data_8WED
# 
_entry.id   8WED 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8WED         pdb_00008wed 10.2210/pdb8wed/pdb 
WWPDB D_1300040326 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2024-11-27 
3 'Structure model' 1 2 2024-12-25 
# 
_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' 'Database references' 
2 3 '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' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.country'                 
2 2 'Structure model' '_citation.journal_abbrev'          
3 2 'Structure model' '_citation.journal_id_ISSN'         
4 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
5 2 'Structure model' '_citation.title'                   
6 3 'Structure model' '_citation.journal_volume'          
7 3 'Structure model' '_citation.page_first'              
8 3 'Structure model' '_citation.page_last'               
9 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8WED 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-17 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              xushutong@mail.hzau.edu.cn 
_pdbx_contact_author.name_first         Shutong 
_pdbx_contact_author.name_last          Xu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9894-1735 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wan, L.H.' 1 0000-0002-2278-8308 
'Hu, Y.X.'  2 0009-0003-3436-8006 
'Wu, H.M.'  3 0009-0001-2371-073X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Plants 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2055-0278 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            10 
_citation.language                  ? 
_citation.page_first                1984 
_citation.page_last                 1998 
_citation.title                     
;Mechanistic study of SCOOPs recognition by MIK2-BAK1 complex reveals the role of N-glycans in plant ligand-receptor-coreceptor complex formation.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41477-024-01836-3 
_citation.pdbx_database_id_PubMed   39511418 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wu, H.'    1  ?                   
primary 'Wan, L.'   2  ?                   
primary 'Liu, Z.'   3  ?                   
primary 'Jian, Y.'  4  ?                   
primary 'Zhang, C.' 5  ?                   
primary 'Mao, X.'   6  ?                   
primary 'Wang, Z.'  7  ?                   
primary 'Wang, Q.'  8  ?                   
primary 'Hu, Y.'    9  ?                   
primary 'Xiong, L.' 10 0000-0003-0490-1474 
primary 'Xia, Z.'   11 ?                   
primary 'Xue, J.'   12 ?                   
primary 'Li, S.'    13 ?                   
primary 'He, P.'    14 0000-0002-5926-8349 
primary 'Shan, L.'  15 0000-0002-4798-9907 
primary 'Xu, S.'    16 0000-0002-9894-1735 
# 
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 'MDIS1-interacting receptor like kinase 2' 75533.305 2 2.7.11.1          L137E/D164K/S564F ? ? 
2  polymer     man 'BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1' 25183.758 2 2.7.10.1,2.7.11.1 ?                 ? 
? 
3  polymer     syn 'a SCOOP-like peptide from F. oxysporum f. sp. conglutinans strain Fo5176' 1349.348  2 ?                 ? ? ? 
4  branched    man 
;alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)][alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose
;
716.682   1 ?                 ?                 ? ? 
5  branched    syn '2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 424.401   8 ? ? ? ? 
6  branched    syn 
'2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose' 570.542   1 
?                 ?                 ? ? 
7  branched    syn 
'beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose' 586.542   2 ? 
?                 ? ? 
8  branched    man 
;beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose
;
732.682   1 ?                 ?                 ? ? 
9  branched    man 'alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose' 367.349   2 ?                 ? ? ? 
10 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208   9 ?                 ?                 ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'AtMIK2,Probable LRR receptor-like serine/threonine-protein kinase At4g08850' 
2 
;AtBAK1,BRI1-associated receptor kinase 1,Protein ELONGATED,Somatic embryogenesis receptor kinase 3,AtSERK3,Somatic embryogenesis receptor-like kinase 3
;
# 
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 
;MNKTNPERKISLTSFKERMACKEKPRDLQVLLIISIVLSCSFAVSATVEEANALLKWKSTFTNQTSSSKLSSWVNPNTSS
FCTSWYGVACSLGSIIRLNLTNTGIEGTFEDFPFSSLPNLTFVDLSMNRFSGTISPEWGRFSKLEYFDLSINQLVGEIPP
ELGKLSNLDTLHLVENKLNGSIPSEIGRLTKVTEIAIYDNLLTGPIPSSFGNLTKLVNLYLFINSLSGSIPSEIGNLPNL
RELCLDRNNLTGKIPSSFGNLKNVTLLNMFENQLSGEIPPEIGNMTALDTLSLHTNKLTGPIPSTLGNIKTLAVLHLYLN
QLNGSIPPELGEMESMIDLEISENKLTGPVPDSFGKLTALEWLFLRDNQLSGPIPPGIANSTELTVLQLDTNNFTGFLPD
TICRGGKLENLTLDDNHFEGPVPKSLRDCKSLIRVRFKGNSFSGDISEAFGVYPTLNFIDLSNNNFHGQLSANWEQSQKL
VAFILSNNSITGAIPPEIWNMTQLSQLDLSSNRITGELPESISNINRISKLQLNGNRLSGKIPSGIRLLTNLEYLDLSSN
RFSFEIPPTLNNLPRLYYMNLSRNDLDQTIPEGLTKLSQLQMLDLSYNQLDGEISSQFRSLQNLERLDLSHNNLSGQIPP
SFKDMLALTHVDVSHNNLQGPIPDNAAFRNAPPDAFEGNKDLC
;
;MNKTNPERKISLTSFKERMACKEKPRDLQVLLIISIVLSCSFAVSATVEEANALLKWKSTFTNQTSSSKLSSWVNPNTSS
FCTSWYGVACSLGSIIRLNLTNTGIEGTFEDFPFSSLPNLTFVDLSMNRFSGTISPEWGRFSKLEYFDLSINQLVGEIPP
ELGKLSNLDTLHLVENKLNGSIPSEIGRLTKVTEIAIYDNLLTGPIPSSFGNLTKLVNLYLFINSLSGSIPSEIGNLPNL
RELCLDRNNLTGKIPSSFGNLKNVTLLNMFENQLSGEIPPEIGNMTALDTLSLHTNKLTGPIPSTLGNIKTLAVLHLYLN
QLNGSIPPELGEMESMIDLEISENKLTGPVPDSFGKLTALEWLFLRDNQLSGPIPPGIANSTELTVLQLDTNNFTGFLPD
TICRGGKLENLTLDDNHFEGPVPKSLRDCKSLIRVRFKGNSFSGDISEAFGVYPTLNFIDLSNNNFHGQLSANWEQSQKL
VAFILSNNSITGAIPPEIWNMTQLSQLDLSSNRITGELPESISNINRISKLQLNGNRLSGKIPSGIRLLTNLEYLDLSSN
RFSFEIPPTLNNLPRLYYMNLSRNDLDQTIPEGLTKLSQLQMLDLSYNQLDGEISSQFRSLQNLERLDLSHNNLSGQIPP
SFKDMLALTHVDVSHNNLQGPIPDNAAFRNAPPDAFEGNKDLC
;
A,D ? 
2 'polypeptide(L)' no no 
;MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANL
SGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSL
TAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSHHHHHHHHHH
;
;MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANL
SGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSL
TAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGSHHHHHHHHHH
;
B,E ? 
