 390 ? 193.727 169.858 184.702 1.00 11.53  ? 300  GLN A O   1 
ATOM   2237 C  CB  . GLN A 1 390 ? 195.768 169.645 182.668 1.00 11.54  ? 300  GLN A CB  1 
ATOM   2238 C  CG  . GLN A 1 390 ? 197.195 169.387 182.240 1.00 11.49  ? 300  GLN A CG  1 
ATOM   2239 C  CD  . GLN A 1 390 ? 197.825 170.595 181.581 1.00 11.57  ? 300  GLN A CD  1 
ATOM   2240 O  OE1 . GLN A 1 390 ? 197.212 171.666 181.488 1.00 11.70  ? 300  GLN A OE1 1 
ATOM   2241 N  NE2 . GLN A 1 390 ? 199.057 170.431 181.115 1.00 11.86  ? 300  GLN A NE2 1 
ATOM   2242 N  N   . SER A 1 391 ? 192.689 168.143 183.674 1.00 11.58  ? 301  SER A N   1 
ATOM   2243 C  CA  . SER A 1 391 ? 191.369 168.399 184.245 1.00 11.49  ? 301  SER A CA  1 
ATOM   2244 C  C   . SER A 1 391 ? 190.823 169.792 183.952 1.00 11.41  ? 301  SER A C   1 
ATOM   2245 O  O   . SER A 1 391 ? 190.344 170.480 184.854 1.00 11.57  ? 301  SER A O   1 
ATOM   2246 C  CB  . SER A 1 391 ? 191.396 168.179 185.748 1.00 11.73  ? 301  SER A CB  1 
ATOM   2247 N  N   . TRP A 1 392 ? 190.847 170.187 182.684 1.00 11.25  ? 302  TRP A N   1 
ATOM   2248 C  CA  . TRP A 1 392 ? 190.223 171.437 182.267 1.00 10.97  ? 302  TRP A CA  1 
ATOM   2249 C  C   . TRP A 1 392 ? 188.715 171.269 182.155 1.00 10.85  ? 302  TRP A C   1 
ATOM   2250 O  O   . TRP A 1 392 ? 188.224 170.174 181.882 1.00 11.15  ? 302  TRP A O   1 
ATOM   2251 C  CB  . TRP A 1 392 ? 190.760 171.905 180.914 1.00 10.79  ? 302  TRP A CB  1 
ATOM   2252 C  CG  . TRP A 1 392 ? 192.133 172.484 180.953 1.00 10.91  ? 302  TRP A CG  1 
ATOM   2253 C  CD1 . TRP A 1 392 ? 193.237 171.951 181.533 1.00 10.97  ? 302  TRP A CD1 1 
ATOM   2254 C  CD2 . TRP A 1 392 ? 192.553 173.733 180.366 1.00 10.90  ? 302  TRP A CD2 1 
ATOM   2255 N  NE1 . TRP A 1 392 ? 194.313 172.777 181.347 1.00 10.86  ? 302  TRP A NE1 1 
ATOM   2256 C  CE2 . TRP A 1 392 ? 193.910 173.874 180.636 1.00 10.72  ? 302  TRP A CE2 1 
ATOM   2257 C  CE3 . TRP A 1 392 ? 191.893 174.727 179.640 1.00 10.37  ? 302  TRP A CE3 1 
ATOM   2258 C  CZ2 . TRP A 1 392 ? 194.630 174.974 180.207 1.00 10.77  ? 302  TRP A CZ2 1 
ATOM   2259 C  CZ3 . TRP A 1 392 ? 192.612 175.826 179.209 1.00 10.21  ? 302  TRP A CZ3 1 
ATOM   2260 C  CH2 . TRP A 1 392 ? 193.947 175.946 179.485 1.00 10.38  ? 302  TRP A CH2 1 
ATOM   2261 N  N   . ASP A 1 393 ? 187.988 172.363 182.332 1.00 10.93  ? 303  ASP A N   1 
ATOM   2262 C  CA  . ASP A 1 393 ? 186.544 172.373 182.142 1.00 10.41  ? 303  ASP A CA  1 
ATOM   2263 C  C   . ASP A 1 393 ? 186.104 173.648 181.429 1.00 10.20  ? 303  ASP A C   1 
ATOM   2264 O  O   . ASP A 1 393 ? 186.937 174.469 181.040 1.00 10.03  ? 303  ASP A O   1 
ATOM   2265 C  CB  . ASP A 1 393 ? 185.830 172.221 183.486 1.00 10.37  ? 303  ASP A CB  1 
ATOM   2266 C  CG  . ASP A 1 393 ? 186.183 173.314 184.477 1.00 10.28  ? 303  ASP A CG  1 
ATOM   2267 O  OD1 . ASP A 1 393 ? 186.710 174.324 184.063 1.00 10.32  ? 303  ASP A OD1 1 
ATOM   2268 O  OD2 . ASP A 1 393 ? 185.921 173.134 185.642 1.00 10.69  ? 303  ASP A OD2 1 
ATOM   2269 N  N   . ALA A 1 394 ? 184.798 173.801 181.223 1.00 10.10  ? 304  ALA A N   1 
ATOM   2270 C  CA  . ALA A 1 394 ? 184.285 174.931 180.456 1.00 9.99   ? 304  ALA A CA  1 
ATOM   2271 C  C   . ALA A 1 394 ? 184.620 176.265 181.106 1.00 9.92   ? 304  ALA A C   1 
ATOM   2272 O  O   . ALA A 1 394 ? 184.918 177.240 180.416 1.00 9.77   ? 304  ALA A O   1 
ATOM   2273 C  CB  . ALA A 1 394 ? 182.783 174.811 180.290 1.00 10.28  ? 304  ALA A CB  1 
ATOM   2274 N  N   . GLU A 1 395 ? 184.566 176.319 182.430 1.00 9.86   ? 305  GLU A N   1 
ATOM   2275 C  CA  . GLU A 1 395 ? 184.824 177.572 183.121 1.00 9.73   ? 305  GLU A CA  1 
ATOM   2276 C  C   . GLU A 1 395 ? 186.273 177.995 182.953 1.00 9.81   ? 305  GLU A C   1 
ATOM   2277 O  O   . GLU A 1 395 ? 186.554 179.160 182.675 1.00 9.40   ? 305  GLU A O   1 
ATOM   2278 C  CB  . GLU A 1 395 ? 184.475 177.464 184.603 1.00 10.06  ? 305  GLU A CB  1 
ATOM   2279 C  CG  . GLU A 1 395 ? 184.612 178.775 185.368 1.00 10.00  ? 305  GLU A CG  1 
ATOM   2280 C  CD  . GLU A 1 395 ? 184.158 178.675 186.792 1.00 10.55  ? 305  GLU A CD  1 
ATOM   2281 O  OE1 . GLU A 1 395 ? 183.739 177.617 187.190 1.00 10.81  ? 305  GLU A OE1 1 
ATOM   2282 O  OE2 . GLU A 1 395 ? 184.229 179.661 187.487 1.00 10.63  ? 305  GLU A OE2 1 
ATOM   2283 N  N   . LYS A 1 396 ? 187.192 177.044 183.103 1.00 9.74   ? 306  LYS A N   1 
ATOM   2284 C  CA  . LYS A 1 396 ? 188.610 177.343 182.958 1.00 9.53   ? 306  LYS A CA  1 
ATOM   2285 C  C   . LYS A 1 396 ? 188.930 177.845 181.558 1.00 9.75   ? 306  LYS A C   1 
ATOM   2286 O  O   . LYS A 1 396 ? 189.735 178.759 181.393 1.00 9.19   ? 306  LYS A O   1 
ATOM   2287 C  CB  . LYS A 1 396 ? 189.467 176.122 183.282 1.00 10.02  ? 306  LYS A CB  1 
ATOM   2288 C  CG  . LYS A 1 396 ? 190.962 176.411 183.290 1.00 10.04  ? 306  LYS A CG  1 
ATOM   2289 C  CD  . LYS A 1 396 ? 191.759 175.216 183.771 1.00 10.38  ? 306  LYS A CD  1 
ATOM   2290 C  CE  . LYS A 1 396 ? 193.253 175.501 183.737 1.00 10.50  ? 306  LYS A CE  1 
ATOM   2291 N  NZ  . LYS A 1 396 ? 193.663 176.448 184.810 1.00 10.16  ? 306  LYS A NZ  1 
ATOM   2292 N  N   . ILE A 1 397 ? 188.287 177.262 180.553 1.00 9.51   ? 307  ILE A N   1 
ATOM   2293 C  CA  . ILE A 1 397 ? 188.524 177.664 179.173 1.00 9.44   ? 307  ILE A CA  1 
ATOM   2294 C  C   . ILE A 1 397 ? 188.170 179.128 178.952 1.00 9.19   ? 307  ILE A C   1 
ATOM   2295 O  O   . ILE A 1 397 ? 188.945 179.876 178.353 1.00 9.00   ? 307  ILE A O   1 
ATOM   2296 C  CB  . ILE A 1 397 ? 187.725 176.775 178.200 1.00 9.54   ? 307  ILE A CB  1 
ATOM   2297 C  CG1 . ILE A 1 397 ? 188.317 175.360 178.202 1.00 9.75   ? 307  ILE A CG1 1 
ATOM   2298 C  CG2 . ILE A 1 397 ? 187.731 177.375 176.799 1.00 9.34   ? 307  ILE A CG2 1 
ATOM   2299 C  CD1 . ILE A 1 397 ? 187.440 174.315 177.552 1.00 10.16  ? 307  ILE A CD1 1 
ATOM   2300 N  N   . PHE A 1 398 ? 187.015 179.546 179.453 1.00 9.07   ? 308  PHE A N   1 
ATOM   2301 C  CA  . PHE A 1 398 ? 186.603 180.935 179.310 1.00 9.00   ? 308  PHE A CA  1 
ATOM   2302 C  C   . PHE A 1 398 ? 187.433 181.873 180.178 1.00 9.14   ? 308  PHE A C   1 
ATOM   2303 O  O   . PHE A 1 398 ? 187.680 183.018 179.796 1.00 8.68   ? 308  PHE A O   1 
ATOM   2304 C  CB  . PHE A 1 398 ? 185.113 181.082 179.600 1.00 9.07   ? 308  PHE A CB  1 
ATOM   2305 C  CG  . PHE A 1 398 ? 184.269 180.746 178.414 1.00 9.08   ? 308  PHE A CG  1 
ATOM   2306 C  CD1 . PHE A 1 398 ? 183.903 181.733 177.522 1.00 9.04   ? 308  PHE A CD1 1 
ATOM   2307 C  CD2 . PHE A 1 398 ? 183.864 179.451 178.165 1.00 9.31   ? 308  PHE A CD2 1 
ATOM   2308 C  CE1 . PHE A 1 398 ? 183.150 181.438 176.412 1.00 9.09   ? 308  PHE A CE1 1 
ATOM   2309 C  CE2 . PHE A 1 398 ? 183.111 179.152 177.056 1.00 9.57   ? 308  PHE A CE2 1 
ATOM   2310 C  CZ  . PHE A 1 398 ? 182.753 180.148 176.179 1.00 9.37   ? 308  PHE A CZ  1 
ATOM   2311 N  N   . LYS A 1 399 ? 187.890 181.389 181.327 1.00 8.82   ? 309  LYS A N   1 
ATOM   2312 C  CA  . LYS A 1 399 ? 188.747 182.191 182.193 1.00 8.90   ? 309  LYS A CA  1 
ATOM   2313 C  C   . LYS A 1 399 ? 190.097 182.463 181.535 1.00 9.02   ? 309  LYS A C   1 
ATOM   2314 O  O   . LYS A 1 399 ? 190.659 183.547 181.689 1.00 8.78   ? 309  LYS A O   1 
ATOM   2315 C  CB  . LYS A 1 399 ? 188.942 181.502 183.543 1.00 8.97   ? 309  LYS A CB  1 
ATOM   2316 C  CG  . LYS A 1 399 ? 187.717 181.532 184.453 1.00 9.09   ? 309  LYS A CG  1 
ATOM   2317 C  CD  . LYS A 1 399 ? 187.585 182.869 185.172 1.00 9.01   ? 309  LYS A CD  1 
ATOM   2318 C  CE  . LYS A 1 399 ? 186.348 182.902 186.060 1.00 9.23   ? 309  LYS A CE  1 
ATOM   2319 N  NZ  . LYS A 1 399 ? 186.367 184.060 186.998 1.00 9.22   ? 309  LYS A NZ  1 
ATOM   2320 N  N   . GLU A 1 400 ? 190.613 181.486 180.793 1.00 8.77   ? 310  GLU A N   1 
ATOM   2321 C  CA  . GLU A 1 400 ? 191.875 181.668 180.086 1.00 8.89   ? 310  GLU A CA  1 
ATOM   2322 C  C   . GLU A 1 400 ? 191.713 182.628 178.917 1.00 8.67   ? 310  GLU A C   1 
ATOM   2323 O  O   . GLU A 1 400 ? 192.612 183.419 178.622 1.00 8.54   ? 310  GLU A O   1 
ATOM   2324 C  CB  . GLU A 1 400 ? 192.429 180.326 179.607 1.00 9.11   ? 310  GLU A CB  1 
ATOM   2325 C  CG  . GLU A 1 400 ? 192.932 179.427 180.728 1.00 9.44   ? 310  GLU A CG  1 
ATOM   2326 C  CD  . GLU A 1 400 ? 194.057 180.044 181.515 1.00 9.55   ? 310  GLU A CD  1 
ATOM   2327 O  OE1 . GLU A 1 400 ? 194.985 180.520 180.913 1.00 9.57   ? 310  GLU A OE1 1 
ATOM   2328 O  OE2 . GLU A 1 400 ? 193.981 180.050 182.725 1.00 9.77   ? 310  GLU A OE2 1 
ATOM   2329 N  N   . ALA A 1 401 ? 190.558 182.578 178.257 1.00 8.51   ? 311  ALA A N   1 
ATOM   2330 C  CA  . ALA A 1 401 ? 190.274 183.518 177.181 1.00 8.34   ? 311  ALA A CA  1 
ATOM   2331 C  C   . ALA A 1 401 ? 190.242 184.938 177.730 1.00 8.46   ? 311  ALA A C   1 
ATOM   2332 O  O   . ALA A 1 401 ? 190.747 185.869 177.102 1.00 8.23   ? 311  ALA A O   1 
ATOM   2333 C  CB  . ALA A 1 401 ? 188.959 183.176 176.502 1.00 8.35   ? 311  ALA A CB  1 
ATOM   2334 N  N   . GLU A 1 402 ? 189.682 185.091 178.927 1.00 8.44   ? 312  GLU A N   1 
ATOM   2335 C  CA  . GLU A 1 402 ? 189.619 186.394 179.575 1.00 8.47   ? 312  GLU A CA  1 
ATOM   2336 C  C   . GLU A 1 402 ? 191.021 186.933 179.854 1.00 8.75   ? 312  GLU A C   1 
ATOM   2337 O  O   . GLU A 1 402 ? 191.297 188.104 179.606 1.00 8.45   ? 312  GLU A O   1 
ATOM   2338 C  CB  . GLU A 1 402 ? 188.806 186.302 180.871 1.00 8.67   ? 312  GLU A CB  1 
ATOM   2339 C  CG  . GLU A 1 402 ? 188.534 187.641 181.551 1.00 8.97   ? 312  GLU A CG  1 
ATOM   2340 C  CD  . GLU A 1 402 ? 187.689 187.503 182.788 1.00 9.21   ? 312  GLU A CD  1 
ATOM   2341 O  OE1 . GLU A 1 402 ? 188.056 186.743 183.649 1.00 9.32   ? 312  GLU A OE1 1 
ATOM   2342 O  OE2 . GLU A 1 402 ? 186.674 188.160 182.877 1.00 9.39   ? 312  GLU A OE2 1 
ATOM   2343 N  N   . LYS A 1 403 ? 191.914 186.066 180.332 1.00 8.48   ? 313  LYS A N   1 
ATOM   2344 C  CA  . LYS A 1 403 ? 193.295 186.464 180.607 1.00 8.56   ? 313  LYS A CA  1 
ATOM   2345 C  C   . LYS A 1 403 ? 193.998 186.968 179.355 1.00 8.67   ? 313  LYS A C   1 
ATOM   2346 O  O   . LYS A 1 403 ? 194.753 187.938 179.404 1.00 8.57   ? 313  LYS A O   1 
ATOM   2347 C  CB  . LYS A 1 403 ? 194.094 185.300 181.179 1.00 8.72   ? 313  LYS A CB  1 
ATOM   2348 C  CG  . LYS A 1 403 ? 193.738 184.911 182.587 1.00 8.95   ? 313  LYS A CG  1 
ATOM   2349 C  CD  . LYS A 1 403 ? 194.563 183.718 183.023 1.00 9.25   ? 313  LYS A CD  1 
ATOM   2350 C  CE  . LYS A 1 403 ? 194.164 183.227 184.395 1.00 9.71   ? 313  LYS A CE  1 
ATOM   2351 N  NZ  . LYS A 1 403 ? 194.885 181.977 184.753 1.00 9.96   ? 313  LYS A NZ  1 
ATOM   2352 N  N   . PHE A 1 404 ? 193.748 186.303 178.232 1.00 8.36   ? 314  PHE A N   1 
ATOM   2353 C  CA  . PHE A 1 404 ? 194.344 186.697 176.966 1.00 8.36   ? 314  PHE A CA  1 
ATOM   2354 C  C   . PHE A 1 404 ? 194.006 188.138 176.623 1.00 8.81   ? 314  PHE A C   1 
ATOM   2355 O  O   . PHE A 1 404 ? 194.893 188.934 176.317 1.00 8.48   ? 314  PHE A O   1 
ATOM   2356 C  CB  . PHE A 1 404 ? 193.870 185.776 175.843 1.00 8.39   ? 314  PHE A CB  1 
ATOM   2357 C  CG  . PHE A 1 404 ? 194.172 186.291 174.473 1.00 8.37   ? 314  PHE A CG  1 
ATOM   2358 C  CD1 . PHE A 1 404 ? 193.167 186.856 173.709 1.00 8.11   ? 314  PHE A CD1 1 
ATOM   2359 C  CD2 . PHE A 1 404 ? 195.449 186.227 173.945 1.00 8.66   ? 314  PHE A CD2 1 
ATOM   2360 C  CE1 . PHE A 1 404 ? 193.427 187.343 172.452 1.00 8.03   ? 314  PHE A CE1 1 
ATOM   2361 C  CE2 . PHE A 1 404 ? 195.713 186.717 172.682 1.00 8.65   ? 314  PHE A CE2 1 
ATOM   2362 C  CZ  . PHE A 1 404 ? 194.698 187.276 171.935 1.00 8.36   ? 314  PHE A CZ  1 
ATOM   2363 N  N   . TYR A 1 405 ? 192.731 188.482 176.703 1.00 8.11   ? 315  TYR A N   1 
ATOM   2364 C  CA  . TYR A 1 405 ? 192.302 189.833 176.366 1.00 8.32   ? 315  TYR A CA  1 
ATOM   2365 C  C   . TYR A 1 405 ? 192.823 190.853 177.374 1.00 8.96   ? 315  TYR A C   1 
ATOM   2366 O  O   . TYR A 1 405 ? 193.197 191.968 177.002 1.00 8.41   ? 315  TYR A O   1 
ATOM   2367 C  CB  . TYR A 1 405 ? 190.782 189.894 176.273 1.00 8.09   ? 315  TYR A CB  1 
ATOM   2368 C  CG  . TYR A 1 405 ? 190.245 189.204 175.055 1.00 7.91   ? 315  TYR A CG  1 
ATOM   2369 C  CD1 . TYR A 1 405 ? 190.413 189.779 173.819 1.00 7.79   ? 315  TYR A CD1 1 
ATOM   2370 C  CD2 . TYR A 1 405 ? 189.592 188.000 175.169 1.00 7.92   ? 315  TYR A CD2 1 
ATOM   2371 C  CE1 . TYR A 1 405 ? 189.939 189.163 172.702 1.00 7.61   ? 315  TYR A CE1 1 
ATOM   2372 C  CE2 . TYR A 1 405 ? 189.118 187.371 174.042 1.00 7.81   ? 315  TYR A CE2 1 
ATOM   2373 C  CZ  . TYR A 1 405 ? 189.292 187.954 172.811 1.00 7.67   ? 315  TYR A CZ  1 
ATOM   2374 O  OH  . TYR A 1 405 ? 188.831 187.342 171.681 1.00 7.61   ? 315  TYR A OH  1 
ATOM   2375 N  N   . LEU A 1 406 ? 192.906 190.461 178.635 1.00 8.57   ? 316  LEU A N   1 
ATOM   2376 C  CA  . LEU A 1 406 ? 193.420 191.365 179.653 1.00 8.79   ? 316  LEU A CA  1 
ATOM   2377 C  C   . LEU A 1 406 ? 194.888 191.697 179.419 1.00 8.81   ? 316  LEU A C   1 
ATOM   2378 O  O   . LEU A 1 406 ? 195.320 192.818 179.684 1.00 8.86   ? 316  LEU A O   1 
ATOM   2379 C  CB  . LEU A 1 406 ? 193.250 190.755 181.047 1.00 8.88   ? 316  LEU A CB  1 
ATOM   2380 C  CG  . LEU A 1 406 ? 191.806 190.636 181.555 1.00 9.17   ? 316  LEU A CG  1 
ATOM   2381 C  CD1 . LEU A 1 406 ? 191.789 189.804 182.819 1.00 9.34   ? 316  LEU A CD1 1 
ATOM   2382 C  CD2 . LEU A 1 406 ? 191.244 192.013 181.833 1.00 9.67   ? 316  LEU A CD2 1 
ATOM   2383 N  N   . SER A 1 407 ? 195.650 190.735 178.897 1.00 8.79   ? 317  SER A N   1 
ATOM   2384 C  CA  . SER A 1 407 ? 197.083 190.923 178.704 1.00 8.94   ? 317  SER A CA  1 
ATOM   2385 C  C   . SER A 1 407 ? 197.378 192.010 177.679 1.00 9.02   ? 317  SER A C   1 
ATOM   2386 O  O   . SER A 1 407 ? 198.502 192.502 177.595 1.00 9.18   ? 317  SER A O   1 
ATOM   2387 C  CB  . SER A 1 407 ? 197.753 189.632 178.260 1.00 9.05   ? 317  SER A CB  1 
ATOM   2388 O  OG  . SER A 1 407 ? 197.513 189.372 176.902 1.00 9.15   ? 317  SER A OG  1 
ATOM   2389 N  N   . VAL A 1 408 ? 196.368 192.376 176.889 1.00 8.84   ? 318  VAL A N   1 
ATOM   2390 C  CA  . VAL A 1 408 ? 196.568 193.378 175.854 1.00 8.89   ? 318  VAL A CA  1 
ATOM   2391 C  C   . VAL A 1 408 ? 195.800 194.662 176.153 1.00 8.76   ? 318  VAL A C   1 
ATOM   2392 O  O   . VAL A 1 408 ? 195.675 195.529 175.294 1.00 8.78   ? 318  VAL A O   1 
ATOM   2393 C  CB  . VAL A 1 408 ? 196.180 192.827 174.465 1.00 8.82   ? 318  VAL A CB  1 
ATOM   2394 C  CG1 . VAL A 1 408 ? 197.047 191.636 174.140 1.00 9.08   ? 318  VAL A CG1 1 
ATOM   2395 C  CG2 . VAL A 1 408 ? 194.714 192.439 174.419 1.00 8.63   ? 318  VAL A CG2 1 
ATOM   2396 N  N   . GLY A 1 409 ? 195.306 194.795 177.382 1.00 8.81   ? 319  GLY A N   1 
ATOM   2397 C  CA  . GLY A 1 409 ? 194.679 196.036 177.823 1.00 8.70   ? 319  GLY A CA  1 
ATOM   2398 C  C   . GLY A 1 409 ? 193.187 196.170 177.525 1.00 8.67   ? 319  GLY A C   1 
ATOM   2399 O  O   . GLY A 1 409 ? 192.661 197.284 177.511 1.00 8.84   ? 319  GLY A O   1 
ATOM   2400 N  N   . LEU A 1 410 ? 192.494 195.057 177.297 1.00 8.61   ? 320  LEU A N   1 
ATOM   2401 C  CA  . LEU A 1 410 ? 191.039 195.113 177.097 1.00 8.62   ? 320  LEU A CA  1 
ATOM   2402 C  C   . LEU A 1 410 ? 190.307 194.679 178.374 1.00 8.75   ? 320  LEU A C   1 
ATOM   2403 O  O   . LEU A 1 410 ? 190.952 194.334 179.357 1.00 9.07   ? 320  LEU A O   1 
ATOM   2404 C  CB  . LEU A 1 410 ? 190.618 194.268 175.894 1.00 8.36   ? 320  LEU A CB  1 
ATOM   2405 C  CG  . LEU A 1 410 ? 191.233 194.657 174.524 1.00 8.33   ? 320  LEU A CG  1 
ATOM   2406 C  CD1 . LEU A 1 410 ? 190.937 193.574 173.529 1.00 7.88   ? 320  LEU A CD1 1 
ATOM   2407 C  CD2 . LEU A 1 410 ? 190.643 195.964 174.041 1.00 8.18   ? 320  LEU A CD2 1 
ATOM   2408 N  N   . HIS A 1 411 ? 188.973 194.800 178.357 1.00 8.85   ? 321  HIS A N   1 
ATOM   2409 C  CA  . HIS A 1 411 ? 188.110 194.667 179.534 1.00 9.11   ? 321  HIS A CA  1 
ATOM   2410 C  C   . HIS A 1 411 ? 188.073 193.251 180.080 1.00 9.19   ? 321  HIS A C   1 
ATOM   2411 O  O   . HIS A 1 411 ? 188.153 192.271 179.303 1.00 9.01   ? 321  HIS A O   1 
ATOM   2412 C  CB  . HIS A 1 411 ? 186.680 195.056 179.173 1.00 8.88   ? 321  HIS A CB  1 
ATOM   2413 C  CG  . HIS A 1 411 ? 186.530 196.434 178.658 1.00 8.96   ? 321  HIS A CG  1 
ATOM   2414 N  ND1 . HIS A 1 411 ? 186.585 196.735 177.311 1.00 8.92   ? 321  HIS A ND1 1 
ATOM   2415 C  CD2 . HIS A 1 411 ? 186.323 197.600 179.293 1.00 9.24   ? 321  HIS A CD2 1 
ATOM   2416 C  CE1 . HIS A 1 411 ? 186.402 198.032 177.147 1.00 8.92   ? 321  HIS A CE1 1 
ATOM   2417 N  NE2 . HIS A 1 411 ? 186.242 198.586 178.331 1.00 9.37   ? 321  HIS A NE2 1 
ATOM   2418 N  N   . ASN A 1 412 ? 187.741 193.103 181.372 1.00 9.65   ? 322  ASN A N   1 
ATOM   2419 C  CA  . ASN A 1 412 ? 187.295 191.826 181.888 1.00 9.55   ? 322  ASN A CA  1 
ATOM   2420 C  C   . ASN A 1 412 ? 185.798 191.688 181.644 1.00 9.32   ? 322  ASN A C   1 
ATOM   2421 O  O   . ASN A 1 412 ? 185.121 192.694 181.377 1.00 9.31   ? 322  ASN A O   1 
ATOM   2422 C  CB  . ASN A 1 412 ? 187.606 191.609 183.382 1.00 9.89   ? 322  ASN A CB  1 
ATOM   2423 C  CG  . ASN A 1 412 ? 188.496 192.658 184.054 1.00 10.28  ? 322  ASN A CG  1 
ATOM   2424 O  OD1 . ASN A 1 412 ? 188.291 193.875 183.889 1.00 10.90  ? 322  ASN A OD1 1 
ATOM   2425 N  ND2 . ASN A 1 412 ? 189.466 192.152 184.820 1.00 10.97  ? 322  ASN A ND2 1 
ATOM   2426 N  N   . MET A 1 413 ? 185.286 190.469 181.778 1.00 9.42   ? 323  MET A N   1 
ATOM   2427 C  CA  . MET A 1 413 ? 183.850 190.213 181.666 1.00 9.39   ? 323  MET A CA  1 
ATOM   2428 C  C   . MET A 1 413 ? 183.183 190.670 182.947 1.00 9.43   ? 323  MET A C   1 
ATOM   2429 O  O   . MET A 1 413 ? 183.781 190.654 184.021 1.00 9.47   ? 323  MET A O   1 
ATOM   2430 C  CB  . MET A 1 413 ? 183.602 188.729 181.394 1.00 9.22   ? 323  MET A CB  1 
ATOM   2431 C  CG  . MET A 1 413 ? 184.169 188.207 180.093 1.00 9.04   ? 323  MET A CG  1 
ATOM   2432 S  SD  . MET A 1 413 ? 183.489 189.023 178.638 1.00 8.88   ? 323  MET A SD  1 
ATOM   2433 C  CE  . MET A 1 413 ? 184.810 190.147 178.191 1.00 8.64   ? 323  MET A CE  1 
ATOM   2434 N  N   . THR A 1 414 ? 181.948 191.120 182.835 1.00 9.46   ? 324  THR A N   1 
ATOM   2435 C  CA  . THR A 1 414 ? 181.233 191.630 183.980 1.00 9.52   ? 324  THR A CA  1 
ATOM   2436 C  C   . THR A 1 414 ? 180.880 190.481 184.938 1.00 9.73   ? 324  THR A C   1 
ATOM   2437 O  O   . THR A 1 414 ? 180.807 189.330 184.513 1.00 9.26   ? 324  THR A O   1 
ATOM   2438 C  CB  . THR A 1 414 ? 179.961 192.346 183.504 1.00 9.66   ? 324  THR A CB  1 
ATOM   2439 O  OG1 . THR A 1 414 ? 179.135 191.410 182.795 1.00 9.54   ? 324  THR A OG1 1 
ATOM   2440 C  CG2 . THR A 1 414 ? 180.340 193.494 182.559 1.00 9.31   ? 324  THR A CG2 1 
ATOM   2441 N  N   . PRO A 1 415 ? 180.652 190.774 186.229 1.00 9.61   ? 325  PRO A N   1 
ATOM   2442 C  CA  . PRO A 1 415 ? 180.117 189.872 187.236 1.00 9.67   ? 325  PRO A CA  1 
ATOM   2443 C  C   . PRO A 1 415 ? 178.831 189.202 186.774 1.00 9.87   ? 325  PRO A C   1 
ATOM   2444 O  O   . PRO A 1 415 ? 178.590 188.032 187.067 1.00 9.73   ? 325  PRO A O   1 
ATOM   2445 C  CB  . PRO A 1 415 ? 179.867 190.822 188.411 1.00 9.65   ? 325  PRO A CB  1 
ATOM   2446 C  CG  . PRO A 1 415 ? 180.923 191.890 188.253 1.00 9.70   ? 325  PRO A CG  1 
ATOM   2447 C  CD  . PRO A 1 415 ? 181.042 192.095 186.748 1.00 9.64   ? 325  PRO A CD  1 
ATOM   2448 N  N   . GLU A 1 416 ? 178.018 189.941 186.025 1.00 9.74   ? 326  GLU A N   1 
ATOM   2449 C  CA  . GLU A 1 416 ? 176.776 189.408 185.490 1.00 9.66   ? 326  GLU A CA  1 
ATOM   2450 C  C   . GLU A 1 416 ? 177.040 188.380 184.402 1.00 10.14  ? 326  GLU A C   1 
ATOM   2451 O  O   . GLU A 1 416 ? 176.388 187.343 184.350 1.00 10.01  ? 326  GLU A O   1 
ATOM   2452 C  CB  . GLU A 1 416 ? 175.906 190.534 184.945 1.00 9.78   ? 326  GLU A CB  1 
ATOM   2453 C  CG  . GLU A 1 416 ? 175.371 191.479 186.005 1.00 9.94   ? 326  GLU A CG  1 
ATOM   2454 C  CD  . GLU A 1 416 ? 176.387 192.490 186.451 1.00 10.09  ? 326  GLU A CD  1 
ATOM   2455 O  OE1 . GLU A 1 416 ? 177.453 192.519 185.885 1.00 9.86   ? 326  GLU A OE1 1 
ATOM   2456 O  OE2 . GLU A 1 416 ? 176.101 193.231 187.361 1.00 10.55  ? 326  GLU A OE2 1 
ATOM   2457 N  N   . PHE A 1 417 ? 178.022 188.650 183.550 1.00 9.61   ? 327  PHE A N   1 
ATOM   2458 C  CA  . PHE A 1 417 ? 178.344 187.738 182.455 1.00 9.48   ? 327  PHE A CA  1 
ATOM   2459 C  C   . PHE A 1 417 ? 178.562 186.331 182.974 1.00 9.81   ? 327  PHE A C   1 
ATOM   2460 O  O   . PHE A 1 417 ? 177.990 185.367 182.456 1.00 9.63   ? 327  PHE A O   1 
ATOM   2461 C  CB  . PHE A 1 417 ? 179.599 188.203 181.715 1.00 9.30   ? 327  PHE A CB  1 
ATOM   2462 C  CG  . PHE A 1 417 ? 180.159 187.191 180.751 1.00 9.16   ? 327  PHE A CG  1 
ATOM   2463 C  CD1 . PHE A 1 417 ? 181.072 186.236 181.186 1.00 9.15   ? 327  PHE A CD1 1 
ATOM   2464 C  CD2 . PHE A 1 417 ? 179.797 187.195 179.420 1.00 9.03   ? 327  PHE A CD2 1 
ATOM   2465 C  CE1 . PHE A 1 417 ? 181.596 185.311 180.318 1.00 9.02   ? 327  PHE A CE1 1 
ATOM   2466 C  CE2 . PHE A 1 417 ? 180.323 186.269 178.551 1.00 8.94   ? 327  PHE A CE2 1 
ATOM   2467 C  CZ  . PHE A 1 417 ? 181.222 185.324 179.003 1.00 8.99   ? 327  PHE A CZ  1 
ATOM   2468 N  N   . TRP A 1 418 ? 179.379 186.213 184.009 1.00 9.24   ? 328  TRP A N   1 
ATOM   2469 C  CA  . TRP A 1 418 ? 179.727 184.912 184.568 1.00 9.71   ? 328  TRP A CA  1 
ATOM   2470 C  C   . TRP A 1 418 ? 178.548 184.172 185.212 1.00 10.01  ? 328  TRP A C   1 
ATOM   2471 O  O   . TRP A 1 418 ? 178.635 182.964 185.436 1.00 10.47  ? 328  TRP A O   1 
ATOM   2472 C  CB  . TRP A 1 418 ? 180.858 185.062 185.589 1.00 9.47   ? 328  TRP A CB  1 
ATOM   2473 C  CG  . TRP A 1 418 ? 182.167 185.405 184.965 1.00 9.30   ? 328  TRP A CG  1 
ATOM   2474 C  CD1 . TRP A 1 418 ? 182.853 186.573 185.087 1.00 9.26   ? 328  TRP A CD1 1 
ATOM   2475 C  CD2 . TRP A 1 418 ? 182.956 184.568 184.096 1.00 9.10   ? 328  TRP A CD2 1 
ATOM   2476 N  NE1 . TRP A 1 418 ? 184.014 186.514 184.356 1.00 9.16   ? 328  TRP A NE1 1 
ATOM   2477 C  CE2 . TRP A 1 418 ? 184.088 185.299 183.742 1.00 9.04   ? 328  TRP A CE2 1 
ATOM   2478 C  CE3 . TRP A 1 418 ? 182.793 183.275 183.592 1.00 9.13   ? 328  TRP A CE3 1 
ATOM   2479 C  CZ2 . TRP A 1 418 ? 185.054 184.787 182.906 1.00 8.98   ? 328  TRP A CZ2 1 
ATOM   2480 C  CZ3 . TRP A 1 418 ? 183.766 182.761 182.754 1.00 8.97   ? 328  TRP A CZ3 1 
ATOM   2481 C  CH2 . TRP A 1 418 ? 184.866 183.502 182.421 1.00 8.93   ? 328  TRP A CH2 1 
ATOM   2482 N  N   . ASN A 1 419 ? 177.468 184.897 185.537 1.00 10.43  ? 329  ASN A N   1 
ATOM   2483 C  CA  . ASN A 1 419 ? 176.290 184.335 186.187 1.00 10.73  ? 329  ASN A CA  1 
ATOM   2484 C  C   . ASN A 1 419 ? 175.185 184.008 185.185 1.00 10.73  ? 329  ASN A C   1 
ATOM   2485 O  O   . ASN A 1 419 ? 174.514 182.984 185.292 1.00 10.90  ? 329  ASN A O   1 
ATOM   2486 C  CB  . ASN A 1 419 ? 175.781 185.284 187.266 1.00 11.69  ? 329  ASN A CB  1 
ATOM   2487 C  CG  . ASN A 1 419 ? 174.713 184.672 188.165 1.00 12.99  ? 329  ASN A CG  1 
ATOM   2488 O  OD1 . ASN A 1 419 ? 174.918 183.595 188.744 1.00 13.37  ? 329  ASN A OD1 1 
ATOM   2489 N  ND2 . ASN A 1 419 ? 173.584 185.345 188.289 1.00 13.63  ? 329  ASN A ND2 1 
ATOM   2490 N  N   . ASN A 1 420 ? 174.976 184.913 184.210 1.00 10.39  ? 330  ASN A N   1 
ATOM   2491 C  CA  . ASN A 1 420 ? 173.873 184.830 183.259 1.00 10.10  ? 330  ASN A CA  1 
ATOM   2492 C  C   . ASN A 1 420 ? 174.169 183.965 182.039 1.00 9.85   ? 330  ASN A C   1 
ATOM   2493 O  O   . ASN A 1 420 ? 173.253 183.411 181.429 1.00 9.98   ? 330  ASN A O   1 
ATOM   2494 C  CB  . ASN A 1 420 ? 173.479 186.220 182.820 1.00 9.94   ? 330  ASN A CB  1 
ATOM   2495 C  CG  . ASN A 1 420 ? 172.898 187.020 183.930 1.00 10.17  ? 330  ASN A CG  1 
ATOM   2496 O  OD1 . ASN A 1 420 ? 172.319 186.474 184.872 1.00 10.76  ? 330  ASN A OD1 1 
ATOM   2497 N  ND2 . ASN A 1 420 ? 173.040 188.313 183.850 1.00 9.82   ? 330  ASN A ND2 1 
ATOM   2498 N  N   . SER A 1 421 ? 175.440 183.859 181.664 1.00 9.96   ? 331  SER A N   1 
ATOM   2499 C  CA  . SER A 1 421 ? 175.818 183.107 180.472 1.00 9.85   ? 331  SER A CA  1 
ATOM   2500 C  C   . SER A 1 421 ? 175.580 181.613 180.626 1.00 10.04  ? 331  SER A C   1 
ATOM   2501 O  O   . SER A 1 421 ? 175.558 181.081 181.734 1.00 10.18  ? 331  SER A O   1 
ATOM   2502 C  CB  . SER A 1 421 ? 177.271 183.351 180.127 1.00 9.56   ? 331  SER A CB  1 
ATOM   2503 O  OG  . SER A 1 421 ? 177.473 184.670 179.701 1.00 9.32   ? 331  SER A OG  1 
ATOM   2504 N  N   . MET A 1 422 ? 175.417 180.937 179.494 1.00 10.14  ? 332  MET A N   1 
ATOM   2505 C  CA  . MET A 1 422 ? 175.279 179.486 179.467 1.00 10.41  ? 332  MET A CA  1 
ATOM   2506 C  C   . MET A 1 422 ? 176.501 178.897 178.783 1.00 10.54  ? 332  MET A C   1 
ATOM   2507 O  O   . MET A 1 422 ? 176.604 178.941 177.559 1.00 10.44  ? 332  MET A O   1 
ATOM   2508 C  CB  . MET A 1 422 ? 174.012 179.081 178.708 1.00 10.59  ? 332  MET A CB  1 
ATOM   2509 C  CG  . MET A 1 422 ? 173.700 177.581 178.732 1.00 11.38  ? 332  MET A CG  1 
ATOM   2510 S  SD  . MET A 1 422 ? 172.553 177.078 177.434 1.00 11.75  ? 332  MET A SD  1 
ATOM   2511 C  CE  . MET A 1 422 ? 173.704 176.677 176.117 1.00 11.36  ? 332  MET A CE  1 
ATOM   2512 N  N   . LEU A 1 423 ? 177.447 178.386 179.565 1.00 10.65  ? 333  LEU A N   1 
ATOM   2513 C  CA  . LEU A 1 423 ? 178.713 177.943 178.993 1.00 10.64  ? 333  LEU A CA  1 
ATOM   2514 C  C   . LEU A 1 423 ? 178.725 176.442 178.712 1.00 11.10  ? 333  LEU A C   1 
ATOM   2515 O  O   . LEU A 1 423 ? 179.549 175.961 177.934 1.00 10.82  ? 333  LEU A O   1 
ATOM   2516 C  CB  . LEU A 1 423 ? 179.879 178.325 179.919 1.00 10.54  ? 333  LEU A CB  1 
ATOM   2517 C  CG  . LEU A 1 423 ? 180.000 179.841 180.280 1.00 10.04  ? 333  LEU A CG  1 
ATOM   2518 C  CD1 . LEU A 1 423 ? 181.209 180.046 181.189 1.00 9.83   ? 333  LEU A CD1 1 
ATOM   2519 C  CD2 . LEU A 1 423 ? 180.125 180.684 179.011 1.00 9.76   ? 333  LEU A CD2 1 
ATOM   2520 N  N   . THR A 1 424 ? 177.812 175.707 179.341 1.00 11.35  ? 334  THR A N   1 
ATOM   2521 C  CA  . THR A 1 424 ? 177.703 174.267 179.128 1.00 11.71  ? 334  THR A CA  1 
ATOM   2522 C  C   . THR A 1 424 ? 176.266 173.878 178.822 1.00 12.20  ? 334  THR A C   1 
ATOM   2523 O  O   . THR A 1 424 ? 175.337 174.621 179.135 1.00 12.14  ? 334  THR A O   1 
ATOM   2524 C  CB  . THR A 1 424 ? 178.194 173.478 180.357 1.00 11.86  ? 334  THR A CB  1 
ATOM   2525 O  OG1 . THR A 1 424 ? 177.359 173.771 181.486 1.00 12.39  ? 334  THR A OG1 1 
ATOM   2526 C  CG2 . THR A 1 424 ? 179.627 173.858 180.678 1.00 11.52  ? 334  THR A CG2 1 
ATOM   2527 N  N   . GLU A 1 425 ? 176.075 172.698 178.241 1.00 12.63  ? 335  GLU A N   1 
ATOM   2528 C  CA  . GLU A 1 425 ? 174.731 172.201 177.963 1.00 12.96  ? 335  GLU A CA  1 
ATOM   2529 C  C   . GLU A 1 425 ? 174.026 171.825 179.269 1.00 13.48  ? 335  GLU A C   1 
ATOM   2530 O  O   . GLU A 1 425 ? 174.613 171.127 180.095 1.00 13.66  ? 335  GLU A O   1 
ATOM   2531 C  CB  . GLU A 1 425 ? 174.796 170.988 177.034 1.00 13.19  ? 335  GLU A CB  1 
ATOM   2532 C  CG  . GLU A 1 425 ? 173.443 170.503 176.538 1.00 13.41  ? 335  GLU A CG  1 
ATOM   2533 C  CD  . GLU A 1 425 ? 173.560 169.424 175.505 1.00 14.07  ? 335  GLU A CD  1 
ATOM   2534 O  OE1 . GLU A 1 425 ? 174.668 169.050 175.191 1.00 13.73  ? 335  GLU A OE1 1 
ATOM   2535 O  OE2 . GLU A 1 425 ? 172.548 168.975 175.024 1.00 14.15  ? 335  GLU A OE2 1 
ATOM   2536 N  N   . PRO A 1 426 ? 172.781 172.274 179.486 1.00 13.91  ? 336  PRO A N   1 
ATOM   2537 C  CA  . PRO A 1 426 ? 171.937 171.960 180.625 1.00 14.35  ? 336  PRO A CA  1 
ATOM   2538 C  C   . PRO A 1 426 ? 171.749 170.458 180.793 1.00 14.90  ? 336  PRO A C   1 
ATOM   2539 O  O   . PRO A 1 426 ? 171.574 169.732 179.817 1.00 14.77  ? 336  PRO A O   1 
ATOM   2540 C  CB  . PRO A 1 426 ? 170.621 172.645 180.252 1.00 14.53  ? 336  PRO A CB  1 
ATOM   2541 C  CG  . PRO A 1 426 ? 171.026 173.780 179.354 1.00 14.00  ? 336  PRO A CG  1 
ATOM   2542 C  CD  . PRO A 1 426 ? 172.195 173.251 178.554 1.00 13.41  ? 336  PRO A CD  1 
ATOM   2543 N  N   . SER A 1 427 ? 171.758 170.008 182.044 1.00 15.19  ? 337  SER A N   1 
ATOM   2544 C  CA  . SER A 1 427 ? 171.558 168.604 182.379 1.00 15.61  ? 337  SER A CA  1 
ATOM   2545 C  C   . SER A 1 427 ? 170.220 168.396 183.074 1.00 16.11  ? 337  SER A C   1 
ATOM   2546 O  O   . SER A 1 427 ? 169.938 167.326 183.606 1.00 16.35  ? 337  SER A O   1 
ATOM   2547 C  CB  . SER A 1 427 ? 172.671 168.130 183.290 1.00 15.74  ? 337  SER A CB  1 
ATOM   2548 N  N   . ASP A 1 428 ? 169.419 169.459 183.116 1.00 16.08  ? 338  ASP A N   1 
ATOM   2549 C  CA  . ASP A 1 428 ? 168.179 169.479 183.879 1.00 16.10  ? 338  ASP A CA  1 
ATOM   2550 C  C   . ASP A 1 428 ? 166.930 169.177 183.043 1.00 16.19  ? 338  ASP A C   1 
ATOM   2551 O  O   . ASP A 1 428 ? 165.811 169.290 183.532 1.00 16.40  ? 338  ASP A O   1 
ATOM   2552 C  CB  . ASP A 1 428 ? 168.031 170.842 184.547 1.00 16.25  ? 338  ASP A CB  1 
ATOM   2553 N  N   . GLY A 1 429 ? 167.133 168.766 181.794 1.00 15.84  ? 339  GLY A N   1 
ATOM   2554 C  CA  . GLY A 1 429 ? 166.020 168.415 180.917 1.00 15.93  ? 339  GLY A CA  1 
ATOM   2555 C  C   . GLY A 1 429 ? 165.695 169.501 179.891 1.00 15.76  ? 339  GLY A C   1 
ATOM   2556 O  O   . GLY A 1 429 ? 164.981 169.243 178.918 1.00 15.55  ? 339  GLY A O   1 
ATOM   2557 N  N   . ARG A 1 430 ? 166.230 170.701 180.086 1.00 15.74  ? 340  ARG A N   1 
ATOM   2558 C  CA  . ARG A 1 430 ? 165.949 171.791 179.154 1.00 14.98  ? 340  ARG A CA  1 
ATOM   2559 C  C   . ARG A 1 430 ? 166.496 171.518 177.765 1.00 14.81  ? 340  ARG A C   1 
ATOM   2560 O  O   . ARG A 1 430 ? 167.605 171.025 177.597 1.00 15.13  ? 340  ARG A O   1 
ATOM   2561 C  CB  . ARG A 1 430 ? 166.520 173.107 179.655 1.00 14.72  ? 340  ARG A CB  1 
ATOM   2562 C  CG  . ARG A 1 430 ? 165.723 173.768 180.769 1.00 14.93  ? 340  ARG A CG  1 
ATOM   2563 C  CD  . ARG A 1 430 ? 166.276 175.097 181.106 1.00 14.87  ? 340  ARG A CD  1 
ATOM   2564 N  NE  . ARG A 1 430 ? 167.478 174.995 181.905 1.00 15.20  ? 340  ARG A NE  1 
ATOM   2565 C  CZ  . ARG A 1 430 ? 168.556 175.801 181.808 1.00 15.17  ? 340  ARG A CZ  1 
ATOM   2566 N  NH1 . ARG A 1 430 ? 169.553 175.611 182.637 1.00 15.44  ? 340  ARG A NH1 1 
ATOM   2567 N  NH2 . ARG A 1 430 ? 168.617 176.763 180.896 1.00 14.57  ? 340  ARG A NH2 1 
ATOM   2568 N  N   . GLN A 1 431 ? 165.700 171.887 176.752 1.00 14.64  ? 341  GLN A N   1 
ATOM   2569 C  CA  . GLN A 1 431 ? 166.125 171.796 175.367 1.00 14.53  ? 341  GLN A CA  1 
ATOM   2570 C  C   . GLN A 1 431 ? 166.688 173.127 174.903 1.00 14.00  ? 341  GLN A C   1 
ATOM   2571 O  O   . GLN A 1 431 ? 166.052 174.168 175.078 1.00 13.63  ? 341  GLN A O   1 
ATOM   2572 C  CB  . GLN A 1 431 ? 164.966 171.377 174.468 1.00 14.56  ? 341  GLN A CB  1 
ATOM   2573 N  N   . VAL A 1 432 ? 167.886 173.099 174.343 1.00 13.90  ? 342  VAL A N   1 
ATOM   2574 C  CA  . VAL A 1 432 ? 168.527 174.318 173.891 1.00 13.13  ? 342  VAL A CA  1 
ATOM   2575 C  C   . VAL A 1 432 ? 169.096 174.170 172.501 1.00 12.95  ? 342  VAL A C   1 
ATOM   2576 O  O   . VAL A 1 432 ? 169.294 173.057 172.015 1.00 12.80  ? 342  VAL A O   1 
ATOM   2577 C  CB  . VAL A 1 432 ? 169.660 174.727 174.856 1.00 12.91  ? 342  VAL A CB  1 
ATOM   2578 C  CG1 . VAL A 1 432 ? 169.106 174.864 176.253 1.00 13.21  ? 342  VAL A CG1 1 
ATOM   2579 C  CG2 . VAL A 1 432 ? 170.789 173.710 174.810 1.00 12.79  ? 342  VAL A CG2 1 
ATOM   2580 N  N   . VAL A 1 433 ? 169.437 175.294 171.903 1.00 12.94  ? 343  VAL A N   1 
ATOM   2581 C  CA  . VAL A 1 433 ? 170.209 175.292 170.665 1.00 12.86  ? 343  VAL A CA  1 
ATOM   2582 C  C   . VAL A 1 433 ? 171.655 175.682 170.990 1.00 12.20  ? 343  VAL A C   1 
ATOM   2583 O  O   . VAL A 1 433 ? 171.928 176.788 171.478 1.00 12.10  ? 343  VAL A O   1 
ATOM   2584 C  CB  . VAL A 1 433 ? 169.577 176.262 169.648 1.00 12.82  ? 343  VAL A CB  1 
ATOM   2585 N  N   . CYS A 1 434 ? 172.588 174.721 170.804 1.00 12.00  ? 344  CYS A N   1 
ATOM   2586 C  CA  . CYS A 1 434 ? 173.962 174.847 171.265 1.00 12.21  ? 344  CYS A CA  1 
ATOM   2587 C  C   . CYS A 1 434 ? 174.799 175.768 170.367 1.00 11.79  ? 344  CYS A C   1 
ATOM   2588 O  O   . CYS A 1 434 ? 175.786 176.336 170.789 1.00 11.30  ? 344  CYS A O   1 
ATOM   2589 C  CB  . CYS A 1 434 ? 174.645 173.493 171.381 1.00 12.84  ? 344  CYS A CB  1 
ATOM   2590 S  SG  . CYS A 1 434 ? 174.136 172.513 172.828 1.00 13.12  ? 344  CYS A SG  1 
ATOM   2591 N  N   . HIS A 1 435 ? 174.385 175.907 169.116 1.00 11.58  ? 345  HIS A N   1 
ATOM   2592 C  CA  . HIS A 1 435 ? 175.143 176.741 168.201 1.00 11.00  ? 345  HIS A CA  1 
ATOM   2593 C  C   . HIS A 1 435 ? 175.640 177.994 168.925 1.00 10.85  ? 345  HIS A C   1 
ATOM   2594 O  O   . HIS A 1 435 ? 174.828 178.769 169.436 1.00 10.74  ? 345  HIS A O   1 
ATOM   2595 C  CB  . HIS A 1 435 ? 174.266 177.165 167.012 1.00 11.15  ? 345  HIS A CB  1 
ATOM   2596 C  CG  . HIS A 1 435 ? 175.014 177.869 165.936 1.00 10.98  ? 345  HIS A CG  1 
ATOM   2597 N  ND1 . HIS A 1 435 ? 175.846 177.205 165.060 1.00 11.09  ? 345  HIS A ND1 1 
ATOM   2598 C  CD2 . HIS A 1 435 ? 175.070 179.177 165.591 1.00 11.00  ? 345  HIS A CD2 1 
ATOM   2599 C  CE1 . HIS A 1 435 ? 176.373 178.076 164.217 1.00 11.00  ? 345  HIS A CE1 1 
ATOM   2600 N  NE2 . HIS A 1 435 ? 175.920 179.278 164.521 1.00 11.06  ? 345  HIS A NE2 1 
ATOM   2601 N  N   . PRO A 1 436 ? 176.956 178.189 169.008 1.00 10.64  ? 346  PRO A N   1 
ATOM   2602 C  CA  . PRO A 1 436 ? 177.619 179.214 169.790 1.00 10.22  ? 346  PRO A CA  1 
ATOM   2603 C  C   . PRO A 1 436 ? 177.342 180.610 169.261 1.00 9.95   ? 346  PRO A C   1 
ATOM   2604 O  O   . PRO A 1 436 ? 177.603 180.895 168.091 1.00 9.97   ? 346  PRO A O   1 
ATOM   2605 C  CB  . PRO A 1 436 ? 179.096 178.845 169.634 1.00 10.01  ? 346  PRO A CB  1 
ATOM   2606 C  CG  . PRO A 1 436 ? 179.172 178.072 168.338 1.00 10.04  ? 346  PRO A CG  1 
ATOM   2607 C  CD  . PRO A 1 436 ? 177.846 177.357 168.211 1.00 10.49  ? 346  PRO A CD  1 
ATOM   2608 N  N   . THR A 1 437 ? 176.853 181.487 170.136 1.00 9.73   ? 347  THR A N   1 
ATOM   2609 C  CA  . THR A 1 437 ? 176.599 182.876 169.768 1.00 9.74   ? 347  THR A CA  1 
ATOM   2610 C  C   . THR A 1 437 ? 176.958 183.844 170.891 1.00 9.45   ? 347  THR A C   1 
ATOM   2611 O  O   . THR A 1 437 ? 176.829 183.528 172.075 1.00 9.48   ? 347  THR A O   1 
ATOM   2612 C  CB  . THR A 1 437 ? 175.119 183.090 169.378 1.00 9.83   ? 347  THR A CB  1 
ATOM   2613 O  OG1 . THR A 1 437 ? 174.280 182.771 170.491 1.00 9.97   ? 347  THR A OG1 1 
ATOM   2614 C  CG2 . THR A 1 437 ? 174.734 182.210 168.194 1.00 10.21  ? 347  THR A CG2 1 
ATOM   2615 N  N   . ALA A 1 438 ? 177.332 185.058 170.510 1.00 9.30   ? 348  ALA A N   1 
ATOM   2616 C  CA  . ALA A 1 438 ? 177.585 186.128 171.468 1.00 9.02   ? 348  ALA A CA  1 
ATOM   2617 C  C   . ALA A 1 438 ? 176.413 187.099 171.477 1.00 8.99   ? 348  ALA A C   1 
ATOM   2618 O  O   . ALA A 1 438 ? 175.941 187.522 170.423 1.00 9.08   ? 348  ALA A O   1 
ATOM   2619 C  CB  . ALA A 1 438 ? 178.880 186.845 171.121 1.00 8.49   ? 348  ALA A CB  1 
ATOM   2620 N  N   . TRP A 1 439 ? 175.920 187.423 172.668 1.00 8.87   ? 349  TRP A N   1 
ATOM   2621 C  CA  . TRP A 1 439 ? 174.752 188.283 172.801 1.00 8.85   ? 349  TRP A CA  1 
ATOM   2622 C  C   . TRP A 1 439 ? 175.061 189.627 173.447 1.00 8.70   ? 349  TRP A C   1 
ATOM   2623 O  O   . TRP A 1 439 ? 175.716 189.698 174.488 1.00 8.53   ? 349  TRP A O   1 
ATOM   2624 C  CB  . TRP A 1 439 ? 173.695 187.590 173.661 1.00 9.01   ? 349  TRP A CB  1 
ATOM   2625 C  CG  . TRP A 1 439 ? 173.061 186.401 173.037 1.00 9.24   ? 349  TRP A CG  1 
ATOM   2626 C  CD1 . TRP A 1 439 ? 173.683 185.273 172.612 1.00 9.44   ? 349  TRP A CD1 1 
ATOM   2627 C  CD2 . TRP A 1 439 ? 171.655 186.196 172.794 1.00 9.56   ? 349  TRP A CD2 1 
ATOM   2628 N  NE1 . TRP A 1 439 ? 172.771 184.394 172.108 1.00 9.70   ? 349  TRP A NE1 1 
ATOM   2629 C  CE2 . TRP A 1 439 ? 171.524 184.936 172.216 1.00 9.77   ? 349  TRP A CE2 1 
ATOM   2630 C  CE3 . TRP A 1 439 ? 170.510 186.967 173.026 1.00 9.87   ? 349  TRP A CE3 1 
ATOM   2631 C  CZ2 . TRP A 1 439 ? 170.296 184.420 171.857 1.00 10.34  ? 349  TRP A CZ2 1 
ATOM   2632 C  CZ3 . TRP A 1 439 ? 169.277 186.447 172.669 1.00 10.40  ? 349  TRP A CZ3 1 
ATOM   2633 C  CH2 . TRP A 1 439 ? 169.176 185.205 172.099 1.00 10.56  ? 349  TRP A CH2 1 
ATOM   2634 N  N   . ASP A 1 440 ? 174.447 190.672 172.904 1.00 8.55   ? 350  ASP A N   1 
ATOM   2635 C  CA  . ASP A 1 440 ? 174.394 191.982 173.545 1.00 8.50   ? 350  ASP A CA  1 
ATOM   2636 C  C   . ASP A 1 440 ? 172.936 192.355 173.751 1.00 8.64   ? 350  ASP A C   1 
ATOM   2637 O  O   . ASP A 1 440 ? 172.214 192.609 172.787 1.00 8.68   ? 350  ASP A O   1 
ATOM   2638 C  CB  . ASP A 1 440 ? 175.086 193.062 172.712 1.00 8.36   ? 350  ASP A CB  1 
ATOM   2639 C  CG  . ASP A 1 440 ? 175.063 194.432 173.409 1.00 8.40   ? 350  ASP A CG  1 
ATOM   2640 O  OD1 . ASP A 1 440 ? 174.448 194.532 174.452 1.00 8.46   ? 350  ASP A OD1 1 
ATOM   2641 O  OD2 . ASP A 1 440 ? 175.629 195.365 172.884 1.00 8.20   ? 350  ASP A OD2 1 
ATOM   2642 N  N   . LEU A 1 441 ? 172.481 192.307 174.994 1.00 8.66   ? 351  LEU A N   1 
ATOM   2643 C  CA  . LEU A 1 441 ? 171.062 192.454 175.272 1.00 8.81   ? 351  LEU A CA  1 
ATOM   2644 C  C   . LEU A 1 441 ? 170.699 193.906 175.548 1.00 8.91   ? 351  LEU A C   1 
ATOM   2645 O  O   . LEU A 1 441 ? 169.524 194.245 175.678 1.00 9.16   ? 351  LEU A O   1 
ATOM   2646 C  CB  . LEU A 1 441 ? 170.666 191.584 176.473 1.00 8.93   ? 351  LEU A CB  1 
ATOM   2647 C  CG  . LEU A 1 441 ? 170.520 190.067 176.201 1.00 9.34   ? 351  LEU A CG  1 
ATOM   2648 C  CD1 . LEU A 1 441 ? 171.882 189.391 176.336 1.00 8.98   ? 351  LEU A CD1 1 
ATOM   2649 C  CD2 . LEU A 1 441 ? 169.519 189.474 177.172 1.00 9.76   ? 351  LEU A CD2 1 
ATOM   2650 N  N   . GLY A 1 442 ? 171.709 194.763 175.641 1.00 8.64   ? 352  GLY A N   1 
ATOM   2651 C  CA  . GLY A 1 442 ? 171.493 196.162 175.988 1.00 8.66   ? 352  GLY A CA  1 
ATOM   2652 C  C   . GLY A 1 442 ? 171.587 196.365 177.494 1.00 8.77   ? 352  GLY A C   1 
ATOM   2653 O  O   . GLY A 1 442 ? 171.650 195.402 178.255 1.00 8.67   ? 352  GLY A O   1 
ATOM   2654 N  N   . LYS A 1 443 ? 171.612 197.621 177.923 1.00 8.69   ? 353  LYS A N   1 
ATOM   2655 C  CA  . LYS A 1 443 ? 171.716 197.949 179.343 1.00 8.57   ? 353  LYS A CA  1 
ATOM   2656 C  C   . LYS A 1 443 ? 172.900 197.261 180.020 1.00 8.44   ? 353  LYS A C   1 
ATOM   2657 O  O   . LYS A 1 443 ? 172.782 196.783 181.147 1.00 8.44   ? 353  LYS A O   1 
ATOM   2658 C  CB  . LYS A 1 443 ? 170.431 197.581 180.084 1.00 8.87   ? 353  LYS A CB  1 
ATOM   2659 C  CG  . LYS A 1 443 ? 169.184 198.317 179.617 1.00 9.12   ? 353  LYS A CG  1 
ATOM   2660 C  CD  . LYS A 1 443 ? 168.029 198.055 180.572 1.00 9.40   ? 353  LYS A CD  1 
ATOM   2661 C  CE  . LYS A 1 443 ? 166.741 198.718 180.113 1.00 9.71   ? 353  LYS A CE  1 
ATOM   2662 N  NZ  . LYS A 1 443 ? 165.623 198.461 181.072 1.00 9.91   ? 353  LYS A NZ  1 
ATOM   2663 N  N   . ASN A 1 444 ? 174.045 197.236 179.344 1.00 8.33   ? 354  ASN A N   1 
ATOM   2664 C  CA  . ASN A 1 444 ? 175.261 196.643 179.897 1.00 8.15   ? 354  ASN A CA  1 
ATOM   2665 C  C   . ASN A 1 444 ? 175.076 195.173 180.265 1.00 8.22   ? 354  ASN A C   1 
ATOM   2666 O  O   . ASN A 1 444 ? 175.614 194.707 181.269 1.00 8.10   ? 354  ASN A O   1 
ATOM   2667 C  CB  . ASN A 1 444 ? 175.713 197.427 181.118 1.00 8.11   ? 354  ASN A CB  1 
ATOM   2668 C  CG  . ASN A 1 444 ? 177.158 197.204 181.476 1.00 8.05   ? 354  ASN A CG  1 
ATOM   2669 O  OD1 . ASN A 1 444 ? 178.024 197.102 180.602 1.00 8.23   ? 354  ASN A OD1 1 
ATOM   2670 N  ND2 . ASN A 1 444 ? 177.433 197.128 182.753 1.00 7.85   ? 354  ASN A ND2 1 
ATOM   2671 N  N   . ASP A 1 445 ? 174.337 194.439 179.441 1.00 8.33   ? 355  ASP A N   1 
ATOM   2672 C  CA  . ASP A 1 445 ? 174.090 193.024 179.688 1.00 8.51   ? 355  ASP A CA  1 
ATOM   2673 C  C   . ASP A 1 445 ? 174.656 192.164 178.560 1.00 8.63   ? 355  ASP A C   1 
ATOM   2674 O  O   . ASP A 1 445 ? 174.109 192.120 177.457 1.00 8.45   ? 355  ASP A O   1 
ATOM   2675 C  CB  . ASP A 1 445 ? 172.587 192.782 179.868 1.00 8.68   ? 355  ASP A CB  1 
ATOM   2676 C  CG  . ASP A 1 445 ? 172.231 191.355 180.269 1.00 9.05   ? 355  ASP A CG  1 
ATOM   2677 O  OD1 . ASP A 1 445 ? 173.049 190.487 180.103 1.00 9.06   ? 355  ASP A OD1 1 
ATOM   2678 O  OD2 . ASP A 1 445 ? 171.141 191.150 180.756 1.00 9.33   ? 355  ASP A OD2 1 
ATOM   2679 N  N   . PHE A 1 446 ? 175.783 191.514 178.831 1.00 8.39   ? 356  PHE A N   1 
ATOM   2680 C  CA  . PHE A 1 446 ? 176.482 190.729 177.819 1.00 8.46   ? 356  PHE A CA  1 
ATOM   2681 C  C   . PHE A 1 446 ? 176.493 189.257 178.207 1.00 8.77   ? 356  PHE A C   1 
ATOM   2682 O  O   . PHE A 1 446 ? 176.693 188.923 179.375 1.00 8.88   ? 356  PHE A O   1 
ATOM   2683 C  CB  . PHE A 1 446 ? 177.913 191.241 177.663 1.00 8.27   ? 356  PHE A CB  1 
ATOM   2684 C  CG  . PHE A 1 446 ? 177.985 192.688 177.292 1.00 8.06   ? 356  PHE A CG  1 
ATOM   2685 C  CD1 . PHE A 1 446 ? 177.858 193.094 175.977 1.00 7.99   ? 356  PHE A CD1 1 
ATOM   2686 C  CD2 . PHE A 1 446 ? 178.171 193.652 178.267 1.00 7.98   ? 356  PHE A CD2 1 
ATOM   2687 C  CE1 . PHE A 1 446 ? 177.913 194.434 175.650 1.00 7.77   ? 356  PHE A CE1 1 
ATOM   2688 C  CE2 . PHE A 1 446 ? 178.227 194.984 177.939 1.00 7.81   ? 356  PHE A CE2 1 
ATOM   2689 C  CZ  . PHE A 1 446 ? 178.097 195.375 176.630 1.00 7.61   ? 356  PHE A CZ  1 
ATOM   2690 N  N   . ARG A 1 447 ? 176.254 188.378 177.237 1.00 8.83   ? 357  ARG A N   1 
ATOM   2691 C  CA  . ARG A 1 447 ? 176.207 186.946 177.519 1.00 8.94   ? 357  ARG A CA  1 
ATOM   2692 C  C   . ARG A 1 447 ? 176.745 186.108 176.368 1.00 9.10   ? 357  ARG A C   1 
ATOM   2693 O  O   . ARG A 1 447 ? 176.661 186.505 175.208 1.00 8.90   ? 357  ARG A O   1 
ATOM   2694 C  CB  . ARG A 1 447 ? 174.777 186.506 177.803 1.00 9.20   ? 357  ARG A CB  1 
ATOM   2695 C  CG  . ARG A 1 447 ? 174.061 187.303 178.868 1.00 9.24   ? 357  ARG A CG  1 
ATOM   2696 C  CD  . ARG A 1 447 ? 172.712 186.775 179.142 1.00 9.55   ? 357  ARG A CD  1 
ATOM   2697 N  NE  . ARG A 1 447 ? 171.924 187.719 179.917 1.00 9.54   ? 357  ARG A NE  1 
ATOM   2698 C  CZ  . ARG A 1 447 ? 170.758 187.437 180.524 1.00 9.79   ? 357  ARG A CZ  1 
ATOM   2699 N  NH1 . ARG A 1 447 ? 170.259 186.228 180.464 1.00 9.90   ? 357  ARG A NH1 1 
ATOM   2700 N  NH2 . ARG A 1 447 ? 170.119 188.384 181.184 1.00 9.53   ? 357  ARG A NH2 1 
ATOM   2701 N  N   . ILE A 1 448 ? 177.223 184.912 176.686 1.00 9.08   ? 358  ILE A N   1 
ATOM   2702 C  CA  . ILE A 1 448 ? 177.538 183.920 175.662 1.00 9.19   ? 358  ILE A CA  1 
ATOM   2703 C  C   . ILE A 1 448 ? 176.723 182.651 175.855 1.00 9.50   ? 358  ILE A C   1 
ATOM   2704 O  O   . ILE A 1 448 ? 176.588 182.150 176.970 1.00 9.70   ? 358  ILE A O   1 
ATOM   2705 C  CB  . ILE A 1 448 ? 179.049 183.597 175.611 1.00 9.22   ? 358  ILE A CB  1 
ATOM   2706 C  CG1 . ILE A 1 448 ? 179.807 184.818 175.061 1.00 8.86   ? 358  ILE A CG1 1 
ATOM   2707 C  CG2 . ILE A 1 448 ? 179.314 182.346 174.758 1.00 9.38   ? 358  ILE A CG2 1 
ATOM   2708 C  CD1 . ILE A 1 448 ? 181.313 184.719 175.139 1.00 8.63   ? 358  ILE A CD1 1 
ATOM   2709 N  N   . LYS A 1 449 ? 176.169 182.149 174.757 1.00 9.73   ? 359  LYS A N   1 
ATOM   2710 C  CA  . LYS A 1 449 ? 175.434 180.893 174.760 1.00 10.08  ? 359  LYS A CA  1 
ATOM   2711 C  C   . LYS A 1 449 ? 176.202 179.841 173.976 1.00 10.27  ? 359  LYS A C   1 
ATOM   2712 O  O   . LYS A 1 449 ? 176.264 179.896 172.748 1.00 10.23  ? 359  LYS A O   1 
ATOM   2713 C  CB  . LYS A 1 449 ? 174.041 181.074 174.155 1.00 10.15  ? 359  LYS A CB  1 
ATOM   2714 C  CG  . LYS A 1 449 ? 173.212 179.795 174.116 1.00 10.53  ? 359  LYS A CG  1 
ATOM   2715 C  CD  . LYS A 1 449 ? 171.853 179.989 173.452 1.00 11.06  ? 359  LYS A CD  1 
ATOM   2716 C  CE  . LYS A 1 449 ? 171.976 180.392 171.976 1.00 11.12  ? 359  LYS A CE  1 
ATOM   2717 N  NZ  . LYS A 1 449 ? 172.936 179.524 171.227 1.00 10.96  ? 359  LYS A NZ  1 
ATOM   2718 N  N   . MET A 1 450 ? 176.807 178.900 174.690 1.00 10.35  ? 360  MET A N   1 
ATOM   2719 C  CA  . MET A 1 450 ? 177.641 177.877 174.072 1.00 10.57  ? 360  MET A CA  1 
ATOM   2720 C  C   . MET A 1 450 ? 177.570 176.574 174.870 1.00 10.99  ? 360  MET A C   1 
ATOM   2721 O  O   . MET A 1 450 ? 177.435 176.605 176.090 1.00 10.84  ? 360  MET A O   1 
ATOM   2722 C  CB  . MET A 1 450 ? 179.080 178.403 173.965 1.00 10.44  ? 360  MET A CB  1 
ATOM   2723 C  CG  . MET A 1 450 ? 180.106 177.434 173.391 1.00 10.59  ? 360  MET A CG  1 
ATOM   2724 S  SD  . MET A 1 450 ? 181.707 178.221 173.110 1.00 10.10  ? 360  MET A SD  1 
ATOM   2725 C  CE  . MET A 1 450 ? 182.741 176.797 172.805 1.00 9.92   ? 360  MET A CE  1 
ATOM   2726 N  N   . CYS A 1 451 ? 177.690 175.429 174.186 1.00 11.15  ? 361  CYS A N   1 
ATOM   2727 C  CA  . CYS A 1 451 ? 177.767 174.118 174.846 1.00 11.43  ? 361  CYS A CA  1 
ATOM   2728 C  C   . CYS A 1 451 ? 179.206 173.606 174.788 1.00 11.11  ? 361  CYS A C   1 
ATOM   2729 O  O   . CYS A 1 451 ? 179.588 172.881 173.868 1.00 11.09  ? 361  CYS A O   1 
ATOM   2730 C  CB  . CYS A 1 451 ? 176.810 173.103 174.192 1.00 12.05  ? 361  CYS A CB  1 
ATOM   2731 S  SG  . CYS A 1 451 ? 175.044 173.529 174.328 1.00 12.67  ? 361  CYS A SG  1 
ATOM   2732 N  N   . THR A 1 452 ? 180.017 174.045 175.745 1.00 11.00  ? 362  THR A N   1 
ATOM   2733 C  CA  . THR A 1 452 ? 181.458 173.859 175.671 1.00 10.80  ? 362  THR A CA  1 
ATOM   2734 C  C   . THR A 1 452 ? 181.909 172.462 176.072 1.00 10.75  ? 362  THR A C   1 
ATOM   2735 O  O   . THR A 1 452 ? 181.543 171.956 177.134 1.00 11.08  ? 362  THR A O   1 
ATOM   2736 C  CB  . THR A 1 452 ? 182.170 174.895 176.561 1.00 10.49  ? 362  THR A CB  1 
ATOM   2737 O  OG1 . THR A 1 452 ? 181.781 176.208 176.159 1.00 10.69  ? 362  THR A OG1 1 
ATOM   2738 C  CG2 . THR A 1 452 ? 183.686 174.770 176.434 1.00 10.41  ? 362  THR A CG2 1 
ATOM   2739 N  N   . LYS A 1 453 ? 182.758 171.873 175.235 1.00 10.92  ? 363  LYS A N   1 
ATOM   2740 C  CA  . LYS A 1 453 ? 183.418 170.607 175.526 1.00 10.89  ? 363  LYS A CA  1 
ATOM   2741 C  C   . LYS A 1 453 ? 184.891 170.867 175.808 1.00 10.87  ? 363  LYS A C   1 
ATOM   2742 O  O   . LYS A 1 453 ? 185.433 171.894 175.402 1.00 10.82  ? 363  LYS A O   1 
ATOM   2743 C  CB  . LYS A 1 453 ? 183.273 169.636 174.351 1.00 10.98  ? 363  LYS A CB  1 
ATOM   2744 C  CG  . LYS A 1 453 ? 181.839 169.370 173.916 1.00 11.05  ? 363  LYS A CG  1 
ATOM   2745 C  CD  . LYS A 1 453 ? 181.042 168.676 175.010 1.00 11.24  ? 363  LYS A CD  1 
ATOM   2746 C  CE  . LYS A 1 453 ? 179.719 168.134 174.483 1.00 11.75  ? 363  LYS A CE  1 
ATOM   2747 N  NZ  . LYS A 1 453 ? 178.792 169.222 174.076 1.00 11.82  ? 363  LYS A NZ  1 
ATOM   2748 N  N   . VAL A 1 454 ? 185.553 169.939 176.486 1.00 10.93  ? 364  VAL A N   1 
ATOM   2749 C  CA  . VAL A 1 454 ? 186.971 170.132 176.752 1.00 10.88  ? 364  VAL A CA  1 
ATOM   2750 C  C   . VAL A 1 454 ? 187.800 169.657 175.572 1.00 10.83  ? 364  VAL A C   1 
ATOM   2751 O  O   . VAL A 1 454 ? 188.389 168.578 175.601 1.00 11.09  ? 364  VAL A O   1 
ATOM   2752 C  CB  . VAL A 1 454 ? 187.389 169.392 178.034 1.00 11.19  ? 364  VAL A CB  1 
ATOM   2753 C  CG1 . VAL A 1 454 ? 188.854 169.678 178.366 1.00 11.02  ? 364  VAL A CG1 1 
ATOM   2754 C  CG2 . VAL A 1 454 ? 186.500 169.838 179.175 1.00 11.00  ? 364  VAL A CG2 1 
ATOM   2755 N  N   . THR A 1 455 ? 187.820 170.476 174.528 1.00 10.78  ? 365  THR A N   1 
ATOM   2756 C  CA  . THR A 1 455 ? 188.554 170.182 173.307 1.00 10.55  ? 365  THR A CA  1 
ATOM   2757 C  C   . THR A 1 455 ? 189.295 171.410 172.814 1.00 10.50  ? 365  THR A C   1 
ATOM   2758 O  O   . THR A 1 455 ? 189.000 172.531 173.228 1.00 10.24  ? 365  THR A O   1 
ATOM   2759 C  CB  . THR A 1 455 ? 187.615 169.695 172.189 1.00 10.52  ? 365  THR A CB  1 
ATOM   2760 O  OG1 . THR A 1 455 ? 186.763 170.778 171.782 1.00 10.36  ? 365  THR A OG1 1 
ATOM   2761 C  CG2 . THR A 1 455 ? 186.762 168.536 172.678 1.00 10.67  ? 365  THR A CG2 1 
ATOM   2762 N  N   . MET A 1 456 ? 190.236 171.205 171.901 1.00 10.48  ? 366  MET A N   1 
ATOM   2763 C  CA  . MET A 1 456 ? 190.965 172.325 171.322 1.00 10.34  ? 366  MET A CA  1 
ATOM   2764 C  C   . MET A 1 456 ? 190.059 173.193 170.458 1.00 10.09  ? 366  MET A C   1 
ATOM   2765 O  O   . MET A 1 456 ? 190.229 174.410 170.394 1.00 9.74   ? 366  MET A O   1 
ATOM   2766 C  CB  . MET A 1 456 ? 192.154 171.834 170.508 1.00 10.67  ? 366  MET A CB  1 
ATOM   2767 C  CG  . MET A 1 456 ? 193.065 172.952 170.017 1.00 10.53  ? 366  MET A CG  1 
ATOM   2768 S  SD  . MET A 1 456 ? 194.518 172.341 169.170 1.00 11.25  ? 366  MET A SD  1 
ATOM   2769 C  CE  . MET A 1 456 ? 195.415 173.858 168.897 1.00 11.17  ? 366  MET A CE  1 
ATOM   2770 N  N   . ASP A 1 457 ? 189.087 172.573 169.800 1.00 10.16  ? 367  ASP A N   1 
ATOM   2771 C  CA  . ASP A 1 457 ? 188.193 173.310 168.920 1.00 9.90   ? 367  ASP A CA  1 
ATOM   2772 C  C   . ASP A 1 457 ? 187.307 174.270 169.698 1.00 9.91   ? 367  ASP A C   1 
ATOM   2773 O  O   . ASP A 1 457 ? 187.104 175.412 169.283 1.00 9.65   ? 367  ASP A O   1 
ATOM   2774 C  CB  . ASP A 1 457 ? 187.318 172.344 168.127 1.00 10.29  ? 367  ASP A CB  1 
ATOM   2775 N  N   . ASP A 1 458 ? 186.801 173.822 170.843 1.00 9.86   ? 368  ASP A N   1 
ATOM   2776 C  CA  . ASP A 1 458 ? 185.972 174.688 171.671 1.00 9.79   ? 368  ASP A CA  1 
ATOM   2777 C  C   . ASP A 1 458 ? 186.813 175.723 172.403 1.00 9.67   ? 368  ASP A C   1 
ATOM   2778 O  O   . ASP A 1 458 ? 186.350 176.832 172.672 1.00 9.28   ? 368  ASP A O   1 
ATOM   2779 C  CB  . ASP A 1 458 ? 185.117 173.879 172.638 1.00 10.15  ? 368  ASP A CB  1 
ATOM   2780 C  CG  . ASP A 1 458 ? 183.937 173.214 171.935 1.00 10.43  ? 368  ASP A CG  1 
ATOM   2781 O  OD1 . ASP A 1 458 ? 183.738 173.478 170.773 1.00 10.33  ? 368  ASP A OD1 1 
ATOM   2782 O  OD2 . ASP A 1 458 ? 183.226 172.482 172.571 1.00 10.64  ? 368  ASP A OD2 1 
ATOM   2783 N  N   . PHE A 1 459 ? 188.063 175.380 172.682 1.00 9.48   ? 369  PHE A N   1 
ATOM   2784 C  CA  . PHE A 1 459 ? 188.999 176.323 173.272 1.00 9.33   ? 369  PHE A CA  1 
ATOM   2785 C  C   . PHE A 1 459 ? 189.138 177.549 172.379 1.00 9.18   ? 369  PHE A C   1 
ATOM   2786 O  O   . PHE A 1 459 ? 188.983 178.684 172.831 1.00 8.80   ? 369  PHE A O   1 
ATOM   2787 C  CB  . PHE A 1 459 ? 190.362 175.654 173.462 1.00 9.47   ? 369  PHE A CB  1 
ATOM   2788 C  CG  . PHE A 1 459 ? 191.444 176.547 173.958 1.00 9.32   ? 369  PHE A CG  1 
ATOM   2789 C  CD1 . PHE A 1 459 ? 191.562 176.837 175.302 1.00 9.47   ? 369  PHE A CD1 1 
ATOM   2790 C  CD2 . PHE A 1 459 ? 192.361 177.096 173.075 1.00 9.13   ? 369  PHE A CD2 1 
ATOM   2791 C  CE1 . PHE A 1 459 ? 192.570 177.659 175.753 1.00 9.36   ? 369  PHE A CE1 1 
ATOM   2792 C  CE2 . PHE A 1 459 ? 193.366 177.917 173.521 1.00 9.17   ? 369  PHE A CE2 1 
ATOM   2793 C  CZ  . PHE A 1 459 ? 193.469 178.199 174.862 1.00 9.29   ? 369  PHE A CZ  1 
ATOM   2794 N  N   . LEU A 1 460 ? 189.398 177.312 171.097 1.00 9.01   ? 370  LEU A N   1 
ATOM   2795 C  CA  . LEU A 1 460 ? 189.566 178.400 170.145 1.00 8.88   ? 370  LEU A CA  1 
ATOM   2796 C  C   . LEU A 1 460 ? 188.251 179.126 169.882 1.00 9.01   ? 370  LEU A C   1 
ATOM   2797 O  O   . LEU A 1 460 ? 188.237 180.344 169.696 1.00 8.47   ? 370  LEU A O   1 
ATOM   2798 C  CB  . LEU A 1 460 ? 190.149 177.855 168.838 1.00 9.05   ? 370  LEU A CB  1 
ATOM   2799 C  CG  . LEU A 1 460 ? 191.584 177.294 168.936 1.00 9.10   ? 370  LEU A CG  1 
ATOM   2800 C  CD1 . LEU A 1 460 ? 191.944 176.608 167.633 1.00 9.27   ? 370  LEU A CD1 1 
ATOM   2801 C  CD2 . LEU A 1 460 ? 192.562 178.426 169.243 1.00 8.88   ? 370  LEU A CD2 1 
ATOM   2802 N  N   . THR A 1 461 ? 187.145 178.389 169.900 1.00 8.85   ? 371  THR A N   1 
ATOM   2803 C  CA  . THR A 1 461 ? 185.834 178.997 169.718 1.00 8.77   ? 371  THR A CA  1 
ATOM   2804 C  C   . THR A 1 461 ? 185.544 179.993 170.836 1.00 8.84   ? 371  THR A C   1 
ATOM   2805 O  O   . THR A 1 461 ? 185.011 181.074 170.589 1.00 8.26   ? 371  THR A O   1 
ATOM   2806 C  CB  . THR A 1 461 ? 184.722 177.935 169.650 1.00 9.11   ? 371  THR A CB  1 
ATOM   2807 O  OG1 . THR A 1 461 ? 184.942 177.085 168.518 1.00 9.28   ? 371  THR A OG1 1 
ATOM   2808 C  CG2 . THR A 1 461 ? 183.359 178.600 169.514 1.00 9.10   ? 371  THR A CG2 1 
ATOM   2809 N  N   . ALA A 1 462 ? 185.914 179.641 172.065 1.00 8.69   ? 372  ALA A N   1 
ATOM   2810 C  CA  . ALA A 1 462 ? 185.695 180.528 173.202 1.00 8.69   ? 372  ALA A CA  1 
ATOM   2811 C  C   . ALA A 1 462 ? 186.376 181.874 172.987 1.00 8.27   ? 372  ALA A C   1 
ATOM   2812 O  O   . ALA A 1 462 ? 185.809 182.918 173.313 1.00 8.13   ? 372  ALA A O   1 
ATOM   2813 C  CB  . ALA A 1 462 ? 186.207 179.886 174.480 1.00 8.82   ? 372  ALA A CB  1 
ATOM   2814 N  N   . HIS A 1 463 ? 187.572 181.862 172.402 1.00 8.29   ? 373  HIS A N   1 
ATOM   2815 C  CA  . HIS A 1 463 ? 188.277 183.107 172.113 1.00 8.14   ? 373  HIS A CA  1 
ATOM   2816 C  C   . HIS A 1 463 ? 187.536 183.902 171.053 1.00 8.04   ? 373  HIS A C   1 
ATOM   2817 O  O   . HIS A 1 463 ? 187.422 185.123 171.143 1.00 7.77   ? 373  HIS A O   1 
ATOM   2818 C  CB  . HIS A 1 463 ? 189.708 182.836 171.641 1.00 8.17   ? 373  HIS A CB  1 
ATOM   2819 C  CG  . HIS A 1 463 ? 190.630 182.453 172.734 1.00 8.17   ? 373  HIS A CG  1 
ATOM   2820 N  ND1 . HIS A 1 463 ? 190.628 181.204 173.295 1.00 8.44   ? 373  HIS A ND1 1 
ATOM   2821 C  CD2 . HIS A 1 463 ? 191.588 183.153 173.377 1.00 8.14   ? 373  HIS A CD2 1 
ATOM   2822 C  CE1 . HIS A 1 463 ? 191.539 181.148 174.240 1.00 8.46   ? 373  HIS A CE1 1 
ATOM   2823 N  NE2 . HIS A 1 463 ? 192.140 182.316 174.309 1.00 8.35   ? 373  HIS A NE2 1 
ATOM   2824 N  N   . HIS A 1 464 ? 187.009 183.199 170.062 1.00 7.90   ? 374  HIS A N   1 
ATOM   2825 C  CA  . HIS A 1 464 ? 186.270 183.829 168.980 1.00 7.79   ? 374  HIS A CA  1 
ATOM   2826 C  C   . HIS A 1 464 ? 185.042 184.565 169.513 1.00 7.89   ? 374  HIS A C   1 
ATOM   2827 O  O   . HIS A 1 464 ? 184.822 185.737 169.204 1.00 7.66   ? 374  HIS A O   1 
ATOM   2828 C  CB  . HIS A 1 464 ? 185.830 182.769 167.967 1.00 7.82   ? 374  HIS A CB  1 
ATOM   2829 C  CG  . HIS A 1 464 ? 185.286 183.317 166.706 1.00 7.65   ? 374  HIS A CG  1 
ATOM   2830 N  ND1 . HIS A 1 464 ? 186.084 183.639 165.638 1.00 7.27   ? 374  HIS A ND1 1 
ATOM   2831 C  CD2 . HIS A 1 464 ? 184.020 183.603 166.328 1.00 7.90   ? 374  HIS A CD2 1 
ATOM   2832 C  CE1 . HIS A 1 464 ? 185.338 184.103 164.658 1.00 7.40   ? 374  HIS A CE1 1 
ATOM   2833 N  NE2 . HIS A 1 464 ? 184.082 184.088 165.049 1.00 7.70   ? 374  HIS A NE2 1 
ATOM   2834 N  N   . GLU A 1 465 ? 184.245 183.871 170.324 1.00 7.96   ? 375  GLU A N   1 
ATOM   2835 C  CA  . GLU A 1 465 ? 183.002 184.433 170.836 1.00 7.99   ? 375  GLU A CA  1 
ATOM   2836 C  C   . GLU A 1 465 ? 183.249 185.572 171.811 1.00 8.28   ? 375  GLU A C   1 
ATOM   2837 O  O   . GLU A 1 465 ? 182.512 186.558 171.822 1.00 7.84   ? 375  GLU A O   1 
ATOM   2838 C  CB  . GLU A 1 465 ? 182.151 183.350 171.494 1.00 8.34   ? 375  GLU A CB  1 
ATOM   2839 C  CG  . GLU A 1 465 ? 181.579 182.336 170.520 1.00 8.67   ? 375  GLU A CG  1 
ATOM   2840 C  CD  . GLU A 1 465 ? 180.762 182.973 169.431 1.00 8.82   ? 375  GLU A CD  1 
ATOM   2841 O  OE1 . GLU A 1 465 ? 180.080 183.928 169.710 1.00 8.82   ? 375  GLU A OE1 1 
ATOM   2842 O  OE2 . GLU A 1 465 ? 180.827 182.515 168.318 1.00 8.87   ? 375  GLU A OE2 1 
ATOM   2843 N  N   . MET A 1 466 ? 184.299 185.459 172.615 1.00 7.89   ? 376  MET A N   1 
ATOM   2844 C  CA  . MET A 1 466 ? 184.613 186.523 173.552 1.00 7.88   ? 376  MET A CA  1 
ATOM   2845 C  C   . MET A 1 466 ? 185.098 187.766 172.816 1.00 7.66   ? 376  MET A C   1 
ATOM   2846 O  O   . MET A 1 466 ? 184.907 188.884 173.294 1.00 7.56   ? 376  MET A O   1 
ATOM   2847 C  CB  . MET A 1 466 ? 185.617 186.052 174.594 1.00 7.94   ? 376  MET A CB  1 
ATOM   2848 C  CG  . MET A 1 466 ? 185.804 187.034 175.752 1.00 8.12   ? 376  MET A CG  1 
ATOM   2849 S  SD  . MET A 1 466 ? 186.783 186.369 177.109 1.00 8.37   ? 376  MET A SD  1 
ATOM   2850 C  CE  . MET A 1 466 ? 185.633 185.234 177.873 1.00 8.54   ? 376  MET A CE  1 
ATOM   2851 N  N   . GLY A 1 467 ? 185.701 187.576 171.642 1.00 7.60   ? 377  GLY A N   1 
ATOM   2852 C  CA  . GLY A 1 467 ? 186.129 188.696 170.810 1.00 7.53   ? 377  GLY A CA  1 
ATOM   2853 C  C   . GLY A 1 467 ? 184.937 189.541 170.374 1.00 7.47   ? 377  GLY A C   1 
ATOM   2854 O  O   . GLY A 1 467 ? 185.031 190.767 170.292 1.00 7.32   ? 377  GLY A O   1 
ATOM   2855 N  N   . HIS A 1 468 ? 183.805 188.886 170.129 1.00 7.41   ? 378  HIS A N   1 
ATOM   2856 C  CA  . HIS A 1 468 ? 182.589 189.600 169.759 1.00 7.38   ? 378  HIS A CA  1 
ATOM   2857 C  C   . HIS A 1 468 ? 182.075 190.419 170.931 1.00 7.66   ? 378  HIS A C   1 
ATOM   2858 O  O   . HIS A 1 468 ? 181.649 191.559 170.760 1.00 7.13   ? 378  HIS A O   1 
ATOM   2859 C  CB  . HIS A 1 468 ? 181.496 188.632 169.297 1.00 7.45   ? 378  HIS A CB  1 
ATOM   2860 C  CG  . HIS A 1 468 ? 181.743 188.035 167.956 1.00 7.46   ? 378  HIS A CG  1 
ATOM   2861 N  ND1 . HIS A 1 468 ? 181.733 188.778 166.803 1.00 7.05   ? 378  HIS A ND1 1 
ATOM   2862 C  CD2 . HIS A 1 468 ? 182.005 186.767 167.581 1.00 7.88   ? 378  HIS A CD2 1 
ATOM   2863 C  CE1 . HIS A 1 468 ? 181.983 187.991 165.775 1.00 7.40   ? 378  HIS A CE1 1 
ATOM   2864 N  NE2 . HIS A 1 468 ? 182.151 186.768 166.223 1.00 7.86   ? 378  HIS A NE2 1 
ATOM   2865 N  N   . ILE A 1 469 ? 182.162 189.854 172.130 1.00 7.48   ? 379  ILE A N   1 
ATOM   2866 C  CA  . ILE A 1 469 ? 181.738 190.565 173.328 1.00 7.50   ? 379  ILE A CA  1 
ATOM   2867 C  C   . ILE A 1 469 ? 182.609 191.795 173.557 1.00 7.40   ? 379  ILE A C   1 
ATOM   2868 O  O   . ILE A 1 469 ? 182.108 192.854 173.933 1.00 7.24   ? 379  ILE A O   1 
ATOM   2869 C  CB  . ILE A 1 469 ? 181.773 189.658 174.577 1.00 7.70   ? 379  ILE A CB  1 