3 'polypeptide(L)' no no ESSSSHSERAGGR ESSSSHSERAGGR C,F ? 
# 
_pdbx_entity_nonpoly.entity_id   10 
_pdbx_entity_nonpoly.name        2-acetamido-2-deoxy-beta-D-glucopyranose 
_pdbx_entity_nonpoly.comp_id     NAG 
# 
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   ASN n 
1 3   LYS n 
1 4   THR n 
1 5   ASN n 
1 6   PRO n 
1 7   GLU n 
1 8   ARG n 
1 9   LYS n 
1 10  ILE n 
1 11  SER n 
1 12  LEU n 
1 13  THR n 
1 14  SER n 
1 15  PHE n 
1 16  LYS n 
1 17  GLU n 
1 18  ARG n 
1 19  MET n 
1 20  ALA n 
1 21  CYS n 
1 22  LYS n 
1 23  GLU n 
1 24  LYS n 
1 25  PRO n 
1 26  ARG n 
1 27  ASP n 
1 28  LEU n 
1 29  GLN n 
1 30  VAL n 
1 31  LEU n 
1 32  LEU n 
1 33  ILE n 
1 34  ILE n 
1 35  SER n 
1 36  ILE n 
1 37  VAL n 
1 38  LEU n 
1 39  SER n 
1 40  CYS n 
1 41  SER n 
1 42  PHE n 
1 43  ALA n 
1 44  VAL n 
1 45  SER n 
1 46  ALA n 
1 47  THR n 
1 48  VAL n 
1 49  GLU n 
1 50  GLU n 
1 51  ALA n 
1 52  ASN n 
1 53  ALA n 
1 54  LEU n 
1 55  LEU n 
1 56  LYS n 
1 57  TRP n 
1 58  LYS n 
1 59  SER n 
1 60  THR n 
1 61  PHE n 
1 62  THR n 
1 63  ASN n 
1 64  GLN n 
1 65  THR n 
1 66  SER n 
1 67  SER n 
1 68  SER n 
1 69  LYS n 
1 70  LEU n 
1 71  SER n 
1 72  SER n 
1 73  TRP n 
1 74  VAL n 
1 75  ASN n 
1 76  PRO n 
1 77  ASN n 
1 78  THR n 
1 79  SER n 
1 80  SER n 
1 81  PHE n 
1 82  CYS n 
1 83  THR n 
1 84  SER n 
1 85  TRP n 
1 86  TYR n 
1 87  GLY n 
1 88  VAL n 
1 89  ALA n 
1 90  CYS n 
1 91  SER n 
1 92  LEU n 
1 93  GLY n 
1 94  SER n 
1 95  ILE n 
1 96  ILE n 
1 97  ARG n 
1 98  LEU n 
1 99  ASN n 
1 100 LEU n 
1 101 THR n 
1 102 ASN n 
1 103 THR n 
1 104 GLY n 
1 105 ILE n 
1 106 GLU n 
1 107 GLY n 
1 108 THR n 
1 109 PHE n 
1 110 GLU n 
1 111 ASP n 
1 112 PHE n 
1 113 PRO n 
1 114 PHE n 
1 115 SER n 
1 116 SER n 
1 117 LEU n 
1 118 PRO n 
1 119 ASN n 
1 120 LEU n 
1 121 THR n 
1 122 PHE n 
1 123 VAL n 
1 124 ASP n 
1 125 LEU n 
1 126 SER n 
1 127 MET n 
1 128 ASN n 
1 129 ARG n 
1 130 PHE n 
1 131 SER n 
1 132 GLY n 
1 133 THR n 
1 134 ILE n 
1 135 SER n 
1 136 PRO n 
1 137 GLU n 
1 138 TRP n 
1 139 GLY n 
1 140 ARG n 
1 141 PHE n 
1 142 SER n 
1 143 LYS n 
1 144 LEU n 
1 145 GLU n 
1 146 TYR n 
1 147 PHE n 
1 148 ASP n 
1 149 LEU n 
1 150 SER n 
1 151 ILE n 
1 152 ASN n 
1 153 GLN n 
1 154 LEU n 
1 155 VAL n 
1 156 GLY n 
1 157 GLU n 
1 158 ILE n 
1 159 PRO n 
1 160 PRO n 
1 161 GLU n 
1 162 LEU n 
1 163 GLY n 
1 164 LYS n 
1 165 LEU n 
1 166 SER n 
1 167 ASN n 
1 168 LEU n 
1 169 ASP n 
1 170 THR n 
1 171 LEU n 
1 172 HIS n 
1 173 LEU n 
1 174 VAL n 
1 175 GLU n 
1 176 ASN n 
1 177 LYS n 
1 178 LEU n 
1 179 ASN n 
1 180 GLY n 
1 181 SER n 
1 182 ILE n 
1 183 PRO n 
1 184 SER n 
1 185 GLU n 
1 186 ILE n 
1 187 GLY n 
1 188 ARG n 
1 189 LEU n 
1 190 THR n 
1 191 LYS n 
1 192 VAL n 
1 193 THR n 
1 194 GLU n 
1 195 ILE n 
1 196 ALA n 
1 197 ILE n 
1 198 TYR n 
1 199 ASP n 
1 200 ASN n 
1 201 LEU n 
1 202 LEU n 
1 203 THR n 
1 204 GLY n 
1 205 PRO n 
1 206 ILE n 
1 207 PRO n 
1 208 SER n 
1 209 SER n 
1 210 PHE n 
1 211 GLY n 
1 212 ASN n 
1 213 LEU n 
1 214 THR n 
1 215 LYS n 
1 216 LEU n 
1 217 VAL n 
1 218 ASN n 
1 219 LEU n 
1 220 TYR n 
1 221 LEU n 
1 222 PHE n 
1 223 ILE n 
1 224 ASN n 
1 225 SER n 
1 226 LEU n 
1 227 SER n 
1 228 GLY n 
1 229 SER n 
1 230 ILE n 
1 231 PRO n 
1 232 SER n 
1 233 GLU n 
1 234 ILE n 
1 235 GLY n 
1 236 ASN n 
1 237 LEU n 
1 238 PRO n 
1 239 ASN n 
1 240 LEU n 
1 241 ARG n 
1 242 GLU n 
1 243 LEU n 
1 244 CYS n 
1 245 LEU n 
1 246 ASP n 
1 247 ARG n 
1 248 ASN n 
1 249 ASN n 
1 250 LEU n 
1 251 THR n 
1 252 GLY n 
1 253 LYS n 
1 254 ILE n 
1 255 PRO n 
1 256 SER n 
1 257 SER n 
1 258 PHE n 
1 259 GLY n 
1 260 ASN n 
1 261 LEU n 
1 262 LYS n 
1 263 ASN n 
1 264 VAL n 
1 265 THR n 
1 266 LEU n 
1 267 LEU n 
1 268 ASN n 
1 269 MET n 
1 270 PHE n 
1 271 GLU n 
1 272 ASN n 
1 273 GLN n 
1 274 LEU n 
1 275 SER n 
1 276 GLY n 
1 277 GLU n 
1 278 ILE n 
1 279 PRO n 
1 280 PRO n 
1 281 GLU n 
1 282 ILE n 
1 283 GLY n 
1 284 ASN n 
1 285 MET n 
1 286 THR n 
1 287 ALA n 
1 288 LEU n 
1 289 ASP n 
1 290 THR n 
1 291 LEU n 
1 292 SER n 
1 293 LEU n 
1 294 HIS n 
1 295 THR n 
1 296 ASN n 
1 297 LYS n 
1 298 LEU n 
1 299 THR n 