ATOM   2870 C  CG1 . ILE A 1 469 ? 180.781 188.472 174.432 1.00 7.87   ? 379  ILE A CG1 1 
ATOM   2871 C  CG2 . ILE A 1 469 ? 181.450 190.479 175.821 1.00 7.84   ? 379  ILE A CG2 1 
ATOM   2872 C  CD1 . ILE A 1 469 ? 179.311 188.856 174.327 1.00 8.20   ? 379  ILE A CD1 1 
ATOM   2873 N  N   . GLN A 1 470 ? 183.914 191.657 173.328 1.00 7.39   ? 380  GLN A N   1 
ATOM   2874 C  CA  . GLN A 1 470 ? 184.841 192.771 173.504 1.00 7.39   ? 380  GLN A CA  1 
ATOM   2875 C  C   . GLN A 1 470 ? 184.491 193.939 172.586 1.00 7.24   ? 380  GLN A C   1 
ATOM   2876 O  O   . GLN A 1 470 ? 184.583 195.101 172.980 1.00 7.17   ? 380  GLN A O   1 
ATOM   2877 C  CB  . GLN A 1 470 ? 186.277 192.324 173.205 1.00 7.50   ? 380  GLN A CB  1 
ATOM   2878 C  CG  . GLN A 1 470 ? 186.897 191.393 174.231 1.00 7.65   ? 380  GLN A CG  1 
ATOM   2879 C  CD  . GLN A 1 470 ? 187.199 192.092 175.536 1.00 7.94   ? 380  GLN A CD  1 
ATOM   2880 O  OE1 . GLN A 1 470 ? 187.264 193.324 175.593 1.00 8.07   ? 380  GLN A OE1 1 
ATOM   2881 N  NE2 . GLN A 1 470 ? 187.396 191.315 176.593 1.00 8.08   ? 380  GLN A NE2 1 
ATOM   2882 N  N   . TYR A 1 471 ? 184.082 193.621 171.366 1.00 7.03   ? 381  TYR A N   1 
ATOM   2883 C  CA  . TYR A 1 471 ? 183.718 194.634 170.385 1.00 6.92   ? 381  TYR A CA  1 
ATOM   2884 C  C   . TYR A 1 471 ? 182.410 195.312 170.798 1.00 6.93   ? 381  TYR A C   1 
ATOM   2885 O  O   . TYR A 1 471 ? 182.287 196.537 170.745 1.00 6.86   ? 381  TYR A O   1 
ATOM   2886 C  CB  . TYR A 1 471 ? 183.625 193.975 169.006 1.00 6.77   ? 381  TYR A CB  1 
ATOM   2887 C  CG  . TYR A 1 471 ? 183.658 194.895 167.792 1.00 6.57   ? 381  TYR A CG  1 
ATOM   2888 C  CD1 . TYR A 1 471 ? 183.698 194.318 166.539 1.00 6.45   ? 381  TYR A CD1 1 
ATOM   2889 C  CD2 . TYR A 1 471 ? 183.666 196.276 167.906 1.00 6.49   ? 381  TYR A CD2 1 
ATOM   2890 C  CE1 . TYR A 1 471 ? 183.740 195.096 165.410 1.00 6.41   ? 381  TYR A CE1 1 
ATOM   2891 C  CE2 . TYR A 1 471 ? 183.708 197.054 166.765 1.00 6.40   ? 381  TYR A CE2 1 
ATOM   2892 C  CZ  . TYR A 1 471 ? 183.744 196.468 165.527 1.00 6.30   ? 381  TYR A CZ  1 
ATOM   2893 O  OH  . TYR A 1 471 ? 183.787 197.250 164.398 1.00 6.18   ? 381  TYR A OH  1 
ATOM   2894 N  N   . ASP A 1 472 ? 181.446 194.513 171.254 1.00 6.94   ? 382  ASP A N   1 
ATOM   2895 C  CA  . ASP A 1 472 ? 180.159 195.033 171.695 1.00 7.11   ? 382  ASP A CA  1 
ATOM   2896 C  C   . ASP A 1 472 ? 180.319 195.990 172.870 1.00 7.16   ? 382  ASP A C   1 
ATOM   2897 O  O   . ASP A 1 472 ? 179.651 197.020 172.942 1.00 6.99   ? 382  ASP A O   1 
ATOM   2898 C  CB  . ASP A 1 472 ? 179.233 193.890 172.115 1.00 7.25   ? 382  ASP A CB  1 
ATOM   2899 C  CG  . ASP A 1 472 ? 178.723 193.046 170.962 1.00 7.33   ? 382  ASP A CG  1 
ATOM   2900 O  OD1 . ASP A 1 472 ? 178.760 193.496 169.846 1.00 7.11   ? 382  ASP A OD1 1 
ATOM   2901 O  OD2 . ASP A 1 472 ? 178.302 191.944 171.214 1.00 7.70   ? 382  ASP A OD2 1 
ATOM   2902 N  N   . MET A 1 473 ? 181.220 195.653 173.788 1.00 7.16   ? 383  MET A N   1 
ATOM   2903 C  CA  . MET A 1 473 ? 181.487 196.505 174.940 1.00 7.22   ? 383  MET A CA  1 
ATOM   2904 C  C   . MET A 1 473 ? 182.170 197.802 174.523 1.00 7.16   ? 383  MET A C   1 
ATOM   2905 O  O   . MET A 1 473 ? 181.865 198.872 175.050 1.00 7.19   ? 383  MET A O   1 
ATOM   2906 C  CB  . MET A 1 473 ? 182.344 195.755 175.959 1.00 7.45   ? 383  MET A CB  1 
ATOM   2907 C  CG  . MET A 1 473 ? 181.631 194.600 176.653 1.00 7.56   ? 383  MET A CG  1 
ATOM   2908 S  SD  . MET A 1 473 ? 182.729 193.563 177.642 1.00 7.81   ? 383  MET A SD  1 
ATOM   2909 C  CE  . MET A 1 473 ? 183.011 194.575 179.082 1.00 8.44   ? 383  MET A CE  1 
ATOM   2910 N  N   . ALA A 1 474 ? 183.084 197.708 173.563 1.00 7.05   ? 384  ALA A N   1 
ATOM   2911 C  CA  . ALA A 1 474 ? 183.879 198.855 173.141 1.00 7.03   ? 384  ALA A CA  1 
ATOM   2912 C  C   . ALA A 1 474 ? 183.025 200.014 172.639 1.00 6.91   ? 384  ALA A C   1 
ATOM   2913 O  O   . ALA A 1 474 ? 183.326 201.171 172.931 1.00 6.99   ? 384  ALA A O   1 
ATOM   2914 C  CB  . ALA A 1 474 ? 184.850 198.437 172.049 1.00 6.87   ? 384  ALA A CB  1 
ATOM   2915 N  N   . TYR A 1 475 ? 181.955 199.722 171.903 1.00 6.87   ? 385  TYR A N   1 
ATOM   2916 C  CA  . TYR A 1 475 ? 181.132 200.800 171.358 1.00 6.88   ? 385  TYR A CA  1 
ATOM   2917 C  C   . TYR A 1 475 ? 179.817 200.970 172.104 1.00 7.00   ? 385  TYR A C   1 
ATOM   2918 O  O   . TYR A 1 475 ? 178.872 201.561 171.585 1.00 6.94   ? 385  TYR A O   1 
ATOM   2919 C  CB  . TYR A 1 475 ? 180.863 200.624 169.855 1.00 6.70   ? 385  TYR A CB  1 
ATOM   2920 C  CG  . TYR A 1 475 ? 180.235 199.311 169.408 1.00 6.62   ? 385  TYR A CG  1 
ATOM   2921 C  CD1 . TYR A 1 475 ? 180.941 198.471 168.571 1.00 6.55   ? 385  TYR A CD1 1 
ATOM   2922 C  CD2 . TYR A 1 475 ? 178.958 198.957 169.810 1.00 6.64   ? 385  TYR A CD2 1 
ATOM   2923 C  CE1 . TYR A 1 475 ? 180.373 197.297 168.131 1.00 6.59   ? 385  TYR A CE1 1 
ATOM   2924 C  CE2 . TYR A 1 475 ? 178.401 197.779 169.376 1.00 6.67   ? 385  TYR A CE2 1 
ATOM   2925 C  CZ  . TYR A 1 475 ? 179.102 196.957 168.537 1.00 6.62   ? 385  TYR A CZ  1 
ATOM   2926 O  OH  . TYR A 1 475 ? 178.541 195.790 168.097 1.00 6.64   ? 385  TYR A OH  1 
ATOM   2927 N  N   . ALA A 1 476 ? 179.758 200.482 173.336 1.00 7.01   ? 386  ALA A N   1 
ATOM   2928 C  CA  . ALA A 1 476 ? 178.544 200.583 174.139 1.00 7.10   ? 386  ALA A CA  1 
ATOM   2929 C  C   . ALA A 1 476 ? 178.189 202.037 174.441 1.00 7.19   ? 386  ALA A C   1 
ATOM   2930 O  O   . ALA A 1 476 ? 177.066 202.337 174.843 1.00 7.23   ? 386  ALA A O   1 
ATOM   2931 C  CB  . ALA A 1 476 ? 178.710 199.809 175.434 1.00 7.13   ? 386  ALA A CB  1 
ATOM   2932 N  N   . LYS A 1 477 ? 179.156 202.933 174.273 1.00 7.15   ? 387  LYS A N   1 
ATOM   2933 C  CA  . LYS A 1 477 ? 178.966 204.353 174.549 1.00 7.16   ? 387  LYS A CA  1 
ATOM   2934 C  C   . LYS A 1 477 ? 178.309 205.101 173.387 1.00 7.18   ? 387  LYS A C   1 
ATOM   2935 O  O   . LYS A 1 477 ? 177.950 206.270 173.523 1.00 7.22   ? 387  LYS A O   1 
ATOM   2936 C  CB  . LYS A 1 477 ? 180.304 205.006 174.895 1.00 7.29   ? 387  LYS A CB  1 
ATOM   2937 C  CG  . LYS A 1 477 ? 181.284 205.106 173.729 1.00 7.28   ? 387  LYS A CG  1 
ATOM   2938 C  CD  . LYS A 1 477 ? 182.601 205.725 174.171 1.00 7.51   ? 387  LYS A CD  1 
ATOM   2939 C  CE  . LYS A 1 477 ? 183.601 205.783 173.026 1.00 7.42   ? 387  LYS A CE  1 
ATOM   2940 N  NZ  . LYS A 1 477 ? 184.905 206.359 173.459 1.00 7.75   ? 387  LYS A NZ  1 
ATOM   2941 N  N   . GLN A 1 478 ? 178.178 204.441 172.241 1.00 7.12   ? 388  GLN A N   1 
ATOM   2942 C  CA  . GLN A 1 478 ? 177.588 205.064 171.062 1.00 7.17   ? 388  GLN A CA  1 
ATOM   2943 C  C   . GLN A 1 478 ? 176.064 205.126 171.202 1.00 7.26   ? 388  GLN A C   1 
ATOM   2944 O  O   . GLN A 1 478 ? 175.489 204.356 171.970 1.00 7.30   ? 388  GLN A O   1 
ATOM   2945 C  CB  . GLN A 1 478 ? 177.964 204.280 169.796 1.00 7.06   ? 388  GLN A CB  1 
ATOM   2946 C  CG  . GLN A 1 478 ? 179.456 204.246 169.475 1.00 6.89   ? 388  GLN A CG  1 
ATOM   2947 C  CD  . GLN A 1 478 ? 180.019 205.604 169.123 1.00 6.75   ? 388  GLN A CD  1 
ATOM   2948 O  OE1 . GLN A 1 478 ? 179.273 206.546 168.851 1.00 6.95   ? 388  GLN A OE1 1 
ATOM   2949 N  NE2 . GLN A 1 478 ? 181.342 205.715 169.121 1.00 6.70   ? 388  GLN A NE2 1 
ATOM   2950 N  N   . PRO A 1 479 ? 175.395 206.032 170.479 1.00 7.28   ? 389  PRO A N   1 
ATOM   2951 C  CA  . PRO A 1 479 ? 173.955 206.097 170.301 1.00 7.56   ? 389  PRO A CA  1 
ATOM   2952 C  C   . PRO A 1 479 ? 173.437 204.758 169.804 1.00 7.64   ? 389  PRO A C   1 
ATOM   2953 O  O   . PRO A 1 479 ? 174.119 204.076 169.045 1.00 7.37   ? 389  PRO A O   1 
ATOM   2954 C  CB  . PRO A 1 479 ? 173.803 207.200 169.250 1.00 7.68   ? 389  PRO A CB  1 
ATOM   2955 C  CG  . PRO A 1 479 ? 175.014 208.080 169.455 1.00 7.59   ? 389  PRO A CG  1 
ATOM   2956 C  CD  . PRO A 1 479 ? 176.131 207.127 169.837 1.00 7.31   ? 389  PRO A CD  1 
ATOM   2957 N  N   . TYR A 1 480 ? 172.241 204.385 170.238 1.00 7.89   ? 390  TYR A N   1 
ATOM   2958 C  CA  . TYR A 1 480 ? 171.684 203.067 169.946 1.00 7.92   ? 390  TYR A CA  1 
ATOM   2959 C  C   . TYR A 1 480 ? 171.841 202.649 168.486 1.00 7.89   ? 390  TYR A C   1 
ATOM   2960 O  O   . TYR A 1 480 ? 172.269 201.531 168.198 1.00 7.75   ? 390  TYR A O   1 
ATOM   2961 C  CB  . TYR A 1 480 ? 170.206 203.029 170.339 1.00 8.38   ? 390  TYR A CB  1 
ATOM   2962 C  CG  . TYR A 1 480 ? 169.527 201.741 169.982 1.00 8.56   ? 390  TYR A CG  1 
ATOM   2963 C  CD1 . TYR A 1 480 ? 169.670 200.635 170.798 1.00 8.67   ? 390  TYR A CD1 1 
ATOM   2964 C  CD2 . TYR A 1 480 ? 168.768 201.659 168.828 1.00 8.53   ? 390  TYR A CD2 1 
ATOM   2965 C  CE1 . TYR A 1 480 ? 169.059 199.450 170.459 1.00 8.93   ? 390  TYR A CE1 1 
ATOM   2966 C  CE2 . TYR A 1 480 ? 168.160 200.476 168.490 1.00 8.79   ? 390  TYR A CE2 1 
ATOM   2967 C  CZ  . TYR A 1 480 ? 168.305 199.374 169.298 1.00 9.12   ? 390  TYR A CZ  1 
ATOM   2968 O  OH  . TYR A 1 480 ? 167.702 198.191 168.958 1.00 9.69   ? 390  TYR A OH  1 
ATOM   2969 N  N   . LEU A 1 481 ? 171.493 203.535 167.564 1.00 7.97   ? 391  LEU A N   1 
ATOM   2970 C  CA  . LEU A 1 481 ? 171.498 203.197 166.143 1.00 7.97   ? 391  LEU A CA  1 
ATOM   2971 C  C   . LEU A 1 481 ? 172.903 202.996 165.586 1.00 7.71   ? 391  LEU A C   1 
ATOM   2972 O  O   . LEU A 1 481 ? 173.073 202.429 164.505 1.00 7.69   ? 391  LEU A O   1 
ATOM   2973 C  CB  . LEU A 1 481 ? 170.793 204.295 165.339 1.00 8.31   ? 391  LEU A CB  1 
ATOM   2974 C  CG  . LEU A 1 481 ? 169.274 204.429 165.546 1.00 8.73   ? 391  LEU A CG  1 
ATOM   2975 C  CD1 . LEU A 1 481 ? 168.793 205.700 164.871 1.00 9.05   ? 391  LEU A CD1 1 
ATOM   2976 C  CD2 . LEU A 1 481 ? 168.563 203.215 164.954 1.00 8.85   ? 391  LEU A CD2 1 
ATOM   2977 N  N   . LEU A 1 482 ? 173.908 203.482 166.301 1.00 7.41   ? 392  LEU A N   1 
ATOM   2978 C  CA  . LEU A 1 482 ? 175.279 203.411 165.822 1.00 7.24   ? 392  LEU A CA  1 
ATOM   2979 C  C   . LEU A 1 482 ? 176.086 202.339 166.553 1.00 7.13   ? 392  LEU A C   1 
ATOM   2980 O  O   . LEU A 1 482 ? 177.308 202.255 166.404 1.00 6.81   ? 392  LEU A O   1 
ATOM   2981 C  CB  . LEU A 1 482 ? 175.945 204.783 165.971 1.00 7.11   ? 392  LEU A CB  1 
ATOM   2982 C  CG  . LEU A 1 482 ? 175.237 205.952 165.235 1.00 7.31   ? 392  LEU A CG  1 
ATOM   2983 C  CD1 . LEU A 1 482 ? 175.979 207.242 165.513 1.00 7.46   ? 392  LEU A CD1 1 
ATOM   2984 C  CD2 . LEU A 1 482 ? 175.180 205.673 163.737 1.00 7.35   ? 392  LEU A CD2 1 
ATOM   2985 N  N   . ARG A 1 483 ? 175.404 201.507 167.335 1.00 7.11   ? 393  ARG A N   1 
ATOM   2986 C  CA  . ARG A 1 483 ? 176.073 200.435 168.065 1.00 6.90   ? 393  ARG A CA  1 
ATOM   2987 C  C   . ARG A 1 483 ? 176.240 199.189 167.210 1.00 6.76   ? 393  ARG A C   1 
ATOM   2988 O  O   . ARG A 1 483 ? 175.574 198.178 167.428 1.00 6.70   ? 393  ARG A O   1 
ATOM   2989 C  CB  . ARG A 1 483 ? 175.312 200.073 169.324 1.00 6.91   ? 393  ARG A CB  1 
ATOM   2990 C  CG  . ARG A 1 483 ? 175.324 201.125 170.392 1.00 7.17   ? 393  ARG A CG  1 
ATOM   2991 C  CD  . ARG A 1 483 ? 174.526 200.716 171.545 1.00 7.23   ? 393  ARG A CD  1 
ATOM   2992 N  NE  . ARG A 1 483 ? 174.420 201.773 172.517 1.00 7.35   ? 393  ARG A NE  1 
ATOM   2993 C  CZ  . ARG A 1 483 ? 173.704 201.695 173.645 1.00 7.61   ? 393  ARG A CZ  1 
ATOM   2994 N  NH1 . ARG A 1 483 ? 173.041 200.596 173.923 1.00 8.09   ? 393  ARG A NH1 1 
ATOM   2995 N  NH2 . ARG A 1 483 ? 173.670 202.722 174.470 1.00 7.73   ? 393  ARG A NH2 1 
ATOM   2996 N  N   . ASN A 1 484 ? 177.124 199.259 166.226 1.00 6.61   ? 394  ASN A N   1 
ATOM   2997 C  CA  . ASN A 1 484 ? 177.394 198.175 165.290 1.00 6.62   ? 394  ASN A CA  1 
ATOM   2998 C  C   . ASN A 1 484 ? 178.824 198.248 164.818 1.00 6.58   ? 394  ASN A C   1 
ATOM   2999 O  O   . ASN A 1 484 ? 179.547 199.132 165.199 1.00 6.41   ? 394  ASN A O   1 
ATOM   3000 C  CB  . ASN A 1 484 ? 176.556 198.391 164.036 1.00 6.72   ? 394  ASN A CB  1 
ATOM   3001 N  N   . GLY A 1 485 ? 179.226 197.324 163.959 1.00 6.35   ? 395  GLY A N   1 
ATOM   3002 C  CA  . GLY A 1 485 ? 180.553 197.369 163.355 1.00 6.21   ? 395  GLY A CA  1 
ATOM   3003 C  C   . GLY A 1 485 ? 180.564 198.346 162.190 1.00 6.04   ? 395  GLY A C   1 
ATOM   3004 O  O   . GLY A 1 485 ? 179.518 198.664 161.627 1.00 6.07   ? 395  GLY A O   1 
ATOM   3005 N  N   . ALA A 1 486 ? 181.752 198.803 161.799 1.00 5.93   ? 396  ALA A N   1 
ATOM   3006 C  CA  . ALA A 1 486 ? 181.870 199.759 160.701 1.00 5.84   ? 396  ALA A CA  1 
ATOM   3007 C  C   . ALA A 1 486 ? 181.263 199.204 159.420 1.00 5.67   ? 396  ALA A C   1 
ATOM   3008 O  O   . ALA A 1 486 ? 180.619 199.929 158.663 1.00 5.63   ? 396  ALA A O   1 
ATOM   3009 C  CB  . ALA A 1 486 ? 183.321 200.129 160.479 1.00 5.80   ? 396  ALA A CB  1 
ATOM   3010 N  N   . ASN A 1 487 ? 181.446 197.906 159.200 1.00 5.66   ? 397  ASN A N   1 
ATOM   3011 C  CA  . ASN A 1 487 ? 180.830 197.203 158.080 1.00 5.61   ? 397  ASN A CA  1 
ATOM   3012 C  C   . ASN A 1 487 ? 180.315 195.853 158.528 1.00 5.58   ? 397  ASN A C   1 
ATOM   3013 O  O   . ASN A 1 487 ? 180.563 195.418 159.654 1.00 5.63   ? 397  ASN A O   1 
ATOM   3014 C  CB  . ASN A 1 487 ? 181.803 196.989 156.930 1.00 5.50   ? 397  ASN A CB  1 
ATOM   3015 C  CG  . ASN A 1 487 ? 181.879 198.106 155.974 1.00 5.52   ? 397  ASN A CG  1 
ATOM   3016 O  OD1 . ASN A 1 487 ? 180.991 198.961 155.899 1.00 5.49   ? 397  ASN A OD1 1 
ATOM   3017 N  ND2 . ASN A 1 487 ? 182.925 198.109 155.197 1.00 5.48   ? 397  ASN A ND2 1 
ATOM   3018 N  N   . GLU A 1 488 ? 179.681 195.148 157.606 1.00 5.34   ? 398  GLU A N   1 
ATOM   3019 C  CA  . GLU A 1 488 ? 179.148 193.822 157.861 1.00 5.24   ? 398  GLU A CA  1 
ATOM   3020 C  C   . GLU A 1 488 ? 180.236 192.780 158.106 1.00 5.41   ? 398  GLU A C   1 
ATOM   3021 O  O   . GLU A 1 488 ? 179.969 191.711 158.650 1.00 5.53   ? 398  GLU A O   1 
ATOM   3022 C  CB  . GLU A 1 488 ? 178.251 193.400 156.696 1.00 4.90   ? 398  GLU A CB  1 
ATOM   3023 C  CG  . GLU A 1 488 ? 178.968 193.259 155.363 1.00 4.76   ? 398  GLU A CG  1 
ATOM   3024 C  CD  . GLU A 1 488 ? 178.028 192.963 154.230 1.00 4.52   ? 398  GLU A CD  1 
ATOM   3025 O  OE1 . GLU A 1 488 ? 176.855 192.854 154.473 1.00 4.41   ? 398  GLU A OE1 1 
ATOM   3026 O  OE2 . GLU A 1 488 ? 178.484 192.846 153.117 1.00 4.40   ? 398  GLU A OE2 1 
ATOM   3027 N  N   . GLY A 1 489 ? 181.467 193.079 157.682 1.00 5.50   ? 399  GLY A N   1 
ATOM   3028 C  CA  . GLY A 1 489 ? 182.562 192.128 157.825 1.00 5.51   ? 399  GLY A CA  1 
ATOM   3029 C  C   . GLY A 1 489 ? 183.500 192.421 158.998 1.00 5.79   ? 399  GLY A C   1 
ATOM   3030 O  O   . GLY A 1 489 ? 184.457 191.681 159.226 1.00 5.84   ? 399  GLY A O   1 
ATOM   3031 N  N   . PHE A 1 490 ? 183.247 193.500 159.741 1.00 5.77   ? 400  PHE A N   1 
ATOM   3032 C  CA  . PHE A 1 490 ? 184.165 193.892 160.810 1.00 5.92   ? 400  PHE A CA  1 
ATOM   3033 C  C   . PHE A 1 490 ? 184.097 192.991 162.036 1.00 6.16   ? 400  PHE A C   1 
ATOM   3034 O  O   . PHE A 1 490 ? 185.124 192.691 162.640 1.00 6.12   ? 400  PHE A O   1 
ATOM   3035 C  CB  . PHE A 1 490 ? 183.949 195.346 161.220 1.00 5.91   ? 400  PHE A CB  1 
ATOM   3036 C  CG  . PHE A 1 490 ? 184.816 196.330 160.466 1.00 5.87   ? 400  PHE A CG  1 
ATOM   3037 C  CD1 . PHE A 1 490 ? 185.687 197.163 161.151 1.00 5.98   ? 400  PHE A CD1 1 
ATOM   3038 C  CD2 . PHE A 1 490 ? 184.777 196.413 159.092 1.00 5.75   ? 400  PHE A CD2 1 
ATOM   3039 C  CE1 . PHE A 1 490 ? 186.490 198.064 160.474 1.00 6.04   ? 400  PHE A CE1 1 
ATOM   3040 C  CE2 . PHE A 1 490 ? 185.576 197.313 158.411 1.00 5.74   ? 400  PHE A CE2 1 
ATOM   3041 C  CZ  . PHE A 1 490 ? 186.432 198.138 159.104 1.00 5.87   ? 400  PHE A CZ  1 
ATOM   3042 N  N   . HIS A 1 491 ? 182.900 192.567 162.424 1.00 6.00   ? 401  HIS A N   1 
ATOM   3043 C  CA  . HIS A 1 491 ? 182.771 191.744 163.621 1.00 6.19   ? 401  HIS A CA  1 
ATOM   3044 C  C   . HIS A 1 491 ? 183.461 190.405 163.457 1.00 6.71   ? 401  HIS A C   1 
ATOM   3045 O  O   . HIS A 1 491 ? 184.110 189.910 164.382 1.00 6.73   ? 401  HIS A O   1 
ATOM   3046 C  CB  . HIS A 1 491 ? 181.301 191.498 163.974 1.00 6.37   ? 401  HIS A CB  1 
ATOM   3047 C  CG  . HIS A 1 491 ? 180.706 192.496 164.909 1.00 6.46   ? 401  HIS A CG  1 
ATOM   3048 N  ND1 . HIS A 1 491 ? 181.025 192.532 166.247 1.00 6.59   ? 401  HIS A ND1 1 
ATOM   3049 C  CD2 . HIS A 1 491 ? 179.798 193.475 164.715 1.00 6.55   ? 401  HIS A CD2 1 
ATOM   3050 C  CE1 . HIS A 1 491 ? 180.337 193.488 166.836 1.00 6.60   ? 401  HIS A CE1 1 
ATOM   3051 N  NE2 . HIS A 1 491 ? 179.584 194.075 165.929 1.00 6.55   ? 401  HIS A NE2 1 
ATOM   3052 N  N   . GLU A 1 492 ? 183.315 189.810 162.285 1.00 6.70   ? 402  GLU A N   1 
ATOM   3053 C  CA  . GLU A 1 492 ? 183.879 188.497 162.047 1.00 6.84   ? 402  GLU A CA  1 
ATOM   3054 C  C   . GLU A 1 492 ? 185.387 188.583 161.891 1.00 6.68   ? 402  GLU A C   1 
ATOM   3055 O  O   . GLU A 1 492 ? 186.113 187.707 162.359 1.00 6.79   ? 402  GLU A O   1 
ATOM   3056 C  CB  . GLU A 1 492 ? 183.244 187.879 160.810 1.00 6.60   ? 402  GLU A CB  1 
ATOM   3057 C  CG  . GLU A 1 492 ? 181.752 187.610 160.931 1.00 7.16   ? 402  GLU A CG  1 
ATOM   3058 C  CD  . GLU A 1 492 ? 181.396 186.651 162.015 1.00 7.47   ? 402  GLU A CD  1 
ATOM   3059 O  OE1 . GLU A 1 492 ? 180.440 186.892 162.710 1.00 7.56   ? 402  GLU A OE1 1 
ATOM   3060 O  OE2 . GLU A 1 492 ? 182.045 185.646 162.157 1.00 7.60   ? 402  GLU A OE2 1 
ATOM   3061 N  N   . ALA A 1 493 ? 185.865 189.650 161.257 1.00 6.32   ? 403  ALA A N   1 
ATOM   3062 C  CA  . ALA A 1 493 ? 187.297 189.836 161.073 1.00 6.38   ? 403  ALA A CA  1 
ATOM   3063 C  C   . ALA A 1 493 ? 187.998 189.980 162.421 1.00 6.59   ? 403  ALA A C   1 
ATOM   3064 O  O   . ALA A 1 493 ? 189.080 189.430 162.626 1.00 6.57   ? 403  ALA A O   1 
ATOM   3065 C  CB  . ALA A 1 493 ? 187.555 191.052 160.201 1.00 6.11   ? 403  ALA A CB  1 
ATOM   3066 N  N   . VAL A 1 494 ? 187.366 190.694 163.350 1.00 6.49   ? 404  VAL A N   1 
ATOM   3067 C  CA  . VAL A 1 494 ? 187.934 190.874 164.681 1.00 6.65   ? 404  VAL A CA  1 
ATOM   3068 C  C   . VAL A 1 494 ? 187.976 189.560 165.453 1.00 6.75   ? 404  VAL A C   1 
ATOM   3069 O  O   . VAL A 1 494 ? 188.966 189.255 166.114 1.00 6.88   ? 404  VAL A O   1 
ATOM   3070 C  CB  . VAL A 1 494 ? 187.151 191.943 165.472 1.00 6.82   ? 404  VAL A CB  1 
ATOM   3071 C  CG1 . VAL A 1 494 ? 187.595 191.960 166.937 1.00 6.98   ? 404  VAL A CG1 1 
ATOM   3072 C  CG2 . VAL A 1 494 ? 187.402 193.310 164.845 1.00 6.87   ? 404  VAL A CG2 1 
ATOM   3073 N  N   . GLY A 1 495 ? 186.908 188.777 165.369 1.00 6.65   ? 405  GLY A N   1 
ATOM   3074 C  CA  . GLY A 1 495 ? 186.874 187.486 166.045 1.00 6.99   ? 405  GLY A CA  1 
ATOM   3075 C  C   . GLY A 1 495 ? 187.947 186.534 165.509 1.00 7.33   ? 405  GLY A C   1 
ATOM   3076 O  O   . GLY A 1 495 ? 188.640 185.867 166.281 1.00 7.04   ? 405  GLY A O   1 
ATOM   3077 N  N   . GLU A 1 496 ? 188.094 186.481 164.186 1.00 6.73   ? 406  GLU A N   1 
ATOM   3078 C  CA  . GLU A 1 496 ? 189.015 185.533 163.566 1.00 6.90   ? 406  GLU A CA  1 
ATOM   3079 C  C   . GLU A 1 496 ? 190.474 185.783 163.934 1.00 7.64   ? 406  GLU A C   1 
ATOM   3080 O  O   . GLU A 1 496 ? 191.222 184.833 164.169 1.00 7.04   ? 406  GLU A O   1 
ATOM   3081 C  CB  . GLU A 1 496 ? 188.870 185.561 162.043 1.00 6.76   ? 406  GLU A CB  1 
ATOM   3082 C  CG  . GLU A 1 496 ? 187.592 184.930 161.495 1.00 6.69   ? 406  GLU A CG  1 
ATOM   3083 C  CD  . GLU A 1 496 ? 187.523 183.439 161.703 1.00 6.92   ? 406  GLU A CD  1 
ATOM   3084 O  OE1 . GLU A 1 496 ? 188.544 182.842 161.941 1.00 7.11   ? 406  GLU A OE1 1 
ATOM   3085 O  OE2 . GLU A 1 496 ? 186.446 182.897 161.615 1.00 6.88   ? 406  GLU A OE2 1 
ATOM   3086 N  N   . ILE A 1 497 ? 190.885 187.046 164.016 1.00 6.87   ? 407  ILE A N   1 
ATOM   3087 C  CA  . ILE A 1 497 ? 192.285 187.327 164.328 1.00 7.01   ? 407  ILE A CA  1 
ATOM   3088 C  C   . ILE A 1 497 ? 192.657 186.888 165.740 1.00 7.50   ? 407  ILE A C   1 
ATOM   3089 O  O   . ILE A 1 497 ? 193.806 186.525 166.001 1.00 7.35   ? 407  ILE A O   1 
ATOM   3090 C  CB  . ILE A 1 497 ? 192.645 188.816 164.108 1.00 6.99   ? 407  ILE A CB  1 
ATOM   3091 C  CG1 . ILE A 1 497 ? 191.800 189.727 165.012 1.00 6.97   ? 407  ILE A CG1 1 
ATOM   3092 C  CG2 . ILE A 1 497 ? 192.479 189.178 162.637 1.00 6.87   ? 407  ILE A CG2 1 
ATOM   3093 C  CD1 . ILE A 1 497 ? 192.243 191.176 165.030 1.00 6.99   ? 407  ILE A CD1 1 
ATOM   3094 N  N   . MET A 1 498 ? 191.686 186.885 166.645 1.00 7.14   ? 408  MET A N   1 
ATOM   3095 C  CA  . MET A 1 498 ? 191.944 186.454 168.010 1.00 7.37   ? 408  MET A CA  1 
ATOM   3096 C  C   . MET A 1 498 ? 192.148 184.948 168.074 1.00 7.62   ? 408  MET A C   1 
ATOM   3097 O  O   . MET A 1 498 ? 192.931 184.451 168.887 1.00 7.82   ? 408  MET A O   1 
ATOM   3098 C  CB  . MET A 1 498 ? 190.803 186.893 168.916 1.00 7.40   ? 408  MET A CB  1 
ATOM   3099 C  CG  . MET A 1 498 ? 190.647 188.398 168.998 1.00 7.29   ? 408  MET A CG  1 
ATOM   3100 S  SD  . MET A 1 498 ? 192.148 189.213 169.549 1.00 7.74   ? 408  MET A SD  1 
ATOM   3101 C  CE  . MET A 1 498 ? 191.750 190.911 169.223 1.00 7.35   ? 408  MET A CE  1 
ATOM   3102 N  N   . SER A 1 499 ? 191.466 184.225 167.192 1.00 7.42   ? 409  SER A N   1 
ATOM   3103 C  CA  . SER A 1 499 ? 191.617 182.779 167.121 1.00 7.70   ? 409  SER A CA  1 
ATOM   3104 C  C   . SER A 1 499 ? 192.971 182.400 166.531 1.00 7.82   ? 409  SER A C   1 
ATOM   3105 O  O   . SER A 1 499 ? 193.588 181.419 166.951 1.00 8.10   ? 409  SER A O   1 
ATOM   3106 C  CB  . SER A 1 499 ? 190.501 182.175 166.293 1.00 7.71   ? 409  SER A CB  1 
ATOM   3107 N  N   . LEU A 1 500 ? 193.441 183.185 165.562 1.00 7.59   ? 410  LEU A N   1 
ATOM   3108 C  CA  . LEU A 1 500 ? 194.725 182.895 164.933 1.00 7.70   ? 410  LEU A CA  1 
ATOM   3109 C  C   . LEU A 1 500 ? 195.860 182.996 165.938 1.00 8.06   ? 410  LEU A C   1 
ATOM   3110 O  O   . LEU A 1 500 ? 196.757 182.156 165.960 1.00 8.30   ? 410  LEU A O   1 
ATOM   3111 C  CB  . LEU A 1 500 ? 195.004 183.871 163.778 1.00 7.37   ? 410  LEU A CB  1 
ATOM   3112 C  CG  . LEU A 1 500 ? 194.139 183.728 162.516 1.00 7.19   ? 410  LEU A CG  1 
ATOM   3113 C  CD1 . LEU A 1 500 ? 194.418 184.910 161.589 1.00 7.01   ? 410  LEU A CD1 1 
ATOM   3114 C  CD2 . LEU A 1 500 ? 194.458 182.413 161.813 1.00 7.03   ? 410  LEU A CD2 1 
ATOM   3115 N  N   . SER A 1 501 ? 195.805 184.020 166.783 1.00 7.98   ? 411  SER A N   1 
ATOM   3116 C  CA  . SER A 1 501 ? 196.841 184.246 167.781 1.00 8.27   ? 411  SER A CA  1 
ATOM   3117 C  C   . SER A 1 501 ? 196.834 183.147 168.838 1.00 8.54   ? 411  SER A C   1 
ATOM   3118 O  O   . SER A 1 501 ? 197.876 182.595 169.186 1.00 8.97   ? 411  SER A O   1 
ATOM   3119 C  CB  . SER A 1 501 ? 196.629 185.600 168.433 1.00 8.31   ? 411  SER A CB  1 
ATOM   3120 N  N   . ALA A 1 502 ? 195.648 182.813 169.335 1.00 8.40   ? 412  ALA A N   1 
ATOM   3121 C  CA  . ALA A 1 502 ? 195.505 181.828 170.403 1.00 8.74   ? 412  ALA A CA  1 
ATOM   3122 C  C   . ALA A 1 502 ? 195.979 180.436 169.984 1.00 8.92   ? 412  ALA A C   1 
ATOM   3123 O  O   . ALA A 1 502 ? 196.376 179.634 170.829 1.00 9.34   ? 412  ALA A O   1 
ATOM   3124 C  CB  . ALA A 1 502 ? 194.056 181.759 170.853 1.00 8.50   ? 412  ALA A CB  1 
ATOM   3125 N  N   . ALA A 1 503 ? 195.892 180.131 168.697 1.00 8.87   ? 413  ALA A N   1 
ATOM   3126 C  CA  . ALA A 1 503 ? 196.201 178.792 168.205 1.00 9.08   ? 413  ALA A CA  1 
ATOM   3127 C  C   . ALA A 1 503 ? 197.689 178.541 167.955 1.00 9.35   ? 413  ALA A C   1 
ATOM   3128 O  O   . ALA A 1 503 ? 198.059 177.437 167.557 1.00 9.64   ? 413  ALA A O   1 
ATOM   3129 C  CB  . ALA A 1 503 ? 195.434 178.534 166.921 1.00 8.84   ? 413  ALA A CB  1 
ATOM   3130 N  N   . THR A 1 504 ? 198.547 179.538 168.155 1.00 9.35   ? 414  THR A N   1 
ATOM   3131 C  CA  . THR A 1 504 ? 199.965 179.322 167.866 1.00 9.56   ? 414  THR A CA  1 
ATOM   3132 C  C   . THR A 1 504 ? 200.594 178.391 168.904 1.00 10.07  ? 414  THR A C   1 
ATOM   3133 O  O   . THR A 1 504 ? 200.209 178.432 170.071 1.00 9.70   ? 414  THR A O   1 
ATOM   3134 C  CB  . THR A 1 504 ? 200.760 180.639 167.876 1.00 9.56   ? 414  THR A CB  1 
ATOM   3135 O  OG1 . THR A 1 504 ? 200.693 181.222 169.183 1.00 9.83   ? 414  THR A OG1 1 
ATOM   3136 C  CG2 . THR A 1 504 ? 200.204 181.608 166.856 1.00 9.22   ? 414  THR A CG2 1 
ATOM   3137 N  N   . PRO A 1 505 ? 201.604 177.599 168.512 1.00 10.18  ? 415  PRO A N   1 
ATOM   3138 C  CA  . PRO A 1 505 ? 202.474 176.803 169.362 1.00 10.19  ? 415  PRO A CA  1 
ATOM   3139 C  C   . PRO A 1 505 ? 203.085 177.667 170.452 1.00 10.43  ? 415  PRO A C   1 
ATOM   3140 O  O   . PRO A 1 505 ? 203.288 177.211 171.576 1.00 10.48  ? 415  PRO A O   1 
ATOM   3141 C  CB  . PRO A 1 505 ? 203.536 176.325 168.372 1.00 10.28  ? 415  PRO A CB  1 
ATOM   3142 C  CG  . PRO A 1 505 ? 202.813 176.258 167.055 1.00 10.11  ? 415  PRO A CG  1 
ATOM   3143 C  CD  . PRO A 1 505 ? 201.848 177.423 167.076 1.00 10.05  ? 415  PRO A CD  1 
ATOM   3144 N  N   . LYS A 1 506 ? 203.368 178.923 170.127 1.00 10.33  ? 416  LYS A N   1 
ATOM   3145 C  CA  . LYS A 1 506 ? 203.936 179.845 171.100 1.00 10.28  ? 416  LYS A CA  1 
ATOM   3146 C  C   . LYS A 1 506 ? 202.984 180.029 172.277 1.00 10.57  ? 416  LYS A C   1 
ATOM   3147 O  O   . LYS A 1 506 ? 203.385 179.926 173.437 1.00 10.77  ? 416  LYS A O   1 
ATOM   3148 C  CB  . LYS A 1 506 ? 204.264 181.180 170.429 1.00 10.35  ? 416  LYS A CB  1 
ATOM   3149 C  CG  . LYS A 1 506 ? 205.009 182.175 171.306 1.00 10.57  ? 416  LYS A CG  1 
ATOM   3150 C  CD  . LYS A 1 506 ? 204.860 183.595 170.764 1.00 10.43  ? 416  LYS A CD  1 
ATOM   3151 C  CE  . LYS A 1 506 ? 205.279 183.695 169.301 1.00 10.47  ? 416  LYS A CE  1 
ATOM   3152 N  NZ  . LYS A 1 506 ? 205.269 185.107 168.817 1.00 9.92   ? 416  LYS A NZ  1 
ATOM   3153 N  N   . HIS A 1 507 ? 201.715 180.281 171.969 1.00 10.26  ? 417  HIS A N   1 
ATOM   3154 C  CA  . HIS A 1 507 ? 200.712 180.485 173.002 1.00 10.51  ? 417  HIS A CA  1 
ATOM   3155 C  C   . HIS A 1 507 ? 200.430 179.215 173.791 1.00 10.65  ? 417  HIS A C   1 
ATOM   3156 O  O   . HIS A 1 507 ? 200.272 179.250 175.014 1.00 10.51  ? 417  HIS A O   1 
ATOM   3157 C  CB  . HIS A 1 507 ? 199.424 180.998 172.348 1.00 9.90   ? 417  HIS A CB  1 
ATOM   3158 C  CG  . HIS A 1 507 ? 198.418 181.519 173.328 1.00 9.84   ? 417  HIS A CG  1 
ATOM   3159 N  ND1 . HIS A 1 507 ? 198.660 182.615 174.121 1.00 9.98   ? 417  HIS A ND1 1 
ATOM   3160 C  CD2 . HIS A 1 507 ? 197.170 181.101 173.639 1.00 9.74   ? 417  HIS A CD2 1 
ATOM   3161 C  CE1 . HIS A 1 507 ? 197.609 182.849 174.878 1.00 9.81   ? 417  HIS A CE1 1 
ATOM   3162 N  NE2 . HIS A 1 507 ? 196.692 181.948 174.605 1.00 9.60   ? 417  HIS A NE2 1 
ATOM   3163 N  N   . LEU A 1 508 ? 200.370 178.087 173.092 1.00 10.26  ? 418  LEU A N   1 
ATOM   3164 C  CA  . LEU A 1 508 ? 200.058 176.817 173.727 1.00 10.49  ? 418  LEU A CA  1 
ATOM   3165 C  C   . LEU A 1 508 ? 201.129 176.411 174.733 1.00 13.81  ? 418  LEU A C   1 
ATOM   3166 O  O   . LEU A 1 508 ? 200.814 175.885 175.800 1.00 10.54  ? 418  LEU A O   1 
ATOM   3167 C  CB  . LEU A 1 508 ? 199.901 175.728 172.665 1.00 10.57  ? 418  LEU A CB  1 
ATOM   3168 C  CG  . LEU A 1 508 ? 198.700 175.877 171.712 1.00 10.36  ? 418  LEU A CG  1 
ATOM   3169 C  CD1 . LEU A 1 508 ? 198.837 174.862 170.593 1.00 10.46  ? 418  LEU A CD1 1 
ATOM   3170 C  CD2 . LEU A 1 508 ? 197.394 175.672 172.478 1.00 10.40  ? 418  LEU A CD2 1 
ATOM   3171 N  N   . LYS A 1 509 ? 202.397 176.674 174.416 1.00 10.58  ? 419  LYS A N   1 
ATOM   3172 C  CA  . LYS A 1 509 ? 203.471 176.368 175.359 1.00 11.05  ? 419  LYS A CA  1 
ATOM   3173 C  C   . LYS A 1 509 ? 203.342 177.192 176.634 1.00 11.27  ? 419  LYS A C   1 
ATOM   3174 O  O   . LYS A 1 509 ? 203.487 176.666 177.736 1.00 11.49  ? 419  LYS A O   1 
ATOM   3175 C  CB  . LYS A 1 509 ? 204.848 176.598 174.735 1.00 11.28  ? 419  LYS A CB  1 
ATOM   3176 C  CG  . LYS A 1 509 ? 205.279 175.534 173.748 1.00 11.65  ? 419  LYS A CG  1 
ATOM   3177 C  CD  . LYS A 1 509 ? 206.662 175.825 173.177 1.00 12.02  ? 419  LYS A CD  1 
ATOM   3178 C  CE  . LYS A 1 509 ? 207.174 174.648 172.363 1.00 12.76  ? 419  LYS A CE  1 
ATOM   3179 N  NZ  . LYS A 1 509 ? 208.499 174.917 171.746 1.00 13.44  ? 419  LYS A NZ  1 
ATOM   3180 N  N   . ASP A 1 510 ? 203.025 178.475 176.492 1.00 11.18  ? 420  ASP A N   1 
ATOM   3181 C  CA  . ASP A 1 510 ? 202.888 179.354 177.647 1.00 11.42  ? 420  ASP A CA  1 
ATOM   3182 C  C   . ASP A 1 510 ? 201.738 178.928 178.554 1.00 11.29  ? 420  ASP A C   1 
ATOM   3183 O  O   . ASP A 1 510 ? 201.809 179.083 179.774 1.00 11.60  ? 420  ASP A O   1 
ATOM   3184 C  CB  . ASP A 1 510 ? 202.692 180.799 177.197 1.00 11.78  ? 420  ASP A CB  1 
ATOM   3185 C  CG  . ASP A 1 510 ? 203.974 181.425 176.668 1.00 12.54  ? 420  ASP A CG  1 
ATOM   3186 O  OD1 . ASP A 1 510 ? 205.033 180.946 177.002 1.00 13.01  ? 420  ASP A OD1 1 
ATOM   3187 O  OD2 . ASP A 1 510 ? 203.883 182.363 175.918 1.00 12.40  ? 420  ASP A OD2 1 
ATOM   3188 N  N   . LEU A 1 511 ? 200.694 178.360 177.962 1.00 11.06  ? 421  LEU A N   1 
ATOM   3189 C  CA  . LEU A 1 511 ? 199.544 177.882 178.722 1.00 10.95  ? 421  LEU A CA  1 
ATOM   3190 C  C   . LEU A 1 511 ? 199.813 176.557 179.423 1.00 11.17  ? 421  LEU A C   1 
ATOM   3191 O  O   . LEU A 1 511 ? 199.019 176.121 180.257 1.00 11.36  ? 421  LEU A O   1 
ATOM   3192 C  CB  . LEU A 1 511 ? 198.338 177.697 177.796 1.00 11.08  ? 421  LEU A CB  1 
ATOM   3193 C  CG  . LEU A 1 511 ? 197.738 178.959 177.191 1.00 10.57  ? 421  LEU A CG  1 
ATOM   3194 C  CD1 . LEU A 1 511 ? 196.715 178.556 176.159 1.00 10.46  ? 421  LEU A CD1 1 
ATOM   3195 C  CD2 . LEU A 1 511 ? 197.091 179.796 178.280 1.00 10.41  ? 421  LEU A CD2 1 
ATOM   3196 N  N   . GLY A 1 512 ? 200.902 175.889 179.054 1.00 11.31  ? 422  GLY A N   1 
ATOM   3197 C  CA  . GLY A 1 512 ? 201.213 174.578 179.604 1.00 11.38  ? 422  GLY A CA  1 
ATOM   3198 C  C   . GLY A 1 512 ? 200.475 173.449 178.887 1.00 11.36  ? 422  GLY A C   1 
ATOM   3199 O  O   . GLY A 1 512 ? 200.408 172.329 179.395 1.00 11.56  ? 422  GLY A O   1 
ATOM   3200 N  N   . LEU A 1 513 ? 199.906 173.738 177.717 1.00 11.27  ? 423  LEU A N   1 
ATOM   3201 C  CA  . LEU A 1 513 ? 199.159 172.726 176.973 1.00 11.36  ? 423  LEU A CA  1 
ATOM   3202 C  C   . LEU A 1 513 ? 200.020 172.015 175.946 1.00 11.43  ? 423  LEU A C   1 
ATOM   3203 O  O   . LEU A 1 513 ? 199.575 171.070 175.295 1.00 11.74  ? 423  LEU A O   1 
ATOM   3204 C  CB  . LEU A 1 513 ? 197.951 173.351 176.267 1.00 11.24  ? 423  LEU A CB  1 
ATOM   3205 C  CG  . LEU A 1 513 ? 196.819 173.862 177.162 1.00 11.24  ? 423  LEU A CG  1 
ATOM   3206 C  CD1 . LEU A 1 513 ? 195.782 174.567 176.292 1.00 10.83  ? 423  LEU A CD1 1 
ATOM   3207 C  CD2 . LEU A 1 513 ? 196.187 172.681 177.899 1.00 11.21  ? 423  LEU A CD2 1 
ATOM   3208 N  N   . LEU A 1 514 ? 201.246 172.481 175.795 1.00 11.39  ? 424  LEU A N   1 
ATOM   3209 C  CA  . LEU A 1 514 ? 202.174 171.919 174.830 1.00 11.57  ? 424  LEU A CA  1 
ATOM   3210 C  C   . LEU A 1 514 ? 203.556 171.862 175.462 1.00 11.87  ? 424  LEU A C   1 
ATOM   3211 O  O   . LEU A 1 514 ? 203.979 172.804 176.130 1.00 11.67  ? 424  LEU A O   1 
ATOM   3212 C  CB  . LEU A 1 514 ? 202.167 172.767 173.545 1.00 11.46  ? 424  LEU A CB  1 
ATOM   3213 C  CG  . LEU A 1 514 ? 203.043 172.286 172.373 1.00 11.99  ? 424  LEU A CG  1 
ATOM   3214 C  CD1 . LEU A 1 514 ? 202.512 170.967 171.838 1.00 12.05  ? 424  LEU A CD1 1 
ATOM   3215 C  CD2 . LEU A 1 514 ? 203.021 173.339 171.272 1.00 11.47  ? 424  LEU A CD2 1 
ATOM   3216 N  N   . ALA A 1 515 ? 204.229 170.727 175.321 1.00 12.31  ? 425  ALA A N   1 
ATOM   3217 C  CA  . ALA A 1 515 ? 205.513 170.533 175.982 1.00 12.53  ? 425  ALA A CA  1 
ATOM   3218 C  C   . ALA A 1 515 ? 206.460 171.676 175.660 1.00 12.63  ? 425  ALA A C   1 
ATOM   3219 O  O   . ALA A 1 515 ? 206.597 172.074 174.506 1.00 12.64  ? 425  ALA A O   1 
ATOM   3220 C  CB  . ALA A 1 515 ? 206.128 169.210 175.562 1.00 13.02  ? 425  ALA A CB  1 
ATOM   3221 N  N   . GLN A 1 516 ? 207.139 172.181 176.682 1.00 12.81  ? 426  GLN A N   1 
ATOM   3222 C  CA  . GLN A 1 516 ? 208.029 173.323 176.513 1.00 12.75  ? 426  GLN A CA  1 
ATOM   3223 C  C   . GLN A 1 516 ? 209.152 173.015 175.534 1.00 13.02  ? 426  GLN A C   1 
ATOM   3224 O  O   . GLN A 1 516 ? 209.609 173.893 174.800 1.00 13.04  ? 426  GLN A O   1 
ATOM   3225 C  CB  . GLN A 1 516 ? 208.615 173.744 177.864 1.00 12.72  ? 426  GLN A CB  1 
ATOM   3226 C  CG  . GLN A 1 516 ? 209.364 175.061 177.830 1.00 13.09  ? 426  GLN A CG  1 
ATOM   3227 C  CD  . GLN A 1 516 ? 208.449 176.233 177.514 1.00 12.84  ? 426  GLN A CD  1 
ATOM   3228 O  OE1 . GLN A 1 516 ? 208.537 176.835 176.440 1.00 12.94  ? 426  GLN A OE1 1 
ATOM   3229 N  NE2 . GLN A 1 516 ? 207.566 176.562 178.449 1.00 12.63  ? 426  GLN A NE2 1 
ATOM   3230 N  N   . ASN A 1 517 ? 209.592 171.765 175.518 1.00 13.21  ? 427  ASN A N   1 
ATOM   3231 C  CA  . ASN A 1 517 ? 210.680 171.345 174.649 1.00 13.23  ? 427  ASN A CA  1 
ATOM   3232 C  C   . ASN A 1 517 ? 210.177 170.779 173.327 1.00 13.28  ? 427  ASN A C   1 
ATOM   3233 O  O   . ASN A 1 517 ? 210.940 170.171 172.577 1.00 13.46  ? 427  ASN A O   1 
ATOM   3234 C  CB  . ASN A 1 517 ? 211.550 170.330 175.357 1.00 13.64  ? 427  ASN A CB  1 
ATOM   3235 N  N   . TYR A 1 518 ? 208.897 170.982 173.036 1.00 13.13  ? 428  TYR A N   1 
ATOM   3236 C  CA  . TYR A 1 518 ? 208.326 170.514 171.783 1.00 13.44  ? 428  TYR A CA  1 
ATOM   3237 C  C   . TYR A 1 518 ? 209.082 171.154 170.613 1.00 13.28  ? 428  TYR A C   1 
ATOM   3238 O  O   . TYR A 1 518 ? 209.158 172.383 170.532 1.00 13.43  ? 428  TYR A O   1 
ATOM   3239 C  CB  . TYR A 1 518 ? 206.837 170.867 171.726 1.00 13.03  ? 428  TYR A CB  1 
ATOM   3240 C  CG  . TYR A 1 518 ? 206.116 170.332 170.534 1.00 13.16  ? 428  TYR A CG  1 
ATOM   3241 C  CD1 . TYR A 1 518 ? 205.648 169.032 170.543 1.00 13.28  ? 428  TYR A CD1 1 
ATOM   3242 C  CD2 . TYR A 1 518 ? 205.916 171.136 169.429 1.00 13.10  ? 428  TYR A CD2 1 
ATOM   3243 C  CE1 . TYR A 1 518 ? 204.980 168.536 169.448 1.00 13.27  ? 428  TYR A CE1 1 
ATOM   3244 C  CE2 . TYR A 1 518 ? 205.249 170.641 168.333 1.00 13.08  ? 428  TYR A CE2 1 
ATOM   3245 C  CZ  . TYR A 1 518 ? 204.781 169.346 168.340 1.00 13.19  ? 428  TYR A CZ  1 
ATOM   3246 O  OH  . TYR A 1 518 ? 204.116 168.847 167.245 1.00 13.55  ? 428  TYR A OH  1 
ATOM   3247 N  N   . PRO A 1 519 ? 209.663 170.347 169.717 1.00 13.39  ? 429  PRO A N   1 
ATOM   3248 C  CA  . PRO A 1 519 ? 210.511 170.752 168.610 1.00 13.42  ? 429  PRO A CA  1 
ATOM   3249 C  C   . PRO A 1 519 ? 209.720 171.398 167.488 1.00 13.49  ? 429  PRO A C   1 
ATOM   3250 O  O   . PRO A 1 519 ? 208.547 171.087 167.288 1.00 13.50  ? 429  PRO A O   1 
ATOM   3251 C  CB  . PRO A 1 519 ? 211.118 169.420 168.163 1.00 13.59  ? 429  PRO A CB  1 
ATOM   3252 C  CG  . PRO A 1 519 ? 210.071 168.387 168.525 1.00 13.54  ? 429  PRO A CG  1 
ATOM   3253 C  CD  . PRO A 1 519 ? 209.437 168.900 169.804 1.00 13.35  ? 429  PRO A CD  1 
ATOM   3254 N  N   . GLU A 1 520 ? 210.386 172.247 166.715 1.00 13.66  ? 430  GLU A N   1 
ATOM   3255 C  CA  . GLU A 1 520 ? 209.783 172.796 165.511 1.00 13.55  ? 430  GLU A CA  1 
ATOM   3256 C  C   . GLU A 1 520 ? 209.929 171.820 164.356 1.00 13.17  ? 430  GLU A C   1 
ATOM   3257 O  O   . GLU A 1 520 ? 210.920 171.095 164.262 1.00 13.20  ? 430  GLU A O   1 
ATOM   3258 C  CB  . GLU A 1 520 ? 210.411 174.142 165.146 1.00 13.76  ? 430  GLU A CB  1 
ATOM   3259 N  N   . ASP A 1 521 ? 208.940 171.808 163.475 1.00 12.94  ? 431  ASP A N   1 
ATOM   3260 C  CA  . ASP A 1 521 ? 208.952 170.935 162.313 1.00 12.34  ? 431  ASP A CA  1 
ATOM   3261 C  C   . ASP A 1 521 ? 208.382 171.664 161.105 1.00 12.03  ? 431  ASP A C   1 
ATOM   3262 O  O   . ASP A 1 521 ? 207.221 172.074 161.106 1.00 11.38  ? 431  ASP A O   1 
ATOM   3263 C  CB  . ASP A 1 521 ? 208.161 169.659 162.607 1.00 12.26  ? 431  ASP A CB  1 
ATOM   3264 C  CG  . ASP A 1 521 ? 208.196 168.644 161.480 1.00 12.32  ? 431  ASP A CG  1 
ATOM   3265 O  OD1 . ASP A 1 521 ? 209.065 167.802 161.470 1.00 13.70  ? 431  ASP A OD1 1 
ATOM   3266 O  OD2 . ASP A 1 521 ? 207.338 168.715 160.633 1.00 12.05  ? 431  ASP A OD2 1 
ATOM   3267 N  N   . TYR A 1 522 ? 209.215 171.851 160.091 1.00 12.18  ? 432  TYR A N   1 
ATOM   3268 C  CA  . TYR A 1 522 ? 208.847 172.660 158.939 1.00 11.94  ? 432  TYR A CA  1 
ATOM   3269 C  C   . TYR A 1 522 ? 207.786 171.978 158.088 1.00 11.28  ? 432  TYR A C   1 
ATOM   3270 O  O   . TYR A 1 522 ? 206.957 172.643 157.466 1.00 10.59  ? 432  TYR A O   1 
ATOM   3271 C  CB  . TYR A 1 522 ? 210.089 172.964 158.107 1.00 13.06  ? 432  TYR A CB  1 
ATOM   3272 C  CG  . TYR A 1 522 ? 211.113 173.750 158.866 1.00 13.92  ? 432  TYR A CG  1 
ATOM   3273 C  CD1 . TYR A 1 522 ? 212.339 173.181 159.153 1.00 15.24  ? 432  TYR A CD1 1 
ATOM   3274 C  CD2 . TYR A 1 522 ? 210.823 175.030 159.298 1.00 13.68  ? 432  TYR A CD2 1 
ATOM   3275 C  CE1 . TYR A 1 522 ? 213.275 173.892 159.869 1.00 16.18  ? 432  TYR A CE1 1 
ATOM   3276 C  CE2 . TYR A 1 522 ? 211.759 175.740 160.012 1.00 14.79  ? 432  TYR A CE2 1 
ATOM   3277 C  CZ  . TYR A 1 522 ? 212.979 175.178 160.298 1.00 15.86  ? 432  TYR A CZ  1 
ATOM   3278 O  OH  . TYR A 1 522 ? 213.908 175.892 161.015 1.00 18.02  ? 432  TYR A OH  1 
ATOM   3279 N  N   . GLU A 1 523 ? 207.801 170.652 158.072 1.00 11.29  ? 433  GLU A N   1 
ATOM   3280 C  CA  . GLU A 1 523 ? 206.813 169.897 157.317 1.00 10.85  ? 433  GLU A CA  1 
ATOM   3281 C  C   . GLU A 1 523 ? 205.432 170.060 157.937 1.00 10.25  ? 433  GLU A C   1 
ATOM   3282 O  O   . GLU A 1 523 ? 204.431 170.161 157.225 1.00 9.23   ? 433  GLU A O   1 
ATOM   3283 C  CB  . GLU A 1 523 ? 207.216 168.430 157.240 1.00 11.28  ? 433  GLU A CB  1 
ATOM   3284 C  CG  . GLU A 1 523 ? 208.442 168.189 156.383 1.00 11.79  ? 433  GLU A CG  1 
ATOM   3285 C  CD  . GLU A 1 523 ? 208.847 166.769 156.326 1.00 12.61  ? 433  GLU A CD  1 
ATOM   3286 O  OE1 . GLU A 1 523 ? 208.181 165.959 156.925 1.00 12.86  ? 433  GLU A OE1 1 
ATOM   3287 O  OE2 . GLU A 1 523 ? 209.831 166.481 155.684 1.00 13.89  ? 433  GLU A OE2 1 
ATOM   3288 N  N   . THR A 1 524 ? 205.388 170.132 159.265 1.00 10.47  ? 434  THR A N   1 
ATOM   3289 C  CA  . THR A 1 524 ? 204.144 170.372 159.982 1.00 9.87   ? 434  THR A CA  1 
ATOM   3290 C  C   . THR A 1 524 ? 203.596 171.753 159.645 1.00 9.50   ? 434  THR A C   1 
ATOM   3291 O  O   . THR A 1 524 ? 202.389 171.921 159.470 1.00 8.56   ? 434  THR A O   1 
ATOM   3292 C  CB  . THR A 1 524 ? 204.334 170.238 161.504 1.00 10.53  ? 434  THR A CB  1 
ATOM   3293 O  OG1 . THR A 1 524 ? 204.785 168.920 161.808 1.00 10.99  ? 434  THR A OG1 1 
ATOM   3294 C  CG2 . THR A 1 524 ? 203.013 170.486 162.226 1.00 10.45  ? 434  THR A CG2 1 
ATOM   3295 N  N   . GLU A 1 525 ? 204.482 172.744 159.550 1.00 9.48   ? 435  GLU A N   1 
ATOM   3296 C  CA  . GLU A 1 525 ? 204.051 174.094 159.207 1.00 9.23   ? 435  GLU A CA  1 
ATOM   3297 C  C   . GLU A 1 525 ? 203.451 174.145 157.805 1.00 8.53   ? 435  GLU A C   1 
ATOM   3298 O  O   . GLU A 1 525 ? 202.454 174.832 157.579 1.00 7.70   ? 435  GLU A O   1 
ATOM   3299 C  CB  . GLU A 1 525 ? 205.211 175.086 159.329 1.00 9.95   ? 435  GLU A CB  1 
ATOM   3300 C  CG  . GLU A 1 525 ? 205.675 175.313 160.764 1.00 10.11  ? 435  GLU A CG  1 
ATOM   3301 C  CD  . GLU A 1 525 ? 206.704 176.400 160.900 1.00 10.88  ? 435  GLU A CD  1 
ATOM   3302 O  OE1 . GLU A 1 525 ? 206.888 177.141 159.968 1.00 11.01  ? 435  GLU A OE1 1 
ATOM   3303 O  OE2 . GLU A 1 525 ? 207.305 176.493 161.949 1.00 11.47  ? 435  GLU A OE2 1 
ATOM   3304 N  N   . ILE A 1 526 ? 204.022 173.382 156.874 1.00 8.67   ? 436  ILE A N   1 
ATOM   3305 C  CA  . ILE A 1 526 ? 203.453 173.292 155.532 1.00 8.21   ? 436  ILE A CA  1 
ATOM   3306 C  C   . ILE A 1 526 ? 202.079 172.634 155.567 1.00 7.73   ? 436  ILE A C   1 
ATOM   3307 O  O   . ILE A 1 526 ? 201.153 173.100 154.903 1.00 7.08   ? 436  ILE A O   1 
ATOM   3308 C  CB  . ILE A 1 526 ? 204.383 172.537 154.559 1.00 8.65   ? 436  ILE A CB  1 
ATOM   3309 C  CG1 . ILE A 1 526 ? 205.686 173.336 154.318 1.00 9.31   ? 436  ILE A CG1 1 
ATOM   3310 C  CG2 . ILE A 1 526 ? 203.664 172.261 153.236 1.00 7.92   ? 436  ILE A CG2 1 
ATOM   3311 C  CD1 . ILE A 1 526 ? 205.499 174.687 153.637 1.00 8.47   ? 436  ILE A CD1 1 
ATOM   3312 N  N   . ASN A 1 527 ? 201.936 171.565 156.351 1.00 7.86   ? 437  ASN A N   1 
ATOM   3313 C  CA  . ASN A 1 527 ? 200.636 170.914 156.487 1.00 7.57   ? 437  ASN A CA  1 
ATOM   3314 C  C   . ASN A 1 527 ? 199.596 171.890 157.016 1.00 7.06   ? 437  ASN A C   1 
ATOM   3315 O  O   . ASN A 1 527 ? 198.462 171.927 156.531 1.00 6.51   ? 437  ASN A O   1 
ATOM   3316 C  CB  . ASN A 1 527 ? 200.717 169.712 157.413 1.00 7.78   ? 437  ASN A CB  1 
ATOM   3317 C  CG  . ASN A 1 527 ? 201.319 168.489 156.790 1.00 8.09   ? 437  ASN A CG  1 
ATOM   3318 O  OD1 . ASN A 1 527 ? 201.448 168.381 155.566 1.00 7.80   ? 437  ASN A OD1 1 
ATOM   3319 N  ND2 . ASN A 1 527 ? 201.674 167.547 157.622 1.00 8.82   ? 437  ASN A ND2 1 
ATOM   3320 N  N   . PHE A 1 528 ? 199.994 172.698 157.992 1.00 7.30   ? 438  PHE A N   1 
ATOM   3321 C  CA  . PHE A 1 528 ? 199.118 173.703 158.579 1.00 6.97   ? 438  PHE A CA  1 
ATOM   3322 C  C   . PHE A 1 528 ? 198.665 174.730 157.551 1.00 6.49   ? 438  PHE A C   1 
ATOM   3323 O  O   . PHE A 1 528 ? 197.475 175.016 157.434 1.00 6.02   ? 438  PHE A O   1 
ATOM   3324 C  CB  . PHE A 1 528 ? 199.820 174.406 159.739 1.00 7.10   ? 438  PHE A CB  1 
ATOM   3325 C  CG  . PHE A 1 528 ? 199.071 175.581 160.276 1.00 6.65   ? 438  PHE A CG  1 
ATOM   3326 C  CD1 . PHE A 1 528 ? 197.971 175.408 161.094 1.00 6.41   ? 438  PHE A CD1 1 
ATOM   3327 C  CD2 . PHE A 1 528 ? 199.463 176.869 159.954 1.00 6.73   ? 438  PHE A CD2 1 
ATOM   3328 C  CE1 . PHE A 1 528 ? 197.280 176.497 161.580 1.00 6.22   ? 438  PHE A CE1 1 
ATOM   3329 C  CE2 . PHE A 1 528 ? 198.776 177.954 160.437 1.00 6.54   ? 438  PHE A CE2 1 
ATOM   3330 C  CZ  . PHE A 1 528 ? 197.683 177.769 161.250 1.00 6.18   ? 438  PHE A CZ  1 
ATOM   3331 N  N   . LEU A 1 529 ? 199.616 175.295 156.817 1.00 6.58   ? 439  LEU A N   1 
ATOM   3332 C  CA  . LEU A 1 529 ? 199.300 176.323 155.836 1.00 6.29   ? 439  LEU A CA  1 
ATOM   3333 C  C   . LEU A 1 529 ? 198.423 175.786 154.717 1.00 5.87   ? 439  LEU A C   1 
ATOM   3334 O  O   . LEU A 1 529 ? 197.531 176.486 154.237 1.00 5.42   ? 439  LEU A O   1 
ATOM   3335 C  CB  . LEU A 1 529 ? 200.587 176.903 155.246 1.00 6.50   ? 439  LEU A CB  1 
ATOM   3336 C  CG  . LEU A 1 529 ? 201.425 177.781 156.183 1.00 7.03   ? 439  LEU A CG  1 
ATOM   3337 C  CD1 . LEU A 1 529 ? 202.783 178.018 155.553 1.00 7.58   ? 439  LEU A CD1 1 
ATOM   3338 C  CD2 . LEU A 1 529 ? 200.707 179.110 156.422 1.00 6.75   ? 439  LEU A CD2 1 
ATOM   3339 N  N   . LEU A 1 530 ? 198.659 174.544 154.312 1.00 5.87   ? 440  LEU A N   1 
ATOM   3340 C  CA  . LEU A 1 530 ? 197.860 173.939 153.259 1.00 5.61   ? 440  LEU A CA  1 
ATOM   3341 C  C   . LEU A 1 530 ? 196.421 173.799 153.727 1.00 5.31   ? 440  LEU A C   1 
ATOM   3342 O  O   . LEU A 1 530 ? 195.490 174.170 153.011 1.00 4.88   ? 440  LEU A O   1 
ATOM   3343 C  CB  . LEU A 1 530 ? 198.448 172.574 152.864 1.00 5.73   ? 440  LEU A CB  1 
ATOM   3344 C  CG  . LEU A 1 530 ? 197.858 171.853 151.598 1.00 5.31   ? 440  LEU A CG  1 
ATOM   3345 C  CD1 . LEU A 1 530 ? 196.635 171.020 151.984 1.00 5.23   ? 440  LEU A CD1 1 
ATOM   3346 C  CD2 . LEU A 1 530 ? 197.498 172.877 150.524 1.00 4.82   ? 440  LEU A CD2 1 
ATOM   3347 N  N   . LYS A 1 531 ? 196.235 173.280 154.937 1.00 5.42   ? 441  LYS A N   1 
ATOM   3348 C  CA  . LYS A 1 531 ? 194.895 173.104 155.475 1.00 5.22   ? 441  LYS A CA  1 
ATOM   3349 C  C   . LYS A 1 531 ? 194.160 174.436 155.559 1.00 5.05   ? 441  LYS A C   1 
ATOM   3350 O  O   . LYS A 1 531 ? 192.962 174.510 155.291 1.00 4.70   ? 441  LYS A O   1 
ATOM   3351 C  CB  . LYS A 1 531 ? 194.944 172.441 156.848 1.00 5.50   ? 441  LYS A CB  1 
ATOM   3352 C  CG  . LYS A 1 531 ? 193.582 172.037 157.385 1.00 5.50   ? 441  LYS A CG  1 
ATOM   3353 C  CD  . LYS A 1 531 ? 193.699 171.219 158.656 1.00 5.65   ? 441  LYS A CD  1 
ATOM   3354 C  CE  . LYS A 1 531 ? 192.330 170.760 159.135 1.00 5.89   ? 441  LYS A CE  1 
ATOM   3355 N  NZ  . LYS A 1 531 ? 192.406 170.019 160.424 1.00 6.46   ? 441  LYS A NZ  1 
ATOM   3356 N  N   . GLN A 1 532 ? 194.885 175.495 155.915 1.00 5.10   ? 442  GLN A N   1 
ATOM   3357 C  CA  . GLN A 1 532 ? 194.296 176.824 155.990 1.00 5.01   ? 442  GLN A CA  1 
ATOM   3358 C  C   . GLN A 1 532 ? 193.895 177.329 154.608 1.00 4.75   ? 442  GLN A C   1 
ATOM   3359 O  O   . GLN A 1 532 ? 192.803 177.866 154.429 1.00 4.42   ? 442  GLN A O   1 
ATOM   3360 C  CB  . GLN A 1 532 ? 195.285 177.810 156.623 1.00 5.16   ? 442  GLN A CB  1 
ATOM   3361 C  CG  . GLN A 1 532 ? 195.568 177.573 158.091 1.00 5.53   ? 442  GLN A CG  1 
ATOM   3362 C  CD  . GLN A 1 532 ? 194.434 178.003 158.980 1.00 5.44   ? 442  GLN A CD  1 
ATOM   3363 O  OE1 . GLN A 1 532 ? 194.020 179.164 158.962 1.00 5.52   ? 442  GLN A OE1 1 
ATOM   3364 N  NE2 . GLN A 1 532 ? 193.916 177.070 159.765 1.00 5.56   ? 442  GLN A NE2 1 
ATOM   3365 N  N   . ALA A 1 533 ? 194.759 177.111 153.620 1.00 4.67   ? 443  ALA A N   1 
ATOM   3366 C  CA  . ALA A 1 533 ? 194.502 177.577 152.260 1.00 4.56   ? 443  ALA A CA  1 
ATOM   3367 C  C   . ALA A 1 533 ? 193.237 176.956 151.683 1.00 4.29   ? 443  ALA A C   1 
ATOM   3368 O  O   . ALA A 1 533 ? 192.477 177.623 150.980 1.00 3.95   ? 443  ALA A O   1 
ATOM   3369 C  CB  . ALA A 1 533 ? 195.686 177.257 151.366 1.00 4.56   ? 443  ALA A CB  1 
ATOM   3370 N  N   . LEU A 1 534 ? 192.985 175.697 152.016 1.00 4.29   ? 444  LEU A N   1 
ATOM   3371 C  CA  . LEU A 1 534 ? 191.818 174.989 151.499 1.00 4.10   ? 444  LEU A CA  1 
ATOM   3372 C  C   . LEU A 1 534 ? 190.512 175.633 151.956 1.00 4.10   ? 444  LEU A C   1 
ATOM   3373 O  O   . LEU A 1 534 ? 189.478 175.500 151.294 1.00 3.80   ? 444  LEU A O   1 
ATOM   3374 C  CB  . LEU A 1 534 ? 191.839 173.524 151.951 1.00 4.15   ? 444  LEU A CB  1 
ATOM   3375 C  CG  . LEU A 1 534 ? 192.959 172.630 151.379 1.00 4.32   ? 444  LEU A CG  1 
ATOM   3376 C  CD1 . LEU A 1 534 ? 192.897 171.271 152.063 1.00 4.52   ? 444  LEU A CD1 1 
ATOM   3377 C  CD2 . LEU A 1 534 ? 192.799 172.478 149.874 1.00 3.95   ? 444  LEU A CD2 1 
ATOM   3378 N  N   . ASN A 1 535 ? 190.548 176.310 153.098 1.00 4.04   ? 445  ASN A N   1 
ATOM   3379 C  CA  . ASN A 1 535 ? 189.356 176.935 153.654 1.00 4.06   ? 445  ASN A CA  1 
ATOM   3380 C  C   . ASN A 1 535 ? 189.289 178.427 153.329 1.00 4.03   ? 445  ASN A C   1 
ATOM   3381 O  O   . ASN A 1 535 ? 188.207 178.981 153.145 1.00 3.89   ? 445  ASN A O   1 
ATOM   3382 C  CB  . ASN A 1 535 ? 189.312 176.718 155.154 1.00 4.05   ? 445  ASN A CB  1 
ATOM   3383 C  CG  . ASN A 1 535 ? 188.015 177.135 155.769 1.00 3.95   ? 445  ASN A CG  1 
ATOM   3384 O  OD1 . ASN A 1 535 ? 186.974 176.511 155.540 1.00 3.94   ? 445  ASN A OD1 1 
ATOM   3385 N  ND2 . ASN A 1 535 ? 188.054 178.180 156.552 1.00 3.92   ? 445  ASN A ND2 1 
ATOM   3386 N  N   . ILE A 1 536 ? 190.449 179.077 153.289 1.00 4.02   ? 446  ILE A N   1 
ATOM   3387 C  CA  . ILE A 1 536 ? 190.525 180.524 153.114 1.00 4.01   ? 446  ILE A CA  1 
ATOM   3388 C  C   . ILE A 1 536 ? 190.693 180.960 151.662 1.00 3.89   ? 446  ILE A C   1 
ATOM   3389 O  O   . ILE A 1 536 ? 190.054 181.913 151.223 1.00 3.76   ? 446  ILE A O   1 
ATOM   3390 C  CB  . ILE A 1 536 ? 191.675 181.102 153.958 1.00 4.14   ? 446  ILE A CB  1 
ATOM   3391 C  CG1 . ILE A 1 536 ? 191.360 180.910 155.451 1.00 4.21   ? 446  ILE A CG1 1 
ATOM   3392 C  CG2 . ILE A 1 536 ? 191.899 182.576 153.621 1.00 4.38   ? 446  ILE A CG2 1 
ATOM   3393 C  CD1 . ILE A 1 536 ? 192.535 181.153 156.370 1.00 4.77   ? 446  ILE A CD1 1 
ATOM   3394 N  N   . VAL A 1 537 ? 191.584 180.301 150.932 1.00 3.83   ? 447  VAL A N   1 
ATOM   3395 C  CA  . VAL A 1 537 ? 191.897 180.708 149.569 1.00 3.72   ? 447  VAL A CA  1 
ATOM   3396 C  C   . VAL A 1 537 ? 190.952 180.058 148.575 1.00 3.62   ? 447  VAL A C   1 
ATOM   3397 O  O   . VAL A 1 537 ? 190.461 180.706 147.652 1.00 3.40   ? 447  VAL A O   1 
ATOM   3398 C  CB  . VAL A 1 537 ? 193.349 180.338 149.215 1.00 3.80   ? 447  VAL A CB  1 
ATOM   3399 C  CG1 . VAL A 1 537 ? 193.638 180.662 147.751 1.00 3.58   ? 447  VAL A CG1 1 
ATOM   3400 C  CG2 . VAL A 1 537 ? 194.297 181.093 150.130 1.00 4.18   ? 447  VAL A CG2 1 
ATOM   3401 N  N   . GLY A 1 538 ? 190.698 178.771 148.775 1.00 3.60   ? 448  GLY A N   1 
ATOM   3402 C  CA  . GLY A 1 538 ? 189.897 177.972 147.855 1.00 3.45   ? 448  GLY A CA  1 
ATOM   3403 C  C   . GLY A 1 538 ? 188.443 178.426 147.785 1.00 3.36   ? 448  GLY A C   1 
ATOM   3404 O  O   . GLY A 1 538 ? 187.686 177.970 146.931 1.00 3.25   ? 448  GLY A O   1 
ATOM   3405 N  N   . THR A 1 539 ? 188.051 179.322 148.685 1.00 3.43   ? 449  THR A N   1 
ATOM   3406 C  CA  . THR A 1 539 ? 186.679 179.811 148.722 1.00 3.33   ? 449  THR A CA  1 
ATOM   3407 C  C   . THR A 1 539 ? 186.519 181.202 148.105 1.00 3.40   ? 449  THR A C   1 
ATOM   3408 O  O   . THR A 1 539 ? 185.398 181.638 147.836 1.00 3.10   ? 449  THR A O   1 
ATOM   3409 C  CB  . THR A 1 539 ? 186.142 179.822 150.167 1.00 3.43   ? 449  THR A CB  1 
ATOM   3410 O  OG1 . THR A 1 539 ? 184.711 179.779 150.140 1.00 3.32   ? 449  THR A OG1 1 
ATOM   3411 C  CG2 . THR A 1 539 ? 186.590 181.079 150.904 1.00 3.46   ? 449  THR A CG2 1 
ATOM   3412 N  N   . LEU A 1 540 ? 187.619 181.928 147.915 1.00 3.26   ? 450  LEU A N   1 
ATOM   3413 C  CA  . LEU A 1 540 ? 187.500 183.308 147.456 1.00 3.27   ? 450  LEU A CA  1 
ATOM   3414 C  C   . LEU A 1 540 ? 186.907 183.449 146.045 1.00 3.15   ? 450  LEU A C   1 
ATOM   3415 O  O   . LEU A 1 540 ? 186.048 184.309 145.847 1.00 3.01   ? 450  LEU A O   1 
ATOM   3416 C  CB  . LEU A 1 540 ? 188.846 184.054 147.577 1.00 3.34   ? 450  LEU A CB  1 
ATOM   3417 C  CG  . LEU A 1 540 ? 189.271 184.456 149.000 1.00 3.52   ? 450  LEU A CG  1 
ATOM   3418 C  CD1 . LEU A 1 540 ? 190.734 184.869 148.985 1.00 3.75   ? 450  LEU A CD1 1 
ATOM   3419 C  CD2 . LEU A 1 540 ? 188.403 185.610 149.493 1.00 3.84   ? 450  LEU A CD2 1 
ATOM   3420 N  N   . PRO A 1 541 ? 187.322 182.638 145.051 1.00 2.96   ? 451  PRO A N   1 
ATOM   3421 C  CA  . PRO A 1 541 ? 186.797 182.626 143.696 1.00 2.90   ? 451  PRO A CA  1 
ATOM   3422 C  C   . PRO A 1 541 ? 185.334 182.207 143.652 1.00 2.95   ? 451  PRO A C   1 
ATOM   3423 O  O   . PRO A 1 541 ? 184.606 182.571 142.733 1.00 2.70   ? 451  PRO A O   1 
ATOM   3424 C  CB  . PRO A 1 541 ? 187.683 181.585 143.000 1.00 2.83   ? 451  PRO A CB  1 
ATOM   3425 C  CG  . PRO A 1 541 ? 188.914 181.493 143.856 1.00 3.02   ? 451  PRO A CG  1 
ATOM   3426 C  CD  . PRO A 1 541 ? 188.425 181.699 145.260 1.00 3.09   ? 451  PRO A CD  1 
ATOM   3427 N  N   . PHE A 1 542 ? 184.903 181.457 144.661 1.00 2.93   ? 452  PHE A N   1 
ATOM   3428 C  CA  . PHE A 1 542 ? 183.520 181.012 144.750 1.00 2.93   ? 452  PHE A CA  1 
ATOM   3429 C  C   . PHE A 1 542 ? 182.633 182.189 145.112 1.00 2.98   ? 452  PHE A C   1 
ATOM   3430 O  O   . PHE A 1 542 ? 181.616 182.443 144.466 1.00 2.75   ? 452  PHE A O   1 
ATOM   3431 C  CB  . PHE A 1 542 ? 183.382 179.906 145.799 1.00 2.98   ? 452  PHE A CB  1 
ATOM   3432 C  CG  . PHE A 1 542 ? 181.996 179.351 145.947 1.00 2.97   ? 452  PHE A CG  1 
ATOM   3433 C  CD1 . PHE A 1 542 ? 181.108 179.900 146.857 1.00 3.01   ? 452  PHE A CD1 1 
ATOM   3434 C  CD2 . PHE A 1 542 ? 181.585 178.268 145.196 1.00 2.94   ? 452  PHE A CD2 1 
ATOM   3435 C  CE1 . PHE A 1 542 ? 179.838 179.388 147.001 1.00 2.99   ? 452  PHE A CE1 1 
ATOM   3436 C  CE2 . PHE A 1 542 ? 180.317 177.752 145.341 1.00 2.96   ? 452  PHE A CE2 1 
ATOM   3437 C  CZ  . PHE A 1 542 ? 179.442 178.315 146.243 1.00 2.96   ? 452  PHE A CZ  1 
ATOM   3438 N  N   . THR A 1 543 ? 183.033 182.910 146.153 1.00 2.92   ? 453  THR A N   1 
ATOM   3439 C  CA  . THR A 1 543 ? 182.282 184.060 146.629 1.00 2.93   ? 453  THR A CA  1 
ATOM   3440 C  C   . THR A 1 543 ? 182.247 185.155 145.574 1.00 2.94   ? 453  THR A C   1 
ATOM   3441 O  O   . THR A 1 543 ? 181.201 185.744 145.305 1.00 2.77   ? 453  THR A O   1 
ATOM   3442 C  CB  . THR A 1 543 ? 182.891 184.604 147.935 1.00 3.17   ? 453  THR A CB  1 
ATOM   3443 O  OG1 . THR A 1 543 ? 182.842 183.589 148.944 1.00 3.18   ? 453  THR A OG1 1 
ATOM   3444 C  CG2 . THR A 1 543 ? 182.124 185.826 148.419 1.00 3.37   ? 453  THR A CG2 1 
ATOM   3445 N  N   . TYR A 1 544 ? 183.402 185.414 144.973 1.00 2.91   ? 454  TYR A N   1 
ATOM   3446 C  CA  . TYR A 1 544 ? 183.520 186.424 143.932 1.00 2.85   ? 454  TYR A CA  1 
ATOM   3447 C  C   . TYR A 1 544 ? 182.622 186.111 142.745 1.00 2.80   ? 454  TYR A C   1 
ATOM   3448 O  O   . TYR A 1 544 ? 181.872 186.971 142.278 1.00 2.66   ? 454  TYR A O   1 
ATOM   3449 C  CB  . TYR A 1 544 ? 184.979 186.538 143.487 1.00 2.94   ? 454  TYR A CB  1 
ATOM   3450 C  CG  . TYR A 1 544 ? 185.186 187.403 142.276 1.00 2.91   ? 454  TYR A CG  1 
ATOM   3451 C  CD1 . TYR A 1 544 ? 185.390 186.811 141.043 1.00 2.89   ? 454  TYR A CD1 1 
ATOM   3452 C  CD2 . TYR A 1 544 ? 185.169 188.778 142.389 1.00 3.14   ? 454  TYR A CD2 1 
ATOM   3453 C  CE1 . TYR A 1 544 ? 185.572 187.588 139.927 1.00 2.93   ? 454  TYR A CE1 1 
ATOM   3454 C  CE2 . TYR A 1 544 ? 185.351 189.560 141.270 1.00 3.28   ? 454  TYR A CE2 1 
ATOM   3455 C  CZ  . TYR A 1 544 ? 185.551 188.967 140.040 1.00 3.13   ? 454  TYR A CZ  1 
ATOM   3456 O  OH  . TYR A 1 544 ? 185.727 189.745 138.916 1.00 3.12   ? 454  TYR A OH  1 
ATOM   3457 N  N   . MET A 1 545 ? 182.713 184.884 142.244 1.00 2.64   ? 455  MET A N   1 
ATOM   3458 C  CA  . MET A 1 545 ? 181.965 184.472 141.065 1.00 2.64   ? 455  MET A CA  1 
ATOM   3459 C  C   . MET A 1 545 ? 180.459 184.495 141.301 1.00 2.62   ? 455  MET A C   1 
ATOM   3460 O  O   . MET A 1 545 ? 179.696 184.896 140.420 1.00 2.45   ? 455  MET A O   1 
ATOM   3461 C  CB  . MET A 1 545 ? 182.438 183.086 140.630 1.00 2.54   ? 455  MET A CB  1 
ATOM   3462 C  CG  . MET A 1 545 ? 181.770 182.533 139.392 1.00 2.40   ? 455  MET A CG  1 
ATOM   3463 S  SD  . MET A 1 545 ? 180.308 181.564 139.766 1.00 2.44   ? 455  MET A SD  1 
ATOM   3464 C  CE  . MET A 1 545 ? 179.495 181.611 138.197 1.00 2.26   ? 455  MET A CE  1 
ATOM   3465 N  N   . LEU A 1 546 ? 180.029 184.067 142.483 1.00 2.57   ? 456  LEU A N   1 
ATOM   3466 C  CA  . LEU A 1 546 ? 178.608 184.003 142.794 1.00 2.65   ? 456  LEU A CA  1 
ATOM   3467 C  C   . LEU A 1 546 ? 177.974 185.386 142.826 1.00 2.66   ? 456  LEU A C   1 
ATOM   3468 O  O   . LEU A 1 546 ? 176.908 185.598 142.245 1.00 2.47   ? 456  LEU A O   1 
ATOM   3469 C  CB  . LEU A 1 546 ? 178.394 183.294 144.139 1.00 2.62   ? 456  LEU A CB  1 
ATOM   3470 C  CG  . LEU A 1 546 ? 176.933 182.956 144.514 1.00 2.59   ? 456  LEU A CG  1 
ATOM   3471 C  CD1 . LEU A 1 546 ? 176.922 181.671 145.312 1.00 2.78   ? 456  LEU A CD1 1 
ATOM   3472 C  CD2 . LEU A 1 546 ? 176.321 184.088 145.341 1.00 2.76   ? 456  LEU A CD2 1 
ATOM   3473 N  N   . GLU A 1 547 ? 178.623 186.334 143.500 1.00 2.63   ? 457  GLU A N   1 
ATOM   3474 C  CA  . GLU A 1 547 ? 178.077 187.683 143.587 1.00 2.69   ? 457  GLU A CA  1 
ATOM   3475 C  C   . GLU A 1 547 ? 178.096 188.377 142.246 1.00 2.91   ? 457  GLU A C   1 
ATOM   3476 O  O   . GLU A 1 547 ? 177.169 189.112 141.910 1.00 2.63   ? 457  GLU A O   1 
ATOM   3477 C  CB  . GLU A 1 547 ? 178.836 188.522 144.610 1.00 2.91   ? 457  GLU A CB  1 
ATOM   3478 C  CG  . GLU A 1 547 ? 178.557 188.156 146.047 1.00 3.01   ? 457  GLU A CG  1 
ATOM   3479 C  CD  . GLU A 1 547 ? 177.131 188.489 146.491 1.00 3.06   ? 457  GLU A CD  1 
ATOM   3480 O  OE1 . GLU A 1 547 ? 176.221 187.924 145.944 1.00 2.95   ? 457  GLU A OE1 1 
ATOM   3481 O  OE2 . GLU A 1 547 ? 176.962 189.273 147.404 1.00 3.22   ? 457  GLU A OE2 1 
ATOM   3482 N  N   . LYS A 1 548 ? 179.142 188.141 141.468 1.00 2.58   ? 458  LYS A N   1 
ATOM   3483 C  CA  . LYS A 1 548 ? 179.246 188.757 140.162 1.00 2.57   ? 458  LYS A CA  1 
ATOM   3484 C  C   . LYS A 1 548 ? 178.072 188.331 139.289 1.00 2.56   ? 458  LYS A C   1 
ATOM   3485 O  O   . LYS A 1 548 ? 177.456 189.158 138.619 1.00 2.45   ? 458  LYS A O   1 
ATOM   3486 C  CB  . LYS A 1 548 ? 180.581 188.400 139.514 1.00 2.45   ? 458  LYS A CB  1 
ATOM   3487 C  CG  . LYS A 1 548 ? 180.868 189.118 138.214 1.00 2.53   ? 458  LYS A CG  1 
ATOM   3488 C  CD  . LYS A 1 548 ? 182.269 188.805 137.719 1.00 2.62   ? 458  LYS A CD  1 
ATOM   3489 C  CE  . LYS A 1 548 ? 182.587 189.557 136.440 1.00 2.60   ? 458  LYS A CE  1 
ATOM   3490 N  NZ  . LYS A 1 548 ? 184.003 189.372 136.027 1.00 2.86   ? 458  LYS A NZ  1 
ATOM   3491 N  N   . TRP A 1 549 ? 177.732 187.041 139.336 1.00 2.39   ? 459  TRP A N   1 
ATOM   3492 C  CA  . TRP A 1 549 ? 176.596 186.531 138.578 1.00 2.45   ? 459  TRP A CA  1 
ATOM   3493 C  C   . TRP A 1 549 ? 175.291 187.172 139.032 1.00 2.57   ? 459  TRP A C   1 
ATOM   3494 O  O   . TRP A 1 549 ? 174.508 187.634 138.201 1.00 2.39   ? 459  TRP A O   1 
ATOM   3495 C  CB  . TRP A 1 549 ? 176.497 185.006 138.713 1.00 2.28   ? 459  TRP A CB  1 
ATOM   3496 C  CG  . TRP A 1 549 ? 175.366 184.376 137.916 1.00 2.24   ? 459  TRP A CG  1 
ATOM   3497 C  CD1 . TRP A 1 549 ? 175.407 183.984 136.612 1.00 2.30   ? 459  TRP A CD1 1 
ATOM   3498 C  CD2 . TRP A 1 549 ? 174.033 184.050 138.385 1.00 2.21   ? 459  TRP A CD2 1 
ATOM   3499 N  NE1 . TRP A 1 549 ? 174.199 183.444 136.243 1.00 2.27   ? 459  TRP A NE1 1 
ATOM   3500 C  CE2 . TRP A 1 549 ? 173.352 183.476 137.312 1.00 2.24   ? 459  TRP A CE2 1 
ATOM   3501 C  CE3 . TRP A 1 549 ? 173.377 184.194 139.609 1.00 2.28   ? 459  TRP A CE3 1 
ATOM   3502 C  CZ2 . TRP A 1 549 ? 172.039 183.049 137.421 1.00 2.22   ? 459  TRP A CZ2 1 