1 300 GLY n 
1 301 PRO n 
1 302 ILE n 
1 303 PRO n 
1 304 SER n 
1 305 THR n 
1 306 LEU n 
1 307 GLY n 
1 308 ASN n 
1 309 ILE n 
1 310 LYS n 
1 311 THR n 
1 312 LEU n 
1 313 ALA n 
1 314 VAL n 
1 315 LEU n 
1 316 HIS n 
1 317 LEU n 
1 318 TYR n 
1 319 LEU n 
1 320 ASN n 
1 321 GLN n 
1 322 LEU n 
1 323 ASN n 
1 324 GLY n 
1 325 SER n 
1 326 ILE n 
1 327 PRO n 
1 328 PRO n 
1 329 GLU n 
1 330 LEU n 
1 331 GLY n 
1 332 GLU n 
1 333 MET n 
1 334 GLU n 
1 335 SER n 
1 336 MET n 
1 337 ILE n 
1 338 ASP n 
1 339 LEU n 
1 340 GLU n 
1 341 ILE n 
1 342 SER n 
1 343 GLU n 
1 344 ASN n 
1 345 LYS n 
1 346 LEU n 
1 347 THR n 
1 348 GLY n 
1 349 PRO n 
1 350 VAL n 
1 351 PRO n 
1 352 ASP n 
1 353 SER n 
1 354 PHE n 
1 355 GLY n 
1 356 LYS n 
1 357 LEU n 
1 358 THR n 
1 359 ALA n 
1 360 LEU n 
1 361 GLU n 
1 362 TRP n 
1 363 LEU n 
1 364 PHE n 
1 365 LEU n 
1 366 ARG n 
1 367 ASP n 
1 368 ASN n 
1 369 GLN n 
1 370 LEU n 
1 371 SER n 
1 372 GLY n 
1 373 PRO n 
1 374 ILE n 
1 375 PRO n 
1 376 PRO n 
1 377 GLY n 
1 378 ILE n 
1 379 ALA n 
1 380 ASN n 
1 381 SER n 
1 382 THR n 
1 383 GLU n 
1 384 LEU n 
1 385 THR n 
1 386 VAL n 
1 387 LEU n 
1 388 GLN n 
1 389 LEU n 
1 390 ASP n 
1 391 THR n 
1 392 ASN n 
1 393 ASN n 
1 394 PHE n 
1 395 THR n 
1 396 GLY n 
1 397 PHE n 
1 398 LEU n 
1 399 PRO n 
1 400 ASP n 
1 401 THR n 
1 402 ILE n 
1 403 CYS n 
1 404 ARG n 
1 405 GLY n 
1 406 GLY n 
1 407 LYS n 
1 408 LEU n 
1 409 GLU n 
1 410 ASN n 
1 411 LEU n 
1 412 THR n 
1 413 LEU n 
1 414 ASP n 
1 415 ASP n 
1 416 ASN n 
1 417 HIS n 
1 418 PHE n 
1 419 GLU n 
1 420 GLY n 
1 421 PRO n 
1 422 VAL n 
1 423 PRO n 
1 424 LYS n 
1 425 SER n 
1 426 LEU n 
1 427 ARG n 
1 428 ASP n 
1 429 CYS n 
1 430 LYS n 
1 431 SER n 
1 432 LEU n 
1 433 ILE n 
1 434 ARG n 
1 435 VAL n 
1 436 ARG n 
1 437 PHE n 
1 438 LYS n 
1 439 GLY n 
1 440 ASN n 
1 441 SER n 
1 442 PHE n 
1 443 SER n 
1 444 GLY n 
1 445 ASP n 
1 446 ILE n 
1 447 SER n 
1 448 GLU n 
1 449 ALA n 
1 450 PHE n 
1 451 GLY n 
1 452 VAL n 
1 453 TYR n 
1 454 PRO n 
1 455 THR n 
1 456 LEU n 
1 457 ASN n 
1 458 PHE n 
1 459 ILE n 
1 460 ASP n 
1 461 LEU n 
1 462 SER n 
1 463 ASN n 
1 464 ASN n 
1 465 ASN n 
1 466 PHE n 
1 467 HIS n 
1 468 GLY n 
1 469 GLN n 
1 470 LEU n 
1 471 SER n 
1 472 ALA n 
1 473 ASN n 
1 474 TRP n 
1 475 GLU n 
1 476 GLN n 
1 477 SER n 
1 478 GLN n 
1 479 LYS n 
1 480 LEU n 
1 481 VAL n 
1 482 ALA n 
1 483 PHE n 
1 484 ILE n 
1 485 LEU n 
1 486 SER n 
1 487 ASN n 
1 488 ASN n 
1 489 SER n 
1 490 ILE n 
1 491 THR n 
1 492 GLY n 
1 493 ALA n 
1 494 ILE n 
1 495 PRO n 
1 496 PRO n 
1 497 GLU n 
1 498 ILE n 
1 499 TRP n 
1 500 ASN n 
1 501 MET n 
1 502 THR n 
1 503 GLN n 
1 504 LEU n 
1 505 SER n 
1 506 GLN n 
1 507 LEU n 
1 508 ASP n 
1 509 LEU n 
1 510 SER n 
1 511 SER n 
1 512 ASN n 
1 513 ARG n 
1 514 ILE n 
1 515 THR n 
1 516 GLY n 
1 517 GLU n 
1 518 LEU n 
1 519 PRO n 
1 520 GLU n 
1 521 SER n 
1 522 ILE n 
1 523 SER n 
1 524 ASN n 
1 525 ILE n 
1 526 ASN n 
1 527 ARG n 
1 528 ILE n 
1 529 SER n 
1 530 LYS n 
1 531 LEU n 
1 532 GLN n 
1 533 LEU n 
1 534 ASN n 
1 535 GLY n 
1 536 ASN n 
1 537 ARG n 
1 538 LEU n 
1 539 SER n 
1 540 GLY n 
1 541 LYS n 
1 542 ILE n 
1 543 PRO n 
1 544 SER n 
1 545 GLY n 
1 546 ILE n 
1 547 ARG n 
1 548 LEU n 
1 549 LEU n 
1 550 THR n 
1 551 ASN n 
1 552 LEU n 
1 553 GLU n 
1 554 TYR n 
1 555 LEU n 
1 556 ASP n 
1 557 LEU n 
1 558 SER n 
1 559 SER n 
1 560 ASN n 
1 561 ARG n 
1 562 PHE n 
1 563 SER n 
1 564 PHE n 
1 565 GLU n 
1 566 ILE n 
1 567 PRO n 
1 568 PRO n 
1 569 THR n 
1 570 LEU n 
1 571 ASN n 
1 572 ASN n 
1 573 LEU n 
1 574 PRO n 
1 575 ARG n 
1 576 LEU n 
1 577 TYR n 
1 578 TYR n 
1 579 MET n 
1 580 ASN n 
1 581 LEU n 
1 582 SER n 
1 583 ARG n 
1 584 ASN n 
1 585 ASP n 
1 586 LEU n 
1 587 ASP n 
1 588 GLN n 
1 589 THR n 
1 590 ILE n 
1 591 PRO n 
1 592 GLU n 
1 593 GLY n 
1 594 LEU n 
1 595 THR n 
1 596 LYS n 
1 597 LEU n 
1 598 SER n 
1 599 GLN n 
1 600 LEU n 
1 601 GLN n 
1 602 MET n 
1 603 LEU n 
1 604 ASP n 
1 605 LEU n 
1 606 SER n 
1 607 TYR n 
1 608 ASN n 
1 609 GLN n 
1 610 LEU n 
1 611 ASP n 
1 612 GLY n 
1 613 GLU n 
1 614 ILE n 
1 615 SER n 
1 616 SER n 
1 617 GLN n 
1 618 PHE n 
1 619 ARG n 
1 620 SER n 
1 621 LEU n 
1 622 GLN n 
1 623 ASN n 
1 624 LEU n 
1 625 GLU n 
1 626 ARG n 
1 627 LEU n 
1 628 ASP n 
1 629 LEU n 
1 630 SER n 
1 631 HIS n 
1 632 ASN n 
1 633 ASN n 
1 634 LEU n 
1 635 SER n 
1 636 GLY n 
1 637 GLN n 
1 638 ILE n 
1 639 PRO n 
1 640 PRO n 
1 641 SER n 
1 642 PHE n 
1 643 LYS n 
1 644 ASP n 
1 645 MET n 
1 646 LEU n 
1 647 ALA n 
1 648 LEU n 
1 649 THR n 
1 650 HIS n 
1 651 VAL n 
1 652 ASP n 
1 653 VAL n 
1 654 SER n 
1 655 HIS n 
1 656 ASN n 
1 657 ASN n 
1 658 LEU n 
1 659 GLN n 
1 660 GLY n 
1 661 PRO n 
1 662 ILE n 
1 663 PRO n 
1 664 ASP n 
1 665 ASN n 
1 666 ALA n 
1 667 ALA n 
1 668 PHE n 
1 669 ARG n 
1 670 ASN n 
1 671 ALA n 
1 672 PRO n 
1 673 PRO n 
1 674 ASP n 
1 675 ALA n 
1 676 PHE n 
1 677 GLU n 
1 678 GLY n 
1 679 ASN n 
1 680 LYS n 
1 681 ASP n 
1 682 LEU n 
1 683 CYS n 
2 1   MET n 
2 2   GLU n 
2 3   ARG n 
2 4   ARG n 
2 5   LEU n 
2 6   MET n 
2 7   ILE n 
2 8   PRO n 
2 9   CYS n 
2 10  PHE n 
2 11  PHE n 
2 12  TRP n 
2 13  LEU n 
2 14  ILE n 
2 15  LEU n 
2 16  VAL n 
2 17  LEU n 
2 18  ASP n 
2 19  LEU n 
2 20  VAL n 
2 21  LEU n 
2 22  ARG n 
2 23  VAL n 
2 24  SER n 
2 25  GLY n 
2 26  ASN n 
2 27  ALA n 
2 28  GLU n 
2 29  GLY n 
2 30  ASP n 
2 31  ALA n 
2 32  LEU n 
2 33  SER n 
2 34  ALA n 
2 35  LEU n 
2 36  LYS n 
2 37  ASN n 
2 38  SER n 
2 39  LEU n 
2 40  ALA n 
2 41  ASP n 
2 42  PRO n 
2 43  ASN n 
2 44  LYS n 
2 45  VAL n 
2 46  LEU n 
2 47  GLN n 
2 48  SER n 
2 49  TRP n 
2 50  ASP n 
2 51  ALA n 
2 52  THR n 
2 53  LEU n 
2 54  VAL n 
2 55  THR n 
2 56  PRO n 
2 57  CYS n 
2 58  THR n 
2 59  TRP n 
2 60  PHE n 
2 61  HIS n 
2 62  VAL n 
2 63  THR n 
2 64  CYS n 
2 65  ASN n 
2 66  SER n 
2 67  ASP n 
2 68  ASN n 
2 69  SER n 
2 70  VAL n 
2 71  THR n 
2 72  ARG n 
2 73  VAL n 
2 74  ASP n 
2 75  LEU n 
2 76  GLY n 
2 77  ASN n 
2 78  ALA n 
2 79  ASN n 
2 80  LEU n 
2 81  SER n 
2 82  GLY n 
2 83  GLN n 
2 84  LEU n 
2 85  VAL n 
2 86  MET n 
2 87  GLN n 
2 88  LEU n 
2 89  GLY n 
2 90  GLN n 
2 91  LEU n 
2 92  PRO n 
2 93  ASN n 
2 94  LEU n 
2 95  GLN n 
2 96  TYR n 
2 97  LEU n 
2 98  GLU n 
2 99  LEU n 
2 100 TYR n 
2 101 SER n 
2 102 ASN n 
2 103 ASN n 
2 104 ILE n 
2 105 THR n 
2 106 GLY n 
2 107 THR n 
2 108 ILE n 
2 109 PRO n 
2 110 GLU n 
2 111 GLN n 
2 112 LEU n 
2 113 GLY n 
2 114 ASN n 
2 115 LEU n 
2 116 THR n 
2 117 GLU n 
2 118 LEU n 
2 119 VAL n 
2 120 SER n 
2 121 LEU n 
2 122 ASP n 
2 123 LEU n 
2 124 TYR n 
2 125 LEU n 
2 126 ASN n 
2 127 ASN n 
2 128 LEU n 
2 129 SER n 
2 130 GLY n 
2 131 PRO n 
2 132 ILE n 
2 133 PRO n 
2 134 SER n 
2 135 THR n 
2 136 LEU n 
2 137 GLY n 
2 138 ARG n 
2 139 LEU n 
2 140 LYS n 
2 141 LYS n 
2 142 LEU n 
2 143 ARG n 
2 144 PHE n 
2 145 LEU n 
2 146 ARG n 
2 147 LEU n 
2 148 ASN n 
2 149 ASN n 
2 150 ASN n 
2 151 SER n 
2 152 LEU n 
2 153 SER n 
2 154 GLY n 
2 155 GLU n 
2 156 ILE n 
2 157 PRO n 
2 158 ARG n 
2 159 SER n 
2 160 LEU n 
2 161 THR n 
2 162 ALA n 
2 163 VAL n 
2 164 LEU n 
2 165 THR n 
2 166 LEU n 
2 167 GLN n 
2 168 VAL n 
2 169 LEU n 
2 170 ASP n 
2 171 LEU n 
2 172 SER n 
2 173 ASN n 
2 174 ASN n 
2 175 PRO n 
2 176 LEU n 
2 177 THR n 
2 178 GLY n 
2 179 ASP n 
2 180 ILE n 
2 181 PRO n 
2 182 VAL n 
2 183 ASN n 
2 184 GLY n 
2 185 SER n 
2 186 PHE n 
2 187 SER n 
2 188 LEU n 
2 189 PHE n 
2 190 THR n 
2 191 PRO n 
2 192 ILE n 
2 193 SER n 
2 194 PHE n 
2 195 ALA n 
2 196 ASN n 
2 197 THR n 
2 198 LYS n 
2 199 LEU n 
2 200 THR n 
2 201 PRO n 
2 202 LEU n 
2 203 PRO n 
2 204 ALA n 
2 205 SER n 
2 206 PRO n 
2 207 PRO n 
2 208 PRO n 
2 209 PRO n 
2 210 ILE n 
2 211 SER n 
2 212 PRO n 
2 213 THR n 
2 214 PRO n 
2 215 PRO n 
2 216 SER n 
2 217 PRO n 
2 218 ALA n 
2 219 GLY n 
2 220 SER n 
2 221 HIS n 
2 222 HIS n 
2 223 HIS n 
2 224 HIS n 
2 225 HIS n 
2 226 HIS n 
2 227 HIS n 
2 228 HIS n 
2 229 HIS n 
2 230 HIS n 
3 1   GLU n 
3 2   SER n 
3 3   SER n 
3 4   SER n 
3 5   SER n 
3 6   HIS n 
3 7   SER n 
3 8   GLU n 
3 9   ARG n 
3 10  ALA n 
3 11  GLY n 
3 12  GLY n 
3 13  ARG 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' 1 683 'Mouse-ear cress' ? 'MIK2, At4g08850, T32A17.160'            ? ? ? ? ? ? 