ATOM   3503 C  CZ3 . TRP A 1 549 ? 172.061 183.770 139.717 1.00 2.25   ? 459  TRP A CZ3 1 
ATOM   3504 C  CH2 . TRP A 1 549 ? 171.408 183.212 138.650 1.00 2.23   ? 459  TRP A CH2 1 
ATOM   3505 N  N   . ARG A 1 550 ? 175.051 187.217 140.343 1.00 2.40   ? 460  ARG A N   1 
ATOM   3506 C  CA  . ARG A 1 550 ? 173.796 187.777 140.836 1.00 2.56   ? 460  ARG A CA  1 
ATOM   3507 C  C   . ARG A 1 550 ? 173.659 189.250 140.491 1.00 2.70   ? 460  ARG A C   1 
ATOM   3508 O  O   . ARG A 1 550 ? 172.582 189.703 140.114 1.00 2.63   ? 460  ARG A O   1 
ATOM   3509 C  CB  . ARG A 1 550 ? 173.651 187.604 142.343 1.00 2.56   ? 460  ARG A CB  1 
ATOM   3510 C  CG  . ARG A 1 550 ? 173.332 186.188 142.795 1.00 2.55   ? 460  ARG A CG  1 
ATOM   3511 C  CD  . ARG A 1 550 ? 172.624 186.153 144.102 1.00 2.62   ? 460  ARG A CD  1 
ATOM   3512 N  NE  . ARG A 1 550 ? 173.456 186.609 145.197 1.00 2.82   ? 460  ARG A NE  1 
ATOM   3513 C  CZ  . ARG A 1 550 ? 173.118 186.547 146.497 1.00 2.91   ? 460  ARG A CZ  1 
ATOM   3514 N  NH1 . ARG A 1 550 ? 171.973 186.039 146.884 1.00 2.77   ? 460  ARG A NH1 1 
ATOM   3515 N  NH2 . ARG A 1 550 ? 173.946 187.011 147.395 1.00 2.99   ? 460  ARG A NH2 1 
ATOM   3516 N  N   . TRP A 1 551 ? 174.757 189.995 140.583 1.00 2.50   ? 461  TRP A N   1 
ATOM   3517 C  CA  . TRP A 1 551 ? 174.725 191.412 140.257 1.00 2.70   ? 461  TRP A CA  1 
ATOM   3518 C  C   . TRP A 1 551 ? 174.318 191.625 138.808 1.00 2.74   ? 461  TRP A C   1 
ATOM   3519 O  O   . TRP A 1 551 ? 173.503 192.497 138.509 1.00 2.67   ? 461  TRP A O   1 
ATOM   3520 C  CB  . TRP A 1 551 ? 176.093 192.056 140.502 1.00 2.72   ? 461  TRP A CB  1 
ATOM   3521 C  CG  . TRP A 1 551 ? 176.424 192.287 141.955 1.00 2.83   ? 461  TRP A CG  1 
ATOM   3522 C  CD1 . TRP A 1 551 ? 175.564 192.253 143.010 1.00 2.90   ? 461  TRP A CD1 1 
ATOM   3523 C  CD2 . TRP A 1 551 ? 177.723 192.602 142.511 1.00 2.92   ? 461  TRP A CD2 1 
ATOM   3524 N  NE1 . TRP A 1 551 ? 176.236 192.522 144.173 1.00 3.09   ? 461  TRP A NE1 1 
ATOM   3525 C  CE2 . TRP A 1 551 ? 177.554 192.735 143.887 1.00 3.05   ? 461  TRP A CE2 1 
ATOM   3526 C  CE3 . TRP A 1 551 ? 178.996 192.779 141.958 1.00 3.03   ? 461  TRP A CE3 1 
ATOM   3527 C  CZ2 . TRP A 1 551 ? 178.612 193.037 144.730 1.00 3.19   ? 461  TRP A CZ2 1 
ATOM   3528 C  CZ3 . TRP A 1 551 ? 180.055 193.084 142.803 1.00 3.35   ? 461  TRP A CZ3 1 
ATOM   3529 C  CH2 . TRP A 1 551 ? 179.867 193.208 144.154 1.00 3.41   ? 461  TRP A CH2 1 
ATOM   3530 N  N   . MET A 1 552 ? 174.871 190.815 137.910 1.00 2.49   ? 462  MET A N   1 
ATOM   3531 C  CA  . MET A 1 552 ? 174.566 190.915 136.490 1.00 2.66   ? 462  MET A CA  1 
ATOM   3532 C  C   . MET A 1 552 ? 173.128 190.499 136.183 1.00 3.21   ? 462  MET A C   1 
ATOM   3533 O  O   . MET A 1 552 ? 172.488 191.056 135.287 1.00 2.52   ? 462  MET A O   1 
ATOM   3534 C  CB  . MET A 1 552 ? 175.560 190.079 135.701 1.00 2.51   ? 462  MET A CB  1 
ATOM   3535 C  CG  . MET A 1 552 ? 176.981 190.621 135.730 1.00 2.53   ? 462  MET A CG  1 
ATOM   3536 S  SD  . MET A 1 552 ? 178.162 189.549 134.899 1.00 2.62   ? 462  MET A SD  1 
ATOM   3537 C  CE  . MET A 1 552 ? 177.757 189.857 133.185 1.00 2.56   ? 462  MET A CE  1 
ATOM   3538 N  N   . VAL A 1 553 ? 172.610 189.538 136.942 1.00 2.52   ? 463  VAL A N   1 
ATOM   3539 C  CA  . VAL A 1 553 ? 171.224 189.107 136.790 1.00 2.60   ? 463  VAL A CA  1 
ATOM   3540 C  C   . VAL A 1 553 ? 170.248 190.193 137.220 1.00 2.74   ? 463  VAL A C   1 
ATOM   3541 O  O   . VAL A 1 553 ? 169.263 190.456 136.530 1.00 2.67   ? 463  VAL A O   1 
ATOM   3542 C  CB  . VAL A 1 553 ? 170.965 187.819 137.591 1.00 2.42   ? 463  VAL A CB  1 
ATOM   3543 C  CG1 . VAL A 1 553 ? 169.473 187.516 137.662 1.00 2.53   ? 463  VAL A CG1 1 
ATOM   3544 C  CG2 . VAL A 1 553 ? 171.681 186.669 136.915 1.00 2.46   ? 463  VAL A CG2 1 
ATOM   3545 N  N   . PHE A 1 554 ? 170.519 190.829 138.354 1.00 2.70   ? 464  PHE A N   1 
ATOM   3546 C  CA  . PHE A 1 554 ? 169.653 191.895 138.837 1.00 2.86   ? 464  PHE A CA  1 
ATOM   3547 C  C   . PHE A 1 554 ? 169.735 193.111 137.927 1.00 3.00   ? 464  PHE A C   1 
ATOM   3548 O  O   . PHE A 1 554 ? 168.719 193.737 137.627 1.00 2.96   ? 464  PHE A O   1 
ATOM   3549 C  CB  . PHE A 1 554 ? 170.023 192.300 140.268 1.00 3.05   ? 464  PHE A CB  1 
ATOM   3550 C  CG  . PHE A 1 554 ? 169.638 191.290 141.312 1.00 3.01   ? 464  PHE A CG  1 
ATOM   3551 C  CD1 . PHE A 1 554 ? 170.596 190.722 142.134 1.00 2.87   ? 464  PHE A CD1 1 
ATOM   3552 C  CD2 . PHE A 1 554 ? 168.324 190.900 141.468 1.00 2.98   ? 464  PHE A CD2 1 
ATOM   3553 C  CE1 . PHE A 1 554 ? 170.247 189.784 143.081 1.00 2.89   ? 464  PHE A CE1 1 
ATOM   3554 C  CE2 . PHE A 1 554 ? 167.972 189.960 142.412 1.00 2.95   ? 464  PHE A CE2 1 
ATOM   3555 C  CZ  . PHE A 1 554 ? 168.938 189.399 143.217 1.00 2.94   ? 464  PHE A CZ  1 
ATOM   3556 N  N   . GLU A 1 555 ? 170.946 193.429 137.475 1.00 2.85   ? 465  GLU A N   1 
ATOM   3557 C  CA  . GLU A 1 555 ? 171.177 194.564 136.592 1.00 2.98   ? 465  GLU A CA  1 
ATOM   3558 C  C   . GLU A 1 555 ? 170.484 194.389 135.249 1.00 2.88   ? 465  GLU A C   1 
ATOM   3559 O  O   . GLU A 1 555 ? 169.963 195.350 134.684 1.00 3.09   ? 465  GLU A O   1 
ATOM   3560 C  CB  . GLU A 1 555 ? 172.674 194.774 136.370 1.00 2.92   ? 465  GLU A CB  1 
ATOM   3561 N  N   . GLY A 1 556 ? 170.491 193.164 134.732 1.00 2.74   ? 466  GLY A N   1 
ATOM   3562 C  CA  . GLY A 1 556 ? 169.883 192.880 133.442 1.00 2.74   ? 466  GLY A CA  1 
ATOM   3563 C  C   . GLY A 1 556 ? 170.930 192.632 132.362 1.00 2.72   ? 466  GLY A C   1 
ATOM   3564 O  O   . GLY A 1 556 ? 170.618 192.659 131.172 1.00 2.77   ? 466  GLY A O   1 
ATOM   3565 N  N   . LYS A 1 557 ? 172.174 192.398 132.776 1.00 2.71   ? 467  LYS A N   1 
ATOM   3566 C  CA  . LYS A 1 557 ? 173.241 192.105 131.830 1.00 2.71   ? 467  LYS A CA  1 
ATOM   3567 C  C   . LYS A 1 557 ? 173.104 190.681 131.323 1.00 2.69   ? 467  LYS A C   1 
ATOM   3568 O  O   . LYS A 1 557 ? 173.442 190.383 130.177 1.00 2.80   ? 467  LYS A O   1 
ATOM   3569 C  CB  . LYS A 1 557 ? 174.610 192.312 132.474 1.00 2.76   ? 467  LYS A CB  1 
ATOM   3570 N  N   . ILE A 1 558 ? 172.584 189.807 132.177 1.00 2.56   ? 468  ILE A N   1 
ATOM   3571 C  CA  . ILE A 1 558 ? 172.322 188.434 131.783 1.00 2.56   ? 468  ILE A CA  1 
ATOM   3572 C  C   . ILE A 1 558 ? 170.812 188.201 131.720 1.00 2.55   ? 468  ILE A C   1 
ATOM   3573 O  O   . ILE A 1 558 ? 170.153 188.203 132.760 1.00 2.50   ? 468  ILE A O   1 
ATOM   3574 C  CB  . ILE A 1 558 ? 172.930 187.433 132.780 1.00 2.48   ? 468  ILE A CB  1 
ATOM   3575 C  CG1 . ILE A 1 558 ? 174.430 187.669 132.925 1.00 2.50   ? 468  ILE A CG1 1 
ATOM   3576 C  CG2 . ILE A 1 558 ? 172.665 186.018 132.286 1.00 2.42   ? 468  ILE A CG2 1 
ATOM   3577 C  CD1 . ILE A 1 558 ? 175.059 186.928 134.093 1.00 2.36   ? 468  ILE A CD1 1 
ATOM   3578 N  N   . PRO A 1 559 ? 170.244 187.996 130.528 1.00 2.48   ? 469  PRO A N   1 
ATOM   3579 C  CA  . PRO A 1 559 ? 168.835 187.769 130.281 1.00 2.43   ? 469  PRO A CA  1 
ATOM   3580 C  C   . PRO A 1 559 ? 168.441 186.379 130.759 1.00 2.50   ? 469  PRO A C   1 
ATOM   3581 O  O   . PRO A 1 559 ? 169.292 185.501 130.882 1.00 2.24   ? 469  PRO A O   1 
ATOM   3582 C  CB  . PRO A 1 559 ? 168.736 187.930 128.762 1.00 2.45   ? 469  PRO A CB  1 
ATOM   3583 C  CG  . PRO A 1 559 ? 170.105 187.549 128.243 1.00 2.49   ? 469  PRO A CG  1 
ATOM   3584 C  CD  . PRO A 1 559 ? 171.082 187.978 129.324 1.00 2.52   ? 469  PRO A CD  1 
ATOM   3585 N  N   . LYS A 1 560 ? 167.152 186.174 131.012 1.00 2.45   ? 470  LYS A N   1 
ATOM   3586 C  CA  . LYS A 1 560 ? 166.663 184.900 131.537 1.00 2.45   ? 470  LYS A CA  1 
ATOM   3587 C  C   . LYS A 1 560 ? 167.092 183.713 130.685 1.00 2.50   ? 470  LYS A C   1 
ATOM   3588 O  O   . LYS A 1 560 ? 167.400 182.643 131.209 1.00 2.34   ? 470  LYS A O   1 
ATOM   3589 C  CB  . LYS A 1 560 ? 165.142 184.922 131.653 1.00 2.41   ? 470  LYS A CB  1 
ATOM   3590 N  N   . GLU A 1 561 ? 167.127 183.911 129.377 1.00 2.42   ? 471  GLU A N   1 
ATOM   3591 C  CA  . GLU A 1 561 ? 167.452 182.850 128.434 1.00 2.47   ? 471  GLU A CA  1 
ATOM   3592 C  C   . GLU A 1 561 ? 168.895 182.369 128.541 1.00 2.48   ? 471  GLU A C   1 
ATOM   3593 O  O   . GLU A 1 561 ? 169.252 181.350 127.952 1.00 2.49   ? 471  GLU A O   1 
ATOM   3594 C  CB  . GLU A 1 561 ? 167.173 183.326 127.008 1.00 2.51   ? 471  GLU A CB  1 
ATOM   3595 C  CG  . GLU A 1 561 ? 165.706 183.621 126.727 1.00 2.52   ? 471  GLU A CG  1 
ATOM   3596 C  CD  . GLU A 1 561 ? 165.267 184.964 127.246 1.00 2.60   ? 471  GLU A CD  1 
ATOM   3597 O  OE1 . GLU A 1 561 ? 166.113 185.740 127.619 1.00 2.52   ? 471  GLU A OE1 1 
ATOM   3598 O  OE2 . GLU A 1 561 ? 164.086 185.211 127.276 1.00 2.74   ? 471  GLU A OE2 1 
ATOM   3599 N  N   . GLN A 1 562 ? 169.740 183.124 129.239 1.00 2.35   ? 472  GLN A N   1 
ATOM   3600 C  CA  . GLN A 1 562 ? 171.147 182.766 129.362 1.00 2.39   ? 472  GLN A CA  1 
ATOM   3601 C  C   . GLN A 1 562 ? 171.605 182.624 130.809 1.00 2.68   ? 472  GLN A C   1 
ATOM   3602 O  O   . GLN A 1 562 ? 172.800 182.711 131.089 1.00 2.17   ? 472  GLN A O   1 
ATOM   3603 C  CB  . GLN A 1 562 ? 172.021 183.804 128.660 1.00 2.35   ? 472  GLN A CB  1 
ATOM   3604 C  CG  . GLN A 1 562 ? 171.788 183.909 127.174 1.00 2.35   ? 472  GLN A CG  1 
ATOM   3605 C  CD  . GLN A 1 562 ? 172.721 184.899 126.520 1.00 2.28   ? 472  GLN A CD  1 
ATOM   3606 O  OE1 . GLN A 1 562 ? 173.192 185.847 127.156 1.00 2.53   ? 472  GLN A OE1 1 
ATOM   3607 N  NE2 . GLN A 1 562 ? 173.001 184.687 125.242 1.00 2.38   ? 472  GLN A NE2 1 
ATOM   3608 N  N   . TRP A 1 563 ? 170.677 182.420 131.737 1.00 2.29   ? 473  TRP A N   1 
ATOM   3609 C  CA  . TRP A 1 563 ? 171.061 182.337 133.143 1.00 2.32   ? 473  TRP A CA  1 
ATOM   3610 C  C   . TRP A 1 563 ? 172.043 181.206 133.420 1.00 2.40   ? 473  TRP A C   1 
ATOM   3611 O  O   . TRP A 1 563 ? 173.098 181.430 134.018 1.00 2.24   ? 473  TRP A O   1 
ATOM   3612 C  CB  . TRP A 1 563 ? 169.832 182.163 134.035 1.00 2.33   ? 473  TRP A CB  1 
ATOM   3613 C  CG  . TRP A 1 563 ? 169.161 183.445 134.419 1.00 2.34   ? 473  TRP A CG  1 
ATOM   3614 C  CD1 . TRP A 1 563 ? 169.414 184.682 133.929 1.00 2.40   ? 473  TRP A CD1 1 
ATOM   3615 C  CD2 . TRP A 1 563 ? 168.121 183.613 135.399 1.00 2.33   ? 473  TRP A CD2 1 
ATOM   3616 N  NE1 . TRP A 1 563 ? 168.607 185.602 134.529 1.00 2.45   ? 473  TRP A NE1 1 
ATOM   3617 C  CE2 . TRP A 1 563 ? 167.810 184.968 135.432 1.00 2.36   ? 473  TRP A CE2 1 
ATOM   3618 C  CE3 . TRP A 1 563 ? 167.440 182.735 136.241 1.00 2.37   ? 473  TRP A CE3 1 
ATOM   3619 C  CZ2 . TRP A 1 563 ? 166.845 185.476 136.275 1.00 2.40   ? 473  TRP A CZ2 1 
ATOM   3620 C  CZ3 . TRP A 1 563 ? 166.473 183.243 137.085 1.00 2.43   ? 473  TRP A CZ3 1 
ATOM   3621 C  CH2 . TRP A 1 563 ? 166.186 184.580 137.103 1.00 2.43   ? 473  TRP A CH2 1 
ATOM   3622 N  N   . MET A 1 564 ? 171.711 179.993 132.983 1.00 2.27   ? 474  MET A N   1 
ATOM   3623 C  CA  . MET A 1 564 ? 172.575 178.846 133.244 1.00 2.32   ? 474  MET A CA  1 
ATOM   3624 C  C   . MET A 1 564 ? 173.755 178.813 132.297 1.00 2.36   ? 474  MET A C   1 
ATOM   3625 O  O   . MET A 1 564 ? 174.839 178.354 132.658 1.00 2.22   ? 474  MET A O   1 
ATOM   3626 C  CB  . MET A 1 564 ? 171.791 177.543 133.174 1.00 2.43   ? 474  MET A CB  1 
ATOM   3627 C  CG  . MET A 1 564 ? 170.759 177.383 134.266 1.00 2.42   ? 474  MET A CG  1 
ATOM   3628 S  SD  . MET A 1 564 ? 171.475 177.457 135.919 1.00 2.53   ? 474  MET A SD  1 
ATOM   3629 C  CE  . MET A 1 564 ? 171.059 179.141 136.389 1.00 2.31   ? 474  MET A CE  1 
ATOM   3630 N  N   . GLU A 1 565 ? 173.561 179.337 131.096 1.00 2.28   ? 475  GLU A N   1 
ATOM   3631 C  CA  . GLU A 1 565 ? 174.654 179.411 130.144 1.00 2.31   ? 475  GLU A CA  1 
ATOM   3632 C  C   . GLU A 1 565 ? 175.811 180.220 130.718 1.00 2.28   ? 475  GLU A C   1 
ATOM   3633 O  O   . GLU A 1 565 ? 176.965 179.794 130.656 1.00 2.18   ? 475  GLU A O   1 
ATOM   3634 C  CB  . GLU A 1 565 ? 174.184 180.036 128.831 1.00 2.26   ? 475  GLU A CB  1 
ATOM   3635 N  N   . LYS A 1 566 ? 175.497 181.374 131.306 1.00 2.19   ? 476  LYS A N   1 
ATOM   3636 C  CA  . LYS A 1 566 ? 176.528 182.240 131.860 1.00 2.25   ? 476  LYS A CA  1 
ATOM   3637 C  C   . LYS A 1 566 ? 177.038 181.735 133.199 1.00 2.42   ? 476  LYS A C   1 
ATOM   3638 O  O   . LYS A 1 566 ? 178.204 181.931 133.534 1.00 2.10   ? 476  LYS A O   1 
ATOM   3639 C  CB  . LYS A 1 566 ? 176.016 183.672 131.997 1.00 2.26   ? 476  LYS A CB  1 
ATOM   3640 C  CG  . LYS A 1 566 ? 175.688 184.355 130.673 1.00 2.28   ? 476  LYS A CG  1 
ATOM   3641 C  CD  . LYS A 1 566 ? 176.895 184.423 129.752 1.00 2.29   ? 476  LYS A CD  1 
ATOM   3642 C  CE  . LYS A 1 566 ? 176.596 185.236 128.507 1.00 2.31   ? 476  LYS A CE  1 
ATOM   3643 N  NZ  . LYS A 1 566 ? 177.729 185.203 127.543 1.00 2.23   ? 476  LYS A NZ  1 
ATOM   3644 N  N   . TRP A 1 567 ? 176.180 181.075 133.965 1.00 2.22   ? 477  TRP A N   1 
ATOM   3645 C  CA  . TRP A 1 567 ? 176.609 180.530 135.243 1.00 2.24   ? 477  TRP A CA  1 
ATOM   3646 C  C   . TRP A 1 567 ? 177.777 179.578 135.055 1.00 2.33   ? 477  TRP A C   1 
ATOM   3647 O  O   . TRP A 1 567 ? 178.806 179.709 135.715 1.00 2.18   ? 477  TRP A O   1 
ATOM   3648 C  CB  . TRP A 1 567 ? 175.457 179.798 135.934 1.00 2.25   ? 477  TRP A CB  1 
ATOM   3649 C  CG  . TRP A 1 567 ? 175.846 179.122 137.219 1.00 2.12   ? 477  TRP A CG  1 
ATOM   3650 C  CD1 . TRP A 1 567 ? 176.014 177.790 137.412 1.00 2.33   ? 477  TRP A CD1 1 
ATOM   3651 C  CD2 . TRP A 1 567 ? 176.110 179.743 138.492 1.00 2.17   ? 477  TRP A CD2 1 
ATOM   3652 N  NE1 . TRP A 1 567 ? 176.361 177.541 138.709 1.00 2.37   ? 477  TRP A NE1 1 
ATOM   3653 C  CE2 . TRP A 1 567 ? 176.426 178.723 139.384 1.00 2.16   ? 477  TRP A CE2 1 
ATOM   3654 C  CE3 . TRP A 1 567 ? 176.102 181.059 138.940 1.00 2.20   ? 477  TRP A CE3 1 
ATOM   3655 C  CZ2 . TRP A 1 567 ? 176.733 178.977 140.707 1.00 2.20   ? 477  TRP A CZ2 1 
ATOM   3656 C  CZ3 . TRP A 1 567 ? 176.410 181.318 140.264 1.00 2.25   ? 477  TRP A CZ3 1 
ATOM   3657 C  CH2 . TRP A 1 567 ? 176.718 180.304 141.125 1.00 2.30   ? 477  TRP A CH2 1 
ATOM   3658 N  N   . TRP A 1 568 ? 177.617 178.610 134.160 1.00 2.19   ? 478  TRP A N   1 
ATOM   3659 C  CA  . TRP A 1 568 ? 178.654 177.608 133.971 1.00 2.29   ? 478  TRP A CA  1 
ATOM   3660 C  C   . TRP A 1 568 ? 179.840 178.118 133.162 1.00 2.33   ? 478  TRP A C   1 
ATOM   3661 O  O   . TRP A 1 568 ? 180.965 177.659 133.356 1.00 2.32   ? 478  TRP A O   1 
ATOM   3662 C  CB  . TRP A 1 568 ? 178.065 176.333 133.382 1.00 2.39   ? 478  TRP A CB  1 
ATOM   3663 C  CG  . TRP A 1 568 ? 177.411 175.516 134.449 1.00 2.46   ? 478  TRP A CG  1 
ATOM   3664 C  CD1 . TRP A 1 568 ? 176.084 175.271 134.615 1.00 2.44   ? 478  TRP A CD1 1 
ATOM   3665 C  CD2 . TRP A 1 568 ? 178.079 174.864 135.549 1.00 2.53   ? 478  TRP A CD2 1 
ATOM   3666 N  NE1 . TRP A 1 568 ? 175.886 174.515 135.744 1.00 2.49   ? 478  TRP A NE1 1 
ATOM   3667 C  CE2 . TRP A 1 568 ? 177.096 174.261 136.324 1.00 2.59   ? 478  TRP A CE2 1 
ATOM   3668 C  CE3 . TRP A 1 568 ? 179.419 174.753 135.935 1.00 2.56   ? 478  TRP A CE3 1 
ATOM   3669 C  CZ2 . TRP A 1 568 ? 177.403 173.556 137.468 1.00 2.56   ? 478  TRP A CZ2 1 
ATOM   3670 C  CZ3 . TRP A 1 568 ? 179.728 174.043 137.079 1.00 2.61   ? 478  TRP A CZ3 1 
ATOM   3671 C  CH2 . TRP A 1 568 ? 178.746 173.461 137.827 1.00 2.60   ? 478  TRP A CH2 1 
ATOM   3672 N  N   . GLU A 1 569 ? 179.614 179.093 132.290 1.00 2.20   ? 479  GLU A N   1 
ATOM   3673 C  CA  . GLU A 1 569 ? 180.730 179.698 131.580 1.00 2.24   ? 479  GLU A CA  1 
ATOM   3674 C  C   . GLU A 1 569 ? 181.655 180.398 132.567 1.00 2.26   ? 479  GLU A C   1 
ATOM   3675 O  O   . GLU A 1 569 ? 182.876 180.250 132.507 1.00 2.18   ? 479  GLU A O   1 
ATOM   3676 C  CB  . GLU A 1 569 ? 180.238 180.691 130.530 1.00 2.19   ? 479  GLU A CB  1 
ATOM   3677 N  N   . MET A 1 570 ? 181.060 181.142 133.494 1.00 2.15   ? 480  MET A N   1 
ATOM   3678 C  CA  . MET A 1 570 ? 181.808 181.842 134.528 1.00 2.27   ? 480  MET A CA  1 
ATOM   3679 C  C   . MET A 1 570 ? 182.508 180.878 135.480 1.00 2.38   ? 480  MET A C   1 
ATOM   3680 O  O   . MET A 1 570 ? 183.632 181.134 135.910 1.00 2.26   ? 480  MET A O   1 
ATOM   3681 C  CB  . MET A 1 570 ? 180.882 182.785 135.284 1.00 2.22   ? 480  MET A CB  1 
ATOM   3682 C  CG  . MET A 1 570 ? 180.433 184.003 134.491 1.00 2.23   ? 480  MET A CG  1 
ATOM   3683 S  SD  . MET A 1 570 ? 179.154 184.966 135.334 1.00 2.44   ? 480  MET A SD  1 
ATOM   3684 C  CE  . MET A 1 570 ? 180.060 185.667 136.701 1.00 2.34   ? 480  MET A CE  1 
ATOM   3685 N  N   . LYS A 1 571 ? 181.867 179.754 135.796 1.00 2.19   ? 481  LYS A N   1 
ATOM   3686 C  CA  . LYS A 1 571 ? 182.488 178.776 136.683 1.00 2.30   ? 481  LYS A CA  1 
ATOM   3687 C  C   . LYS A 1 571 ? 183.790 178.239 136.087 1.00 2.43   ? 481  LYS A C   1 
ATOM   3688 O  O   . LYS A 1 571 ? 184.803 178.151 136.781 1.00 2.22   ? 481  LYS A O   1 
ATOM   3689 C  CB  . LYS A 1 571 ? 181.536 177.607 136.958 1.00 2.29   ? 481  LYS A CB  1 
ATOM   3690 C  CG  . LYS A 1 571 ? 180.329 177.938 137.839 1.00 2.21   ? 481  LYS A CG  1 
ATOM   3691 C  CD  . LYS A 1 571 ? 180.648 177.854 139.326 1.00 2.20   ? 481  LYS A CD  1 
ATOM   3692 C  CE  . LYS A 1 571 ? 180.640 176.418 139.817 1.00 2.20   ? 481  LYS A CE  1 
ATOM   3693 N  NZ  . LYS A 1 571 ? 180.715 176.336 141.299 1.00 2.37   ? 481  LYS A NZ  1 
ATOM   3694 N  N   . ARG A 1 572 ? 183.774 177.938 134.790 1.00 2.25   ? 482  ARG A N   1 
ATOM   3695 C  CA  . ARG A 1 572 ? 184.970 177.409 134.138 1.00 2.38   ? 482  ARG A CA  1 
ATOM   3696 C  C   . ARG A 1 572 ? 186.093 178.440 134.046 1.00 2.50   ? 482  ARG A C   1 
ATOM   3697 O  O   . ARG A 1 572 ? 187.258 178.108 134.257 1.00 2.29   ? 482  ARG A O   1 
ATOM   3698 C  CB  . ARG A 1 572 ? 184.662 176.922 132.726 1.00 2.47   ? 482  ARG A CB  1 
ATOM   3699 C  CG  . ARG A 1 572 ? 183.821 175.656 132.606 1.00 2.80   ? 482  ARG A CG  1 
ATOM   3700 C  CD  . ARG A 1 572 ? 183.688 175.251 131.173 1.00 3.13   ? 482  ARG A CD  1 
ATOM   3701 N  NE  . ARG A 1 572 ? 182.690 174.208 130.953 1.00 3.49   ? 482  ARG A NE  1 
ATOM   3702 C  CZ  . ARG A 1 572 ? 182.643 173.420 129.854 1.00 3.82   ? 482  ARG A CZ  1 
ATOM   3703 N  NH1 . ARG A 1 572 ? 181.689 172.530 129.721 1.00 4.08   ? 482  ARG A NH1 1 
ATOM   3704 N  NH2 . ARG A 1 572 ? 183.558 173.537 128.899 1.00 3.99   ? 482  ARG A NH2 1 
ATOM   3705 N  N   . GLU A 1 573 ? 185.746 179.684 133.721 1.00 2.28   ? 483  GLU A N   1 
ATOM   3706 C  CA  . GLU A 1 573 ? 186.753 180.724 133.515 1.00 2.33   ? 483  GLU A CA  1 
ATOM   3707 C  C   . GLU A 1 573 ? 187.305 181.316 134.810 1.00 2.37   ? 483  GLU A C   1 
ATOM   3708 O  O   . GLU A 1 573 ? 188.488 181.654 134.884 1.00 2.35   ? 483  GLU A O   1 
ATOM   3709 C  CB  . GLU A 1 573 ? 186.180 181.852 132.660 1.00 2.22   ? 483  GLU A CB  1 
ATOM   3710 N  N   . ILE A 1 574 ? 186.458 181.474 135.817 1.00 2.28   ? 484  ILE A N   1 
ATOM   3711 C  CA  . ILE A 1 574 ? 186.870 182.139 137.048 1.00 2.37   ? 484  ILE A CA  1 
ATOM   3712 C  C   . ILE A 1 574 ? 187.355 181.162 138.108 1.00 2.47   ? 484  ILE A C   1 
ATOM   3713 O  O   . ILE A 1 574 ? 188.360 181.414 138.773 1.00 2.49   ? 484  ILE A O   1 
ATOM   3714 C  CB  . ILE A 1 574 ? 185.720 182.987 137.630 1.00 2.39   ? 484  ILE A CB  1 
ATOM   3715 C  CG1 . ILE A 1 574 ? 185.356 184.116 136.655 1.00 2.35   ? 484  ILE A CG1 1 
ATOM   3716 C  CG2 . ILE A 1 574 ? 186.118 183.556 138.988 1.00 2.60   ? 484  ILE A CG2 1 
ATOM   3717 C  CD1 . ILE A 1 574 ? 184.073 184.846 137.004 1.00 2.42   ? 484  ILE A CD1 1 
ATOM   3718 N  N   . VAL A 1 575 ? 186.618 180.077 138.308 1.00 2.33   ? 485  VAL A N   1 
ATOM   3719 C  CA  . VAL A 1 575 ? 186.916 179.164 139.399 1.00 2.41   ? 485  VAL A CA  1 
ATOM   3720 C  C   . VAL A 1 575 ? 187.741 177.977 138.913 1.00 2.49   ? 485  VAL A C   1 
ATOM   3721 O  O   . VAL A 1 575 ? 188.608 177.478 139.626 1.00 2.42   ? 485  VAL A O   1 
ATOM   3722 C  CB  . VAL A 1 575 ? 185.613 178.673 140.055 1.00 2.42   ? 485  VAL A CB  1 
ATOM   3723 C  CG1 . VAL A 1 575 ? 185.933 177.750 141.209 1.00 2.46   ? 485  VAL A CG1 1 
ATOM   3724 C  CG2 . VAL A 1 575 ? 184.795 179.864 140.524 1.00 2.47   ? 485  VAL A CG2 1 
ATOM   3725 N  N   . GLY A 1 576 ? 187.452 177.506 137.708 1.00 2.38   ? 486  GLY A N   1 
ATOM   3726 C  CA  . GLY A 1 576 ? 188.154 176.353 137.162 1.00 2.57   ? 486  GLY A CA  1 
ATOM   3727 C  C   . GLY A 1 576 ? 187.420 175.064 137.489 1.00 2.50   ? 486  GLY A C   1 
ATOM   3728 O  O   . GLY A 1 576 ? 188.041 174.022 137.715 1.00 2.47   ? 486  GLY A O   1 
ATOM   3729 N  N   . VAL A 1 577 ? 186.096 175.152 137.528 1.00 2.40   ? 487  VAL A N   1 
ATOM   3730 C  CA  . VAL A 1 577 ? 185.232 174.014 137.815 1.00 2.53   ? 487  VAL A CA  1 
ATOM   3731 C  C   . VAL A 1 577 ? 184.269 173.750 136.667 1.00 2.71   ? 487  VAL A C   1 
ATOM   3732 O  O   . VAL A 1 577 ? 183.696 174.679 136.101 1.00 2.52   ? 487  VAL A O   1 
ATOM   3733 C  CB  . VAL A 1 577 ? 184.471 174.251 139.128 1.00 2.51   ? 487  VAL A CB  1 
ATOM   3734 C  CG1 . VAL A 1 577 ? 183.438 173.170 139.356 1.00 2.62   ? 487  VAL A CG1 1 
ATOM   3735 C  CG2 . VAL A 1 577 ? 185.471 174.251 140.263 1.00 2.52   ? 487  VAL A CG2 1 
ATOM   3736 N  N   . VAL A 1 578 ? 184.122 172.479 136.308 1.00 2.70   ? 488  VAL A N   1 
ATOM   3737 C  CA  . VAL A 1 578 ? 183.284 172.080 135.184 1.00 2.91   ? 488  VAL A CA  1 
ATOM   3738 C  C   . VAL A 1 578 ? 182.168 171.126 135.602 1.00 3.22   ? 488  VAL A C   1 
ATOM   3739 O  O   . VAL A 1 578 ? 182.370 170.229 136.423 1.00 3.05   ? 488  VAL A O   1 
ATOM   3740 C  CB  . VAL A 1 578 ? 184.155 171.442 134.082 1.00 3.22   ? 488  VAL A CB  1 
ATOM   3741 C  CG1 . VAL A 1 578 ? 184.900 170.223 134.620 1.00 3.19   ? 488  VAL A CG1 1 
ATOM   3742 C  CG2 . VAL A 1 578 ? 183.295 171.057 132.901 1.00 3.76   ? 488  VAL A CG2 1 
ATOM   3743 N  N   . GLU A 1 579 ? 180.986 171.337 135.035 1.00 3.18   ? 489  GLU A N   1 
ATOM   3744 C  CA  . GLU A 1 579 ? 179.827 170.510 135.330 1.00 3.44   ? 489  GLU A CA  1 
ATOM   3745 C  C   . GLU A 1 579 ? 180.010 169.094 134.763 1.00 3.89   ? 489  GLU A C   1 
ATOM   3746 O  O   . GLU A 1 579 ? 180.505 168.939 133.649 1.00 4.10   ? 489  GLU A O   1 
ATOM   3747 C  CB  . GLU A 1 579 ? 178.573 171.165 134.743 1.00 3.43   ? 489  GLU A CB  1 
ATOM   3748 C  CG  . GLU A 1 579 ? 178.447 171.096 133.221 1.00 3.76   ? 489  GLU A CG  1 
ATOM   3749 C  CD  . GLU A 1 579 ? 179.345 172.053 132.470 1.00 3.72   ? 489  GLU A CD  1 
ATOM   3750 O  OE1 . GLU A 1 579 ? 179.988 172.876 133.080 1.00 3.24   ? 489  GLU A OE1 1 
ATOM   3751 O  OE2 . GLU A 1 579 ? 179.399 171.940 131.272 1.00 4.36   ? 489  GLU A OE2 1 
ATOM   3752 N  N   . PRO A 1 580 ? 179.649 168.053 135.526 1.00 3.75   ? 490  PRO A N   1 
ATOM   3753 C  CA  . PRO A 1 580 ? 179.562 166.655 135.124 1.00 4.17   ? 490  PRO A CA  1 
ATOM   3754 C  C   . PRO A 1 580 ? 178.579 166.406 133.989 1.00 4.51   ? 490  PRO A C   1 
ATOM   3755 O  O   . PRO A 1 580 ? 178.742 165.470 133.208 1.00 4.83   ? 490  PRO A O   1 
ATOM   3756 C  CB  . PRO A 1 580 ? 179.064 165.988 136.405 1.00 4.00   ? 490  PRO A CB  1 
ATOM   3757 C  CG  . PRO A 1 580 ? 179.498 166.903 137.511 1.00 3.46   ? 490  PRO A CG  1 
ATOM   3758 C  CD  . PRO A 1 580 ? 179.410 168.280 136.945 1.00 3.48   ? 490  PRO A CD  1 
ATOM   3759 N  N   . LEU A 1 581 ? 177.543 167.230 133.926 1.00 4.50   ? 491  LEU A N   1 
ATOM   3760 C  CA  . LEU A 1 581 ? 176.482 167.090 132.939 1.00 4.81   ? 491  LEU A CA  1 
ATOM   3761 C  C   . LEU A 1 581 ? 176.015 168.472 132.519 1.00 4.78   ? 491  LEU A C   1 
ATOM   3762 O  O   . LEU A 1 581 ? 175.915 169.357 133.365 1.00 4.26   ? 491  LEU A O   1 
ATOM   3763 C  CB  . LEU A 1 581 ? 175.301 166.328 133.557 1.00 5.03   ? 491  LEU A CB  1 
ATOM   3764 C  CG  . LEU A 1 581 ? 175.559 164.876 133.970 1.00 5.32   ? 491  LEU A CG  1 
ATOM   3765 C  CD1 . LEU A 1 581 ? 174.481 164.445 134.933 1.00 5.16   ? 491  LEU A CD1 1 
ATOM   3766 C  CD2 . LEU A 1 581 ? 175.561 163.981 132.735 1.00 6.49   ? 491  LEU A CD2 1 
ATOM   3767 N  N   . PRO A 1 582 ? 175.690 168.675 131.244 1.00 5.00   ? 492  PRO A N   1 
ATOM   3768 C  CA  . PRO A 1 582 ? 175.190 169.915 130.692 1.00 4.67   ? 492  PRO A CA  1 
ATOM   3769 C  C   . PRO A 1 582 ? 173.805 170.218 131.235 1.00 4.43   ? 492  PRO A C   1 
ATOM   3770 O  O   . PRO A 1 582 ? 172.939 169.345 131.258 1.00 4.64   ? 492  PRO A O   1 
ATOM   3771 C  CB  . PRO A 1 582 ? 175.165 169.621 129.193 1.00 6.40   ? 492  PRO A CB  1 
ATOM   3772 C  CG  . PRO A 1 582 ? 175.037 168.117 129.092 1.00 6.93   ? 492  PRO A CG  1 
ATOM   3773 C  CD  . PRO A 1 582 ? 175.771 167.570 130.298 1.00 5.90   ? 492  PRO A CD  1 
ATOM   3774 N  N   . HIS A 1 583 ? 173.589 171.461 131.642 1.00 3.99   ? 493  HIS A N   1 
ATOM   3775 C  CA  . HIS A 1 583 ? 172.296 171.883 132.162 1.00 3.48   ? 493  HIS A CA  1 
ATOM   3776 C  C   . HIS A 1 583 ? 171.699 172.993 131.317 1.00 3.29   ? 493  HIS A C   1 
ATOM   3777 O  O   . HIS A 1 583 ? 172.379 173.956 130.966 1.00 3.37   ? 493  HIS A O   1 
ATOM   3778 C  CB  . HIS A 1 583 ? 172.420 172.352 133.613 1.00 3.25   ? 493  HIS A CB  1 
ATOM   3779 C  CG  . HIS A 1 583 ? 172.685 171.255 134.607 1.00 3.28   ? 493  HIS A CG  1 
ATOM   3780 N  ND1 . HIS A 1 583 ? 173.003 171.513 135.915 1.00 3.07   ? 493  HIS A ND1 1 
ATOM   3781 C  CD2 . HIS A 1 583 ? 172.651 169.904 134.493 1.00 3.58   ? 493  HIS A CD2 1 
ATOM   3782 C  CE1 . HIS A 1 583 ? 173.163 170.378 136.561 1.00 3.16   ? 493  HIS A CE1 1 
ATOM   3783 N  NE2 . HIS A 1 583 ? 172.954 169.389 135.725 1.00 3.46   ? 493  HIS A NE2 1 
ATOM   3784 N  N   . ASP A 1 584 ? 170.420 172.853 130.997 1.00 3.09   ? 494  ASP A N   1 
ATOM   3785 C  CA  . ASP A 1 584 ? 169.696 173.848 130.222 1.00 2.92   ? 494  ASP A CA  1 
ATOM   3786 C  C   . ASP A 1 584 ? 169.004 174.848 131.137 1.00 2.87   ? 494  ASP A C   1 
ATOM   3787 O  O   . ASP A 1 584 ? 169.280 174.904 132.336 1.00 2.76   ? 494  ASP A O   1 
ATOM   3788 C  CB  . ASP A 1 584 ? 168.689 173.172 129.291 1.00 2.97   ? 494  ASP A CB  1 
ATOM   3789 C  CG  . ASP A 1 584 ? 167.609 172.445 130.037 1.00 2.88   ? 494  ASP A CG  1 
ATOM   3790 O  OD1 . ASP A 1 584 ? 167.535 172.617 131.228 1.00 2.79   ? 494  ASP A OD1 1 
ATOM   3791 O  OD2 . ASP A 1 584 ? 166.866 171.723 129.422 1.00 2.91   ? 494  ASP A OD2 1 
ATOM   3792 N  N   . GLU A 1 585 ? 168.125 175.663 130.568 1.00 2.72   ? 495  GLU A N   1 
ATOM   3793 C  CA  . GLU A 1 585 ? 167.543 176.772 131.306 1.00 2.64   ? 495  GLU A CA  1 
ATOM   3794 C  C   . GLU A 1 585 ? 166.312 176.382 132.120 1.00 2.71   ? 495  GLU A C   1 
ATOM   3795 O  O   . GLU A 1 585 ? 165.576 177.250 132.585 1.00 2.54   ? 495  GLU A O   1 
ATOM   3796 C  CB  . GLU A 1 585 ? 167.202 177.920 130.356 1.00 2.56   ? 495  GLU A CB  1 
ATOM   3797 C  CG  . GLU A 1 585 ? 168.404 178.492 129.592 1.00 2.61   ? 495  GLU A CG  1 
ATOM   3798 C  CD  . GLU A 1 585 ? 169.507 179.055 130.482 1.00 2.50   ? 495  GLU A CD  1 
ATOM   3799 O  OE1 . GLU A 1 585 ? 170.647 179.016 130.071 1.00 2.43   ? 495  GLU A OE1 1 
ATOM   3800 O  OE2 . GLU A 1 585 ? 169.218 179.511 131.565 1.00 2.42   ? 495  GLU A OE2 1 
ATOM   3801 N  N   . THR A 1 586 ? 166.103 175.085 132.341 1.00 2.65   ? 496  THR A N   1 
ATOM   3802 C  CA  . THR A 1 586 ? 165.060 174.677 133.276 1.00 2.69   ? 496  THR A CA  1 
ATOM   3803 C  C   . THR A 1 586 ? 165.662 174.562 134.671 1.00 2.70   ? 496  THR A C   1 
ATOM   3804 O  O   . THR A 1 586 ? 164.947 174.431 135.662 1.00 2.66   ? 496  THR A O   1 
ATOM   3805 C  CB  . THR A 1 586 ? 164.407 173.344 132.877 1.00 2.75   ? 496  THR A CB  1 
ATOM   3806 O  OG1 . THR A 1 586 ? 165.353 172.284 133.013 1.00 2.82   ? 496  THR A OG1 1 
ATOM   3807 C  CG2 . THR A 1 586 ? 163.932 173.412 131.438 1.00 2.68   ? 496  THR A CG2 1 
ATOM   3808 N  N   . TYR A 1 587 ? 166.989 174.620 134.737 1.00 2.61   ? 497  TYR A N   1 
ATOM   3809 C  CA  . TYR A 1 587 ? 167.726 174.525 135.990 1.00 2.64   ? 497  TYR A CA  1 
ATOM   3810 C  C   . TYR A 1 587 ? 167.964 175.902 136.591 1.00 2.66   ? 497  TYR A C   1 
ATOM   3811 O  O   . TYR A 1 587 ? 167.983 176.908 135.882 1.00 2.52   ? 497  TYR A O   1 
ATOM   3812 C  CB  . TYR A 1 587 ? 169.085 173.850 135.773 1.00 2.68   ? 497  TYR A CB  1 
ATOM   3813 C  CG  . TYR A 1 587 ? 169.065 172.355 135.535 1.00 2.88   ? 497  TYR A CG  1 
ATOM   3814 C  CD1 . TYR A 1 587 ? 168.851 171.856 134.266 1.00 2.91   ? 497  TYR A CD1 1 
ATOM   3815 C  CD2 . TYR A 1 587 ? 169.312 171.483 136.587 1.00 2.87   ? 497  TYR A CD2 1 
ATOM   3816 C  CE1 . TYR A 1 587 ? 168.883 170.497 134.045 1.00 2.99   ? 497  TYR A CE1 1 
ATOM   3817 C  CE2 . TYR A 1 587 ? 169.346 170.122 136.364 1.00 3.05   ? 497  TYR A CE2 1 
ATOM   3818 C  CZ  . TYR A 1 587 ? 169.134 169.629 135.100 1.00 3.06   ? 497  TYR A CZ  1 
ATOM   3819 O  OH  . TYR A 1 587 ? 169.185 168.271 134.865 1.00 3.41   ? 497  TYR A OH  1 
ATOM   3820 N  N   . CYS A 1 588 ? 168.174 175.939 137.898 1.00 2.53   ? 498  CYS A N   1 
ATOM   3821 C  CA  . CYS A 1 588 ? 168.578 177.164 138.569 1.00 2.45   ? 498  CYS A CA  1 
ATOM   3822 C  C   . CYS A 1 588 ? 169.583 176.840 139.656 1.00 2.53   ? 498  CYS A C   1 
ATOM   3823 O  O   . CYS A 1 588 ? 169.268 176.885 140.843 1.00 2.39   ? 498  CYS A O   1 
ATOM   3824 C  CB  . CYS A 1 588 ? 167.380 177.880 139.177 1.00 2.49   ? 498  CYS A CB  1 
ATOM   3825 S  SG  . CYS A 1 588 ? 167.724 179.569 139.703 1.00 2.54   ? 498  CYS A SG  1 
ATOM   3826 N  N   . ASP A 1 589 ? 170.787 176.475 139.234 1.00 2.41   ? 499  ASP A N   1 
ATOM   3827 C  CA  . ASP A 1 589 ? 171.802 175.939 140.128 1.00 2.47   ? 499  ASP A CA  1 
ATOM   3828 C  C   . ASP A 1 589 ? 172.157 176.840 141.315 1.00 2.44   ? 499  ASP A C   1 
ATOM   3829 O  O   . ASP A 1 589 ? 172.344 176.332 142.415 1.00 2.45   ? 499  ASP A O   1 
ATOM   3830 C  CB  . ASP A 1 589 ? 173.066 175.564 139.346 1.00 2.34   ? 499  ASP A CB  1 
ATOM   3831 C  CG  . ASP A 1 589 ? 172.851 174.369 138.439 1.00 2.58   ? 499  ASP A CG  1 
ATOM   3832 O  OD1 . ASP A 1 589 ? 171.853 173.704 138.581 1.00 2.55   ? 499  ASP A OD1 1 
ATOM   3833 O  OD2 . ASP A 1 589 ? 173.686 174.134 137.601 1.00 2.48   ? 499  ASP A OD2 1 
ATOM   3834 N  N   . PRO A 1 590 ? 172.278 178.163 141.148 1.00 2.28   ? 500  PRO A N   1 
ATOM   3835 C  CA  . PRO A 1 590 ? 172.593 179.104 142.202 1.00 2.37   ? 500  PRO A CA  1 
ATOM   3836 C  C   . PRO A 1 590 ? 171.560 179.084 143.320 1.00 2.50   ? 500  PRO A C   1 
ATOM   3837 O  O   . PRO A 1 590 ? 171.872 179.392 144.467 1.00 2.44   ? 500  PRO A O   1 
ATOM   3838 C  CB  . PRO A 1 590 ? 172.575 180.442 141.459 1.00 2.30   ? 500  PRO A CB  1 
ATOM   3839 C  CG  . PRO A 1 590 ? 172.835 180.075 140.029 1.00 2.37   ? 500  PRO A CG  1 
ATOM   3840 C  CD  . PRO A 1 590 ? 172.137 178.773 139.834 1.00 2.36   ? 500  PRO A CD  1 
ATOM   3841 N  N   . ALA A 1 591 ? 170.328 178.706 142.996 1.00 2.46   ? 501  ALA A N   1 
ATOM   3842 C  CA  . ALA A 1 591 ? 169.251 178.758 143.974 1.00 2.50   ? 501  ALA A CA  1 
ATOM   3843 C  C   . ALA A 1 591 ? 169.264 177.528 144.858 1.00 2.59   ? 501  ALA A C   1 
ATOM   3844 O  O   . ALA A 1 591 ? 168.511 177.443 145.825 1.00 2.54   ? 501  ALA A O   1 
ATOM   3845 C  CB  . ALA A 1 591 ? 167.911 178.904 143.277 1.00 2.52   ? 501  ALA A CB  1 
ATOM   3846 N  N   . SER A 1 592 ? 170.148 176.589 144.547 1.00 2.51   ? 502  SER A N   1 
ATOM   3847 C  CA  . SER A 1 592 ? 170.266 175.375 145.331 1.00 2.63   ? 502  SER A CA  1 
ATOM   3848 C  C   . SER A 1 592 ? 171.187 175.606 146.519 1.00 2.75   ? 502  SER A C   1 
ATOM   3849 O  O   . SER A 1 592 ? 171.455 174.684 147.288 1.00 2.71   ? 502  SER A O   1 
ATOM   3850 C  CB  . SER A 1 592 ? 170.783 174.236 144.478 1.00 2.65   ? 502  SER A CB  1 
ATOM   3851 O  OG  . SER A 1 592 ? 172.154 174.369 144.224 1.00 2.69   ? 502  SER A OG  1 
ATOM   3852 N  N   . LEU A 1 593 ? 171.698 176.834 146.642 1.00 2.64   ? 503  LEU A N   1 
ATOM   3853 C  CA  . LEU A 1 593 ? 172.534 177.234 147.768 1.00 2.80   ? 503  LEU A CA  1 
ATOM   3854 C  C   . LEU A 1 593 ? 171.691 178.007 148.784 1.00 2.87   ? 503  LEU A C   1 
ATOM   3855 O  O   . LEU A 1 593 ? 170.796 178.767 148.414 1.00 2.67   ? 503  LEU A O   1 
ATOM   3856 C  CB  . LEU A 1 593 ? 173.712 178.096 147.288 1.00 2.67   ? 503  LEU A CB  1 
ATOM   3857 C  CG  . LEU A 1 593 ? 174.738 178.538 148.373 1.00 2.77   ? 503  LEU A CG  1 
ATOM   3858 C  CD1 . LEU A 1 593 ? 175.521 177.330 148.871 1.00 2.90   ? 503  LEU A CD1 1 
ATOM   3859 C  CD2 . LEU A 1 593 ? 175.673 179.577 147.784 1.00 2.85   ? 503  LEU A CD2 1 
ATOM   3860 N  N   . PHE A 1 594 ? 171.982 177.813 150.065 1.00 2.80   ? 504  PHE A N   1 
ATOM   3861 C  CA  . PHE A 1 594 ? 171.207 178.420 151.146 1.00 2.89   ? 504  PHE A CA  1 
ATOM   3862 C  C   . PHE A 1 594 ? 171.043 179.928 151.016 1.00 2.96   ? 504  PHE A C   1 
ATOM   3863 O  O   . PHE A 1 594 ? 169.941 180.454 151.173 1.00 2.80   ? 504  PHE A O   1 
ATOM   3864 C  CB  . PHE A 1 594 ? 171.866 178.124 152.493 1.00 2.95   ? 504  PHE A CB  1 
ATOM   3865 C  CG  . PHE A 1 594 ? 171.192 178.804 153.643 1.00 2.95   ? 504  PHE A CG  1 
ATOM   3866 C  CD1 . PHE A 1 594 ? 170.065 178.259 154.224 1.00 2.97   ? 504  PHE A CD1 1 
ATOM   3867 C  CD2 . PHE A 1 594 ? 171.680 180.002 154.139 1.00 2.97   ? 504  PHE A CD2 1 
ATOM   3868 C  CE1 . PHE A 1 594 ? 169.439 178.893 155.273 1.00 2.90   ? 504  PHE A CE1 1 
ATOM   3869 C  CE2 . PHE A 1 594 ? 171.056 180.637 155.185 1.00 2.98   ? 504  PHE A CE2 1 
ATOM   3870 C  CZ  . PHE A 1 594 ? 169.933 180.082 155.753 1.00 2.94   ? 504  PHE A CZ  1 
ATOM   3871 N  N   . HIS A 1 595 ? 172.142 180.631 150.775 1.00 2.79   ? 505  HIS A N   1 
ATOM   3872 C  CA  . HIS A 1 595 ? 172.131 182.088 150.806 1.00 2.92   ? 505  HIS A CA  1 
ATOM   3873 C  C   . HIS A 1 595 ? 171.351 182.691 149.651 1.00 3.02   ? 505  HIS A C   1 
ATOM   3874 O  O   . HIS A 1 595 ? 170.794 183.782 149.769 1.00 2.76   ? 505  HIS A O   1 
ATOM   3875 C  CB  . HIS A 1 595 ? 173.560 182.624 150.801 1.00 2.91   ? 505  HIS A CB  1 
ATOM   3876 C  CG  . HIS A 1 595 ? 174.281 182.338 152.065 1.00 3.02   ? 505  HIS A CG  1 
ATOM   3877 N  ND1 . HIS A 1 595 ? 174.846 181.112 152.333 1.00 3.05   ? 505  HIS A ND1 1 
ATOM   3878 C  CD2 . HIS A 1 595 ? 174.524 183.108 153.146 1.00 3.10   ? 505  HIS A CD2 1 
ATOM   3879 C  CE1 . HIS A 1 595 ? 175.405 181.141 153.525 1.00 3.16   ? 505  HIS A CE1 1 
ATOM   3880 N  NE2 . HIS A 1 595 ? 175.223 182.339 154.040 1.00 3.19   ? 505  HIS A NE2 1 
ATOM   3881 N  N   . VAL A 1 596 ? 171.307 181.994 148.528 1.00 2.70   ? 506  VAL A N   1 
ATOM   3882 C  CA  . VAL A 1 596 ? 170.580 182.505 147.381 1.00 2.68   ? 506  VAL A CA  1 
ATOM   3883 C  C   . VAL A 1 596 ? 169.084 182.306 147.582 1.00 2.76   ? 506  VAL A C   1 
ATOM   3884 O  O   . VAL A 1 596 ? 168.295 183.230 147.386 1.00 2.76   ? 506  VAL A O   1 
ATOM   3885 C  CB  . VAL A 1 596 ? 171.053 181.815 146.096 1.00 2.60   ? 506  VAL A CB  1 
ATOM   3886 C  CG1 . VAL A 1 596 ? 170.211 182.263 144.906 1.00 2.57   ? 506  VAL A CG1 1 
ATOM   3887 C  CG2 . VAL A 1 596 ? 172.523 182.140 145.868 1.00 2.62   ? 506  VAL A CG2 1 
ATOM   3888 N  N   . ALA A 1 597 ? 168.702 181.107 148.005 1.00 2.72   ? 507  ALA A N   1 
ATOM   3889 C  CA  . ALA A 1 597 ? 167.300 180.780 148.237 1.00 2.77   ? 507  ALA A CA  1 
ATOM   3890 C  C   . ALA A 1 597 ? 166.691 181.651 149.334 1.00 2.81   ? 507  ALA A C   1 
ATOM   3891 O  O   . ALA A 1 597 ? 165.511 181.992 149.278 1.00 2.87   ? 507  ALA A O   1 
ATOM   3892 C  CB  . ALA A 1 597 ? 167.161 179.311 148.606 1.00 2.81   ? 507  ALA A CB  1 
ATOM   3893 N  N   . ASN A 1 598 ? 167.495 182.013 150.332 1.00 2.79   ? 508  ASN A N   1 
ATOM   3894 C  CA  . ASN A 1 598 ? 167.001 182.767 151.481 1.00 2.85   ? 508  ASN A CA  1 
ATOM   3895 C  C   . ASN A 1 598 ? 167.275 184.269 151.424 1.00 2.87   ? 508  ASN A C   1 
ATOM   3896 O  O   . ASN A 1 598 ? 167.112 184.961 152.428 1.00 2.89   ? 508  ASN A O   1 
ATOM   3897 C  CB  . ASN A 1 598 ? 167.564 182.187 152.760 1.00 2.85   ? 508  ASN A CB  1 
ATOM   3898 C  CG  . ASN A 1 598 ? 166.958 180.871 153.106 1.00 2.92   ? 508  ASN A CG  1 
ATOM   3899 O  OD1 . ASN A 1 598 ? 165.919 180.815 153.769 1.00 2.80   ? 508  ASN A OD1 1 
ATOM   3900 N  ND2 . ASN A 1 598 ? 167.568 179.810 152.664 1.00 2.88   ? 508  ASN A ND2 1 
ATOM   3901 N  N   . ASP A 1 599 ? 167.623 184.786 150.249 1.00 2.85   ? 509  ASP A N   1 
ATOM   3902 C  CA  . ASP A 1 599 ? 167.802 186.229 150.060 1.00 2.90   ? 509  ASP A CA  1 
ATOM   3903 C  C   . ASP A 1 599 ? 168.845 186.865 150.984 1.00 2.95   ? 509  ASP A C   1 
ATOM   3904 O  O   . ASP A 1 599 ? 168.575 187.881 151.625 1.00 2.91   ? 509  ASP A O   1 
ATOM   3905 C  CB  . ASP A 1 599 ? 166.456 186.950 150.243 1.00 2.95   ? 509  ASP A CB  1 
ATOM   3906 C  CG  . ASP A 1 599 ? 166.460 188.427 149.797 1.00 3.13   ? 509  ASP A CG  1 
ATOM   3907 O  OD1 . ASP A 1 599 ? 167.363 188.826 149.101 1.00 3.06   ? 509  ASP A OD1 1 
ATOM   3908 O  OD2 . ASP A 1 599 ? 165.542 189.136 150.154 1.00 3.29   ? 509  ASP A OD2 1 
ATOM   3909 N  N   . TYR A 1 600 ? 170.049 186.302 151.016 1.00 2.85   ? 510  TYR A N   1 
ATOM   3910 C  CA  . TYR A 1 600 ? 171.150 186.909 151.760 1.00 2.91   ? 510  TYR A CA  1 
ATOM   3911 C  C   . TYR A 1 600 ? 172.243 187.396 150.819 1.00 3.02   ? 510  TYR A C   1 
ATOM   3912 O  O   . TYR A 1 600 ? 172.497 186.779 149.784 1.00 2.87   ? 510  TYR A O   1 
ATOM   3913 C  CB  . TYR A 1 600 ? 171.755 185.920 152.758 1.00 2.89   ? 510  TYR A CB  1 
ATOM   3914 C  CG  . TYR A 1 600 ? 170.859 185.553 153.905 1.00 2.93   ? 510  TYR A CG  1 
ATOM   3915 C  CD1 . TYR A 1 600 ? 170.328 184.281 153.989 1.00 2.89   ? 510  TYR A CD1 1 
ATOM   3916 C  CD2 . TYR A 1 600 ? 170.568 186.489 154.877 1.00 3.01   ? 510  TYR A CD2 1 
ATOM   3917 C  CE1 . TYR A 1 600 ? 169.514 183.946 155.046 1.00 2.96   ? 510  TYR A CE1 1 
ATOM   3918 C  CE2 . TYR A 1 600 ? 169.750 186.155 155.932 1.00 3.10   ? 510  TYR A CE2 1 
ATOM   3919 C  CZ  . TYR A 1 600 ? 169.225 184.888 156.018 1.00 3.03   ? 510  TYR A CZ  1 
ATOM   3920 O  OH  . TYR A 1 600 ? 168.408 184.550 157.070 1.00 3.16   ? 510  TYR A OH  1 
ATOM   3921 N  N   . SER A 1 601 ? 172.921 188.477 151.199 1.00 3.06   ? 511  SER A N   1 
ATOM   3922 C  CA  . SER A 1 601 ? 174.093 188.937 150.463 1.00 3.12   ? 511  SER A CA  1 
ATOM   3923 C  C   . SER A 1 601 ? 175.267 188.011 150.764 1.00 3.18   ? 511  SER A C   1 
ATOM   3924 O  O   . SER A 1 601 ? 175.298 187.367 151.812 1.00 3.27   ? 511  SER A O   1 
ATOM   3925 C  CB  . SER A 1 601 ? 174.420 190.367 150.838 1.00 3.28   ? 511  SER A CB  1 
ATOM   3926 N  N   . PHE A 1 602 ? 176.222 187.921 149.842 1.00 3.22   ? 512  PHE A N   1 
ATOM   3927 C  CA  . PHE A 1 602 ? 177.296 186.945 149.989 1.00 3.30   ? 512  PHE A CA  1 
ATOM   3928 C  C   . PHE A 1 602 ? 178.679 187.604 150.029 1.00 3.69   ? 512  PHE A C   1 
ATOM   3929 O  O   . PHE A 1 602 ? 179.612 187.063 150.620 1.00 3.42   ? 512  PHE A O   1 
ATOM   3930 C  CB  . PHE A 1 602 ? 177.193 185.920 148.854 1.00 3.20   ? 512  PHE A CB  1 
ATOM   3931 C  CG  . PHE A 1 602 ? 177.758 184.569 149.147 1.00 3.12   ? 512  PHE A CG  1 
ATOM   3932 C  CD1 . PHE A 1 602 ? 178.847 184.088 148.461 1.00 3.09   ? 512  PHE A CD1 1 
ATOM   3933 C  CD2 . PHE A 1 602 ? 177.174 183.762 150.107 1.00 3.15   ? 512  PHE A CD2 1 
ATOM   3934 C  CE1 . PHE A 1 602 ? 179.345 182.831 148.728 1.00 3.06   ? 512  PHE A CE1 1 
ATOM   3935 C  CE2 . PHE A 1 602 ? 177.671 182.509 150.375 1.00 3.21   ? 512  PHE A CE2 1 
ATOM   3936 C  CZ  . PHE A 1 602 ? 178.758 182.044 149.683 1.00 3.16   ? 512  PHE A CZ  1 
ATOM   3937 N  N   . ILE A 1 603 ? 178.815 188.774 149.411 1.00 3.44   ? 513  ILE A N   1 
ATOM   3938 C  CA  . ILE A 1 603 ? 180.119 189.422 149.257 1.00 3.52   ? 513  ILE A CA  1 
ATOM   3939 C  C   . ILE A 1 603 ? 180.809 189.674 150.596 1.00 3.88   ? 513  ILE A C   1 
ATOM   3940 O  O   . ILE A 1 603 ? 182.028 189.831 150.652 1.00 3.90   ? 513  ILE A O   1 
ATOM   3941 C  CB  . ILE A 1 603 ? 179.992 190.759 148.484 1.00 3.43   ? 513  ILE A CB  1 
ATOM   3942 C  CG1 . ILE A 1 603 ? 181.369 191.214 147.929 1.00 3.48   ? 513  ILE A CG1 1 
ATOM   3943 C  CG2 . ILE A 1 603 ? 179.410 191.843 149.380 1.00 3.72   ? 513  ILE A CG2 1 
ATOM   3944 C  CD1 . ILE A 1 603 ? 181.939 190.317 146.834 1.00 3.44   ? 513  ILE A CD1 1 
ATOM   3945 N  N   . ARG A 1 604 ? 180.041 189.683 151.678 1.00 3.77   ? 514  ARG A N   1 
ATOM   3946 C  CA  . ARG A 1 604 ? 180.592 189.924 153.005 1.00 4.04   ? 514  ARG A CA  1 
ATOM   3947 C  C   . ARG A 1 604 ? 181.706 188.947 153.352 1.00 4.20   ? 514  ARG A C   1 
ATOM   3948 O  O   . ARG A 1 604 ? 182.575 189.254 154.167 1.00 4.31   ? 514  ARG A O   1 
ATOM   3949 C  CB  . ARG A 1 604 ? 179.511 189.809 154.066 1.00 4.09   ? 514  ARG A CB  1 
ATOM   3950 C  CG  . ARG A 1 604 ? 178.993 188.404 154.316 1.00 3.90   ? 514  ARG A CG  1 
ATOM   3951 C  CD  . ARG A 1 604 ? 177.955 188.395 155.364 1.00 3.96   ? 514  ARG A CD  1 
ATOM   3952 N  NE  . ARG A 1 604 ? 176.765 189.113 154.948 1.00 4.02   ? 514  ARG A NE  1 
ATOM   3953 C  CZ  . ARG A 1 604 ? 175.793 189.535 155.777 1.00 4.07   ? 514  ARG A CZ  1 
ATOM   3954 N  NH1 . ARG A 1 604 ? 175.879 189.304 157.068 1.00 4.29   ? 514  ARG A NH1 1 
ATOM   3955 N  NH2 . ARG A 1 604 ? 174.753 190.186 155.290 1.00 3.96   ? 514  ARG A NH2 1 
ATOM   3956 N  N   . TYR A 1 605 ? 181.680 187.766 152.746 1.00 3.96   ? 515  TYR A N   1 
ATOM   3957 C  CA  . TYR A 1 605 ? 182.674 186.749 153.043 1.00 4.08   ? 515  TYR A CA  1 
ATOM   3958 C  C   . TYR A 1 605 ? 183.991 187.065 152.347 1.00 4.28   ? 515  TYR A C   1 
ATOM   3959 O  O   . TYR A 1 605 ? 185.067 186.711 152.834 1.00 4.54   ? 515  TYR A O   1 
ATOM   3960 C  CB  . TYR A 1 605 ? 182.152 185.373 152.634 1.00 3.85   ? 515  TYR A CB  1 
ATOM   3961 C  CG  . TYR A 1 605 ? 180.904 184.982 153.388 1.00 3.81   ? 515  TYR A CG  1 
ATOM   3962 C  CD1 . TYR A 1 605 ? 180.962 184.748 154.749 1.00 3.87   ? 515  TYR A CD1 1 
ATOM   3963 C  CD2 . TYR A 1 605 ? 179.697 184.877 152.722 1.00 3.55   ? 515  TYR A CD2 1 
ATOM   3964 C  CE1 . TYR A 1 605 ? 179.817 184.420 155.438 1.00 3.69   ? 515  TYR A CE1 1 
ATOM   3965 C  CE2 . TYR A 1 605 ? 178.554 184.552 153.412 1.00 3.48   ? 515  TYR A CE2 1 
ATOM   3966 C  CZ  . TYR A 1 605 ? 178.612 184.327 154.763 1.00 3.54   ? 515  TYR A CZ  1 
ATOM   3967 O  OH  . TYR A 1 605 ? 177.469 184.013 155.451 1.00 3.67   ? 515  TYR A OH  1 
ATOM   3968 N  N   . PHE A 1 606 ? 183.901 187.743 151.209 1.00 4.14   ? 516  PHE A N   1 
ATOM   3969 C  CA  . PHE A 1 606 ? 185.075 188.122 150.443 1.00 4.23   ? 516  PHE A CA  1 
ATOM   3970 C  C   . PHE A 1 606 ? 185.828 189.224 151.172 1.00 4.70   ? 516  PHE A C   1 
ATOM   3971 O  O   . PHE A 1 606 ? 187.045 189.153 151.352 1.00 4.67   ? 516  PHE A O   1 
ATOM   3972 C  CB  . PHE A 1 606 ? 184.656 188.612 149.053 1.00 3.99   ? 516  PHE A CB  1 
ATOM   3973 C  CG  . PHE A 1 606 ? 185.786 188.883 148.115 1.00 4.00   ? 516  PHE A CG  1 
ATOM   3974 C  CD1 . PHE A 1 606 ? 186.339 187.858 147.366 1.00 3.69   ? 516  PHE A CD1 1 
ATOM   3975 C  CD2 . PHE A 1 606 ? 186.298 190.159 147.973 1.00 4.16   ? 516  PHE A CD2 1 
ATOM   3976 C  CE1 . PHE A 1 606 ? 187.375 188.105 146.493 1.00 3.68   ? 516  PHE A CE1 1 
ATOM   3977 C  CE2 . PHE A 1 606 ? 187.335 190.407 147.104 1.00 4.16   ? 516  PHE A CE2 1 
ATOM   3978 C  CZ  . PHE A 1 606 ? 187.872 189.379 146.361 1.00 3.90   ? 516  PHE A CZ  1 
ATOM   3979 N  N   . THR A 1 607 ? 185.087 190.247 151.588 1.00 4.47   ? 517  THR A N   1 
ATOM   3980 C  CA  . THR A 1 607 ? 185.671 191.415 152.225 1.00 4.73   ? 517  THR A CA  1 
ATOM   3981 C  C   . THR A 1 607 ? 186.161 191.102 153.628 1.00 5.11   ? 517  THR A C   1 
ATOM   3982 O  O   . THR A 1 607 ? 187.161 191.657 154.081 1.00 5.21   ? 517  THR A O   1 
ATOM   3983 C  CB  . THR A 1 607 ? 184.648 192.561 152.280 1.00 4.72   ? 517  THR A CB  1 
ATOM   3984 O  OG1 . THR A 1 607 ? 183.506 192.133 153.024 1.00 4.58   ? 517  THR A OG1 1 
ATOM   3985 C  CG2 . THR A 1 607 ? 184.214 192.945 150.859 1.00 4.60   ? 517  THR A CG2 1 
ATOM   3986 N  N   . ARG A 1 608 ? 185.475 190.191 154.309 1.00 4.89   ? 518  ARG A N   1 
ATOM   3987 C  CA  . ARG A 1 608 ? 185.866 189.804 155.654 1.00 5.33   ? 518  ARG A CA  1 
ATOM   3988 C  C   . ARG A 1 608 ? 187.261 189.212 155.647 1.00 5.47   ? 518  ARG A C   1 
ATOM   3989 O  O   . ARG A 1 608 ? 188.099 189.567 156.475 1.00 5.56   ? 518  ARG A O   1 
ATOM   3990 C  CB  . ARG A 1 608 ? 184.892 188.785 156.220 1.00 5.27   ? 518  ARG A CB  1 
ATOM   3991 C  CG  . ARG A 1 608 ? 185.096 188.430 157.673 1.00 5.78   ? 518  ARG A CG  1 
ATOM   3992 C  CD  . ARG A 1 608 ? 185.871 187.170 157.862 1.00 5.94   ? 518  ARG A CD  1 
ATOM   3993 N  NE  . ARG A 1 608 ? 185.124 186.008 157.413 1.00 6.04   ? 518  ARG A NE  1 
ATOM   3994 C  CZ  . ARG A 1 608 ? 185.633 184.768 157.276 1.00 6.18   ? 518  ARG A CZ  1 
ATOM   3995 N  NH1 . ARG A 1 608 ? 186.899 184.522 157.555 1.00 6.28   ? 518  ARG A NH1 1 
ATOM   3996 N  NH2 . ARG A 1 608 ? 184.852 183.786 156.859 1.00 5.84   ? 518  ARG A NH2 1 
ATOM   3997 N  N   . THR A 1 609 ? 187.512 188.318 154.696 1.00 5.31   ? 519  THR A N   1 
ATOM   3998 C  CA  . THR A 1 609 ? 188.800 187.650 154.595 1.00 5.47   ? 519  THR A CA  1 
ATOM   3999 C  C   . THR A 1 609 ? 189.932 188.644 154.370 1.00 5.61   ? 519  THR A C   1 
ATOM   4000 O  O   . THR A 1 609 ? 190.989 188.551 154.997 1.00 5.63   ? 519  THR A O   1 
ATOM   4001 C  CB  . THR A 1 609 ? 188.788 186.618 153.451 1.00 5.15   ? 519  THR A CB  1 
ATOM   4002 O  OG1 . THR A 1 609 ? 187.783 185.628 153.705 1.00 5.26   ? 519  THR A OG1 1 
ATOM   4003 C  CG2 . THR A 1 609 ? 190.139 185.941 153.348 1.00 5.10   ? 519  THR A CG2 1 
ATOM   4004 N  N   . ILE A 1 610 ? 189.710 189.603 153.482 1.00 5.35   ? 520  ILE A N   1 
ATOM   4005 C  CA  . ILE A 1 610 ? 190.746 190.576 153.162 1.00 5.46   ? 520  ILE A CA  1 
ATOM   4006 C  C   . ILE A 1 610 ? 191.056 191.468 154.364 1.00 5.78   ? 520  ILE A C   1 
ATOM   4007 O  O   . ILE A 1 610 ? 192.224 191.718 154.669 1.00 5.69   ? 520  ILE A O   1 
ATOM   4008 C  CB  . ILE A 1 610 ? 190.331 191.429 151.945 1.00 5.40   ? 520  ILE A CB  1 
ATOM   4009 C  CG1 . ILE A 1 610 ? 190.108 190.522 150.700 1.00 5.15   ? 520  ILE A CG1 1 
ATOM   4010 C  CG2 . ILE A 1 610 ? 191.385 192.499 151.651 1.00 5.53   ? 520  ILE A CG2 1 
ATOM   4011 C  CD1 . ILE A 1 610 ? 191.326 189.741 150.227 1.00 5.26   ? 520  ILE A CD1 1 
ATOM   4012 N  N   . LEU A 1 611 ? 190.015 191.931 155.057 1.00 5.57   ? 521  LEU A N   1 
ATOM   4013 C  CA  . LEU A 1 611 ? 190.196 192.780 156.234 1.00 5.73   ? 521  LEU A CA  1 
ATOM   4014 C  C   . LEU A 1 611 ? 190.908 192.032 157.348 1.00 6.84   ? 521  LEU A C   1 
ATOM   4015 O  O   . LEU A 1 611 ? 191.779 192.576 158.023 1.00 6.01   ? 521  LEU A O   1 
ATOM   4016 C  CB  . LEU A 1 611 ? 188.840 193.256 156.760 1.00 5.75   ? 521  LEU A CB  1 
ATOM   4017 C  CG  . LEU A 1 611 ? 188.080 194.270 155.904 1.00 5.68   ? 521  LEU A CG  1 
ATOM   4018 C  CD1 . LEU A 1 611 ? 186.659 194.377 156.430 1.00 5.55   ? 521  LEU A CD1 1 
ATOM   4019 C  CD2 . LEU A 1 611 ? 188.779 195.625 155.966 1.00 5.78   ? 521  LEU A CD2 1 
ATOM   4020 N  N   . GLU A 1 612 ? 190.551 190.767 157.516 1.00 5.84   ? 522  GLU A N   1 
ATOM   4021 C  CA  . GLU A 1 612 ? 191.116 189.931 158.563 1.00 6.16   ? 522  GLU A CA  1 
ATOM   4022 C  C   . GLU A 1 612 ? 192.635 189.939 158.540 1.00 6.29   ? 522  GLU A C   1 
ATOM   4023 O  O   . GLU A 1 612 ? 193.279 190.064 159.583 1.00 6.39   ? 522  GLU A O   1 
ATOM   4024 C  CB  . GLU A 1 612 ? 190.605 188.502 158.391 1.00 6.15   ? 522  GLU A CB  1 
ATOM   4025 C  CG  . GLU A 1 612 ? 191.122 187.499 159.382 1.00 6.42   ? 522  GLU A CG  1 
ATOM   4026 C  CD  . GLU A 1 612 ? 190.585 186.138 159.096 1.00 6.59   ? 522  GLU A CD  1 
ATOM   4027 O  OE1 . GLU A 1 612 ? 189.502 186.057 158.560 1.00 6.48   ? 522  GLU A OE1 1 
ATOM   4028 O  OE2 . GLU A 1 612 ? 191.247 185.177 159.397 1.00 6.87   ? 522  GLU A OE2 1 
ATOM   4029 N  N   . PHE A 1 613 ? 193.212 189.812 157.352 1.00 5.98   ? 523  PHE A N   1 
ATOM   4030 C  CA  . PHE A 1 613 ? 194.662 189.778 157.237 1.00 6.19   ? 523  PHE A CA  1 
ATOM   4031 C  C   . PHE A 1 613 ? 195.288 191.162 157.347 1.00 6.43   ? 523  PHE A C   1 
ATOM   4032 O  O   . PHE A 1 613 ? 196.427 191.290 157.797 1.00 6.49   ? 523  PHE A O   1 
ATOM   4033 C  CB  . PHE A 1 613 ? 195.077 189.080 155.952 1.00 5.97   ? 523  PHE A CB  1 
ATOM   4034 C  CG  . PHE A 1 613 ? 194.836 187.611 156.023 1.00 5.96   ? 523  PHE A CG  1 
ATOM   4035 C  CD1 . PHE A 1 613 ? 193.791 187.031 155.337 1.00 5.84   ? 523  PHE A CD1 1 
ATOM   4036 C  CD2 . PHE A 1 613 ? 195.639 186.805 156.806 1.00 5.99   ? 523  PHE A CD2 1 
ATOM   4037 C  CE1 . PHE A 1 613 ? 193.558 185.677 155.425 1.00 5.78   ? 523  PHE A CE1 1 
ATOM   4038 C  CE2 . PHE A 1 613 ? 195.404 185.455 156.897 1.00 6.03   ? 523  PHE A CE2 1 
ATOM   4039 C  CZ  . PHE A 1 613 ? 194.367 184.892 156.207 1.00 5.87   ? 523  PHE A CZ  1 
ATOM   4040 N  N   . GLN A 1 614 ? 194.549 192.204 156.973 1.00 6.16   ? 524  GLN A N   1 
ATOM   4041 C  CA  . GLN A 1 614 ? 195.059 193.559 157.157 1.00 6.31   ? 524  GLN A CA  1 
ATOM   4042 C  C   . GLN A 1 614 ? 195.198 193.879 158.640 1.00 6.61   ? 524  GLN A C   1 
ATOM   4043 O  O   . GLN A 1 614 ? 196.184 194.486 159.063 1.00 6.84   ? 524  GLN A O   1 
ATOM   4044 C  CB  . GLN A 1 614 ? 194.153 194.598 156.488 1.00 6.11   ? 524  GLN A CB  1 
ATOM   4045 C  CG  . GLN A 1 614 ? 194.223 194.607 154.979 1.00 5.92   ? 524  GLN A CG  1 
ATOM   4046 C  CD  . GLN A 1 614 ? 193.306 195.633 154.348 1.00 5.83   ? 524  GLN A CD  1 
ATOM   4047 O  OE1 . GLN A 1 614 ? 192.101 195.414 154.199 1.00 5.79   ? 524  GLN A OE1 1 
ATOM   4048 N  NE2 . GLN A 1 614 ? 193.882 196.767 153.965 1.00 5.91   ? 524  GLN A NE2 1 
ATOM   4049 N  N   . PHE A 1 615 ? 194.223 193.440 159.433 1.00 6.52   ? 525  PHE A N   1 
ATOM   4050 C  CA  . PHE A 1 615 ? 194.251 193.679 160.869 1.00 6.75   ? 525  PHE A CA  1 
ATOM   4051 C  C   . PHE A 1 615 ? 195.382 192.891 161.516 1.00 7.21   ? 525  PHE A C   1 
ATOM   4052 O  O   . PHE A 1 615 ? 196.098 193.409 162.372 1.00 7.41   ? 525  PHE A O   1 
ATOM   4053 C  CB  . PHE A 1 615 ? 192.929 193.264 161.528 1.00 6.61   ? 525  PHE A CB  1 
ATOM   4054 C  CG  . PHE A 1 615 ? 191.694 194.034 161.103 1.00 6.60   ? 525  PHE A CG  1 
ATOM   4055 C  CD1 . PHE A 1 615 ? 191.767 195.221 160.386 1.00 6.55   ? 525  PHE A CD1 1 
ATOM   4056 C  CD2 . PHE A 1 615 ? 190.436 193.550 161.438 1.00 6.55   ? 525  PHE A CD2 1 
ATOM   4057 C  CE1 . PHE A 1 615 ? 190.614 195.891 160.017 1.00 6.37   ? 525  PHE A CE1 1 
ATOM   4058 C  CE2 . PHE A 1 615 ? 189.290 194.224 161.069 1.00 6.49   ? 525  PHE A CE2 1 
ATOM   4059 C  CZ  . PHE A 1 615 ? 189.382 195.392 160.357 1.00 6.23   ? 525  PHE A CZ  1 
ATOM   4060 N  N   . GLN A 1 616 ? 195.545 191.633 161.109 1.00 6.96   ? 526  GLN A N   1 
ATOM   4061 C  CA  . GLN A 1 616 ? 196.558 190.775 161.711 1.00 7.28   ? 526  GLN A CA  1 
ATOM   4062 C  C   . GLN A 1 616 ? 197.961 191.283 161.430 1.00 7.89   ? 526  GLN A C   1 
ATOM   4063 O  O   . GLN A 1 616 ? 198.808 191.300 162.322 1.00 8.00   ? 526  GLN A O   1 
ATOM   4064 C  CB  . GLN A 1 616 ? 196.427 189.341 161.192 1.00 7.13   ? 526  GLN A CB  1 
ATOM   4065 C  CG  . GLN A 1 616 ? 197.353 188.325 161.868 1.00 7.58   ? 526  GLN A CG  1 
ATOM   4066 C  CD  . GLN A 1 616 ? 196.992 188.079 163.325 1.00 7.55   ? 526  GLN A CD  1 
ATOM   4067 O  OE1 . GLN A 1 616 ? 195.815 187.953 163.661 1.00 7.35   ? 526  GLN A OE1 1 
ATOM   4068 N  NE2 . GLN A 1 616 ? 197.992 188.000 164.193 1.00 8.32   ? 526  GLN A NE2 1 
ATOM   4069 N  N   . GLU A 1 617 ? 198.214 191.709 160.197 1.00 7.41   ? 527  GLU A N   1 
ATOM   4070 C  CA  . GLU A 1 617 ? 199.545 192.186 159.854 1.00 7.69   ? 527  GLU A CA  1 
ATOM   4071 C  C   . GLU A 1 617 ? 199.885 193.464 160.598 1.00 8.37   ? 527  GLU A C   1 
ATOM   4072 O  O   . GLU A 1 617 ? 200.989 193.607 161.126 1.00 8.50   ? 527  GLU A O   1 
ATOM   4073 C  CB  . GLU A 1 617 ? 199.677 192.422 158.353 1.00 7.32   ? 527  GLU A CB  1 
ATOM   4074 C  CG  . GLU A 1 617 ? 201.063 192.883 157.942 1.00 7.72   ? 527  GLU A CG  1 
ATOM   4075 C  CD  . GLU A 1 617 ? 201.243 192.998 156.467 1.00 7.55   ? 527  GLU A CD  1 
ATOM   4076 O  OE1 . GLU A 1 617 ? 201.248 194.099 155.973 1.00 7.76   ? 527  GLU A OE1 1 
ATOM   4077 O  OE2 . GLU A 1 617 ? 201.381 191.985 155.826 1.00 7.05   ? 527  GLU A OE2 1 
ATOM   4078 N  N   . ALA A 1 618 ? 198.939 194.396 160.639 1.00 7.83   ? 528  ALA A N   1 
ATOM   4079 C  CA  . ALA A 1 618 ? 199.174 195.674 161.292 1.00 8.10   ? 528  ALA A CA  1 
ATOM   4080 C  C   . ALA A 1 618 ? 199.478 195.485 162.770 1.00 8.75   ? 528  ALA A C   1 
ATOM   4081 O  O   . ALA A 1 618 ? 200.379 196.126 163.314 1.00 9.00   ? 528  ALA A O   1 
ATOM   4082 C  CB  . ALA A 1 618 ? 197.963 196.572 161.114 1.00 7.48   ? 528  ALA A CB  1 
ATOM   4083 N  N   . LEU A 1 619 ? 198.753 194.578 163.415 1.00 8.30   ? 529  LEU A N   1 
ATOM   4084 C  CA  . LEU A 1 619 ? 198.960 194.337 164.836 1.00 8.64   ? 529  LEU A CA  1 
ATOM   4085 C  C   . LEU A 1 619 ? 200.288 193.626 165.126 1.00 9.50   ? 529  LEU A C   1 
ATOM   4086 O  O   . LEU A 1 619 ? 200.902 193.874 166.166 1.00 9.57   ? 529  LEU A O   1 
ATOM   4087 C  CB  . LEU A 1 619 ? 197.772 193.548 165.417 1.00 8.43   ? 529  LEU A CB  1 
ATOM   4088 C  CG  . LEU A 1 619 ? 196.395 194.306 165.467 1.00 8.24   ? 529  LEU A CG  1 
ATOM   4089 C  CD1 . LEU A 1 619 ? 195.321 193.374 166.015 1.00 8.01   ? 529  LEU A CD1 1 
ATOM   4090 C  CD2 . LEU A 1 619 ? 196.509 195.558 166.327 1.00 8.16   ? 529  LEU A CD2 1 
ATOM   4091 N  N   . CYS A 1 620 ? 200.748 192.768 164.203 1.00 8.99   ? 530  CYS A N   1 
ATOM   4092 C  CA  . CYS A 1 620 ? 202.008 192.040 164.362 1.00 9.44   ? 530  CYS A CA  1 
ATOM   4093 C  C   . CYS A 1 620 ? 203.210 192.955 164.206 1.00 10.19  ? 530  CYS A C   1 
ATOM   4094 O  O   . CYS A 1 620 ? 204.259 192.730 164.823 1.00 10.65  ? 530  CYS A O   1 
ATOM   4095 C  CB  . CYS A 1 620 ? 202.092 190.898 163.344 1.00 9.34   ? 530  CYS A CB  1 
ATOM   4096 S  SG  . CYS A 1 620 ? 200.921 189.565 163.651 1.00 9.03   ? 530  CYS A SG  1 
ATOM   4097 N  N   . GLN A 1 621 ? 203.079 193.999 163.388 1.00 9.72   ? 531  GLN A N   1 
ATOM   4098 C  CA  . GLN A 1 621 ? 204.167 194.953 163.231 1.00 9.95   ? 531  GLN A CA  1 
ATOM   4099 C  C   . GLN A 1 621 ? 204.350 195.749 164.513 1.00 10.80  ? 531  GLN A C   1 
ATOM   4100 O  O   . GLN A 1 621 ? 205.470 195.960 164.970 1.00 11.73  ? 531  GLN A O   1 
ATOM   4101 C  CB  . GLN A 1 621 ? 203.899 195.899 162.061 1.00 9.65   ? 531  GLN A CB  1 
ATOM   4102 N  N   . ILE A 1 622 ? 203.237 196.139 165.122 1.00 10.40  ? 532  ILE A N   1 
ATOM   4103 C  CA  . ILE A 1 622 ? 203.259 196.893 166.369 1.00 10.73  ? 532  ILE A CA  1 
ATOM   4104 C  C   . ILE A 1 622 ? 203.870 196.072 167.493 1.00 11.44  ? 532  ILE A C   1 
ATOM   4105 O  O   . ILE A 1 622 ? 204.624 196.586 168.319 1.00 12.92  ? 532  ILE A O   1 
ATOM   4106 C  CB  . ILE A 1 622 ? 201.845 197.352 166.749 1.00 10.13  ? 532  ILE A CB  1 
ATOM   4107 C  CG1 . ILE A 1 622 ? 201.365 198.390 165.734 1.00 9.73   ? 532  ILE A CG1 1 
ATOM   4108 C  CG2 . ILE A 1 622 ? 201.837 197.927 168.153 1.00 10.14  ? 532  ILE A CG2 1 
ATOM   4109 C  CD1 . ILE A 1 622 ? 199.900 198.711 165.830 1.00 8.99   ? 532  ILE A CD1 1 
ATOM   4110 N  N   . ALA A 1 623 ? 203.541 194.787 167.515 1.00 11.14  ? 533  ALA A N   1 
ATOM   4111 C  CA  . ALA A 1 623 ? 204.049 193.860 168.522 1.00 11.41  ? 533  ALA A CA  1 
ATOM   4112 C  C   . ALA A 1 623 ? 205.511 193.436 168.260 1.00 12.61  ? 533  ALA A C   1 
ATOM   4113 O  O   . ALA A 1 623 ? 206.076 192.664 169.041 1.00 13.15  ? 533  ALA A O   1 
ATOM   4114 C  CB  . ALA A 1 623 ? 203.141 192.639 168.573 1.00 10.77  ? 533  ALA A CB  1 
ATOM   4115 N  N   . ASN A 1 624 ? 206.114 193.953 167.178 1.00 12.47  ? 534  ASN A N   1 
ATOM   4116 C  CA  . ASN A 1 624 ? 207.500 193.683 166.764 1.00 12.91  ? 534  ASN A CA  1 
ATOM   4117 C  C   . ASN A 1 624 ? 207.751 192.205 166.513 1.00 12.82  ? 534  ASN A C   1 
ATOM   4118 O  O   . ASN A 1 624 ? 208.853 191.695 166.817 1.00 12.85  ? 534  ASN A O   1 
ATOM   4119 C  CB  . ASN A 1 624 ? 208.479 194.272 167.778 1.00 15.22  ? 534  ASN A CB  1 
ATOM   4120 C  CG  . ASN A 1 624 ? 208.616 195.789 167.668 1.00 17.67  ? 534  ASN A CG  1 
ATOM   4121 O  OD1 . ASN A 1 624 ? 208.075 196.420 166.753 1.00 16.47  ? 534  ASN A OD1 1 
ATOM   4122 N  ND2 . ASN A 1 624 ? 209.344 196.380 168.609 1.00 21.10  ? 534  ASN A ND2 1 
ATOM   4123 N  N   . HIS A 1 625 ? 206.799 191.513 165.893 1.00 12.08  ? 535  HIS A N   1 
ATOM   4124 C  CA  . HIS A 1 625 ? 206.940 190.121 165.504 1.00 11.42  ? 535  HIS A CA  1 
ATOM   4125 C  C   . HIS A 1 625 ? 207.931 189.942 164.356 1.00 11.31  ? 535  HIS A C   1 
ATOM   4126 O  O   . HIS A 1 625 ? 207.855 190.638 163.344 1.00 11.44  ? 535  HIS A O   1 
ATOM   4127 C  CB  . HIS A 1 625 ? 205.595 189.525 165.077 1.00 10.72  ? 535  HIS A CB  1 
ATOM   4128 C  CG  . HIS A 1 625 ? 205.712 188.124 164.618 1.00 10.47  ? 535  HIS A CG  1 
ATOM   4129 N  ND1 . HIS A 1 625 ? 206.071 187.099 165.459 1.00 10.15  ? 535  HIS A ND1 1 
ATOM   4130 C  CD2 . HIS A 1 625 ? 205.529 187.566 163.401 1.00 10.06  ? 535  HIS A CD2 1 
ATOM   4131 C  CE1 . HIS A 1 625 ? 206.106 185.970 164.779 1.00 10.01  ? 535  HIS A CE1 1 
ATOM   4132 N  NE2 . HIS A 1 625 ? 205.777 186.226 163.527 1.00 9.97   ? 535  HIS A NE2 1 
ATOM   4133 N  N   . THR A 1 626 ? 208.850 188.994 164.525 1.00 11.32  ? 536  THR A N   1 
ATOM   4134 C  CA  . THR A 1 626 ? 209.840 188.666 163.487 1.00 11.31  ? 536  THR A CA  1 
ATOM   4135 C  C   . THR A 1 626 ? 209.601 187.251 163.013 1.00 11.27  ? 536  THR A C   1 
ATOM   4136 O  O   . THR A 1 626 ? 209.238 186.396 163.827 1.00 11.09  ? 536  THR A O   1 
ATOM   4137 C  CB  . THR A 1 626 ? 211.244 188.827 164.064 1.00 12.24  ? 536  THR A CB  1 
ATOM   4138 O  OG1 . THR A 1 626 ? 211.272 188.007 165.227 1.00 13.58  ? 536  THR A OG1 1 
ATOM   4139 C  CG2 . THR A 1 626 ? 211.557 190.262 164.446 1.00 12.73  ? 536  THR A CG2 1 
ATOM   4140 N  N   . GLY A 1 627 ? 209.784 187.011 161.723 1.00 11.33  ? 537  GLY A N   1 
ATOM   4141 C  CA  . GLY A 1 627 ? 209.570 185.684 161.158 1.00 11.17  ? 537  GLY A CA  1 
ATOM   4142 C  C   . GLY A 1 627 ? 208.212 185.633 160.469 1.00 10.24  ? 537  GLY A C   1 
ATOM   4143 O  O   . GLY A 1 627 ? 207.587 186.673 160.258 1.00 10.15  ? 537  GLY A O   1 
ATOM   4144 N  N   . PRO A 1 628 ? 207.757 184.443 160.086 1.00 10.17  ? 538  PRO A N   1 
ATOM   4145 C  CA  . PRO A 1 628 ? 206.529 184.162 159.358 1.00 9.69   ? 538  PRO A CA  1 
ATOM   4146 C  C   . PRO A 1 628 ? 205.299 184.708 160.077 1.00 9.30   ? 538  PRO A C   1 
ATOM   4147 O  O   . PRO A 1 628 ? 205.165 184.574 161.292 1.00 9.30   ? 538  PRO A O   1 
ATOM   4148 C  CB  . PRO A 1 628 ? 206.525 182.632 159.319 1.00 9.63   ? 538  PRO A CB  1 
ATOM   4149 C  CG  . PRO A 1 628 ? 207.979 182.246 159.432 1.00 10.61  ? 538  PRO A CG  1 
ATOM   4150 C  CD  . PRO A 1 628 ? 208.568 183.263 160.374 1.00 10.72  ? 538  PRO A CD  1 
ATOM   4151 N  N   . LEU A 1 629 ? 204.381 185.289 159.313 1.00 9.05   ? 539  LEU A N   1 
ATOM   4152 C  CA  . LEU A 1 629 ? 203.186 185.909 159.876 1.00 8.77   ? 539  LEU A CA  1 
ATOM   4153 C  C   . LEU A 1 629 ? 202.276 184.905 160.577 1.00 8.55   ? 539  LEU A C   1 
ATOM   4154 O  O   . LEU A 1 629 ? 201.611 185.245 161.555 1.00 8.57   ? 539  LEU A O   1 
ATOM   4155 C  CB  . LEU A 1 629 ? 202.407 186.645 158.774 1.00 7.90   ? 539  LEU A CB  1 
ATOM   4156 C  CG  . LEU A 1 629 ? 201.164 187.472 159.221 1.00 7.91   ? 539  LEU A CG  1 
ATOM   4157 C  CD1 . LEU A 1 629 ? 201.568 188.536 160.240 1.00 8.26   ? 539  LEU A CD1 1 
ATOM   4158 C  CD2 . LEU A 1 629 ? 200.541 188.130 157.992 1.00 7.28   ? 539  LEU A CD2 1 
ATOM   4159 N  N   . HIS A 1 630 ? 202.229 183.672 160.081 1.00 8.34   ? 540  HIS A N   1 
ATOM   4160 C  CA  . HIS A 1 630 ? 201.328 182.677 160.649 1.00 8.25   ? 540  HIS A CA  1 
ATOM   4161 C  C   . HIS A 1 630 ? 201.779 182.208 162.028 1.00 8.59   ? 540  HIS A C   1 
ATOM   4162 O  O   . HIS A 1 630 ? 201.049 181.489 162.710 1.00 8.53   ? 540  HIS A O   1 
ATOM   4163 C  CB  . HIS A 1 630 ? 201.169 181.474 159.716 1.00 7.72   ? 540  HIS A CB  1 
ATOM   4164 C  CG  . HIS A 1 630 ? 202.381 180.620 159.588 1.00 8.08   ? 540  HIS A CG  1 
ATOM   4165 N  ND1 . HIS A 1 630 ? 203.469 180.984 158.835 1.00 8.41   ? 540  HIS A ND1 1 
ATOM   4166 C  CD2 . HIS A 1 630 ? 202.671 179.407 160.107 1.00 8.26   ? 540  HIS A CD2 1 
ATOM   4167 C  CE1 . HIS A 1 630 ? 204.381 180.030 158.901 1.00 8.82   ? 540  HIS A CE1 1 
ATOM   4168 N  NE2 . HIS A 1 630 ? 203.920 179.066 159.664 1.00 8.76   ? 540  HIS A NE2 1 
ATOM   4169 N  N   . LYS A 1 631 ? 202.970 182.622 162.445 1.00 8.84   ? 541  LYS A N   1 
ATOM   4170 C  CA  . LYS A 1 631 ? 203.473 182.292 163.776 1.00 8.95   ? 541  LYS A CA  1 
ATOM   4171 C  C   . LYS A 1 631 ? 203.389 183.477 164.752 1.00 9.13   ? 541  LYS A C   1 
ATOM   4172 O  O   . LYS A 1 631 ? 203.991 183.437 165.827 1.00 9.23   ? 541  LYS A O   1 
ATOM   4173 C  CB  . LYS A 1 631 ? 204.911 181.783 163.681 1.00 9.11   ? 541  LYS A CB  1 
ATOM   4174 C  CG  . LYS A 1 631 ? 205.044 180.494 162.888 1.00 9.36   ? 541  LYS A CG  1 
ATOM   4175 C  CD  . LYS A 1 631 ? 206.493 180.059 162.710 1.00 9.88   ? 541  LYS A CD  1 
ATOM   4176 C  CE  . LYS A 1 631 ? 207.066 179.439 163.978 1.00 10.88  ? 541  LYS A CE  1 
ATOM   4177 N  NZ  . LYS A 1 631 ? 208.320 178.681 163.696 1.00 11.60  ? 541  LYS A NZ  1 
ATOM   4178 N  N   . CYS A 1 632 ? 202.654 184.530 164.366 1.00 9.21   ? 542  CYS A N   1 
ATOM   4179 C  CA  . CYS A 1 632 ? 202.477 185.742 165.162 1.00 9.37   ? 542  CYS A CA  1 
ATOM   4180 C  C   . CYS A 1 632 ? 201.518 185.543 166.333 1.00 9.34   ? 542  CYS A C   1 
ATOM   4181 O  O   . CYS A 1 632 ? 200.461 184.925 166.202 1.00 9.13   ? 542  CYS A O   1 
ATOM   4182 C  CB  . CYS A 1 632 ? 201.969 186.888 164.279 1.00 9.37   ? 542  CYS A CB  1 
ATOM   4183 S  SG  . CYS A 1 632 ? 201.741 188.468 165.138 1.00 9.57   ? 542  CYS A SG  1 
ATOM   4184 N  N   . ASP A 1 633 ? 201.891 186.110 167.472 1.00 9.43   ? 543  ASP A N   1 
ATOM   4185 C  CA  . ASP A 1 633 ? 201.090 186.083 168.689 1.00 9.40   ? 543  ASP A CA  1 
ATOM   4186 C  C   . ASP A 1 633 ? 201.139 187.449 169.363 1.00 9.47   ? 543  ASP A C   1 
ATOM   4187 O  O   . ASP A 1 633 ? 202.217 187.951 169.679 1.00 9.62   ? 543  ASP A O   1 
ATOM   4188 C  CB  . ASP A 1 633 ? 201.588 184.992 169.641 1.00 9.55   ? 543  ASP A CB  1 
ATOM   4189 C  CG  . ASP A 1 633 ? 200.767 184.886 170.915 1.00 9.60   ? 543  ASP A CG  1 
ATOM   4190 O  OD1 . ASP A 1 633 ? 199.998 185.780 171.183 1.00 9.66   ? 543  ASP A OD1 1 
ATOM   4191 O  OD2 . ASP A 1 633 ? 200.923 183.922 171.615 1.00 9.80   ? 543  ASP A OD2 1 
ATOM   4192 N  N   . ILE A 1 634 ? 199.980 188.084 169.514 1.00 9.44   ? 544  ILE A N   1 
ATOM   4193 C  CA  . ILE A 1 634 ? 199.924 189.457 170.012 1.00 9.54   ? 544  ILE A CA  1 
ATOM   4194 C  C   . ILE A 1 634 ? 199.649 189.522 171.510 1.00 9.33   ? 544  ILE A C   1 
ATOM   4195 O  O   . ILE A 1 634 ? 199.334 190.586 172.044 1.00 9.65   ? 544  ILE A O   1 
ATOM   4196 C  CB  . ILE A 1 634 ? 198.860 190.277 169.258 1.00 9.42   ? 544  ILE A CB  1 
ATOM   4197 C  CG1 . ILE A 1 634 ? 197.463 189.673 169.503 1.00 9.17   ? 544  ILE A CG1 1 
ATOM   4198 C  CG2 . ILE A 1 634 ? 199.200 190.318 167.763 1.00 9.40   ? 544  ILE A CG2 1 
ATOM   4199 C  CD1 . ILE A 1 634 ? 196.318 190.561 169.072 1.00 9.12   ? 544  ILE A CD1 1 
ATOM   4200 N  N   . SER A 1 635 ? 199.776 188.390 172.187 1.00 9.57   ? 545  SER A N   1 
ATOM   4201 C  CA  . SER A 1 635 ? 199.583 188.353 173.625 1.00 9.57   ? 545  SER A CA  1 
ATOM   4202 C  C   . SER A 1 635 ? 200.614 189.239 174.308 1.00 9.82   ? 545  SER A C   1 
ATOM   4203 O  O   . SER A 1 635 ? 201.724 189.402 173.806 1.00 9.78   ? 545  SER A O   1 
ATOM   4204 C  CB  . SER A 1 635 ? 199.710 186.942 174.148 1.00 10.02  ? 545  SER A CB  1 
ATOM   4205 N  N   . ASN A 1 636 ? 200.221 189.834 175.436 1.00 9.80   ? 546  ASN A N   1 
ATOM   4206 C  CA  . ASN A 1 636 ? 201.086 190.710 176.257 1.00 9.97   ? 546  ASN A CA  1 
ATOM   4207 C  C   . ASN A 1 636 ? 201.501 191.979 175.525 1.00 9.61   ? 546  ASN A C   1 
ATOM   4208 O  O   . ASN A 1 636 ? 202.353 192.735 176.051 1.00 9.82   ? 546  ASN A O   1 
ATOM   4209 C  CB  . ASN A 1 636 ? 202.305 189.940 176.758 1.00 10.92  ? 546  ASN A CB  1 
ATOM   4210 C  CG  . ASN A 1 636 ? 202.041 189.141 178.018 1.00 11.48  ? 546  ASN A CG  1 
ATOM   4211 O  OD1 . ASN A 1 636 ? 201.358 189.621 178.940 1.00 11.49  ? 546  ASN A OD1 1 
ATOM   4212 N  ND2 . ASN A 1 636 ? 202.573 187.941 178.076 1.00 12.72  ? 546  ASN A ND2 1 
ATOM   4213 N  N   . SER A 1 637 ? 200.918 192.295 174.368 1.00 9.67   ? 547  SER A N   1 
ATOM   4214 C  CA  . SER A 1 637 ? 201.199 193.545 173.665 1.00 9.40   ? 547  SER A CA  1 
ATOM   4215 C  C   . SER A 1 637 ? 200.093 194.561 173.892 1.00 9.45   ? 547  SER A C   1 
ATOM   4216 O  O   . SER A 1 637 ? 199.025 194.491 173.279 1.00 9.07   ? 547  SER A O   1 
ATOM   4217 C  CB  . SER A 1 637 ? 201.366 193.302 172.181 1.00 9.54   ? 547  SER A CB  1 
ATOM   4218 O  OG  . SER A 1 637 ? 201.615 194.509 171.510 1.00 9.71   ? 547  SER A OG  1 
ATOM   4219 N  N   . THR A 1 638 ? 200.363 195.533 174.752 1.00 9.23   ? 548  THR A N   1 
ATOM   4220 C  CA  . THR A 1 638 ? 199.364 196.537 175.072 1.00 9.21   ? 548  THR A CA  1 
ATOM   4221 C  C   . THR A 1 638 ? 199.349 197.624 174.014 1.00 9.20   ? 548  THR A C   1 
ATOM   4222 O  O   . THR A 1 638 ? 198.349 198.318 173.843 1.00 8.90   ? 548  THR A O   1 
ATOM   4223 C  CB  . THR A 1 638 ? 199.610 197.139 176.466 1.00 9.23   ? 548  THR A CB  1 
ATOM   4224 O  OG1 . THR A 1 638 ? 200.910 197.737 176.514 1.00 9.53   ? 548  THR A OG1 1 
ATOM   4225 C  CG2 . THR A 1 638 ? 199.517 196.047 177.520 1.00 9.12   ? 548  THR A CG2 1 
ATOM   4226 N  N   . GLU A 1 639 ? 200.441 197.731 173.261 1.00 9.38   ? 549  GLU A N   1 
ATOM   4227 C  CA  . GLU A 1 639 ? 200.501 198.669 172.153 1.00 9.25   ? 549  GLU A CA  1 
ATOM   4228 C  C   . GLU A 1 639 ? 199.594 198.203 171.024 1.00 9.05   ? 549  GLU A C   1 
ATOM   4229 O  O   . GLU A 1 639 ? 198.839 198.995 170.456 1.00 8.65   ? 549  GLU A O   1 
ATOM   4230 C  CB  . GLU A 1 639 ? 201.938 198.808 171.653 1.00 10.04  ? 549  GLU A CB  1 
ATOM   4231 N  N   . ALA A 1 640 ? 199.639 196.905 170.720 1.00 9.07   ? 550  ALA A N   1 
ATOM   4232 C  CA  . ALA A 1 640 ? 198.760 196.339 169.704 1.00 8.87   ? 550  ALA A CA  1 
ATOM   4233 C  C   . ALA A 1 640 ? 197.314 196.439 170.165 1.00 8.44   ? 550  ALA A C   1 
ATOM   4234 O  O   . ALA A 1 640 ? 196.417 196.735 169.372 1.00 8.09   ? 550  ALA A O   1 
ATOM   4235 C  CB  . ALA A 1 640 ? 199.137 194.892 169.421 1.00 9.10   ? 550  ALA A CB  1 
ATOM   4236 N  N   . GLY A 1 641 ? 197.095 196.221 171.457 1.00 8.66   ? 551  GLY A N   1 
ATOM   4237 C  CA  . GLY A 1 641 ? 195.759 196.291 172.035 1.00 8.40   ? 551  GLY A CA  1 
ATOM   4238 C  C   . GLY A 1 641 ? 195.165 197.684 171.904 1.00 7.93   ? 551  GLY A C   1 
ATOM   4239 O  O   . GLY A 1 641 ? 194.004 197.836 171.523 1.00 7.67   ? 551  GLY A O   1 
ATOM   4240 N  N   . LYS A 1 642 ? 195.964 198.709 172.195 1.00 8.22   ? 552  LYS A N   1 
ATOM   4241 C  CA  . LYS A 1 642 ? 195.501 200.083 172.103 1.00 7.98   ? 552  LYS A CA  1 
ATOM   4242 C  C   . LYS A 1 642 ? 195.129 200.451 170.671 1.00 8.14   ? 552  LYS A C   1 
ATOM   4243 O  O   . LYS A 1 642 ? 194.102 201.090 170.437 1.00 7.52   ? 552  LYS A O   1 
ATOM   4244 C  CB  . LYS A 1 642 ? 196.572 201.039 172.628 1.00 8.12   ? 552  LYS A CB  1 
ATOM   4245 C  CG  . LYS A 1 642 ? 196.226 202.526 172.529 1.00 8.03   ? 552  LYS A CG  1 
ATOM   4246 C  CD  . LYS A 1 642 ? 195.623 203.060 173.827 1.00 8.27   ? 552  LYS A CD  1 
ATOM   4247 C  CE  . LYS A 1 642 ? 194.113 203.209 173.718 1.00 8.04   ? 552  LYS A CE  1 
ATOM   4248 N  NZ  . LYS A 1 642 ? 193.548 203.966 174.872 1.00 7.93   ? 552  LYS A NZ  1 
ATOM   4249 N  N   . GLN A 1 643 ? 195.948 200.034 169.711 1.00 7.79   ? 553  GLN A N   1 
ATOM   4250 C  CA  . GLN A 1 643 ? 195.691 200.354 168.316 1.00 7.68   ? 553  GLN A CA  1 
ATOM   4251 C  C   . GLN A 1 643 ? 194.348 199.787 167.878 1.00 7.65   ? 553  GLN A C   1 
ATOM   4252 O  O   . GLN A 1 643 ? 193.605 200.411 167.121 1.00 7.19   ? 553  GLN A O   1 
ATOM   4253 C  CB  . GLN A 1 643 ? 196.784 199.773 167.419 1.00 7.88   ? 553  GLN A CB  1 
ATOM   4254 C  CG  . GLN A 1 643 ? 196.797 200.326 166.002 1.00 7.60   ? 553  GLN A CG  1 
ATOM   4255 C  CD  . GLN A 1 643 ? 197.372 201.727 165.941 1.00 7.64   ? 553  GLN A CD  1 
ATOM   4256 O  OE1 . GLN A 1 643 ? 198.484 201.970 166.417 1.00 8.22   ? 553  GLN A OE1 1 
ATOM   4257 N  NE2 . GLN A 1 643 ? 196.632 202.656 165.357 1.00 7.50   ? 553  GLN A NE2 1 
ATOM   4258 N  N   . LEU A 1 644 ? 194.042 198.589 168.369 1.00 7.40   ? 554  LEU A N   1 
ATOM   4259 C  CA  . LEU A 1 644 ? 192.789 197.918 168.068 1.00 7.26   ? 554  LEU A CA  1 
ATOM   4260 C  C   . LEU A 1 644 ? 191.608 198.588 168.762 1.00 7.70   ? 554  LEU A C   1 
ATOM   4261 O  O   . LEU A 1 644 ? 190.585 198.861 168.134 1.00 6.86   ? 554  LEU A O   1 
ATOM   4262 C  CB  . LEU A 1 644 ? 192.883 196.448 168.501 1.00 7.41   ? 554  LEU A CB  1 
ATOM   4263 C  CG  . LEU A 1 644 ? 191.620 195.595 168.351 1.00 7.15   ? 554  LEU A CG  1 
ATOM   4264 C  CD1 . LEU A 1 644 ? 191.189 195.517 166.896 1.00 7.12   ? 554  LEU A CD1 1 
ATOM   4265 C  CD2 . LEU A 1 644 ? 191.895 194.219 168.900 1.00 7.16   ? 554  LEU A CD2 1 
ATOM   4266 N  N   . LYS A 1 645 ? 191.760 198.885 170.048 1.00 7.10   ? 555  LYS A N   1 
ATOM   4267 C  CA  . LYS A 1 645 ? 190.690 199.494 170.827 1.00 7.15   ? 555  LYS A CA  1 
ATOM   4268 C  C   . LYS A 1 645 ? 190.228 200.804 170.201 1.00 8.04   ? 555  LYS A C   1 
ATOM   4269 O  O   . LYS A 1 645 ? 189.036 201.110 170.192 1.00 6.93   ? 555  LYS A O   1 
ATOM   4270 C  CB  . LYS A 1 645 ? 191.140 199.711 172.272 1.00 7.53   ? 555  LYS A CB  1 
ATOM   4271 C  CG  . LYS A 1 645 ? 190.086 200.339 173.189 1.00 7.64   ? 555  LYS A CG  1 
ATOM   4272 C  CD  . LYS A 1 645 ? 190.519 200.264 174.655 1.00 7.94   ? 555  LYS A CD  1 
ATOM   4273 C  CE  . LYS A 1 645 ? 189.735 201.239 175.541 1.00 8.21   ? 555  LYS A CE  1 
ATOM   4274 N  NZ  . LYS A 1 645 ? 188.269 201.002 175.487 1.00 8.69   ? 555  LYS A NZ  1 
ATOM   4275 N  N   . ASN A 1 646 ? 191.175 201.559 169.650 1.00 7.06   ? 556  ASN A N   1 
ATOM   4276 C  CA  . ASN A 1 646 ? 190.873 202.839 169.019 1.00 7.17   ? 556  ASN A CA  1 
ATOM   4277 C  C   . ASN A 1 646 ? 189.932 202.682 167.829 1.00 6.94   ? 556  ASN A C   1 
ATOM   4278 O  O   . ASN A 1 646 ? 189.220 203.618 167.469 1.00 6.92   ? 556  ASN A O   1 
ATOM   4279 C  CB  . ASN A 1 646 ? 192.148 203.526 168.572 1.00 7.24   ? 556  ASN A CB  1 
ATOM   4280 C  CG  . ASN A 1 646 ? 192.941 204.087 169.708 1.00 7.48   ? 556  ASN A CG  1 
ATOM   4281 O  OD1 . ASN A 1 646 ? 192.444 204.210 170.835 1.00 7.70   ? 556  ASN A OD1 1 
ATOM   4282 N  ND2 . ASN A 1 646 ? 194.170 204.444 169.433 1.00 7.71   ? 556  ASN A ND2 1 
ATOM   4283 N  N   . MET A 1 647 ? 189.948 201.512 167.203 1.00 6.86   ? 557  MET A N   1 
ATOM   4284 C  CA  . MET A 1 647 ? 189.078 201.247 166.072 1.00 6.76   ? 557  MET A CA  1 
ATOM   4285 C  C   . MET A 1 647 ? 187.745 200.697 166.558 1.00 6.72   ? 557  MET A C   1 
ATOM   4286 O  O   . MET A 1 647 ? 186.683 201.053 166.053 1.00 6.69   ? 557  MET A O   1 
ATOM   4287 C  CB  . MET A 1 647 ? 189.755 200.273 165.101 1.00 6.73   ? 557  MET A CB  1 
ATOM   4288 C  CG  . MET A 1 647 ? 188.957 199.953 163.840 1.00 6.54   ? 557  MET A CG  1 
ATOM   4289 S  SD  . MET A 1 647 ? 187.767 198.615 164.051 1.00 6.51   ? 557  MET A SD  1 
ATOM   4290 C  CE  . MET A 1 647 ? 188.834 197.180 163.969 1.00 6.62   ? 557  MET A CE  1 
ATOM   4291 N  N   . LEU A 1 648 ? 187.804 199.818 167.555 1.00 6.71   ? 558  LEU A N   1 
ATOM   4292 C  CA  . LEU A 1 648 ? 186.625 199.101 168.008 1.00 6.70   ? 558  LEU A CA  1 
ATOM   4293 C  C   . LEU A 1 648 ? 185.561 200.029 168.591 1.00 6.70   ? 558  LEU A C   1 
ATOM   4294 O  O   . LEU A 1 648 ? 184.368 199.839 168.357 1.00 6.61   ? 558  LEU A O   1 
ATOM   4295 C  CB  . LEU A 1 648 ? 187.013 198.072 169.085 1.00 6.68   ? 558  LEU A CB  1 
ATOM   4296 C  CG  . LEU A 1 648 ? 187.928 196.906 168.650 1.00 6.72   ? 558  LEU A CG  1 
ATOM   4297 C  CD1 . LEU A 1 648 ? 188.245 196.049 169.872 1.00 6.76   ? 558  LEU A CD1 1 
ATOM   4298 C  CD2 . LEU A 1 648 ? 187.263 196.083 167.572 1.00 6.61   ? 558  LEU A CD2 1 
ATOM   4299 N  N   . GLU A 1 649 ? 185.988 201.036 169.336 1.00 6.75   ? 559  GLU A N   1 
ATOM   4300 C  CA  . GLU A 1 649 ? 185.047 201.903 170.040 1.00 6.87   ? 559  GLU A CA  1 
ATOM   4301 C  C   . GLU A 1 649 ? 184.265 202.843 169.135 1.00 6.77   ? 559  GLU A C   1 
ATOM   4302 O  O   . GLU A 1 649 ? 183.360 203.538 169.597 1.00 6.79   ? 559  GLU A O   1 
ATOM   4303 C  CB  . GLU A 1 649 ? 185.759 202.724 171.105 1.00 6.92   ? 559  GLU A CB  1 
ATOM   4304 C  CG  . GLU A 1 649 ? 186.631 203.833 170.568 1.00 7.00   ? 559  GLU A CG  1 
ATOM   4305 C  CD  . GLU A 1 649 ? 187.249 204.647 171.658 1.00 7.39   ? 559  GLU A CD  1 
ATOM   4306 O  OE1 . GLU A 1 649 ? 187.072 205.847 171.647 1.00 7.56   ? 559  GLU A OE1 1 
ATOM   4307 O  OE2 . GLU A 1 649 ? 187.877 204.070 172.520 1.00 7.53   ? 559  GLU A OE2 1 
ATOM   4308 N  N   . LEU A 1 650 ? 184.633 202.903 167.860 1.00 6.64   ? 560  LEU A N   1 
ATOM   4309 C  CA  . LEU A 1 650 ? 183.986 203.828 166.940 1.00 6.62   ? 560  LEU A CA  1 
ATOM   4310 C  C   . LEU A 1 650 ? 182.599 203.351 166.543 1.00 6.55   ? 560  LEU A C   1 
ATOM   4311 O  O   . LEU A 1 650 ? 181.778 204.143 166.075 1.00 6.46   ? 560  LEU A O   1 
ATOM   4312 C  CB  . LEU A 1 650 ? 184.831 203.998 165.672 1.00 6.59   ? 560  LEU A CB  1 
ATOM   4313 C  CG  . LEU A 1 650 ? 186.201 204.670 165.840 1.00 6.59   ? 560  LEU A CG  1 
ATOM   4314 C  CD1 . LEU A 1 650 ? 186.958 204.580 164.526 1.00 6.50   ? 560  LEU A CD1 1 
ATOM   4315 C  CD2 . LEU A 1 650 ? 186.021 206.122 166.256 1.00 6.68   ? 560  LEU A CD2 1 
ATOM   4316 N  N   . GLY A 1 651 ? 182.349 202.054 166.682 1.00 6.55   ? 561  GLY A N   1 
ATOM   4317 C  CA  . GLY A 1 651 ? 181.086 201.500 166.221 1.00 6.51   ? 561  GLY A CA  1 
ATOM   4318 C  C   . GLY A 1 651 ? 180.944 201.798 164.739 1.00 6.38   ? 561  GLY A C   1 
ATOM   4319 O  O   . GLY A 1 651 ? 181.875 201.573 163.966 1.00 6.29   ? 561  GLY A O   1 
ATOM   4320 N  N   . LYS A 1 652 ? 179.799 202.346 164.349 1.00 6.37   ? 562  LYS A N   1 
ATOM   4321 C  CA  . LYS A 1 652 ? 179.595 202.743 162.964 1.00 6.33   ? 562  LYS A CA  1 
ATOM   4322 C  C   . LYS A 1 652 ? 179.292 204.233 162.858 1.00 6.45   ? 562  LYS A C   1 
ATOM   4323 O  O   . LYS A 1 652 ? 178.568 204.666 161.965 1.00 6.52   ? 562  LYS A O   1 
ATOM   4324 C  CB  . LYS A 1 652 ? 178.487 201.916 162.310 1.00 6.43   ? 562  LYS A CB  1 
ATOM   4325 C  CG  . LYS A 1 652 ? 177.113 202.115 162.901 1.00 6.73   ? 562  LYS A CG  1 
ATOM   4326 C  CD  . LYS A 1 652 ? 176.074 201.270 162.191 1.00 6.92   ? 562  LYS A CD  1 
ATOM   4327 C  CE  . LYS A 1 652 ? 175.561 201.949 160.935 1.00 7.28   ? 562  LYS A CE  1 
ATOM   4328 N  NZ  . LYS A 1 652 ? 174.432 201.192 160.322 1.00 7.67   ? 562  LYS A NZ  1 
ATOM   4329 N  N   . SER A 1 653 ? 179.862 205.022 163.770 1.00 6.39   ? 563  SER A N   1 
ATOM   4330 C  CA  . SER A 1 653 ? 179.677 206.470 163.762 1.00 6.31   ? 563  SER A CA  1 
ATOM   4331 C  C   . SER A 1 653 ? 180.556 207.155 162.714 1.00 6.13   ? 563  SER A C   1 
ATOM   4332 O  O   . SER A 1 653 ? 180.329 208.313 162.364 1.00 6.23   ? 563  SER A O   1 
ATOM   4333 C  CB  . SER A 1 653 ? 179.973 207.043 165.133 1.00 6.27   ? 563  SER A CB  1 
ATOM   4334 O  OG  . SER A 1 653 ? 181.325 206.883 165.470 1.00 6.29   ? 563  SER A OG  1 
ATOM   4335 N  N   . LYS A 1 654 ? 181.555 206.433 162.223 1.00 6.07   ? 564  LYS A N   1 
ATOM   4336 C  CA  . LYS A 1 654 ? 182.487 206.943 161.225 1.00 6.07   ? 564  LYS A CA  1 
ATOM   4337 C  C   . LYS A 1 654 ? 182.465 206.038 159.994 1.00 6.08   ? 564  LYS A C   1 
ATOM   4338 O  O   . LYS A 1 654 ? 182.066 204.879 160.097 1.00 6.09   ? 564  LYS A O   1 
ATOM   4339 C  CB  . LYS A 1 654 ? 183.908 207.005 161.806 1.00 6.12   ? 564  LYS A CB  1 
ATOM   4340 C  CG  . LYS A 1 654 ? 184.055 207.842 163.074 1.00 6.12   ? 564  LYS A CG  1 
ATOM   4341 C  CD  . LYS A 1 654 ? 183.843 209.331 162.822 1.00 5.94   ? 564  LYS A CD  1 
ATOM   4342 C  CE  . LYS A 1 654 ? 185.051 209.968 162.158 1.00 6.21   ? 564  LYS A CE  1 
ATOM   4343 N  NZ  . LYS A 1 654 ? 184.907 211.447 162.048 1.00 6.68   ? 564  LYS A NZ  1 
ATOM   4344 N  N   . PRO A 1 655 ? 182.894 206.531 158.826 1.00 6.03   ? 565  PRO A N   1 
ATOM   4345 C  CA  . PRO A 1 655 ? 183.112 205.774 157.610 1.00 6.10   ? 565  PRO A CA  1 
ATOM   4346 C  C   . PRO A 1 655 ? 184.046 204.607 157.878 1.00 6.11   ? 565  PRO A C   1 
ATOM   4347 O  O   . PRO A 1 655 ? 185.024 204.752 158.612 1.00 6.09   ? 565  PRO A O   1 
ATOM   4348 C  CB  . PRO A 1 655 ? 183.757 206.817 156.692 1.00 6.25   ? 565  PRO A CB  1 
ATOM   4349 C  CG  . PRO A 1 655 ? 183.220 208.138 157.191 1.00 6.20   ? 565  PRO A CG  1 
ATOM   4350 C  CD  . PRO A 1 655 ? 183.116 207.974 158.691 1.00 5.97   ? 565  PRO A CD  1 
ATOM   4351 N  N   . TRP A 1 656 ? 183.767 203.458 157.277 1.00 5.99   ? 566  TRP A N   1 
ATOM   4352 C  CA  . TRP A 1 656 ? 184.609 202.292 157.510 1.00 5.94   ? 566  TRP A CA  1 
ATOM   4353 C  C   . TRP A 1 656 ? 186.026 202.498 157.000 1.00 6.16   ? 566  TRP A C   1 
ATOM   4354 O  O   . TRP A 1 656 ? 186.958 201.870 157.497 1.00 5.99   ? 566  TRP A O   1 
ATOM   4355 C  CB  . TRP A 1 656 ? 184.000 201.035 156.885 1.00 5.75   ? 566  TRP A CB  1 
ATOM   4356 C  CG  . TRP A 1 656 ? 183.921 201.050 155.404 1.00 5.69   ? 566  TRP A CG  1 
ATOM   4357 C  CD1 . TRP A 1 656 ? 182.863 201.447 154.656 1.00 5.66   ? 566  TRP A CD1 1 
ATOM   4358 C  CD2 . TRP A 1 656 ? 184.935 200.629 154.469 1.00 5.61   ? 566  TRP A CD2 1 
ATOM   4359 N  NE1 . TRP A 1 656 ? 183.146 201.309 153.328 1.00 5.54   ? 566  TRP A NE1 1 
ATOM   4360 C  CE2 . TRP A 1 656 ? 184.410 200.809 153.194 1.00 5.50   ? 566  TRP A CE2 1 
ATOM   4361 C  CE3 . TRP A 1 656 ? 186.232 200.116 154.610 1.00 5.69   ? 566  TRP A CE3 1 
ATOM   4362 C  CZ2 . TRP A 1 656 ? 185.125 200.501 152.062 1.00 5.35   ? 566  TRP A CZ2 1 
ATOM   4363 C  CZ3 . TRP A 1 656 ? 186.952 199.811 153.469 1.00 5.68   ? 566  TRP A CZ3 1 
ATOM   4364 C  CH2 . TRP A 1 656 ? 186.409 199.999 152.227 1.00 5.44   ? 566  TRP A CH2 1 
ATOM   4365 N  N   . THR A 1 657 ? 186.199 203.398 156.039 1.00 5.98   ? 567  THR A N   1 
ATOM   4366 C  CA  . THR A 1 657 ? 187.530 203.703 155.537 1.00 6.11   ? 567  THR A CA  1 
ATOM   4367 C  C   . THR A 1 657 ? 188.335 204.426 156.611 1.00 6.31   ? 567  THR A C   1 
ATOM   4368 O  O   . THR A 1 657 ? 189.552 204.270 156.699 1.00 6.22   ? 567  THR A O   1 
ATOM   4369 C  CB  . THR A 1 657 ? 187.459 204.561 154.263 1.00 6.28   ? 567  THR A CB  1 
ATOM   4370 O  OG1 . THR A 1 657 ? 186.751 205.763 154.542 1.00 6.46   ? 567  THR A OG1 1 
ATOM   4371 C  CG2 . THR A 1 657 ? 186.745 203.807 153.149 1.00 6.03   ? 567  THR A CG2 1 
ATOM   4372 N  N   . PHE A 1 658 ? 187.642 205.189 157.451 1.00 6.22   ? 568  PHE A N   1 
ATOM   4373 C  CA  . PHE A 1 658 ? 188.259 205.858 158.590 1.00 6.34   ? 568  PHE A CA  1 
ATOM   4374 C  C   . PHE A 1 658 ? 188.639 204.828 159.639 1.00 6.32   ? 568  PHE A C   1 
ATOM   4375 O  O   . PHE A 1 658 ? 189.742 204.856 160.189 1.00 6.35   ? 568  PHE A O   1 
ATOM   4376 C  CB  . PHE A 1 658 ? 187.308 206.890 159.197 1.00 6.32   ? 568  PHE A CB  1 
ATOM   4377 C  CG  . PHE A 1 658 ? 187.876 207.632 160.365 1.00 6.35   ? 568  PHE A CG  1 
ATOM   4378 C  CD1 . PHE A 1 658 ? 188.647 208.761 160.180 1.00 6.59   ? 568  PHE A CD1 1 
ATOM   4379 C  CD2 . PHE A 1 658 ? 187.647 207.191 161.659 1.00 6.32   ? 568  PHE A CD2 1 
ATOM   4380 C  CE1 . PHE A 1 658 ? 189.173 209.438 161.258 1.00 6.64   ? 568  PHE A CE1 1 
ATOM   4381 C  CE2 . PHE A 1 658 ? 188.173 207.863 162.738 1.00 6.43   ? 568  PHE A CE2 1 
ATOM   4382 C  CZ  . PHE A 1 658 ? 188.936 208.988 162.538 1.00 6.58   ? 568  PHE A CZ  1 
ATOM   4383 N  N   . ALA A 1 659 ? 187.705 203.931 159.935 1.00 6.19   ? 569  ALA A N   1 
ATOM   4384 C  CA  . ALA A 1 659 ? 187.919 202.893 160.935 1.00 6.28   ? 569  ALA A CA  1 
ATOM   4385 C  C   . ALA A 1 659 ? 189.083 201.997 160.537 1.00 6.30   ? 569  ALA A C   1 
ATOM   4386 O  O   . ALA A 1 659 ? 189.872 201.580 161.385 1.00 6.35   ? 569  ALA A O   1 
ATOM   4387 C  CB  . ALA A 1 659 ? 186.656 202.069 161.110 1.00 6.21   ? 569  ALA A CB  1 
ATOM   4388 N  N   . LEU A 1 660 ? 189.201 201.719 159.243 1.00 6.17   ? 570  LEU A N   1 
ATOM   4389 C  CA  . LEU A 1 660 ? 190.287 200.893 158.736 1.00 6.25   ? 570  LEU A CA  1 
ATOM   4390 C  C   . LEU A 1 660 ? 191.625 201.600 158.883 1.00 6.83   ? 570  LEU A C   1 
ATOM   4391 O  O   . LEU A 1 660 ? 192.603 201.004 159.325 1.00 6.31   ? 570  LEU A O   1 
ATOM   4392 C  CB  . LEU A 1 660 ? 190.039 200.546 157.259 1.00 6.18   ? 570  LEU A CB  1 
ATOM   4393 C  CG  . LEU A 1 660 ? 191.122 199.694 156.554 1.00 6.26   ? 570  LEU A CG  1 
ATOM   4394 C  CD1 . LEU A 1 660 ? 191.277 198.359 157.259 1.00 6.30   ? 570  LEU A CD1 1 
ATOM   4395 C  CD2 . LEU A 1 660 ? 190.723 199.493 155.100 1.00 6.13   ? 570  LEU A CD2 1 
ATOM   4396 N  N   . GLU A 1 661 ? 191.664 202.884 158.546 1.00 6.38   ? 571  GLU A N   1 
ATOM   4397 C  CA  . GLU A 1 661 ? 192.888 203.661 158.660 1.00 6.74   ? 571  GLU A CA  1 
ATOM   4398 C  C   . GLU A 1 661 ? 193.414 203.669 160.094 1.00 6.63   ? 571  GLU A C   1 
ATOM   4399 O  O   . GLU A 1 661 ? 194.621 203.596 160.325 1.00 6.53   ? 571  GLU A O   1 
ATOM   4400 C  CB  . GLU A 1 661 ? 192.658 205.088 158.171 1.00 6.51   ? 571  GLU A CB  1 
ATOM   4401 C  CG  . GLU A 1 661 ? 193.914 205.933 158.063 1.00 6.62   ? 571  GLU A CG  1 
ATOM   4402 C  CD  . GLU A 1 661 ? 193.624 207.334 157.623 1.00 7.06   ? 571  GLU A CD  1 
ATOM   4403 O  OE1 . GLU A 1 661 ? 192.888 208.000 158.309 1.00 7.21   ? 571  GLU A OE1 1 
ATOM   4404 O  OE2 . GLU A 1 661 ? 194.129 207.742 156.604 1.00 7.13   ? 571  GLU A OE2 1 
ATOM   4405 N  N   . GLN A 1 662 ? 192.501 203.715 161.055 1.00 6.41   ? 572  GLN A N   1 
ATOM   4406 C  CA  . GLN A 1 662 ? 192.864 203.756 162.472 1.00 6.58   ? 572  GLN A CA  1 
ATOM   4407 C  C   . GLN A 1 662 ? 193.639 202.521 162.922 1.00 6.71   ? 572  GLN A C   1 
ATOM   4408 O  O   . GLN A 1 662 ? 194.307 202.559 163.954 1.00 6.90   ? 572  GLN A O   1 
ATOM   4409 C  CB  . GLN A 1 662 ? 191.616 203.899 163.345 1.00 6.57   ? 572  GLN A CB  1 
ATOM   4410 C  CG  . GLN A 1 662 ? 190.943 205.254 163.259 1.00 6.58   ? 572  GLN A CG  1 
ATOM   4411 C  CD  . GLN A 1 662 ? 191.765 206.343 163.884 1.00 6.68   ? 572  GLN A CD  1 
ATOM   4412 O  OE1 . GLN A 1 662 ? 192.043 206.317 165.085 1.00 7.11   ? 572  GLN A OE1 1 
ATOM   4413 N  NE2 . GLN A 1 662 ? 192.177 207.307 163.075 1.00 6.89   ? 572  GLN A NE2 1 
ATOM   4414 N  N   . ILE A 1 663 ? 193.525 201.419 162.189 1.00 6.57   ? 573  ILE A N   1 
ATOM   4415 C  CA  . ILE A 1 663 ? 194.191 200.185 162.576 1.00 6.77   ? 573  ILE A CA  1 
ATOM   4416 C  C   . ILE A 1 663 ? 195.263 199.732 161.576 1.00 6.73   ? 573  ILE A C   1 
ATOM   4417 O  O   . ILE A 1 663 ? 196.346 199.310 161.972 1.00 6.94   ? 573  ILE A O   1 
ATOM   4418 C  CB  . ILE A 1 663 ? 193.166 199.052 162.833 1.00 6.71   ? 573  ILE A CB  1 
ATOM   4419 C  CG1 . ILE A 1 663 ? 193.879 197.835 163.463 1.00 6.99   ? 573  ILE A CG1 1 
ATOM   4420 C  CG2 . ILE A 1 663 ? 192.393 198.669 161.567 1.00 6.58   ? 573  ILE A CG2 1 
ATOM   4421 C  CD1 . ILE A 1 663 ? 192.937 196.749 163.972 1.00 7.08   ? 573  ILE A CD1 1 
ATOM   4422 N  N   . ALA A 1 664 ? 194.941 199.788 160.288 1.00 6.60   ? 574  ALA A N   1 
ATOM   4423 C  CA  . ALA A 1 664 ? 195.811 199.243 159.250 1.00 6.69   ? 574  ALA A CA  1 
ATOM   4424 C  C   . ALA A 1 664 ? 196.530 200.406 158.579 1.00 6.73   ? 574  ALA A C   1 
ATOM   4425 O  O   . ALA A 1 664 ? 197.344 200.207 157.677 1.00 6.83   ? 574  ALA A O   1 
ATOM   4426 C  CB  . ALA A 1 664 ? 194.982 198.445 158.254 1.00 6.60   ? 574  ALA A CB  1 
ATOM   4427 N  N   . ARG A 1 665 ? 196.238 201.626 159.013 1.00 6.66   ? 575  ARG A N   1 
ATOM   4428 C  CA  . ARG A 1 665 ? 196.836 202.834 158.448 1.00 6.71   ? 575  ARG A CA  1 
ATOM   4429 C  C   . ARG A 1 665 ? 196.707 202.889 156.915 1.00 6.72   ? 575  ARG A C   1 
ATOM   4430 O  O   . ARG A 1 665 ? 197.662 203.171 156.199 1.00 7.00   ? 575  ARG A O   1 
ATOM   4431 C  CB  . ARG A 1 665 ? 198.313 202.905 158.817 1.00 6.92   ? 575  ARG A CB  1 
ATOM   4432 C  CG  . ARG A 1 665 ? 198.592 203.099 160.306 1.00 7.08   ? 575  ARG A CG  1 
ATOM   4433 C  CD  . ARG A 1 665 ? 200.053 203.111 160.594 1.00 7.37   ? 575  ARG A CD  1 
ATOM   4434 N  NE  . ARG A 1 665 ? 200.345 203.319 162.016 1.00 7.68   ? 575  ARG A NE  1 
ATOM   4435 C  CZ  . ARG A 1 665 ? 200.342 202.347 162.952 1.00 8.34   ? 575  ARG A CZ  1 
ATOM   4436 N  NH1 . ARG A 1 665 ? 200.642 202.615 164.188 1.00 8.30   ? 575  ARG A NH1 1 
ATOM   4437 N  NH2 . ARG A 1 665 ? 199.998 201.099 162.619 1.00 8.27   ? 575  ARG A NH2 1 
ATOM   4438 N  N   . THR A 1 666 ? 195.493 202.622 156.432 1.00 6.62   ? 576  THR A N   1 
ATOM   4439 C  CA  . THR A 1 666 ? 195.188 202.641 155.008 1.00 6.65   ? 576  THR A CA  1 
ATOM   4440 C  C   . THR A 1 666 ? 193.687 202.863 154.886 1.00 6.52   ? 576  THR A C   1 
ATOM   4441 O  O   . THR A 1 666 ? 192.922 202.484 155.768 1.00 6.39   ? 576  THR A O   1 
ATOM   4442 C  CB  . THR A 1 666 ? 195.586 201.388 154.224 1.00 6.69   ? 576  THR A CB  1 
ATOM   4443 N  N   . LYS A 1 667 ? 193.268 203.450 153.776 1.00 6.51   ? 577  LYS A N   1 
ATOM   4444 C  CA  . LYS A 1 667 ? 191.854 203.674 153.507 1.00 6.45   ? 577  LYS A CA  1 
ATOM   4445 C  C   . LYS A 1 667 ? 191.314 202.690 152.476 1.00 6.37   ? 577  LYS A C   1 
ATOM   4446 O  O   . LYS A 1 667 ? 190.169 202.803 152.038 1.00 6.25   ? 577  LYS A O   1 
ATOM   4447 C  CB  . LYS A 1 667 ? 191.616 205.106 153.030 1.00 6.52   ? 577  LYS A CB  1 
ATOM   4448 C  CG  . LYS A 1 667 ? 191.917 206.187 154.068 1.00 6.72   ? 577  LYS A CG  1 
ATOM   4449 C  CD  . LYS A 1 667 ? 191.470 207.564 153.591 1.00 7.05   ? 577  LYS A CD  1 
ATOM   4450 C  CE  . LYS A 1 667 ? 192.445 208.185 152.610 1.00 7.09   ? 577  LYS A CE  1 
ATOM   4451 N  NZ  . LYS A 1 667 ? 193.712 208.591 153.271 1.00 7.03   ? 577  LYS A NZ  1 
ATOM   4452 N  N   . GLU A 1 668 ? 192.149 201.743 152.072 1.00 6.38   ? 578  GLU A N   1 
ATOM   4453 C  CA  . GLU A 1 668 ? 191.775 200.798 151.029 1.00 6.20   ? 578  GLU A CA  1 
ATOM   4454 C  C   . GLU A 1 668 ? 191.963 199.356 151.473 1.00 6.02   ? 578  GLU A C   1 
ATOM   4455 O  O   . GLU A 1 668 ? 192.796 199.064 152.334 1.00 6.08   ? 578  GLU A O   1 
ATOM   4456 C  CB  . GLU A 1 668 ? 192.594 201.057 149.761 1.00 6.24   ? 578  GLU A CB  1 
ATOM   4457 N  N   . MET A 1 669 ? 191.210 198.452 150.860 1.00 5.83   ? 579  MET A N   1 
ATOM   4458 C  CA  . MET A 1 669 ? 191.397 197.028 151.098 1.00 5.69   ? 579  MET A CA  1 
ATOM   4459 C  C   . MET A 1 669 ? 192.602 196.531 150.307 1.00 5.61   ? 579  MET A C   1 
ATOM   4460 O  O   . MET A 1 669 ? 192.799 196.912 149.152 1.00 5.56   ? 579  MET A O   1 
ATOM   4461 C  CB  . MET A 1 669 ? 190.130 196.257 150.734 1.00 5.55   ? 579  MET A CB  1 
ATOM   4462 C  CG  . MET A 1 669 ? 188.943 196.527 151.654 1.00 5.57   ? 579  MET A CG  1 
ATOM   4463 S  SD  . MET A 1 669 ? 187.482 195.570 151.194 1.00 5.80   ? 579  MET A SD  1 
ATOM   4464 C  CE  . MET A 1 669 ? 186.288 196.112 152.418 1.00 5.40   ? 579  MET A CE  1 
ATOM   4465 N  N   . ASP A 1 670 ? 193.421 195.704 150.942 1.00 5.73   ? 580  ASP A N   1 
ATOM   4466 C  CA  . ASP A 1 670 ? 194.684 195.262 150.364 1.00 5.71   ? 580  ASP A CA  1 
ATOM   4467 C  C   . ASP A 1 670 ? 194.882 193.760 150.514 1.00 5.71   ? 580  ASP A C   1 
ATOM   4468 O  O   . ASP A 1 670 ? 194.770 193.217 151.611 1.00 5.73   ? 580  ASP A O   1 
ATOM   4469 C  CB  . ASP A 1 670 ? 195.856 196.003 151.014 1.00 5.84   ? 580  ASP A CB  1 
ATOM   4470 N  N   . ALA A 1 671 ? 195.133 193.089 149.396 1.00 5.67   ? 581  ALA A N   1 
ATOM   4471 C  CA  . ALA A 1 671 ? 195.297 191.639 149.371 1.00 5.59   ? 581  ALA A CA  1 
ATOM   4472 C  C   . ALA A 1 671 ? 196.706 191.198 149.754 1.00 5.68   ? 581  ALA A C   1 
ATOM   4473 O  O   . ALA A 1 671 ? 196.954 190.007 149.943 1.00 5.59   ? 581  ALA A O   1 
ATOM   4474 C  CB  . ALA A 1 671 ? 194.975 191.106 147.991 1.00 5.10   ? 581  ALA A CB  1 
ATOM   4475 N  N   . LYS A 1 672 ? 197.640 192.140 149.836 1.00 5.68   ? 582  LYS A N   1 
ATOM   4476 C  CA  . LYS A 1 672 ? 199.031 191.777 150.083 1.00 5.75   ? 582  LYS A CA  1 
ATOM   4477 C  C   . LYS A 1 672 ? 199.256 191.018 151.400 1.00 5.84   ? 582  LYS A C   1 
ATOM   4478 O  O   . LYS A 1 672 ? 199.986 190.030 151.395 1.00 5.81   ? 582  LYS A O   1 
ATOM   4479 C  CB  . LYS A 1 672 ? 199.947 192.995 149.977 1.00 5.78   ? 582  LYS A CB  1 
ATOM   4480 C  CG  . LYS A 1 672 ? 200.175 193.472 148.566 1.00 5.75   ? 582  LYS A CG  1 
ATOM   4481 C  CD  . LYS A 1 672 ? 201.105 194.669 148.552 1.00 5.77   ? 582  LYS A CD  1 
ATOM   4482 C  CE  . LYS A 1 672 ? 201.375 195.147 147.139 1.00 5.75   ? 582  LYS A CE  1 
ATOM   4483 N  NZ  . LYS A 1 672 ? 200.170 195.766 146.528 1.00 5.53   ? 582  LYS A NZ  1 
ATOM   4484 N  N   . PRO A 1 673 ? 198.674 191.448 152.534 1.00 5.89   ? 583  PRO A N   1 
ATOM   4485 C  CA  . PRO A 1 673 ? 198.719 190.771 153.821 1.00 6.03   ? 583  PRO A CA  1 
ATOM   4486 C  C   . PRO A 1 673 ? 198.320 189.299 153.732 1.00 6.09   ? 583  PRO A C   1 
ATOM   4487 O  O   . PRO A 1 673 ? 198.899 188.454 154.414 1.00 5.99   ? 583  PRO A O   1 
ATOM   4488 C  CB  . PRO A 1 673 ? 197.715 191.586 154.637 1.00 6.16   ? 583  PRO A CB  1 
ATOM   4489 C  CG  . PRO A 1 673 ? 197.805 192.965 154.051 1.00 6.10   ? 583  PRO A CG  1 
ATOM   4490 C  CD  . PRO A 1 673 ? 197.970 192.739 152.572 1.00 5.91   ? 583  PRO A CD  1 
ATOM   4491 N  N   . LEU A 1 674 ? 197.337 188.989 152.886 1.00 5.74   ? 584  LEU A N   1 
ATOM   4492 C  CA  . LEU A 1 674 ? 196.904 187.607 152.705 1.00 5.77   ? 584  LEU A CA  1 
ATOM   4493 C  C   . LEU A 1 674 ? 197.979 186.827 151.972 1.00 5.85   ? 584  LEU A C   1 
ATOM   4494 O  O   . LEU A 1 674 ? 198.318 185.702 152.343 1.00 5.83   ? 584  LEU A O   1 
ATOM   4495 C  CB  . LEU A 1 674 ? 195.586 187.553 151.915 1.00 5.64   ? 584  LEU A CB  1 
ATOM   4496 C  CG  . LEU A 1 674 ? 194.848 186.184 151.883 1.00 5.45   ? 584  LEU A CG  1 
ATOM   4497 C  CD1 . LEU A 1 674 ? 193.365 186.434 151.702 1.00 5.42   ? 584  LEU A CD1 1 
ATOM   4498 C  CD2 . LEU A 1 674 ? 195.373 185.316 150.744 1.00 5.27   ? 584  LEU A CD2 1 
ATOM   4499 N  N   . LEU A 1 675 ? 198.512 187.434 150.920 1.00 5.73   ? 585  LEU A N   1 
ATOM   4500 C  CA  . LEU A 1 675 ? 199.532 186.799 150.104 1.00 5.72   ? 585  LEU A CA  1 
ATOM   4501 C  C   . LEU A 1 675 ? 200.811 186.593 150.906 1.00 6.06   ? 585  LEU A C   1 
ATOM   4502 O  O   . LEU A 1 675 ? 201.525 185.611 150.708 1.00 6.15   ? 585  LEU A O   1 
ATOM   4503 C  CB  . LEU A 1 675 ? 199.813 187.652 148.863 1.00 5.67   ? 585  LEU A CB  1 
ATOM   4504 C  CG  . LEU A 1 675 ? 198.642 187.790 147.857 1.00 5.45   ? 585  LEU A CG  1 
ATOM   4505 C  CD1 . LEU A 1 675 ? 199.005 188.828 146.811 1.00 5.18   ? 585  LEU A CD1 1 
ATOM   4506 C  CD2 . LEU A 1 675 ? 198.353 186.447 147.199 1.00 4.84   ? 585  LEU A CD2 1 
ATOM   4507 N  N   . ASN A 1 676 ? 201.081 187.509 151.832 1.00 6.06   ? 586  ASN A N   1 
ATOM   4508 C  CA  . ASN A 1 676 ? 202.242 187.401 152.710 1.00 6.23   ? 586  ASN A CA  1 
ATOM   4509 C  C   . ASN A 1 676 ? 202.060 186.267 153.712 1.00 6.34   ? 586  ASN A C   1 
ATOM   4510 O  O   . ASN A 1 676 ? 202.978 185.488 153.959 1.00 6.55   ? 586  ASN A O   1 
ATOM   4511 C  CB  . ASN A 1 676 ? 202.487 188.720 153.421 1.00 6.24   ? 586  ASN A CB  1 
ATOM   4512 C  CG  . ASN A 1 676 ? 203.775 188.741 154.185 1.00 6.56   ? 586  ASN A CG  1 
ATOM   4513 O  OD1 . ASN A 1 676 ? 204.852 188.548 153.614 1.00 6.83   ? 586  ASN A OD1 1 
ATOM   4514 N  ND2 . ASN A 1 676 ? 203.687 188.973 155.468 1.00 6.82   ? 586  ASN A ND2 1 
ATOM   4515 N  N   . TYR A 1 677 ? 200.853 186.140 154.251 1.00 6.25   ? 587  TYR A N   1 
ATOM   4516 C  CA  . TYR A 1 677 ? 200.537 185.076 155.193 1.00 6.30   ? 587  TYR A CA  1 
ATOM   4517 C  C   . TYR A 1 677 ? 200.853 183.707 154.594 1.00 6.22   ? 587  TYR A C   1 
ATOM   4518 O  O   . TYR A 1 677 ? 201.479 182.864 155.237 1.00 6.52   ? 587  TYR A O   1 
ATOM   4519 C  CB  . TYR A 1 677 ? 199.060 185.143 155.588 1.00 6.17   ? 587  TYR A CB  1 
ATOM   4520 C  CG  . TYR A 1 677 ? 198.636 184.151 156.649 1.00 6.31   ? 587  TYR A CG  1 
ATOM   4521 C  CD1 . TYR A 1 677 ? 198.697 184.499 157.987 1.00 6.64   ? 587  TYR A CD1 1 
ATOM   4522 C  CD2 . TYR A 1 677 ? 198.176 182.902 156.285 1.00 6.05   ? 587  TYR A CD2 1 
ATOM   4523 C  CE1 . TYR A 1 677 ? 198.287 183.606 158.952 1.00 6.73   ? 587  TYR A CE1 1 
ATOM   4524 C  CE2 . TYR A 1 677 ? 197.770 182.006 157.248 1.00 6.07   ? 587  TYR A CE2 1 
ATOM   4525 C  CZ  . TYR A 1 677 ? 197.821 182.354 158.576 1.00 6.47   ? 587  TYR A CZ  1 
ATOM   4526 O  OH  . TYR A 1 677 ? 197.404 181.461 159.536 1.00 6.45   ? 587  TYR A OH  1 
ATOM   4527 N  N   . PHE A 1 678 ? 200.446 183.505 153.346 1.00 6.15   ? 588  PHE A N   1 
ATOM   4528 C  CA  . PHE A 1 678 ? 200.625 182.226 152.666 1.00 6.26   ? 588  PHE A CA  1 
ATOM   4529 C  C   . PHE A 1 678 ? 201.881 182.178 151.801 1.00 6.64   ? 588  PHE A C   1 
ATOM   4530 O  O   . PHE A 1 678 ? 202.029 181.281 150.972 1.00 6.52   ? 588  PHE A O   1 
ATOM   4531 C  CB  . PHE A 1 678 ? 199.410 181.920 151.783 1.00 5.80   ? 588  PHE A CB  1 
ATOM   4532 C  CG  . PHE A 1 678 ? 198.159 181.591 152.540 1.00 5.65   ? 588  PHE A CG  1 
ATOM   4533 C  CD1 . PHE A 1 678 ? 197.131 182.510 152.645 1.00 5.50   ? 588  PHE A CD1 1 
ATOM   4534 C  CD2 . PHE A 1 678 ? 198.005 180.356 153.144 1.00 5.58   ? 588  PHE A CD2 1 
ATOM   4535 C  CE1 . PHE A 1 678 ? 195.978 182.205 153.336 1.00 5.36   ? 588  PHE A CE1 1 
ATOM   4536 C  CE2 . PHE A 1 678 ? 196.857 180.049 153.833 1.00 5.23   ? 588  PHE A CE2 1 
ATOM   4537 C  CZ  . PHE A 1 678 ? 195.840 180.973 153.929 1.00 5.03   ? 588  PHE A CZ  1 
ATOM   4538 N  N   . LYS A 1 679 ? 202.780 183.139 151.982 1.00 6.66   ? 589  LYS A N   1 
ATOM   4539 C  CA  . LYS A 1 679 ? 203.998 183.211 151.182 1.00 6.93   ? 589  LYS A CA  1 
ATOM   4540 C  C   . LYS A 1 679 ? 204.818 181.905 151.141 1.00 7.26   ? 589  LYS A C   1 
ATOM   4541 O  O   . LYS A 1 679 ? 205.171 181.466 150.047 1.00 7.14   ? 589  LYS A O   1 
ATOM   4542 C  CB  . LYS A 1 679 ? 204.864 184.394 151.622 1.00 7.21   ? 589  LYS A CB  1 
ATOM   4543 C  CG  . LYS A 1 679 ? 206.103 184.615 150.772 1.00 8.10   ? 589  LYS A CG  1 
ATOM   4544 C  CD  . LYS A 1 679 ? 206.895 185.817 151.257 1.00 8.42   ? 589  LYS A CD  1 
ATOM   4545 C  CE  . LYS A 1 679 ? 208.141 186.037 150.411 1.00 9.68   ? 589  LYS A CE  1 
ATOM   4546 N  NZ  . LYS A 1 679 ? 208.928 187.212 150.878 1.00 9.74   ? 589  LYS A NZ  1 
ATOM   4547 N  N   . PRO A 1 680 ? 205.177 181.282 152.287 1.00 7.51   ? 590  PRO A N   1 
ATOM   4548 C  CA  . PRO A 1 680 ? 205.899 180.019 152.355 1.00 7.82   ? 590  PRO A CA  1 
ATOM   4549 C  C   . PRO A 1 680 ? 205.174 178.858 151.682 1.00 7.12   ? 590  PRO A C   1 
ATOM   4550 O  O   . PRO A 1 680 ? 205.815 177.952 151.147 1.00 7.24   ? 590  PRO A O   1 
ATOM   4551 C  CB  . PRO A 1 680 ? 206.041 179.789 153.869 1.00 8.84   ? 590  PRO A CB  1 
ATOM   4552 C  CG  . PRO A 1 680 ? 205.051 180.735 154.518 1.00 7.92   ? 590  PRO A CG  1 
ATOM   4553 C  CD  . PRO A 1 680 ? 204.967 181.911 153.600 1.00 7.44   ? 590  PRO A CD  1 
ATOM   4554 N  N   . LEU A 1 681 ? 203.845 178.894 151.658 1.00 6.81   ? 591  LEU A N   1 
ATOM   4555 C  CA  . LEU A 1 681 ? 203.099 177.843 150.986 1.00 6.74   ? 591  LEU A CA  1 
ATOM   4556 C  C   . LEU A 1 681 ? 203.183 178.034 149.484 1.00 6.42   ? 591  LEU A C   1 
ATOM   4557 O  O   . LEU A 1 681 ? 203.348 177.077 148.731 1.00 6.15   ? 591  LEU A O   1 
ATOM   4558 C  CB  . LEU A 1 681 ? 201.631 177.842 151.419 1.00 6.40   ? 591  LEU A CB  1 
ATOM   4559 C  CG  . LEU A 1 681 ? 200.738 176.744 150.795 1.00 5.98   ? 591  LEU A CG  1 
ATOM   4560 C  CD1 . LEU A 1 681 ? 201.238 175.356 151.209 1.00 6.01   ? 591  LEU A CD1 1 
ATOM   4561 C  CD2 . LEU A 1 681 ? 199.309 176.961 151.236 1.00 5.67   ? 591  LEU A CD2 1 
ATOM   4562 N  N   . PHE A 1 682 ? 203.074 179.286 149.058 1.00 6.36   ? 592  PHE A N   1 
ATOM   4563 C  CA  . PHE A 1 682 ? 203.143 179.631 147.649 1.00 6.18   ? 592  PHE A CA  1 
ATOM   4564 C  C   . PHE A 1 682 ? 204.456 179.165 147.046 1.00 6.26   ? 592  PHE A C   1 
ATOM   4565 O  O   . PHE A 1 682 ? 204.473 178.548 145.983 1.00 5.78   ? 592  PHE A O   1 
ATOM   4566 C  CB  . PHE A 1 682 ? 202.986 181.140 147.462 1.00 6.07   ? 592  PHE A CB  1 
ATOM   4567 C  CG  . PHE A 1 682 ? 203.074 181.604 146.039 1.00 5.71   ? 592  PHE A CG  1 
ATOM   4568 C  CD1 . PHE A 1 682 ? 201.994 181.481 145.184 1.00 4.99   ? 592  PHE A CD1 1 
ATOM   4569 C  CD2 . PHE A 1 682 ? 204.235 182.172 145.555 1.00 5.93   ? 592  PHE A CD2 1 
ATOM   4570 C  CE1 . PHE A 1 682 ? 202.070 181.915 143.882 1.00 4.77   ? 592  PHE A CE1 1 
ATOM   4571 C  CE2 . PHE A 1 682 ? 204.315 182.606 144.251 1.00 5.82   ? 592  PHE A CE2 1 
ATOM   4572 C  CZ  . PHE A 1 682 ? 203.228 182.476 143.414 1.00 5.37   ? 592  PHE A CZ  1 
ATOM   4573 N  N   . SER A 1 683 ? 205.559 179.455 147.729 1.00 6.47   ? 593  SER A N   1 
ATOM   4574 C  CA  . SER A 1 683 ? 206.876 179.083 147.224 1.00 6.50   ? 593  SER A CA  1 
ATOM   4575 C  C   . SER A 1 683 ? 207.037 177.571 147.119 1.00 6.31   ? 593  SER A C   1 
ATOM   4576 O  O   . SER A 1 683 ? 207.589 177.066 146.139 1.00 6.09   ? 593  SER A O   1 
ATOM   4577 C  CB  . SER A 1 683 ? 207.956 179.659 148.113 1.00 7.49   ? 593  SER A CB  1 
ATOM   4578 O  OG  . SER A 1 683 ? 207.968 181.057 148.039 1.00 8.07   ? 593  SER A OG  1 
ATOM   4579 N  N   . TRP A 1 684 ? 206.537 176.843 148.112 1.00 6.67   ? 594  TRP A N   1 
ATOM   4580 C  CA  . TRP A 1 684 ? 206.600 175.388 148.083 1.00 6.81   ? 594  TRP A CA  1 
ATOM   4581 C  C   . TRP A 1 684 ? 205.783 174.821 146.923 1.00 6.14   ? 594  TRP A C   1 
ATOM   4582 O  O   . TRP A 1 684 ? 206.259 173.958 146.182 1.00 6.00   ? 594  TRP A O   1 
ATOM   4583 C  CB  . TRP A 1 684 ? 206.118 174.808 149.414 1.00 7.12   ? 594  TRP A CB  1 
ATOM   4584 C  CG  . TRP A 1 684 ? 206.172 173.315 149.478 1.00 7.31   ? 594  TRP A CG  1 
ATOM   4585 C  CD1 . TRP A 1 684 ? 207.275 172.555 149.691 1.00 8.21   ? 594  TRP A CD1 1 
ATOM   4586 C  CD2 . TRP A 1 684 ? 205.069 172.390 149.346 1.00 6.88   ? 594  TRP A CD2 1 
ATOM   4587 N  NE1 . TRP A 1 684 ? 206.941 171.228 149.690 1.00 8.31   ? 594  TRP A NE1 1 
ATOM   4588 C  CE2 . TRP A 1 684 ? 205.595 171.109 149.484 1.00 7.38   ? 594  TRP A CE2 1 
ATOM   4589 C  CE3 . TRP A 1 684 ? 203.699 172.546 149.127 1.00 6.54   ? 594  TRP A CE3 1 
ATOM   4590 C  CZ2 . TRP A 1 684 ? 204.802 169.981 149.409 1.00 7.25   ? 594  TRP A CZ2 1 
ATOM   4591 C  CZ3 . TRP A 1 684 ? 202.903 171.415 149.052 1.00 6.23   ? 594  TRP A CZ3 1 
ATOM   4592 C  CH2 . TRP A 1 684 ? 203.441 170.167 149.188 1.00 6.50   ? 594  TRP A CH2 1 
ATOM   4593 N  N   . LEU A 1 685 ? 204.557 175.314 146.755 1.00 5.86   ? 595  LEU A N   1 
ATOM   4594 C  CA  . LEU A 1 685 ? 203.692 174.835 145.684 1.00 5.61   ? 595  LEU A CA  1 
ATOM   4595 C  C   . LEU A 1 685 ? 204.267 175.161 144.316 1.00 5.53   ? 595  LEU A C   1 
ATOM   4596 O  O   . LEU A 1 685 ? 204.204 174.343 143.403 1.00 4.96   ? 595  LEU A O   1 
ATOM   4597 C  CB  . LEU A 1 685 ? 202.295 175.468 145.787 1.00 5.12   ? 595  LEU A CB  1 
ATOM   4598 C  CG  . LEU A 1 685 ? 201.411 175.025 146.962 1.00 5.20   ? 595  LEU A CG  1 
ATOM   4599 C  CD1 . LEU A 1 685 ? 200.194 175.934 147.031 1.00 4.84   ? 595  LEU A CD1 1 
ATOM   4600 C  CD2 . LEU A 1 685 ? 200.979 173.587 146.766 1.00 4.97   ? 595  LEU A CD2 1 
ATOM   4601 N  N   . LYS A 1 686 ? 204.834 176.353 144.172 1.00 5.31   ? 596  LYS A N   1 
ATOM   4602 C  CA  . LYS A 1 686 ? 205.370 176.783 142.890 1.00 5.21   ? 596  LYS A CA  1 
ATOM   4603 C  C   . LYS A 1 686 ? 206.481 175.860 142.410 1.00 5.30   ? 596  LYS A C   1 
ATOM   4604 O  O   . LYS A 1 686 ? 206.507 175.465 141.244 1.00 5.02   ? 596  LYS A O   1 
ATOM   4605 C  CB  . LYS A 1 686 ? 205.870 178.225 142.980 1.00 5.35   ? 596  LYS A CB  1 
ATOM   4606 C  CG  . LYS A 1 686 ? 206.384 178.800 141.672 1.00 5.16   ? 596  LYS A CG  1 
ATOM   4607 C  CD  . LYS A 1 686 ? 206.764 180.265 141.824 1.00 5.52   ? 596  LYS A CD  1 
ATOM   4608 C  CE  . LYS A 1 686 ? 207.338 180.823 140.528 1.00 5.52   ? 596  LYS A CE  1 
ATOM   4609 N  NZ  . LYS A 1 686 ? 207.733 182.253 140.660 1.00 5.87   ? 596  LYS A NZ  1 
ATOM   4610 N  N   . GLU A 1 687 ? 207.383 175.496 143.314 1.00 5.46   ? 597  GLU A N   1 
ATOM   4611 C  CA  . GLU A 1 687 ? 208.493 174.616 142.971 1.00 5.43   ? 597  GLU A CA  1 
ATOM   4612 C  C   . GLU A 1 687 ? 207.995 173.223 142.601 1.00 5.30   ? 597  GLU A C   1 
ATOM   4613 O  O   . GLU A 1 687 ? 208.518 172.588 141.684 1.00 5.25   ? 597  GLU A O   1 
ATOM   4614 C  CB  . GLU A 1 687 ? 209.472 174.522 144.144 1.00 5.90   ? 597  GLU A CB  1 
ATOM   4615 N  N   . LEU A 1 688 ? 206.980 172.756 143.317 1.00 5.25   ? 598  LEU A N   1 
ATOM   4616 C  CA  . LEU A 1 688 ? 206.419 171.427 143.106 1.00 5.14   ? 598  LEU A CA  1 
ATOM   4617 C  C   . LEU A 1 688 ? 205.590 171.322 141.825 1.00 4.91   ? 598  LEU A C   1 
ATOM   4618 O  O   . LEU A 1 688 ? 205.674 170.326 141.107 1.00 4.88   ? 598  LEU A O   1 
ATOM   4619 C  CB  . LEU A 1 688 ? 205.549 171.055 144.313 1.00 5.09   ? 598  LEU A CB  1 
ATOM   4620 C  CG  . LEU A 1 688 ? 204.892 169.674 144.298 1.00 4.92   ? 598  LEU A CG  1 
ATOM   4621 C  CD1 . LEU A 1 688 ? 205.956 168.588 144.230 1.00 5.09   ? 598  LEU A CD1 1 
ATOM   4622 C  CD2 . LEU A 1 688 ? 204.057 169.529 145.550 1.00 5.37   ? 598  LEU A CD2 1 
ATOM   4623 N  N   . ASN A 1 689 ? 204.771 172.334 141.556 1.00 4.83   ? 599  ASN A N   1 
ATOM   4624 C  CA  . ASN A 1 689 ? 203.870 172.313 140.409 1.00 4.65   ? 599  ASN A CA  1 
ATOM   4625 C  C   . ASN A 1 689 ? 204.598 172.542 139.092 1.00 4.62   ? 599  ASN A C   1 
ATOM   4626 O  O   . ASN A 1 689 ? 204.196 172.017 138.053 1.00 4.53   ? 599  ASN A O   1 
ATOM   4627 C  CB  . ASN A 1 689 ? 202.770 173.342 140.577 1.00 4.48   ? 599  ASN A CB  1 
ATOM   4628 C  CG  . ASN A 1 689 ? 201.746 172.953 141.596 1.00 4.16   ? 599  ASN A CG  1 
ATOM   4629 O  OD1 . ASN A 1 689 ? 201.473 171.767 141.811 1.00 3.99   ? 599  ASN A OD1 1 
ATOM   4630 N  ND2 . ASN A 1 689 ? 201.169 173.934 142.233 1.00 4.04   ? 599  ASN A ND2 1 
ATOM   4631 N  N   . GLY A 1 690 ? 205.669 173.320 139.128 1.00 4.74   ? 600  GLY A N   1 
ATOM   4632 C  CA  . GLY A 1 690 ? 206.427 173.601 137.919 1.00 4.67   ? 600  GLY A CA  1 
ATOM   4633 C  C   . GLY A 1 690 ? 205.585 174.349 136.893 1.00 4.52   ? 600  GLY A C   1 
ATOM   4634 O  O   . GLY A 1 690 ? 205.005 175.392 137.193 1.00 4.55   ? 600  GLY A O   1 
ATOM   4635 N  N   . ASN A 1 691 ? 205.524 173.816 135.677 1.00 4.52   ? 601  ASN A N   1 
ATOM   4636 C  CA  . ASN A 1 691 ? 204.795 174.463 134.593 1.00 4.49   ? 601  ASN A CA  1 
ATOM   4637 C  C   . ASN A 1 691 ? 203.452 173.803 134.293 1.00 4.35   ? 601  ASN A C   1 
ATOM   4638 O  O   . ASN A 1 691 ? 202.897 173.983 133.210 1.00 4.41   ? 601  ASN A O   1 
ATOM   4639 C  CB  . ASN A 1 691 ? 205.655 174.511 133.347 1.00 4.60   ? 601  ASN A CB  1 
ATOM   4640 N  N   . SER A 1 692 ? 202.911 173.073 135.261 1.00 4.34   ? 602  SER A N   1 
ATOM   4641 C  CA  . SER A 1 692 ? 201.608 172.434 135.097 1.00 4.19   ? 602  SER A CA  1 
ATOM   4642 C  C   . SER A 1 692 ? 200.471 173.310 135.615 1.00 3.90   ? 602  SER A C   1 
ATOM   4643 O  O   . SER A 1 692 ? 199.325 172.871 135.699 1.00 3.59   ? 602  SER A O   1 
ATOM   4644 C  CB  . SER A 1 692 ? 201.580 171.097 135.808 1.00 4.17   ? 602  SER A CB  1 
ATOM   4645 O  OG  . SER A 1 692 ? 201.694 171.256 137.193 1.00 4.24   ? 602  SER A OG  1 
ATOM   4646 N  N   . VAL A 1 693 ? 200.797 174.537 135.995 1.00 3.93   ? 603  VAL A N   1 
ATOM   4647 C  CA  . VAL A 1 693 ? 199.826 175.449 136.585 1.00 3.68   ? 603  VAL A CA  1 
ATOM   4648 C  C   . VAL A 1 693 ? 198.942 176.114 135.535 1.00 3.56   ? 603  VAL A C   1 
ATOM   4649 O  O   . VAL A 1 693 ? 199.434 176.632 134.534 1.00 3.70   ? 603  VAL A O   1 
ATOM   4650 C  CB  . VAL A 1 693 ? 200.561 176.518 137.406 1.00 3.75   ? 603  VAL A CB  1 
ATOM   4651 C  CG1 . VAL A 1 693 ? 199.581 177.512 137.999 1.00 3.52   ? 603  VAL A CG1 1 
ATOM   4652 C  CG2 . VAL A 1 693 ? 201.352 175.836 138.488 1.00 3.88   ? 603  VAL A CG2 1 
ATOM   4653 N  N   . GLY A 1 694 ? 197.633 176.108 135.778 1.00 3.39   ? 604  GLY A N   1 
ATOM   4654 C  CA  . GLY A 1 694 ? 196.667 176.719 134.870 1.00 3.16   ? 604  GLY A CA  1 
ATOM   4655 C  C   . GLY A 1 694 ? 195.689 175.681 134.338 1.00 3.01   ? 604  GLY A C   1 
ATOM   4656 O  O   . GLY A 1 694 ? 195.872 174.483 134.549 1.00 2.89   ? 604  GLY A O   1 
ATOM   4657 N  N   . TRP A 1 695 ? 194.647 176.138 133.655 1.00 2.86   ? 605  TRP A N   1 
ATOM   4658 C  CA  . TRP A 1 695 ? 193.664 175.220 133.098 1.00 2.81   ? 605  TRP A CA  1 
ATOM   4659 C  C   . TRP A 1 695 ? 193.021 175.768 131.835 1.00 2.88   ? 605  TRP A C   1 
ATOM   4660 O  O   . TRP A 1 695 ? 192.924 176.981 131.652 1.00 2.82   ? 605  TRP A O   1 
ATOM   4661 C  CB  . TRP A 1 695 ? 192.555 174.925 134.112 1.00 2.70   ? 605  TRP A CB  1 
ATOM   4662 C  CG  . TRP A 1 695 ? 191.716 176.125 134.492 1.00 2.64   ? 605  TRP A CG  1 
ATOM   4663 C  CD1 . TRP A 1 695 ? 190.622 176.585 133.826 1.00 2.60   ? 605  TRP A CD1 1 
ATOM   4664 C  CD2 . TRP A 1 695 ? 191.864 176.987 135.649 1.00 2.55   ? 605  TRP A CD2 1 
ATOM   4665 N  NE1 . TRP A 1 695 ? 190.094 177.670 134.471 1.00 2.56   ? 605  TRP A NE1 1 
ATOM   4666 C  CE2 . TRP A 1 695 ? 190.835 177.929 135.587 1.00 2.51   ? 605  TRP A CE2 1 
ATOM   4667 C  CE3 . TRP A 1 695 ? 192.763 177.028 136.718 1.00 2.61   ? 605  TRP A CE3 1 
ATOM   4668 C  CZ2 . TRP A 1 695 ? 190.677 178.904 136.552 1.00 2.48   ? 605  TRP A CZ2 1 
ATOM   4669 C  CZ3 . TRP A 1 695 ? 192.598 178.005 137.688 1.00 2.67   ? 605  TRP A CZ3 1 
ATOM   4670 C  CH2 . TRP A 1 695 ? 191.582 178.917 137.605 1.00 2.54   ? 605  TRP A CH2 1 
ATOM   4671 N  N   . SER A 1 696 ? 192.518 174.867 130.998 1.00 2.85   ? 606  SER A N   1 
ATOM   4672 C  CA  . SER A 1 696 ? 191.692 175.260 129.866 1.00 3.00   ? 606  SER A CA  1 
ATOM   4673 C  C   . SER A 1 696 ? 190.227 175.086 130.232 1.00 3.07   ? 606  SER A C   1 
ATOM   4674 O  O   . SER A 1 696 ? 189.903 174.405 131.202 1.00 2.96   ? 606  SER A O   1 
ATOM   4675 C  CB  . SER A 1 696 ? 192.017 174.435 128.636 1.00 3.13   ? 606  SER A CB  1 
ATOM   4676 N  N   . ALA A 1 697 ? 189.339 175.680 129.446 1.00 3.24   ? 607  ALA A N   1 
ATOM   4677 C  CA  . ALA A 1 697 ? 187.906 175.553 129.687 1.00 3.33   ? 607  ALA A CA  1 
ATOM   4678 C  C   . ALA A 1 697 ? 187.244 174.778 128.558 1.00 3.69   ? 607  ALA A C   1 
ATOM   4679 O  O   . ALA A 1 697 ? 186.040 174.901 128.332 1.00 3.75   ? 607  ALA A O   1 
ATOM   4680 C  CB  . ALA A 1 697 ? 187.273 176.929 129.830 1.00 2.95   ? 607  ALA A CB  1 
ATOM   4681 N  N   . ASP A 1 698 ? 188.046 174.007 127.831 1.00 3.86   ? 608  ASP A N   1 
ATOM   4682 C  CA  . ASP A 1 698 ? 187.565 173.258 126.676 1.00 4.02   ? 608  ASP A CA  1 
ATOM   4683 C  C   . ASP A 1 698 ? 187.150 171.836 127.032 1.00 4.34   ? 608  ASP A C   1 
ATOM   4684 O  O   . ASP A 1 698 ? 186.269 171.261 126.394 1.00 4.79   ? 608  ASP A O   1 
ATOM   4685 C  CB  . ASP A 1 698 ? 188.650 173.214 125.604 1.00 3.89   ? 608  ASP A CB  1 
ATOM   4686 N  N   . TRP A 1 699 ? 187.810 171.260 128.027 1.00 4.38   ? 609  TRP A N   1 
ATOM   4687 C  CA  . TRP A 1 699 ? 187.568 169.878 128.417 1.00 4.83   ? 609  TRP A CA  1 
ATOM   4688 C  C   . TRP A 1 699 ? 186.441 169.754 129.429 1.00 5.00   ? 609  TRP A C   1 
ATOM   4689 O  O   . TRP A 1 699 ? 186.344 170.542 130.369 1.00 4.56   ? 609  TRP A O   1 
ATOM   4690 C  CB  . TRP A 1 699 ? 188.836 169.261 129.010 1.00 4.63   ? 609  TRP A CB  1 
ATOM   4691 C  CG  . TRP A 1 699 ? 188.652 167.847 129.469 1.00 4.79   ? 609  TRP A CG  1 
ATOM   4692 C  CD1 . TRP A 1 699 ? 188.824 166.725 128.723 1.00 5.10   ? 609  TRP A CD1 1 
ATOM   4693 C  CD2 . TRP A 1 699 ? 188.254 167.395 130.786 1.00 4.62   ? 609  TRP A CD2 1 
ATOM   4694 N  NE1 . TRP A 1 699 ? 188.562 165.613 129.475 1.00 5.10   ? 609  TRP A NE1 1 
ATOM   4695 C  CE2 . TRP A 1 699 ? 188.210 166.005 130.740 1.00 4.78   ? 609  TRP A CE2 1 
ATOM   4696 C  CE3 . TRP A 1 699 ? 187.931 168.053 131.981 1.00 4.39   ? 609  TRP A CE3 1 
ATOM   4697 C  CZ2 . TRP A 1 699 ? 187.860 165.250 131.843 1.00 4.59   ? 609  TRP A CZ2 1 
ATOM   4698 C  CZ3 . TRP A 1 699 ? 187.581 167.295 133.084 1.00 4.32   ? 609  TRP A CZ3 1 
ATOM   4699 C  CH2 . TRP A 1 699 ? 187.546 165.930 133.016 1.00 4.36   ? 609  TRP A CH2 1 
ATOM   4700 N  N   . SER A 1 700 ? 185.636 168.715 129.276 1.00 5.23   ? 610  SER A N   1 
ATOM   4701 C  CA  . SER A 1 700 ? 184.622 168.374 130.261 1.00 5.20   ? 610  SER A CA  1 
ATOM   4702 C  C   . SER A 1 700 ? 184.494 166.854 130.313 1.00 5.76   ? 610  SER A C   1 
ATOM   4703 O  O   . SER A 1 700 ? 184.821 166.185 129.333 1.00 5.75   ? 610  SER A O   1 
ATOM   4704 C  CB  . SER A 1 700 ? 183.299 169.025 129.896 1.00 5.37   ? 610  SER A CB  1 
ATOM   4705 O  OG  . SER A 1 700 ? 182.734 168.433 128.769 1.00 5.94   ? 610  SER A OG  1 
ATOM   4706 N  N   . PRO A 1 701 ? 184.002 166.288 131.420 1.00 5.54   ? 611  PRO A N   1 
ATOM   4707 C  CA  . PRO A 1 701 ? 183.835 164.864 131.670 1.00 5.74   ? 611  PRO A CA  1 
ATOM   4708 C  C   . PRO A 1 701 ? 183.064 164.131 130.577 1.00 6.47   ? 611  PRO A C   1 
ATOM   4709 O  O   . PRO A 1 701 ? 183.200 162.917 130.428 1.00 6.91   ? 611  PRO A O   1 
ATOM   4710 C  CB  . PRO A 1 701 ? 183.048 164.864 132.987 1.00 5.36   ? 611  PRO A CB  1 
ATOM   4711 C  CG  . PRO A 1 701 ? 183.454 166.140 133.671 1.00 4.79   ? 611  PRO A CG  1 
ATOM   4712 C  CD  . PRO A 1 701 ? 183.621 167.140 132.562 1.00 5.00   ? 611  PRO A CD  1 
ATOM   4713 N  N   . TYR A 1 702 ? 182.242 164.855 129.828 1.00 6.57   ? 612  TYR A N   1 
ATOM   4714 C  CA  . TYR A 1 702 ? 181.405 164.238 128.811 1.00 7.37   ? 612  TYR A CA  1 
ATOM   4715 C  C   . TYR A 1 702 ? 181.772 164.623 127.378 1.00 7.98   ? 612  TYR A C   1 
ATOM   4716 O  O   . TYR A 1 702 ? 181.080 164.235 126.438 1.00 8.74   ? 612  TYR A O   1 
ATOM   4717 C  CB  . TYR A 1 702 ? 179.945 164.595 129.085 1.00 7.42   ? 612  TYR A CB  1 
ATOM   4718 C  CG  . TYR A 1 702 ? 179.677 166.088 129.119 1.00 6.94   ? 612  TYR A CG  1 
ATOM   4719 C  CD1 . TYR A 1 702 ? 179.374 166.761 127.952 1.00 7.29   ? 612  TYR A CD1 1 
ATOM   4720 C  CD2 . TYR A 1 702 ? 179.732 166.781 130.320 1.00 6.00   ? 612  TYR A CD2 1 
ATOM   4721 C  CE1 . TYR A 1 702 ? 179.127 168.112 127.978 1.00 7.04   ? 612  TYR A CE1 1 
ATOM   4722 C  CE2 . TYR A 1 702 ? 179.485 168.139 130.344 1.00 5.41   ? 612  TYR A CE2 1 
ATOM   4723 C  CZ  . TYR A 1 702 ? 179.181 168.802 129.177 1.00 5.86   ? 612  TYR A CZ  1 
ATOM   4724 O  OH  . TYR A 1 702 ? 178.932 170.153 129.186 1.00 5.61   ? 612  TYR A OH  1 
ATOM   4725 N  N   . SER A 1 703 ? 182.834 165.403 127.205 1.00 7.59   ? 613  SER A N   1 
ATOM   4726 C  CA  . SER A 1 703 ? 183.167 165.940 125.883 1.00 8.30   ? 613  SER A CA  1 
ATOM   4727 C  C   . SER A 1 703 ? 183.859 164.937 124.967 1.00 9.20   ? 613  SER A C   1 
ATOM   4728 O  O   . SER A 1 703 ? 183.728 165.009 123.745 1.00 9.72   ? 613  SER A O   1 
ATOM   4729 C  CB  . SER A 1 703 ? 184.064 167.151 126.022 1.00 7.21   ? 613  SER A CB  1 
ATOM   4730 O  OG  . SER A 1 703 ? 185.314 166.793 126.546 1.00 6.86   ? 613  SER A OG  1 
ATOM   4731 N  N   . GLU A 1 704 ? 184.591 163.998 125.550 1.00 9.19   ? 614  GLU A N   1 
ATOM   4732 C  CA  . GLU A 1 704 ? 185.413 163.078 124.770 1.00 9.61   ? 614  GLU A CA  1 
ATOM   4733 C  C   . GLU A 1 704 ? 184.593 162.130 123.910 1.00 10.20  ? 614  GLU A C   1 
ATOM   4734 O  O   . GLU A 1 704 ? 185.065 161.650 122.880 1.00 11.06  ? 614  GLU A O   1 
ATOM   4735 C  CB  . GLU A 1 704 ? 186.318 162.264 125.694 1.00 9.64   ? 614  GLU A CB  1 
ATOM   4736 N  N   . GLN A 1 705 ? 183.378 161.840 124.343 1.00 10.49  ? 615  GLN A N   1 
ATOM   4737 C  CA  . GLN A 1 705 ? 182.525 160.899 123.639 1.00 11.65  ? 615  GLN A CA  1 
ATOM   4738 C  C   . GLN A 1 705 ? 181.264 161.550 123.089 1.00 11.97  ? 615  GLN A C   1 
ATOM   4739 O  O   . GLN A 1 705 ? 180.267 160.873 122.845 1.00 12.78  ? 615  GLN A O   1 
ATOM   4740 C  CB  . GLN A 1 705 ? 182.177 159.724 124.548 1.00 12.08  ? 615  GLN A CB  1 
ATOM   4741 C  CG  . GLN A 1 705 ? 181.668 160.120 125.900 1.00 10.72  ? 615  GLN A CG  1 
ATOM   4742 C  CD  . GLN A 1 705 ? 182.784 160.237 126.911 1.00 10.31  ? 615  GLN A CD  1 
ATOM   4743 O  OE1 . GLN A 1 705 ? 183.895 159.759 126.671 1.00 10.57  ? 615  GLN A OE1 1 
ATOM   4744 N  NE2 . GLN A 1 705 ? 182.509 160.868 128.039 1.00 9.62   ? 615  GLN A NE2 1 
ATOM   4745 N  N   . SER A 1 706 ? 181.312 162.860 122.903 1.00 11.99  ? 616  SER A N   1 
ATOM   4746 C  CA  . SER A 1 706 ? 180.179 163.581 122.338 1.00 13.06  ? 616  SER A CA  1 
ATOM   4747 C  C   . SER A 1 706 ? 180.267 163.660 120.820 1.00 14.66  ? 616  SER A C   1 
ATOM   4748 O  O   . SER A 1 706 ? 181.353 163.747 120.249 1.00 14.89  ? 616  SER A O   1 
ATOM   4749 C  CB  . SER A 1 706 ? 180.095 164.966 122.935 1.00 12.67  ? 616  SER A CB  1 
ATOM   4750 O  OG  . SER A 1 706 ? 179.653 164.921 124.267 1.00 10.89  ? 616  SER A OG  1 
ATOM   4751 N  N   . ILE A 1 707 ? 179.109 163.641 120.170 1.00 15.75  ? 617  ILE A N   1 
ATOM   4752 C  CA  . ILE A 1 707 ? 179.029 163.721 118.715 1.00 17.27  ? 617  ILE A CA  1 
ATOM   4753 C  C   . ILE A 1 707 ? 178.449 165.056 118.275 1.00 18.25  ? 617  ILE A C   1 
ATOM   4754 O  O   . ILE A 1 707 ? 177.429 165.496 118.800 1.00 18.16  ? 617  ILE A O   1 
ATOM   4755 C  CB  . ILE A 1 707 ? 178.178 162.568 118.147 1.00 17.73  ? 617  ILE A CB  1 
ATOM   4756 C  CG1 . ILE A 1 707 ? 178.823 161.227 118.514 1.00 17.35  ? 617  ILE A CG1 1 
ATOM   4757 C  CG2 . ILE A 1 707 ? 178.025 162.705 116.621 1.00 20.29  ? 617  ILE A CG2 1 
ATOM   4758 C  CD1 . ILE A 1 707 ? 177.946 160.029 118.257 1.00 18.94  ? 617  ILE A CD1 1 
ATOM   4759 N  N   . LYS A 1 708 ? 179.116 165.715 117.328 1.00 20.00  ? 618  LYS A N   1 
ATOM   4760 C  CA  . LYS A 1 708 ? 178.646 166.995 116.821 1.00 21.26  ? 618  LYS A CA  1 
ATOM   4761 C  C   . LYS A 1 708 ? 177.749 166.820 115.602 1.00 23.06  ? 618  LYS A C   1 
ATOM   4762 O  O   . LYS A 1 708 ? 178.084 166.098 114.661 1.00 23.52  ? 618  LYS A O   1 
ATOM   4763 C  CB  . LYS A 1 708 ? 179.814 167.925 116.492 1.00 21.90  ? 618  LYS A CB  1 
ATOM   4764 C  CG  . LYS A 1 708 ? 179.381 169.331 116.088 1.00 22.90  ? 618  LYS A CG  1 
ATOM   4765 C  CD  . LYS A 1 708 ? 180.561 170.268 115.903 1.00 23.68  ? 618  LYS A CD  1 
ATOM   4766 C  CE  . LYS A 1 708 ? 180.095 171.641 115.442 1.00 25.66  ? 618  LYS A CE  1 
ATOM   4767 N  NZ  . LYS A 1 708 ? 181.231 172.583 115.243 1.00 25.35  ? 618  LYS A NZ  1 
ATOM   4768 N  N   . VAL A 1 709 ? 176.599 167.481 115.633 1.00 23.28  ? 619  VAL A N   1 
ATOM   4769 C  CA  . VAL A 1 709 ? 175.624 167.404 114.560 1.00 24.65  ? 619  VAL A CA  1 