'Arabidopsis thaliana' 3702 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 230 'Mouse-ear cress' ? 'BAK1, ELG, SERK3, At4g33430, F17M5.190' ? ? ? ? ? ? 
'Arabidopsis thaliana' 3702 ? ? ? ? ? ? ? ? 'Spodoptera frugiperda' 7108 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
_pdbx_entity_src_syn.entity_id              3 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       13 
_pdbx_entity_src_syn.organism_scientific    'Fusarium oxysporum f. sp. pisi HDV247' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       1080344 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_pdbx_entity_branch.entity_id 
_pdbx_entity_branch.type 
4 oligosaccharide 
5 oligosaccharide 
6 oligosaccharide 
7 oligosaccharide 
8 oligosaccharide 
9 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  4 'LFucpa1-3[DGlcpNAcb1-4][LFucpa1-6]DGlcpNAcb1-ROH'                                                  
'Glycam Condensed Sequence' GMML       1.0   
2  4 'WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2-1-2/a3-b1_a4-c1_a6-d1'                WURCS PDB2Glycan 1.1.0 
3  4 '[][D-1-deoxy-GlcpNAc]{[(3+1)][a-L-Fucp]{}[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}'               LINUCS PDB-CARE   ?     
4  5 DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                          
'Glycam Condensed Sequence' GMML       1.0   
5  5 'WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1'                                               WURCS PDB2Glycan 1.1.0 
6  5 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}'                                                     LINUCS PDB-CARE   ?     
7  6 'DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROH'                                                             
'Glycam Condensed Sequence' GMML       1.0   
8  6 '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 
9  6 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}'                                  LINUCS PDB-CARE   ?     
10 7 DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROH                                                                 
'Glycam Condensed Sequence' GMML       1.0   
11 7 '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 
12 7 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}'                                  LINUCS PDB-CARE   ?     
13 8 'DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROH'                                                    
'Glycam Condensed Sequence' GMML       1.0   
14 8 'WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1' WURCS PDB2Glycan 1.1.0 
15 8 '[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}'               LINUCS PDB-CARE   ?     
16 9 LFucpa1-6DGlcpNAcb1-ROH                                                                             
'Glycam Condensed Sequence' GMML       1.0   
17 9 'WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1'                                WURCS PDB2Glycan 1.1.0 
18 9 '[][D-1-deoxy-GlcpNAc]{[(6+1)][a-L-Fucp]{}}'                                                        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  4 2 FUC C1 O1 1 NAG O3 HO3 sing ? 
2  4 3 NAG C1 O1 1 NAG O4 HO4 sing ? 
3  4 4 FUC C1 O1 1 NAG O6 HO6 sing ? 
4  5 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
5  6 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
6  6 3 FUC C1 O1 1 NAG O6 HO6 sing ? 
7  7 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
8  7 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
9  8 2 NAG C1 O1 1 NAG O4 HO4 sing ? 
10 8 3 BMA C1 O1 2 NAG O4 HO4 sing ? 
11 8 4 FUC C1 O1 1 NAG O6 HO6 sing ? 