ATOM   4770 C  C   . VAL A 1 709 ? 175.377 168.770 113.936 1.00 26.73  ? 619  VAL A C   1 
ATOM   4771 O  O   . VAL A 1 709 ? 175.098 169.746 114.639 1.00 25.74  ? 619  VAL A O   1 
ATOM   4772 C  CB  . VAL A 1 709 ? 174.300 166.829 115.102 1.00 23.66  ? 619  VAL A CB  1 
ATOM   4773 C  CG1 . VAL A 1 709 ? 173.248 166.741 113.996 1.00 26.41  ? 619  VAL A CG1 1 
ATOM   4774 C  CG2 . VAL A 1 709 ? 174.564 165.470 115.694 1.00 23.24  ? 619  VAL A CG2 1 
ATOM   4775 N  N   . ARG A 1 710 ? 175.479 168.843 112.613 1.00 28.29  ? 620  ARG A N   1 
ATOM   4776 C  CA  . ARG A 1 710 ? 175.218 170.083 111.892 1.00 29.01  ? 620  ARG A CA  1 
ATOM   4777 C  C   . ARG A 1 710 ? 174.129 169.881 110.850 1.00 30.15  ? 620  ARG A C   1 
ATOM   4778 O  O   . ARG A 1 710 ? 174.204 168.968 110.021 1.00 30.42  ? 620  ARG A O   1 
ATOM   4779 C  CB  . ARG A 1 710 ? 176.485 170.608 111.228 1.00 29.03  ? 620  ARG A CB  1 
ATOM   4780 N  N   . ILE A 1 711 ? 173.100 170.715 110.908 1.00 31.56  ? 621  ILE A N   1 
ATOM   4781 C  CA  . ILE A 1 711 ? 171.958 170.584 110.012 1.00 32.69  ? 621  ILE A CA  1 
ATOM   4782 C  C   . ILE A 1 711 ? 171.719 171.823 109.169 1.00 33.49  ? 621  ILE A C   1 
ATOM   4783 O  O   . ILE A 1 711 ? 171.747 172.949 109.669 1.00 33.36  ? 621  ILE A O   1 
ATOM   4784 C  CB  . ILE A 1 711 ? 170.676 170.250 110.796 1.00 32.94  ? 621  ILE A CB  1 
ATOM   4785 C  CG1 . ILE A 1 711 ? 170.835 168.902 111.490 1.00 31.79  ? 621  ILE A CG1 1 
ATOM   4786 C  CG2 . ILE A 1 711 ? 169.467 170.247 109.865 1.00 34.23  ? 621  ILE A CG2 1 
ATOM   4787 C  CD1 . ILE A 1 711 ? 169.761 168.590 112.516 1.00 31.01  ? 621  ILE A CD1 1 
ATOM   4788 N  N   . SER A 1 712 ? 171.456 171.608 107.889 1.00 34.95  ? 622  SER A N   1 
ATOM   4789 C  CA  . SER A 1 712 ? 171.082 172.694 106.995 1.00 36.78  ? 622  SER A CA  1 
ATOM   4790 C  C   . SER A 1 712 ? 169.692 172.445 106.430 1.00 38.16  ? 622  SER A C   1 
ATOM   4791 O  O   . SER A 1 712 ? 169.503 171.569 105.585 1.00 38.30  ? 622  SER A O   1 
ATOM   4792 C  CB  . SER A 1 712 ? 172.081 172.821 105.867 1.00 37.53  ? 622  SER A CB  1 
ATOM   4793 N  N   . LEU A 1 713 ? 168.715 173.209 106.905 1.00 39.00  ? 623  LEU A N   1 
ATOM   4794 C  CA  . LEU A 1 713 ? 167.331 172.983 106.507 1.00 40.28  ? 623  LEU A CA  1 
ATOM   4795 C  C   . LEU A 1 713 ? 166.992 173.710 105.214 1.00 40.27  ? 623  LEU A C   1 
ATOM   4796 O  O   . LEU A 1 713 ? 166.133 173.269 104.450 1.00 41.40  ? 623  LEU A O   1 
ATOM   4797 C  CB  . LEU A 1 713 ? 166.373 173.444 107.616 1.00 40.16  ? 623  LEU A CB  1 
ATOM   4798 N  N   . LYS A 1 714 ? 167.652 174.840 104.979 1.00 40.71  ? 624  LYS A N   1 
ATOM   4799 C  CA  . LYS A 1 714 ? 167.359 175.653 103.803 1.00 41.58  ? 624  LYS A CA  1 
ATOM   4800 C  C   . LYS A 1 714 ? 167.813 174.959 102.526 1.00 41.43  ? 624  LYS A C   1 
ATOM   4801 O  O   . LYS A 1 714 ? 167.115 174.986 101.512 1.00 42.21  ? 624  LYS A O   1 
ATOM   4802 C  CB  . LYS A 1 714 ? 168.023 177.023 103.917 1.00 42.39  ? 624  LYS A CB  1 
ATOM   4803 N  N   . SER A 1 715 ? 168.970 174.310 102.586 1.00 41.16  ? 625  SER A N   1 
ATOM   4804 C  CA  . SER A 1 715 ? 169.530 173.634 101.423 1.00 41.18  ? 625  SER A CA  1 
ATOM   4805 C  C   . SER A 1 715 ? 168.849 172.293 101.192 1.00 41.49  ? 625  SER A C   1 
ATOM   4806 O  O   . SER A 1 715 ? 169.025 171.666 100.148 1.00 40.63  ? 625  SER A O   1 
ATOM   4807 C  CB  . SER A 1 715 ? 171.019 173.425 101.612 1.00 40.37  ? 625  SER A CB  1 
ATOM   4808 N  N   . ALA A 1 716 ? 168.082 171.851 102.179 1.00 41.22  ? 626  ALA A N   1 
ATOM   4809 C  CA  . ALA A 1 716 ? 167.388 170.575 102.100 1.00 41.09  ? 626  ALA A CA  1 
ATOM   4810 C  C   . ALA A 1 716 ? 166.007 170.733 101.492 1.00 41.71  ? 626  ALA A C   1 
ATOM   4811 O  O   . ALA A 1 716 ? 165.624 169.988 100.589 1.00 42.66  ? 626  ALA A O   1 
ATOM   4812 C  CB  . ALA A 1 716 ? 167.257 169.961 103.486 1.00 40.84  ? 626  ALA A CB  1 
ATOM   4813 N  N   . LEU A 1 717 ? 165.241 171.676 102.028 1.00 42.19  ? 627  LEU A N   1 
ATOM   4814 C  CA  . LEU A 1 717 ? 163.841 171.808 101.659 1.00 42.80  ? 627  LEU A CA  1 
ATOM   4815 C  C   . LEU A 1 717 ? 163.518 173.098 100.907 1.00 42.88  ? 627  LEU A C   1 
ATOM   4816 O  O   . LEU A 1 717 ? 162.443 173.217 100.315 1.00 44.38  ? 627  LEU A O   1 
ATOM   4817 C  CB  . LEU A 1 717 ? 162.991 171.694 102.923 1.00 42.15  ? 627  LEU A CB  1 
ATOM   4818 N  N   . GLY A 1 718 ? 164.422 174.073 100.937 1.00 43.23  ? 628  GLY A N   1 
ATOM   4819 C  CA  . GLY A 1 718 ? 164.163 175.347 100.277 1.00 43.54  ? 628  GLY A CA  1 
ATOM   4820 C  C   . GLY A 1 718 ? 162.959 176.051 100.885 1.00 44.03  ? 628  GLY A C   1 
ATOM   4821 O  O   . GLY A 1 718 ? 162.933 176.347 102.080 1.00 43.82  ? 628  GLY A O   1 
ATOM   4822 N  N   . GLU A 1 719 ? 161.959 176.318 100.054 1.00 44.49  ? 629  GLU A N   1 
ATOM   4823 C  CA  . GLU A 1 719 ? 160.747 177.007 100.480 1.00 43.36  ? 629  GLU A CA  1 
ATOM   4824 C  C   . GLU A 1 719 ? 159.963 176.200 101.512 1.00 43.58  ? 629  GLU A C   1 
ATOM   4825 O  O   . GLU A 1 719 ? 159.131 176.747 102.236 1.00 43.96  ? 629  GLU A O   1 
ATOM   4826 C  CB  . GLU A 1 719 ? 159.857 177.303 99.270  1.00 44.40  ? 629  GLU A CB  1 
ATOM   4827 N  N   . LYS A 1 720 ? 160.220 174.897 101.566 1.00 44.11  ? 630  LYS A N   1 
ATOM   4828 C  CA  . LYS A 1 720 ? 159.526 174.012 102.493 1.00 43.41  ? 630  LYS A CA  1 
ATOM   4829 C  C   . LYS A 1 720 ? 160.283 173.863 103.812 1.00 42.81  ? 630  LYS A C   1 
ATOM   4830 O  O   . LYS A 1 720 ? 159.868 173.104 104.689 1.00 41.89  ? 630  LYS A O   1 
ATOM   4831 C  CB  . LYS A 1 720 ? 159.300 172.642 101.853 1.00 43.99  ? 630  LYS A CB  1 
ATOM   4832 N  N   . ALA A 1 721 ? 161.403 174.570 103.944 1.00 42.42  ? 631  ALA A N   1 
ATOM   4833 C  CA  . ALA A 1 721 ? 162.224 174.488 105.146 1.00 41.65  ? 631  ALA A CA  1 
ATOM   4834 C  C   . ALA A 1 721 ? 161.468 175.002 106.362 1.00 40.78  ? 631  ALA A C   1 
ATOM   4835 O  O   . ALA A 1 721 ? 160.727 175.982 106.282 1.00 41.11  ? 631  ALA A O   1 
ATOM   4836 C  CB  . ALA A 1 721 ? 163.515 175.270 104.957 1.00 41.50  ? 631  ALA A CB  1 
ATOM   4837 N  N   . TYR A 1 722 ? 161.678 174.340 107.493 1.00 39.65  ? 632  TYR A N   1 
ATOM   4838 C  CA  . TYR A 1 722 ? 161.034 174.700 108.748 1.00 39.72  ? 632  TYR A CA  1 
ATOM   4839 C  C   . TYR A 1 722 ? 162.022 175.314 109.730 1.00 38.49  ? 632  TYR A C   1 
ATOM   4840 O  O   . TYR A 1 722 ? 163.209 175.448 109.433 1.00 38.71  ? 632  TYR A O   1 
ATOM   4841 C  CB  . TYR A 1 722 ? 160.363 173.469 109.359 1.00 38.32  ? 632  TYR A CB  1 
ATOM   4842 C  CG  . TYR A 1 722 ? 161.303 172.300 109.535 1.00 37.68  ? 632  TYR A CG  1 
ATOM   4843 C  CD1 . TYR A 1 722 ? 162.014 172.137 110.715 1.00 37.37  ? 632  TYR A CD1 1 
ATOM   4844 C  CD2 . TYR A 1 722 ? 161.457 171.388 108.504 1.00 38.11  ? 632  TYR A CD2 1 
ATOM   4845 C  CE1 . TYR A 1 722 ? 162.874 171.067 110.855 1.00 36.82  ? 632  TYR A CE1 1 
ATOM   4846 C  CE2 . TYR A 1 722 ? 162.315 170.322 108.648 1.00 36.82  ? 632  TYR A CE2 1 
ATOM   4847 C  CZ  . TYR A 1 722 ? 163.021 170.161 109.812 1.00 36.73  ? 632  TYR A CZ  1 
ATOM   4848 O  OH  . TYR A 1 722 ? 163.876 169.099 109.941 1.00 35.12  ? 632  TYR A OH  1 
ATOM   4849 N  N   . GLU A 1 723 ? 161.518 175.710 110.894 1.00 38.40  ? 633  GLU A N   1 
ATOM   4850 C  CA  . GLU A 1 723 ? 162.355 176.272 111.945 1.00 37.26  ? 633  GLU A CA  1 
ATOM   4851 C  C   . GLU A 1 723 ? 162.759 175.205 112.952 1.00 35.97  ? 633  GLU A C   1 
ATOM   4852 O  O   . GLU A 1 723 ? 161.915 174.469 113.464 1.00 36.05  ? 633  GLU A O   1 
ATOM   4853 C  CB  . GLU A 1 723 ? 161.620 177.406 112.661 1.00 38.09  ? 633  GLU A CB  1 
ATOM   4854 N  N   . TRP A 1 724 ? 164.049 175.132 113.258 1.00 35.26  ? 634  TRP A N   1 
ATOM   4855 C  CA  . TRP A 1 724 ? 164.529 174.151 114.224 1.00 34.67  ? 634  TRP A CA  1 
ATOM   4856 C  C   . TRP A 1 724 ? 164.280 174.628 115.646 1.00 33.80  ? 634  TRP A C   1 
ATOM   4857 O  O   . TRP A 1 724 ? 165.181 175.137 116.313 1.00 34.01  ? 634  TRP A O   1 
ATOM   4858 C  CB  . TRP A 1 724 ? 166.017 173.887 114.034 1.00 32.85  ? 634  TRP A CB  1 
ATOM   4859 C  CG  . TRP A 1 724 ? 166.525 172.724 114.836 1.00 32.35  ? 634  TRP A CG  1 
ATOM   4860 C  CD1 . TRP A 1 724 ? 167.111 172.776 116.062 1.00 31.58  ? 634  TRP A CD1 1 
ATOM   4861 C  CD2 . TRP A 1 724 ? 166.498 171.327 114.466 1.00 32.25  ? 634  TRP A CD2 1 
ATOM   4862 N  NE1 . TRP A 1 724 ? 167.448 171.515 116.479 1.00 30.52  ? 634  TRP A NE1 1 
ATOM   4863 C  CE2 . TRP A 1 724 ? 167.080 170.616 115.519 1.00 30.67  ? 634  TRP A CE2 1 
ATOM   4864 C  CE3 . TRP A 1 724 ? 166.037 170.634 113.346 1.00 33.53  ? 634  TRP A CE3 1 
ATOM   4865 C  CZ2 . TRP A 1 724 ? 167.212 169.240 115.490 1.00 29.87  ? 634  TRP A CZ2 1 
ATOM   4866 C  CZ3 . TRP A 1 724 ? 166.170 169.255 113.315 1.00 32.28  ? 634  TRP A CZ3 1 
ATOM   4867 C  CH2 . TRP A 1 724 ? 166.742 168.575 114.361 1.00 31.22  ? 634  TRP A CH2 1 
ATOM   4868 N  N   . ASN A 1 725 ? 163.043 174.478 116.092 1.00 33.83  ? 635  ASN A N   1 
ATOM   4869 C  CA  . ASN A 1 725 ? 162.631 174.926 117.413 1.00 34.40  ? 635  ASN A CA  1 
ATOM   4870 C  C   . ASN A 1 725 ? 162.814 173.826 118.453 1.00 32.07  ? 635  ASN A C   1 
ATOM   4871 O  O   . ASN A 1 725 ? 163.371 172.765 118.164 1.00 33.11  ? 635  ASN A O   1 
ATOM   4872 C  CB  . ASN A 1 725 ? 161.197 175.416 117.376 1.00 32.91  ? 635  ASN A CB  1 
ATOM   4873 C  CG  . ASN A 1 725 ? 160.227 174.327 117.040 1.00 33.96  ? 635  ASN A CG  1 
ATOM   4874 O  OD1 . ASN A 1 725 ? 160.564 173.136 117.082 1.00 32.55  ? 635  ASN A OD1 1 
ATOM   4875 N  ND2 . ASN A 1 725 ? 159.022 174.708 116.700 1.00 33.87  ? 635  ASN A ND2 1 
ATOM   4876 N  N   . ASP A 1 726 ? 162.352 174.088 119.672 1.00 32.27  ? 636  ASP A N   1 
ATOM   4877 C  CA  . ASP A 1 726 ? 162.511 173.143 120.769 1.00 31.88  ? 636  ASP A CA  1 
ATOM   4878 C  C   . ASP A 1 726 ? 161.820 171.816 120.482 1.00 31.63  ? 636  ASP A C   1 
ATOM   4879 O  O   . ASP A 1 726 ? 162.281 170.762 120.921 1.00 30.52  ? 636  ASP A O   1 
ATOM   4880 C  CB  . ASP A 1 726 ? 161.953 173.731 122.063 1.00 32.84  ? 636  ASP A CB  1 
ATOM   4881 N  N   . ASN A 1 727 ? 160.712 171.866 119.751 1.00 32.25  ? 637  ASN A N   1 
ATOM   4882 C  CA  . ASN A 1 727 ? 159.968 170.656 119.435 1.00 32.12  ? 637  ASN A CA  1 
ATOM   4883 C  C   . ASN A 1 727 ? 160.756 169.762 118.486 1.00 29.44  ? 637  ASN A C   1 
ATOM   4884 O  O   . ASN A 1 727 ? 160.689 168.534 118.577 1.00 29.14  ? 637  ASN A O   1 
ATOM   4885 C  CB  . ASN A 1 727 ? 158.616 171.004 118.847 1.00 31.77  ? 637  ASN A CB  1 
ATOM   4886 C  CG  . ASN A 1 727 ? 157.689 171.604 119.861 1.00 32.01  ? 637  ASN A CG  1 
ATOM   4887 O  OD1 . ASN A 1 727 ? 157.848 171.402 121.070 1.00 32.43  ? 637  ASN A OD1 1 
ATOM   4888 N  ND2 . ASN A 1 727 ? 156.720 172.345 119.393 1.00 32.11  ? 637  ASN A ND2 1 
ATOM   4889 N  N   . GLU A 1 728 ? 161.529 170.378 117.595 1.00 30.45  ? 638  GLU A N   1 
ATOM   4890 C  CA  . GLU A 1 728 ? 162.359 169.616 116.670 1.00 29.36  ? 638  GLU A CA  1 
ATOM   4891 C  C   . GLU A 1 728 ? 163.513 168.963 117.417 1.00 28.86  ? 638  GLU A C   1 
ATOM   4892 O  O   . GLU A 1 728 ? 163.887 167.826 117.127 1.00 28.38  ? 638  GLU A O   1 
ATOM   4893 C  CB  . GLU A 1 728 ? 162.887 170.509 115.546 1.00 31.83  ? 638  GLU A CB  1 
ATOM   4894 N  N   . MET A 1 729 ? 164.046 169.667 118.413 1.00 27.49  ? 639  MET A N   1 
ATOM   4895 C  CA  . MET A 1 729 ? 165.112 169.111 119.235 1.00 28.33  ? 639  MET A CA  1 
ATOM   4896 C  C   . MET A 1 729 ? 164.607 167.916 120.031 1.00 27.26  ? 639  MET A C   1 
ATOM   4897 O  O   . MET A 1 729 ? 165.310 166.915 120.177 1.00 24.36  ? 639  MET A O   1 
ATOM   4898 C  CB  . MET A 1 729 ? 165.678 170.168 120.177 1.00 27.93  ? 639  MET A CB  1 
ATOM   4899 C  CG  . MET A 1 729 ? 166.882 169.694 120.987 1.00 25.69  ? 639  MET A CG  1 
ATOM   4900 S  SD  . MET A 1 729 ? 168.292 169.254 119.952 1.00 24.05  ? 639  MET A SD  1 
ATOM   4901 C  CE  . MET A 1 729 ? 169.036 170.859 119.705 1.00 25.75  ? 639  MET A CE  1 
ATOM   4902 N  N   . TYR A 1 730 ? 163.378 168.015 120.531 1.00 27.27  ? 640  TYR A N   1 
ATOM   4903 C  CA  . TYR A 1 730 ? 162.762 166.909 121.252 1.00 25.90  ? 640  TYR A CA  1 
ATOM   4904 C  C   . TYR A 1 730 ? 162.650 165.682 120.359 1.00 24.85  ? 640  TYR A C   1 
ATOM   4905 O  O   . TYR A 1 730 ? 163.003 164.574 120.765 1.00 23.37  ? 640  TYR A O   1 
ATOM   4906 C  CB  . TYR A 1 730 ? 161.387 167.298 121.789 1.00 25.84  ? 640  TYR A CB  1 
ATOM   4907 C  CG  . TYR A 1 730 ? 160.683 166.153 122.471 1.00 25.05  ? 640  TYR A CG  1 
ATOM   4908 C  CD1 . TYR A 1 730 ? 161.023 165.801 123.766 1.00 23.93  ? 640  TYR A CD1 1 
ATOM   4909 C  CD2 . TYR A 1 730 ? 159.706 165.444 121.795 1.00 25.08  ? 640  TYR A CD2 1 
ATOM   4910 C  CE1 . TYR A 1 730 ? 160.388 164.743 124.382 1.00 23.44  ? 640  TYR A CE1 1 
ATOM   4911 C  CE2 . TYR A 1 730 ? 159.072 164.388 122.410 1.00 23.83  ? 640  TYR A CE2 1 
ATOM   4912 C  CZ  . TYR A 1 730 ? 159.409 164.037 123.697 1.00 24.20  ? 640  TYR A CZ  1 
ATOM   4913 O  OH  . TYR A 1 730 ? 158.774 162.982 124.309 1.00 25.45  ? 640  TYR A OH  1 
ATOM   4914 N  N   . LEU A 1 731 ? 162.159 165.884 119.137 1.00 24.46  ? 641  LEU A N   1 
ATOM   4915 C  CA  . LEU A 1 731 ? 162.023 164.788 118.190 1.00 26.16  ? 641  LEU A CA  1 
ATOM   4916 C  C   . LEU A 1 731 ? 163.373 164.144 117.912 1.00 24.05  ? 641  LEU A C   1 
ATOM   4917 O  O   . LEU A 1 731 ? 163.474 162.921 117.801 1.00 23.94  ? 641  LEU A O   1 
ATOM   4918 C  CB  . LEU A 1 731 ? 161.402 165.286 116.875 1.00 26.85  ? 641  LEU A CB  1 
ATOM   4919 C  CG  . LEU A 1 731 ? 161.220 164.225 115.754 1.00 27.40  ? 641  LEU A CG  1 
ATOM   4920 C  CD1 . LEU A 1 731 ? 160.295 163.112 116.235 1.00 27.15  ? 641  LEU A CD1 1 
ATOM   4921 C  CD2 . LEU A 1 731 ? 160.651 164.900 114.511 1.00 29.06  ? 641  LEU A CD2 1 
ATOM   4922 N  N   . PHE A 1 732 ? 164.413 164.965 117.793 1.00 26.15  ? 642  PHE A N   1 
ATOM   4923 C  CA  . PHE A 1 732 ? 165.750 164.451 117.532 1.00 24.60  ? 642  PHE A CA  1 
ATOM   4924 C  C   . PHE A 1 732 ? 166.198 163.521 118.649 1.00 24.79  ? 642  PHE A C   1 
ATOM   4925 O  O   . PHE A 1 732 ? 166.673 162.416 118.387 1.00 21.27  ? 642  PHE A O   1 
ATOM   4926 C  CB  . PHE A 1 732 ? 166.755 165.592 117.377 1.00 24.39  ? 642  PHE A CB  1 
ATOM   4927 C  CG  . PHE A 1 732 ? 168.139 165.121 117.052 1.00 24.76  ? 642  PHE A CG  1 
ATOM   4928 C  CD1 . PHE A 1 732 ? 168.515 164.891 115.738 1.00 24.83  ? 642  PHE A CD1 1 
ATOM   4929 C  CD2 . PHE A 1 732 ? 169.064 164.888 118.058 1.00 23.90  ? 642  PHE A CD2 1 
ATOM   4930 C  CE1 . PHE A 1 732 ? 169.785 164.443 115.437 1.00 24.11  ? 642  PHE A CE1 1 
ATOM   4931 C  CE2 . PHE A 1 732 ? 170.331 164.437 117.760 1.00 22.38  ? 642  PHE A CE2 1 
ATOM   4932 C  CZ  . PHE A 1 732 ? 170.691 164.215 116.449 1.00 22.87  ? 642  PHE A CZ  1 
ATOM   4933 N  N   . ARG A 1 733 ? 166.037 163.961 119.893 1.00 21.34  ? 643  ARG A N   1 
ATOM   4934 C  CA  . ARG A 1 733 ? 166.444 163.153 121.036 1.00 20.84  ? 643  ARG A CA  1 
ATOM   4935 C  C   . ARG A 1 733 ? 165.661 161.850 121.096 1.00 21.20  ? 643  ARG A C   1 
ATOM   4936 O  O   . ARG A 1 733 ? 166.208 160.802 121.441 1.00 19.03  ? 643  ARG A O   1 
ATOM   4937 C  CB  . ARG A 1 733 ? 166.257 163.916 122.332 1.00 19.10  ? 643  ARG A CB  1 
ATOM   4938 C  CG  . ARG A 1 733 ? 167.214 165.068 122.530 1.00 18.26  ? 643  ARG A CG  1 
ATOM   4939 C  CD  . ARG A 1 733 ? 167.319 165.441 123.948 1.00 16.19  ? 643  ARG A CD  1 
ATOM   4940 N  NE  . ARG A 1 733 ? 166.094 165.997 124.464 1.00 16.84  ? 643  ARG A NE  1 
ATOM   4941 C  CZ  . ARG A 1 733 ? 165.773 166.040 125.768 1.00 16.57  ? 643  ARG A CZ  1 
ATOM   4942 N  NH1 . ARG A 1 733 ? 166.601 165.550 126.667 1.00 15.67  ? 643  ARG A NH1 1 
ATOM   4943 N  NH2 . ARG A 1 733 ? 164.627 166.575 126.147 1.00 17.46  ? 643  ARG A NH2 1 
ATOM   4944 N  N   . SER A 1 734 ? 164.386 161.911 120.732 1.00 21.51  ? 644  SER A N   1 
ATOM   4945 C  CA  . SER A 1 734 ? 163.549 160.720 120.702 1.00 20.63  ? 644  SER A CA  1 
ATOM   4946 C  C   . SER A 1 734 ? 164.018 159.755 119.619 1.00 21.01  ? 644  SER A C   1 
ATOM   4947 O  O   . SER A 1 734 ? 164.029 158.540 119.822 1.00 20.77  ? 644  SER A O   1 
ATOM   4948 C  CB  . SER A 1 734 ? 162.103 161.109 120.467 1.00 21.90  ? 644  SER A CB  1 
ATOM   4949 N  N   . SER A 1 735 ? 164.438 160.304 118.479 1.00 21.69  ? 645  SER A N   1 
ATOM   4950 C  CA  . SER A 1 735 ? 164.939 159.498 117.372 1.00 21.45  ? 645  SER A CA  1 
ATOM   4951 C  C   . SER A 1 735 ? 166.247 158.809 117.740 1.00 21.38  ? 645  SER A C   1 
ATOM   4952 O  O   . SER A 1 735 ? 166.469 157.650 117.387 1.00 21.64  ? 645  SER A O   1 
ATOM   4953 C  CB  . SER A 1 735 ? 165.149 160.365 116.146 1.00 23.03  ? 645  SER A CB  1 
ATOM   4954 N  N   . VAL A 1 736 ? 167.103 159.513 118.478 1.00 20.78  ? 646  VAL A N   1 
ATOM   4955 C  CA  . VAL A 1 736 ? 168.355 158.923 118.927 1.00 20.64  ? 646  VAL A CA  1 
ATOM   4956 C  C   . VAL A 1 736 ? 168.085 157.793 119.905 1.00 20.69  ? 646  VAL A C   1 
ATOM   4957 O  O   . VAL A 1 736 ? 168.674 156.719 119.790 1.00 20.17  ? 646  VAL A O   1 
ATOM   4958 C  CB  . VAL A 1 736 ? 169.268 159.978 119.584 1.00 19.84  ? 646  VAL A CB  1 
ATOM   4959 C  CG1 . VAL A 1 736 ? 170.471 159.302 120.237 1.00 18.60  ? 646  VAL A CG1 1 
ATOM   4960 C  CG2 . VAL A 1 736 ? 169.741 160.969 118.532 1.00 20.61  ? 646  VAL A CG2 1 
ATOM   4961 N  N   . ALA A 1 737 ? 167.181 158.020 120.854 1.00 19.92  ? 647  ALA A N   1 
ATOM   4962 C  CA  . ALA A 1 737 ? 166.844 156.990 121.826 1.00 18.98  ? 647  ALA A CA  1 
ATOM   4963 C  C   . ALA A 1 737 ? 166.329 155.744 121.120 1.00 20.61  ? 647  ALA A C   1 
ATOM   4964 O  O   . ALA A 1 737 ? 166.682 154.624 121.488 1.00 19.11  ? 647  ALA A O   1 
ATOM   4965 C  CB  . ALA A 1 737 ? 165.809 157.510 122.806 1.00 18.19  ? 647  ALA A CB  1 
ATOM   4966 N  N   . TYR A 1 738 ? 165.528 155.942 120.074 1.00 20.83  ? 648  TYR A N   1 
ATOM   4967 C  CA  . TYR A 1 738 ? 165.033 154.830 119.276 1.00 20.86  ? 648  TYR A CA  1 
ATOM   4968 C  C   . TYR A 1 738 ? 166.184 154.048 118.662 1.00 21.93  ? 648  TYR A C   1 
ATOM   4969 O  O   . TYR A 1 738 ? 166.238 152.821 118.770 1.00 21.56  ? 648  TYR A O   1 
ATOM   4970 C  CB  . TYR A 1 738 ? 164.097 155.331 118.175 1.00 21.48  ? 648  TYR A CB  1 
ATOM   4971 C  CG  . TYR A 1 738 ? 163.690 154.259 117.195 1.00 22.53  ? 648  TYR A CG  1 
ATOM   4972 C  CD1 . TYR A 1 738 ? 162.696 153.356 117.527 1.00 23.05  ? 648  TYR A CD1 1 
ATOM   4973 C  CD2 . TYR A 1 738 ? 164.315 154.180 115.959 1.00 23.19  ? 648  TYR A CD2 1 
ATOM   4974 C  CE1 . TYR A 1 738 ? 162.327 152.376 116.630 1.00 23.52  ? 648  TYR A CE1 1 
ATOM   4975 C  CE2 . TYR A 1 738 ? 163.947 153.199 115.062 1.00 24.70  ? 648  TYR A CE2 1 
ATOM   4976 C  CZ  . TYR A 1 738 ? 162.956 152.299 115.395 1.00 24.34  ? 648  TYR A CZ  1 
ATOM   4977 O  OH  . TYR A 1 738 ? 162.585 151.320 114.503 1.00 25.55  ? 648  TYR A OH  1 
ATOM   4978 N  N   . ALA A 1 739 ? 167.107 154.760 118.023 1.00 21.26  ? 649  ALA A N   1 
ATOM   4979 C  CA  . ALA A 1 739 ? 168.247 154.123 117.376 1.00 21.25  ? 649  ALA A CA  1 
ATOM   4980 C  C   . ALA A 1 739 ? 169.058 153.317 118.379 1.00 22.41  ? 649  ALA A C   1 
ATOM   4981 O  O   . ALA A 1 739 ? 169.575 152.248 118.052 1.00 21.30  ? 649  ALA A O   1 
ATOM   4982 C  CB  . ALA A 1 739 ? 169.129 155.172 116.715 1.00 22.40  ? 649  ALA A CB  1 
ATOM   4983 N  N   . MET A 1 740 ? 169.169 153.835 119.601 1.00 20.32  ? 650  MET A N   1 
ATOM   4984 C  CA  . MET A 1 740 ? 169.929 153.158 120.643 1.00 20.59  ? 650  MET A CA  1 
ATOM   4985 C  C   . MET A 1 740 ? 169.239 151.876 121.088 1.00 21.41  ? 650  MET A C   1 
ATOM   4986 O  O   . MET A 1 740 ? 169.901 150.885 121.398 1.00 21.27  ? 650  MET A O   1 
ATOM   4987 C  CB  . MET A 1 740 ? 170.134 154.084 121.839 1.00 18.84  ? 650  MET A CB  1 
ATOM   4988 C  CG  . MET A 1 740 ? 171.022 155.290 121.573 1.00 18.34  ? 650  MET A CG  1 
ATOM   4989 S  SD  . MET A 1 740 ? 172.618 154.863 120.882 1.00 18.69  ? 650  MET A SD  1 
ATOM   4990 C  CE  . MET A 1 740 ? 173.333 153.916 122.196 1.00 18.14  ? 650  MET A CE  1 
ATOM   4991 N  N   . ARG A 1 741 ? 167.906 151.883 121.103 1.00 19.81  ? 651  ARG A N   1 
ATOM   4992 C  CA  . ARG A 1 741 ? 167.165 150.694 121.506 1.00 20.71  ? 651  ARG A CA  1 
ATOM   4993 C  C   . ARG A 1 741 ? 167.334 149.590 120.478 1.00 22.35  ? 651  ARG A C   1 
ATOM   4994 O  O   . ARG A 1 741 ? 167.525 148.425 120.827 1.00 23.21  ? 651  ARG A O   1 
ATOM   4995 C  CB  . ARG A 1 741 ? 165.677 150.981 121.660 1.00 20.30  ? 651  ARG A CB  1 
ATOM   4996 C  CG  . ARG A 1 741 ? 165.288 151.834 122.850 1.00 18.64  ? 651  ARG A CG  1 
ATOM   4997 C  CD  . ARG A 1 741 ? 163.813 151.933 122.985 1.00 17.70  ? 651  ARG A CD  1 
ATOM   4998 N  NE  . ARG A 1 741 ? 163.423 152.802 124.080 1.00 16.78  ? 651  ARG A NE  1 
ATOM   4999 C  CZ  . ARG A 1 741 ? 162.250 152.736 124.740 1.00 16.52  ? 651  ARG A CZ  1 
ATOM   5000 N  NH1 . ARG A 1 741 ? 161.354 151.826 124.427 1.00 16.38  ? 651  ARG A NH1 1 
ATOM   5001 N  NH2 . ARG A 1 741 ? 162.008 153.599 125.708 1.00 16.19  ? 651  ARG A NH2 1 
ATOM   5002 N  N   . VAL A 1 742 ? 167.278 149.967 119.205 1.00 22.33  ? 652  VAL A N   1 
ATOM   5003 C  CA  . VAL A 1 742 ? 167.386 149.007 118.119 1.00 22.76  ? 652  VAL A CA  1 
ATOM   5004 C  C   . VAL A 1 742 ? 168.772 148.386 118.080 1.00 23.84  ? 652  VAL A C   1 
ATOM   5005 O  O   . VAL A 1 742 ? 168.913 147.170 117.948 1.00 24.33  ? 652  VAL A O   1 
ATOM   5006 C  CB  . VAL A 1 742 ? 167.085 149.687 116.772 1.00 23.48  ? 652  VAL A CB  1 
ATOM   5007 C  CG1 . VAL A 1 742 ? 167.360 148.728 115.627 1.00 24.69  ? 652  VAL A CG1 1 
ATOM   5008 C  CG2 . VAL A 1 742 ? 165.637 150.146 116.748 1.00 23.07  ? 652  VAL A CG2 1 
ATOM   5009 N  N   . TYR A 1 743 ? 169.794 149.225 118.197 1.00 23.32  ? 653  TYR A N   1 
ATOM   5010 C  CA  . TYR A 1 743 ? 171.169 148.756 118.181 1.00 23.96  ? 653  TYR A CA  1 
ATOM   5011 C  C   . TYR A 1 743 ? 171.436 147.739 119.276 1.00 22.75  ? 653  TYR A C   1 
ATOM   5012 O  O   . TYR A 1 743 ? 171.972 146.663 119.017 1.00 25.24  ? 653  TYR A O   1 
ATOM   5013 C  CB  . TYR A 1 743 ? 172.126 149.932 118.326 1.00 22.95  ? 653  TYR A CB  1 
ATOM   5014 C  CG  . TYR A 1 743 ? 173.551 149.521 118.558 1.00 23.91  ? 653  TYR A CG  1 
ATOM   5015 C  CD1 . TYR A 1 743 ? 174.350 149.142 117.498 1.00 23.90  ? 653  TYR A CD1 1 
ATOM   5016 C  CD2 . TYR A 1 743 ? 174.058 149.516 119.847 1.00 23.39  ? 653  TYR A CD2 1 
ATOM   5017 C  CE1 . TYR A 1 743 ? 175.653 148.758 117.727 1.00 23.78  ? 653  TYR A CE1 1 
ATOM   5018 C  CE2 . TYR A 1 743 ? 175.356 149.131 120.076 1.00 23.14  ? 653  TYR A CE2 1 
ATOM   5019 C  CZ  . TYR A 1 743 ? 176.153 148.752 119.022 1.00 23.44  ? 653  TYR A CZ  1 
ATOM   5020 O  OH  . TYR A 1 743 ? 177.451 148.365 119.249 1.00 22.98  ? 653  TYR A OH  1 
ATOM   5021 N  N   . PHE A 1 744 ? 171.069 148.074 120.506 1.00 23.84  ? 654  PHE A N   1 
ATOM   5022 C  CA  . PHE A 1 744 ? 171.352 147.187 121.623 1.00 24.37  ? 654  PHE A CA  1 
ATOM   5023 C  C   . PHE A 1 744 ? 170.585 145.877 121.533 1.00 23.66  ? 654  PHE A C   1 
ATOM   5024 O  O   . PHE A 1 744 ? 171.129 144.815 121.839 1.00 24.57  ? 654  PHE A O   1 
ATOM   5025 C  CB  . PHE A 1 744 ? 171.070 147.882 122.952 1.00 22.30  ? 654  PHE A CB  1 
ATOM   5026 C  CG  . PHE A 1 744 ? 172.270 148.597 123.502 1.00 22.43  ? 654  PHE A CG  1 
ATOM   5027 C  CD1 . PHE A 1 744 ? 172.455 149.955 123.317 1.00 21.39  ? 654  PHE A CD1 1 
ATOM   5028 C  CD2 . PHE A 1 744 ? 173.227 147.895 124.209 1.00 23.18  ? 654  PHE A CD2 1 
ATOM   5029 C  CE1 . PHE A 1 744 ? 173.571 150.588 123.830 1.00 20.57  ? 654  PHE A CE1 1 
ATOM   5030 C  CE2 . PHE A 1 744 ? 174.337 148.528 124.719 1.00 22.38  ? 654  PHE A CE2 1 
ATOM   5031 C  CZ  . PHE A 1 744 ? 174.507 149.875 124.527 1.00 20.34  ? 654  PHE A CZ  1 
ATOM   5032 N  N   . LEU A 1 745 ? 169.336 145.937 121.087 1.00 25.28  ? 655  LEU A N   1 
ATOM   5033 C  CA  . LEU A 1 745 ? 168.531 144.730 120.980 1.00 25.21  ? 655  LEU A CA  1 
ATOM   5034 C  C   . LEU A 1 745 ? 169.063 143.776 119.914 1.00 26.05  ? 655  LEU A C   1 
ATOM   5035 O  O   . LEU A 1 745 ? 169.083 142.563 120.119 1.00 26.16  ? 655  LEU A O   1 
ATOM   5036 C  CB  . LEU A 1 745 ? 167.075 145.091 120.664 1.00 23.96  ? 655  LEU A CB  1 
ATOM   5037 C  CG  . LEU A 1 745 ? 166.087 143.912 120.556 1.00 24.84  ? 655  LEU A CG  1 
ATOM   5038 C  CD1 . LEU A 1 745 ? 166.043 143.147 121.881 1.00 24.10  ? 655  LEU A CD1 1 
ATOM   5039 C  CD2 . LEU A 1 745 ? 164.713 144.453 120.195 1.00 25.05  ? 655  LEU A CD2 1 
ATOM   5040 N  N   . LYS A 1 746 ? 169.479 144.317 118.771 1.00 25.22  ? 656  LYS A N   1 
ATOM   5041 C  CA  . LYS A 1 746 ? 169.948 143.482 117.670 1.00 25.02  ? 656  LYS A CA  1 
ATOM   5042 C  C   . LYS A 1 746 ? 171.398 143.026 117.820 1.00 25.68  ? 656  LYS A C   1 
ATOM   5043 O  O   . LYS A 1 746 ? 171.761 141.945 117.357 1.00 25.48  ? 656  LYS A O   1 
ATOM   5044 C  CB  . LYS A 1 746 ? 169.792 144.217 116.338 1.00 25.54  ? 656  LYS A CB  1 
ATOM   5045 N  N   . VAL A 1 747 ? 172.236 143.860 118.428 1.00 25.23  ? 657  VAL A N   1 
ATOM   5046 C  CA  . VAL A 1 747 ? 173.666 143.577 118.492 1.00 24.86  ? 657  VAL A CA  1 
ATOM   5047 C  C   . VAL A 1 747 ? 174.098 142.906 119.792 1.00 24.93  ? 657  VAL A C   1 
ATOM   5048 O  O   . VAL A 1 747 ? 174.924 141.995 119.776 1.00 25.77  ? 657  VAL A O   1 
ATOM   5049 C  CB  . VAL A 1 747 ? 174.466 144.876 118.285 1.00 25.30  ? 657  VAL A CB  1 
ATOM   5050 C  CG1 . VAL A 1 747 ? 175.958 144.625 118.456 1.00 24.90  ? 657  VAL A CG1 1 
ATOM   5051 C  CG2 . VAL A 1 747 ? 174.170 145.413 116.899 1.00 25.03  ? 657  VAL A CG2 1 
ATOM   5052 N  N   . LYS A 1 748 ? 173.586 143.387 120.920 1.00 24.38  ? 658  LYS A N   1 
ATOM   5053 C  CA  . LYS A 1 748 ? 174.005 142.874 122.218 1.00 25.46  ? 658  LYS A CA  1 
ATOM   5054 C  C   . LYS A 1 748 ? 172.972 141.913 122.787 1.00 25.99  ? 658  LYS A C   1 
ATOM   5055 O  O   . LYS A 1 748 ? 173.186 141.300 123.832 1.00 25.62  ? 658  LYS A O   1 
ATOM   5056 C  CB  . LYS A 1 748 ? 174.232 144.029 123.195 1.00 24.78  ? 658  LYS A CB  1 
ATOM   5057 N  N   . ASN A 1 749 ? 171.833 141.818 122.109 1.00 25.75  ? 659  ASN A N   1 
ATOM   5058 C  CA  . ASN A 1 749 ? 170.696 141.044 122.594 1.00 26.07  ? 659  ASN A CA  1 
ATOM   5059 C  C   . ASN A 1 749 ? 170.253 141.537 123.965 1.00 25.55  ? 659  ASN A C   1 
ATOM   5060 O  O   . ASN A 1 749 ? 169.898 140.744 124.839 1.00 25.52  ? 659  ASN A O   1 
ATOM   5061 C  CB  . ASN A 1 749 ? 171.030 139.564 122.632 1.00 25.66  ? 659  ASN A CB  1 
ATOM   5062 N  N   . GLU A 1 750 ? 170.270 142.855 124.147 1.00 25.19  ? 660  GLU A N   1 
ATOM   5063 C  CA  . GLU A 1 750 ? 169.865 143.460 125.409 1.00 23.81  ? 660  GLU A CA  1 
ATOM   5064 C  C   . GLU A 1 750 ? 168.693 144.400 125.208 1.00 23.18  ? 660  GLU A C   1 
ATOM   5065 O  O   . GLU A 1 750 ? 168.657 145.162 124.243 1.00 23.49  ? 660  GLU A O   1 
ATOM   5066 C  CB  . GLU A 1 750 ? 171.024 144.242 126.034 1.00 23.92  ? 660  GLU A CB  1 
ATOM   5067 N  N   . THR A 1 751 ? 167.757 144.384 126.143 1.00 22.61  ? 661  THR A N   1 
ATOM   5068 C  CA  . THR A 1 751 ? 166.641 145.314 126.078 1.00 21.62  ? 661  THR A CA  1 
ATOM   5069 C  C   . THR A 1 751 ? 166.860 146.463 127.046 1.00 20.62  ? 661  THR A C   1 
ATOM   5070 O  O   . THR A 1 751 ? 166.810 146.282 128.263 1.00 20.08  ? 661  THR A O   1 
ATOM   5071 C  CB  . THR A 1 751 ? 165.309 144.613 126.401 1.00 21.71  ? 661  THR A CB  1 
ATOM   5072 N  N   . ILE A 1 752 ? 167.112 147.644 126.500 1.00 19.92  ? 662  ILE A N   1 
ATOM   5073 C  CA  . ILE A 1 752 ? 167.382 148.816 127.315 1.00 18.93  ? 662  ILE A CA  1 
ATOM   5074 C  C   . ILE A 1 752 ? 166.432 149.946 126.936 1.00 17.76  ? 662  ILE A C   1 
ATOM   5075 O  O   . ILE A 1 752 ? 166.448 150.400 125.794 1.00 17.51  ? 662  ILE A O   1 
ATOM   5076 C  CB  . ILE A 1 752 ? 168.833 149.289 127.136 1.00 18.51  ? 662  ILE A CB  1 
ATOM   5077 C  CG1 . ILE A 1 752 ? 169.802 148.158 127.506 1.00 20.18  ? 662  ILE A CG1 1 
ATOM   5078 C  CG2 . ILE A 1 752 ? 169.082 150.520 128.000 1.00 17.40  ? 662  ILE A CG2 1 
ATOM   5079 C  CD1 . ILE A 1 752 ? 171.240 148.445 127.152 1.00 20.95  ? 662  ILE A CD1 1 
ATOM   5080 N  N   . PRO A 1 753 ? 165.609 150.420 127.871 1.00 17.12  ? 663  PRO A N   1 
ATOM   5081 C  CA  . PRO A 1 753 ? 164.582 151.422 127.686 1.00 16.78  ? 663  PRO A CA  1 
ATOM   5082 C  C   . PRO A 1 753 ? 165.149 152.833 127.620 1.00 16.11  ? 663  PRO A C   1 
ATOM   5083 O  O   . PRO A 1 753 ? 164.893 153.649 128.503 1.00 15.88  ? 663  PRO A O   1 
ATOM   5084 C  CB  . PRO A 1 753 ? 163.717 151.218 128.930 1.00 16.47  ? 663  PRO A CB  1 
ATOM   5085 C  CG  . PRO A 1 753 ? 164.691 150.751 129.986 1.00 16.24  ? 663  PRO A CG  1 
ATOM   5086 C  CD  . PRO A 1 753 ? 165.693 149.890 129.239 1.00 17.12  ? 663  PRO A CD  1 
ATOM   5087 N  N   . PHE A 1 754 ? 165.904 153.121 126.565 1.00 16.14  ? 664  PHE A N   1 
ATOM   5088 C  CA  . PHE A 1 754 ? 166.438 154.463 126.369 1.00 15.67  ? 664  PHE A CA  1 
ATOM   5089 C  C   . PHE A 1 754 ? 165.307 155.436 126.082 1.00 16.02  ? 664  PHE A C   1 
ATOM   5090 O  O   . PHE A 1 754 ? 164.439 155.162 125.254 1.00 16.14  ? 664  PHE A O   1 
ATOM   5091 C  CB  . PHE A 1 754 ? 167.424 154.503 125.198 1.00 16.37  ? 664  PHE A CB  1 
ATOM   5092 C  CG  . PHE A 1 754 ? 168.748 153.857 125.455 1.00 16.36  ? 664  PHE A CG  1 
ATOM   5093 C  CD1 . PHE A 1 754 ? 169.025 152.600 124.958 1.00 17.56  ? 664  PHE A CD1 1 
ATOM   5094 C  CD2 . PHE A 1 754 ? 169.731 154.511 126.177 1.00 15.30  ? 664  PHE A CD2 1 
ATOM   5095 C  CE1 . PHE A 1 754 ? 170.249 152.011 125.173 1.00 18.21  ? 664  PHE A CE1 1 
ATOM   5096 C  CE2 . PHE A 1 754 ? 170.958 153.921 126.395 1.00 15.01  ? 664  PHE A CE2 1 
ATOM   5097 C  CZ  . PHE A 1 754 ? 171.216 152.670 125.891 1.00 16.84  ? 664  PHE A CZ  1 
ATOM   5098 N  N   . ARG A 1 755 ? 165.346 156.590 126.730 1.00 14.81  ? 665  ARG A N   1 
ATOM   5099 C  CA  . ARG A 1 755 ? 164.354 157.636 126.511 1.00 14.52  ? 665  ARG A CA  1 
ATOM   5100 C  C   . ARG A 1 755 ? 165.009 158.909 125.999 1.00 15.05  ? 665  ARG A C   1 
ATOM   5101 O  O   . ARG A 1 755 ? 166.231 159.037 126.018 1.00 14.67  ? 665  ARG A O   1 
ATOM   5102 C  CB  . ARG A 1 755 ? 163.604 157.939 127.796 1.00 14.88  ? 665  ARG A CB  1 
ATOM   5103 C  CG  . ARG A 1 755 ? 162.775 156.793 128.345 1.00 15.03  ? 665  ARG A CG  1 
ATOM   5104 C  CD  . ARG A 1 755 ? 162.105 157.171 129.611 1.00 14.97  ? 665  ARG A CD  1 
ATOM   5105 N  NE  . ARG A 1 755 ? 163.062 157.382 130.684 1.00 14.80  ? 665  ARG A NE  1 
ATOM   5106 C  CZ  . ARG A 1 755 ? 162.788 158.004 131.847 1.00 15.39  ? 665  ARG A CZ  1 
ATOM   5107 N  NH1 . ARG A 1 755 ? 161.581 158.475 132.074 1.00 15.20  ? 665  ARG A NH1 1 
ATOM   5108 N  NH2 . ARG A 1 755 ? 163.731 158.142 132.763 1.00 15.33  ? 665  ARG A NH2 1 
ATOM   5109 N  N   . ALA A 1 756 ? 164.198 159.863 125.555 1.00 15.10  ? 666  ALA A N   1 
ATOM   5110 C  CA  . ALA A 1 756 ? 164.718 161.147 125.098 1.00 15.69  ? 666  ALA A CA  1 
ATOM   5111 C  C   . ALA A 1 756 ? 165.488 161.838 126.215 1.00 14.81  ? 666  ALA A C   1 
ATOM   5112 O  O   . ALA A 1 756 ? 166.444 162.568 125.966 1.00 14.95  ? 666  ALA A O   1 
ATOM   5113 C  CB  . ALA A 1 756 ? 163.587 162.038 124.614 1.00 17.43  ? 666  ALA A CB  1 
ATOM   5114 N  N   . GLU A 1 757 ? 165.068 161.601 127.451 1.00 14.51  ? 667  GLU A N   1 
ATOM   5115 C  CA  . GLU A 1 757 ? 165.696 162.193 128.625 1.00 14.06  ? 667  GLU A CA  1 
ATOM   5116 C  C   . GLU A 1 757 ? 167.099 161.647 128.877 1.00 13.56  ? 667  GLU A C   1 
ATOM   5117 O  O   . GLU A 1 757 ? 167.859 162.216 129.661 1.00 12.48  ? 667  GLU A O   1 
ATOM   5118 C  CB  . GLU A 1 757 ? 164.815 161.969 129.853 1.00 14.07  ? 667  GLU A CB  1 
ATOM   5119 N  N   . ASP A 1 758 ? 167.438 160.539 128.226 1.00 13.83  ? 668  ASP A N   1 
ATOM   5120 C  CA  . ASP A 1 758 ? 168.746 159.919 128.385 1.00 13.01  ? 668  ASP A CA  1 
ATOM   5121 C  C   . ASP A 1 758 ? 169.708 160.434 127.328 1.00 13.11  ? 668  ASP A C   1 
ATOM   5122 O  O   . ASP A 1 758 ? 170.876 160.043 127.286 1.00 12.27  ? 668  ASP A O   1 
ATOM   5123 C  CB  . ASP A 1 758 ? 168.630 158.400 128.286 1.00 13.48  ? 668  ASP A CB  1 
ATOM   5124 C  CG  . ASP A 1 758 ? 167.799 157.805 129.406 1.00 13.40  ? 668  ASP A CG  1 
ATOM   5125 O  OD1 . ASP A 1 758 ? 168.010 158.162 130.540 1.00 13.13  ? 668  ASP A OD1 1 
ATOM   5126 O  OD2 . ASP A 1 758 ? 166.938 157.008 129.113 1.00 14.12  ? 668  ASP A OD2 1 
ATOM   5127 N  N   . VAL A 1 759 ? 169.212 161.323 126.475 1.00 13.05  ? 669  VAL A N   1 
ATOM   5128 C  CA  . VAL A 1 759 ? 170.037 161.943 125.456 1.00 12.88  ? 669  VAL A CA  1 
ATOM   5129 C  C   . VAL A 1 759 ? 170.323 163.377 125.869 1.00 12.51  ? 669  VAL A C   1 
ATOM   5130 O  O   . VAL A 1 759 ? 169.411 164.194 126.006 1.00 13.30  ? 669  VAL A O   1 
ATOM   5131 C  CB  . VAL A 1 759 ? 169.333 161.910 124.087 1.00 14.42  ? 669  VAL A CB  1 
ATOM   5132 C  CG1 . VAL A 1 759 ? 170.223 162.551 123.026 1.00 14.53  ? 669  VAL A CG1 1 
ATOM   5133 C  CG2 . VAL A 1 759 ? 168.994 160.472 123.719 1.00 14.99  ? 669  VAL A CG2 1 
ATOM   5134 N  N   . TRP A 1 760 ? 171.587 163.665 126.115 1.00 11.90  ? 670  TRP A N   1 
ATOM   5135 C  CA  . TRP A 1 760 ? 171.983 164.962 126.629 1.00 11.47  ? 670  TRP A CA  1 
ATOM   5136 C  C   . TRP A 1 760 ? 172.467 165.842 125.495 1.00 12.37  ? 670  TRP A C   1 
ATOM   5137 O  O   . TRP A 1 760 ? 173.213 165.389 124.631 1.00 13.15  ? 670  TRP A O   1 
ATOM   5138 C  CB  . TRP A 1 760 ? 173.076 164.777 127.671 1.00 10.17  ? 670  TRP A CB  1 
ATOM   5139 C  CG  . TRP A 1 760 ? 172.608 164.031 128.884 1.00 9.61   ? 670  TRP A CG  1 
ATOM   5140 C  CD1 . TRP A 1 760 ? 172.509 162.681 129.010 1.00 10.04  ? 670  TRP A CD1 1 
ATOM   5141 C  CD2 . TRP A 1 760 ? 172.182 164.579 130.149 1.00 8.31   ? 670  TRP A CD2 1 
ATOM   5142 N  NE1 . TRP A 1 760 ? 172.044 162.353 130.252 1.00 9.31   ? 670  TRP A NE1 1 
ATOM   5143 C  CE2 . TRP A 1 760 ? 171.841 163.500 130.965 1.00 8.28   ? 670  TRP A CE2 1 
ATOM   5144 C  CE3 . TRP A 1 760 ? 172.062 165.878 130.649 1.00 7.19   ? 670  TRP A CE3 1 
ATOM   5145 C  CZ2 . TRP A 1 760 ? 171.385 163.676 132.257 1.00 7.31   ? 670  TRP A CZ2 1 
ATOM   5146 C  CZ3 . TRP A 1 760 ? 171.607 166.054 131.947 1.00 6.35   ? 670  TRP A CZ3 1 
ATOM   5147 C  CH2 . TRP A 1 760 ? 171.276 164.981 132.730 1.00 6.25   ? 670  TRP A CH2 1 
ATOM   5148 N  N   . VAL A 1 761 ? 172.032 167.095 125.490 1.00 12.98  ? 671  VAL A N   1 
ATOM   5149 C  CA  . VAL A 1 761 ? 172.398 168.029 124.432 1.00 13.97  ? 671  VAL A CA  1 
ATOM   5150 C  C   . VAL A 1 761 ? 173.064 169.271 125.000 1.00 13.79  ? 671  VAL A C   1 
ATOM   5151 O  O   . VAL A 1 761 ? 172.604 169.836 125.992 1.00 13.64  ? 671  VAL A O   1 
ATOM   5152 C  CB  . VAL A 1 761 ? 171.157 168.413 123.603 1.00 14.81  ? 671  VAL A CB  1 
ATOM   5153 C  CG1 . VAL A 1 761 ? 171.520 169.451 122.551 1.00 17.17  ? 671  VAL A CG1 1 
ATOM   5154 C  CG2 . VAL A 1 761 ? 170.601 167.165 122.932 1.00 15.21  ? 671  VAL A CG2 1 
ATOM   5155 N  N   . SER A 1 762 ? 174.161 169.682 124.376 1.00 14.72  ? 672  SER A N   1 
ATOM   5156 C  CA  . SER A 1 762 ? 174.934 170.818 124.856 1.00 15.13  ? 672  SER A CA  1 
ATOM   5157 C  C   . SER A 1 762 ? 175.532 171.638 123.724 1.00 17.85  ? 672  SER A C   1 
ATOM   5158 O  O   . SER A 1 762 ? 175.544 171.214 122.568 1.00 18.09  ? 672  SER A O   1 
ATOM   5159 C  CB  . SER A 1 762 ? 176.047 170.330 125.758 1.00 13.19  ? 672  SER A CB  1 
ATOM   5160 N  N   . ASP A 1 763 ? 176.049 172.814 124.076 1.00 18.30  ? 673  ASP A N   1 
ATOM   5161 C  CA  . ASP A 1 763 ? 176.724 173.697 123.128 1.00 19.80  ? 673  ASP A CA  1 
ATOM   5162 C  C   . ASP A 1 763 ? 175.846 173.995 121.921 1.00 21.55  ? 673  ASP A C   1 
ATOM   5163 O  O   . ASP A 1 763 ? 176.301 173.942 120.779 1.00 22.01  ? 673  ASP A O   1 
ATOM   5164 C  CB  . ASP A 1 763 ? 178.053 173.080 122.676 1.00 19.31  ? 673  ASP A CB  1 
ATOM   5165 N  N   . GLU A 1 764 ? 174.585 174.313 122.184 1.00 21.41  ? 674  GLU A N   1 
ATOM   5166 C  CA  . GLU A 1 764 ? 173.638 174.622 121.124 1.00 22.17  ? 674  GLU A CA  1 
ATOM   5167 C  C   . GLU A 1 764 ? 173.726 176.085 120.708 1.00 24.37  ? 674  GLU A C   1 
ATOM   5168 O  O   . GLU A 1 764 ? 173.677 176.986 121.546 1.00 23.90  ? 674  GLU A O   1 
ATOM   5169 C  CB  . GLU A 1 764 ? 172.216 174.289 121.576 1.00 22.63  ? 674  GLU A CB  1 
ATOM   5170 N  N   . LYS A 1 765 ? 173.846 176.310 119.406 1.00 24.88  ? 675  LYS A N   1 
ATOM   5171 C  CA  . LYS A 1 765 ? 173.926 177.652 118.838 1.00 25.48  ? 675  LYS A CA  1 
ATOM   5172 C  C   . LYS A 1 765 ? 172.595 178.077 118.227 1.00 26.73  ? 675  LYS A C   1 
ATOM   5173 O  O   . LYS A 1 765 ? 171.657 177.286 118.154 1.00 26.69  ? 675  LYS A O   1 
ATOM   5174 C  CB  . LYS A 1 765 ? 175.030 177.714 117.782 1.00 26.34  ? 675  LYS A CB  1 
ATOM   5175 N  N   . ILE A 1 766 ? 172.516 179.331 117.782 1.00 27.50  ? 676  ILE A N   1 
ATOM   5176 C  CA  . ILE A 1 766 ? 171.323 179.809 117.085 1.00 27.90  ? 676  ILE A CA  1 
ATOM   5177 C  C   . ILE A 1 766 ? 171.132 179.028 115.790 1.00 28.29  ? 676  ILE A C   1 
ATOM   5178 O  O   . ILE A 1 766 ? 170.030 178.576 115.480 1.00 28.61  ? 676  ILE A O   1 
ATOM   5179 C  CB  . ILE A 1 766 ? 171.416 181.316 116.781 1.00 28.67  ? 676  ILE A CB  1 
ATOM   5180 N  N   . ARG A 1 767 ? 172.225 178.850 115.053 1.00 28.40  ? 677  ARG A N   1 
ATOM   5181 C  CA  . ARG A 1 767 ? 172.228 177.990 113.878 1.00 29.09  ? 677  ARG A CA  1 
ATOM   5182 C  C   . ARG A 1 767 ? 172.087 176.552 114.345 1.00 28.31  ? 677  ARG A C   1 
ATOM   5183 O  O   . ARG A 1 767 ? 172.379 176.245 115.501 1.00 27.84  ? 677  ARG A O   1 
ATOM   5184 C  CB  . ARG A 1 767 ? 173.513 178.156 113.084 1.00 28.50  ? 677  ARG A CB  1 
ATOM   5185 N  N   . VAL A 1 768 ? 171.646 175.657 113.476 1.00 29.06  ? 678  VAL A N   1 
ATOM   5186 C  CA  . VAL A 1 768 ? 171.388 174.310 113.961 1.00 29.19  ? 678  VAL A CA  1 
ATOM   5187 C  C   . VAL A 1 768 ? 172.674 173.507 114.059 1.00 28.47  ? 678  VAL A C   1 
ATOM   5188 O  O   . VAL A 1 768 ? 173.018 172.730 113.167 1.00 28.71  ? 678  VAL A O   1 
ATOM   5189 C  CB  . VAL A 1 768 ? 170.365 173.584 113.076 1.00 30.86  ? 678  VAL A CB  1 
ATOM   5190 N  N   . SER A 1 769 ? 173.370 173.714 115.166 1.00 27.75  ? 679  SER A N   1 
ATOM   5191 C  CA  . SER A 1 769 ? 174.627 173.046 115.471 1.00 25.91  ? 679  SER A CA  1 
ATOM   5192 C  C   . SER A 1 769 ? 174.703 172.750 116.962 1.00 24.72  ? 679  SER A C   1 
ATOM   5193 O  O   . SER A 1 769 ? 174.590 173.656 117.790 1.00 24.51  ? 679  SER A O   1 
ATOM   5194 C  CB  . SER A 1 769 ? 175.797 173.913 115.051 1.00 26.40  ? 679  SER A CB  1 
ATOM   5195 N  N   . PHE A 1 770 ? 174.861 171.475 117.302 1.00 23.95  ? 680  PHE A N   1 
ATOM   5196 C  CA  . PHE A 1 770 ? 174.886 171.056 118.700 1.00 21.70  ? 680  PHE A CA  1 
ATOM   5197 C  C   . PHE A 1 770 ? 175.637 169.745 118.883 1.00 21.38  ? 680  PHE A C   1 
ATOM   5198 O  O   . PHE A 1 770 ? 175.878 169.016 117.922 1.00 20.88  ? 680  PHE A O   1 
ATOM   5199 C  CB  . PHE A 1 770 ? 173.460 170.907 119.228 1.00 21.97  ? 680  PHE A CB  1 
ATOM   5200 C  CG  . PHE A 1 770 ? 172.657 169.879 118.490 1.00 22.22  ? 680  PHE A CG  1 
ATOM   5201 C  CD1 . PHE A 1 770 ? 172.594 168.571 118.940 1.00 20.95  ? 680  PHE A CD1 1 
ATOM   5202 C  CD2 . PHE A 1 770 ? 171.966 170.218 117.335 1.00 24.28  ? 680  PHE A CD2 1 
ATOM   5203 C  CE1 . PHE A 1 770 ? 171.860 167.628 118.258 1.00 21.63  ? 680  PHE A CE1 1 
ATOM   5204 C  CE2 . PHE A 1 770 ? 171.230 169.275 116.651 1.00 24.63  ? 680  PHE A CE2 1 
ATOM   5205 C  CZ  . PHE A 1 770 ? 171.177 167.979 117.113 1.00 24.37  ? 680  PHE A CZ  1 
ATOM   5206 N  N   . LYS A 1 771 ? 175.986 169.433 120.127 1.00 19.62  ? 681  LYS A N   1 
ATOM   5207 C  CA  . LYS A 1 771 ? 176.615 168.156 120.449 1.00 17.97  ? 681  LYS A CA  1 
ATOM   5208 C  C   . LYS A 1 771 ? 175.704 167.327 121.343 1.00 16.94  ? 681  LYS A C   1 
ATOM   5209 O  O   . LYS A 1 771 ? 174.921 167.881 122.113 1.00 16.41  ? 681  LYS A O   1 
ATOM   5210 C  CB  . LYS A 1 771 ? 177.953 168.381 121.147 1.00 17.57  ? 681  LYS A CB  1 
ATOM   5211 C  CG  . LYS A 1 771 ? 179.001 169.068 120.301 1.00 18.66  ? 681  LYS A CG  1 
ATOM   5212 C  CD  . LYS A 1 771 ? 180.295 169.234 121.072 1.00 17.99  ? 681  LYS A CD  1 
ATOM   5213 C  CE  . LYS A 1 771 ? 181.336 169.983 120.261 1.00 19.40  ? 681  LYS A CE  1 
ATOM   5214 N  NZ  . LYS A 1 771 ? 182.606 170.152 121.017 1.00 18.51  ? 681  LYS A NZ  1 
ATOM   5215 N  N   . PHE A 1 772 ? 175.830 166.002 121.280 1.00 16.05  ? 682  PHE A N   1 
ATOM   5216 C  CA  . PHE A 1 772 ? 175.036 165.164 122.174 1.00 14.56  ? 682  PHE A CA  1 
ATOM   5217 C  C   . PHE A 1 772 ? 175.765 163.899 122.623 1.00 13.82  ? 682  PHE A C   1 
ATOM   5218 O  O   . PHE A 1 772 ? 176.708 163.439 121.977 1.00 14.19  ? 682  PHE A O   1 
ATOM   5219 C  CB  . PHE A 1 772 ? 173.713 164.771 121.503 1.00 15.24  ? 682  PHE A CB  1 
ATOM   5220 C  CG  . PHE A 1 772 ? 173.834 163.694 120.448 1.00 15.75  ? 682  PHE A CG  1 
ATOM   5221 C  CD1 . PHE A 1 772 ? 173.606 162.367 120.783 1.00 15.50  ? 682  PHE A CD1 1 
ATOM   5222 C  CD2 . PHE A 1 772 ? 174.176 163.990 119.140 1.00 17.24  ? 682  PHE A CD2 1 
ATOM   5223 C  CE1 . PHE A 1 772 ? 173.715 161.369 119.842 1.00 16.54  ? 682  PHE A CE1 1 
ATOM   5224 C  CE2 . PHE A 1 772 ? 174.285 162.985 118.198 1.00 18.24  ? 682  PHE A CE2 1 
ATOM   5225 C  CZ  . PHE A 1 772 ? 174.054 161.676 118.551 1.00 18.60  ? 682  PHE A CZ  1 
ATOM   5226 N  N   . PHE A 1 773 ? 175.281 163.317 123.721 1.00 12.86  ? 683  PHE A N   1 
ATOM   5227 C  CA  . PHE A 1 773 ? 175.763 162.025 124.211 1.00 12.34  ? 683  PHE A CA  1 
ATOM   5228 C  C   . PHE A 1 773 ? 174.633 161.261 124.903 1.00 12.17  ? 683  PHE A C   1 
ATOM   5229 O  O   . PHE A 1 773 ? 173.592 161.830 125.224 1.00 12.11  ? 683  PHE A O   1 
ATOM   5230 C  CB  . PHE A 1 773 ? 176.965 162.186 125.154 1.00 11.43  ? 683  PHE A CB  1 
ATOM   5231 C  CG  . PHE A 1 773 ? 176.684 162.886 126.449 1.00 10.48  ? 683  PHE A CG  1 
ATOM   5232 C  CD1 . PHE A 1 773 ? 176.311 162.174 127.579 1.00 10.31  ? 683  PHE A CD1 1 
ATOM   5233 C  CD2 . PHE A 1 773 ? 176.814 164.253 126.547 1.00 10.19  ? 683  PHE A CD2 1 
ATOM   5234 C  CE1 . PHE A 1 773 ? 176.073 162.819 128.768 1.00 9.43   ? 683  PHE A CE1 1 
ATOM   5235 C  CE2 . PHE A 1 773 ? 176.576 164.896 127.735 1.00 8.94   ? 683  PHE A CE2 1 
ATOM   5236 C  CZ  . PHE A 1 773 ? 176.207 164.178 128.847 1.00 8.54   ? 683  PHE A CZ  1 
ATOM   5237 N  N   . VAL A 1 774 ? 174.826 159.961 125.090 1.00 11.76  ? 684  VAL A N   1 
ATOM   5238 C  CA  . VAL A 1 774 ? 173.783 159.101 125.646 1.00 12.12  ? 684  VAL A CA  1 
ATOM   5239 C  C   . VAL A 1 774 ? 174.226 158.391 126.922 1.00 12.12  ? 684  VAL A C   1 
ATOM   5240 O  O   . VAL A 1 774 ? 175.315 157.822 126.967 1.00 12.26  ? 684  VAL A O   1 
ATOM   5241 C  CB  . VAL A 1 774 ? 173.372 158.047 124.595 1.00 13.20  ? 684  VAL A CB  1 
ATOM   5242 C  CG1 . VAL A 1 774 ? 172.284 157.131 125.144 1.00 13.56  ? 684  VAL A CG1 1 
ATOM   5243 C  CG2 . VAL A 1 774 ? 172.900 158.749 123.332 1.00 14.07  ? 684  VAL A CG2 1 
ATOM   5244 N  N   . THR A 1 775 ? 173.368 158.402 127.941 1.00 11.88  ? 685  THR A N   1 
ATOM   5245 C  CA  . THR A 1 775 ? 173.633 157.688 129.190 1.00 11.71  ? 685  THR A CA  1 
ATOM   5246 C  C   . THR A 1 775 ? 172.674 156.515 129.373 1.00 11.98  ? 685  THR A C   1 
ATOM   5247 O  O   . THR A 1 775 ? 171.617 156.467 128.746 1.00 12.35  ? 685  THR A O   1 
ATOM   5248 C  CB  . THR A 1 775 ? 173.524 158.628 130.411 1.00 11.15  ? 685  THR A CB  1 
ATOM   5249 O  OG1 . THR A 1 775 ? 172.223 159.237 130.436 1.00 11.49  ? 685  THR A OG1 1 
ATOM   5250 C  CG2 . THR A 1 775 ? 174.592 159.700 130.361 1.00 10.61  ? 685  THR A CG2 1 
ATOM   5251 N  N   . SER A 1 776 ? 173.034 155.581 130.252 1.00 11.72  ? 686  SER A N   1 
ATOM   5252 C  CA  . SER A 1 776 ? 172.145 154.464 130.576 1.00 11.70  ? 686  SER A CA  1 
ATOM   5253 C  C   . SER A 1 776 ? 170.954 154.936 131.421 1.00 11.67  ? 686  SER A C   1 
ATOM   5254 O  O   . SER A 1 776 ? 171.129 155.751 132.324 1.00 11.47  ? 686  SER A O   1 
ATOM   5255 C  CB  . SER A 1 776 ? 172.901 153.387 131.326 1.00 11.40  ? 686  SER A CB  1 
ATOM   5256 O  OG  . SER A 1 776 ? 173.869 152.787 130.510 1.00 11.70  ? 686  SER A OG  1 
ATOM   5257 N  N   . PRO A 1 777 ? 169.741 154.422 131.180 1.00 12.04  ? 687  PRO A N   1 
ATOM   5258 C  CA  . PRO A 1 777 ? 168.518 154.743 131.899 1.00 11.91  ? 687  PRO A CA  1 
ATOM   5259 C  C   . PRO A 1 777 ? 168.649 154.654 133.422 1.00 11.44  ? 687  PRO A C   1 
ATOM   5260 O  O   . PRO A 1 777 ? 168.054 155.454 134.142 1.00 11.58  ? 687  PRO A O   1 
ATOM   5261 C  CB  . PRO A 1 777 ? 167.553 153.681 131.374 1.00 12.68  ? 687  PRO A CB  1 
ATOM   5262 C  CG  . PRO A 1 777 ? 168.035 153.395 129.987 1.00 13.75  ? 687  PRO A CG  1 
ATOM   5263 C  CD  . PRO A 1 777 ? 169.549 153.479 130.071 1.00 12.80  ? 687  PRO A CD  1 
ATOM   5264 N  N   . THR A 1 778 ? 169.427 153.692 133.914 1.00 11.32  ? 688  THR A N   1 
ATOM   5265 C  CA  . THR A 1 778 ? 169.553 153.501 135.358 1.00 10.82  ? 688  THR A CA  1 
ATOM   5266 C  C   . THR A 1 778 ? 170.948 153.870 135.913 1.00 10.31  ? 688  THR A C   1 
ATOM   5267 O  O   . THR A 1 778 ? 171.298 153.430 136.999 1.00 10.08  ? 688  THR A O   1 
ATOM   5268 C  CB  . THR A 1 778 ? 169.242 152.045 135.753 1.00 10.68  ? 688  THR A CB  1 
ATOM   5269 N  N   . ASN A 1 779 ? 171.730 154.604 135.108 1.00 10.60  ? 689  ASN A N   1 
ATOM   5270 C  CA  . ASN A 1 779 ? 173.081 155.005 135.516 1.00 10.09  ? 689  ASN A CA  1 
ATOM   5271 C  C   . ASN A 1 779 ? 173.510 156.258 134.804 1.00 10.24  ? 689  ASN A C   1 
ATOM   5272 O  O   . ASN A 1 779 ? 173.488 156.326 133.540 1.00 10.45  ? 689  ASN A O   1 
ATOM   5273 C  CB  . ASN A 1 779 ? 174.070 153.862 135.294 1.00 10.20  ? 689  ASN A CB  1 
ATOM   5274 C  CG  . ASN A 1 779 ? 175.408 154.076 136.013 1.00 10.21  ? 689  ASN A CG  1 
ATOM   5275 O  OD1 . ASN A 1 779 ? 175.805 155.207 136.314 1.00 9.45   ? 689  ASN A OD1 1 
ATOM   5276 N  ND2 . ASN A 1 779 ? 176.056 152.985 136.293 1.00 9.80   ? 689  ASN A ND2 1 
ATOM   5277 N  N   . VAL A 1 780 ? 173.833 157.311 135.559 1.00 9.44   ? 690  VAL A N   1 
ATOM   5278 C  CA  . VAL A 1 780 ? 174.167 158.625 135.027 1.00 9.46   ? 690  VAL A CA  1 
ATOM   5279 C  C   . VAL A 1 780 ? 175.678 158.808 134.902 1.00 9.39   ? 690  VAL A C   1 
ATOM   5280 O  O   . VAL A 1 780 ? 176.153 159.760 134.270 1.00 9.09   ? 690  VAL A O   1 
ATOM   5281 C  CB  . VAL A 1 780 ? 173.548 159.700 135.936 1.00 8.76   ? 690  VAL A CB  1 
ATOM   5282 C  CG1 . VAL A 1 780 ? 174.378 159.880 137.205 1.00 7.58   ? 690  VAL A CG1 1 
ATOM   5283 C  CG2 . VAL A 1 780 ? 173.428 160.984 135.170 1.00 8.41   ? 690  VAL A CG2 1 
ATOM   5284 N  N   . SER A 1 781 ? 176.435 157.895 135.511 1.00 9.34   ? 691  SER A N   1 
ATOM   5285 C  CA  . SER A 1 781 ? 177.897 157.916 135.422 1.00 9.44   ? 691  SER A CA  1 
ATOM   5286 C  C   . SER A 1 781 ? 178.346 157.020 134.280 1.00 10.01  ? 691  SER A C   1 
ATOM   5287 O  O   . SER A 1 781 ? 179.537 156.882 134.006 1.00 9.99   ? 691  SER A O   1 
ATOM   5288 C  CB  . SER A 1 781 ? 178.512 157.445 136.737 1.00 8.79   ? 691  SER A CB  1 
ATOM   5289 N  N   . ASP A 1 782 ? 177.374 156.383 133.628 1.00 10.25  ? 692  ASP A N   1 
ATOM   5290 C  CA  . ASP A 1 782 ? 177.640 155.452 132.544 1.00 10.58  ? 692  ASP A CA  1 
ATOM   5291 C  C   . ASP A 1 782 ? 177.298 156.063 131.192 1.00 11.01  ? 692  ASP A C   1 
ATOM   5292 O  O   . ASP A 1 782 ? 176.128 156.112 130.803 1.00 11.32  ? 692  ASP A O   1 
ATOM   5293 C  CB  . ASP A 1 782 ? 176.836 154.169 132.744 1.00 10.64  ? 692  ASP A CB  1 
ATOM   5294 C  CG  . ASP A 1 782 ? 177.150 153.086 131.730 1.00 11.23  ? 692  ASP A CG  1 
ATOM   5295 O  OD1 . ASP A 1 782 ? 177.853 153.362 130.787 1.00 11.84  ? 692  ASP A OD1 1 
ATOM   5296 O  OD2 . ASP A 1 782 ? 176.687 151.984 131.911 1.00 11.16  ? 692  ASP A OD2 1 
ATOM   5297 N  N   . ILE A 1 783 ? 178.312 156.545 130.493 1.00 11.30  ? 693  ILE A N   1 
ATOM   5298 C  CA  . ILE A 1 783 ? 178.102 157.188 129.205 1.00 11.77  ? 693  ILE A CA  1 
ATOM   5299 C  C   . ILE A 1 783 ? 178.384 156.195 128.090 1.00 12.84  ? 693  ILE A C   1 
ATOM   5300 O  O   . ILE A 1 783 ? 179.483 155.662 127.994 1.00 13.26  ? 693  ILE A O   1 
ATOM   5301 C  CB  . ILE A 1 783 ? 178.987 158.441 129.051 1.00 11.38  ? 693  ILE A CB  1 
ATOM   5302 C  CG1 . ILE A 1 783 ? 178.631 159.448 130.146 1.00 10.75  ? 693  ILE A CG1 1 
ATOM   5303 C  CG2 . ILE A 1 783 ? 178.803 159.057 127.680 1.00 11.41  ? 693  ILE A CG2 1 
ATOM   5304 C  CD1 . ILE A 1 783 ? 179.500 160.678 130.174 1.00 9.68   ? 693  ILE A CD1 1 
ATOM   5305 N  N   . ILE A 1 784 ? 177.378 155.944 127.258 1.00 13.21  ? 694  ILE A N   1 
ATOM   5306 C  CA  . ILE A 1 784 ? 177.524 154.942 126.217 1.00 14.42  ? 694  ILE A CA  1 
ATOM   5307 C  C   . ILE A 1 784 ? 178.677 155.350 125.310 1.00 15.17  ? 694  ILE A C   1 
ATOM   5308 O  O   . ILE A 1 784 ? 178.688 156.470 124.803 1.00 15.03  ? 694  ILE A O   1 
ATOM   5309 C  CB  . ILE A 1 784 ? 176.246 154.798 125.357 1.00 14.74  ? 694  ILE A CB  1 
ATOM   5310 C  CG1 . ILE A 1 784 ? 175.007 154.448 126.224 1.00 14.05  ? 694  ILE A CG1 1 
ATOM   5311 C  CG2 . ILE A 1 784 ? 176.471 153.728 124.285 1.00 16.65  ? 694  ILE A CG2 1 
ATOM   5312 C  CD1 . ILE A 1 784 ? 175.146 153.208 127.074 1.00 14.36  ? 694  ILE A CD1 1 
ATOM   5313 N  N   . PRO A 1 785 ? 179.644 154.465 125.073 1.00 16.24  ? 695  PRO A N   1 
ATOM   5314 C  CA  . PRO A 1 785 ? 180.811 154.677 124.246 1.00 16.51  ? 695  PRO A CA  1 
ATOM   5315 C  C   . PRO A 1 785 ? 180.407 155.272 122.910 1.00 17.59  ? 695  PRO A C   1 
ATOM   5316 O  O   . PRO A 1 785 ? 179.398 154.911 122.330 1.00 18.01  ? 695  PRO A O   1 
ATOM   5317 C  CB  . PRO A 1 785 ? 181.357 153.255 124.109 1.00 17.52  ? 695  PRO A CB  1 
ATOM   5318 C  CG  . PRO A 1 785 ? 180.961 152.585 125.402 1.00 17.35  ? 695  PRO A CG  1 
ATOM   5319 C  CD  . PRO A 1 785 ? 179.610 153.161 125.740 1.00 16.46  ? 695  PRO A CD  1 
ATOM   5320 N  N   . ARG A 1 786 ? 181.224 156.219 122.439 1.00 17.44  ? 696  ARG A N   1 
ATOM   5321 C  CA  . ARG A 1 786 ? 180.916 156.927 121.211 1.00 17.49  ? 696  ARG A CA  1 
ATOM   5322 C  C   . ARG A 1 786 ? 180.807 155.999 120.016 1.00 19.84  ? 696  ARG A C   1 
ATOM   5323 O  O   . ARG A 1 786 ? 180.015 156.252 119.101 1.00 19.14  ? 696  ARG A O   1 
ATOM   5324 C  CB  . ARG A 1 786 ? 181.971 157.977 120.932 1.00 16.56  ? 696  ARG A CB  1 
ATOM   5325 C  CG  . ARG A 1 786 ? 181.711 158.768 119.685 1.00 17.48  ? 696  ARG A CG  1 
ATOM   5326 C  CD  . ARG A 1 786 ? 182.539 159.962 119.604 1.00 16.37  ? 696  ARG A CD  1 
ATOM   5327 N  NE  . ARG A 1 786 ? 182.477 160.528 118.286 1.00 17.99  ? 696  ARG A NE  1 
ATOM   5328 C  CZ  . ARG A 1 786 ? 182.875 161.763 117.961 1.00 18.06  ? 696  ARG A CZ  1 
ATOM   5329 N  NH1 . ARG A 1 786 ? 183.366 162.560 118.881 1.00 16.73  ? 696  ARG A NH1 1 
ATOM   5330 N  NH2 . ARG A 1 786 ? 182.772 162.172 116.712 1.00 19.63  ? 696  ARG A NH2 1 
ATOM   5331 N  N   . SER A 1 787 ? 181.606 154.928 120.004 1.00 19.36  ? 697  SER A N   1 
ATOM   5332 C  CA  . SER A 1 787 ? 181.593 153.987 118.900 1.00 20.20  ? 697  SER A CA  1 
ATOM   5333 C  C   . SER A 1 787 ? 180.281 153.217 118.833 1.00 20.92  ? 697  SER A C   1 
ATOM   5334 O  O   . SER A 1 787 ? 179.797 152.898 117.748 1.00 21.71  ? 697  SER A O   1 
ATOM   5335 C  CB  . SER A 1 787 ? 182.750 153.011 119.038 1.00 20.23  ? 697  SER A CB  1 
ATOM   5336 N  N   . GLU A 1 788 ? 179.684 152.948 119.991 1.00 19.91  ? 698  GLU A N   1 
ATOM   5337 C  CA  . GLU A 1 788 ? 178.413 152.239 120.051 1.00 21.07  ? 698  GLU A CA  1 
ATOM   5338 C  C   . GLU A 1 788 ? 177.286 153.158 119.606 1.00 22.46  ? 698  GLU A C   1 
ATOM   5339 O  O   . GLU A 1 788 ? 176.326 152.720 118.965 1.00 20.88  ? 698  GLU A O   1 
ATOM   5340 C  CB  . GLU A 1 788 ? 178.157 151.701 121.460 1.00 20.08  ? 698  GLU A CB  1 
ATOM   5341 N  N   . VAL A 1 789 ? 177.412 154.438 119.925 1.00 20.04  ? 699  VAL A N   1 
ATOM   5342 C  CA  . VAL A 1 789 ? 176.419 155.413 119.524 1.00 20.54  ? 699  VAL A CA  1 
ATOM   5343 C  C   . VAL A 1 789 ? 176.491 155.653 118.015 1.00 22.38  ? 699  VAL A C   1 
ATOM   5344 O  O   . VAL A 1 789 ? 175.469 155.663 117.337 1.00 22.22  ? 699  VAL A O   1 
ATOM   5345 C  CB  . VAL A 1 789 ? 176.586 156.736 120.291 1.00 19.45  ? 699  VAL A CB  1 
ATOM   5346 C  CG1 . VAL A 1 789 ? 175.624 157.773 119.745 1.00 19.53  ? 699  VAL A CG1 1 
ATOM   5347 C  CG2 . VAL A 1 789 ? 176.330 156.495 121.767 1.00 18.12  ? 699  VAL A CG2 1 
ATOM   5348 N  N   . GLU A 1 790 ? 177.707 155.813 117.486 1.00 21.40  ? 700  GLU A N   1 
ATOM   5349 C  CA  . GLU A 1 790 ? 177.879 155.983 116.047 1.00 22.72  ? 700  GLU A CA  1 
ATOM   5350 C  C   . GLU A 1 790 ? 177.340 154.787 115.268 1.00 23.81  ? 700  GLU A C   1 
ATOM   5351 O  O   . GLU A 1 790 ? 176.708 154.958 114.224 1.00 24.12  ? 700  GLU A O   1 
ATOM   5352 C  CB  . GLU A 1 790 ? 179.355 156.203 115.677 1.00 22.29  ? 700  GLU A CB  1 
ATOM   5353 C  CG  . GLU A 1 790 ? 179.888 157.608 115.960 1.00 21.72  ? 700  GLU A CG  1 
ATOM   5354 C  CD  . GLU A 1 790 ? 181.376 157.694 115.802 1.00 21.64  ? 700  GLU A CD  1 
ATOM   5355 O  OE1 . GLU A 1 790 ? 181.983 156.701 115.457 1.00 21.95  ? 700  GLU A OE1 1 
ATOM   5356 O  OE2 . GLU A 1 790 ? 181.912 158.747 116.037 1.00 21.11  ? 700  GLU A OE2 1 
ATOM   5357 N  N   . ASP A 1 791 ? 177.552 153.570 115.784 1.00 23.32  ? 701  ASP A N   1 
ATOM   5358 C  CA  . ASP A 1 791 ? 177.011 152.392 115.117 1.00 24.01  ? 701  ASP A CA  1 
ATOM   5359 C  C   . ASP A 1 791 ? 175.487 152.416 115.114 1.00 24.72  ? 701  ASP A C   1 
ATOM   5360 O  O   . ASP A 1 791 ? 174.854 152.065 114.117 1.00 25.70  ? 701  ASP A O   1 
ATOM   5361 C  CB  . ASP A 1 791 ? 177.469 151.083 115.788 1.00 23.04  ? 701  ASP A CB  1 
ATOM   5362 C  CG  . ASP A 1 791 ? 178.945 150.746 115.580 1.00 23.69  ? 701  ASP A CG  1 
ATOM   5363 O  OD1 . ASP A 1 791 ? 179.578 151.360 114.755 1.00 24.04  ? 701  ASP A OD1 1 
ATOM   5364 O  OD2 . ASP A 1 791 ? 179.417 149.848 116.236 1.00 23.49  ? 701  ASP A OD2 1 
ATOM   5365 N  N   . ALA A 1 792 ? 174.895 152.856 116.228 1.00 23.70  ? 702  ALA A N   1 
ATOM   5366 C  CA  . ALA A 1 792 ? 173.440 152.931 116.317 1.00 24.07  ? 702  ALA A CA  1 
ATOM   5367 C  C   . ALA A 1 792 ? 172.881 153.932 115.320 1.00 25.14  ? 702  ALA A C   1 
ATOM   5368 O  O   . ALA A 1 792 ? 171.834 153.695 114.710 1.00 25.65  ? 702  ALA A O   1 
ATOM   5369 C  CB  . ALA A 1 792 ? 173.015 153.317 117.730 1.00 22.26  ? 702  ALA A CB  1 
ATOM   5370 N  N   . ILE A 1 793 ? 173.582 155.048 115.141 1.00 24.83  ? 703  ILE A N   1 
ATOM   5371 C  CA  . ILE A 1 793 ? 173.128 156.082 114.223 1.00 25.91  ? 703  ILE A CA  1 
ATOM   5372 C  C   . ILE A 1 793 ? 173.138 155.587 112.786 1.00 25.83  ? 703  ILE A C   1 
ATOM   5373 O  O   . ILE A 1 793 ? 172.184 155.817 112.047 1.00 27.58  ? 703  ILE A O   1 
ATOM   5374 C  CB  . ILE A 1 793 ? 173.978 157.366 114.348 1.00 24.67  ? 703  ILE A CB  1 
ATOM   5375 C  CG1 . ILE A 1 793 ? 173.800 158.010 115.759 1.00 24.26  ? 703  ILE A CG1 1 
ATOM   5376 C  CG2 . ILE A 1 793 ? 173.612 158.365 113.239 1.00 26.55  ? 703  ILE A CG2 1 
ATOM   5377 C  CD1 . ILE A 1 793 ? 172.405 158.540 116.066 1.00 23.59  ? 703  ILE A CD1 1 
ATOM   5378 N  N   . ARG A 1 794 ? 174.202 154.898 112.383 1.00 26.77  ? 704  ARG A N   1 
ATOM   5379 C  CA  . ARG A 1 794 ? 174.267 154.389 111.014 1.00 27.34  ? 704  ARG A CA  1 
ATOM   5380 C  C   . ARG A 1 794 ? 173.156 153.379 110.752 1.00 27.75  ? 704  ARG A C   1 
ATOM   5381 O  O   . ARG A 1 794 ? 172.489 153.435 109.716 1.00 28.55  ? 704  ARG A O   1 
ATOM   5382 C  CB  . ARG A 1 794 ? 175.611 153.741 110.727 1.00 25.45  ? 704  ARG A CB  1 
ATOM   5383 C  CG  . ARG A 1 794 ? 176.773 154.699 110.635 1.00 26.10  ? 704  ARG A CG  1 
ATOM   5384 C  CD  . ARG A 1 794 ? 177.964 154.063 110.014 1.00 26.03  ? 704  ARG A CD  1 
ATOM   5385 N  NE  . ARG A 1 794 ? 178.453 152.935 110.786 1.00 25.47  ? 704  ARG A NE  1 
ATOM   5386 C  CZ  . ARG A 1 794 ? 179.339 153.013 111.799 1.00 25.37  ? 704  ARG A CZ  1 
ATOM   5387 N  NH1 . ARG A 1 794 ? 179.829 154.175 112.176 1.00 24.87  ? 704  ARG A NH1 1 
ATOM   5388 N  NH2 . ARG A 1 794 ? 179.717 151.915 112.417 1.00 25.02  ? 704  ARG A NH2 1 
ATOM   5389 N  N   . MET A 1 795 ? 172.925 152.485 111.708 1.00 27.15  ? 705  MET A N   1 
ATOM   5390 C  CA  . MET A 1 795 ? 171.919 151.437 111.562 1.00 26.31  ? 705  MET A CA  1 
ATOM   5391 C  C   . MET A 1 795 ? 170.532 152.010 111.303 1.00 27.39  ? 705  MET A C   1 
ATOM   5392 O  O   . MET A 1 795 ? 169.774 151.480 110.488 1.00 28.73  ? 705  MET A O   1 
ATOM   5393 C  CB  . MET A 1 795 ? 171.898 150.566 112.814 1.00 26.74  ? 705  MET A CB  1 
ATOM   5394 C  CG  . MET A 1 795 ? 170.962 149.366 112.742 1.00 27.10  ? 705  MET A CG  1 
ATOM   5395 S  SD  . MET A 1 795 ? 170.957 148.399 114.264 1.00 26.99  ? 705  MET A SD  1 
ATOM   5396 C  CE  . MET A 1 795 ? 172.523 147.549 114.153 1.00 27.29  ? 705  MET A CE  1 
ATOM   5397 N  N   . SER A 1 796 ? 170.198 153.089 112.000 1.00 27.70  ? 706  SER A N   1 
ATOM   5398 C  CA  . SER A 1 796 ? 168.889 153.716 111.880 1.00 28.15  ? 706  SER A CA  1 
ATOM   5399 C  C   . SER A 1 796 ? 168.966 155.060 111.171 1.00 29.32  ? 706  SER A C   1 
ATOM   5400 O  O   . SER A 1 796 ? 168.048 155.873 111.273 1.00 30.13  ? 706  SER A O   1 
ATOM   5401 C  CB  . SER A 1 796 ? 168.273 153.906 113.251 1.00 27.30  ? 706  SER A CB  1 
ATOM   5402 N  N   . ARG A 1 797 ? 170.061 155.298 110.456 1.00 29.24  ? 707  ARG A N   1 
ATOM   5403 C  CA  . ARG A 1 797 ? 170.283 156.583 109.813 1.00 30.24  ? 707  ARG A CA  1 
ATOM   5404 C  C   . ARG A 1 797 ? 169.162 156.909 108.837 1.00 31.63  ? 707  ARG A C   1 
ATOM   5405 O  O   . ARG A 1 797 ? 168.723 158.053 108.744 1.00 32.18  ? 707  ARG A O   1 
ATOM   5406 C  CB  . ARG A 1 797 ? 171.617 156.593 109.086 1.00 29.95  ? 707  ARG A CB  1 
ATOM   5407 C  CG  . ARG A 1 797 ? 171.997 157.898 108.419 1.00 31.09  ? 707  ARG A CG  1 
ATOM   5408 C  CD  . ARG A 1 797 ? 172.365 158.936 109.420 1.00 31.17  ? 707  ARG A CD  1 
ATOM   5409 N  NE  . ARG A 1 797 ? 172.878 160.134 108.786 1.00 31.46  ? 707  ARG A NE  1 
ATOM   5410 C  CZ  . ARG A 1 797 ? 174.150 160.299 108.365 1.00 32.43  ? 707  ARG A CZ  1 
ATOM   5411 N  NH1 . ARG A 1 797 ? 175.030 159.330 108.512 1.00 31.68  ? 707  ARG A NH1 1 
ATOM   5412 N  NH2 . ARG A 1 797 ? 174.523 161.435 107.799 1.00 32.34  ? 707  ARG A NH2 1 
ATOM   5413 N  N   . GLY A 1 798 ? 168.696 155.894 108.114 1.00 31.53  ? 708  GLY A N   1 
ATOM   5414 C  CA  . GLY A 1 798 ? 167.640 156.081 107.128 1.00 31.90  ? 708  GLY A CA  1 
ATOM   5415 C  C   . GLY A 1 798 ? 166.343 156.569 107.764 1.00 32.57  ? 708  GLY A C   1 
ATOM   5416 O  O   . GLY A 1 798 ? 165.613 157.361 107.168 1.00 33.04  ? 708  GLY A O   1 
ATOM   5417 N  N   . ARG A 1 799 ? 166.051 156.088 108.970 1.00 31.90  ? 709  ARG A N   1 
ATOM   5418 C  CA  . ARG A 1 799 ? 164.815 156.463 109.645 1.00 32.83  ? 709  ARG A CA  1 
ATOM   5419 C  C   . ARG A 1 799 ? 164.938 157.853 110.251 1.00 32.57  ? 709  ARG A C   1 
ATOM   5420 O  O   . ARG A 1 799 ? 163.985 158.636 110.233 1.00 32.64  ? 709  ARG A O   1 
ATOM   5421 C  CB  . ARG A 1 799 ? 164.470 155.450 110.725 1.00 30.40  ? 709  ARG A CB  1 
ATOM   5422 C  CG  . ARG A 1 799 ? 164.131 154.049 110.208 1.00 30.75  ? 709  ARG A CG  1 
ATOM   5423 C  CD  . ARG A 1 799 ? 162.806 154.001 109.517 1.00 31.63  ? 709  ARG A CD  1 
ATOM   5424 N  NE  . ARG A 1 799 ? 161.716 154.358 110.412 1.00 30.85  ? 709  ARG A NE  1 
ATOM   5425 C  CZ  . ARG A 1 799 ? 161.100 153.504 111.252 1.00 29.48  ? 709  ARG A CZ  1 
ATOM   5426 N  NH1 . ARG A 1 799 ? 161.470 152.242 111.304 1.00 29.24  ? 709  ARG A NH1 1 
ATOM   5427 N  NH2 . ARG A 1 799 ? 160.121 153.934 112.027 1.00 28.98  ? 709  ARG A NH2 1 
ATOM   5428 N  N   . ILE A 1 800 ? 166.131 158.175 110.740 1.00 32.26  ? 710  ILE A N   1 
ATOM   5429 C  CA  . ILE A 1 800 ? 166.401 159.499 111.281 1.00 32.55  ? 710  ILE A CA  1 
ATOM   5430 C  C   . ILE A 1 800 ? 166.264 160.525 110.166 1.00 32.39  ? 710  ILE A C   1 
ATOM   5431 O  O   . ILE A 1 800 ? 165.687 161.596 110.355 1.00 33.74  ? 710  ILE A O   1 
ATOM   5432 C  CB  . ILE A 1 800 ? 167.812 159.570 111.901 1.00 31.90  ? 710  ILE A CB  1 
ATOM   5433 C  CG1 . ILE A 1 800 ? 167.888 158.666 113.151 1.00 29.44  ? 710  ILE A CG1 1 
ATOM   5434 C  CG2 . ILE A 1 800 ? 168.141 161.017 112.267 1.00 31.14  ? 710  ILE A CG2 1 
ATOM   5435 C  CD1 . ILE A 1 800 ? 169.303 158.384 113.636 1.00 27.99  ? 710  ILE A CD1 1 
ATOM   5436 N  N   . ASN A 1 801 ? 166.788 160.182 108.993 1.00 33.21  ? 711  ASN A N   1 
ATOM   5437 C  CA  . ASN A 1 801 ? 166.693 161.037 107.820 1.00 34.19  ? 711  ASN A CA  1 
ATOM   5438 C  C   . ASN A 1 801 ? 165.243 161.346 107.471 1.00 34.98  ? 711  ASN A C   1 
ATOM   5439 O  O   . ASN A 1 801 ? 164.865 162.509 107.320 1.00 34.45  ? 711  ASN A O   1 
ATOM   5440 C  CB  . ASN A 1 801 ? 167.366 160.380 106.631 1.00 34.07  ? 711  ASN A CB  1 
ATOM   5441 C  CG  . ASN A 1 801 ? 168.859 160.436 106.673 1.00 33.19  ? 711  ASN A CG  1 
ATOM   5442 O  OD1 . ASN A 1 801 ? 169.454 161.163 107.472 1.00 32.73  ? 711  ASN A OD1 1 
ATOM   5443 N  ND2 . ASN A 1 801 ? 169.480 159.680 105.807 1.00 33.35  ? 711  ASN A ND2 1 
ATOM   5444 N  N   . ASP A 1 802 ? 164.418 160.304 107.358 1.00 33.73  ? 712  ASP A N   1 
ATOM   5445 C  CA  . ASP A 1 802 ? 163.025 160.494 106.968 1.00 34.79  ? 712  ASP A CA  1 
ATOM   5446 C  C   . ASP A 1 802 ? 162.278 161.370 107.963 1.00 34.33  ? 712  ASP A C   1 
ATOM   5447 O  O   . ASP A 1 802 ? 161.465 162.209 107.576 1.00 35.08  ? 712  ASP A O   1 
ATOM   5448 C  CB  . ASP A 1 802 ? 162.308 159.148 106.840 1.00 34.47  ? 712  ASP A CB  1 
ATOM   5449 N  N   . ALA A 1 803 ? 162.588 161.207 109.244 1.00 33.90  ? 713  ALA A N   1 
ATOM   5450 C  CA  . ALA A 1 803 ? 161.904 161.936 110.307 1.00 34.25  ? 713  ALA A CA  1 
ATOM   5451 C  C   . ALA A 1 803 ? 161.981 163.448 110.114 1.00 34.31  ? 713  ALA A C   1 
ATOM   5452 O  O   . ALA A 1 803 ? 161.068 164.173 110.511 1.00 34.02  ? 713  ALA A O   1 
ATOM   5453 C  CB  . ALA A 1 803 ? 162.500 161.566 111.657 1.00 33.61  ? 713  ALA A CB  1 
ATOM   5454 N  N   . PHE A 1 804 ? 163.082 163.929 109.544 1.00 34.19  ? 714  PHE A N   1 
ATOM   5455 C  CA  . PHE A 1 804 ? 163.283 165.362 109.373 1.00 34.31  ? 714  PHE A CA  1 
ATOM   5456 C  C   . PHE A 1 804 ? 163.308 165.773 107.907 1.00 36.50  ? 714  PHE A C   1 
ATOM   5457 O  O   . PHE A 1 804 ? 163.630 166.916 107.584 1.00 35.86  ? 714  PHE A O   1 
ATOM   5458 C  CB  . PHE A 1 804 ? 164.583 165.788 110.048 1.00 34.22  ? 714  PHE A CB  1 
ATOM   5459 C  CG  . PHE A 1 804 ? 164.553 165.632 111.528 1.00 33.40  ? 714  PHE A CG  1 
ATOM   5460 C  CD1 . PHE A 1 804 ? 165.101 164.515 112.134 1.00 32.97  ? 714  PHE A CD1 1 
ATOM   5461 C  CD2 . PHE A 1 804 ? 163.970 166.603 112.322 1.00 31.91  ? 714  PHE A CD2 1 
ATOM   5462 C  CE1 . PHE A 1 804 ? 165.062 164.375 113.503 1.00 30.16  ? 714  PHE A CE1 1 
ATOM   5463 C  CE2 . PHE A 1 804 ? 163.934 166.465 113.686 1.00 31.19  ? 714  PHE A CE2 1 
ATOM   5464 C  CZ  . PHE A 1 804 ? 164.478 165.352 114.274 1.00 29.18  ? 714  PHE A CZ  1 
ATOM   5465 N  N   . ARG A 1 805 ? 162.997 164.831 107.022 1.00 35.40  ? 715  ARG A N   1 
ATOM   5466 C  CA  . ARG A 1 805 ? 163.082 165.055 105.581 1.00 36.32  ? 715  ARG A CA  1 
ATOM   5467 C  C   . ARG A 1 805 ? 164.467 165.548 105.160 1.00 36.26  ? 715  ARG A C   1 
ATOM   5468 O  O   . ARG A 1 805 ? 164.584 166.449 104.328 1.00 37.42  ? 715  ARG A O   1 
ATOM   5469 C  CB  . ARG A 1 805 ? 162.041 166.071 105.135 1.00 37.94  ? 715  ARG A CB  1 
ATOM   5470 C  CG  . ARG A 1 805 ? 160.609 165.695 105.434 1.00 38.34  ? 715  ARG A CG  1 
ATOM   5471 C  CD  . ARG A 1 805 ? 159.665 166.725 104.946 1.00 39.83  ? 715  ARG A CD  1 
ATOM   5472 N  NE  . ARG A 1 805 ? 158.289 166.394 105.273 1.00 41.97  ? 715  ARG A NE  1 
ATOM   5473 C  CZ  . ARG A 1 805 ? 157.232 167.201 105.059 1.00 40.30  ? 715  ARG A CZ  1 
ATOM   5474 N  NH1 . ARG A 1 805 ? 157.405 168.388 104.518 1.00 41.46  ? 715  ARG A NH1 1 
ATOM   5475 N  NH2 . ARG A 1 805 ? 156.019 166.799 105.397 1.00 41.61  ? 715  ARG A NH2 1 
ATOM   5476 N  N   . LEU A 1 806 ? 165.514 164.956 105.729 1.00 36.09  ? 716  LEU A N   1 
ATOM   5477 C  CA  . LEU A 1 806 ? 166.883 165.352 105.407 1.00 35.58  ? 716  LEU A CA  1 
ATOM   5478 C  C   . LEU A 1 806 ? 167.661 164.216 104.761 1.00 34.93  ? 716  LEU A C   1 
ATOM   5479 O  O   . LEU A 1 806 ? 167.435 163.046 105.062 1.00 34.02  ? 716  LEU A O   1 
ATOM   5480 C  CB  . LEU A 1 806 ? 167.612 165.814 106.675 1.00 35.47  ? 716  LEU A CB  1 
ATOM   5481 C  CG  . LEU A 1 806 ? 166.969 166.988 107.433 1.00 35.51  ? 716  LEU A CG  1 
ATOM   5482 C  CD1 . LEU A 1 806 ? 167.733 167.234 108.724 1.00 34.91  ? 716  LEU A CD1 1 
ATOM   5483 C  CD2 . LEU A 1 806 ? 166.969 168.234 106.555 1.00 36.56  ? 716  LEU A CD2 1 
ATOM   5484 N  N   . ASP A 1 807 ? 168.593 164.566 103.882 1.00 36.18  ? 717  ASP A N   1 
ATOM   5485 C  CA  . ASP A 1 807 ? 169.486 163.584 103.278 1.00 35.42  ? 717  ASP A CA  1 
ATOM   5486 C  C   . ASP A 1 807 ? 170.813 163.536 104.033 1.00 35.59  ? 717  ASP A C   1 
ATOM   5487 O  O   . ASP A 1 807 ? 170.953 164.147 105.095 1.00 45.72  ? 717  ASP A O   1 
ATOM   5488 C  CB  . ASP A 1 807 ? 169.691 163.883 101.788 1.00 36.69  ? 717  ASP A CB  1 
ATOM   5489 N  N   . ASP A 1 808 ? 171.781 162.792 103.501 1.00 33.80  ? 718  ASP A N   1 
ATOM   5490 C  CA  . ASP A 1 808 ? 173.039 162.550 104.206 1.00 35.60  ? 718  ASP A CA  1 
ATOM   5491 C  C   . ASP A 1 808 ? 174.040 163.688 104.040 1.00 35.21  ? 718  ASP A C   1 
ATOM   5492 O  O   . ASP A 1 808 ? 175.173 163.602 104.515 1.00 35.11  ? 718  ASP A O   1 
ATOM   5493 C  CB  . ASP A 1 808 ? 173.673 161.242 103.730 1.00 35.02  ? 718  ASP A CB  1 
ATOM   5494 N  N   . LYS A 1 809 ? 173.625 164.750 103.361 1.00 36.00  ? 719  LYS A N   1 
ATOM   5495 C  CA  . LYS A 1 809 ? 174.469 165.924 103.191 1.00 35.61  ? 719  LYS A CA  1 
ATOM   5496 C  C   . LYS A 1 809 ? 173.950 167.073 104.043 1.00 34.98  ? 719  LYS A C   1 
ATOM   5497 O  O   . LYS A 1 809 ? 174.724 167.893 104.537 1.00 35.54  ? 719  LYS A O   1 
ATOM   5498 C  CB  . LYS A 1 809 ? 174.521 166.340 101.720 1.00 36.73  ? 719  LYS A CB  1 
ATOM   5499 N  N   . THR A 1 810 ? 172.635 167.121 104.229 1.00 35.18  ? 720  THR A N   1 
ATOM   5500 C  CA  . THR A 1 810 ? 172.012 168.178 105.008 1.00 35.35  ? 720  THR A CA  1 
ATOM   5501 C  C   . THR A 1 810 ? 171.874 167.792 106.479 1.00 34.25  ? 720  THR A C   1 
ATOM   5502 O  O   . THR A 1 810 ? 171.714 168.658 107.339 1.00 35.53  ? 720  THR A O   1 
ATOM   5503 C  CB  . THR A 1 810 ? 170.650 168.563 104.412 1.00 36.57  ? 720  THR A CB  1 
ATOM   5504 N  N   . LEU A 1 811 ? 171.993 166.498 106.775 1.00 34.79  ? 721  LEU A N   1 
ATOM   5505 C  CA  . LEU A 1 811 ? 172.079 166.031 108.155 1.00 33.19  ? 721  LEU A CA  1 
ATOM   5506 C  C   . LEU A 1 811 ? 173.404 165.332 108.373 1.00 32.49  ? 721  LEU A C   1 
ATOM   5507 O  O   . LEU A 1 811 ? 173.568 164.159 108.020 1.00 32.01  ? 721  LEU A O   1 
ATOM   5508 C  CB  . LEU A 1 811 ? 170.925 165.081 108.484 1.00 33.12  ? 721  LEU A CB  1 
ATOM   5509 C  CG  . LEU A 1 811 ? 170.984 164.403 109.867 1.00 32.91  ? 721  LEU A CG  1 
ATOM   5510 C  CD1 . LEU A 1 811 ? 170.979 165.444 110.964 1.00 31.89  ? 721  LEU A CD1 1 
ATOM   5511 C  CD2 . LEU A 1 811 ? 169.796 163.481 110.014 1.00 33.25  ? 721  LEU A CD2 1 
ATOM   5512 N  N   . GLU A 1 812 ? 174.364 166.060 108.933 1.00 31.82  ? 722  GLU A N   1 
ATOM   5513 C  CA  . GLU A 1 812 ? 175.716 165.547 109.065 1.00 31.11  ? 722  GLU A CA  1 
ATOM   5514 C  C   . GLU A 1 812 ? 176.047 165.174 110.498 1.00 28.92  ? 722  GLU A C   1 
ATOM   5515 O  O   . GLU A 1 812 ? 175.931 165.989 111.417 1.00 28.37  ? 722  GLU A O   1 
ATOM   5516 C  CB  . GLU A 1 812 ? 176.723 166.590 108.564 1.00 29.31  ? 722  GLU A CB  1 
ATOM   5517 N  N   . PHE A 1 813 ? 176.527 163.953 110.674 1.00 28.39  ? 723  PHE A N   1 
ATOM   5518 C  CA  . PHE A 1 813 ? 177.048 163.531 111.963 1.00 26.79  ? 723  PHE A CA  1 
ATOM   5519 C  C   . PHE A 1 813 ? 178.561 163.460 111.870 1.00 26.52  ? 723  PHE A C   1 
ATOM   5520 O  O   . PHE A 1 813 ? 179.112 162.585 111.194 1.00 27.49  ? 723  PHE A O   1 
ATOM   5521 C  CB  . PHE A 1 813 ? 176.491 162.172 112.380 1.00 26.27  ? 723  PHE A CB  1 
ATOM   5522 C  CG  . PHE A 1 813 ? 175.047 162.173 112.764 1.00 27.10  ? 723  PHE A CG  1 
ATOM   5523 C  CD1 . PHE A 1 813 ? 174.690 162.218 114.096 1.00 25.96  ? 723  PHE A CD1 1 
ATOM   5524 C  CD2 . PHE A 1 813 ? 174.041 162.125 111.809 1.00 29.18  ? 723  PHE A CD2 1 
ATOM   5525 C  CE1 . PHE A 1 813 ? 173.367 162.213 114.477 1.00 25.37  ? 723  PHE A CE1 1 
ATOM   5526 C  CE2 . PHE A 1 813 ? 172.712 162.120 112.192 1.00 29.09  ? 723  PHE A CE2 1 
ATOM   5527 C  CZ  . PHE A 1 813 ? 172.378 162.166 113.528 1.00 27.51  ? 723  PHE A CZ  1 
ATOM   5528 N  N   . LEU A 1 814 ? 179.238 164.410 112.511 1.00 26.23  ? 724  LEU A N   1 
ATOM   5529 C  CA  . LEU A 1 814 ? 180.679 164.496 112.359 1.00 25.25  ? 724  LEU A CA  1 
ATOM   5530 C  C   . LEU A 1 814 ? 181.322 163.227 112.884 1.00 25.84  ? 724  LEU A C   1 
ATOM   5531 O  O   . LEU A 1 814 ? 181.010 162.775 113.982 1.00 24.80  ? 724  LEU A O   1 
ATOM   5532 C  CB  . LEU A 1 814 ? 181.227 165.716 113.110 1.00 25.29  ? 724  LEU A CB  1 
ATOM   5533 C  CG  . LEU A 1 814 ? 181.236 167.040 112.324 1.00 26.16  ? 724  LEU A CG  1 
ATOM   5534 C  CD1 . LEU A 1 814 ? 179.818 167.623 112.260 1.00 25.97  ? 724  LEU A CD1 1 
ATOM   5535 C  CD2 . LEU A 1 814 ? 182.193 168.003 113.004 1.00 25.38  ? 724  LEU A CD2 1 
ATOM   5536 N  N   . GLY A 1 815 ? 182.204 162.639 112.083 1.00 25.68  ? 725  GLY A N   1 
ATOM   5537 C  CA  . GLY A 1 815 ? 182.837 161.371 112.437 1.00 25.73  ? 725  GLY A CA  1 
ATOM   5538 C  C   . GLY A 1 815 ? 182.261 160.154 111.703 1.00 25.57  ? 725  GLY A C   1 
ATOM   5539 O  O   . GLY A 1 815 ? 182.876 159.084 111.695 1.00 25.24  ? 725  GLY A O   1 
ATOM   5540 N  N   . ILE A 1 816 ? 181.082 160.313 111.073 1.00 26.28  ? 726  ILE A N   1 
ATOM   5541 C  CA  . ILE A 1 816 ? 180.413 159.237 110.340 1.00 25.93  ? 726  ILE A CA  1 
ATOM   5542 C  C   . ILE A 1 816 ? 180.469 159.535 108.839 1.00 26.35  ? 726  ILE A C   1 
ATOM   5543 O  O   . ILE A 1 816 ? 179.608 160.226 108.285 1.00 26.61  ? 726  ILE A O   1 
ATOM   5544 C  CB  . ILE A 1 816 ? 178.936 159.053 110.832 1.00 26.92  ? 726  ILE A CB  1 
ATOM   5545 N  N   . LEU B 2 61  ? 242.005 182.448 177.260 1.00 65.61  ? 389  LEU B N   1 
ATOM   5546 C  CA  . LEU B 2 61  ? 241.391 183.262 176.222 1.00 63.46  ? 389  LEU B CA  1 
ATOM   5547 C  C   . LEU B 2 61  ? 242.409 183.613 175.142 1.00 64.78  ? 389  LEU B C   1 
ATOM   5548 O  O   . LEU B 2 61  ? 242.069 184.224 174.132 1.00 62.91  ? 389  LEU B O   1 
ATOM   5549 C  CB  . LEU B 2 61  ? 240.842 184.569 176.817 1.00 64.69  ? 389  LEU B CB  1 
ATOM   5550 C  CG  . LEU B 2 61  ? 239.778 184.445 177.930 1.00 62.56  ? 389  LEU B CG  1 
ATOM   5551 C  CD1 . LEU B 2 61  ? 239.419 185.842 178.426 1.00 63.61  ? 389  LEU B CD1 1 
ATOM   5552 C  CD2 . LEU B 2 61  ? 238.549 183.732 177.401 1.00 57.79  ? 389  LEU B CD2 1 
ATOM   5553 N  N   . PHE B 2 62  ? 243.670 183.260 175.387 1.00 65.19  ? 390  PHE B N   1 
ATOM   5554 C  CA  . PHE B 2 62  ? 244.758 183.621 174.488 1.00 64.83  ? 390  PHE B CA  1 
ATOM   5555 C  C   . PHE B 2 62  ? 245.427 182.406 173.862 1.00 65.09  ? 390  PHE B C   1 
ATOM   5556 O  O   . PHE B 2 62  ? 246.546 182.506 173.363 1.00 64.52  ? 390  PHE B O   1 
ATOM   5557 C  CB  . PHE B 2 62  ? 245.821 184.420 175.246 1.00 65.06  ? 390  PHE B CB  1 
ATOM   5558 N  N   . ARG B 2 63  ? 244.763 181.257 173.896 1.00 64.69  ? 391  ARG B N   1 
ATOM   5559 C  CA  . ARG B 2 63  ? 245.366 180.040 173.364 1.00 64.04  ? 391  ARG B CA  1 
ATOM   5560 C  C   . ARG B 2 63  ? 244.556 179.449 172.220 1.00 61.84  ? 391  ARG B C   1 
ATOM   5561 O  O   . ARG B 2 63  ? 243.330 179.547 172.194 1.00 62.73  ? 391  ARG B O   1 
ATOM   5562 C  CB  . ARG B 2 63  ? 245.526 178.996 174.458 1.00 64.50  ? 391  ARG B CB  1 
ATOM   5563 N  N   . GLY B 2 64  ? 245.258 178.827 171.277 1.00 61.88  ? 392  GLY B N   1 
ATOM   5564 C  CA  . GLY B 2 64  ? 244.621 178.194 170.128 1.00 59.11  ? 392  GLY B CA  1 
ATOM   5565 C  C   . GLY B 2 64  ? 244.097 179.245 169.155 1.00 57.79  ? 392  GLY B C   1 
ATOM   5566 O  O   . GLY B 2 64  ? 244.356 180.436 169.329 1.00 58.35  ? 392  GLY B O   1 
ATOM   5567 N  N   . PRO B 2 65  ? 243.397 178.806 168.106 1.00 57.25  ? 393  PRO B N   1 
ATOM   5568 C  CA  . PRO B 2 65  ? 242.690 179.604 167.120 1.00 55.52  ? 393  PRO B CA  1 
ATOM   5569 C  C   . PRO B 2 65  ? 241.566 180.377 167.786 1.00 53.22  ? 393  PRO B C   1 
ATOM   5570 O  O   . PRO B 2 65  ? 241.005 179.923 168.782 1.00 53.08  ? 393  PRO B O   1 
ATOM   5571 C  CB  . PRO B 2 65  ? 242.137 178.539 166.160 1.00 55.66  ? 393  PRO B CB  1 
ATOM   5572 C  CG  . PRO B 2 65  ? 243.000 177.315 166.395 1.00 57.34  ? 393  PRO B CG  1 
ATOM   5573 C  CD  . PRO B 2 65  ? 243.341 177.367 167.861 1.00 56.07  ? 393  PRO B CD  1 
ATOM   5574 N  N   . VAL B 2 66  ? 241.218 181.531 167.232 1.00 52.23  ? 394  VAL B N   1 
ATOM   5575 C  CA  . VAL B 2 66  ? 240.116 182.309 167.776 1.00 50.32  ? 394  VAL B CA  1 
ATOM   5576 C  C   . VAL B 2 66  ? 238.789 181.800 167.210 1.00 47.95  ? 394  VAL B C   1 
ATOM   5577 O  O   . VAL B 2 66  ? 238.643 181.714 165.985 1.00 48.08  ? 394  VAL B O   1 
ATOM   5578 C  CB  . VAL B 2 66  ? 240.274 183.801 167.438 1.00 49.39  ? 394  VAL B CB  1 
ATOM   5579 C  CG1 . VAL B 2 66  ? 239.125 184.589 168.048 1.00 49.16  ? 394  VAL B CG1 1 
ATOM   5580 C  CG2 . VAL B 2 66  ? 241.606 184.313 167.949 1.00 52.48  ? 394  VAL B CG2 1 
ATOM   5581 N  N   . PRO B 2 67  ? 237.821 181.443 168.064 1.00 46.51  ? 395  PRO B N   1 
ATOM   5582 C  CA  . PRO B 2 67  ? 236.483 180.995 167.729 1.00 44.90  ? 395  PRO B CA  1 
ATOM   5583 C  C   . PRO B 2 67  ? 235.770 182.012 166.856 1.00 42.80  ? 395  PRO B C   1 
ATOM   5584 O  O   . PRO B 2 67  ? 235.988 183.212 167.005 1.00 45.64  ? 395  PRO B O   1 
ATOM   5585 C  CB  . PRO B 2 67  ? 235.816 180.883 169.103 1.00 44.91  ? 395  PRO B CB  1 
ATOM   5586 C  CG  . PRO B 2 67  ? 236.951 180.638 170.058 1.00 47.50  ? 395  PRO B CG  1 
ATOM   5587 C  CD  . PRO B 2 67  ? 238.111 181.428 169.501 1.00 48.62  ? 395  PRO B CD  1 
ATOM   5588 N  N   . GLN B 2 68  ? 234.927 181.534 165.956 1.00 44.05  ? 396  GLN B N   1 
ATOM   5589 C  CA  . GLN B 2 68  ? 234.150 182.399 165.072 1.00 42.48  ? 396  GLN B CA  1 
ATOM   5590 C  C   . GLN B 2 68  ? 232.770 182.644 165.696 1.00 36.65  ? 396  GLN B C   1 
ATOM   5591 O  O   . GLN B 2 68  ? 232.377 181.908 166.598 1.00 39.52  ? 396  GLN B O   1 
ATOM   5592 C  CB  . GLN B 2 68  ? 234.060 181.749 163.689 1.00 40.04  ? 396  GLN B CB  1 
ATOM   5593 C  CG  . GLN B 2 68  ? 235.409 181.483 163.049 1.00 40.00  ? 396  GLN B CG  1 
ATOM   5594 C  CD  . GLN B 2 68  ? 236.192 182.752 162.788 1.00 40.99  ? 396  GLN B CD  1 
ATOM   5595 O  OE1 . GLN B 2 68  ? 235.802 183.590 161.964 1.00 40.19  ? 396  GLN B OE1 1 
ATOM   5596 N  NE2 . GLN B 2 68  ? 237.307 182.913 163.497 1.00 43.75  ? 396  GLN B NE2 1 
ATOM   5597 N  N   . PRO B 2 69  ? 232.025 183.670 165.261 1.00 41.29  ? 397  PRO B N   1 
ATOM   5598 C  CA  . PRO B 2 69  ? 230.717 184.075 165.768 1.00 40.53  ? 397  PRO B CA  1 
ATOM   5599 C  C   . PRO B 2 69  ? 229.698 182.940 165.868 1.00 38.78  ? 397  PRO B C   1 
ATOM   5600 O  O   . PRO B 2 69  ? 228.805 182.983 166.712 1.00 39.04  ? 397  PRO B O   1 
ATOM   5601 C  CB  . PRO B 2 69  ? 230.280 185.110 164.726 1.00 39.34  ? 397  PRO B CB  1 
ATOM   5602 C  CG  . PRO B 2 69  ? 231.568 185.702 164.224 1.00 40.39  ? 397  PRO B CG  1 
ATOM   5603 C  CD  . PRO B 2 69  ? 232.531 184.538 164.182 1.00 39.89  ? 397  PRO B CD  1 
ATOM   5604 N  N   . TYR B 2 70  ? 229.816 181.931 165.012 1.00 37.98  ? 398  TYR B N   1 
ATOM   5605 C  CA  . TYR B 2 70  ? 228.860 180.825 165.005 1.00 38.07  ? 398  TYR B CA  1 
ATOM   5606 C  C   . TYR B 2 70  ? 229.314 179.661 165.883 1.00 38.75  ? 398  TYR B C   1 
ATOM   5607 O  O   . TYR B 2 70  ? 228.615 178.656 166.014 1.00 37.90  ? 398  TYR B O   1 
ATOM   5608 C  CB  . TYR B 2 70  ? 228.633 180.343 163.574 1.00 36.48  ? 398  TYR B CB  1 
ATOM   5609 C  CG  . TYR B 2 70  ? 229.916 180.067 162.846 1.00 36.57  ? 398  TYR B CG  1 
ATOM   5610 C  CD1 . TYR B 2 70  ? 230.445 181.024 161.998 1.00 36.16  ? 398  TYR B CD1 1 
ATOM   5611 C  CD2 . TYR B 2 70  ? 230.583 178.872 163.044 1.00 35.32  ? 398  TYR B CD2 1 
ATOM   5612 C  CE1 . TYR B 2 70  ? 231.633 180.784 161.353 1.00 35.32  ? 398  TYR B CE1 1 
ATOM   5613 C  CE2 . TYR B 2 70  ? 231.772 178.637 162.400 1.00 35.64  ? 398  TYR B CE2 1 
ATOM   5614 C  CZ  . TYR B 2 70  ? 232.297 179.586 161.559 1.00 35.28  ? 398  TYR B CZ  1 
ATOM   5615 O  OH  . TYR B 2 70  ? 233.490 179.351 160.926 1.00 36.02  ? 398  TYR B OH  1 
ATOM   5616 N  N   . GLU B 2 71  ? 230.492 179.804 166.475 1.00 39.03  ? 399  GLU B N   1 
ATOM   5617 C  CA  . GLU B 2 71  ? 231.059 178.810 167.379 1.00 40.16  ? 399  GLU B CA  1 
ATOM   5618 C  C   . GLU B 2 71  ? 231.803 179.518 168.492 1.00 42.32  ? 399  GLU B C   1 
ATOM   5619 O  O   . GLU B 2 71  ? 232.946 179.179 168.808 1.00 41.88  ? 399  GLU B O   1 
ATOM   5620 C  CB  . GLU B 2 71  ? 231.992 177.849 166.635 1.00 40.05  ? 399  GLU B CB  1 
ATOM   5621 C  CG  . GLU B 2 71  ? 233.131 178.527 165.893 1.00 39.04  ? 399  GLU B CG  1 
ATOM   5622 C  CD  . GLU B 2 71  ? 234.096 177.565 165.282 1.00 38.59  ? 399  GLU B CD  1 
ATOM   5623 O  OE1 . GLU B 2 71  ? 235.258 177.915 165.153 1.00 39.73  ? 399  GLU B OE1 1 
ATOM   5624 O  OE2 . GLU B 2 71  ? 233.686 176.468 164.952 1.00 37.25  ? 399  GLU B OE2 1 
ATOM   5625 N  N   . PHE B 2 72  ? 231.174 180.532 169.069 1.00 40.99  ? 400  PHE B N   1 
ATOM   5626 C  CA  . PHE B 2 72  ? 231.820 181.388 170.049 1.00 43.58  ? 400  PHE B CA  1 
ATOM   5627 C  C   . PHE B 2 72  ? 232.258 180.598 171.271 1.00 44.30  ? 400  PHE B C   1 
ATOM   5628 O  O   . PHE B 2 72  ? 231.672 179.564 171.597 1.00 43.72  ? 400  PHE B O   1 
ATOM   5629 C  CB  . PHE B 2 72  ? 230.879 182.519 170.457 1.00 44.01  ? 400  PHE B CB  1 
ATOM   5630 C  CG  . PHE B 2 72  ? 229.581 182.051 171.024 1.00 43.74  ? 400  PHE B CG  1 
ATOM   5631 C  CD1 . PHE B 2 72  ? 229.426 181.867 172.386 1.00 44.69  ? 400  PHE B CD1 1 
ATOM   5632 C  CD2 . PHE B 2 72  ? 228.508 181.794 170.192 1.00 41.27  ? 400  PHE B CD2 1 
ATOM   5633 C  CE1 . PHE B 2 72  ? 228.222 181.439 172.906 1.00 45.25  ? 400  PHE B CE1 1 
ATOM   5634 C  CE2 . PHE B 2 72  ? 227.308 181.370 170.707 1.00 41.61  ? 400  PHE B CE2 1 
ATOM   5635 C  CZ  . PHE B 2 72  ? 227.162 181.190 172.066 1.00 41.97  ? 400  PHE B CZ  1 
ATOM   5636 N  N   . GLY B 2 73  ? 233.302 181.077 171.937 1.00 47.26  ? 401  GLY B N   1 
ATOM   5637 C  CA  . GLY B 2 73  ? 233.806 180.412 173.132 1.00 48.96  ? 401  GLY B CA  1 
ATOM   5638 C  C   . GLY B 2 73  ? 232.977 180.801 174.343 1.00 50.07  ? 401  GLY B C   1 
ATOM   5639 O  O   . GLY B 2 73  ? 232.435 181.905 174.397 1.00 50.94  ? 401  GLY B O   1 
ATOM   5640 N  N   . ARG B 2 74  ? 232.919 179.913 175.330 1.00 51.72  ? 402  ARG B N   1 
ATOM   5641 C  CA  . ARG B 2 74  ? 232.202 180.187 176.574 1.00 54.38  ? 402  ARG B CA  1 
ATOM   5642 C  C   . ARG B 2 74  ? 233.003 179.683 177.766 1.00 54.56  ? 402  ARG B C   1 
ATOM   5643 O  O   . ARG B 2 74  ? 233.294 178.492 177.868 1.00 54.76  ? 402  ARG B O   1 
ATOM   5644 C  CB  . ARG B 2 74  ? 230.841 179.500 176.570 1.00 51.99  ? 402  ARG B CB  1 
ATOM   5645 C  CG  . ARG B 2 74  ? 229.946 179.849 177.750 1.00 52.82  ? 402  ARG B CG  1 
ATOM   5646 C  CD  . ARG B 2 74  ? 228.858 180.781 177.363 1.00 51.06  ? 402  ARG B CD  1 
ATOM   5647 N  NE  . ARG B 2 74  ? 227.706 180.067 176.829 1.00 47.93  ? 402  ARG B NE  1 
ATOM   5648 C  CZ  . ARG B 2 74  ? 226.578 180.643 176.357 1.00 47.02  ? 402  ARG B CZ  1 
ATOM   5649 N  NH1 . ARG B 2 74  ? 226.449 181.953 176.337 1.00 46.92  ? 402  ARG B NH1 1 
ATOM   5650 N  NH2 . ARG B 2 74  ? 225.587 179.884 175.915 1.00 44.42  ? 402  ARG B NH2 1 
ATOM   5651 N  N   . LEU B 2 75  ? 233.349 180.585 178.674 1.00 56.40  ? 403  LEU B N   1 
ATOM   5652 C  CA  . LEU B 2 75  ? 234.155 180.212 179.832 1.00 58.34  ? 403  LEU B CA  1 
ATOM   5653 C  C   . LEU B 2 75  ? 233.616 180.885 181.089 1.00 61.46  ? 403  LEU B C   1 
ATOM   5654 O  O   . LEU B 2 75  ? 233.346 182.087 181.092 1.00 59.42  ? 403  LEU B O   1 
ATOM   5655 C  CB  . LEU B 2 75  ? 235.610 180.624 179.584 1.00 57.97  ? 403  LEU B CB  1 
ATOM   5656 N  N   . VAL B 2 76  ? 233.443 180.107 182.156 1.00 61.59  ? 404  VAL B N   1 
ATOM   5657 C  CA  . VAL B 2 76  ? 232.879 180.655 183.388 1.00 63.89  ? 404  VAL B CA  1 
ATOM   5658 C  C   . VAL B 2 76  ? 233.851 180.574 184.562 1.00 65.21  ? 404  VAL B C   1 
ATOM   5659 O  O   . VAL B 2 76  ? 234.388 179.516 184.875 1.00 64.39  ? 404  VAL B O   1 
ATOM   5660 C  CB  . VAL B 2 76  ? 231.568 179.928 183.736 1.00 65.27  ? 404  VAL B CB  1 
ATOM   5661 N  N   . TYR B 2 82  ? 239.690 188.447 190.041 1.00 73.62  ? 410  TYR B N   1 
ATOM   5662 C  CA  . TYR B 2 82  ? 240.169 188.951 188.764 1.00 74.11  ? 410  TYR B CA  1 
ATOM   5663 C  C   . TYR B 2 82  ? 240.532 190.420 188.849 1.00 76.22  ? 410  TYR B C   1 
ATOM   5664 O  O   . TYR B 2 82  ? 239.977 191.163 189.658 1.00 73.94  ? 410  TYR B O   1 
ATOM   5665 C  CB  . TYR B 2 82  ? 239.099 188.750 187.698 1.00 71.61  ? 410  TYR B CB  1 
ATOM   5666 N  N   . ASN B 2 83  ? 241.441 190.842 187.979 1.00 73.71  ? 411  ASN B N   1 
ATOM   5667 C  CA  . ASN B 2 83  ? 241.816 192.244 187.863 1.00 73.81  ? 411  ASN B CA  1 
ATOM   5668 C  C   . ASN B 2 83  ? 241.370 192.774 186.502 1.00 74.86  ? 411  ASN B C   1 
ATOM   5669 O  O   . ASN B 2 83  ? 241.993 192.479 185.481 1.00 73.22  ? 411  ASN B O   1 
ATOM   5670 C  CB  . ASN B 2 83  ? 243.313 192.396 188.065 1.00 76.31  ? 411  ASN B CB  1 
ATOM   5671 N  N   . PHE B 2 84  ? 240.258 193.515 186.496 1.00 75.97  ? 412  PHE B N   1 
ATOM   5672 C  CA  . PHE B 2 84  ? 239.660 193.967 185.255 1.00 75.45  ? 412  PHE B CA  1 
ATOM   5673 C  C   . PHE B 2 84  ? 240.652 194.818 184.467 1.00 79.15  ? 412  PHE B C   1 
ATOM   5674 O  O   . PHE B 2 84  ? 240.819 194.653 183.256 1.00 69.84  ? 412  PHE B O   1 
ATOM   5675 C  CB  . PHE B 2 84  ? 238.371 194.744 185.538 1.00 73.53  ? 412  PHE B CB  1 
ATOM   5676 N  N   . THR B 2 85  ? 241.325 195.731 185.175 1.00 74.76  ? 413  THR B N   1 
ATOM   5677 C  CA  . THR B 2 85  ? 242.321 196.568 184.515 1.00 75.63  ? 413  THR B CA  1 
ATOM   5678 C  C   . THR B 2 85  ? 243.444 195.744 183.889 1.00 74.31  ? 413  THR B C   1 
ATOM   5679 O  O   . THR B 2 85  ? 243.887 196.038 182.778 1.00 76.07  ? 413  THR B O   1 
ATOM   5680 C  CB  . THR B 2 85  ? 242.935 197.605 185.483 1.00 75.93  ? 413  THR B CB  1 
ATOM   5681 N  N   . LYS B 2 86  ? 243.925 194.733 184.612 1.00 64.69  ? 414  LYS B N   1 
ATOM   5682 C  CA  . LYS B 2 86  ? 245.027 193.909 184.113 1.00 88.93  ? 414  LYS B CA  1 
ATOM   5683 C  C   . LYS B 2 86  ? 244.651 193.219 182.816 1.00 76.27  ? 414  LYS B C   1 
ATOM   5684 O  O   . LYS B 2 86  ? 245.460 193.117 181.901 1.00 72.04  ? 414  LYS B O   1 
ATOM   5685 C  CB  . LYS B 2 86  ? 245.461 192.865 185.139 1.00 71.82  ? 414  LYS B CB  1 
ATOM   5686 N  N   . LEU B 2 87  ? 243.424 192.742 182.721 1.00 70.36  ? 415  LEU B N   1 
ATOM   5687 C  CA  . LEU B 2 87  ? 243.027 192.081 181.490 1.00 72.28  ? 415  LEU B CA  1 
ATOM   5688 C  C   . LEU B 2 87  ? 243.046 193.084 180.335 1.00 76.73  ? 415  LEU B C   1 
ATOM   5689 O  O   . LEU B 2 87  ? 243.526 192.779 179.234 1.00 69.05  ? 415  LEU B O   1 
ATOM   5690 C  CB  . LEU B 2 87  ? 241.643 191.454 181.636 1.00 73.37  ? 415  LEU B CB  1 
ATOM   5691 N  N   . LEU B 2 88  ? 242.572 194.295 180.596 1.00 68.09  ? 416  LEU B N   1 
ATOM   5692 C  CA  . LEU B 2 88  ? 242.579 195.353 179.584 1.00 72.30  ? 416  LEU B CA  1 
ATOM   5693 C  C   . LEU B 2 88  ? 243.940 196.028 179.477 1.00 70.67  ? 416  LEU B C   1 
ATOM   5694 O  O   . LEU B 2 88  ? 244.071 197.242 179.709 1.00 72.54  ? 416  LEU B O   1 
ATOM   5695 C  CB  . LEU B 2 88  ? 241.506 196.402 179.904 1.00 72.64  ? 416  LEU B CB  1 
ATOM   5696 C  CG  . LEU B 2 88  ? 240.058 195.919 179.867 1.00 71.32  ? 416  LEU B CG  1 
ATOM   5697 C  CD1 . LEU B 2 88  ? 239.150 197.044 180.371 1.00 73.42  ? 416  LEU B CD1 1 
ATOM   5698 C  CD2 . LEU B 2 88  ? 239.715 195.479 178.418 1.00 69.40  ? 416  LEU B CD2 1 
ATOM   5699 N  N   . SER B 2 89  ? 244.930 195.245 179.091 1.00 70.18  ? 417  SER B N   1 
ATOM   5700 C  CA  . SER B 2 89  ? 246.290 195.694 178.886 1.00 70.65  ? 417  SER B CA  1 
ATOM   5701 C  C   . SER B 2 89  ? 246.926 194.824 177.820 1.00 69.13  ? 417  SER B C   1 
ATOM   5702 O  O   . SER B 2 89  ? 248.046 195.068 177.377 1.00 67.37  ? 417  SER B O   1 
ATOM   5703 C  CB  . SER B 2 89  ? 247.104 195.618 180.158 1.00 71.51  ? 417  SER B CB  1 
ATOM   5704 N  N   . TYR B 2 90  ? 246.184 193.813 177.385 1.00 68.25  ? 418  TYR B N   1 
ATOM   5705 C  CA  . TYR B 2 90  ? 246.636 192.967 176.290 1.00 66.39  ? 418  TYR B CA  1 
ATOM   5706 C  C   . TYR B 2 90  ? 246.106 193.485 174.964 1.00 64.96  ? 418  TYR B C   1 
ATOM   5707 O  O   . TYR B 2 90  ? 246.709 193.247 173.918 1.00 64.64  ? 418  TYR B O   1 
ATOM   5708 C  CB  . TYR B 2 90  ? 246.191 191.507 176.473 1.00 66.71  ? 418  TYR B CB  1 
ATOM   5709 N  N   . PHE B 2 91  ? 244.967 194.176 174.996 1.00 63.98  ? 419  PHE B N   1 
ATOM   5710 C  CA  . PHE B 2 91  ? 244.314 194.585 173.759 1.00 62.80  ? 419  PHE B CA  1 
ATOM   5711 C  C   . PHE B 2 91  ? 244.216 196.098 173.640 1.00 60.70  ? 419  PHE B C   1 
ATOM   5712 O  O   . PHE B 2 91  ? 243.997 196.796 174.632 1.00 62.90  ? 419  PHE B O   1 
ATOM   5713 C  CB  . PHE B 2 91  ? 242.892 194.021 173.691 1.00 62.66  ? 419  PHE B CB  1 
ATOM   5714 N  N   . GLN B 2 92  ? 244.291 196.590 172.413 1.00 60.45  ? 420  GLN B N   1 
ATOM   5715 C  CA  . GLN B 2 92  ? 243.997 197.987 172.129 1.00 59.12  ? 420  GLN B CA  1 
ATOM   5716 C  C   . GLN B 2 92  ? 242.512 198.143 171.880 1.00 61.13  ? 420  GLN B C   1 
ATOM   5717 O  O   . GLN B 2 92  ? 241.975 197.602 170.915 1.00 81.37  ? 420  GLN B O   1 
ATOM   5718 C  CB  . GLN B 2 92  ? 244.772 198.474 170.904 1.00 61.56  ? 420  GLN B CB  1 
ATOM   5719 N  N   . VAL B 2 93  ? 241.842 198.862 172.769 1.00 60.61  ? 421  VAL B N   1 
ATOM   5720 C  CA  . VAL B 2 93  ? 240.393 198.999 172.689 1.00 59.79  ? 421  VAL B CA  1 
ATOM   5721 C  C   . VAL B 2 93  ? 239.985 200.055 171.676 1.00 59.91  ? 421  VAL B C   1 
ATOM   5722 O  O   . VAL B 2 93  ? 240.491 201.184 171.704 1.00 60.50  ? 421  VAL B O   1 
ATOM   5723 C  CB  . VAL B 2 93  ? 239.819 199.345 174.080 1.00 61.08  ? 421  VAL B CB  1 
ATOM   5724 C  CG1 . VAL B 2 93  ? 238.308 199.551 173.995 1.00 58.94  ? 421  VAL B CG1 1 
ATOM   5725 C  CG2 . VAL B 2 93  ? 240.158 198.223 175.069 1.00 59.64  ? 421  VAL B CG2 1 
ATOM   5726 N  N   . ASP B 2 94  ? 239.086 199.688 170.762 1.00 60.63  ? 422  ASP B N   1 
ATOM   5727 C  CA  . ASP B 2 94  ? 238.567 200.617 169.761 1.00 60.71  ? 422  ASP B CA  1 
ATOM   5728 C  C   . ASP B 2 94  ? 237.228 201.181 170.198 1.00 59.72  ? 422  ASP B C   1 
ATOM   5729 O  O   . ASP B 2 94  ? 236.896 202.331 169.902 1.00 59.35  ? 422  ASP B O   1 
ATOM   5730 C  CB  . ASP B 2 94  ? 238.414 199.942 168.397 1.00 60.17  ? 422  ASP B CB  1 
ATOM   5731 N  N   . ALA B 2 95  ? 236.461 200.364 170.905 1.00 59.64  ? 423  ALA B N   1 
ATOM   5732 C  CA  . ALA B 2 95  ? 235.162 200.781 171.397 1.00 58.83  ? 423  ALA B CA  1 
ATOM   5733 C  C   . ALA B 2 95  ? 234.835 200.070 172.692 1.00 60.09  ? 423  ALA B C   1 
ATOM   5734 O  O   . ALA B 2 95  ? 235.336 198.981 172.967 1.00 59.60  ? 423  ALA B O   1 
ATOM   5735 C  CB  . ALA B 2 95  ? 234.088 200.518 170.360 1.00 58.11  ? 423  ALA B CB  1 
ATOM   5736 N  N   . PHE B 2 96  ? 233.995 200.703 173.501 1.00 59.80  ? 424  PHE B N   1 
ATOM   5737 C  CA  . PHE B 2 96  ? 233.571 200.120 174.761 1.00 61.77  ? 424  PHE B CA  1 
ATOM   5738 C  C   . PHE B 2 96  ? 232.203 200.651 175.175 1.00 62.92  ? 424  PHE B C   1 
ATOM   5739 O  O   . PHE B 2 96  ? 231.947 201.851 175.093 1.00 62.64  ? 424  PHE B O   1 
ATOM   5740 C  CB  . PHE B 2 96  ? 234.605 200.419 175.848 1.00 60.53  ? 424  PHE B CB  1 
ATOM   5741 C  CG  . PHE B 2 96  ? 234.279 199.820 177.179 1.00 61.53  ? 424  PHE B CG  1 
ATOM   5742 C  CD1 . PHE B 2 96  ? 234.594 198.502 177.454 1.00 60.95  ? 424  PHE B CD1 1 
ATOM   5743 C  CD2 . PHE B 2 96  ? 233.656 200.570 178.159 1.00 62.85  ? 424  PHE B CD2 1 
ATOM   5744 C  CE1 . PHE B 2 96  ? 234.296 197.944 178.683 1.00 61.93  ? 424  PHE B CE1 1 
ATOM   5745 C  CE2 . PHE B 2 96  ? 233.355 200.014 179.384 1.00 62.09  ? 424  PHE B CE2 1 
ATOM   5746 C  CZ  . PHE B 2 96  ? 233.678 198.698 179.643 1.00 65.79  ? 424  PHE B CZ  1 
ATOM   5747 N  N   . GLU B 2 97  ? 231.334 199.747 175.621 1.00 62.99  ? 425  GLU B N   1 
ATOM   5748 C  CA  . GLU B 2 97  ? 230.004 200.122 176.093 1.00 62.24  ? 425  GLU B CA  1 
ATOM   5749 C  C   . GLU B 2 97  ? 229.507 199.122 177.133 1.00 62.91  ? 425  GLU B C   1 
ATOM   5750 O  O   . GLU B 2 97  ? 229.940 197.969 177.127 1.00 62.41  ? 425  GLU B O   1 
ATOM   5751 C  CB  . GLU B 2 97  ? 229.030 200.195 174.907 1.00 62.27  ? 425  GLU B CB  1 
ATOM   5752 N  N   . CYS B 2 98  ? 228.586 199.544 178.015 1.00 63.98  ? 426  CYS B N   1 
ATOM   5753 C  CA  . CYS B 2 98  ? 227.968 198.686 179.006 1.00 63.08  ? 426  CYS B CA  1 
ATOM   5754 C  C   . CYS B 2 98  ? 226.460 198.808 179.019 1.00 63.55  ? 426  CYS B C   1 
ATOM   5755 O  O   . CYS B 2 98  ? 225.912 199.852 178.623 1.00 67.31  ? 426  CYS B O   1 
ATOM   5756 C  CB  . CYS B 2 98  ? 228.496 198.981 180.419 1.00 64.90  ? 426  CYS B CB  1 
ATOM   5757 S  SG  . CYS B 2 98  ? 230.271 198.675 180.654 1.00 67.29  ? 426  CYS B SG  1 
ATOM   5758 N  N   . LYS B 2 99  ? 225.787 197.819 179.580 1.00 64.42  ? 427  LYS B N   1 
ATOM   5759 C  CA  . LYS B 2 99  ? 224.357 197.927 179.769 1.00 65.64  ? 427  LYS B CA  1 
ATOM   5760 C  C   . LYS B 2 99  ? 223.939 197.428 181.153 1.00 65.26  ? 427  LYS B C   1 
ATOM   5761 O  O   . LYS B 2 99  ? 224.333 196.340 181.585 1.00 64.54  ? 427  LYS B O   1 
ATOM   5762 C  CB  . LYS B 2 99  ? 223.640 197.178 178.649 1.00 61.15  ? 427  LYS B CB  1 
ATOM   5763 C  CG  . LYS B 2 99  ? 222.166 197.420 178.599 1.00 60.95  ? 427  LYS B CG  1 
ATOM   5764 C  CD  . LYS B 2 99  ? 221.551 196.938 177.305 1.00 57.79  ? 427  LYS B CD  1 
ATOM   5765 C  CE  . LYS B 2 99  ? 220.054 197.170 177.330 1.00 57.78  ? 427  LYS B CE  1 
ATOM   5766 N  NZ  . LYS B 2 99  ? 219.369 196.649 176.125 1.00 55.57  ? 427  LYS B NZ  1 
ATOM   5767 N  N   . LYS B 2 100 ? 223.159 198.254 181.856 1.00 66.51  ? 428  LYS B N   1 
ATOM   5768 C  CA  . LYS B 2 100 ? 222.722 197.987 183.226 1.00 66.33  ? 428  LYS B CA  1 
ATOM   5769 C  C   . LYS B 2 100 ? 223.900 197.928 184.192 1.00 65.88  ? 428  LYS B C   1 
ATOM   5770 O  O   . LYS B 2 100 ? 223.820 197.283 185.237 1.00 64.76  ? 428  LYS B O   1 
ATOM   5771 C  CB  . LYS B 2 100 ? 221.935 196.671 183.307 1.00 64.76  ? 428  LYS B CB  1 
ATOM   5772 C  CG  . LYS B 2 100 ? 220.726 196.585 182.386 1.00 66.22  ? 428  LYS B CG  1 
ATOM   5773 C  CD  . LYS B 2 100 ? 219.578 197.451 182.882 1.00 67.45  ? 428  LYS B CD  1 
ATOM   5774 C  CE  . LYS B 2 100 ? 218.330 197.272 182.023 1.00 69.25  ? 428  LYS B CE  1 
ATOM   5775 N  NZ  . LYS B 2 100 ? 217.879 195.849 181.977 1.00 66.39  ? 428  LYS B NZ  1 
ATOM   5776 N  N   . VAL B 2 101 ? 225.001 198.588 183.827 1.00 66.34  ? 429  VAL B N   1 
ATOM   5777 C  CA  . VAL B 2 101 ? 226.190 198.571 184.669 1.00 68.27  ? 429  VAL B CA  1 
ATOM   5778 C  C   . VAL B 2 101 ? 227.220 199.605 184.222 1.00 70.12  ? 429  VAL B C   1 
ATOM   5779 O  O   . VAL B 2 101 ? 227.288 199.960 183.047 1.00 68.11  ? 429  VAL B O   1 
ATOM   5780 C  CB  . VAL B 2 101 ? 226.804 197.156 184.653 1.00 66.99  ? 429  VAL B CB  1 
ATOM   5781 N  N   . THR B 2 102 ? 228.045 200.047 185.159 1.00 70.92  ? 430  THR B N   1 
ATOM   5782 C  CA  . THR B 2 102 ? 229.186 200.905 184.855 1.00 69.12  ? 430  THR B CA  1 
ATOM   5783 C  C   . THR B 2 102 ? 230.482 200.135 185.132 1.00 78.84  ? 430  THR B C   1 
ATOM   5784 O  O   . THR B 2 102 ? 230.562 199.417 186.133 1.00 114.96 ? 430  THR B O   1 
ATOM   5785 C  CB  . THR B 2 102 ? 229.118 202.192 185.708 1.00 74.65  ? 430  THR B CB  1 
ATOM   5786 N  N   . PRO B 2 103 ? 231.519 200.309 184.296 1.00 69.53  ? 431  PRO B N   1 
ATOM   5787 C  CA  . PRO B 2 103 ? 232.778 199.582 184.308 1.00 70.51  ? 431  PRO B CA  1 
ATOM   5788 C  C   . PRO B 2 103 ? 233.503 199.730 185.635 1.00 75.66  ? 431  PRO B C   1 
ATOM   5789 O  O   . PRO B 2 103 ? 234.292 198.868 186.006 1.00 74.23  ? 431  PRO B O   1 
ATOM   5790 C  CB  . PRO B 2 103 ? 233.554 200.238 183.156 1.00 71.51  ? 431  PRO B CB  1 
ATOM   5791 C  CG  . PRO B 2 103 ? 232.907 201.592 182.981 1.00 71.66  ? 431  PRO B CG  1 
ATOM   5792 C  CD  . PRO B 2 103 ? 231.446 201.354 183.275 1.00 72.21  ? 431  PRO B CD  1 
ATOM   5793 N  N   . GLU B 2 104 ? 233.218 200.798 186.361 1.00 77.16  ? 432  GLU B N   1 
ATOM   5794 C  CA  . GLU B 2 104 ? 233.811 201.006 187.667 1.00 76.59  ? 432  GLU B CA  1 
ATOM   5795 C  C   . GLU B 2 104 ? 233.330 199.932 188.627 1.00 75.33  ? 432  GLU B C   1 
ATOM   5796 O  O   . GLU B 2 104 ? 234.086 199.495 189.487 1.00 73.53  ? 432  GLU B O   1 
ATOM   5797 C  CB  . GLU B 2 104 ? 233.480 202.400 188.195 1.00 75.08  ? 432  GLU B CB  1 
ATOM   5798 N  N   . SER B 2 105 ? 232.078 199.501 188.460 1.00 74.39  ? 433  SER B N   1 
ATOM   5799 C  CA  . SER B 2 105 ? 231.459 198.500 189.324 1.00 73.61  ? 433  SER B CA  1 
ATOM   5800 C  C   . SER B 2 105 ? 231.962 197.108 188.973 1.00 72.68  ? 433  SER B C   1 
ATOM   5801 O  O   . SER B 2 105 ? 232.079 196.239 189.839 1.00 79.66  ? 433  SER B O   1 
ATOM   5802 C  CB  . SER B 2 105 ? 229.952 198.546 189.188 1.00 74.32  ? 433  SER B CB  1 
ATOM   5803 N  N   . ILE B 2 106 ? 232.313 196.914 187.700 1.00 69.15  ? 434  ILE B N   1 
ATOM   5804 C  CA  . ILE B 2 106 ? 232.889 195.642 187.261 1.00 79.59  ? 434  ILE B CA  1 
ATOM   5805 C  C   . ILE B 2 106 ? 234.200 195.431 187.990 1.00 79.00  ? 434  ILE B C   1 
ATOM   5806 O  O   . ILE B 2 106 ? 234.485 194.326 188.437 1.00 73.90  ? 434  ILE B O   1 
ATOM   5807 C  CB  . ILE B 2 106 ? 233.146 195.605 185.741 1.00 74.81  ? 434  ILE B CB  1 
ATOM   5808 N  N   . ALA B 2 107 ? 234.989 196.492 188.118 1.00 72.28  ? 435  ALA B N   1 
ATOM   5809 C  CA  . ALA B 2 107 ? 236.266 196.401 188.802 1.00 76.78  ? 435  ALA B CA  1 
ATOM   5810 C  C   . ALA B 2 107 ? 236.123 196.391 190.327 1.00 73.53  ? 435  ALA B C   1 
ATOM   5811 O  O   . ALA B 2 107 ? 236.906 195.742 191.021 1.00 74.60  ? 435  ALA B O   1 
ATOM   5812 C  CB  . ALA B 2 107 ? 237.144 197.556 188.374 1.00 75.74  ? 435  ALA B CB  1 
ATOM   5813 N  N   . THR B 2 108 ? 235.131 197.111 190.852 1.00 78.26  ? 436  THR B N   1 
ATOM   5814 C  CA  . THR B 2 108 ? 234.976 197.213 192.303 1.00 73.56  ? 436  THR B CA  1 
ATOM   5815 C  C   . THR B 2 108 ? 233.701 196.537 192.785 1.00 74.82  ? 436  THR B C   1 
ATOM   5816 O  O   . THR B 2 108 ? 232.681 197.197 193.006 1.00 74.67  ? 436  THR B O   1 
ATOM   5817 C  CB  . THR B 2 108 ? 234.950 198.679 192.784 1.00 75.22  ? 436  THR B CB  1 
ATOM   5818 N  N   . SER B 2 113 ? 229.555 184.602 190.114 1.00 69.44  ? 441  SER B N   1 
ATOM   5819 C  CA  . SER B 2 113 ? 230.224 184.099 188.922 1.00 68.91  ? 441  SER B CA  1 
ATOM   5820 C  C   . SER B 2 113 ? 230.552 185.224 187.951 1.00 68.10  ? 441  SER B C   1 
ATOM   5821 O  O   . SER B 2 113 ? 229.848 186.235 187.889 1.00 67.16  ? 441  SER B O   1 
ATOM   5822 C  CB  . SER B 2 113 ? 229.355 183.067 188.229 1.00 67.02  ? 441  SER B CB  1 
ATOM   5823 N  N   . LEU B 2 114 ? 231.591 185.005 187.153 1.00 67.64  ? 442  LEU B N   1 
ATOM   5824 C  CA  . LEU B 2 114 ? 231.949 185.891 186.049 1.00 67.09  ? 442  LEU B CA  1 
ATOM   5825 C  C   . LEU B 2 114 ? 231.984 185.093 184.752 1.00 66.19  ? 442  LEU B C   1 
ATOM   5826 O  O   . LEU B 2 114 ? 232.674 184.079 184.658 1.00 68.05  ? 442  LEU B O   1 
ATOM   5827 C  CB  . LEU B 2 114 ? 233.321 186.538 186.312 1.00 67.32  ? 442  LEU B CB  1 
ATOM   5828 N  N   . THR B 2 115 ? 231.221 185.526 183.759 1.00 64.06  ? 443  THR B N   1 
ATOM   5829 C  CA  . THR B 2 115 ? 231.123 184.771 182.511 1.00 63.24  ? 443  THR B CA  1 
ATOM   5830 C  C   . THR B 2 115 ? 231.665 185.545 181.322 1.00 60.41  ? 443  THR B C   1 
ATOM   5831 O  O   . THR B 2 115 ? 231.287 186.695 181.082 1.00 60.11  ? 443  THR B O   1 
ATOM   5832 C  CB  . THR B 2 115 ? 229.668 184.357 182.227 1.00 63.66  ? 443  THR B CB  1 
ATOM   5833 N  N   . VAL B 2 116 ? 232.546 184.906 180.560 1.00 60.42  ? 444  VAL B N   1 
ATOM   5834 C  CA  . VAL B 2 116 ? 233.110 185.552 179.383 1.00 57.22  ? 444  VAL B CA  1 
ATOM   5835 C  C   . VAL B 2 116 ? 232.786 184.788 178.110 1.00 55.77  ? 444  VAL B C   1 
ATOM   5836 O  O   . VAL B 2 116 ? 233.162 183.623 177.948 1.00 56.00  ? 444  VAL B O   1 
ATOM   5837 C  CB  . VAL B 2 116 ? 234.638 185.692 179.527 1.00 57.94  ? 444  VAL B CB  1 
ATOM   5838 C  CG1 . VAL B 2 116 ? 235.221 186.381 178.292 1.00 56.75  ? 444  VAL B CG1 1 
ATOM   5839 C  CG2 . VAL B 2 116 ? 234.955 186.476 180.798 1.00 60.15  ? 444  VAL B CG2 1 
ATOM   5840 N  N   . ASP B 2 117 ? 232.117 185.473 177.187 1.00 54.49  ? 445  ASP B N   1 
ATOM   5841 C  CA  . ASP B 2 117 ? 231.837 184.940 175.859 1.00 53.74  ? 445  ASP B CA  1 
ATOM   5842 C  C   . ASP B 2 117 ? 232.641 185.737 174.849 1.00 51.97  ? 445  ASP B C   1 
ATOM   5843 O  O   . ASP B 2 117 ? 232.692 186.961 174.924 1.00 52.60  ? 445  ASP B O   1 
ATOM   5844 C  CB  . ASP B 2 117 ? 230.345 185.029 175.533 1.00 51.63  ? 445  ASP B CB  1 
ATOM   5845 C  CG  . ASP B 2 117 ? 229.486 184.172 176.447 1.00 51.46  ? 445  ASP B CG  1 
ATOM   5846 O  OD1 . ASP B 2 117 ? 230.033 183.452 177.246 1.00 52.61  ? 445  ASP B OD1 1 
ATOM   5847 O  OD2 . ASP B 2 117 ? 228.284 184.227 176.328 1.00 50.12  ? 445  ASP B OD2 1 
ATOM   5848 N  N   . TRP B 2 118 ? 233.299 185.064 173.917 1.00 50.52  ? 446  TRP B N   1 
ATOM   5849 C  CA  . TRP B 2 118 ? 234.122 185.807 172.973 1.00 51.22  ? 446  TRP B CA  1 
ATOM   5850 C  C   . TRP B 2 118 ? 234.211 185.133 171.616 1.00 49.30  ? 446  TRP B C   1 
ATOM   5851 O  O   . TRP B 2 118 ? 234.043 183.914 171.496 1.00 49.29  ? 446  TRP B O   1 
ATOM   5852 C  CB  . TRP B 2 118 ? 235.526 186.007 173.551 1.00 52.17  ? 446  TRP B CB  1 
ATOM   5853 C  CG  . TRP B 2 118 ? 236.377 184.785 173.514 1.00 52.19  ? 446  TRP B CG  1 
ATOM   5854 C  CD1 . TRP B 2 118 ? 237.358 184.519 172.615 1.00 51.83  ? 446  TRP B CD1 1 
ATOM   5855 C  CD2 . TRP B 2 118 ? 236.318 183.641 174.393 1.00 50.05  ? 446  TRP B CD2 1 
ATOM   5856 N  NE1 . TRP B 2 118 ? 237.918 183.297 172.874 1.00 52.87  ? 446  TRP B NE1 1 
ATOM   5857 C  CE2 . TRP B 2 118 ? 237.289 182.743 173.956 1.00 52.88  ? 446  TRP B CE2 1 
ATOM   5858 C  CE3 . TRP B 2 118 ? 235.528 183.309 175.497 1.00 53.12  ? 446  TRP B CE3 1 
ATOM   5859 C  CZ2 . TRP B 2 118 ? 237.496 181.528 174.579 1.00 53.58  ? 446  TRP B CZ2 1 
ATOM   5860 C  CZ3 . TRP B 2 118 ? 235.732 182.094 176.119 1.00 53.94  ? 446  TRP B CZ3 1 
ATOM   5861 C  CH2 . TRP B 2 118 ? 236.691 181.223 175.673 1.00 53.68  ? 446  TRP B CH2 1 
ATOM   5862 N  N   . PHE B 2 119 ? 234.490 185.935 170.598 1.00 48.37  ? 447  PHE B N   1 
ATOM   5863 C  CA  . PHE B 2 119 ? 234.658 185.428 169.245 1.00 46.03  ? 447  PHE B CA  1 
ATOM   5864 C  C   . PHE B 2 119 ? 235.426 186.410 168.374 1.00 49.11  ? 447  PHE B C   1 
ATOM   5865 O  O   . PHE B 2 119 ? 235.529 187.597 168.695 1.00 48.82  ? 447  PHE B O   1 
ATOM   5866 C  CB  . PHE B 2 119 ? 233.299 185.112 168.615 1.00 46.11  ? 447  PHE B CB  1 
ATOM   5867 C  CG  . PHE B 2 119 ? 232.297 186.233 168.656 1.00 45.36  ? 447  PHE B CG  1 
ATOM   5868 C  CD1 . PHE B 2 119 ? 232.253 187.191 167.660 1.00 45.71  ? 447  PHE B CD1 1 
ATOM   5869 C  CD2 . PHE B 2 119 ? 231.376 186.311 169.685 1.00 46.05  ? 447  PHE B CD2 1 
ATOM   5870 C  CE1 . PHE B 2 119 ? 231.315 188.200 167.691 1.00 44.38  ? 447  PHE B CE1 1 
ATOM   5871 C  CE2 . PHE B 2 119 ? 230.438 187.318 169.719 1.00 46.44  ? 447  PHE B CE2 1 
ATOM   5872 C  CZ  . PHE B 2 119 ? 230.406 188.263 168.718 1.00 45.92  ? 447  PHE B CZ  1 
ATOM   5873 N  N   . ALA B 2 120 ? 235.944 185.918 167.263 1.00 46.84  ? 448  ALA B N   1 
ATOM   5874 C  CA  . ALA B 2 120 ? 236.625 186.750 166.288 1.00 47.69  ? 448  ALA B CA  1 
ATOM   5875 C  C   . ALA B 2 120 ? 235.616 187.657 165.600 1.00 47.65  ? 448  ALA B C   1 
ATOM   5876 O  O   . ALA B 2 120 ? 234.536 187.220 165.220 1.00 46.24  ? 448  ALA B O   1 
ATOM   5877 C  CB  . ALA B 2 120 ? 237.326 185.884 165.255 1.00 46.26  ? 448  ALA B CB  1 
ATOM   5878 N  N   . TYR B 2 121 ? 235.983 188.915 165.414 1.00 48.23  ? 449  TYR B N   1 
ATOM   5879 C  CA  . TYR B 2 121 ? 235.140 189.839 164.691 1.00 47.54  ? 449  TYR B CA  1 
ATOM   5880 C  C   . TYR B 2 121 ? 236.007 190.940 164.125 1.00 48.39  ? 449  TYR B C   1 
ATOM   5881 O  O   . TYR B 2 121 ? 237.214 190.978 164.398 1.00 49.14  ? 449  TYR B O   1 
ATOM   5882 C  CB  . TYR B 2 121 ? 234.041 190.392 165.600 1.00 48.23  ? 449  TYR B CB  1 
ATOM   5883 C  CG  . TYR B 2 121 ? 232.827 190.867 164.836 1.00 47.49  ? 449  TYR B CG  1 
ATOM   5884 C  CD1 . TYR B 2 121 ? 232.482 192.207 164.820 1.00 47.89  ? 449  TYR B CD1 1 
ATOM   5885 C  CD2 . TYR B 2 121 ? 232.075 189.951 164.118 1.00 46.37  ? 449  TYR B CD2 1 
ATOM   5886 C  CE1 . TYR B 2 121 ? 231.379 192.620 164.105 1.00 47.60  ? 449  TYR B CE1 1 
ATOM   5887 C  CE2 . TYR B 2 121 ? 230.980 190.368 163.403 1.00 44.78  ? 449  TYR B CE2 1 
ATOM   5888 C  CZ  . TYR B 2 121 ? 230.633 191.692 163.393 1.00 45.27  ? 449  TYR B CZ  1 
ATOM   5889 O  OH  . TYR B 2 121 ? 229.542 192.094 162.674 1.00 44.97  ? 449  TYR B OH  1 
ATOM   5890 N  N   . ARG B 2 122 ? 235.406 191.887 163.400 1.00 48.44  ? 450  ARG B N   1 
ATOM   5891 C  CA  . ARG B 2 122 ? 236.203 192.980 162.868 1.00 49.49  ? 450  ARG B CA  1 
ATOM   5892 C  C   . ARG B 2 122 ? 235.888 194.257 163.601 1.00 49.02  ? 450  ARG B C   1 
ATOM   5893 O  O   . ARG B 2 122 ? 234.720 194.556 163.859 1.00 50.32  ? 450  ARG B O   1 
ATOM   5894 C  CB  . ARG B 2 122 ? 235.958 193.156 161.380 1.00 48.92  ? 450  ARG B CB  1 
ATOM   5895 C  CG  . ARG B 2 122 ? 236.311 191.955 160.539 1.00 48.50  ? 450  ARG B CG  1 
ATOM   5896 C  CD  . ARG B 2 122 ? 236.621 192.346 159.140 1.00 47.39  ? 450  ARG B CD  1 
ATOM   5897 N  NE  . ARG B 2 122 ? 235.583 193.194 158.567 1.00 47.23  ? 450  ARG B NE  1 
ATOM   5898 C  CZ  . ARG B 2 122 ? 235.619 193.719 157.332 1.00 47.34  ? 450  ARG B CZ  1 
ATOM   5899 N  NH1 . ARG B 2 122 ? 236.617 193.456 156.522 1.00 46.39  ? 450  ARG B NH1 1 
ATOM   5900 N  NH2 . ARG B 2 122 ? 234.634 194.501 156.940 1.00 46.53  ? 450  ARG B NH2 1 
ATOM   5901 N  N   . VAL B 2 123 ? 236.908 195.027 163.922 1.00 50.36  ? 451  VAL B N   1 
ATOM   5902 C  CA  . VAL B 2 123 ? 236.696 196.277 164.634 1.00 50.85  ? 451  VAL B CA  1 
ATOM   5903 C  C   . VAL B 2 123 ? 236.010 197.285 163.726 1.00 50.80  ? 451  VAL B C   1 
ATOM   5904 O  O   . VAL B 2 123 ? 235.222 198.106 164.186 1.00 50.46  ? 451  VAL B O   1 
ATOM   5905 C  CB  . VAL B 2 123 ? 238.019 196.830 165.183 1.00 52.34  ? 451  VAL B CB  1 
ATOM   5906 N  N   . ALA B 2 124 ? 236.262 197.167 162.428 1.00 50.01  ? 452  ALA B N   1 
ATOM   5907 C  CA  . ALA B 2 124 ? 235.628 198.029 161.444 1.00 50.08  ? 452  ALA B CA  1 
ATOM   5908 C  C   . ALA B 2 124 ? 234.107 197.906 161.514 1.00 48.94  ? 452  ALA B C   1 
ATOM   5909 O  O   . ALA B 2 124 ? 233.382 198.830 161.151 1.00 49.41  ? 452  ALA B O   1 
ATOM   5910 C  CB  . ALA B 2 124 ? 236.113 197.656 160.054 1.00 50.57  ? 452  ALA B CB  1 
ATOM   5911 N  N   . ASP B 2 125 ? 233.642 196.740 161.946 1.00 49.65  ? 453  ASP B N   1 
ATOM   5912 C  CA  . ASP B 2 125 ? 232.224 196.411 161.979 1.00 49.87  ? 453  ASP B CA  1 
ATOM   5913 C  C   . ASP B 2 125 ? 231.645 196.453 163.390 1.00 45.65  ? 453  ASP B C   1 
ATOM   5914 O  O   . ASP B 2 125 ? 230.600 195.862 163.653 1.00 47.98  ? 453  ASP B O   1 
ATOM   5915 C  CB  . ASP B 2 125 ? 231.995 195.029 161.362 1.00 49.01  ? 453  ASP B CB  1 
ATOM   5916 C  CG  . ASP B 2 125 ? 232.194 195.009 159.839 1.00 48.74  ? 453  ASP B CG  1 
ATOM   5917 O  OD1 . ASP B 2 125 ? 232.866 194.078 159.355 1.00 48.94  ? 453  ASP B OD1 1 
ATOM   5918 O  OD2 . ASP B 2 125 ? 231.675 195.900 159.163 1.00 48.95  ? 453  ASP B OD2 1 
ATOM   5919 N  N   . LYS B 2 126 ? 232.305 197.173 164.297 1.00 49.82  ? 454  LYS B N   1 
ATOM   5920 C  CA  . LYS B 2 126 ? 231.884 197.200 165.702 1.00 49.31  ? 454  LYS B CA  1 
ATOM   5921 C  C   . LYS B 2 126 ? 230.462 197.720 165.895 1.00 48.23  ? 454  LYS B C   1 
ATOM   5922 O  O   . LYS B 2 126 ? 229.837 197.438 166.914 1.00 47.93  ? 454  LYS B O   1 
ATOM   5923 C  CB  . LYS B 2 126 ? 232.852 198.044 166.534 1.00 50.69  ? 454  LYS B CB  1 
ATOM   5924 N  N   . SER B 2 127 ? 229.949 198.463 164.919 1.00 47.87  ? 455  SER B N   1 
ATOM   5925 C  CA  . SER B 2 127 ? 228.615 199.028 165.037 1.00 48.25  ? 455  SER B CA  1 
ATOM   5926 C  C   . SER B 2 127 ? 227.556 197.935 165.144 1.00 47.77  ? 455  SER B C   1 
ATOM   5927 O  O   . SER B 2 127 ? 226.450 198.166 165.615 1.00 47.41  ? 455  SER B O   1 
ATOM   5928 C  CB  . SER B 2 127 ? 228.294 199.921 163.848 1.00 47.27  ? 455  SER B CB  1 
ATOM   5929 N  N   . ASP B 2 128 ? 227.908 196.722 164.697 1.00 47.24  ? 456  ASP B N   1 
ATOM   5930 C  CA  . ASP B 2 128 ? 226.990 195.585 164.693 1.00 45.90  ? 456  ASP B CA  1 
ATOM   5931 C  C   . ASP B 2 128 ? 226.916 194.860 166.030 1.00 46.58  ? 456  ASP B C   1 
ATOM   5932 O  O   . ASP B 2 128 ? 226.054 194.007 166.240 1.00 44.41  ? 456  ASP B O   1 
ATOM   5933 C  CB  . ASP B 2 128 ? 227.392 194.571 163.628 1.00 44.22  ? 456  ASP B CB  1 
ATOM   5934 C  CG  . ASP B 2 128 ? 227.208 195.072 162.214 1.00 45.85  ? 456  ASP B CG  1 
ATOM   5935 O  OD1 . ASP B 2 128 ? 226.468 196.006 162.008 1.00 43.95  ? 456  ASP B OD1 1 
ATOM   5936 O  OD2 . ASP B 2 128 ? 227.795 194.488 161.330 1.00 46.06  ? 456  ASP B OD2 1 
ATOM   5937 N  N   . LEU B 2 129 ? 227.860 195.162 166.932 1.00 46.55  ? 457  LEU B N   1 
ATOM   5938 C  CA  . LEU B 2 129 ? 227.926 194.487 168.205 1.00 47.03  ? 457  LEU B CA  1 
ATOM   5939 C  C   . LEU B 2 129 ? 226.995 195.180 169.193 1.00 47.11  ? 457  LEU B C   1 
ATOM   5940 O  O   . LEU B 2 129 ? 226.731 194.668 170.287 1.00 48.19  ? 457  LEU B O   1 
ATOM   5941 C  CB  . LEU B 2 129 ? 229.358 194.558 168.753 1.00 47.81  ? 457  LEU B CB  1 
ATOM   5942 C  CG  . LEU B 2 129 ? 230.453 193.941 167.878 1.00 48.02  ? 457  LEU B CG  1 
ATOM   5943 C  CD1 . LEU B 2 129 ? 231.810 194.327 168.444 1.00 50.56  ? 457  LEU B CD1 1 
ATOM   5944 C  CD2 . LEU B 2 129 ? 230.303 192.434 167.863 1.00 47.47  ? 457  LEU B CD2 1 
ATOM   5945 N  N   . LEU B 2 130 ? 226.541 196.360 168.807 1.00 46.86  ? 458  LEU B N   1 
ATOM   5946 C  CA  . LEU B 2 130 ? 225.734 197.207 169.681 1.00 46.93  ? 458  LEU B CA  1 
ATOM   5947 C  C   . LEU B 2 130 ? 224.291 196.728 169.770 1.00 46.37  ? 458  LEU B C   1 
ATOM   5948 O  O   . LEU B 2 130 ? 223.753 196.193 168.794 1.00 45.83  ? 458  LEU B O   1 
ATOM   5949 C  CB  . LEU B 2 130 ? 225.768 198.646 169.164 1.00 46.88  ? 458  LEU B CB  1 
ATOM   5950 N  N   . PRO B 2 131 ? 223.634 196.951 170.907 1.00 47.38  ? 459  PRO B N   1 
ATOM   5951 C  CA  . PRO B 2 131 ? 222.214 196.745 171.136 1.00 47.03  ? 459  PRO B CA  1 
ATOM   5952 C  C   . PRO B 2 131 ? 221.410 197.527 170.122 1.00 46.12  ? 459  PRO B C   1 
ATOM   5953 O  O   . PRO B 2 131 ? 221.738 198.664 169.806 1.00 45.85  ? 459  PRO B O   1 
ATOM   5954 C  CB  . PRO B 2 131 ? 222.025 197.307 172.544 1.00 48.13  ? 459  PRO B CB  1 
ATOM   5955 C  CG  . PRO B 2 131 ? 223.374 197.188 173.203 1.00 48.49  ? 459  PRO B CG  1 
ATOM   5956 C  CD  . PRO B 2 131 ? 224.372 197.421 172.090 1.00 47.85  ? 459  PRO B CD  1 
ATOM   5957 N  N   . GLY B 2 132 ? 220.352 196.913 169.616 1.00 44.03  ? 460  GLY B N   1 
ATOM   5958 C  CA  . GLY B 2 132 ? 219.481 197.574 168.651 1.00 42.86  ? 460  GLY B CA  1 
ATOM   5959 C  C   . GLY B 2 132 ? 219.899 197.273 167.217 1.00 42.93  ? 460  GLY B C   1 
ATOM   5960 O  O   . GLY B 2 132 ? 219.178 197.617 166.276 1.00 40.99  ? 460  GLY B O   1 
ATOM   5961 N  N   . SER B 2 133 ? 221.046 196.630 167.048 1.00 43.92  ? 461  SER B N   1 
ATOM   5962 C  CA  . SER B 2 133 ? 221.518 196.280 165.712 1.00 41.88  ? 461  SER B CA  1 
ATOM   5963 C  C   . SER B 2 133 ? 220.598 195.291 165.021 1.00 41.14  ? 461  SER B C   1 
ATOM   5964 O  O   . SER B 2 133 ? 220.057 194.378 165.642 1.00 42.09  ? 461  SER B O   1 
ATOM   5965 C  CB  . SER B 2 133 ? 222.911 195.697 165.777 1.00 42.17  ? 461  SER B CB  1 
ATOM   5966 N  N   . SER B 2 134 ? 220.447 195.468 163.710 1.00 40.56  ? 462  SER B N   1 
ATOM   5967 C  CA  . SER B 2 134 ? 219.654 194.572 162.880 1.00 40.65  ? 462  SER B CA  1 
ATOM   5968 C  C   . SER B 2 134 ? 220.546 193.775 161.937 1.00 39.18  ? 462  SER B C   1 
ATOM   5969 O  O   . SER B 2 134 ? 220.079 193.236 160.933 1.00 38.10  ? 462  SER B O   1 
ATOM   5970 C  CB  . SER B 2 134 ? 218.642 195.361 162.076 1.00 39.96  ? 462  SER B CB  1 
ATOM   5971 N  N   . SER B 2 135 ? 221.840 193.743 162.248 1.00 39.87  ? 463  SER B N   1 
ATOM   5972 C  CA  . SER B 2 135 ? 222.833 193.077 161.410 1.00 38.25  ? 463  SER B CA  1 
ATOM   5973 C  C   . SER B 2 135 ? 222.722 191.563 161.471 1.00 37.25  ? 463  SER B C   1 
ATOM   5974 O  O   . SER B 2 135 ? 222.064 191.006 162.348 1.00 36.66  ? 463  SER B O   1 
ATOM   5975 C  CB  . SER B 2 135 ? 224.229 193.481 161.826 1.00 39.66  ? 463  SER B CB  1 
ATOM   5976 N  N   . ASP B 2 136 ? 223.401 190.897 160.540 1.00 35.93  ? 464  ASP B N   1 
ATOM   5977 C  CA  . ASP B 2 136 ? 223.380 189.443 160.451 1.00 35.01  ? 464  ASP B CA  1 
ATOM   5978 C  C   . ASP B 2 136 ? 223.949 188.780 161.698 1.00 37.48  ? 464  ASP B C   1 
ATOM   5979 O  O   . ASP B 2 136 ? 223.473 187.727 162.123 1.00 32.94  ? 464  ASP B O   1 
ATOM   5980 C  CB  . ASP B 2 136 ? 224.170 188.979 159.230 1.00 33.56  ? 464  ASP B CB  1 
ATOM   5981 C  CG  . ASP B 2 136 ? 223.474 189.295 157.915 1.00 32.69  ? 464  ASP B CG  1 
ATOM   5982 O  OD1 . ASP B 2 136 ? 222.292 189.536 157.926 1.00 32.77  ? 464  ASP B OD1 1 
ATOM   5983 O  OD2 . ASP B 2 136 ? 224.142 189.318 156.912 1.00 31.98  ? 464  ASP B OD2 1 
ATOM   5984 N  N   . LEU B 2 137 ? 224.951 189.403 162.303 1.00 36.33  ? 465  LEU B N   1 
ATOM   5985 C  CA  . LEU B 2 137 ? 225.599 188.821 163.468 1.00 36.68  ? 465  LEU B CA  1 
ATOM   5986 C  C   . LEU B 2 137 ? 224.590 188.384 164.520 1.00 37.11  ? 465  LEU B C   1 
ATOM   5987 O  O   . LEU B 2 137 ? 224.640 187.257 165.008 1.00 35.97  ? 465  LEU B O   1 
ATOM   5988 C  CB  . LEU B 2 137 ? 226.563 189.831 164.098 1.00 38.68  ? 465  LEU B CB  1 
ATOM   5989 C  CG  . LEU B 2 137 ? 227.237 189.394 165.415 1.00 40.10  ? 465  LEU B CG  1 
ATOM   5990 C  CD1 . LEU B 2 137 ? 228.194 188.246 165.160 1.00 39.81  ? 465  LEU B CD1 1 
ATOM   5991 C  CD2 . LEU B 2 137 ? 227.961 190.565 166.010 1.00 42.39  ? 465  LEU B CD2 1 
ATOM   5992 N  N   . GLN B 2 138 ? 223.668 189.270 164.870 1.00 36.85  ? 466  GLN B N   1 
ATOM   5993 C  CA  . GLN B 2 138 ? 222.741 188.983 165.955 1.00 37.64  ? 466  GLN B CA  1 
ATOM   5994 C  C   . GLN B 2 138 ? 221.494 188.250 165.490 1.00 35.61  ? 466  GLN B C   1 
ATOM   5995 O  O   . GLN B 2 138 ? 220.598 187.977 166.286 1.00 36.79  ? 466  GLN B O   1 
ATOM   5996 C  CB  . GLN B 2 138 ? 222.358 190.267 166.691 1.00 39.29  ? 466  GLN B CB  1 
ATOM   5997 C  CG  . GLN B 2 138 ? 223.510 190.902 167.457 1.00 39.83  ? 466  GLN B CG  1 
ATOM   5998 C  CD  . GLN B 2 138 ? 223.088 192.125 168.248 1.00 42.13  ? 466  GLN B CD  1 
ATOM   5999 O  OE1 . GLN B 2 138 ? 222.030 192.133 168.900 1.00 42.18  ? 466  GLN B OE1 1 
ATOM   6000 N  NE2 . GLN B 2 138 ? 223.909 193.171 168.198 1.00 44.20  ? 466  GLN B NE2 1 
ATOM   6001 N  N   . ARG B 2 139 ? 221.425 187.932 164.207 1.00 35.39  ? 467  ARG B N   1 
ATOM   6002 C  CA  . ARG B 2 139 ? 220.282 187.200 163.691 1.00 32.84  ? 467  ARG B CA  1 
ATOM   6003 C  C   . ARG B 2 139 ? 220.613 185.724 163.551 1.00 31.48  ? 467  ARG B C   1 
ATOM   6004 O  O   . ARG B 2 139 ? 219.790 184.864 163.862 1.00 31.17  ? 467  ARG B O   1 
ATOM   6005 C  CB  . ARG B 2 139 ? 219.848 187.753 162.344 1.00 31.90  ? 467  ARG B CB  1 
ATOM   6006 C  CG  . ARG B 2 139 ? 219.241 189.141 162.390 1.00 32.99  ? 467  ARG B CG  1 
ATOM   6007 C  CD  . ARG B 2 139 ? 219.032 189.699 161.028 1.00 32.65  ? 467  ARG B CD  1 
ATOM   6008 N  NE  . ARG B 2 139 ? 217.984 188.994 160.300 1.00 29.85  ? 467  ARG B NE  1 
ATOM   6009 C  CZ  . ARG B 2 139 ? 217.837 189.005 158.959 1.00 30.19  ? 467  ARG B CZ  1 
ATOM   6010 N  NH1 . ARG B 2 139 ? 218.678 189.680 158.204 1.00 31.53  ? 467  ARG B NH1 1 
ATOM   6011 N  NH2 . ARG B 2 139 ? 216.844 188.337 158.399 1.00 30.01  ? 467  ARG B NH2 1 
ATOM   6012 N  N   . PHE B 2 140 ? 221.819 185.430 163.076 1.00 32.77  ? 468  PHE B N   1 
ATOM   6013 C  CA  . PHE B 2 140 ? 222.179 184.053 162.774 1.00 32.38  ? 468  PHE B CA  1 
ATOM   6014 C  C   . PHE B 2 140 ? 223.372 183.511 163.556 1.00 33.86  ? 468  PHE B C   1 
ATOM   6015 O  O   . PHE B 2 140 ? 223.630 182.310 163.515 1.00 33.34  ? 468  PHE B O   1 
ATOM   6016 C  CB  . PHE B 2 140 ? 222.457 183.924 161.277 1.00 31.40  ? 468  PHE B CB  1 
ATOM   6017 C  CG  . PHE B 2 140 ? 221.301 184.363 160.434 1.00 30.20  ? 468  PHE B CG  1 
ATOM   6018 C  CD1 . PHE B 2 140 ? 220.141 183.611 160.382 1.00 28.34  ? 468  PHE B CD1 1 
ATOM   6019 C  CD2 . PHE B 2 140 ? 221.364 185.535 159.705 1.00 30.38  ? 468  PHE B CD2 1 
ATOM   6020 C  CE1 . PHE B 2 140 ? 219.070 184.019 159.622 1.00 26.85  ? 468  PHE B CE1 1 
ATOM   6021 C  CE2 . PHE B 2 140 ? 220.295 185.946 158.943 1.00 29.75  ? 468  PHE B CE2 1 
ATOM   6022 C  CZ  . PHE B 2 140 ? 219.146 185.186 158.902 1.00 28.05  ? 468  PHE B CZ  1 
ATOM   6023 N  N   . ASN B 2 141 ? 224.126 184.377 164.229 1.00 34.60  ? 469  ASN B N   1 
ATOM   6024 C  CA  . ASN B 2 141 ? 225.374 183.933 164.843 1.00 35.11  ? 469  ASN B CA  1 
ATOM   6025 C  C   . ASN B 2 141 ? 225.351 184.017 166.366 1.00 36.91  ? 469  ASN B C   1 
ATOM   6026 O  O   . ASN B 2 141 ? 225.434 182.997 167.050 1.00 37.76  ? 469  ASN B O   1 
ATOM   6027 C  CB  . ASN B 2 141 ? 226.528 184.738 164.290 1.00 35.92  ? 469  ASN B CB  1 
ATOM   6028 C  CG  . ASN B 2 141 ? 226.734 184.514 162.832 1.00 37.36  ? 469  ASN B CG  1 
ATOM   6029 O  OD1 . ASN B 2 141 ? 227.488 183.631 162.407 1.00 34.48  ? 469  ASN B OD1 1 
ATOM   6030 N  ND2 . ASN B 2 141 ? 226.052 185.299 162.040 1.00 33.69  ? 469  ASN B ND2 1 
ATOM   6031 N  N   . TYR B 2 142 ? 225.283 185.232 166.899 1.00 37.40  ? 470  TYR B N   1 
ATOM   6032 C  CA  . TYR B 2 142 ? 225.353 185.437 168.343 1.00 39.84  ? 470  TYR B CA  1 
ATOM   6033 C  C   . TYR B 2 142 ? 224.546 186.630 168.812 1.00 40.82  ? 470  TYR B C   1 
ATOM   6034 O  O   . TYR B 2 142 ? 224.716 187.740 168.314 1.00 40.08  ? 470  TYR B O   1 
ATOM   6035 C  CB  . TYR B 2 142 ? 226.797 185.645 168.794 1.00 41.22  ? 470  TYR B CB  1 
ATOM   6036 C  CG  . TYR B 2 142 ? 226.905 186.024 170.264 1.00 42.97  ? 470  TYR B CG  1 