12 9 2 FUC C1 O1 1 NAG O6 HO6 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 
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 
# 
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   1   ?   ?   ?   A . n 
A 1 2   ASN 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   ?   ?   ?   A . n 
A 1 4   THR 4   4   ?   ?   ?   A . n 
A 1 5   ASN 5   5   ?   ?   ?   A . n 
A 1 6   PRO 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   ARG 8   8   ?   ?   ?   A . n 
A 1 9   LYS 9   9   ?   ?   ?   A . n 
A 1 10  ILE 10  10  ?   ?   ?   A . n 
A 1 11  SER 11  11  ?   ?   ?   A . n 
A 1 12  LEU 12  12  ?   ?   ?   A . n 
A 1 13  THR 13  13  ?   ?   ?   A . n 
A 1 14  SER 14  14  ?   ?   ?   A . n 
A 1 15  PHE 15  15  ?   ?   ?   A . n 
A 1 16  LYS 16  16  ?   ?   ?   A . n 
A 1 17  GLU 17  17  ?   ?   ?   A . n 
A 1 18  ARG 18  18  ?   ?   ?   A . n 
A 1 19  MET 19  19  ?   ?   ?   A . n 
A 1 20  ALA 20  20  ?   ?   ?   A . n 
A 1 21  CYS 21  21  ?   ?   ?   A . n 
A 1 22  LYS 22  22  ?   ?   ?   A . n 
A 1 23  GLU 23  23  ?   ?   ?   A . n 
A 1 24  LYS 24  24  ?   ?   ?   A . n 
A 1 25  PRO 25  25  ?   ?   ?   A . n 
A 1 26  ARG 26  26  ?   ?   ?   A . n 
A 1 27  ASP 27  27  ?   ?   ?   A . n 
A 1 28  LEU 28  28  ?   ?   ?   A . n 
A 1 29  GLN 29  29  ?   ?   ?   A . n 
A 1 30  VAL 30  30  ?   ?   ?   A . n 
A 1 31  LEU 31  31  ?   ?   ?   A . n 
A 1 32  LEU 32  32  ?   ?   ?   A . n 
A 1 33  ILE 33  33  ?   ?   ?   A . n 
A 1 34  ILE 34  34  ?   ?   ?   A . n 
A 1 35  SER 35  35  ?   ?   ?   A . n 
A 1 36  ILE 36  36  ?   ?   ?   A . n 
A 1 37  VAL 37  37  ?   ?   ?   A . n 
A 1 38  LEU 38  38  ?   ?   ?   A . n 
A 1 39  SER 39  39  ?   ?   ?   A . n 
A 1 40  CYS 40  40  ?   ?   ?   A . n 
A 1 41  SER 41  41  ?   ?   ?   A . n 
A 1 42  PHE 42  42  ?   ?   ?   A . n 
A 1 43  ALA 43  43  ?   ?   ?   A . n 
A 1 44  VAL 44  44  ?   ?   ?   A . n 
A 1 45  SER 45  45  ?   ?   ?   A . n 
A 1 46  ALA 46  46  ?   ?   ?   A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  TRP 57  57  57  TRP TRP A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  GLN 64  64  64  GLN GLN A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  TRP 73  73  73  TRP TRP A . n 
A 1 74  VAL 74  74  74  VAL VAL A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  THR 78  78  78  THR THR A . n 
A 1 79  SER 79  79  79  SER SER A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  CYS 82  82  82  CYS CYS A . n 
A 1 83  THR 83  83  83  THR THR A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  TRP 85  85  85  TRP TRP A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  GLY 87  87  87  GLY GLY A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  CYS 90  90  90  CYS CYS A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  SER 94  94  94  SER SER A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  ARG 97  97  97  ARG ARG A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 THR 101 101 101 THR THR A . n 
A 1 102 ASN 102 102 102 ASN ASN A . n 
A 1 103 THR 103 103 103 THR THR A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 ASP 111 111 111 ASP ASP A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 PHE 122 122 122 PHE PHE A . n 
A 1 123 VAL 123 123 123 VAL VAL A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 MET 127 127 127 MET MET A . n 
A 1 128 ASN 128 128 128 ASN ASN A . n 
A 1 129 ARG 129 129 129 ARG ARG A . n 
A 1 130 PHE 130 130 130 PHE PHE A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 THR 133 133 133 THR THR A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 SER 135 135 135 SER SER A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 TRP 138 138 138 TRP TRP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 LYS 143 143 143 LYS LYS A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
A 1 154 LEU 154 154 154 LEU LEU A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 GLY 156 156 156 GLY GLY A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 PRO 160 160 160 PRO PRO A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 ASN 167 167 167 ASN ASN A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 LEU 173 173 173 LEU LEU A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 LYS 177 177 177 LYS LYS A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ASN 179 179 179 ASN ASN A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 PRO 183 183 183 PRO PRO A . n 
A 1 184 SER 184 184 184 SER SER A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 LYS 191 191 191 LYS LYS A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 GLU 194 194 194 GLU GLU A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ILE 197 197 197 ILE ILE A . n 
A 1 198 TYR 198 198 198 TYR TYR A . n 
A 1 199 ASP 199 199 199 ASP ASP A . n 
A 1 200 ASN 200 200 200 ASN ASN A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 PRO 205 205 205 PRO PRO A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 PRO 207 207 207 PRO PRO A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 TYR 220 220 220 TYR TYR A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 ILE 223 223 223 ILE ILE A . n 
A 1 224 ASN 224 224 224 ASN ASN A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 SER 227 227 227 SER SER A . n 
A 1 228 GLY 228 228 228 GLY GLY A . n 
A 1 229 SER 229 229 229 SER SER A . n 
A 1 230 ILE 230 230 230 ILE ILE A . n 
A 1 231 PRO 231 231 231 PRO PRO A . n 
A 1 232 SER 232 232 232 SER SER A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 GLY 235 235 235 GLY GLY A . n 
A 1 236 ASN 236 236 236 ASN ASN A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 PRO 238 238 238 PRO PRO A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 ARG 241 241 241 ARG ARG A . n 