ATOM   6037 C  CD1 . TYR B 2 142 ? 226.903 185.047 171.237 1.00 43.58  ? 470  TYR B CD1 1 
ATOM   6038 C  CD2 . TYR B 2 142 ? 226.982 187.362 170.632 1.00 44.88  ? 470  TYR B CD2 1 
ATOM   6039 C  CE1 . TYR B 2 142 ? 226.987 185.394 172.569 1.00 44.60  ? 470  TYR B CE1 1 
ATOM   6040 C  CE2 . TYR B 2 142 ? 227.064 187.707 171.964 1.00 45.53  ? 470  TYR B CE2 1 
ATOM   6041 C  CZ  . TYR B 2 142 ? 227.070 186.729 172.929 1.00 46.07  ? 470  TYR B CZ  1 
ATOM   6042 O  OH  . TYR B 2 142 ? 227.155 187.073 174.256 1.00 48.02  ? 470  TYR B OH  1 
ATOM   6043 N  N   . LYS B 2 143 ? 223.749 186.422 169.849 1.00 42.27  ? 471  LYS B N   1 
ATOM   6044 C  CA  . LYS B 2 143 ? 223.011 187.519 170.444 1.00 42.97  ? 471  LYS B CA  1 
ATOM   6045 C  C   . LYS B 2 143 ? 223.003 187.393 171.973 1.00 44.59  ? 471  LYS B C   1 
ATOM   6046 O  O   . LYS B 2 143 ? 222.724 186.317 172.497 1.00 43.96  ? 471  LYS B O   1 
ATOM   6047 C  CB  . LYS B 2 143 ? 221.585 187.539 169.898 1.00 41.03  ? 471  LYS B CB  1 
ATOM   6048 C  CG  . LYS B 2 143 ? 220.797 188.785 170.239 1.00 41.93  ? 471  LYS B CG  1 
ATOM   6049 C  CD  . LYS B 2 143 ? 219.471 188.814 169.506 1.00 41.29  ? 471  LYS B CD  1 
ATOM   6050 C  CE  . LYS B 2 143 ? 218.695 190.085 169.822 1.00 43.15  ? 471  LYS B CE  1 
ATOM   6051 N  NZ  . LYS B 2 143 ? 219.214 191.274 169.065 1.00 41.13  ? 471  LYS B NZ  1 
ATOM   6052 N  N   . PRO B 2 144 ? 223.352 188.470 172.696 1.00 45.14  ? 472  PRO B N   1 
ATOM   6053 C  CA  . PRO B 2 144 ? 223.345 188.587 174.146 1.00 47.01  ? 472  PRO B CA  1 
ATOM   6054 C  C   . PRO B 2 144 ? 221.924 188.719 174.683 1.00 48.60  ? 472  PRO B C   1 
ATOM   6055 O  O   . PRO B 2 144 ? 221.045 189.227 173.989 1.00 48.75  ? 472  PRO B O   1 
ATOM   6056 C  CB  . PRO B 2 144 ? 224.166 189.863 174.367 1.00 47.88  ? 472  PRO B CB  1 
ATOM   6057 C  CG  . PRO B 2 144 ? 223.940 190.679 173.113 1.00 47.69  ? 472  PRO B CG  1 
ATOM   6058 C  CD  . PRO B 2 144 ? 223.825 189.673 171.999 1.00 45.97  ? 472  PRO B CD  1 
ATOM   6059 N  N   . THR B 2 145 ? 221.709 188.314 175.935 1.00 49.39  ? 473  THR B N   1 
ATOM   6060 C  CA  . THR B 2 145 ? 220.396 188.476 176.559 1.00 50.67  ? 473  THR B CA  1 
ATOM   6061 C  C   . THR B 2 145 ? 220.309 189.756 177.373 1.00 52.72  ? 473  THR B C   1 
ATOM   6062 O  O   . THR B 2 145 ? 219.229 190.320 177.541 1.00 53.00  ? 473  THR B O   1 
ATOM   6063 C  CB  . THR B 2 145 ? 220.082 187.312 177.517 1.00 51.20  ? 473  THR B CB  1 
ATOM   6064 N  N   . TYR B 2 146 ? 221.444 190.183 177.916 1.00 52.94  ? 474  TYR B N   1 
ATOM   6065 C  CA  . TYR B 2 146 ? 221.496 191.322 178.824 1.00 54.22  ? 474  TYR B CA  1 
ATOM   6066 C  C   . TYR B 2 146 ? 220.584 191.130 180.033 1.00 55.49  ? 474  TYR B C   1 
ATOM   6067 O  O   . TYR B 2 146 ? 220.093 192.101 180.608 1.00 57.77  ? 474  TYR B O   1 
ATOM   6068 C  CB  . TYR B 2 146 ? 221.146 192.622 178.094 1.00 53.90  ? 474  TYR B CB  1 
ATOM   6069 C  CG  . TYR B 2 146 ? 222.190 193.056 177.093 1.00 54.38  ? 474  TYR B CG  1 
ATOM   6070 C  CD1 . TYR B 2 146 ? 223.429 193.467 177.545 1.00 54.54  ? 474  TYR B CD1 1 
ATOM   6071 C  CD2 . TYR B 2 146 ? 221.911 193.064 175.737 1.00 51.87  ? 474  TYR B CD2 1 
ATOM   6072 C  CE1 . TYR B 2 146 ? 224.394 193.879 176.654 1.00 54.46  ? 474  TYR B CE1 1 
ATOM   6073 C  CE2 . TYR B 2 146 ? 222.879 193.481 174.840 1.00 51.07  ? 474  TYR B CE2 1 
ATOM   6074 C  CZ  . TYR B 2 146 ? 224.118 193.885 175.298 1.00 51.35  ? 474  TYR B CZ  1 
ATOM   6075 O  OH  . TYR B 2 146 ? 225.086 194.298 174.411 1.00 51.55  ? 474  TYR B OH  1 
ATOM   6076 N  N   . ALA B 2 147 ? 220.386 189.874 180.437 1.00 56.23  ? 475  ALA B N   1 
ATOM   6077 C  CA  . ALA B 2 147 ? 219.602 189.577 181.631 1.00 58.52  ? 475  ALA B CA  1 
ATOM   6078 C  C   . ALA B 2 147 ? 220.346 190.049 182.870 1.00 58.46  ? 475  ALA B C   1 
ATOM   6079 O  O   . ALA B 2 147 ? 219.745 190.518 183.837 1.00 59.83  ? 475  ALA B O   1 
ATOM   6080 C  CB  . ALA B 2 147 ? 219.321 188.086 181.724 1.00 57.69  ? 475  ALA B CB  1 
ATOM   6081 N  N   . HIS B 2 148 ? 221.664 189.913 182.823 1.00 60.20  ? 476  HIS B N   1 
ATOM   6082 C  CA  . HIS B 2 148 ? 222.553 190.309 183.901 1.00 60.57  ? 476  HIS B CA  1 
ATOM   6083 C  C   . HIS B 2 148 ? 223.416 191.472 183.422 1.00 61.38  ? 476  HIS B C   1 
ATOM   6084 O  O   . HIS B 2 148 ? 223.590 191.645 182.216 1.00 60.61  ? 476  HIS B O   1 
ATOM   6085 C  CB  . HIS B 2 148 ? 223.439 189.124 184.309 1.00 61.58  ? 476  HIS B CB  1 
ATOM   6086 C  CG  . HIS B 2 148 ? 222.682 187.984 184.918 1.00 61.64  ? 476  HIS B CG  1 
ATOM   6087 N  ND1 . HIS B 2 148 ? 223.238 186.736 185.093 1.00 62.23  ? 476  HIS B ND1 1 
ATOM   6088 C  CD2 . HIS B 2 148 ? 221.420 187.905 185.403 1.00 61.47  ? 476  HIS B CD2 1 
ATOM   6089 C  CE1 . HIS B 2 148 ? 222.349 185.936 185.654 1.00 63.84  ? 476  HIS B CE1 1 
ATOM   6090 N  NE2 . HIS B 2 148 ? 221.239 186.621 185.852 1.00 62.19  ? 476  HIS B NE2 1 
ATOM   6091 N  N   . PRO B 2 149 ? 223.973 192.269 184.336 1.00 61.23  ? 477  PRO B N   1 
ATOM   6092 C  CA  . PRO B 2 149 ? 224.922 193.329 184.061 1.00 62.43  ? 477  PRO B CA  1 
ATOM   6093 C  C   . PRO B 2 149 ? 226.002 192.826 183.118 1.00 63.39  ? 477  PRO B C   1 
ATOM   6094 O  O   . PRO B 2 149 ? 226.662 191.823 183.397 1.00 63.03  ? 477  PRO B O   1 
ATOM   6095 C  CB  . PRO B 2 149 ? 225.458 193.620 185.466 1.00 63.58  ? 477  PRO B CB  1 
ATOM   6096 C  CG  . PRO B 2 149 ? 224.279 193.334 186.371 1.00 62.47  ? 477  PRO B CG  1 
ATOM   6097 C  CD  . PRO B 2 149 ? 223.586 192.141 185.746 1.00 61.35  ? 477  PRO B CD  1 
ATOM   6098 N  N   . THR B 2 150 ? 226.155 193.516 181.987 1.00 63.85  ? 478  THR B N   1 
ATOM   6099 C  CA  . THR B 2 150 ? 227.082 193.093 180.940 1.00 62.50  ? 478  THR B CA  1 
ATOM   6100 C  C   . THR B 2 150 ? 227.821 194.287 180.336 1.00 62.75  ? 478  THR B C   1 
ATOM   6101 O  O   . THR B 2 150 ? 227.244 195.369 180.204 1.00 63.00  ? 478  THR B O   1 
ATOM   6102 C  CB  . THR B 2 150 ? 226.318 192.334 179.821 1.00 63.33  ? 478  THR B CB  1 
ATOM   6103 N  N   . CYS B 2 151 ? 229.082 194.071 179.930 1.00 61.47  ? 479  CYS B N   1 
ATOM   6104 C  CA  . CYS B 2 151 ? 229.864 195.062 179.186 1.00 62.04  ? 479  CYS B CA  1 
ATOM   6105 C  C   . CYS B 2 151 ? 230.413 194.478 177.880 1.00 59.18  ? 479  CYS B C   1 
ATOM   6106 O  O   . CYS B 2 151 ? 230.781 193.303 177.801 1.00 59.85  ? 479  CYS B O   1 
ATOM   6107 C  CB  . CYS B 2 151 ? 231.009 195.634 180.041 1.00 65.27  ? 479  CYS B CB  1 
ATOM   6108 S  SG  . CYS B 2 151 ? 230.460 196.680 181.446 1.00 62.07  ? 479  CYS B SG  1 
ATOM   6109 N  N   . LEU B 2 152 ? 230.441 195.320 176.854 1.00 59.67  ? 480  LEU B N   1 
ATOM   6110 C  CA  . LEU B 2 152 ? 230.933 194.979 175.523 1.00 60.25  ? 480  LEU B CA  1 
ATOM   6111 C  C   . LEU B 2 152 ? 232.301 195.584 175.244 1.00 60.08  ? 480  LEU B C   1 
ATOM   6112 O  O   . LEU B 2 152 ? 232.496 196.796 175.348 1.00 57.25  ? 480  LEU B O   1 
ATOM   6113 C  CB  . LEU B 2 152 ? 229.942 195.476 174.461 1.00 58.22  ? 480  LEU B CB  1 
ATOM   6114 N  N   . ILE B 2 153 ? 233.242 194.735 174.857 1.00 58.29  ? 481  ILE B N   1 
ATOM   6115 C  CA  . ILE B 2 153 ? 234.585 195.174 174.510 1.00 59.36  ? 481  ILE B CA  1 
ATOM   6116 C  C   . ILE B 2 153 ? 234.921 194.758 173.084 1.00 57.13  ? 481  ILE B C   1 
ATOM   6117 O  O   . ILE B 2 153 ? 234.793 193.591 172.729 1.00 57.24  ? 481  ILE B O   1 
ATOM   6118 C  CB  . ILE B 2 153 ? 235.627 194.547 175.462 1.00 58.28  ? 481  ILE B CB  1 
ATOM   6119 N  N   . SER B 2 154 ? 235.410 195.699 172.285 1.00 57.65  ? 482  SER B N   1 
ATOM   6120 C  CA  . SER B 2 154 ? 235.912 195.353 170.957 1.00 60.01  ? 482  SER B CA  1 
ATOM   6121 C  C   . SER B 2 154 ? 237.324 195.907 170.810 1.00 56.77  ? 482  SER B C   1 
ATOM   6122 O  O   . SER B 2 154 ? 237.561 197.106 170.951 1.00 57.95  ? 482  SER B O   1 
ATOM   6123 C  CB  . SER B 2 154 ? 234.999 195.877 169.870 1.00 57.11  ? 482  SER B CB  1 
ATOM   6124 N  N   . ALA B 2 155 ? 238.271 194.995 170.595 1.00 58.87  ? 483  ALA B N   1 
ATOM   6125 C  CA  . ALA B 2 155 ? 239.684 195.346 170.670 1.00 59.48  ? 483  ALA B CA  1 
ATOM   6126 C  C   . ALA B 2 155 ? 240.538 194.397 169.837 1.00 58.31  ? 483  ALA B C   1 
ATOM   6127 O  O   . ALA B 2 155 ? 240.055 193.363 169.380 1.00 57.05  ? 483  ALA B O   1 
ATOM   6128 C  CB  . ALA B 2 155 ? 240.131 195.312 172.119 1.00 59.38  ? 483  ALA B CB  1 
ATOM   6129 N  N   . TYR B 2 156 ? 241.811 194.748 169.640 1.00 58.33  ? 484  TYR B N   1 
ATOM   6130 C  CA  . TYR B 2 156 ? 242.710 193.877 168.884 1.00 58.04  ? 484  TYR B CA  1 
ATOM   6131 C  C   . TYR B 2 156 ? 244.080 193.696 169.543 1.00 59.36  ? 484  TYR B C   1 
ATOM   6132 O  O   . TYR B 2 156 ? 244.531 194.533 170.327 1.00 56.17  ? 484  TYR B O   1 
ATOM   6133 C  CB  . TYR B 2 156 ? 242.875 194.393 167.453 1.00 58.14  ? 484  TYR B CB  1 
ATOM   6134 N  N   . THR B 2 157 ? 244.740 192.584 169.214 1.00 59.18  ? 485  THR B N   1 
ATOM   6135 C  CA  . THR B 2 157 ? 246.071 192.278 169.748 1.00 59.30  ? 485  THR B CA  1 
ATOM   6136 C  C   . THR B 2 157 ? 246.795 191.241 168.900 1.00 61.72  ? 485  THR B C   1 
ATOM   6137 O  O   . THR B 2 157 ? 246.175 190.513 168.131 1.00 59.19  ? 485  THR B O   1 
ATOM   6138 C  CB  . THR B 2 157 ? 245.995 191.747 171.185 1.00 61.03  ? 485  THR B CB  1 
ATOM   6139 N  N   . ASP B 2 158 ? 248.107 191.145 169.078 1.00 59.42  ? 486  ASP B N   1 
ATOM   6140 C  CA  . ASP B 2 158 ? 248.868 190.060 168.469 1.00 62.12  ? 486  ASP B CA  1 
ATOM   6141 C  C   . ASP B 2 158 ? 248.933 188.873 169.423 1.00 60.20  ? 486  ASP B C   1 
ATOM   6142 O  O   . ASP B 2 158 ? 249.632 188.915 170.436 1.00 63.06  ? 486  ASP B O   1 
ATOM   6143 C  CB  . ASP B 2 158 ? 250.278 190.512 168.097 1.00 60.36  ? 486  ASP B CB  1 
ATOM   6144 N  N   . LEU B 2 159 ? 248.163 187.832 169.124 1.00 58.72  ? 487  LEU B N   1 
ATOM   6145 C  CA  . LEU B 2 159 ? 248.016 186.708 170.034 1.00 59.14  ? 487  LEU B CA  1 
ATOM   6146 C  C   . LEU B 2 159 ? 249.182 185.735 169.944 1.00 65.49  ? 487  LEU B C   1 
ATOM   6147 O  O   . LEU B 2 159 ? 249.334 184.871 170.806 1.00 77.36  ? 487  LEU B O   1 
ATOM   6148 C  CB  . LEU B 2 159 ? 246.714 185.947 169.737 1.00 61.53  ? 487  LEU B CB  1 
ATOM   6149 N  N   . SER B 2 160 ? 249.992 185.843 168.893 1.00 59.23  ? 488  SER B N   1 
ATOM   6150 C  CA  . SER B 2 160 ? 251.040 184.846 168.690 1.00 62.85  ? 488  SER B CA  1 
ATOM   6151 C  C   . SER B 2 160 ? 252.074 184.921 169.802 1.00 61.80  ? 488  SER B C   1 
ATOM   6152 O  O   . SER B 2 160 ? 252.604 183.904 170.251 1.00 62.99  ? 488  SER B O   1 
ATOM   6153 C  CB  . SER B 2 160 ? 251.724 185.039 167.349 1.00 62.07  ? 488  SER B CB  1 
ATOM   6154 N  N   . ALA B 2 161 ? 252.301 186.130 170.299 1.00 62.34  ? 489  ALA B N   1 
ATOM   6155 C  CA  . ALA B 2 161 ? 253.288 186.358 171.342 1.00 62.49  ? 489  ALA B CA  1 
ATOM   6156 C  C   . ALA B 2 161 ? 252.735 185.983 172.708 1.00 62.67  ? 489  ALA B C   1 
ATOM   6157 O  O   . ALA B 2 161 ? 253.448 186.040 173.709 1.00 63.99  ? 489  ALA B O   1 
ATOM   6158 C  CB  . ALA B 2 161 ? 253.729 187.814 171.335 1.00 65.68  ? 489  ALA B CB  1 
ATOM   6159 N  N   . LEU B 2 162 ? 251.455 185.627 172.752 1.00 62.67  ? 490  LEU B N   1 
ATOM   6160 C  CA  . LEU B 2 162 ? 250.810 185.272 174.005 1.00 62.84  ? 490  LEU B CA  1 
ATOM   6161 C  C   . LEU B 2 162 ? 250.495 183.780 174.066 1.00 62.96  ? 490  LEU B C   1 
ATOM   6162 O  O   . LEU B 2 162 ? 249.829 183.316 174.992 1.00 62.49  ? 490  LEU B O   1 
ATOM   6163 C  CB  . LEU B 2 162 ? 249.539 186.110 174.181 1.00 64.70  ? 490  LEU B CB  1 
ATOM   6164 N  N   . GLY B 2 163 ? 251.000 183.024 173.091 1.00 62.55  ? 491  GLY B N   1 
ATOM   6165 C  CA  . GLY B 2 163 ? 250.819 181.574 173.070 1.00 64.45  ? 491  GLY B CA  1 
ATOM   6166 C  C   . GLY B 2 163 ? 249.627 181.121 172.227 1.00 62.73  ? 491  GLY B C   1 
ATOM   6167 O  O   . GLY B 2 163 ? 249.284 179.936 172.220 1.00 64.11  ? 491  GLY B O   1 
ATOM   6168 N  N   . GLY B 2 164 ? 248.998 182.055 171.521 1.00 61.59  ? 492  GLY B N   1 
ATOM   6169 C  CA  . GLY B 2 164 ? 247.856 181.736 170.673 1.00 62.25  ? 492  GLY B CA  1 
ATOM   6170 C  C   . GLY B 2 164 ? 248.202 181.915 169.203 1.00 62.21  ? 492  GLY B C   1 
ATOM   6171 O  O   . GLY B 2 164 ? 249.358 181.772 168.803 1.00 61.40  ? 492  GLY B O   1 
ATOM   6172 N  N   . SER B 2 165 ? 247.194 182.223 168.397 1.00 59.94  ? 493  SER B N   1 
ATOM   6173 C  CA  . SER B 2 165 ? 247.396 182.428 166.971 1.00 58.90  ? 493  SER B CA  1 
ATOM   6174 C  C   . SER B 2 165 ? 246.413 183.448 166.425 1.00 57.99  ? 493  SER B C   1 
ATOM   6175 O  O   . SER B 2 165 ? 245.300 183.588 166.931 1.00 56.89  ? 493  SER B O   1 
ATOM   6176 C  CB  . SER B 2 165 ? 247.247 181.115 166.227 1.00 59.10  ? 493  SER B CB  1 
ATOM   6177 N  N   . ASN B 2 166 ? 246.821 184.155 165.378 1.00 57.36  ? 494  ASN B N   1 
ATOM   6178 C  CA  . ASN B 2 166 ? 245.952 185.143 164.761 1.00 57.26  ? 494  ASN B CA  1 
ATOM   6179 C  C   . ASN B 2 166 ? 245.230 184.513 163.572 1.00 54.98  ? 494  ASN B C   1 
ATOM   6180 O  O   . ASN B 2 166 ? 245.820 183.699 162.861 1.00 54.32  ? 494  ASN B O   1 
ATOM   6181 C  CB  . ASN B 2 166 ? 246.759 186.354 164.324 1.00 56.72  ? 494  ASN B CB  1 
ATOM   6182 C  CG  . ASN B 2 166 ? 247.504 186.999 165.468 1.00 56.71  ? 494  ASN B CG  1 
ATOM   6183 O  OD1 . ASN B 2 166 ? 246.965 187.177 166.567 1.00 58.75  ? 494  ASN B OD1 1 
ATOM   6184 N  ND2 . ASN B 2 166 ? 248.745 187.343 165.225 1.00 59.98  ? 494  ASN B ND2 1 
ATOM   6185 N  N   . PRO B 2 167 ? 243.964 184.869 163.346 1.00 53.75  ? 495  PRO B N   1 
ATOM   6186 C  CA  . PRO B 2 167 ? 243.139 184.448 162.233 1.00 50.77  ? 495  PRO B CA  1 
ATOM   6187 C  C   . PRO B 2 167 ? 243.605 185.106 160.944 1.00 50.05  ? 495  PRO B C   1 
ATOM   6188 O  O   . PRO B 2 167 ? 244.113 186.227 160.963 1.00 50.42  ? 495  PRO B O   1 
ATOM   6189 C  CB  . PRO B 2 167 ? 241.747 184.926 162.657 1.00 50.78  ? 495  PRO B CB  1 
ATOM   6190 C  CG  . PRO B 2 167 ? 242.008 186.103 163.575 1.00 52.09  ? 495  PRO B CG  1 
ATOM   6191 C  CD  . PRO B 2 167 ? 243.303 185.772 164.287 1.00 54.49  ? 495  PRO B CD  1 
ATOM   6192 N  N   . THR B 2 168 ? 243.390 184.427 159.822 1.00 49.32  ? 496  THR B N   1 
ATOM   6193 C  CA  . THR B 2 168 ? 243.717 184.996 158.516 1.00 47.16  ? 496  THR B CA  1 
ATOM   6194 C  C   . THR B 2 168 ? 242.518 185.679 157.846 1.00 47.17  ? 496  THR B C   1 
ATOM   6195 O  O   . THR B 2 168 ? 242.697 186.544 156.988 1.00 46.17  ? 496  THR B O   1 
ATOM   6196 C  CB  . THR B 2 168 ? 244.293 183.911 157.589 1.00 47.53  ? 496  THR B CB  1 
ATOM   6197 N  N   . ASN B 2 169 ? 241.301 185.307 158.265 1.00 45.64  ? 497  ASN B N   1 
ATOM   6198 C  CA  . ASN B 2 169 ? 240.057 185.920 157.791 1.00 44.86  ? 497  ASN B CA  1 
ATOM   6199 C  C   . ASN B 2 169 ? 238.957 185.716 158.831 1.00 44.45  ? 497  ASN B C   1 
ATOM   6200 O  O   . ASN B 2 169 ? 239.116 184.936 159.765 1.00 44.73  ? 497  ASN B O   1 
ATOM   6201 C  CB  . ASN B 2 169 ? 239.657 185.361 156.429 1.00 43.42  ? 497  ASN B CB  1 
ATOM   6202 C  CG  . ASN B 2 169 ? 239.597 183.829 156.380 1.00 42.21  ? 497  ASN B CG  1 
ATOM   6203 O  OD1 . ASN B 2 169 ? 238.877 183.199 157.170 1.00 41.77  ? 497  ASN B OD1 1 
ATOM   6204 N  ND2 . ASN B 2 169 ? 240.337 183.231 155.467 1.00 41.90  ? 497  ASN B ND2 1 
ATOM   6205 N  N   . TYR B 2 170 ? 237.819 186.396 158.630 1.00 43.54  ? 498  TYR B N   1 
ATOM   6206 C  CA  . TYR B 2 170 ? 236.677 186.320 159.546 1.00 42.36  ? 498  TYR B CA  1 
ATOM   6207 C  C   . TYR B 2 170 ? 235.435 185.805 158.835 1.00 41.60  ? 498  TYR B C   1 
ATOM   6208 O  O   . TYR B 2 170 ? 235.092 186.279 157.753 1.00 40.63  ? 498  TYR B O   1 
ATOM   6209 C  CB  . TYR B 2 170 ? 236.423 187.702 160.145 1.00 44.32  ? 498  TYR B CB  1 
ATOM   6210 C  CG  . TYR B 2 170 ? 237.614 188.226 160.909 1.00 46.40  ? 498  TYR B CG  1 
ATOM   6211 C  CD1 . TYR B 2 170 ? 237.649 188.135 162.281 1.00 47.23  ? 498  TYR B CD1 1 
ATOM   6212 C  CD2 . TYR B 2 170 ? 238.692 188.771 160.224 1.00 46.54  ? 498  TYR B CD2 1 
ATOM   6213 C  CE1 . TYR B 2 170 ? 238.755 188.584 162.971 1.00 48.33  ? 498  TYR B CE1 1 
ATOM   6214 C  CE2 . TYR B 2 170 ? 239.796 189.210 160.916 1.00 48.20  ? 498  TYR B CE2 1 
ATOM   6215 C  CZ  . TYR B 2 170 ? 239.831 189.116 162.282 1.00 49.11  ? 498  TYR B CZ  1 
ATOM   6216 O  OH  . TYR B 2 170 ? 240.939 189.552 162.970 1.00 51.56  ? 498  TYR B OH  1 
ATOM   6217 N  N   . THR B 2 171 ? 234.756 184.836 159.444 1.00 40.04  ? 499  THR B N   1 
ATOM   6218 C  CA  . THR B 2 171 ? 233.579 184.244 158.817 1.00 37.54  ? 499  THR B CA  1 
ATOM   6219 C  C   . THR B 2 171 ? 232.343 184.351 159.695 1.00 37.43  ? 499  THR B C   1 
ATOM   6220 O  O   . THR B 2 171 ? 232.397 184.083 160.894 1.00 37.82  ? 499  THR B O   1 
ATOM   6221 C  CB  . THR B 2 171 ? 233.821 182.760 158.462 1.00 37.40  ? 499  THR B CB  1 
ATOM   6222 O  OG1 . THR B 2 171 ? 234.946 182.656 157.592 1.00 37.91  ? 499  THR B OG1 1 
ATOM   6223 C  CG2 . THR B 2 171 ? 232.601 182.171 157.752 1.00 35.34  ? 499  THR B CG2 1 
ATOM   6224 N  N   . LEU B 2 172 ? 231.223 184.718 159.086 1.00 35.91  ? 500  LEU B N   1 
ATOM   6225 C  CA  . LEU B 2 172 ? 229.942 184.741 159.783 1.00 34.99  ? 500  LEU B CA  1 
ATOM   6226 C  C   . LEU B 2 172 ? 228.841 184.181 158.896 1.00 34.03  ? 500  LEU B C   1 
ATOM   6227 O  O   . LEU B 2 172 ? 228.925 184.252 157.670 1.00 33.68  ? 500  LEU B O   1 
ATOM   6228 C  CB  . LEU B 2 172 ? 229.568 186.164 160.220 1.00 35.08  ? 500  LEU B CB  1 
ATOM   6229 C  CG  . LEU B 2 172 ? 228.954 187.079 159.136 1.00 34.79  ? 500  LEU B CG  1 
ATOM   6230 C  CD1 . LEU B 2 172 ? 228.124 188.163 159.812 1.00 34.74  ? 500  LEU B CD1 1 
ATOM   6231 C  CD2 . LEU B 2 172 ? 230.060 187.685 158.292 1.00 36.56  ? 500  LEU B CD2 1 
ATOM   6232 N  N   . LEU B 2 173 ? 227.794 183.655 159.511 1.00 33.19  ? 501  LEU B N   1 
ATOM   6233 C  CA  . LEU B 2 173 ? 226.621 183.240 158.758 1.00 32.72  ? 501  LEU B CA  1 
ATOM   6234 C  C   . LEU B 2 173 ? 225.808 184.459 158.355 1.00 32.48  ? 501  LEU B C   1 
ATOM   6235 O  O   . LEU B 2 173 ? 225.555 185.340 159.177 1.00 32.24  ? 501  LEU B O   1 
ATOM   6236 C  CB  . LEU B 2 173 ? 225.756 182.302 159.606 1.00 31.97  ? 501  LEU B CB  1 
ATOM   6237 C  CG  . LEU B 2 173 ? 226.398 180.968 160.001 1.00 32.39  ? 501  LEU B CG  1 
ATOM   6238 C  CD1 . LEU B 2 173 ? 225.548 180.303 161.068 1.00 31.65  ? 501  LEU B CD1 1 
ATOM   6239 C  CD2 . LEU B 2 173 ? 226.509 180.071 158.771 1.00 30.96  ? 501  LEU B CD2 1 
ATOM   6240 N  N   . THR B 2 174 ? 225.379 184.506 157.098 1.00 30.89  ? 502  THR B N   1 
ATOM   6241 C  CA  . THR B 2 174 ? 224.554 185.613 156.628 1.00 30.63  ? 502  THR B CA  1 
ATOM   6242 C  C   . THR B 2 174 ? 223.118 185.166 156.415 1.00 29.19  ? 502  THR B C   1 
ATOM   6243 O  O   . THR B 2 174 ? 222.202 185.985 156.372 1.00 28.91  ? 502  THR B O   1 
ATOM   6244 C  CB  . THR B 2 174 ? 225.114 186.227 155.334 1.00 30.87  ? 502  THR B CB  1 
ATOM   6245 O  OG1 . THR B 2 174 ? 225.120 185.246 154.292 1.00 30.47  ? 502  THR B OG1 1 
ATOM   6246 C  CG2 . THR B 2 174 ? 226.532 186.719 155.569 1.00 32.76  ? 502  THR B CG2 1 
ATOM   6247 N  N   . ASN B 2 175 ? 222.920 183.859 156.305 1.00 28.62  ? 503  ASN B N   1 
ATOM   6248 C  CA  . ASN B 2 175 ? 221.574 183.310 156.223 1.00 27.11  ? 503  ASN B CA  1 
ATOM   6249 C  C   . ASN B 2 175 ? 221.557 181.839 156.621 1.00 26.39  ? 503  ASN B C   1 
ATOM   6250 O  O   . ASN B 2 175 ? 222.556 181.136 156.455 1.00 26.44  ? 503  ASN B O   1 
ATOM   6251 C  CB  . ASN B 2 175 ? 220.990 183.502 154.832 1.00 26.75  ? 503  ASN B CB  1 
ATOM   6252 C  CG  . ASN B 2 175 ? 219.483 183.438 154.828 1.00 25.05  ? 503  ASN B CG  1 
ATOM   6253 O  OD1 . ASN B 2 175 ? 218.859 183.151 155.859 1.00 25.05  ? 503  ASN B OD1 1 
ATOM   6254 N  ND2 . ASN B 2 175 ? 218.890 183.703 153.694 1.00 25.44  ? 503  ASN B ND2 1 
ATOM   6255 N  N   . CYS B 2 176 ? 220.404 181.379 157.099 1.00 25.35  ? 504  CYS B N   1 
ATOM   6256 C  CA  . CYS B 2 176 ? 220.126 179.974 157.388 1.00 23.61  ? 504  CYS B CA  1 
ATOM   6257 C  C   . CYS B 2 176 ? 218.628 179.758 157.478 1.00 22.13  ? 504  CYS B C   1 
ATOM   6258 O  O   . CYS B 2 176 ? 217.917 180.549 158.129 1.00 22.19  ? 504  CYS B O   1 
ATOM   6259 C  CB  . CYS B 2 176 ? 220.814 179.522 158.689 1.00 24.41  ? 504  CYS B CB  1 
ATOM   6260 S  SG  . CYS B 2 176 ? 220.794 177.714 158.965 1.00 24.09  ? 504  CYS B SG  1 
ATOM   6261 N  N   . TYR B 2 177 ? 218.121 178.737 156.809 1.00 21.22  ? 505  TYR B N   1 
ATOM   6262 C  CA  . TYR B 2 177 ? 216.691 178.468 156.733 1.00 19.90  ? 505  TYR B CA  1 
ATOM   6263 C  C   . TYR B 2 177 ? 216.388 176.988 156.544 1.00 19.58  ? 505  TYR B C   1 
ATOM   6264 O  O   . TYR B 2 177 ? 217.246 176.214 156.114 1.00 19.96  ? 505  TYR B O   1 
ATOM   6265 C  CB  . TYR B 2 177 ? 216.059 179.309 155.622 1.00 18.72  ? 505  TYR B CB  1 
ATOM   6266 C  CG  . TYR B 2 177 ? 216.788 179.241 154.303 1.00 19.11  ? 505  TYR B CG  1 
ATOM   6267 C  CD1 . TYR B 2 177 ? 216.442 178.310 153.339 1.00 18.30  ? 505  TYR B CD1 1 
ATOM   6268 C  CD2 . TYR B 2 177 ? 217.811 180.137 154.062 1.00 20.61  ? 505  TYR B CD2 1 
ATOM   6269 C  CE1 . TYR B 2 177 ? 217.124 178.286 152.141 1.00 18.64  ? 505  TYR B CE1 1 
ATOM   6270 C  CE2 . TYR B 2 177 ? 218.491 180.108 152.874 1.00 20.64  ? 505  TYR B CE2 1 
ATOM   6271 C  CZ  . TYR B 2 177 ? 218.151 179.191 151.915 1.00 20.04  ? 505  TYR B CZ  1 
ATOM   6272 O  OH  . TYR B 2 177 ? 218.836 179.166 150.726 1.00 20.32  ? 505  TYR B OH  1 
ATOM   6273 N  N   . GLY B 2 178 ? 215.176 176.591 156.914 1.00 18.10  ? 506  GLY B N   1 
ATOM   6274 C  CA  . GLY B 2 178 ? 214.789 175.184 156.925 1.00 17.82  ? 506  GLY B CA  1 
ATOM   6275 C  C   . GLY B 2 178 ? 214.451 174.623 155.545 1.00 17.54  ? 506  GLY B C   1 
ATOM   6276 O  O   . GLY B 2 178 ? 214.213 175.370 154.600 1.00 17.41  ? 506  GLY B O   1 
ATOM   6277 N  N   . CYS B 2 179 ? 214.415 173.277 155.494 1.00 17.57  ? 507  CYS B N   1 
ATOM   6278 C  CA  . CYS B 2 179 ? 214.046 172.541 154.252 1.00 17.00  ? 507  CYS B CA  1 
ATOM   6279 C  C   . CYS B 2 179 ? 213.061 171.418 154.624 1.00 16.50  ? 507  CYS B C   1 
ATOM   6280 O  O   . CYS B 2 179 ? 213.186 170.739 155.596 1.00 16.92  ? 507  CYS B O   1 
ATOM   6281 C  CB  . CYS B 2 179 ? 215.305 171.894 153.643 1.00 17.88  ? 507  CYS B CB  1 
ATOM   6282 S  SG  . CYS B 2 179 ? 216.640 173.062 153.228 1.00 18.81  ? 507  CYS B SG  1 
ATOM   6283 N  N   . VAL B 2 180 ? 212.112 171.202 153.688 1.00 16.40  ? 508  VAL B N   1 
ATOM   6284 C  CA  . VAL B 2 180 ? 211.122 170.141 153.881 1.00 15.60  ? 508  VAL B CA  1 
ATOM   6285 C  C   . VAL B 2 180 ? 211.282 169.005 152.873 1.00 15.77  ? 508  VAL B C   1 
ATOM   6286 O  O   . VAL B 2 180 ? 211.589 169.238 151.704 1.00 16.65  ? 508  VAL B O   1 
ATOM   6287 C  CB  . VAL B 2 180 ? 209.701 170.727 153.769 1.00 13.50  ? 508  VAL B CB  1 
ATOM   6288 C  CG1 . VAL B 2 180 ? 209.461 171.707 154.895 1.00 13.21  ? 508  VAL B CG1 1 
ATOM   6289 C  CG2 . VAL B 2 180 ? 209.519 171.417 152.422 1.00 13.16  ? 508  VAL B CG2 1 
ATOM   6290 N  N   . GLY B 2 181 ? 211.064 167.773 153.334 1.00 15.26  ? 509  GLY B N   1 
ATOM   6291 C  CA  . GLY B 2 181 ? 211.147 166.603 152.469 1.00 16.83  ? 509  GLY B CA  1 
ATOM   6292 C  C   . GLY B 2 181 ? 212.555 166.026 152.429 1.00 18.87  ? 509  GLY B C   1 
ATOM   6293 O  O   . GLY B 2 181 ? 213.517 166.666 152.853 1.00 19.29  ? 509  GLY B O   1 
ATOM   6294 N  N   . GLN B 2 182 ? 212.672 164.811 151.907 1.00 19.73  ? 510  GLN B N   1 
ATOM   6295 C  CA  . GLN B 2 182 ? 213.967 164.163 151.751 1.00 20.65  ? 510  GLN B CA  1 
ATOM   6296 C  C   . GLN B 2 182 ? 214.326 164.110 150.268 1.00 21.08  ? 510  GLN B C   1 
ATOM   6297 O  O   . GLN B 2 182 ? 213.431 164.112 149.424 1.00 20.64  ? 510  GLN B O   1 
ATOM   6298 C  CB  . GLN B 2 182 ? 213.933 162.749 152.342 1.00 20.92  ? 510  GLN B CB  1 
ATOM   6299 C  CG  . GLN B 2 182 ? 213.612 162.696 153.825 1.00 21.37  ? 510  GLN B CG  1 
ATOM   6300 C  CD  . GLN B 2 182 ? 214.686 163.343 154.686 1.00 21.90  ? 510  GLN B CD  1 
ATOM   6301 O  OE1 . GLN B 2 182 ? 215.886 163.104 154.500 1.00 22.30  ? 510  GLN B OE1 1 
ATOM   6302 N  NE2 . GLN B 2 182 ? 214.254 164.153 155.643 1.00 22.06  ? 510  GLN B NE2 1 
ATOM   6303 N  N   . PRO B 2 183 ? 215.614 164.044 149.922 1.00 20.94  ? 511  PRO B N   1 
ATOM   6304 C  CA  . PRO B 2 183 ? 216.121 163.882 148.575 1.00 21.39  ? 511  PRO B CA  1 
ATOM   6305 C  C   . PRO B 2 183 ? 215.468 162.677 147.909 1.00 21.67  ? 511  PRO B C   1 
ATOM   6306 O  O   . PRO B 2 183 ? 215.220 161.668 148.565 1.00 21.60  ? 511  PRO B O   1 
ATOM   6307 C  CB  . PRO B 2 183 ? 217.617 163.654 148.817 1.00 21.87  ? 511  PRO B CB  1 
ATOM   6308 C  CG  . PRO B 2 183 ? 217.900 164.381 150.111 1.00 21.68  ? 511  PRO B CG  1 
ATOM   6309 C  CD  . PRO B 2 183 ? 216.656 164.182 150.951 1.00 21.34  ? 511  PRO B CD  1 
ATOM   6310 N  N   . PRO B 2 184 ? 215.195 162.773 146.608 1.00 21.75  ? 512  PRO B N   1 
ATOM   6311 C  CA  . PRO B 2 184 ? 215.421 163.872 145.682 1.00 21.62  ? 512  PRO B CA  1 
ATOM   6312 C  C   . PRO B 2 184 ? 214.287 164.896 145.664 1.00 21.39  ? 512  PRO B C   1 
ATOM   6313 O  O   . PRO B 2 184 ? 214.165 165.670 144.716 1.00 21.50  ? 512  PRO B O   1 
ATOM   6314 C  CB  . PRO B 2 184 ? 215.501 163.121 144.353 1.00 22.04  ? 512  PRO B CB  1 
ATOM   6315 C  CG  . PRO B 2 184 ? 214.505 161.991 144.518 1.00 22.07  ? 512  PRO B CG  1 
ATOM   6316 C  CD  . PRO B 2 184 ? 214.615 161.584 145.986 1.00 21.86  ? 512  PRO B CD  1 
ATOM   6317 N  N   . LYS B 2 185 ? 213.430 164.872 146.683 1.00 21.26  ? 513  LYS B N   1 
ATOM   6318 C  CA  . LYS B 2 185 ? 212.258 165.740 146.724 1.00 20.89  ? 513  LYS B CA  1 
ATOM   6319 C  C   . LYS B 2 185 ? 212.404 166.823 147.785 1.00 19.77  ? 513  LYS B C   1 
ATOM   6320 O  O   . LYS B 2 185 ? 211.417 167.416 148.221 1.00 19.24  ? 513  LYS B O   1 
ATOM   6321 C  CB  . LYS B 2 185 ? 210.998 164.922 146.987 1.00 21.35  ? 513  LYS B CB  1 
ATOM   6322 C  CG  . LYS B 2 185 ? 210.656 163.924 145.891 1.00 21.98  ? 513  LYS B CG  1 
ATOM   6323 C  CD  . LYS B 2 185 ? 209.357 163.192 146.202 1.00 22.89  ? 513  LYS B CD  1 
ATOM   6324 C  CE  . LYS B 2 185 ? 208.996 162.201 145.108 1.00 24.23  ? 513  LYS B CE  1 
ATOM   6325 N  NZ  . LYS B 2 185 ? 207.749 161.457 145.430 1.00 23.84  ? 513  LYS B NZ  1 
ATOM   6326 N  N   . ARG B 2 186 ? 213.640 167.070 148.197 1.00 19.72  ? 514  ARG B N   1 
ATOM   6327 C  CA  . ARG B 2 186 ? 213.922 168.073 149.212 1.00 18.98  ? 514  ARG B CA  1 
ATOM   6328 C  C   . ARG B 2 186 ? 213.815 169.482 148.646 1.00 17.89  ? 514  ARG B C   1 
ATOM   6329 O  O   . ARG B 2 186 ? 214.464 169.824 147.659 1.00 17.96  ? 514  ARG B O   1 
ATOM   6330 C  CB  . ARG B 2 186 ? 215.319 167.867 149.768 1.00 19.77  ? 514  ARG B CB  1 
ATOM   6331 C  CG  . ARG B 2 186 ? 215.710 168.783 150.910 1.00 19.34  ? 514  ARG B CG  1 
ATOM   6332 C  CD  . ARG B 2 186 ? 217.097 168.505 151.349 1.00 20.50  ? 514  ARG B CD  1 
ATOM   6333 N  NE  . ARG B 2 186 ? 218.059 168.867 150.324 1.00 20.97  ? 514  ARG B NE  1 
ATOM   6334 C  CZ  . ARG B 2 186 ? 219.283 168.323 150.179 1.00 21.77  ? 514  ARG B CZ  1 
ATOM   6335 N  NH1 . ARG B 2 186 ? 219.695 167.385 150.996 1.00 22.12  ? 514  ARG B NH1 1 
ATOM   6336 N  NH2 . ARG B 2 186 ? 220.073 168.739 149.206 1.00 21.86  ? 514  ARG B NH2 1 
ATOM   6337 N  N   . THR B 2 187 ? 212.988 170.294 149.289 1.00 17.22  ? 515  THR B N   1 
ATOM   6338 C  CA  . THR B 2 187 ? 212.761 171.671 148.864 1.00 16.64  ? 515  THR B CA  1 
ATOM   6339 C  C   . THR B 2 187 ? 213.100 172.645 149.996 1.00 16.36  ? 515  THR B C   1 
ATOM   6340 O  O   . THR B 2 187 ? 212.585 172.512 151.107 1.00 16.20  ? 515  THR B O   1 
ATOM   6341 C  CB  . THR B 2 187 ? 211.291 171.858 148.437 1.00 15.01  ? 515  THR B CB  1 
ATOM   6342 O  OG1 . THR B 2 187 ? 210.982 170.960 147.374 1.00 15.74  ? 515  THR B OG1 1 
ATOM   6343 C  CG2 . THR B 2 187 ? 211.053 173.276 147.965 1.00 13.68  ? 515  THR B CG2 1 
ATOM   6344 N  N   . CYS B 2 188 ? 213.989 173.610 149.733 1.00 16.41  ? 516  CYS B N   1 
ATOM   6345 C  CA  . CYS B 2 188 ? 214.439 174.563 150.749 1.00 16.37  ? 516  CYS B CA  1 
ATOM   6346 C  C   . CYS B 2 188 ? 213.744 175.914 150.604 1.00 15.87  ? 516  CYS B C   1 
ATOM   6347 O  O   . CYS B 2 188 ? 213.621 176.464 149.504 1.00 15.83  ? 516  CYS B O   1 
ATOM   6348 C  CB  . CYS B 2 188 ? 215.964 174.718 150.717 1.00 17.88  ? 516  CYS B CB  1 
ATOM   6349 S  SG  . CYS B 2 188 ? 216.860 173.193 151.158 1.00 18.85  ? 516  CYS B SG  1 
ATOM   6350 N  N   . LEU B 2 189 ? 213.245 176.424 151.723 1.00 15.69  ? 517  LEU B N   1 
ATOM   6351 C  CA  . LEU B 2 189 ? 212.380 177.604 151.764 1.00 15.08  ? 517  LEU B CA  1 
ATOM   6352 C  C   . LEU B 2 189 ? 212.980 178.746 152.563 1.00 15.46  ? 517  LEU B C   1 
ATOM   6353 O  O   . LEU B 2 189 ? 213.244 178.610 153.759 1.00 15.63  ? 517  LEU B O   1 
ATOM   6354 C  CB  . LEU B 2 189 ? 211.027 177.229 152.397 1.00 14.34  ? 517  LEU B CB  1 
ATOM   6355 C  CG  . LEU B 2 189 ? 209.912 176.453 151.526 1.00 12.98  ? 517  LEU B CG  1 
ATOM   6356 C  CD1 . LEU B 2 189 ? 210.577 175.914 150.290 1.00 13.57  ? 517  LEU B CD1 1 
ATOM   6357 C  CD2 . LEU B 2 189 ? 209.035 175.818 152.574 1.00 11.24  ? 517  LEU B CD2 1 
ATOM   6358 N  N   . GLU B 2 190 ? 213.203 179.875 151.916 1.00 15.26  ? 518  GLU B N   1 
ATOM   6359 C  CA  . GLU B 2 190 ? 213.816 181.040 152.553 1.00 15.73  ? 518  GLU B CA  1 
ATOM   6360 C  C   . GLU B 2 190 ? 212.832 181.707 153.498 1.00 14.87  ? 518  GLU B C   1 
ATOM   6361 O  O   . GLU B 2 190 ? 213.200 182.561 154.300 1.00 15.37  ? 518  GLU B O   1 
ATOM   6362 C  CB  . GLU B 2 190 ? 214.279 182.044 151.507 1.00 16.11  ? 518  GLU B CB  1 
ATOM   6363 C  CG  . GLU B 2 190 ? 215.389 181.532 150.590 1.00 17.20  ? 518  GLU B CG  1 
ATOM   6364 C  CD  . GLU B 2 190 ? 215.767 182.524 149.529 1.00 18.25  ? 518  GLU B CD  1 
ATOM   6365 O  OE1 . GLU B 2 190 ? 215.278 183.634 149.572 1.00 18.01  ? 518  GLU B OE1 1 
ATOM   6366 O  OE2 . GLU B 2 190 ? 216.529 182.173 148.669 1.00 18.59  ? 518  GLU B OE2 1 
ATOM   6367 N  N   . GLU B 2 191 ? 211.576 181.287 153.405 1.00 14.47  ? 519  GLU B N   1 
ATOM   6368 C  CA  . GLU B 2 191 ? 210.498 181.825 154.217 1.00 13.99  ? 519  GLU B CA  1 
ATOM   6369 C  C   . GLU B 2 191 ? 210.477 181.227 155.614 1.00 14.15  ? 519  GLU B C   1 
ATOM   6370 O  O   . GLU B 2 191 ? 209.704 181.664 156.464 1.00 13.49  ? 519  GLU B O   1 
ATOM   6371 C  CB  . GLU B 2 191 ? 209.166 181.582 153.514 1.00 12.29  ? 519  GLU B CB  1 
ATOM   6372 C  CG  . GLU B 2 191 ? 209.022 182.325 152.197 1.00 11.10  ? 519  GLU B CG  1 
ATOM   6373 C  CD  . GLU B 2 191 ? 209.832 181.726 151.086 1.00 12.26  ? 519  GLU B CD  1 
ATOM   6374 O  OE1 . GLU B 2 191 ? 210.157 180.563 151.169 1.00 13.03  ? 519  GLU B OE1 1 
ATOM   6375 O  OE2 . GLU B 2 191 ? 210.141 182.433 150.160 1.00 12.25  ? 519  GLU B OE2 1 
ATOM   6376 N  N   . PHE B 2 192 ? 211.335 180.238 155.855 1.00 14.80  ? 520  PHE B N   1 
ATOM   6377 C  CA  . PHE B 2 192 ? 211.447 179.617 157.173 1.00 15.23  ? 520  PHE B CA  1 
ATOM   6378 C  C   . PHE B 2 192 ? 212.842 179.797 157.759 1.00 16.43  ? 520  PHE B C   1 
ATOM   6379 O  O   . PHE B 2 192 ? 213.600 178.825 157.846 1.00 17.30  ? 520  PHE B O   1 
ATOM   6380 C  CB  . PHE B 2 192 ? 211.162 178.111 157.107 1.00 14.58  ? 520  PHE B CB  1 
ATOM   6381 C  CG  . PHE B 2 192 ? 209.754 177.686 156.779 1.00 13.47  ? 520  PHE B CG  1 
ATOM   6382 C  CD1 . PHE B 2 192 ? 209.526 176.410 156.296 1.00 13.05  ? 520  PHE B CD1 1 
ATOM   6383 C  CD2 . PHE B 2 192 ? 208.659 178.521 156.977 1.00 12.38  ? 520  PHE B CD2 1 
ATOM   6384 C  CE1 . PHE B 2 192 ? 208.253 175.975 156.015 1.00 11.94  ? 520  PHE B CE1 1 
ATOM   6385 C  CE2 . PHE B 2 192 ? 207.383 178.084 156.693 1.00 11.33  ? 520  PHE B CE2 1 
ATOM   6386 C  CZ  . PHE B 2 192 ? 207.182 176.807 156.214 1.00 10.91  ? 520  PHE B CZ  1 
ATOM   6387 N  N   . PRO B 2 193 ? 213.212 181.018 158.169 1.00 17.45  ? 521  PRO B N   1 
ATOM   6388 C  CA  . PRO B 2 193 ? 214.524 181.396 158.649 1.00 18.84  ? 521  PRO B CA  1 
ATOM   6389 C  C   . PRO B 2 193 ? 214.808 180.753 159.992 1.00 20.11  ? 521  PRO B C   1 
ATOM   6390 O  O   . PRO B 2 193 ? 213.901 180.570 160.804 1.00 20.45  ? 521  PRO B O   1 
ATOM   6391 C  CB  . PRO B 2 193 ? 214.413 182.919 158.763 1.00 20.12  ? 521  PRO B CB  1 
ATOM   6392 C  CG  . PRO B 2 193 ? 212.940 183.178 158.985 1.00 17.85  ? 521  PRO B CG  1 
ATOM   6393 C  CD  . PRO B 2 193 ? 212.230 182.106 158.187 1.00 16.45  ? 521  PRO B CD  1 
ATOM   6394 N  N   . SER B 2 194 ? 216.071 180.455 160.243 1.00 21.22  ? 522  SER B N   1 
ATOM   6395 C  CA  . SER B 2 194 ? 216.485 179.925 161.532 1.00 22.71  ? 522  SER B CA  1 
ATOM   6396 C  C   . SER B 2 194 ? 217.319 180.945 162.277 1.00 24.92  ? 522  SER B C   1 
ATOM   6397 O  O   . SER B 2 194 ? 218.486 181.161 161.961 1.00 25.73  ? 522  SER B O   1 
ATOM   6398 C  CB  . SER B 2 194 ? 217.279 178.648 161.347 1.00 23.10  ? 522  SER B CB  1 
ATOM   6399 O  OG  . SER B 2 194 ? 217.782 178.186 162.572 1.00 24.62  ? 522  SER B OG  1 
ATOM   6400 N  N   . PHE B 2 195 ? 216.711 181.576 163.269 1.00 25.65  ? 523  PHE B N   1 
ATOM   6401 C  CA  . PHE B 2 195 ? 217.382 182.628 164.014 1.00 27.42  ? 523  PHE B CA  1 
ATOM   6402 C  C   . PHE B 2 195 ? 218.028 182.061 165.262 1.00 29.70  ? 523  PHE B C   1 
ATOM   6403 O  O   . PHE B 2 195 ? 217.541 181.082 165.830 1.00 30.34  ? 523  PHE B O   1 
ATOM   6404 C  CB  . PHE B 2 195 ? 216.399 183.735 164.391 1.00 27.43  ? 523  PHE B CB  1 
ATOM   6405 C  CG  . PHE B 2 195 ? 215.855 184.490 163.211 1.00 25.41  ? 523  PHE B CG  1 
ATOM   6406 C  CD1 . PHE B 2 195 ? 214.488 184.575 162.995 1.00 23.11  ? 523  PHE B CD1 1 
ATOM   6407 C  CD2 . PHE B 2 195 ? 216.706 185.104 162.309 1.00 26.41  ? 523  PHE B CD2 1 
ATOM   6408 C  CE1 . PHE B 2 195 ? 213.989 185.262 161.910 1.00 20.87  ? 523  PHE B CE1 1 
ATOM   6409 C  CE2 . PHE B 2 195 ? 216.209 185.787 161.224 1.00 26.20  ? 523  PHE B CE2 1 
ATOM   6410 C  CZ  . PHE B 2 195 ? 214.848 185.868 161.024 1.00 24.53  ? 523  PHE B CZ  1 
ATOM   6411 N  N   . VAL B 2 196 ? 219.122 182.671 165.689 1.00 31.23  ? 524  VAL B N   1 
ATOM   6412 C  CA  . VAL B 2 196 ? 219.770 182.260 166.924 1.00 33.51  ? 524  VAL B CA  1 
ATOM   6413 C  C   . VAL B 2 196 ? 219.026 182.848 168.114 1.00 34.89  ? 524  VAL B C   1 
ATOM   6414 O  O   . VAL B 2 196 ? 218.648 184.020 168.103 1.00 35.12  ? 524  VAL B O   1 
ATOM   6415 C  CB  . VAL B 2 196 ? 221.250 182.703 166.946 1.00 33.82  ? 524  VAL B CB  1 
ATOM   6416 C  CG1 . VAL B 2 196 ? 221.365 184.223 167.062 1.00 35.00  ? 524  VAL B CG1 1 
ATOM   6417 C  CG2 . VAL B 2 196 ? 221.972 182.027 168.103 1.00 35.62  ? 524  VAL B CG2 1 
ATOM   6418 N  N   . GLU B 2 197 ? 218.810 182.035 169.137 1.00 36.59  ? 525  GLU B N   1 
ATOM   6419 C  CA  . GLU B 2 197 ? 218.169 182.517 170.349 1.00 38.60  ? 525  GLU B CA  1 
ATOM   6420 C  C   . GLU B 2 197 ? 219.186 183.249 171.206 1.00 39.47  ? 525  GLU B C   1 
ATOM   6421 O  O   . GLU B 2 197 ? 220.338 182.829 171.298 1.00 39.45  ? 525  GLU B O   1 
ATOM   6422 C  CB  . GLU B 2 197 ? 217.549 181.359 171.128 1.00 39.39  ? 525  GLU B CB  1 
ATOM   6423 N  N   . ALA B 2 198 ? 218.771 184.344 171.829 1.00 40.12  ? 526  ALA B N   1 
ATOM   6424 C  CA  . ALA B 2 198 ? 219.696 185.095 172.660 1.00 42.48  ? 526  ALA B CA  1 
ATOM   6425 C  C   . ALA B 2 198 ? 220.221 184.215 173.782 1.00 42.63  ? 526  ALA B C   1 
ATOM   6426 O  O   . ALA B 2 198 ? 219.452 183.552 174.479 1.00 42.82  ? 526  ALA B O   1 
ATOM   6427 C  CB  . ALA B 2 198 ? 219.021 186.339 173.219 1.00 43.16  ? 526  ALA B CB  1 
ATOM   6428 N  N   . GLY B 2 199 ? 221.537 184.220 173.961 1.00 43.02  ? 527  GLY B N   1 
ATOM   6429 C  CA  . GLY B 2 199 ? 222.186 183.432 175.001 1.00 41.83  ? 527  GLY B CA  1 
ATOM   6430 C  C   . GLY B 2 199 ? 222.507 182.002 174.561 1.00 42.24  ? 527  GLY B C   1 
ATOM   6431 O  O   . GLY B 2 199 ? 223.026 181.212 175.352 1.00 41.70  ? 527  GLY B O   1 
ATOM   6432 N  N   . TYR B 2 200 ? 222.189 181.663 173.312 1.00 41.09  ? 528  TYR B N   1 
ATOM   6433 C  CA  . TYR B 2 200 ? 222.383 180.304 172.808 1.00 40.31  ? 528  TYR B CA  1 
ATOM   6434 C  C   . TYR B 2 200 ? 223.245 180.251 171.556 1.00 39.01  ? 528  TYR B C   1 
ATOM   6435 O  O   . TYR B 2 200 ? 223.383 181.242 170.838 1.00 39.28  ? 528  TYR B O   1 
ATOM   6436 C  CB  . TYR B 2 200 ? 221.033 179.649 172.521 1.00 39.74  ? 528  TYR B CB  1 
ATOM   6437 C  CG  . TYR B 2 200 ? 220.203 179.427 173.749 1.00 41.53  ? 528  TYR B CG  1 
ATOM   6438 C  CD1 . TYR B 2 200 ? 219.299 180.388 174.156 1.00 41.34  ? 528  TYR B CD1 1 
ATOM   6439 C  CD2 . TYR B 2 200 ? 220.350 178.259 174.473 1.00 41.31  ? 528  TYR B CD2 1 
ATOM   6440 C  CE1 . TYR B 2 200 ? 218.542 180.184 175.289 1.00 42.02  ? 528  TYR B CE1 1 
ATOM   6441 C  CE2 . TYR B 2 200 ? 219.594 178.053 175.604 1.00 41.63  ? 528  TYR B CE2 1 
ATOM   6442 C  CZ  . TYR B 2 200 ? 218.692 179.010 176.013 1.00 42.28  ? 528  TYR B CZ  1 
ATOM   6443 O  OH  . TYR B 2 200 ? 217.938 178.805 177.145 1.00 42.97  ? 528  TYR B OH  1 
ATOM   6444 N  N   . ARG B 2 201 ? 223.822 179.084 171.296 1.00 38.70  ? 529  ARG B N   1 
ATOM   6445 C  CA  . ARG B 2 201 ? 224.558 178.839 170.061 1.00 37.55  ? 529  ARG B CA  1 
ATOM   6446 C  C   . ARG B 2 201 ? 223.567 178.500 168.938 1.00 36.71  ? 529  ARG B C   1 
ATOM   6447 O  O   . ARG B 2 201 ? 222.490 177.971 169.219 1.00 36.00  ? 529  ARG B O   1 
ATOM   6448 C  CB  . ARG B 2 201 ? 225.561 177.708 170.259 1.00 37.92  ? 529  ARG B CB  1 
ATOM   6449 C  CG  . ARG B 2 201 ? 226.746 177.725 169.303 1.00 38.02  ? 529  ARG B CG  1 
ATOM   6450 C  CD  . ARG B 2 201 ? 227.905 176.981 169.824 1.00 39.35  ? 529  ARG B CD  1 
ATOM   6451 N  NE  . ARG B 2 201 ? 228.504 177.657 170.960 1.00 41.04  ? 529  ARG B NE  1 
ATOM   6452 C  CZ  . ARG B 2 201 ? 229.585 177.221 171.628 1.00 41.16  ? 529  ARG B CZ  1 
ATOM   6453 N  NH1 . ARG B 2 201 ? 230.186 176.108 171.263 1.00 41.34  ? 529  ARG B NH1 1 
ATOM   6454 N  NH2 . ARG B 2 201 ? 230.047 177.910 172.653 1.00 42.95  ? 529  ARG B NH2 1 
ATOM   6455 N  N   . PRO B 2 202 ? 223.883 178.823 167.675 1.00 35.35  ? 530  PRO B N   1 
ATOM   6456 C  CA  . PRO B 2 202 ? 223.175 178.408 166.474 1.00 34.07  ? 530  PRO B CA  1 
ATOM   6457 C  C   . PRO B 2 202 ? 223.106 176.889 166.358 1.00 32.67  ? 530  PRO B C   1 
ATOM   6458 O  O   . PRO B 2 202 ? 223.957 176.178 166.892 1.00 32.34  ? 530  PRO B O   1 
ATOM   6459 C  CB  . PRO B 2 202 ? 224.023 179.033 165.359 1.00 33.26  ? 530  PRO B CB  1 
ATOM   6460 C  CG  . PRO B 2 202 ? 224.701 180.209 166.011 1.00 35.08  ? 530  PRO B CG  1 
ATOM   6461 C  CD  . PRO B 2 202 ? 224.976 179.772 167.420 1.00 35.46  ? 530  PRO B CD  1 
ATOM   6462 N  N   . LYS B 2 203 ? 222.080 176.401 165.668 1.00 31.04  ? 531  LYS B N   1 
ATOM   6463 C  CA  . LYS B 2 203 ? 221.868 174.961 165.508 1.00 29.68  ? 531  LYS B CA  1 
ATOM   6464 C  C   . LYS B 2 203 ? 223.091 174.301 164.872 1.00 29.37  ? 531  LYS B C   1 
ATOM   6465 O  O   . LYS B 2 203 ? 223.718 174.899 163.998 1.00 29.21  ? 531  LYS B O   1 
ATOM   6466 C  CB  . LYS B 2 203 ? 220.634 174.714 164.638 1.00 28.29  ? 531  LYS B CB  1 
ATOM   6467 C  CG  . LYS B 2 203 ? 219.344 175.334 165.162 1.00 27.95  ? 531  LYS B CG  1 
ATOM   6468 C  CD  . LYS B 2 203 ? 218.796 174.577 166.359 1.00 28.84  ? 531  LYS B CD  1 
ATOM   6469 C  CE  . LYS B 2 203 ? 217.424 175.111 166.758 1.00 29.93  ? 531  LYS B CE  1 
ATOM   6470 N  NZ  . LYS B 2 203 ? 216.905 174.455 167.990 1.00 31.27  ? 531  LYS B NZ  1 
ATOM   6471 N  N   . PRO B 2 204 ? 223.427 173.061 165.256 1.00 29.60  ? 532  PRO B N   1 
ATOM   6472 C  CA  . PRO B 2 204 ? 224.518 172.243 164.740 1.00 28.07  ? 532  PRO B CA  1 
ATOM   6473 C  C   . PRO B 2 204 ? 224.569 172.224 163.214 1.00 28.31  ? 532  PRO B C   1 
ATOM   6474 O  O   . PRO B 2 204 ? 225.645 172.281 162.620 1.00 28.49  ? 532  PRO B O   1 
ATOM   6475 C  CB  . PRO B 2 204 ? 224.166 170.866 165.313 1.00 27.90  ? 532  PRO B CB  1 
ATOM   6476 C  CG  . PRO B 2 204 ? 223.479 171.178 166.620 1.00 27.79  ? 532  PRO B CG  1 
ATOM   6477 C  CD  . PRO B 2 204 ? 222.663 172.422 166.343 1.00 28.32  ? 532  PRO B CD  1 
ATOM   6478 N  N   . SER B 2 205 ? 223.401 172.173 162.573 1.00 28.19  ? 533  SER B N   1 
ATOM   6479 C  CA  . SER B 2 205 ? 223.337 172.200 161.116 1.00 27.79  ? 533  SER B CA  1 
ATOM   6480 C  C   . SER B 2 205 ? 223.642 173.579 160.502 1.00 28.67  ? 533  SER B C   1 
ATOM   6481 O  O   . SER B 2 205 ? 224.114 173.654 159.368 1.00 28.37  ? 533  SER B O   1 
ATOM   6482 C  CB  . SER B 2 205 ? 221.977 171.706 160.667 1.00 26.72  ? 533  SER B CB  1 
ATOM   6483 O  OG  . SER B 2 205 ? 220.964 172.446 161.279 1.00 26.62  ? 533  SER B OG  1 
ATOM   6484 N  N   . CYS B 2 206 ? 223.424 174.669 161.258 1.00 28.59  ? 534  CYS B N   1 
ATOM   6485 C  CA  . CYS B 2 206 ? 223.771 176.019 160.799 1.00 28.07  ? 534  CYS B CA  1 
ATOM   6486 C  C   . CYS B 2 206 ? 225.263 176.245 161.036 1.00 29.04  ? 534  CYS B C   1 
ATOM   6487 O  O   . CYS B 2 206 ? 225.959 176.857 160.220 1.00 29.73  ? 534  CYS B O   1 
ATOM   6488 C  CB  . CYS B 2 206 ? 222.960 177.103 161.544 1.00 28.58  ? 534  CYS B CB  1 
ATOM   6489 S  SG  . CYS B 2 206 ? 221.171 177.165 161.146 1.00 27.04  ? 534  CYS B SG  1 
ATOM   6490 N  N   . ALA B 2 207 ? 225.744 175.743 162.169 1.00 29.18  ? 535  ALA B N   1 
ATOM   6491 C  CA  . ALA B 2 207 ? 227.142 175.880 162.551 1.00 29.33  ? 535  ALA B CA  1 
ATOM   6492 C  C   . ALA B 2 207 ? 228.039 175.167 161.554 1.00 30.27  ? 535  ALA B C   1 
ATOM   6493 O  O   . ALA B 2 207 ? 229.118 175.655 161.210 1.00 31.08  ? 535  ALA B O   1 
ATOM   6494 C  CB  . ALA B 2 207 ? 227.353 175.315 163.947 1.00 29.94  ? 535  ALA B CB  1 
ATOM   6495 N  N   . ARG B 2 208 ? 227.566 174.028 161.064 1.00 29.54  ? 536  ARG B N   1 
ATOM   6496 C  CA  . ARG B 2 208 ? 228.290 173.240 160.079 1.00 29.41  ? 536  ARG B CA  1 
ATOM   6497 C  C   . ARG B 2 208 ? 228.575 174.046 158.822 1.00 30.78  ? 536  ARG B C   1 
ATOM   6498 O  O   . ARG B 2 208 ? 229.649 173.934 158.230 1.00 30.31  ? 536  ARG B O   1 
ATOM   6499 C  CB  . ARG B 2 208 ? 227.471 172.024 159.691 1.00 29.25  ? 536  ARG B CB  1 
ATOM   6500 C  CG  . ARG B 2 208 ? 228.093 171.160 158.621 1.00 29.52  ? 536  ARG B CG  1 
ATOM   6501 C  CD  . ARG B 2 208 ? 228.878 170.059 159.184 1.00 29.34  ? 536  ARG B CD  1 
ATOM   6502 N  NE  . ARG B 2 208 ? 228.027 168.913 159.442 1.00 28.25  ? 536  ARG B NE  1 
ATOM   6503 C  CZ  . ARG B 2 208 ? 228.382 167.820 160.127 1.00 28.38  ? 536  ARG B CZ  1 
ATOM   6504 N  NH1 . ARG B 2 208 ? 229.587 167.725 160.639 1.00 28.96  ? 536  ARG B NH1 1 
ATOM   6505 N  NH2 . ARG B 2 208 ? 227.508 166.840 160.277 1.00 28.56  ? 536  ARG B NH2 1 
ATOM   6506 N  N   . ILE B 2 209 ? 227.605 174.857 158.405 1.00 29.42  ? 537  ILE B N   1 
ATOM   6507 C  CA  . ILE B 2 209 ? 227.749 175.636 157.189 1.00 29.92  ? 537  ILE B CA  1 
ATOM   6508 C  C   . ILE B 2 209 ? 228.837 176.684 157.359 1.00 30.47  ? 537  ILE B C   1 
ATOM   6509 O  O   . ILE B 2 209 ? 229.662 176.879 156.467 1.00 31.72  ? 537  ILE B O   1 
ATOM   6510 C  CB  . ILE B 2 209 ? 226.423 176.306 156.788 1.00 29.30  ? 537  ILE B CB  1 
ATOM   6511 C  CG1 . ILE B 2 209 ? 225.407 175.223 156.402 1.00 27.65  ? 537  ILE B CG1 1 
ATOM   6512 C  CG2 . ILE B 2 209 ? 226.660 177.277 155.620 1.00 28.76  ? 537  ILE B CG2 1 
ATOM   6513 C  CD1 . ILE B 2 209 ? 223.991 175.715 156.257 1.00 26.11  ? 537  ILE B CD1 1 
ATOM   6514 N  N   . GLY B 2 210 ? 228.838 177.357 158.505 1.00 30.68  ? 538  GLY B N   1 
ATOM   6515 C  CA  . GLY B 2 210 ? 229.847 178.368 158.789 1.00 31.79  ? 538  GLY B CA  1 
ATOM   6516 C  C   . GLY B 2 210 ? 231.250 177.768 158.773 1.00 35.46  ? 538  GLY B C   1 
ATOM   6517 O  O   . GLY B 2 210 ? 232.182 178.357 158.226 1.00 33.08  ? 538  GLY B O   1 
ATOM   6518 N  N   . MET B 2 211 ? 231.396 176.586 159.373 1.00 31.77  ? 539  MET B N   1 
ATOM   6519 C  CA  . MET B 2 211 ? 232.685 175.905 159.450 1.00 32.42  ? 539  MET B CA  1 
ATOM   6520 C  C   . MET B 2 211 ? 233.225 175.554 158.074 1.00 33.26  ? 539  MET B C   1 
ATOM   6521 O  O   . MET B 2 211 ? 234.382 175.836 157.754 1.00 33.79  ? 539  MET B O   1 
ATOM   6522 C  CB  . MET B 2 211 ? 232.551 174.643 160.294 1.00 32.47  ? 539  MET B CB  1 
ATOM   6523 C  CG  . MET B 2 211 ? 232.258 174.921 161.739 1.00 33.07  ? 539  MET B CG  1 
ATOM   6524 S  SD  . MET B 2 211 ? 231.958 173.445 162.690 1.00 33.06  ? 539  MET B SD  1 
ATOM   6525 C  CE  . MET B 2 211 ? 231.295 174.202 164.163 1.00 31.84  ? 539  MET B CE  1 
ATOM   6526 N  N   . GLN B 2 212 ? 232.375 174.946 157.249 1.00 32.66  ? 540  GLN B N   1 
ATOM   6527 C  CA  . GLN B 2 212 ? 232.772 174.565 155.905 1.00 32.91  ? 540  GLN B CA  1 
ATOM   6528 C  C   . GLN B 2 212 ? 233.045 175.795 155.058 1.00 34.71  ? 540  GLN B C   1 
ATOM   6529 O  O   . GLN B 2 212 ? 233.970 175.810 154.250 1.00 33.53  ? 540  GLN B O   1 
ATOM   6530 C  CB  . GLN B 2 212 ? 231.690 173.713 155.246 1.00 31.88  ? 540  GLN B CB  1 
ATOM   6531 C  CG  . GLN B 2 212 ? 231.518 172.350 155.866 1.00 31.18  ? 540  GLN B CG  1 
ATOM   6532 C  CD  . GLN B 2 212 ? 230.462 171.535 155.161 1.00 30.73  ? 540  GLN B CD  1 
ATOM   6533 O  OE1 . GLN B 2 212 ? 230.687 170.373 154.818 1.00 30.34  ? 540  GLN B OE1 1 
ATOM   6534 N  NE2 . GLN B 2 212 ? 229.305 172.137 154.930 1.00 30.35  ? 540  GLN B NE2 1 
ATOM   6535 N  N   . GLY B 2 213 ? 232.252 176.841 155.272 1.00 32.60  ? 541  GLY B N   1 
ATOM   6536 C  CA  . GLY B 2 213 ? 232.432 178.089 154.554 1.00 33.44  ? 541  GLY B CA  1 
ATOM   6537 C  C   . GLY B 2 213 ? 233.788 178.694 154.866 1.00 34.35  ? 541  GLY B C   1 
ATOM   6538 O  O   . GLY B 2 213 ? 234.539 179.057 153.962 1.00 35.62  ? 541  GLY B O   1 
ATOM   6539 N  N   . HIS B 2 214 ? 234.114 178.781 156.147 1.00 35.05  ? 542  HIS B N   1 
ATOM   6540 C  CA  . HIS B 2 214 ? 235.378 179.352 156.585 1.00 35.82  ? 542  HIS B CA  1 
ATOM   6541 C  C   . HIS B 2 214 ? 236.547 178.670 155.887 1.00 37.30  ? 542  HIS B C   1 
ATOM   6542 O  O   . HIS B 2 214 ? 237.458 179.329 155.388 1.00 38.14  ? 542  HIS B O   1 
ATOM   6543 C  CB  . HIS B 2 214 ? 235.522 179.199 158.105 1.00 36.30  ? 542  HIS B CB  1 
ATOM   6544 C  CG  . HIS B 2 214 ? 236.761 179.812 158.689 1.00 37.58  ? 542  HIS B CG  1 
ATOM   6545 N  ND1 . HIS B 2 214 ? 236.869 181.160 158.961 1.00 38.79  ? 542  HIS B ND1 1 
ATOM   6546 C  CD2 . HIS B 2 214 ? 237.936 179.259 159.062 1.00 38.53  ? 542  HIS B CD2 1 
ATOM   6547 C  CE1 . HIS B 2 214 ? 238.058 181.407 159.477 1.00 39.67  ? 542  HIS B CE1 1 
ATOM   6548 N  NE2 . HIS B 2 214 ? 238.725 180.272 159.548 1.00 40.20  ? 542  HIS B NE2 1 
ATOM   6549 N  N   . ALA B 2 215 ? 236.516 177.344 155.849 1.00 36.29  ? 543  ALA B N   1 
ATOM   6550 C  CA  . ALA B 2 215 ? 237.618 176.553 155.311 1.00 36.59  ? 543  ALA B CA  1 
ATOM   6551 C  C   . ALA B 2 215 ? 237.488 176.247 153.811 1.00 37.27  ? 543  ALA B C   1 
ATOM   6552 O  O   . ALA B 2 215 ? 238.273 175.465 153.277 1.00 39.14  ? 543  ALA B O   1 
ATOM   6553 C  CB  . ALA B 2 215 ? 237.726 175.253 156.088 1.00 37.61  ? 543  ALA B CB  1 
ATOM   6554 N  N   . SER B 2 216 ? 236.491 176.818 153.134 1.00 36.42  ? 544  SER B N   1 
ATOM   6555 C  CA  . SER B 2 216 ? 236.290 176.513 151.714 1.00 36.24  ? 544  SER B CA  1 
ATOM   6556 C  C   . SER B 2 216 ? 237.167 177.352 150.789 1.00 38.04  ? 544  SER B C   1 
ATOM   6557 O  O   . SER B 2 216 ? 237.441 176.953 149.657 1.00 37.58  ? 544  SER B O   1 
ATOM   6558 C  CB  . SER B 2 216 ? 234.843 176.731 151.308 1.00 36.01  ? 544  SER B CB  1 
ATOM   6559 O  OG  . SER B 2 216 ? 234.506 178.090 151.360 1.00 36.29  ? 544  SER B OG  1 
ATOM   6560 N  N   . GLY B 2 217 ? 237.579 178.528 151.250 1.00 38.27  ? 545  GLY B N   1 
ATOM   6561 C  CA  . GLY B 2 217 ? 238.312 179.462 150.391 1.00 37.64  ? 545  GLY B CA  1 
ATOM   6562 C  C   . GLY B 2 217 ? 237.400 180.164 149.379 1.00 37.76  ? 545  GLY B C   1 
ATOM   6563 O  O   . GLY B 2 217 ? 237.834 180.515 148.281 1.00 37.83  ? 545  GLY B O   1 
ATOM   6564 N  N   . ASN B 2 218 ? 236.135 180.348 149.763 1.00 37.42  ? 546  ASN B N   1 
ATOM   6565 C  CA  . ASN B 2 218 ? 235.082 180.942 148.950 1.00 36.26  ? 546  ASN B CA  1 
ATOM   6566 C  C   . ASN B 2 218 ? 234.449 182.110 149.698 1.00 37.27  ? 546  ASN B C   1 
ATOM   6567 O  O   . ASN B 2 218 ? 233.941 181.927 150.816 1.00 37.93  ? 546  ASN B O   1 
ATOM   6568 C  CB  . ASN B 2 218 ? 234.040 179.889 148.582 1.00 36.24  ? 546  ASN B CB  1 
ATOM   6569 C  CG  . ASN B 2 218 ? 233.417 180.081 147.204 1.00 36.20  ? 546  ASN B CG  1 
ATOM   6570 O  OD1 . ASN B 2 218 ? 233.108 181.209 146.794 1.00 37.64  ? 546  ASN B OD1 1 
ATOM   6571 N  ND2 . ASN B 2 218 ? 233.225 178.983 146.498 1.00 36.64  ? 546  ASN B ND2 1 
ATOM   6572 N  N   . GLU B 2 219 ? 234.487 183.314 149.118 1.00 36.85  ? 547  GLU B N   1 
ATOM   6573 C  CA  . GLU B 2 219 ? 233.977 184.520 149.781 1.00 36.55  ? 547  GLU B CA  1 
ATOM   6574 C  C   . GLU B 2 219 ? 232.495 184.389 150.128 1.00 36.72  ? 547  GLU B C   1 
ATOM   6575 O  O   . GLU B 2 219 ? 232.054 184.840 151.185 1.00 36.74  ? 547  GLU B O   1 
ATOM   6576 C  CB  . GLU B 2 219 ? 234.213 185.751 148.902 1.00 37.68  ? 547  GLU B CB  1 
ATOM   6577 N  N   . THR B 2 220 ? 231.742 183.733 149.251 1.00 35.64  ? 548  THR B N   1 
ATOM   6578 C  CA  . THR B 2 220 ? 230.347 183.414 149.525 1.00 34.99  ? 548  THR B CA  1 
ATOM   6579 C  C   . THR B 2 220 ? 230.133 181.912 149.370 1.00 34.75  ? 548  THR B C   1 
ATOM   6580 O  O   . THR B 2 220 ? 230.293 181.367 148.280 1.00 35.76  ? 548  THR B O   1 
ATOM   6581 C  CB  . THR B 2 220 ? 229.397 184.178 148.587 1.00 35.81  ? 548  THR B CB  1 
ATOM   6582 N  N   . TYR B 2 221 ? 229.769 181.244 150.460 1.00 33.28  ? 549  TYR B N   1 
ATOM   6583 C  CA  . TYR B 2 221 ? 229.625 179.792 150.445 1.00 33.30  ? 549  TYR B CA  1 
ATOM   6584 C  C   . TYR B 2 221 ? 228.207 179.350 150.776 1.00 31.61  ? 549  TYR B C   1 
ATOM   6585 O  O   . TYR B 2 221 ? 227.684 179.661 151.846 1.00 31.30  ? 549  TYR B O   1 
ATOM   6586 C  CB  . TYR B 2 221 ? 230.604 179.166 151.435 1.00 33.43  ? 549  TYR B CB  1 
ATOM   6587 C  CG  . TYR B 2 221 ? 230.535 177.668 151.509 1.00 32.92  ? 549  TYR B CG  1 
ATOM   6588 C  CD1 . TYR B 2 221 ? 231.217 176.902 150.589 1.00 32.58  ? 549  TYR B CD1 1 
ATOM   6589 C  CD2 . TYR B 2 221 ? 229.795 177.059 152.509 1.00 32.10  ? 549  TYR B CD2 1 
ATOM   6590 C  CE1 . TYR B 2 221 ? 231.163 175.527 150.666 1.00 32.28  ? 549  TYR B CE1 1 
ATOM   6591 C  CE2 . TYR B 2 221 ? 229.741 175.688 152.586 1.00 31.77  ? 549  TYR B CE2 1 
ATOM   6592 C  CZ  . TYR B 2 221 ? 230.422 174.922 151.669 1.00 32.34  ? 549  TYR B CZ  1 
ATOM   6593 O  OH  . TYR B 2 221 ? 230.370 173.552 151.743 1.00 31.93  ? 549  TYR B OH  1 
ATOM   6594 N  N   . THR B 2 222 ? 227.596 178.604 149.864 1.00 31.83  ? 550  THR B N   1 
ATOM   6595 C  CA  . THR B 2 222 ? 226.227 178.131 150.051 1.00 29.91  ? 550  THR B CA  1 
ATOM   6596 C  C   . THR B 2 222 ? 226.176 176.609 150.114 1.00 29.73  ? 550  THR B C   1 
ATOM   6597 O  O   . THR B 2 222 ? 226.775 175.929 149.283 1.00 30.20  ? 550  THR B O   1 
ATOM   6598 C  CB  . THR B 2 222 ? 225.315 178.627 148.913 1.00 29.98  ? 550  THR B CB  1 
ATOM   6599 O  OG1 . THR B 2 222 ? 225.332 180.056 148.873 1.00 29.91  ? 550  THR B OG1 1 
ATOM   6600 C  CG2 . THR B 2 222 ? 223.888 178.158 149.139 1.00 28.86  ? 550  THR B CG2 1 
ATOM   6601 N  N   . ALA B 2 223 ? 225.465 176.072 151.103 1.00 28.18  ? 551  ALA B N   1 
ATOM   6602 C  CA  . ALA B 2 223 ? 225.385 174.622 151.251 1.00 26.83  ? 551  ALA B CA  1 
ATOM   6603 C  C   . ALA B 2 223 ? 224.120 174.169 151.971 1.00 25.16  ? 551  ALA B C   1 
ATOM   6604 O  O   . ALA B 2 223 ? 223.504 174.933 152.715 1.00 25.15  ? 551  ALA B O   1 
ATOM   6605 C  CB  . ALA B 2 223 ? 226.602 174.114 152.005 1.00 27.82  ? 551  ALA B CB  1 
ATOM   6606 N  N   . VAL B 2 224 ? 223.758 172.903 151.753 1.00 24.93  ? 552  VAL B N   1 
ATOM   6607 C  CA  . VAL B 2 224 ? 222.663 172.251 152.466 1.00 23.78  ? 552  VAL B CA  1 
ATOM   6608 C  C   . VAL B 2 224 ? 223.220 171.089 153.271 1.00 24.01  ? 552  VAL B C   1 
ATOM   6609 O  O   . VAL B 2 224 ? 223.827 170.177 152.707 1.00 24.40  ? 552  VAL B O   1 
ATOM   6610 C  CB  . VAL B 2 224 ? 221.607 171.707 151.484 1.00 22.89  ? 552  VAL B CB  1 
ATOM   6611 C  CG1 . VAL B 2 224 ? 220.459 171.071 152.259 1.00 22.65  ? 552  VAL B CG1 1 
ATOM   6612 C  CG2 . VAL B 2 224 ? 221.103 172.811 150.598 1.00 23.29  ? 552  VAL B CG2 1 
ATOM   6613 N  N   . VAL B 2 225 ? 223.061 171.137 154.584 1.00 23.72  ? 553  VAL B N   1 
ATOM   6614 C  CA  . VAL B 2 225 ? 223.678 170.132 155.433 1.00 24.14  ? 553  VAL B CA  1 
ATOM   6615 C  C   . VAL B 2 225 ? 222.719 169.565 156.464 1.00 24.36  ? 553  VAL B C   1 
ATOM   6616 O  O   . VAL B 2 225 ? 221.665 170.139 156.746 1.00 23.89  ? 553  VAL B O   1 
ATOM   6617 C  CB  . VAL B 2 225 ? 224.890 170.730 156.166 1.00 25.52  ? 553  VAL B CB  1 
ATOM   6618 C  CG1 . VAL B 2 225 ? 225.892 171.283 155.169 1.00 25.71  ? 553  VAL B CG1 1 
ATOM   6619 C  CG2 . VAL B 2 225 ? 224.426 171.807 157.113 1.00 26.30  ? 553  VAL B CG2 1 
ATOM   6620 N  N   . THR B 2 226 ? 223.130 168.460 157.065 1.00 24.80  ? 554  THR B N   1 
ATOM   6621 C  CA  . THR B 2 226 ? 222.456 167.887 158.219 1.00 25.17  ? 554  THR B CA  1 
ATOM   6622 C  C   . THR B 2 226 ? 223.526 167.517 159.244 1.00 26.34  ? 554  THR B C   1 
ATOM   6623 O  O   . THR B 2 226 ? 224.649 167.169 158.874 1.00 26.45  ? 554  THR B O   1 
ATOM   6624 C  CB  . THR B 2 226 ? 221.616 166.657 157.825 1.00 24.68  ? 554  THR B CB  1 
ATOM   6625 O  OG1 . THR B 2 226 ? 220.889 166.184 158.971 1.00 24.85  ? 554  THR B OG1 1 
ATOM   6626 C  CG2 . THR B 2 226 ? 222.519 165.548 157.290 1.00 25.20  ? 554  THR B CG2 1 
ATOM   6627 N  N   . ASN B 2 227 ? 223.206 167.630 160.527 1.00 26.67  ? 555  ASN B N   1 
ATOM   6628 C  CA  . ASN B 2 227 ? 224.205 167.354 161.552 1.00 26.90  ? 555  ASN B CA  1 
ATOM   6629 C  C   . ASN B 2 227 ? 223.621 166.635 162.753 1.00 27.28  ? 555  ASN B C   1 
ATOM   6630 O  O   . ASN B 2 227 ? 223.445 167.223 163.816 1.00 27.82  ? 555  ASN B O   1 
ATOM   6631 C  CB  . ASN B 2 227 ? 224.889 168.639 161.986 1.00 28.06  ? 555  ASN B CB  1 
ATOM   6632 C  CG  . ASN B 2 227 ? 226.119 168.378 162.822 1.00 28.07  ? 555  ASN B CG  1 
ATOM   6633 O  OD1 . ASN B 2 227 ? 226.520 167.222 163.002 1.00 28.07  ? 555  ASN B OD1 1 
ATOM   6634 N  ND2 . ASN B 2 227 ? 226.732 169.422 163.322 1.00 28.25  ? 555  ASN B ND2 1 
ATOM   6635 N  N   . ASN B 2 228 ? 223.323 165.352 162.570 1.00 27.53  ? 556  ASN B N   1 
ATOM   6636 C  CA  . ASN B 2 228 ? 222.785 164.510 163.632 1.00 27.43  ? 556  ASN B CA  1 
ATOM   6637 C  C   . ASN B 2 228 ? 221.506 165.075 164.243 1.00 27.18  ? 556  ASN B C   1 
ATOM   6638 O  O   . ASN B 2 228 ? 221.268 164.933 165.443 1.00 27.36  ? 556  ASN B O   1 
ATOM   6639 C  CB  . ASN B 2 228 ? 223.833 164.291 164.706 1.00 28.35  ? 556  ASN B CB  1 
ATOM   6640 N  N   . GLU B 2 229 ? 220.670 165.687 163.413 1.00 26.83  ? 557  GLU B N   1 
ATOM   6641 C  CA  . GLU B 2 229 ? 219.398 166.225 163.877 1.00 26.18  ? 557  GLU B CA  1 
ATOM   6642 C  C   . GLU B 2 229 ? 218.244 165.448 163.262 1.00 25.82  ? 557  GLU B C   1 
ATOM   6643 O  O   . GLU B 2 229 ? 218.021 165.512 162.054 1.00 25.18  ? 557  GLU B O   1 
ATOM   6644 C  CB  . GLU B 2 229 ? 219.275 167.714 163.524 1.00 26.22  ? 557  GLU B CB  1 
ATOM   6645 N  N   . LEU B 2 230 ? 217.530 164.686 164.086 1.00 25.54  ? 558  LEU B N   1 
ATOM   6646 C  CA  . LEU B 2 230 ? 216.427 163.869 163.591 1.00 24.94  ? 558  LEU B CA  1 
ATOM   6647 C  C   . LEU B 2 230 ? 215.083 164.405 164.051 1.00 24.55  ? 558  LEU B C   1 
ATOM   6648 O  O   . LEU B 2 230 ? 214.972 164.986 165.132 1.00 24.81  ? 558  LEU B O   1 
ATOM   6649 C  CB  . LEU B 2 230 ? 216.574 162.418 164.059 1.00 24.97  ? 558  LEU B CB  1 
ATOM   6650 C  CG  . LEU B 2 230 ? 217.879 161.711 163.676 1.00 25.37  ? 558  LEU B CG  1 
ATOM   6651 C  CD1 . LEU B 2 230 ? 217.869 160.307 164.252 1.00 25.53  ? 558  LEU B CD1 1 
ATOM   6652 C  CD2 . LEU B 2 230 ? 218.016 161.674 162.164 1.00 25.00  ? 558  LEU B CD2 1 
ATOM   6653 N  N   . ASP B 2 231 ? 214.059 164.197 163.231 1.00 24.13  ? 559  ASP B N   1 
ATOM   6654 C  CA  . ASP B 2 231 ? 212.707 164.611 163.576 1.00 23.65  ? 559  ASP B CA  1 
ATOM   6655 C  C   . ASP B 2 231 ? 211.943 163.490 164.282 1.00 24.23  ? 559  ASP B C   1 
ATOM   6656 O  O   . ASP B 2 231 ? 212.520 162.471 164.664 1.00 23.68  ? 559  ASP B O   1 
ATOM   6657 C  CB  . ASP B 2 231 ? 211.940 165.072 162.335 1.00 22.80  ? 559  ASP B CB  1 
ATOM   6658 C  CG  . ASP B 2 231 ? 211.571 163.942 161.404 1.00 22.57  ? 559  ASP B CG  1 
ATOM   6659 O  OD1 . ASP B 2 231 ? 211.783 162.806 161.767 1.00 23.34  ? 559  ASP B OD1 1 
ATOM   6660 O  OD2 . ASP B 2 231 ? 211.049 164.215 160.348 1.00 21.68  ? 559  ASP B OD2 1 
ATOM   6661 N  N   . SER B 2 232 ? 210.644 163.704 164.474 1.00 23.22  ? 560  SER B N   1 
ATOM   6662 C  CA  . SER B 2 232 ? 209.792 162.806 165.253 1.00 23.51  ? 560  SER B CA  1 
ATOM   6663 C  C   . SER B 2 232 ? 209.596 161.422 164.635 1.00 23.23  ? 560  SER B C   1 
ATOM   6664 O  O   . SER B 2 232 ? 209.098 160.514 165.303 1.00 23.37  ? 560  SER B O   1 
ATOM   6665 C  CB  . SER B 2 232 ? 208.435 163.445 165.472 1.00 23.66  ? 560  SER B CB  1 
ATOM   6666 N  N   . VAL B 2 233 ? 209.960 161.252 163.367 1.00 23.52  ? 561  VAL B N   1 
ATOM   6667 C  CA  . VAL B 2 233 ? 209.798 159.955 162.719 1.00 23.29  ? 561  VAL B CA  1 
ATOM   6668 C  C   . VAL B 2 233 ? 211.151 159.330 162.393 1.00 23.40  ? 561  VAL B C   1 
ATOM   6669 O  O   . VAL B 2 233 ? 211.221 158.294 161.733 1.00 23.62  ? 561  VAL B O   1 
ATOM   6670 C  CB  . VAL B 2 233 ? 208.946 160.072 161.439 1.00 22.86  ? 561  VAL B CB  1 