A 1 242 GLU 242 242 242 GLU GLU A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 CYS 244 244 244 CYS CYS A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 GLY 252 252 252 GLY GLY A . n 
A 1 253 LYS 253 253 253 LYS LYS A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 PHE 258 258 258 PHE PHE A . n 
A 1 259 GLY 259 259 259 GLY GLY A . n 
A 1 260 ASN 260 260 260 ASN ASN A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 LYS 262 262 262 LYS LYS A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 VAL 264 264 264 VAL VAL A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 LEU 266 266 266 LEU LEU A . n 
A 1 267 LEU 267 267 267 LEU LEU A . n 
A 1 268 ASN 268 268 268 ASN ASN A . n 
A 1 269 MET 269 269 269 MET MET A . n 
A 1 270 PHE 270 270 270 PHE PHE A . n 
A 1 271 GLU 271 271 271 GLU GLU A . n 
A 1 272 ASN 272 272 272 ASN ASN A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 GLY 276 276 276 GLY GLY A . n 
A 1 277 GLU 277 277 277 GLU GLU A . n 
A 1 278 ILE 278 278 278 ILE ILE A . n 
A 1 279 PRO 279 279 279 PRO PRO A . n 
A 1 280 PRO 280 280 280 PRO PRO A . n 
A 1 281 GLU 281 281 281 GLU GLU A . n 
A 1 282 ILE 282 282 282 ILE ILE A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 MET 285 285 285 MET MET A . n 
A 1 286 THR 286 286 286 THR THR A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 THR 290 290 290 THR THR A . n 
A 1 291 LEU 291 291 291 LEU LEU A . n 
A 1 292 SER 292 292 292 SER SER A . n 
A 1 293 LEU 293 293 293 LEU LEU A . n 
A 1 294 HIS 294 294 294 HIS HIS A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 ASN 296 296 296 ASN ASN A . n 
A 1 297 LYS 297 297 297 LYS LYS A . n 
A 1 298 LEU 298 298 298 LEU LEU A . n 
A 1 299 THR 299 299 299 THR THR A . n 
A 1 300 GLY 300 300 300 GLY GLY A . n 
A 1 301 PRO 301 301 301 PRO PRO A . n 
A 1 302 ILE 302 302 302 ILE ILE A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 SER 304 304 304 SER SER A . n 
A 1 305 THR 305 305 305 THR THR A . n 
A 1 306 LEU 306 306 306 LEU LEU A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 ASN 308 308 308 ASN ASN A . n 
A 1 309 ILE 309 309 309 ILE ILE A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 THR 311 311 311 THR THR A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 VAL 314 314 314 VAL VAL A . n 
A 1 315 LEU 315 315 315 LEU LEU A . n 
A 1 316 HIS 316 316 316 HIS HIS A . n 
A 1 317 LEU 317 317 317 LEU LEU A . n 
A 1 318 TYR 318 318 318 TYR TYR A . n 
A 1 319 LEU 319 319 319 LEU LEU A . n 
A 1 320 ASN 320 320 320 ASN ASN A . n 
A 1 321 GLN 321 321 321 GLN GLN A . n 
A 1 322 LEU 322 322 322 LEU LEU A . n 
A 1 323 ASN 323 323 323 ASN ASN A . n 
A 1 324 GLY 324 324 324 GLY GLY A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 ILE 326 326 326 ILE ILE A . n 
A 1 327 PRO 327 327 327 PRO PRO A . n 
A 1 328 PRO 328 328 328 PRO PRO A . n 
A 1 329 GLU 329 329 329 GLU GLU A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 GLU 332 332 332 GLU GLU A . n 
A 1 333 MET 333 333 333 MET MET A . n 
A 1 334 GLU 334 334 334 GLU GLU A . n 
A 1 335 SER 335 335 335 SER SER A . n 
A 1 336 MET 336 336 336 MET MET A . n 
A 1 337 ILE 337 337 337 ILE ILE A . n 
A 1 338 ASP 338 338 338 ASP ASP A . n 
A 1 339 LEU 339 339 339 LEU LEU A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 GLU 343 343 343 GLU GLU A . n 
A 1 344 ASN 344 344 344 ASN ASN A . n 
A 1 345 LYS 345 345 345 LYS LYS A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 THR 347 347 347 THR THR A . n 
A 1 348 GLY 348 348 348 GLY GLY A . n 
A 1 349 PRO 349 349 349 PRO PRO A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 PRO 351 351 351 PRO PRO A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 SER 353 353 353 SER SER A . n 
A 1 354 PHE 354 354 354 PHE PHE A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 LEU 357 357 357 LEU LEU A . n 
A 1 358 THR 358 358 358 THR THR A . n 
A 1 359 ALA 359 359 359 ALA ALA A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 GLU 361 361 361 GLU GLU A . n 
A 1 362 TRP 362 362 362 TRP TRP A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 PHE 364 364 364 PHE PHE A . n 
A 1 365 LEU 365 365 365 LEU LEU A . n 
A 1 366 ARG 366 366 366 ARG ARG A . n 
A 1 367 ASP 367 367 367 ASP ASP A . n 
A 1 368 ASN 368 368 368 ASN ASN A . n 
A 1 369 GLN 369 369 369 GLN GLN A . n 
A 1 370 LEU 370 370 370 LEU LEU A . n 
A 1 371 SER 371 371 371 SER SER A . n 
A 1 372 GLY 372 372 372 GLY GLY A . n 
A 1 373 PRO 373 373 373 PRO PRO A . n 
A 1 374 ILE 374 374 374 ILE ILE A . n 
A 1 375 PRO 375 375 375 PRO PRO A . n 
A 1 376 PRO 376 376 376 PRO PRO A . n 
A 1 377 GLY 377 377 377 GLY GLY A . n 
A 1 378 ILE 378 378 378 ILE ILE A . n 
A 1 379 ALA 379 379 379 ALA ALA A . n 
A 1 380 ASN 380 380 380 ASN ASN A . n 
A 1 381 SER 381 381 381 SER SER A . n 
A 1 382 THR 382 382 382 THR THR A . n 
A 1 383 GLU 383 383 383 GLU GLU A . n 
A 1 384 LEU 384 384 384 LEU LEU A . n 
A 1 385 THR 385 385 385 THR THR A . n 
A 1 386 VAL 386 386 386 VAL VAL A . n 
A 1 387 LEU 387 387 387 LEU LEU A . n 
A 1 388 GLN 388 388 388 GLN GLN A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 ASP 390 390 390 ASP ASP A . n 
A 1 391 THR 391 391 391 THR THR A . n 
A 1 392 ASN 392 392 392 ASN ASN A . n 
A 1 393 ASN 393 393 393 ASN ASN A . n 
A 1 394 PHE 394 394 394 PHE PHE A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 GLY 396 396 396 GLY GLY A . n 
A 1 397 PHE 397 397 397 PHE PHE A . n 
A 1 398 LEU 398 398 398 LEU LEU A . n 
A 1 399 PRO 399 399 399 PRO PRO A . n 
A 1 400 ASP 400 400 400 ASP ASP A . n 
A 1 401 THR 401 401 401 THR THR A . n 
A 1 402 ILE 402 402 402 ILE ILE A . n 
A 1 403 CYS 403 403 403 CYS CYS A . n 
A 1 404 ARG 404 404 404 ARG ARG A . n 
A 1 405 GLY 405 405 405 GLY GLY A . n 
A 1 406 GLY 406 406 406 GLY GLY A . n 
A 1 407 LYS 407 407 407 LYS LYS A . n 