ATOM   6671 N  N   . GLY B 2 234 ? 212.225 159.963 162.866 1.00 23.89  ? 562  GLY B N   1 
ATOM   6672 C  CA  . GLY B 2 234 ? 213.576 159.445 162.674 1.00 23.90  ? 562  GLY B CA  1 
ATOM   6673 C  C   . GLY B 2 234 ? 214.243 159.915 161.383 1.00 23.94  ? 562  GLY B C   1 
ATOM   6674 O  O   . GLY B 2 234 ? 215.296 159.398 161.009 1.00 24.21  ? 562  GLY B O   1 
ATOM   6675 N  N   . ASP B 2 235 ? 213.643 160.882 160.695 1.00 23.78  ? 563  ASP B N   1 
ATOM   6676 C  CA  . ASP B 2 235 ? 214.231 161.383 159.458 1.00 23.36  ? 563  ASP B CA  1 
ATOM   6677 C  C   . ASP B 2 235 ? 215.202 162.528 159.756 1.00 24.47  ? 563  ASP B C   1 
ATOM   6678 O  O   . ASP B 2 235 ? 215.002 163.263 160.721 1.00 23.11  ? 563  ASP B O   1 
ATOM   6679 C  CB  . ASP B 2 235 ? 213.148 161.851 158.484 1.00 23.62  ? 563  ASP B CB  1 
ATOM   6680 C  CG  . ASP B 2 235 ? 212.382 160.696 157.826 1.00 23.34  ? 563  ASP B CG  1 
ATOM   6681 O  OD1 . ASP B 2 235 ? 212.947 159.641 157.658 1.00 23.61  ? 563  ASP B OD1 1 
ATOM   6682 O  OD2 . ASP B 2 235 ? 211.235 160.887 157.493 1.00 22.66  ? 563  ASP B OD2 1 
ATOM   6683 N  N   . PRO B 2 236 ? 216.264 162.688 158.958 1.00 23.98  ? 564  PRO B N   1 
ATOM   6684 C  CA  . PRO B 2 236 ? 217.208 163.792 158.990 1.00 23.88  ? 564  PRO B CA  1 
ATOM   6685 C  C   . PRO B 2 236 ? 216.540 165.146 158.800 1.00 23.67  ? 564  PRO B C   1 
ATOM   6686 O  O   . PRO B 2 236 ? 215.687 165.317 157.928 1.00 23.42  ? 564  PRO B O   1 
ATOM   6687 C  CB  . PRO B 2 236 ? 218.123 163.472 157.800 1.00 23.77  ? 564  PRO B CB  1 
ATOM   6688 C  CG  . PRO B 2 236 ? 218.032 161.979 157.635 1.00 23.65  ? 564  PRO B CG  1 
ATOM   6689 C  CD  . PRO B 2 236 ? 216.609 161.627 158.005 1.00 23.67  ? 564  PRO B CD  1 
ATOM   6690 N  N   . ILE B 2 237 ? 216.988 166.125 159.575 1.00 24.03  ? 565  ILE B N   1 
ATOM   6691 C  CA  . ILE B 2 237 ? 216.532 167.498 159.425 1.00 23.80  ? 565  ILE B CA  1 
ATOM   6692 C  C   . ILE B 2 237 ? 217.567 168.294 158.659 1.00 23.24  ? 565  ILE B C   1 
ATOM   6693 O  O   . ILE B 2 237 ? 218.716 168.411 159.083 1.00 23.75  ? 565  ILE B O   1 
ATOM   6694 C  CB  . ILE B 2 237 ? 216.273 168.157 160.791 1.00 24.37  ? 565  ILE B CB  1 
ATOM   6695 C  CG1 . ILE B 2 237 ? 215.172 167.392 161.530 1.00 24.40  ? 565  ILE B CG1 1 
ATOM   6696 C  CG2 . ILE B 2 237 ? 215.894 169.629 160.602 1.00 24.00  ? 565  ILE B CG2 1 
ATOM   6697 C  CD1 . ILE B 2 237 ? 215.044 167.757 162.990 1.00 25.02  ? 565  ILE B CD1 1 
ATOM   6698 N  N   . TRP B 2 238 ? 217.162 168.821 157.516 1.00 22.82  ? 566  TRP B N   1 
ATOM   6699 C  CA  . TRP B 2 238 ? 218.078 169.535 156.646 1.00 22.64  ? 566  TRP B CA  1 
ATOM   6700 C  C   . TRP B 2 238 ? 217.951 171.036 156.814 1.00 21.55  ? 566  TRP B C   1 
ATOM   6701 O  O   . TRP B 2 238 ? 216.851 171.559 156.995 1.00 20.82  ? 566  TRP B O   1 
ATOM   6702 C  CB  . TRP B 2 238 ? 217.806 169.163 155.193 1.00 21.74  ? 566  TRP B CB  1 
ATOM   6703 C  CG  . TRP B 2 238 ? 218.095 167.744 154.888 1.00 22.47  ? 566  TRP B CG  1 
ATOM   6704 C  CD1 . TRP B 2 238 ? 217.212 166.709 154.914 1.00 22.45  ? 566  TRP B CD1 1 
ATOM   6705 C  CD2 . TRP B 2 238 ? 219.360 167.183 154.508 1.00 23.00  ? 566  TRP B CD2 1 
ATOM   6706 N  NE1 . TRP B 2 238 ? 217.843 165.546 154.577 1.00 22.72  ? 566  TRP B NE1 1 
ATOM   6707 C  CE2 . TRP B 2 238 ? 219.159 165.816 154.325 1.00 22.91  ? 566  TRP B CE2 1 
ATOM   6708 C  CE3 . TRP B 2 238 ? 220.630 167.722 154.313 1.00 23.05  ? 566  TRP B CE3 1 
ATOM   6709 C  CZ2 . TRP B 2 238 ? 220.184 164.974 153.952 1.00 23.40  ? 566  TRP B CZ2 1 
ATOM   6710 C  CZ3 . TRP B 2 238 ? 221.658 166.881 153.937 1.00 23.60  ? 566  TRP B CZ3 1 
ATOM   6711 C  CH2 . TRP B 2 238 ? 221.442 165.541 153.762 1.00 24.08  ? 566  TRP B CH2 1 
ATOM   6712 N  N   . ARG B 2 239 ? 219.077 171.726 156.707 1.00 22.01  ? 567  ARG B N   1 
ATOM   6713 C  CA  . ARG B 2 239 ? 219.086 173.180 156.686 1.00 21.36  ? 567  ARG B CA  1 
ATOM   6714 C  C   . ARG B 2 239 ? 220.044 173.732 155.652 1.00 22.09  ? 567  ARG B C   1 
ATOM   6715 O  O   . ARG B 2 239 ? 221.115 173.175 155.402 1.00 22.98  ? 567  ARG B O   1 
ATOM   6716 C  CB  . ARG B 2 239 ? 219.394 173.768 158.052 1.00 22.88  ? 567  ARG B CB  1 
ATOM   6717 C  CG  . ARG B 2 239 ? 218.156 174.148 158.849 1.00 22.10  ? 567  ARG B CG  1 
ATOM   6718 C  CD  . ARG B 2 239 ? 218.480 174.790 160.133 1.00 22.91  ? 567  ARG B CD  1 
ATOM   6719 N  NE  . ARG B 2 239 ? 218.530 173.843 161.221 1.00 25.23  ? 567  ARG B NE  1 
ATOM   6720 C  CZ  . ARG B 2 239 ? 217.462 173.484 161.956 1.00 24.73  ? 567  ARG B CZ  1 
ATOM   6721 N  NH1 . ARG B 2 239 ? 216.291 174.013 161.696 1.00 23.07  ? 567  ARG B NH1 1 
ATOM   6722 N  NH2 . ARG B 2 239 ? 217.579 172.609 162.935 1.00 25.72  ? 567  ARG B NH2 1 
ATOM   6723 N  N   . MET B 2 240 ? 219.635 174.831 155.043 1.00 21.77  ? 568  MET B N   1 
ATOM   6724 C  CA  . MET B 2 240 ? 220.412 175.498 154.021 1.00 22.35  ? 568  MET B CA  1 
ATOM   6725 C  C   . MET B 2 240 ? 220.812 176.875 154.497 1.00 22.43  ? 568  MET B C   1 
ATOM   6726 O  O   . MET B 2 240 ? 220.057 177.533 155.207 1.00 22.11  ? 568  MET B O   1 
ATOM   6727 C  CB  . MET B 2 240 ? 219.605 175.585 152.737 1.00 21.51  ? 568  MET B CB  1 
ATOM   6728 C  CG  . MET B 2 240 ? 220.340 176.226 151.584 1.00 22.17  ? 568  MET B CG  1 
ATOM   6729 S  SD  . MET B 2 240 ? 219.466 176.057 150.035 1.00 23.38  ? 568  MET B SD  1 
ATOM   6730 C  CE  . MET B 2 240 ? 220.686 176.728 148.932 1.00 23.02  ? 568  MET B CE  1 
ATOM   6731 N  N   . GLY B 2 241 ? 221.996 177.320 154.117 1.00 23.91  ? 569  GLY B N   1 
ATOM   6732 C  CA  . GLY B 2 241 ? 222.427 178.640 154.538 1.00 24.91  ? 569  GLY B CA  1 
ATOM   6733 C  C   . GLY B 2 241 ? 223.647 179.130 153.789 1.00 26.67  ? 569  GLY B C   1 
ATOM   6734 O  O   . GLY B 2 241 ? 224.197 178.435 152.931 1.00 27.94  ? 569  GLY B O   1 
ATOM   6735 N  N   . VAL B 2 242 ? 224.040 180.355 154.108 1.00 27.52  ? 570  VAL B N   1 
ATOM   6736 C  CA  . VAL B 2 242 ? 225.138 181.026 153.440 1.00 28.87  ? 570  VAL B CA  1 
ATOM   6737 C  C   . VAL B 2 242 ? 226.133 181.590 154.443 1.00 29.71  ? 570  VAL B C   1 
ATOM   6738 O  O   . VAL B 2 242 ? 225.749 182.258 155.405 1.00 29.86  ? 570  VAL B O   1 
ATOM   6739 C  CB  . VAL B 2 242 ? 224.602 182.170 152.558 1.00 28.87  ? 570  VAL B CB  1 
ATOM   6740 C  CG1 . VAL B 2 242 ? 225.755 182.872 151.854 1.00 29.40  ? 570  VAL B CG1 1 
ATOM   6741 C  CG2 . VAL B 2 242 ? 223.613 181.615 151.548 1.00 29.06  ? 570  VAL B CG2 1 
ATOM   6742 N  N   . ALA B 2 243 ? 227.411 181.339 154.198 1.00 30.50  ? 571  ALA B N   1 
ATOM   6743 C  CA  . ALA B 2 243 ? 228.474 181.894 155.022 1.00 32.24  ? 571  ALA B CA  1 
ATOM   6744 C  C   . ALA B 2 243 ? 229.275 182.908 154.218 1.00 32.63  ? 571  ALA B C   1 
ATOM   6745 O  O   . ALA B 2 243 ? 229.518 182.716 153.026 1.00 33.92  ? 571  ALA B O   1 
ATOM   6746 C  CB  . ALA B 2 243 ? 229.378 180.785 155.535 1.00 31.98  ? 571  ALA B CB  1 
ATOM   6747 N  N   . GLN B 2 244 ? 229.701 183.981 154.874 1.00 34.28  ? 572  GLN B N   1 
ATOM   6748 C  CA  . GLN B 2 244 ? 230.503 185.005 154.215 1.00 35.27  ? 572  GLN B CA  1 
ATOM   6749 C  C   . GLN B 2 244 ? 231.857 185.183 154.878 1.00 36.46  ? 572  GLN B C   1 
ATOM   6750 O  O   . GLN B 2 244 ? 231.950 185.300 156.101 1.00 36.08  ? 572  GLN B O   1 
ATOM   6751 C  CB  . GLN B 2 244 ? 229.763 186.342 154.203 1.00 35.46  ? 572  GLN B CB  1 
ATOM   6752 C  CG  . GLN B 2 244 ? 230.515 187.459 153.502 1.00 36.62  ? 572  GLN B CG  1 
ATOM   6753 C  CD  . GLN B 2 244 ? 229.736 188.747 153.475 1.00 37.06  ? 572  GLN B CD  1 
ATOM   6754 O  OE1 . GLN B 2 244 ? 229.209 189.195 154.497 1.00 38.53  ? 572  GLN B OE1 1 
ATOM   6755 N  NE2 . GLN B 2 244 ? 229.654 189.358 152.301 1.00 36.95  ? 572  GLN B NE2 1 
ATOM   6756 N  N   . THR B 2 245 ? 232.907 185.224 154.063 1.00 36.92  ? 573  THR B N   1 
ATOM   6757 C  CA  . THR B 2 245 ? 234.260 185.415 154.574 1.00 38.42  ? 573  THR B CA  1 
ATOM   6758 C  C   . THR B 2 245 ? 234.773 186.809 154.219 1.00 40.36  ? 573  THR B C   1 
ATOM   6759 O  O   . THR B 2 245 ? 234.659 187.247 153.074 1.00 39.31  ? 573  THR B O   1 
ATOM   6760 C  CB  . THR B 2 245 ? 235.233 184.356 154.013 1.00 38.21  ? 573  THR B CB  1 
ATOM   6761 O  OG1 . THR B 2 245 ? 234.760 183.043 154.330 1.00 38.10  ? 573  THR B OG1 1 
ATOM   6762 C  CG2 . THR B 2 245 ? 236.606 184.540 154.646 1.00 39.78  ? 573  THR B CG2 1 
ATOM   6763 N  N   . LYS B 2 246 ? 235.334 187.501 155.207 1.00 41.78  ? 574  LYS B N   1 
ATOM   6764 C  CA  . LYS B 2 246 ? 235.876 188.842 155.016 1.00 43.05  ? 574  LYS B CA  1 
ATOM   6765 C  C   . LYS B 2 246 ? 237.349 188.921 155.411 1.00 44.22  ? 574  LYS B C   1 
ATOM   6766 O  O   . LYS B 2 246 ? 237.809 188.196 156.295 1.00 43.80  ? 574  LYS B O   1 
ATOM   6767 C  CB  . LYS B 2 246 ? 235.069 189.855 155.828 1.00 43.93  ? 574  LYS B CB  1 
ATOM   6768 C  CG  . LYS B 2 246 ? 233.606 189.975 155.413 1.00 42.51  ? 574  LYS B CG  1 
ATOM   6769 C  CD  . LYS B 2 246 ? 232.876 191.059 156.211 1.00 43.87  ? 574  LYS B CD  1 
ATOM   6770 C  CE  . LYS B 2 246 ? 232.515 190.579 157.612 1.00 44.61  ? 574  LYS B CE  1 
ATOM   6771 N  NZ  . LYS B 2 246 ? 231.666 191.574 158.350 1.00 45.38  ? 574  LYS B NZ  1 
ATOM   6772 N  N   . GLU B 2 247 ? 238.078 189.835 154.777 1.00 45.29  ? 575  GLU B N   1 
ATOM   6773 C  CA  . GLU B 2 247 ? 239.478 190.085 155.113 1.00 46.86  ? 575  GLU B CA  1 
ATOM   6774 C  C   . GLU B 2 247 ? 239.593 190.832 156.450 1.00 47.17  ? 575  GLU B C   1 
ATOM   6775 O  O   . GLU B 2 247 ? 238.633 191.473 156.874 1.00 47.32  ? 575  GLU B O   1 
ATOM   6776 C  CB  . GLU B 2 247 ? 240.146 190.895 153.998 1.00 47.02  ? 575  GLU B CB  1 
ATOM   6777 N  N   . PRO B 2 248 ? 240.745 190.750 157.132 1.00 47.53  ? 576  PRO B N   1 
ATOM   6778 C  CA  . PRO B 2 248 ? 241.106 191.530 158.306 1.00 49.29  ? 576  PRO B CA  1 
ATOM   6779 C  C   . PRO B 2 248 ? 241.125 193.023 157.999 1.00 49.64  ? 576  PRO B C   1 
ATOM   6780 O  O   . PRO B 2 248 ? 241.395 193.424 156.866 1.00 50.14  ? 576  PRO B O   1 
ATOM   6781 C  CB  . PRO B 2 248 ? 242.516 191.018 158.634 1.00 49.96  ? 576  PRO B CB  1 
ATOM   6782 C  CG  . PRO B 2 248 ? 242.598 189.649 157.990 1.00 47.83  ? 576  PRO B CG  1 
ATOM   6783 C  CD  . PRO B 2 248 ? 241.750 189.746 156.743 1.00 46.86  ? 576  PRO B CD  1 
ATOM   6784 N  N   . SER B 2 249 ? 240.838 193.841 159.011 1.00 51.47  ? 577  SER B N   1 
ATOM   6785 C  CA  . SER B 2 249 ? 240.879 195.292 158.857 1.00 52.93  ? 577  SER B CA  1 
ATOM   6786 C  C   . SER B 2 249 ? 242.180 195.856 159.413 1.00 53.42  ? 577  SER B C   1 
ATOM   6787 O  O   . SER B 2 249 ? 242.691 196.868 158.932 1.00 55.08  ? 577  SER B O   1 
ATOM   6788 C  CB  . SER B 2 249 ? 239.705 195.928 159.572 1.00 50.92  ? 577  SER B CB  1 
ATOM   6789 N  N   . VAL B 2 250 ? 242.717 195.184 160.424 1.00 53.91  ? 578  VAL B N   1 
ATOM   6790 C  CA  . VAL B 2 250 ? 243.950 195.604 161.070 1.00 56.06  ? 578  VAL B CA  1 
ATOM   6791 C  C   . VAL B 2 250 ? 245.083 194.677 160.656 1.00 55.57  ? 578  VAL B C   1 
ATOM   6792 O  O   . VAL B 2 250 ? 244.966 193.457 160.767 1.00 56.24  ? 578  VAL B O   1 
ATOM   6793 C  CB  . VAL B 2 250 ? 243.792 195.580 162.602 1.00 57.29  ? 578  VAL B CB  1 
ATOM   6794 N  N   . THR B 2 251 ? 246.168 195.250 160.156 1.00 57.79  ? 579  THR B N   1 
ATOM   6795 C  CA  . THR B 2 251 ? 247.277 194.440 159.670 1.00 58.71  ? 579  THR B CA  1 
ATOM   6796 C  C   . THR B 2 251 ? 247.992 193.704 160.800 1.00 59.47  ? 579  THR B C   1 
ATOM   6797 O  O   . THR B 2 251 ? 248.381 194.306 161.801 1.00 59.47  ? 579  THR B O   1 
ATOM   6798 C  CB  . THR B 2 251 ? 248.289 195.303 158.888 1.00 58.73  ? 579  THR B CB  1 
ATOM   6799 N  N   . ASP B 2 252 ? 248.181 192.400 160.608 1.00 58.11  ? 580  ASP B N   1 
ATOM   6800 C  CA  . ASP B 2 252 ? 248.916 191.538 161.533 1.00 59.82  ? 580  ASP B CA  1 
ATOM   6801 C  C   . ASP B 2 252 ? 248.412 191.600 162.972 1.00 58.94  ? 580  ASP B C   1 
ATOM   6802 O  O   . ASP B 2 252 ? 249.208 191.583 163.912 1.00 59.93  ? 580  ASP B O   1 
ATOM   6803 C  CB  . ASP B 2 252 ? 250.407 191.874 161.503 1.00 58.75  ? 580  ASP B CB  1 
ATOM   6804 N  N   . LYS B 2 253 ? 247.096 191.647 163.146 1.00 58.35  ? 581  LYS B N   1 
ATOM   6805 C  CA  . LYS B 2 253 ? 246.496 191.640 164.476 1.00 57.54  ? 581  LYS B CA  1 
ATOM   6806 C  C   . LYS B 2 253 ? 245.243 190.782 164.500 1.00 57.21  ? 581  LYS B C   1 
ATOM   6807 O  O   . LYS B 2 253 ? 244.520 190.689 163.510 1.00 57.29  ? 581  LYS B O   1 
ATOM   6808 C  CB  . LYS B 2 253 ? 246.138 193.056 164.932 1.00 58.25  ? 581  LYS B CB  1 
ATOM   6809 N  N   . ALA B 2 254 ? 244.955 190.206 165.656 1.00 57.55  ? 582  ALA B N   1 
ATOM   6810 C  CA  . ALA B 2 254 ? 243.702 189.508 165.870 1.00 55.04  ? 582  ALA B CA  1 
ATOM   6811 C  C   . ALA B 2 254 ? 242.659 190.480 166.384 1.00 55.19  ? 582  ALA B C   1 
ATOM   6812 O  O   . ALA B 2 254 ? 242.878 191.162 167.384 1.00 57.08  ? 582  ALA B O   1 
ATOM   6813 C  CB  . ALA B 2 254 ? 243.881 188.370 166.859 1.00 56.57  ? 582  ALA B CB  1 
ATOM   6814 N  N   . GLU B 2 255 ? 241.530 190.542 165.699 1.00 55.20  ? 583  GLU B N   1 
ATOM   6815 C  CA  . GLU B 2 255 ? 240.441 191.425 166.083 1.00 54.14  ? 583  GLU B CA  1 
ATOM   6816 C  C   . GLU B 2 255 ? 239.361 190.615 166.797 1.00 54.17  ? 583  GLU B C   1 
ATOM   6817 O  O   . GLU B 2 255 ? 238.847 189.645 166.242 1.00 51.06  ? 583  GLU B O   1 
ATOM   6818 C  CB  . GLU B 2 255 ? 239.887 192.112 164.833 1.00 51.81  ? 583  GLU B CB  1 
ATOM   6819 C  CG  . GLU B 2 255 ? 240.914 192.974 164.065 1.00 53.45  ? 583  GLU B CG  1 
ATOM   6820 C  CD  . GLU B 2 255 ? 240.417 193.421 162.714 1.00 51.32  ? 583  GLU B CD  1 
ATOM   6821 O  OE1 . GLU B 2 255 ? 239.421 194.090 162.666 1.00 51.25  ? 583  GLU B OE1 1 
ATOM   6822 O  OE2 . GLU B 2 255 ? 241.032 193.090 161.724 1.00 52.25  ? 583  GLU B OE2 1 
ATOM   6823 N  N   . LEU B 2 256 ? 239.075 190.960 168.049 1.00 55.03  ? 584  LEU B N   1 
ATOM   6824 C  CA  . LEU B 2 256 ? 238.167 190.154 168.863 1.00 52.29  ? 584  LEU B CA  1 
ATOM   6825 C  C   . LEU B 2 256 ? 237.038 190.961 169.490 1.00 51.59  ? 584  LEU B C   1 
ATOM   6826 O  O   . LEU B 2 256 ? 237.200 192.136 169.825 1.00 53.10  ? 584  LEU B O   1 
ATOM   6827 C  CB  . LEU B 2 256 ? 238.951 189.453 169.981 1.00 53.62  ? 584  LEU B CB  1 
ATOM   6828 N  N   . ALA B 2 257 ? 235.905 190.297 169.701 1.00 52.39  ? 585  ALA B N   1 
ATOM   6829 C  CA  . ALA B 2 257 ? 234.789 190.874 170.439 1.00 52.73  ? 585  ALA B CA  1 
ATOM   6830 C  C   . ALA B 2 257 ? 234.545 190.078 171.718 1.00 52.20  ? 585  ALA B C   1 
ATOM   6831 O  O   . ALA B 2 257 ? 234.532 188.845 171.699 1.00 51.07  ? 585  ALA B O   1 
ATOM   6832 C  CB  . ALA B 2 257 ? 233.536 190.895 169.575 1.00 51.62  ? 585  ALA B CB  1 
ATOM   6833 N  N   . PHE B 2 258 ? 234.338 190.781 172.827 1.00 51.90  ? 586  PHE B N   1 
ATOM   6834 C  CA  . PHE B 2 258 ? 234.083 190.119 174.101 1.00 53.01  ? 586  PHE B CA  1 
ATOM   6835 C  C   . PHE B 2 258 ? 232.792 190.615 174.739 1.00 54.21  ? 586  PHE B C   1 
ATOM   6836 O  O   . PHE B 2 258 ? 232.528 191.814 174.801 1.00 55.34  ? 586  PHE B O   1 
ATOM   6837 C  CB  . PHE B 2 258 ? 235.227 190.375 175.090 1.00 54.38  ? 586  PHE B CB  1 
ATOM   6838 C  CG  . PHE B 2 258 ? 236.585 189.926 174.633 1.00 53.02  ? 586  PHE B CG  1 
ATOM   6839 C  CD1 . PHE B 2 258 ? 237.367 190.755 173.841 1.00 53.91  ? 586  PHE B CD1 1 
ATOM   6840 C  CD2 . PHE B 2 258 ? 237.096 188.689 175.006 1.00 52.87  ? 586  PHE B CD2 1 
ATOM   6841 C  CE1 . PHE B 2 258 ? 238.621 190.358 173.426 1.00 54.93  ? 586  PHE B CE1 1 
ATOM   6842 C  CE2 . PHE B 2 258 ? 238.352 188.291 174.588 1.00 54.56  ? 586  PHE B CE2 1 
ATOM   6843 C  CZ  . PHE B 2 258 ? 239.110 189.126 173.797 1.00 55.45  ? 586  PHE B CZ  1 
ATOM   6844 N  N   . PHE B 2 259 ? 232.023 189.680 175.274 1.00 52.50  ? 587  PHE B N   1 
ATOM   6845 C  CA  . PHE B 2 259 ? 230.839 189.995 176.055 1.00 54.31  ? 587  PHE B CA  1 
ATOM   6846 C  C   . PHE B 2 259 ? 231.032 189.484 177.471 1.00 56.30  ? 587  PHE B C   1 
ATOM   6847 O  O   . PHE B 2 259 ? 231.104 188.276 177.704 1.00 56.27  ? 587  PHE B O   1 
ATOM   6848 C  CB  . PHE B 2 259 ? 229.590 189.389 175.415 1.00 52.88  ? 587  PHE B CB  1 
ATOM   6849 C  CG  . PHE B 2 259 ? 229.240 190.021 174.103 1.00 51.25  ? 587  PHE B CG  1 
ATOM   6850 C  CD1 . PHE B 2 259 ? 229.942 189.695 172.955 1.00 50.90  ? 587  PHE B CD1 1 
ATOM   6851 C  CD2 . PHE B 2 259 ? 228.207 190.941 174.012 1.00 51.56  ? 587  PHE B CD2 1 
ATOM   6852 C  CE1 . PHE B 2 259 ? 229.627 190.276 171.746 1.00 49.77  ? 587  PHE B CE1 1 
ATOM   6853 C  CE2 . PHE B 2 259 ? 227.885 191.520 172.802 1.00 51.10  ? 587  PHE B CE2 1 
ATOM   6854 C  CZ  . PHE B 2 259 ? 228.598 191.186 171.666 1.00 50.02  ? 587  PHE B CZ  1 
ATOM   6855 N  N   . VAL B 2 260 ? 231.181 190.406 178.410 1.00 56.92  ? 588  VAL B N   1 
ATOM   6856 C  CA  . VAL B 2 260 ? 231.524 190.037 179.774 1.00 56.22  ? 588  VAL B CA  1 
ATOM   6857 C  C   . VAL B 2 260 ? 230.382 190.348 180.727 1.00 60.30  ? 588  VAL B C   1 
ATOM   6858 O  O   . VAL B 2 260 ? 229.935 191.493 180.821 1.00 60.66  ? 588  VAL B O   1 
ATOM   6859 C  CB  . VAL B 2 260 ? 232.802 190.780 180.204 1.00 58.18  ? 588  VAL B CB  1 
ATOM   6860 N  N   . SER B 2 261 ? 229.897 189.326 181.421 1.00 62.31  ? 589  SER B N   1 
ATOM   6861 C  CA  . SER B 2 261 ? 228.743 189.493 182.300 1.00 63.30  ? 589  SER B CA  1 
ATOM   6862 C  C   . SER B 2 261 ? 229.011 188.904 183.680 1.00 63.31  ? 589  SER B C   1 
ATOM   6863 O  O   . SER B 2 261 ? 229.881 188.046 183.839 1.00 63.79  ? 589  SER B O   1 
ATOM   6864 C  CB  . SER B 2 261 ? 227.522 188.837 181.684 1.00 63.17  ? 589  SER B CB  1 
HETATM 6865 C  C1  . NAG C 3 .   ? 159.300 207.038 151.963 1.00 10.86  ? 1    NAG C C1  1 
HETATM 6866 C  C2  . NAG C 3 .   ? 160.049 208.286 151.394 1.00 11.23  ? 1    NAG C C2  1 
HETATM 6867 C  C3  . NAG C 3 .   ? 159.235 209.531 151.750 1.00 11.63  ? 1    NAG C C3  1 
HETATM 6868 C  C4  . NAG C 3 .   ? 157.841 209.385 151.126 1.00 12.12  ? 1    NAG C C4  1 
HETATM 6869 C  C5  . NAG C 3 .   ? 157.191 208.127 151.684 1.00 11.78  ? 1    NAG C C5  1 
HETATM 6870 C  C6  . NAG C 3 .   ? 155.816 207.898 151.064 1.00 12.18  ? 1    NAG C C6  1 
HETATM 6871 C  C7  . NAG C 3 .   ? 162.431 207.970 151.364 1.00 11.00  ? 1    NAG C C7  1 
HETATM 6872 C  C8  . NAG C 3 .   ? 163.788 208.062 151.999 1.00 10.80  ? 1    NAG C C8  1 
HETATM 6873 N  N2  . NAG C 3 .   ? 161.371 208.383 152.029 1.00 11.11  ? 1    NAG C N2  1 
HETATM 6874 O  O3  . NAG C 3 .   ? 159.898 210.687 151.242 1.00 12.07  ? 1    NAG C O3  1 
HETATM 6875 O  O4  . NAG C 3 .   ? 157.042 210.542 151.468 1.00 13.25  ? 1    NAG C O4  1 
HETATM 6876 O  O5  . NAG C 3 .   ? 158.011 206.942 151.385 1.00 11.42  ? 1    NAG C O5  1 
HETATM 6877 O  O6  . NAG C 3 .   ? 155.233 206.692 151.554 1.00 11.79  ? 1    NAG C O6  1 
HETATM 6878 O  O7  . NAG C 3 .   ? 162.307 207.465 150.243 1.00 11.36  ? 1    NAG C O7  1 
HETATM 6879 C  C1  . NAG C 3 .   ? 156.648 211.355 150.287 1.00 13.56  ? 2    NAG C C1  1 
HETATM 6880 C  C2  . NAG C 3 .   ? 155.628 212.435 150.717 1.00 13.81  ? 2    NAG C C2  1 
HETATM 6881 C  C3  . NAG C 3 .   ? 155.193 213.246 149.475 1.00 14.41  ? 2    NAG C C3  1 
HETATM 6882 C  C4  . NAG C 3 .   ? 156.455 213.885 148.838 1.00 14.56  ? 2    NAG C C4  1 
HETATM 6883 C  C5  . NAG C 3 .   ? 157.448 212.760 148.457 1.00 14.22  ? 2    NAG C C5  1 
HETATM 6884 C  C6  . NAG C 3 .   ? 158.737 213.327 147.884 1.00 14.30  ? 2    NAG C C6  1 
HETATM 6885 C  C7  . NAG C 3 .   ? 154.273 211.750 152.612 1.00 14.02  ? 2    NAG C C7  1 
HETATM 6886 C  C8  . NAG C 3 .   ? 153.072 211.053 153.187 1.00 14.15  ? 2    NAG C C8  1 
HETATM 6887 N  N2  . NAG C 3 .   ? 154.446 211.776 151.294 1.00 14.16  ? 2    NAG C N2  1 
HETATM 6888 O  O3  . NAG C 3 .   ? 154.286 214.273 149.877 1.00 14.34  ? 2    NAG C O3  1 
HETATM 6889 O  O4  . NAG C 3 .   ? 156.066 214.621 147.680 1.00 14.67  ? 2    NAG C O4  1 
HETATM 6890 O  O5  . NAG C 3 .   ? 157.798 211.970 149.652 1.00 13.84  ? 2    NAG C O5  1 
HETATM 6891 O  O6  . NAG C 3 .   ? 159.431 212.359 147.103 1.00 15.00  ? 2    NAG C O6  1 
HETATM 6892 O  O7  . NAG C 3 .   ? 155.099 212.251 153.369 1.00 14.08  ? 2    NAG C O7  1 
HETATM 6893 C  C1  . FUC C 3 .   ? 154.363 206.894 152.728 1.00 11.96  ? 3    FUC C C1  1 
HETATM 6894 C  C2  . FUC C 3 .   ? 153.437 205.661 152.860 1.00 11.75  ? 3    FUC C C2  1 
HETATM 6895 C  C3  . FUC C 3 .   ? 154.314 204.424 153.150 1.00 11.07  ? 3    FUC C C3  1 
HETATM 6896 C  C4  . FUC C 3 .   ? 155.111 204.667 154.447 1.00 11.17  ? 3    FUC C C4  1 
HETATM 6897 C  C5  . FUC C 3 .   ? 155.975 205.946 154.273 1.00 11.32  ? 3    FUC C C5  1 
HETATM 6898 C  C6  . FUC C 3 .   ? 156.732 206.292 155.523 1.00 11.28  ? 3    FUC C C6  1 
HETATM 6899 O  O2  . FUC C 3 .   ? 152.747 205.480 151.636 1.00 11.85  ? 3    FUC C O2  1 
HETATM 6900 O  O3  . FUC C 3 .   ? 153.480 203.262 153.270 1.00 10.88  ? 3    FUC C O3  1 
HETATM 6901 O  O4  . FUC C 3 .   ? 154.214 204.800 155.551 1.00 11.74  ? 3    FUC C O4  1 
HETATM 6902 O  O5  . FUC C 3 .   ? 155.136 207.088 153.944 1.00 11.99  ? 3    FUC C O5  1 
HETATM 6903 C  C1  . NAG D 4 .   ? 185.340 210.245 146.376 1.00 8.97   ? 1    NAG D C1  1 
HETATM 6904 C  C2  . NAG D 4 .   ? 185.486 209.065 145.363 1.00 8.98   ? 1    NAG D C2  1 
HETATM 6905 C  C3  . NAG D 4 .   ? 186.356 209.558 144.185 1.00 9.92   ? 1    NAG D C3  1 
HETATM 6906 C  C4  . NAG D 4 .   ? 185.684 210.779 143.505 1.00 10.53  ? 1    NAG D C4  1 
HETATM 6907 C  C5  . NAG D 4 .   ? 185.530 211.885 144.573 1.00 10.51  ? 1    NAG D C5  1 
HETATM 6908 C  C6  . NAG D 4 .   ? 184.796 213.101 144.016 1.00 11.30  ? 1    NAG D C6  1 
HETATM 6909 C  C7  . NAG D 4 .   ? 185.586 206.745 146.083 1.00 7.14   ? 1    NAG D C7  1 
HETATM 6910 C  C8  . NAG D 4 .   ? 186.292 205.603 146.737 1.00 6.57   ? 1    NAG D C8  1 
HETATM 6911 N  N2  . NAG D 4 .   ? 186.167 207.938 146.016 1.00 8.37   ? 1    NAG D N2  1 
HETATM 6912 O  O3  . NAG D 4 .   ? 186.519 208.493 143.246 1.00 10.28  ? 1    NAG D O3  1 
HETATM 6913 O  O4  . NAG D 4 .   ? 186.537 211.265 142.465 1.00 11.73  ? 1    NAG D O4  1 
HETATM 6914 O  O5  . NAG D 4 .   ? 184.759 211.386 145.707 1.00 9.70   ? 1    NAG D O5  1 
HETATM 6915 O  O6  . NAG D 4 .   ? 185.074 214.271 144.799 1.00 12.16  ? 1    NAG D O6  1 
HETATM 6916 O  O7  . NAG D 4 .   ? 184.461 206.559 145.604 1.00 7.04   ? 1    NAG D O7  1 
HETATM 6917 C  C1  . NAG D 4 .   ? 185.990 211.015 141.089 1.00 11.99  ? 2    NAG D C1  1 
HETATM 6918 C  C2  . NAG D 4 .   ? 186.747 211.946 140.081 1.00 12.00  ? 2    NAG D C2  1 
HETATM 6919 C  C3  . NAG D 4 .   ? 186.178 211.697 138.669 1.00 12.46  ? 2    NAG D C3  1 
HETATM 6920 C  C4  . NAG D 4 .   ? 186.354 210.209 138.306 1.00 12.63  ? 2    NAG D C4  1 
HETATM 6921 C  C5  . NAG D 4 .   ? 185.615 209.351 139.363 1.00 12.37  ? 2    NAG D C5  1 
HETATM 6922 C  C6  . NAG D 4 .   ? 185.797 207.866 139.095 1.00 12.68  ? 2    NAG D C6  1 
HETATM 6923 C  C7  . NAG D 4 .   ? 187.482 214.031 141.072 1.00 12.29  ? 2    NAG D C7  1 
HETATM 6924 C  C8  . NAG D 4 .   ? 187.245 215.466 141.439 1.00 12.30  ? 2    NAG D C8  1 
HETATM 6925 N  N2  . NAG D 4 .   ? 186.531 213.340 140.450 1.00 12.20  ? 2    NAG D N2  1 
HETATM 6926 O  O3  . NAG D 4 .   ? 186.878 212.509 137.719 1.00 12.51  ? 2    NAG D O3  1 
HETATM 6927 O  O4  . NAG D 4 .   ? 185.811 209.973 137.010 1.00 12.77  ? 2    NAG D O4  1 
HETATM 6928 O  O5  . NAG D 4 .   ? 186.132 209.639 140.707 1.00 11.92  ? 2    NAG D O5  1 
HETATM 6929 O  O6  . NAG D 4 .   ? 187.175 207.512 139.074 1.00 12.91  ? 2    NAG D O6  1 
HETATM 6930 O  O7  . NAG D 4 .   ? 188.566 213.501 141.352 1.00 12.21  ? 2    NAG D O7  1 
HETATM 6931 C  C1  . NAG E 4 .   ? 190.206 162.343 157.529 1.00 9.35   ? 1    NAG E C1  1 
HETATM 6932 C  C2  . NAG E 4 .   ? 188.682 162.024 157.692 1.00 9.70   ? 1    NAG E C2  1 
HETATM 6933 C  C3  . NAG E 4 .   ? 188.336 162.076 159.188 1.00 10.70  ? 1    NAG E C3  1 
HETATM 6934 C  C4  . NAG E 4 .   ? 189.203 161.050 159.958 1.00 11.31  ? 1    NAG E C4  1 
HETATM 6935 C  C5  . NAG E 4 .   ? 190.688 161.402 159.716 1.00 11.19  ? 1    NAG E C5  1 
HETATM 6936 C  C6  . NAG E 4 .   ? 191.623 160.413 160.392 1.00 11.87  ? 1    NAG E C6  1 
HETATM 6937 C  C7  . NAG E 4 .   ? 187.384 162.798 155.786 1.00 8.46   ? 1    NAG E C7  1 
HETATM 6938 C  C8  . NAG E 4 .   ? 186.603 163.842 155.061 1.00 6.65   ? 1    NAG E C8  1 
HETATM 6939 N  N2  . NAG E 4 .   ? 187.907 163.052 156.982 1.00 9.32   ? 1    NAG E N2  1 
HETATM 6940 O  O3  . NAG E 4 .   ? 186.948 161.766 159.348 1.00 11.15  ? 1    NAG E O3  1 
HETATM 6941 O  O4  . NAG E 4 .   ? 188.916 161.175 161.350 1.00 12.95  ? 1    NAG E O4  1 
HETATM 6942 O  O5  . NAG E 4 .   ? 190.986 161.392 158.287 1.00 10.26  ? 1    NAG E O5  1 
HETATM 6943 O  O6  . NAG E 4 .   ? 192.972 160.896 160.377 1.00 11.86  ? 1    NAG E O6  1 
HETATM 6944 O  O7  . NAG E 4 .   ? 187.552 161.691 155.258 1.00 8.32   ? 1    NAG E O7  1 
HETATM 6945 C  C1  . NAG E 4 .   ? 188.430 159.892 161.956 1.00 13.04  ? 2    NAG E C1  1 
HETATM 6946 C  C2  . NAG E 4 .   ? 188.574 160.000 163.511 1.00 12.64  ? 2    NAG E C2  1 
HETATM 6947 C  C3  . NAG E 4 .   ? 188.084 158.676 164.128 1.00 13.94  ? 2    NAG E C3  1 
HETATM 6948 C  C4  . NAG E 4 .   ? 186.619 158.426 163.707 1.00 13.91  ? 2    NAG E C4  1 
HETATM 6949 C  C5  . NAG E 4 .   ? 186.548 158.363 162.160 1.00 13.90  ? 2    NAG E C5  1 
HETATM 6950 C  C6  . NAG E 4 .   ? 185.115 158.170 161.672 1.00 14.31  ? 2    NAG E C6  1 
HETATM 6951 C  C7  . NAG E 4 .   ? 190.422 161.404 164.218 1.00 13.22  ? 2    NAG E C7  1 
HETATM 6952 C  C8  . NAG E 4 .   ? 191.865 161.588 164.581 1.00 13.32  ? 2    NAG E C8  1 
HETATM 6953 N  N2  . NAG E 4 .   ? 189.976 160.202 163.865 1.00 13.39  ? 2    NAG E N2  1 
HETATM 6954 O  O3  . NAG E 4 .   ? 188.170 158.761 165.553 1.00 13.67  ? 2    NAG E O3  1 
HETATM 6955 O  O4  . NAG E 4 .   ? 186.176 157.194 164.273 1.00 13.86  ? 2    NAG E O4  1 
HETATM 6956 O  O5  . NAG E 4 .   ? 187.066 159.608 161.585 1.00 13.05  ? 2    NAG E O5  1 
HETATM 6957 O  O6  . NAG E 4 .   ? 184.272 159.228 162.114 1.00 14.16  ? 2    NAG E O6  1 
HETATM 6958 O  O7  . NAG E 4 .   ? 189.653 162.375 164.255 1.00 13.05  ? 2    NAG E O7  1 
HETATM 6959 C  C1  . NAG F 3 .   ? 209.548 197.871 168.601 1.00 24.94  ? 1    NAG F C1  1 
HETATM 6960 C  C2  . NAG F 3 .   ? 209.392 198.446 170.030 1.00 24.66  ? 1    NAG F C2  1 
HETATM 6961 C  C3  . NAG F 3 .   ? 209.611 199.975 169.961 1.00 27.11  ? 1    NAG F C3  1 
HETATM 6962 C  C4  . NAG F 3 .   ? 211.014 200.242 169.396 1.00 29.61  ? 1    NAG F C4  1 
HETATM 6963 C  C5  . NAG F 3 .   ? 211.087 199.619 167.998 1.00 29.81  ? 1    NAG F C5  1 
HETATM 6964 C  C6  . NAG F 3 .   ? 212.450 199.844 167.364 1.00 32.20  ? 1    NAG F C6  1 
HETATM 6965 C  C7  . NAG F 3 .   ? 207.896 197.574 171.683 1.00 22.55  ? 1    NAG F C7  1 
HETATM 6966 C  C8  . NAG F 3 .   ? 206.514 197.292 172.194 1.00 19.20  ? 1    NAG F C8  1 
HETATM 6967 N  N2  . NAG F 3 .   ? 208.041 198.188 170.515 1.00 23.62  ? 1    NAG F N2  1 
HETATM 6968 O  O3  . NAG F 3 .   ? 209.498 200.523 171.281 1.00 28.15  ? 1    NAG F O3  1 
HETATM 6969 O  O4  . NAG F 3 .   ? 211.215 201.668 169.271 1.00 30.40  ? 1    NAG F O4  1 
HETATM 6970 O  O5  . NAG F 3 .   ? 210.852 198.170 168.081 1.00 27.88  ? 1    NAG F O5  1 
HETATM 6971 O  O6  . NAG F 3 .   ? 213.440 199.005 167.933 1.00 32.44  ? 1    NAG F O6  1 
HETATM 6972 O  O7  . NAG F 3 .   ? 208.881 197.227 172.338 1.00 24.16  ? 1    NAG F O7  1 
HETATM 6973 C  C1  . NAG F 3 .   ? 212.168 202.211 170.295 1.00 31.29  ? 2    NAG F C1  1 
HETATM 6974 C  C2  . NAG F 3 .   ? 212.702 203.569 169.760 1.00 32.34  ? 2    NAG F C2  1 
HETATM 6975 C  C3  . NAG F 3 .   ? 213.700 204.125 170.789 1.00 32.43  ? 2    NAG F C3  1 
HETATM 6976 C  C4  . NAG F 3 .   ? 212.975 204.296 172.143 1.00 33.16  ? 2    NAG F C4  1 
HETATM 6977 C  C5  . NAG F 3 .   ? 212.423 202.926 172.602 1.00 32.51  ? 2    NAG F C5  1 
HETATM 6978 C  C6  . NAG F 3 .   ? 211.607 203.048 173.879 1.00 32.19  ? 2    NAG F C6  1 
HETATM 6979 C  C7  . NAG F 3 .   ? 212.930 203.868 167.354 1.00 32.65  ? 2    NAG F C7  1 
HETATM 6980 C  C8  . NAG F 3 .   ? 213.666 203.650 166.068 1.00 33.55  ? 2    NAG F C8  1 
HETATM 6981 N  N2  . NAG F 3 .   ? 213.408 203.366 168.478 1.00 32.48  ? 2    NAG F N2  1 
HETATM 6982 O  O3  . NAG F 3 .   ? 214.192 205.391 170.356 1.00 32.70  ? 2    NAG F O3  1 
HETATM 6983 O  O4  . NAG F 3 .   ? 213.889 204.805 173.107 1.00 32.88  ? 2    NAG F O4  1 
HETATM 6984 O  O5  . NAG F 3 .   ? 211.529 202.385 171.568 1.00 31.55  ? 2    NAG F O5  1 
HETATM 6985 O  O6  . NAG F 3 .   ? 211.481 201.796 174.551 1.00 32.26  ? 2    NAG F O6  1 
HETATM 6986 O  O7  . NAG F 3 .   ? 211.866 204.502 167.344 1.00 32.47  ? 2    NAG F O7  1 
HETATM 6987 C  C1  . FUC F 3 .   ? 214.633 198.878 167.038 1.00 35.02  ? 3    FUC F C1  1 
HETATM 6988 C  C2  . FUC F 3 .   ? 215.659 197.935 167.718 1.00 35.57  ? 3    FUC F C2  1 
HETATM 6989 C  C3  . FUC F 3 .   ? 214.994 196.544 167.834 1.00 36.18  ? 3    FUC F C3  1 
HETATM 6990 C  C4  . FUC F 3 .   ? 214.579 196.037 166.441 1.00 36.38  ? 3    FUC F C4  1 
HETATM 6991 C  C5  . FUC F 3 .   ? 213.629 197.082 165.806 1.00 34.99  ? 3    FUC F C5  1 
HETATM 6992 C  C6  . FUC F 3 .   ? 213.166 196.665 164.446 1.00 35.38  ? 3    FUC F C6  1 
HETATM 6993 O  O2  . FUC F 3 .   ? 216.055 198.407 168.994 1.00 36.99  ? 3    FUC F O2  1 
HETATM 6994 O  O3  . FUC F 3 .   ? 215.865 195.607 168.470 1.00 38.33  ? 3    FUC F O3  1 
HETATM 6995 O  O4  . FUC F 3 .   ? 215.727 195.839 165.596 1.00 38.06  ? 3    FUC F O4  1 
HETATM 6996 O  O5  . FUC F 3 .   ? 214.253 198.408 165.740 1.00 34.79  ? 3    FUC F O5  1 
HETATM 6997 C  C1  . NAG G 5 .   ? 202.395 187.102 179.295 1.00 14.17  ? 1    NAG G C1  1 
HETATM 6998 C  C2  . NAG G 5 .   ? 202.829 185.627 179.011 1.00 14.44  ? 1    NAG G C2  1 
HETATM 6999 C  C3  . NAG G 5 .   ? 202.683 184.817 180.337 1.00 15.75  ? 1    NAG G C3  1 
HETATM 7000 C  C4  . NAG G 5 .   ? 203.564 185.437 181.456 1.00 16.74  ? 1    NAG G C4  1 
HETATM 7001 C  C5  . NAG G 5 .   ? 203.123 186.916 181.611 1.00 15.96  ? 1    NAG G C5  1 
HETATM 7002 C  C6  . NAG G 5 .   ? 203.992 187.630 182.634 1.00 16.75  ? 1    NAG G C6  1 
HETATM 7003 C  C7  . NAG G 5 .   ? 202.317 184.982 176.722 1.00 13.29  ? 1    NAG G C7  1 
HETATM 7004 C  C8  . NAG G 5 .   ? 201.394 184.418 175.696 1.00 12.06  ? 1    NAG G C8  1 
HETATM 7005 N  N2  . NAG G 5 .   ? 201.927 185.072 177.996 1.00 13.80  ? 1    NAG G N2  1 
HETATM 7006 O  O3  . NAG G 5 .   ? 203.104 183.480 180.128 1.00 15.56  ? 1    NAG G O3  1 
HETATM 7007 O  O4  . NAG G 5 .   ? 203.366 184.730 182.695 1.00 18.23  ? 1    NAG G O4  1 
HETATM 7008 O  O5  . NAG G 5 .   ? 203.217 187.645 180.353 1.00 14.79  ? 1    NAG G O5  1 
HETATM 7009 O  O6  . NAG G 5 .   ? 205.352 187.657 182.247 1.00 16.78  ? 1    NAG G O6  1 
HETATM 7010 O  O7  . NAG G 5 .   ? 203.449 185.362 176.378 1.00 13.30  ? 1    NAG G O7  1 
HETATM 7011 C  C1  . NAG G 5 .   ? 204.453 183.954 183.118 1.00 19.10  ? 2    NAG G C1  1 
HETATM 7012 C  C2  . NAG G 5 .   ? 204.750 184.012 184.616 1.00 19.23  ? 2    NAG G C2  1 
HETATM 7013 C  C3  . NAG G 5 .   ? 206.097 183.353 184.894 1.00 20.82  ? 2    NAG G C3  1 
HETATM 7014 C  C4  . NAG G 5 .   ? 206.135 181.955 184.286 1.00 21.52  ? 2    NAG G C4  1 
HETATM 7015 C  C5  . NAG G 5 .   ? 205.882 182.058 182.781 1.00 19.98  ? 2    NAG G C5  1 
HETATM 7016 C  C6  . NAG G 5 .   ? 205.849 180.723 182.078 1.00 20.83  ? 2    NAG G C6  1 
HETATM 7017 C  C7  . NAG G 5 .   ? 203.788 185.885 185.875 1.00 20.63  ? 2    NAG G C7  1 
HETATM 7018 C  C8  . NAG G 5 .   ? 202.653 184.969 186.215 1.00 20.99  ? 2    NAG G C8  1 
HETATM 7019 N  N2  . NAG G 5 .   ? 204.742 185.376 185.096 1.00 20.29  ? 2    NAG G N2  1 
HETATM 7020 O  O3  . NAG G 5 .   ? 206.316 183.307 186.296 1.00 21.88  ? 2    NAG G O3  1 
HETATM 7021 O  O4  . NAG G 5 .   ? 207.363 181.285 184.632 1.00 22.38  ? 2    NAG G O4  1 
HETATM 7022 O  O5  . NAG G 5 .   ? 204.582 182.648 182.574 1.00 20.66  ? 2    NAG G O5  1 
HETATM 7023 O  O6  . NAG G 5 .   ? 205.345 180.850 180.751 1.00 19.12  ? 2    NAG G O6  1 
HETATM 7024 O  O7  . NAG G 5 .   ? 203.838 187.041 186.284 1.00 19.93  ? 2    NAG G O7  1 
HETATM 7025 C  C1  . BMA G 5 .   ? 207.456 179.933 185.006 1.00 23.21  ? 3    BMA G C1  1 
HETATM 7026 C  C2  . BMA G 5 .   ? 208.715 179.587 185.856 1.00 23.35  ? 3    BMA G C2  1 
HETATM 7027 C  C3  . BMA G 5 .   ? 208.702 178.102 186.218 1.00 24.25  ? 3    BMA G C3  1 
HETATM 7028 C  C4  . BMA G 5 .   ? 207.380 177.789 186.965 1.00 24.14  ? 3    BMA G C4  1 
HETATM 7029 C  C5  . BMA G 5 .   ? 206.163 178.158 186.076 1.00 24.39  ? 3    BMA G C5  1 
HETATM 7030 C  C6  . BMA G 5 .   ? 204.861 177.899 186.827 1.00 24.34  ? 3    BMA G C6  1 
HETATM 7031 O  O2  . BMA G 5 .   ? 208.765 180.389 187.031 1.00 23.90  ? 3    BMA G O2  1 
HETATM 7032 O  O3  . BMA G 5 .   ? 209.829 177.820 187.076 1.00 23.99  ? 3    BMA G O3  1 
HETATM 7033 O  O4  . BMA G 5 .   ? 207.366 176.405 187.314 1.00 25.05  ? 3    BMA G O4  1 
HETATM 7034 O  O5  . BMA G 5 .   ? 206.240 179.590 185.727 1.00 23.20  ? 3    BMA G O5  1 
HETATM 7035 O  O6  . BMA G 5 .   ? 203.749 177.809 185.942 1.00 24.71  ? 3    BMA G O6  1 
HETATM 7036 C  C1  . NAG H 4 .   ? 177.371 152.902 136.935 1.00 9.90   ? 1    NAG H C1  1 
HETATM 7037 C  C2  . NAG H 4 .   ? 177.601 151.769 137.937 1.00 10.27  ? 1    NAG H C2  1 
HETATM 7038 C  C3  . NAG H 4 .   ? 179.041 151.770 138.444 1.00 10.43  ? 1    NAG H C3  1 
HETATM 7039 C  C4  . NAG H 4 .   ? 180.035 151.848 137.293 1.00 11.31  ? 1    NAG H C4  1 
HETATM 7040 C  C5  . NAG H 4 .   ? 179.713 153.086 136.464 1.00 10.87  ? 1    NAG H C5  1 
HETATM 7041 C  C6  . NAG H 4 .   ? 180.635 153.262 135.282 1.00 10.88  ? 1    NAG H C6  1 
HETATM 7042 C  C7  . NAG H 4 .   ? 175.721 151.024 139.339 1.00 9.88   ? 1    NAG H C7  1 
HETATM 7043 C  C8  . NAG H 4 .   ? 175.488 149.941 138.333 1.00 10.70  ? 1    NAG H C8  1 
HETATM 7044 N  N2  . NAG H 4 .   ? 176.721 151.864 139.080 1.00 9.97   ? 1    NAG H N2  1 
HETATM 7045 O  O3  . NAG H 4 .   ? 179.234 150.599 139.221 1.00 11.46  ? 1    NAG H O3  1 
HETATM 7046 O  O4  . NAG H 4 .   ? 181.374 151.974 137.772 1.00 12.01  ? 1    NAG H O4  1 
HETATM 7047 O  O5  . NAG H 4 .   ? 178.379 152.965 135.939 1.00 10.47  ? 1    NAG H O5  1 
HETATM 7048 O  O6  . NAG H 4 .   ? 180.817 154.637 134.958 1.00 10.18  ? 1    NAG H O6  1 
HETATM 7049 O  O7  . NAG H 4 .   ? 175.032 151.137 140.346 1.00 9.59   ? 1    NAG H O7  1 
HETATM 7050 C  C1  . NAG H 4 .   ? 182.146 150.881 138.169 1.00 12.52  ? 2    NAG H C1  1 
HETATM 7051 C  C2  . NAG H 4 .   ? 183.584 151.012 137.590 1.00 12.51  ? 2    NAG H C2  1 
HETATM 7052 C  C3  . NAG H 4 .   ? 184.337 149.697 137.893 1.00 13.46  ? 2    NAG H C3  1 
HETATM 7053 C  C4  . NAG H 4 .   ? 184.363 149.478 139.416 1.00 13.57  ? 2    NAG H C4  1 
HETATM 7054 C  C5  . NAG H 4 .   ? 182.915 149.424 139.962 1.00 13.38  ? 2    NAG H C5  1 
HETATM 7055 C  C6  . NAG H 4 .   ? 182.896 149.345 141.485 1.00 13.88  ? 2    NAG H C6  1 
HETATM 7056 C  C7  . NAG H 4 .   ? 184.195 152.244 135.598 1.00 12.26  ? 2    NAG H C7  1 
HETATM 7057 C  C8  . NAG H 4 .   ? 184.130 152.479 134.120 1.00 12.33  ? 2    NAG H C8  1 
HETATM 7058 N  N2  . NAG H 4 .   ? 183.521 151.231 136.150 1.00 12.49  ? 2    NAG H N2  1 
HETATM 7059 O  O3  . NAG H 4 .   ? 185.671 149.786 137.383 1.00 13.42  ? 2    NAG H O3  1 
HETATM 7060 O  O4  . NAG H 4 .   ? 185.026 148.247 139.705 1.00 13.93  ? 2    NAG H O4  1 
HETATM 7061 O  O5  . NAG H 4 .   ? 182.196 150.644 139.594 1.00 12.95  ? 2    NAG H O5  1 
HETATM 7062 O  O6  . NAG H 4 .   ? 181.898 148.444 141.951 1.00 14.42  ? 2    NAG H O6  1 
HETATM 7063 O  O7  . NAG H 4 .   ? 184.861 153.008 136.301 1.00 11.67  ? 2    NAG H O7  1 
HETATM 7064 C  C1  . NAG I 5 .   ? 240.283 181.747 155.313 1.00 40.88  ? 1    NAG I C1  1 
HETATM 7065 C  C2  . NAG I 5 .   ? 240.383 181.387 153.797 1.00 40.82  ? 1    NAG I C2  1 
HETATM 7066 C  C3  . NAG I 5 .   ? 240.368 179.861 153.671 1.00 40.03  ? 1    NAG I C3  1 
HETATM 7067 C  C4  . NAG I 5 .   ? 241.512 179.207 154.468 1.00 40.63  ? 1    NAG I C4  1 
HETATM 7068 C  C5  . NAG I 5 .   ? 241.365 179.669 155.941 1.00 39.99  ? 1    NAG I C5  1 
HETATM 7069 C  C6  . NAG I 5 .   ? 242.490 179.138 156.829 1.00 41.05  ? 1    NAG I C6  1 
HETATM 7070 C  C7  . NAG I 5 .   ? 239.314 182.813 152.146 1.00 40.27  ? 1    NAG I C7  1 
HETATM 7071 C  C8  . NAG I 5 .   ? 238.101 183.348 151.454 1.00 39.54  ? 1    NAG I C8  1 
HETATM 7072 N  N2  . NAG I 5 .   ? 239.197 181.917 153.116 1.00 40.82  ? 1    NAG I N2  1 
HETATM 7073 O  O3  . NAG I 5 .   ? 240.544 179.539 152.298 1.00 39.57  ? 1    NAG I O3  1 
HETATM 7074 O  O4  . NAG I 5 .   ? 241.320 177.781 154.470 1.00 40.36  ? 1    NAG I O4  1 
HETATM 7075 O  O5  . NAG I 5 .   ? 241.372 181.132 156.037 1.00 40.56  ? 1    NAG I O5  1 
HETATM 7076 O  O6  . NAG I 5 .   ? 242.142 179.217 158.224 1.00 42.08  ? 1    NAG I O6  1 
HETATM 7077 O  O7  . NAG I 5 .   ? 240.425 183.224 151.794 1.00 40.93  ? 1    NAG I O7  1 
HETATM 7078 C  C1  . NAG I 5 .   ? 242.161 177.014 153.480 1.00 40.47  ? 2    NAG I C1  1 
HETATM 7079 C  C2  . NAG I 5 .   ? 242.295 175.556 154.018 1.00 41.20  ? 2    NAG I C2  1 
HETATM 7080 C  C3  . NAG I 5 .   ? 243.110 174.734 153.003 1.00 42.48  ? 2    NAG I C3  1 
HETATM 7081 C  C4  . NAG I 5 .   ? 242.384 174.746 151.630 1.00 42.04  ? 2    NAG I C4  1 
HETATM 7082 C  C5  . NAG I 5 .   ? 242.272 176.212 151.171 1.00 41.70  ? 2    NAG I C5  1 
HETATM 7083 C  C6  . NAG I 5 .   ? 241.505 176.322 149.863 1.00 40.96  ? 2    NAG I C6  1 
HETATM 7084 C  C7  . NAG I 5 .   ? 242.552 174.874 156.316 1.00 41.79  ? 2    NAG I C7  1 
HETATM 7085 C  C8  . NAG I 5 .   ? 243.271 174.919 157.621 1.00 42.10  ? 2    NAG I C8  1 
HETATM 7086 N  N2  . NAG I 5 .   ? 242.995 175.590 155.301 1.00 42.01  ? 2    NAG I N2  1 
HETATM 7087 O  O3  . NAG I 5 .   ? 243.261 173.390 153.493 1.00 42.61  ? 2    NAG I O3  1 
HETATM 7088 O  O4  . NAG I 5 .   ? 243.163 173.992 150.698 1.00 43.14  ? 2    NAG I O4  1 
HETATM 7089 O  O5  . NAG I 5 .   ? 241.557 176.992 152.170 1.00 39.77  ? 2    NAG I O5  1 
HETATM 7090 O  O6  . NAG I 5 .   ? 241.600 177.642 149.331 1.00 40.73  ? 2    NAG I O6  1 
HETATM 7091 O  O7  . NAG I 5 .   ? 241.539 174.165 156.200 1.00 40.92  ? 2    NAG I O7  1 
HETATM 7092 C  C1  . BMA I 5 .   ? 242.389 172.853 150.110 1.00 44.36  ? 3    BMA I C1  1 
HETATM 7093 C  C2  . BMA I 5 .   ? 243.097 172.354 148.808 1.00 44.33  ? 3    BMA I C2  1 
HETATM 7094 C  C3  . BMA I 5 .   ? 242.292 171.183 148.229 1.00 45.78  ? 3    BMA I C3  1 
HETATM 7095 C  C4  . BMA I 5 .   ? 242.152 170.063 149.282 1.00 46.06  ? 3    BMA I C4  1 
HETATM 7096 C  C5  . BMA I 5 .   ? 241.468 170.648 150.542 1.00 45.28  ? 3    BMA I C5  1 
HETATM 7097 C  C6  . BMA I 5 .   ? 241.353 169.599 151.639 1.00 44.88  ? 3    BMA I C6  1 
HETATM 7098 O  O2  . BMA I 5 .   ? 244.438 171.977 149.088 1.00 43.74  ? 3    BMA I O2  1 
HETATM 7099 O  O3  . BMA I 5 .   ? 242.959 170.666 147.071 1.00 44.87  ? 3    BMA I O3  1 
HETATM 7100 O  O4  . BMA I 5 .   ? 241.352 169.018 148.734 1.00 44.21  ? 3    BMA I O4  1 
HETATM 7101 O  O5  . BMA I 5 .   ? 242.251 171.774 151.062 1.00 44.93  ? 3    BMA I O5  1 
HETATM 7102 O  O6  . BMA I 5 .   ? 242.631 169.167 152.100 1.00 44.52  ? 3    BMA I O6  1 
HETATM 7103 C  C1  . NAG J 6 .   ? 176.797 216.633 166.450 1.00 13.31  ? 901  NAG A C1  1 
HETATM 7104 C  C2  . NAG J 6 .   ? 178.033 217.437 166.986 1.00 13.51  ? 901  NAG A C2  1 
HETATM 7105 C  C3  . NAG J 6 .   ? 178.570 216.724 168.247 1.00 13.87  ? 901  NAG A C3  1 
HETATM 7106 C  C4  . NAG J 6 .   ? 177.439 216.642 169.297 1.00 13.90  ? 901  NAG A C4  1 
HETATM 7107 C  C5  . NAG J 6 .   ? 176.250 215.858 168.695 1.00 13.71  ? 901  NAG A C5  1 
HETATM 7108 C  C6  . NAG J 6 .   ? 175.074 215.789 169.645 1.00 13.67  ? 901  NAG A C6  1 
HETATM 7109 C  C7  . NAG J 6 .   ? 179.192 218.474 165.122 1.00 13.74  ? 901  NAG A C7  1 
HETATM 7110 C  C8  . NAG J 6 .   ? 180.250 218.468 164.058 1.00 14.20  ? 901  NAG A C8  1 
HETATM 7111 N  N2  . NAG J 6 .   ? 179.071 217.443 165.950 1.00 13.65  ? 901  NAG A N2  1 
HETATM 7112 O  O3  . NAG J 6 .   ? 179.671 217.475 168.778 1.00 13.98  ? 901  NAG A O3  1 
HETATM 7113 O  O4  . NAG J 6 .   ? 177.928 215.971 170.456 1.00 14.12  ? 901  NAG A O4  1 
HETATM 7114 O  O5  . NAG J 6 .   ? 175.791 216.536 167.478 1.00 13.45  ? 901  NAG A O5  1 
HETATM 7115 O  O6  . NAG J 6 .   ? 174.044 214.966 169.113 1.00 13.66  ? 901  NAG A O6  1 
HETATM 7116 O  O7  . NAG J 6 .   ? 178.421 219.440 165.209 1.00 13.91  ? 901  NAG A O7  1 
HETATM 7117 C  C1  . NAG K 6 .   ? 190.378 192.931 185.721 1.00 11.40  ? 902  NAG A C1  1 
HETATM 7118 C  C2  . NAG K 6 .   ? 190.503 194.506 185.845 1.00 11.39  ? 902  NAG A C2  1 
HETATM 7119 C  C3  . NAG K 6 .   ? 191.334 194.818 187.116 1.00 11.98  ? 902  NAG A C3  1 
HETATM 7120 C  C4  . NAG K 6 .   ? 190.648 194.185 188.351 1.00 12.08  ? 902  NAG A C4  1 
HETATM 7121 C  C5  . NAG K 6 .   ? 190.542 192.662 188.129 1.00 12.04  ? 902  NAG A C5  1 
HETATM 7122 C  C6  . NAG K 6 .   ? 189.934 191.911 189.305 1.00 12.31  ? 902  NAG A C6  1 
HETATM 7123 C  C7  . NAG K 6 .   ? 190.949 196.253 184.217 1.00 11.23  ? 902  NAG A C7  1 
HETATM 7124 C  C8  . NAG K 6 .   ? 191.693 196.740 183.014 1.00 10.88  ? 902  NAG A C8  1 
HETATM 7125 N  N2  . NAG K 6 .   ? 191.195 195.040 184.669 1.00 11.36  ? 902  NAG A N2  1 
HETATM 7126 O  O3  . NAG K 6 .   ? 191.454 196.239 187.277 1.00 12.07  ? 902  NAG A O3  1 
HETATM 7127 O  O4  . NAG K 6 .   ? 191.393 194.490 189.510 1.00 12.32  ? 902  NAG A O4  1 
HETATM 7128 O  O5  . NAG K 6 .   ? 189.755 192.391 186.917 1.00 11.81  ? 902  NAG A O5  1 
HETATM 7129 O  O6  . NAG K 6 .   ? 188.618 192.333 189.604 1.00 12.94  ? 902  NAG A O6  1 
HETATM 7130 O  O7  . NAG K 6 .   ? 190.132 196.998 184.759 1.00 11.80  ? 902  NAG A O7  1 
HETATM 7131 C  C1  . NAG L 6 .   ? 172.488 184.830 189.165 1.00 14.06  ? 903  NAG A C1  1 
HETATM 7132 C  C2  . NAG L 6 .   ? 172.643 185.431 190.608 1.00 14.67  ? 903  NAG A C2  1 
HETATM 7133 C  C3  . NAG L 6 .   ? 171.480 184.915 191.478 1.00 15.12  ? 903  NAG A C3  1 
HETATM 7134 C  C4  . NAG L 6 .   ? 170.147 185.350 190.843 1.00 15.31  ? 903  NAG A C4  1 
HETATM 7135 C  C5  . NAG L 6 .   ? 170.063 184.761 189.420 1.00 15.21  ? 903  NAG A C5  1 
HETATM 7136 C  C6  . NAG L 6 .   ? 168.794 185.184 188.699 1.00 15.42  ? 903  NAG A C6  1 
HETATM 7137 C  C7  . NAG L 6 .   ? 174.944 185.800 191.293 1.00 14.73  ? 903  NAG A C7  1 
HETATM 7138 C  C8  . NAG L 6 .   ? 176.232 185.319 191.890 1.00 14.75  ? 903  NAG A C8  1 
HETATM 7139 N  N2  . NAG L 6 .   ? 173.910 184.975 191.192 1.00 14.83  ? 903  NAG A N2  1 
HETATM 7140 O  O3  . NAG L 6 .   ? 171.588 185.461 192.793 1.00 15.56  ? 903  NAG A O3  1 
HETATM 7141 O  O4  . NAG L 6 .   ? 169.066 184.870 191.629 1.00 15.63  ? 903  NAG A O4  1 
HETATM 7142 O  O5  . NAG L 6 .   ? 171.203 185.216 188.622 1.00 14.65  ? 903  NAG A O5  1 
HETATM 7143 O  O6  . NAG L 6 .   ? 168.648 186.599 188.674 1.00 15.44  ? 903  NAG A O6  1 
HETATM 7144 O  O7  . NAG L 6 .   ? 174.857 186.966 190.896 1.00 14.98  ? 903  NAG A O7  1 
HETATM 7145 ZN ZN  . ZN  M 7 .   ? 181.381 184.871 164.887 1.00 64.77  ? 904  ZN  A ZN  1 
HETATM 7146 C  C1  . NAG N 6 .   ? 232.572 179.014 145.152 1.00 36.27  ? 701  NAG B C1  1 
HETATM 7147 C  C2  . NAG N 6 .   ? 231.031 178.808 145.320 1.00 36.37  ? 701  NAG B C2  1 
HETATM 7148 C  C3  . NAG N 6 .   ? 230.384 178.811 143.916 1.00 37.07  ? 701  NAG B C3  1 
HETATM 7149 C  C4  . NAG N 6 .   ? 230.700 180.158 143.232 1.00 37.18  ? 701  NAG B C4  1 
HETATM 7150 C  C5  . NAG N 6 .   ? 232.232 180.322 143.129 1.00 37.57  ? 701  NAG B C5  1 
HETATM 7151 C  C6  . NAG N 6 .   ? 232.606 181.654 142.501 1.00 38.17  ? 701  NAG B C6  1 
HETATM 7152 C  C7  . NAG N 6 .   ? 229.876 177.382 146.912 1.00 34.20  ? 701  NAG B C7  1 
HETATM 7153 C  C8  . NAG N 6 .   ? 229.648 176.061 147.578 1.00 33.77  ? 701  NAG B C8  1 
HETATM 7154 N  N2  . NAG N 6 .   ? 230.805 177.511 145.973 1.00 35.97  ? 701  NAG B N2  1 
HETATM 7155 O  O3  . NAG N 6 .   ? 228.968 178.643 144.033 1.00 36.62  ? 701  NAG B O3  1 
HETATM 7156 O  O4  . NAG N 6 .   ? 230.114 180.178 141.935 1.00 38.02  ? 701  NAG B O4  1 
HETATM 7157 O  O5  . NAG N 6 .   ? 232.826 180.265 144.469 1.00 37.22  ? 701  NAG B O5  1 
HETATM 7158 O  O6  . NAG N 6 .   ? 233.986 181.696 142.159 1.00 37.86  ? 701  NAG B O6  1 
HETATM 7159 O  O7  . NAG N 6 .   ? 229.182 178.353 147.246 1.00 34.47  ? 701  NAG B O7  1 
HETATM 7160 O  O   . HOH O 8 .   ? 174.971 195.208 176.188 1.00 34.81  ? 1001 HOH A O   1 
HETATM 7161 O  O   . HOH O 8 .   ? 181.225 169.093 145.424 1.00 26.09  ? 1002 HOH A O   1 
HETATM 7162 O  O   . HOH O 8 .   ? 184.165 171.181 126.147 1.00 29.70  ? 1003 HOH A O   1 
HETATM 7163 O  O   . HOH O 8 .   ? 180.190 193.944 161.263 1.00 31.99  ? 1004 HOH A O   1 
HETATM 7164 O  O   . HOH O 8 .   ? 190.174 168.178 135.141 1.00 24.29  ? 1005 HOH A O   1 
HETATM 7165 O  O   . HOH O 8 .   ? 187.712 206.216 150.159 1.00 39.87  ? 1006 HOH A O   1 
HETATM 7166 O  O   . HOH O 8 .   ? 166.176 203.579 140.043 1.00 32.31  ? 1007 HOH A O   1 
HETATM 7167 O  O   . HOH O 8 .   ? 189.133 203.397 150.035 1.00 37.64  ? 1008 HOH A O   1 
HETATM 7168 O  O   . HOH O 8 .   ? 178.188 160.086 122.128 1.00 45.23  ? 1009 HOH A O   1 
HETATM 7169 O  O   . HOH O 8 .   ? 204.950 176.719 139.147 1.00 31.33  ? 1010 HOH A O   1 
HETATM 7170 O  O   . HOH O 8 .   ? 186.997 178.189 144.680 1.00 24.74  ? 1011 HOH A O   1 
HETATM 7171 O  O   . HOH O 8 .   ? 181.057 190.203 160.186 1.00 32.97  ? 1012 HOH A O   1 
HETATM 7172 O  O   . HOH O 8 .   ? 191.890 161.170 137.046 1.00 27.44  ? 1013 HOH A O   1 
HETATM 7173 O  O   . HOH O 8 .   ? 165.174 156.100 143.015 1.00 34.53  ? 1014 HOH A O   1 
HETATM 7174 O  O   . HOH O 8 .   ? 184.846 175.764 144.271 1.00 24.99  ? 1015 HOH A O   1 
HETATM 7175 O  O   . HOH O 8 .   ? 199.211 185.197 162.200 1.00 37.19  ? 1016 HOH A O   1 
HETATM 7176 O  O   . HOH O 8 .   ? 188.199 172.084 131.143 1.00 25.00  ? 1017 HOH A O   1 
HETATM 7177 O  O   . HOH O 8 .   ? 157.290 193.888 139.417 1.00 31.20  ? 1018 HOH A O   1 
HETATM 7178 O  O   . HOH O 8 .   ? 162.057 217.230 168.127 1.00 41.30  ? 1019 HOH A O   1 
HETATM 7179 O  O   . HOH O 8 .   ? 170.351 158.168 132.623 1.00 38.79  ? 1020 HOH A O   1 
HETATM 7180 O  O   . HOH O 8 .   ? 167.624 167.165 133.168 1.00 30.72  ? 1021 HOH A O   1 
HETATM 7181 O  O   . HOH O 8 .   ? 203.214 182.997 157.127 1.00 30.51  ? 1022 HOH A O   1 
HETATM 7182 O  O   . HOH O 8 .   ? 169.179 173.187 139.442 1.00 23.63  ? 1023 HOH A O   1 
HETATM 7183 O  O   . HOH O 8 .   ? 180.344 210.155 160.548 1.00 33.78  ? 1024 HOH A O   1 
HETATM 7184 O  O   . HOH O 8 .   ? 176.186 194.196 150.159 1.00 31.66  ? 1025 HOH A O   1 
HETATM 7185 O  O   . HOH O 8 .   ? 168.016 188.761 134.142 1.00 29.09  ? 1026 HOH A O   1 
HETATM 7186 O  O   . HOH O 8 .   ? 194.463 191.140 153.161 1.00 29.60  ? 1027 HOH A O   1 
HETATM 7187 O  O   . HOH O 8 .   ? 176.826 197.683 172.980 1.00 30.75  ? 1028 HOH A O   1 
HETATM 7188 O  O   . HOH O 8 .   ? 158.148 214.257 162.171 1.00 41.88  ? 1029 HOH A O   1 
HETATM 7189 O  O   . HOH O 8 .   ? 177.770 197.209 160.324 1.00 30.01  ? 1030 HOH A O   1 
HETATM 7190 O  O   . HOH O 8 .   ? 163.172 178.202 132.140 1.00 25.51  ? 1031 HOH A O   1 
HETATM 7191 O  O   . HOH O 8 .   ? 177.591 158.762 124.131 1.00 37.57  ? 1032 HOH A O   1 
HETATM 7192 O  O   . HOH O 8 .   ? 166.176 169.179 152.611 1.00 34.10  ? 1033 HOH A O   1 
HETATM 7193 O  O   . HOH O 8 .   ? 179.147 209.107 168.178 1.00 32.82  ? 1034 HOH A O   1 
HETATM 7194 O  O   . HOH O 8 .   ? 182.397 175.186 143.023 1.00 23.45  ? 1035 HOH A O   1 
HETATM 7195 O  O   . HOH O 8 .   ? 167.950 160.462 142.166 1.00 34.26  ? 1036 HOH A O   1 
HETATM 7196 O  O   . HOH O 8 .   ? 197.102 180.190 164.174 1.00 33.56  ? 1037 HOH A O   1 
HETATM 7197 O  O   . HOH O 8 .   ? 184.608 195.207 182.193 1.00 39.14  ? 1038 HOH A O   1 
HETATM 7198 O  O   . HOH O 8 .   ? 169.179 185.461 146.154 1.00 21.10  ? 1039 HOH A O   1 
HETATM 7199 O  O   . HOH O 8 .   ? 201.212 169.433 139.147 1.00 30.09  ? 1040 HOH A O   1 
HETATM 7200 O  O   . HOH O 8 .   ? 198.078 181.483 162.173 1.00 33.57  ? 1041 HOH A O   1 
HETATM 7201 O  O   . HOH O 8 .   ? 174.183 155.510 149.285 1.00 33.94  ? 1042 HOH A O   1 
HETATM 7202 O  O   . HOH O 8 .   ? 163.589 183.195 151.086 1.00 27.72  ? 1043 HOH A O   1 
HETATM 7203 O  O   . HOH O 8 .   ? 184.195 200.110 164.398 1.00 29.17  ? 1044 HOH A O   1 
HETATM 7204 O  O   . HOH O 8 .   ? 162.925 188.289 136.188 1.00 28.04  ? 1045 HOH A O   1 
HETATM 7205 O  O   . HOH O 8 .   ? 190.669 181.341 133.140 1.00 35.74  ? 1046 HOH A O   1 
HETATM 7206 O  O   . HOH O 8 .   ? 177.307 154.115 143.550 1.00 33.94  ? 1047 HOH A O   1 
HETATM 7207 O  O   . HOH O 8 .   ? 165.808 197.693 137.479 1.00 26.92  ? 1048 HOH A O   1 
HETATM 7208 O  O   . HOH O 8 .   ? 198.421 165.471 159.168 1.00 35.18  ? 1049 HOH A O   1 
HETATM 7209 O  O   . HOH O 8 .   ? 162.172 174.296 136.135 1.00 28.42  ? 1050 HOH A O   1 
HETATM 7210 O  O   . HOH O 8 .   ? 161.170 190.364 178.189 1.00 35.87  ? 1051 HOH A O   1 
HETATM 7211 O  O   . HOH O 8 .   ? 157.165 173.239 143.518 1.00 26.09  ? 1052 HOH A O   1 
HETATM 7212 O  O   . HOH O 8 .   ? 171.012 224.054 164.305 1.00 46.97  ? 1053 HOH A O   1 
HETATM 7213 O  O   . HOH O 8 .   ? 192.223 169.573 129.121 1.00 27.31  ? 1054 HOH A O   1 
HETATM 7214 O  O   . HOH O 8 .   ? 183.188 203.471 162.322 1.00 28.43  ? 1055 HOH A O   1 
HETATM 7215 O  O   . HOH O 8 .   ? 212.540 167.177 156.165 1.00 40.90  ? 1056 HOH A O   1 
HETATM 7216 O  O   . HOH O 8 .   ? 182.192 156.520 128.135 1.00 38.08  ? 1057 HOH A O   1 
HETATM 7217 O  O   . HOH O 8 .   ? 195.651 175.374 138.039 1.00 21.81  ? 1058 HOH A O   1 
HETATM 7218 O  O   . HOH O 8 .   ? 189.581 165.176 154.615 1.00 34.14  ? 1059 HOH A O   1 
HETATM 7219 O  O   . HOH O 8 .   ? 198.210 163.107 150.158 1.00 31.75  ? 1060 HOH A O   1 
HETATM 7220 O  O   . HOH O 8 .   ? 173.498 194.828 140.148 1.00 24.91  ? 1061 HOH A O   1 
HETATM 7221 O  O   . HOH O 8 .   ? 157.708 175.479 141.926 1.00 29.25  ? 1062 HOH A O   1 
HETATM 7222 O  O   . HOH O 8 .   ? 199.422 189.200 142.686 1.00 27.81  ? 1063 HOH A O   1 
HETATM 7223 O  O   . HOH O 8 .   ? 201.212 194.743 153.164 1.00 33.35  ? 1064 HOH A O   1 
HETATM 7224 O  O   . HOH O 8 .   ? 189.201 197.211 138.894 1.00 34.09  ? 1065 HOH A O   1 
HETATM 7225 O  O   . HOH O 8 .   ? 164.614 204.688 151.160 1.00 36.68  ? 1066 HOH A O   1 
HETATM 7226 O  O   . HOH O 8 .   ? 172.485 176.190 129.136 1.00 26.47  ? 1067 HOH A O   1 
HETATM 7227 O  O   . HOH O 8 .   ? 199.210 170.239 133.536 1.00 32.30  ? 1068 HOH A O   1 
HETATM 7228 O  O   . HOH O 8 .   ? 159.685 194.708 173.142 1.00 40.02  ? 1069 HOH A O   1 
HETATM 7229 O  O   . HOH O 8 .   ? 170.180 169.606 130.423 1.00 28.97  ? 1070 HOH A O   1 
HETATM 7230 O  O   . HOH O 8 .   ? 182.416 166.446 120.063 1.00 47.77  ? 1071 HOH A O   1 
HETATM 7231 O  O   . HOH O 8 .   ? 184.195 179.190 130.137 1.00 27.89  ? 1072 HOH A O   1 
HETATM 7232 O  O   . HOH O 8 .   ? 149.157 189.200 146.730 1.00 37.37  ? 1073 HOH A O   1 
HETATM 7233 O  O   . HOH O 8 .   ? 161.573 205.367 149.010 1.00 38.37  ? 1074 HOH A O   1 
HETATM 7234 O  O   . HOH O 8 .   ? 189.423 163.375 151.649 1.00 34.56  ? 1075 HOH A O   1 
HETATM 7235 O  O   . HOH O 8 .   ? 185.196 162.172 134.104 1.00 30.39  ? 1076 HOH A O   1 
HETATM 7236 O  O   . HOH O 8 .   ? 150.226 184.195 146.154 1.00 34.19  ? 1077 HOH A O   1 
HETATM 7237 O  O   . HOH O 8 .   ? 205.222 162.173 155.164 1.00 40.09  ? 1078 HOH A O   1 
HETATM 7238 O  O   . HOH O 8 .   ? 201.531 184.140 148.160 1.00 30.91  ? 1079 HOH A O   1 
HETATM 7239 O  O   . HOH O 8 .   ? 164.717 162.171 144.151 1.00 32.59  ? 1080 HOH A O   1 
HETATM 7240 O  O   . HOH O 8 .   ? 190.587 185.340 184.194 1.00 36.03  ? 1081 HOH A O   1 
HETATM 7241 O  O   . HOH O 8 .   ? 173.183 150.222 129.224 1.00 45.49  ? 1082 HOH A O   1 
HETATM 7242 O  O   . HOH O 8 .   ? 169.179 209.445 174.570 1.00 38.75  ? 1083 HOH A O   1 
HETATM 7243 O  O   . HOH O 8 .   ? 170.176 161.483 140.674 1.00 29.53  ? 1084 HOH A O   1 
HETATM 7244 O  O   . HOH O 8 .   ? 175.185 188.199 129.183 1.00 30.19  ? 1085 HOH A O   1 
HETATM 7245 O  O   . HOH O 8 .   ? 177.188 197.209 156.165 1.00 40.76  ? 1086 HOH A O   1 
HETATM 7246 O  O   . HOH O 8 .   ? 207.111 163.173 156.990 1.00 42.22  ? 1087 HOH A O   1 
HETATM 7247 O  O   . HOH O 8 .   ? 183.310 156.166 149.619 1.00 34.41  ? 1088 HOH A O   1 
HETATM 7248 O  O   . HOH O 8 .   ? 154.163 198.484 143.233 1.00 37.62  ? 1089 HOH A O   1 
HETATM 7249 O  O   . HOH O 8 .   ? 185.196 155.956 142.799 1.00 28.04  ? 1090 HOH A O   1 
HETATM 7250 O  O   . HOH O 8 .   ? 177.185 205.744 145.651 1.00 32.07  ? 1091 HOH A O   1 
HETATM 7251 O  O   . HOH O 8 .   ? 194.204 160.032 135.956 1.00 32.90  ? 1092 HOH A O   1 
HETATM 7252 O  O   . HOH O 8 .   ? 198.153 195.692 157.128 1.00 35.65  ? 1093 HOH A O   1 
HETATM 7253 O  O   . HOH O 8 .   ? 177.425 177.191 129.208 1.00 25.45  ? 1094 HOH A O   1 
HETATM 7254 O  O   . HOH O 8 .   ? 168.893 164.174 136.143 1.00 29.53  ? 1095 HOH A O   1 
HETATM 7255 O  O   . HOH O 8 .   ? 170.180 198.296 136.233 1.00 29.77  ? 1096 HOH A O   1 
HETATM 7256 O  O   . HOH O 8 .   ? 200.460 181.122 139.347 1.00 27.57  ? 1097 HOH A O   1 
HETATM 7257 O  O   . HOH O 8 .   ? 161.907 177.188 156.166 1.00 34.14  ? 1098 HOH A O   1 
HETATM 7258 O  O   . HOH O 8 .   ? 180.029 208.394 148.158 1.00 34.46  ? 1099 HOH A O   1 
HETATM 7259 O  O   . HOH O 8 .   ? 189.200 199.944 149.122 1.00 35.97  ? 1100 HOH A O   1 
HETATM 7260 O  O   . HOH O 8 .   ? 177.613 200.213 158.170 1.00 32.46  ? 1101 HOH A O   1 
HETATM 7261 O  O   . HOH O 8 .   ? 165.175 200.650 152.161 1.00 37.04  ? 1102 HOH A O   1 
HETATM 7262 O  O   . HOH O 8 .   ? 167.044 192.203 135.339 1.00 29.72  ? 1103 HOH A O   1 
HETATM 7263 O  O   . HOH O 8 .   ? 188.673 190.203 138.146 1.00 31.78  ? 1104 HOH A O   1 
HETATM 7264 O  O   . HOH O 8 .   ? 176.184 192.254 147.392 1.00 30.61  ? 1105 HOH A O   1 
HETATM 7265 O  O   . HOH O 8 .   ? 175.185 154.698 145.544 1.00 30.93  ? 1106 HOH A O   1 
HETATM 7266 O  O   . HOH O 8 .   ? 181.030 191.197 179.888 1.00 32.71  ? 1107 HOH A O   1 
HETATM 7267 O  O   . HOH O 8 .   ? 195.287 161.310 146.430 1.00 35.64  ? 1108 HOH A O   1 
HETATM 7268 O  O   . HOH O 8 .   ? 161.170 210.223 169.187 1.00 38.83  ? 1109 HOH A O   1 
HETATM 7269 O  O   . HOH O 8 .   ? 177.194 156.166 152.161 1.00 37.73  ? 1110 HOH A O   1 
HETATM 7270 O  O   . HOH O 8 .   ? 175.159 175.368 131.041 1.00 25.92  ? 1111 HOH A O   1 
HETATM 7271 O  O   . HOH O 8 .   ? 194.203 179.271 134.301 1.00 27.47  ? 1112 HOH A O   1 
HETATM 7272 O  O   . HOH O 8 .   ? 176.157 173.185 131.138 1.00 25.64  ? 1113 HOH A O   1 
HETATM 7273 O  O   . HOH O 8 .   ? 195.098 193.379 140.148 1.00 33.23  ? 1114 HOH A O   1 
HETATM 7274 O  O   . HOH O 8 .   ? 177.022 178.189 182.678 1.00 38.23  ? 1115 HOH A O   1 
HETATM 7275 O  O   . HOH O 8 .   ? 179.189 172.520 142.152 1.00 24.98  ? 1116 HOH A O   1 
HETATM 7276 O  O   . HOH O 8 .   ? 196.207 187.673 137.626 1.00 31.82  ? 1117 HOH A O   1 
HETATM 7277 O  O   . HOH O 8 .   ? 178.169 176.186 143.152 1.00 27.49  ? 1118 HOH A O   1 
HETATM 7278 O  O   . HOH O 8 .   ? 197.195 184.451 137.145 1.00 31.39  ? 1119 HOH A O   1 
HETATM 7279 O  O   . HOH O 8 .   ? 177.844 208.220 155.164 1.00 41.07  ? 1120 HOH A O   1 
HETATM 7280 O  O   . HOH O 8 .   ? 165.175 212.735 153.162 1.00 41.17  ? 1121 HOH A O   1 
HETATM 7281 O  O   . HOH O 8 .   ? 172.200 211.212 169.178 1.00 38.49  ? 1122 HOH A O   1 
HETATM 7282 O  O   . HOH O 8 .   ? 198.200 169.492 137.708 1.00 27.44  ? 1123 HOH A O   1 
HETATM 7283 O  O   . HOH O 8 .   ? 180.401 176.186 129.794 1.00 24.44  ? 1124 HOH A O   1 
HETATM 7284 O  O   . HOH O 8 .   ? 150.159 186.545 147.974 1.00 31.46  ? 1125 HOH A O   1 
HETATM 7285 O  O   . HOH O 8 .   ? 198.209 173.106 132.647 1.00 29.18  ? 1126 HOH A O   1 
HETATM 7286 O  O   . HOH O 8 .   ? 181.396 155.165 138.578 1.00 33.95  ? 1127 HOH A O   1 
HETATM 7287 O  O   . HOH O 8 .   ? 177.304 204.753 143.151 1.00 35.05  ? 1128 HOH A O   1 
HETATM 7288 O  O   . HOH O 8 .   ? 176.186 174.682 141.145 1.00 19.29  ? 1129 HOH A O   1 
HETATM 7289 O  O   . HOH O 8 .   ? 195.206 199.037 148.420 1.00 36.24  ? 1130 HOH A O   1 
HETATM 7290 O  O   . HOH O 8 .   ? 176.235 167.177 125.131 1.00 40.38  ? 1131 HOH A O   1 
HETATM 7291 O  O   . HOH O 8 .   ? 180.192 180.141 142.456 1.00 25.17  ? 1132 HOH A O   1 
HETATM 7292 O  O   . HOH O 8 .   ? 199.804 172.182 163.172 1.00 42.77  ? 1133 HOH A O   1 
HETATM 7293 O  O   . HOH O 8 .   ? 175.185 198.092 175.312 1.00 34.80  ? 1134 HOH A O   1 
HETATM 7294 O  O   . HOH O 8 .   ? 199.338 178.189 164.177 1.00 33.90  ? 1135 HOH A O   1 
HETATM 7295 O  O   . HOH O 8 .   ? 203.025 182.294 140.044 1.00 31.61  ? 1136 HOH A O   1 
HETATM 7296 O  O   . HOH O 8 .   ? 180.700 188.100 157.903 1.00 32.83  ? 1137 HOH A O   1 
HETATM 7297 O  O   . HOH O 8 .   ? 176.319 195.206 138.140 1.00 29.76  ? 1138 HOH A O   1 
HETATM 7298 O  O   . HOH O 8 .   ? 168.178 163.519 139.147 1.00 29.99  ? 1139 HOH A O   1 
HETATM 7299 O  O   . HOH P 8 .   ? 218.379 179.190 166.176 1.00 52.82  ? 801  HOH B O   1 
HETATM 7300 O  O   . HOH P 8 .   ? 214.231 169.179 156.995 1.00 47.12  ? 802  HOH B O   1 
HETATM 7301 O  O   . HOH P 8 .   ? 209.221 168.869 149.277 1.00 38.82  ? 803  HOH B O   1 
HETATM 7302 O  O   . HOH P 8 .   ? 221.031 180.209 163.199 1.00 52.11  ? 804  HOH B O   1 
HETATM 7303 O  O   . HOH P 8 .   ? 215.098 173.501 146.774 1.00 45.96  ? 805  HOH B O   1 
# 