A 1 408 LEU 408 408 408 LEU LEU A . n 
A 1 409 GLU 409 409 409 GLU GLU A . n 
A 1 410 ASN 410 410 410 ASN ASN A . n 
A 1 411 LEU 411 411 411 LEU LEU A . n 
A 1 412 THR 412 412 412 THR THR A . n 
A 1 413 LEU 413 413 413 LEU LEU A . n 
A 1 414 ASP 414 414 414 ASP ASP A . n 
A 1 415 ASP 415 415 415 ASP ASP A . n 
A 1 416 ASN 416 416 416 ASN ASN A . n 
A 1 417 HIS 417 417 417 HIS HIS A . n 
A 1 418 PHE 418 418 418 PHE PHE A . n 
A 1 419 GLU 419 419 419 GLU GLU A . n 
A 1 420 GLY 420 420 420 GLY GLY A . n 
A 1 421 PRO 421 421 421 PRO PRO A . n 
A 1 422 VAL 422 422 422 VAL VAL A . n 
A 1 423 PRO 423 423 423 PRO PRO A . n 
A 1 424 LYS 424 424 424 LYS LYS A . n 
A 1 425 SER 425 425 425 SER SER A . n 
A 1 426 LEU 426 426 426 LEU LEU A . n 
A 1 427 ARG 427 427 427 ARG ARG A . n 
A 1 428 ASP 428 428 428 ASP ASP A . n 
A 1 429 CYS 429 429 429 CYS CYS A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 SER 431 431 431 SER SER A . n 
A 1 432 LEU 432 432 432 LEU LEU A . n 
A 1 433 ILE 433 433 433 ILE ILE A . n 
A 1 434 ARG 434 434 434 ARG ARG A . n 
A 1 435 VAL 435 435 435 VAL VAL A . n 
A 1 436 ARG 436 436 436 ARG ARG A . n 
A 1 437 PHE 437 437 437 PHE PHE A . n 
A 1 438 LYS 438 438 438 LYS LYS A . n 
A 1 439 GLY 439 439 439 GLY GLY A . n 
A 1 440 ASN 440 440 440 ASN ASN A . n 
A 1 441 SER 441 441 441 SER SER A . n 
A 1 442 PHE 442 442 442 PHE PHE A . n 
A 1 443 SER 443 443 443 SER SER A . n 
A 1 444 GLY 444 444 444 GLY GLY A . n 
A 1 445 ASP 445 445 445 ASP ASP A . n 
A 1 446 ILE 446 446 446 ILE ILE A . n 
A 1 447 SER 447 447 447 SER SER A . n 
A 1 448 GLU 448 448 448 GLU GLU A . n 
A 1 449 ALA 449 449 449 ALA ALA A . n 
A 1 450 PHE 450 450 450 PHE PHE A . n 
A 1 451 GLY 451 451 451 GLY GLY A . n 
A 1 452 VAL 452 452 452 VAL VAL A . n 
A 1 453 TYR 453 453 453 TYR TYR A . n 
A 1 454 PRO 454 454 454 PRO PRO A . n 
A 1 455 THR 455 455 455 THR THR A . n 
A 1 456 LEU 456 456 456 LEU LEU A . n 
A 1 457 ASN 457 457 457 ASN ASN A . n 
A 1 458 PHE 458 458 458 PHE PHE A . n 
A 1 459 ILE 459 459 459 ILE ILE A . n 
A 1 460 ASP 460 460 460 ASP ASP A . n 
A 1 461 LEU 461 461 461 LEU LEU A . n 
A 1 462 SER 462 462 462 SER SER A . n 
A 1 463 ASN 463 463 463 ASN ASN A . n 
A 1 464 ASN 464 464 464 ASN ASN A . n 
A 1 465 ASN 465 465 465 ASN ASN A . n 
A 1 466 PHE 466 466 466 PHE PHE A . n 
A 1 467 HIS 467 467 467 HIS HIS A . n 
A 1 468 GLY 468 468 468 GLY GLY A . n 
A 1 469 GLN 469 469 469 GLN GLN A . n 
A 1 470 LEU 470 470 470 LEU LEU A . n 
A 1 471 SER 471 471 471 SER SER A . n 
A 1 472 ALA 472 472 472 ALA ALA A . n 
A 1 473 ASN 473 473 473 ASN ASN A . n 
A 1 474 TRP 474 474 474 TRP TRP A . n 
A 1 475 GLU 475 475 475 GLU GLU A . n 
A 1 476 GLN 476 476 476 GLN GLN A . n 
A 1 477 SER 477 477 477 SER SER A . n 
A 1 478 GLN 478 478 478 GLN GLN A . n 
A 1 479 LYS 479 479 479 LYS LYS A . n 
A 1 480 LEU 480 480 480 LEU LEU A . n 
A 1 481 VAL 481 481 481 VAL VAL A . n 
A 1 482 ALA 482 482 482 ALA ALA A . n 
A 1 483 PHE 483 483 483 PHE PHE A . n 
A 1 484 ILE 484 484 484 ILE ILE A . n 
A 1 485 LEU 485 485 485 LEU LEU A . n 
A 1 486 SER 486 486 486 SER SER A . n 
A 1 487 ASN 487 487 487 ASN ASN A . n 
A 1 488 ASN 488 488 488 ASN ASN A . n 
A 1 489 SER 489 489 489 SER SER A . n 
A 1 490 ILE 490 490 490 ILE ILE A . n 
A 1 491 THR 491 491 491 THR THR A . n 
A 1 492 GLY 492 492 492 GLY GLY A . n 
A 1 493 ALA 493 493 493 ALA ALA A . n 
A 1 494 ILE 494 494 494 ILE ILE A . n 
A 1 495 PRO 495 495 495 PRO PRO A . n 
A 1 496 PRO 496 496 496 PRO PRO A . n 
A 1 497 GLU 497 497 497 GLU GLU A . n 
A 1 498 ILE 498 498 498 ILE ILE A . n 
A 1 499 TRP 499 499 499 TRP TRP A . n 
A 1 500 ASN 500 500 500 ASN ASN A . n 
A 1 501 MET 501 501 501 MET MET A . n 
A 1 502 THR 502 502 502 THR THR A . n 
A 1 503 GLN 503 503 503 GLN GLN A . n 
A 1 504 LEU 504 504 504 LEU LEU A . n 
A 1 505 SER 505 505 505 SER SER A . n 
A 1 506 GLN 506 506 506 GLN GLN A . n 
A 1 507 LEU 507 507 507 LEU LEU A . n 
A 1 508 ASP 508 508 508 ASP ASP A . n 
A 1 509 LEU 509 509 509 LEU LEU A . n 
A 1 510 SER 510 510 510 SER SER A . n 
A 1 511 SER 511 511 511 SER SER A . n 
A 1 512 ASN 512 512 512 ASN ASN A . n 
A 1 513 ARG 513 513 513 ARG ARG A . n 
A 1 514 ILE 514 514 514 ILE ILE A . n 
A 1 515 THR 515 515 515 THR THR A . n 
A 1 516 GLY 516 516 516 GLY GLY A . n 
A 1 517 GLU 517 517 517 GLU GLU A . n 
A 1 518 LEU 518 518 518 LEU LEU A . n 
A 1 519 PRO 519 519 519 PRO PRO A . n 
A 1 520 GLU 520 520 520 GLU GLU A . n 
A 1 521 SER 521 521 521 SER SER A . n 
A 1 522 ILE 522 522 522 ILE ILE A . n 
A 1 523 SER 523 523 523 SER SER A . n 
A 1 524 ASN 524 524 524 ASN ASN A . n 
A 1 525 ILE 525 525 525 ILE ILE A . n 
A 1 526 ASN 526 526 526 ASN ASN A . n 
A 1 527 ARG 527 527 527 ARG ARG A . n 
A 1 528 ILE 528 528 528 ILE ILE A . n 
A 1 529 SER 529 529 529 SER SER A . n 
A 1 530 LYS 530 530 530 LYS LYS A . n 
A 1 531 LEU 531 531 531 LEU LEU A . n 
A 1 532 GLN 532 532 532 GLN GLN A . n 
A 1 533 LEU 533 533 533 LEU LEU A . n 
A 1 534 ASN 534 534 534 ASN ASN A . n 
A 1 535 GLY 535 535 535 GLY GLY A . n 
A 1 536 ASN 536 536 536 ASN ASN A . n 
A 1 537 ARG 537 537 537 ARG ARG A . n 
A 1 538 LEU 538 538 538 LEU LEU A . n 
A 1 539 SER 539 539 539 SER SER A . n 
A 1 540 GLY 540 540 540 GLY GLY A . n 
A 1 541 LYS 541 541 541 LYS LYS A . n 
A 1 542 ILE 542 542 542 ILE ILE A . n 
A 1 543 PRO 543 543 543 PRO PRO A . n 
A 1 544 SER 544 544 544 SER SER A . n 
A 1 545 GLY 545 545 545 GLY GLY A . n 
A 1 546 ILE 546 546 546 ILE ILE A . n 
A 1 547 ARG 547 547 547 ARG ARG A . n 
A 1 548 LEU 548 548 548 LEU LEU A . n 
A 1 549 LEU 549 549 549 LEU LEU A . n 
A 1 550 THR 550 550 550 THR THR A . n 
A 1 551 ASN 551 551 551 ASN ASN A . n 
A 1 552 LEU 552 552 552 LEU LEU A . n 
A 1 553 GLU 553 553 553 GLU GLU A . n 
A 1 554 TYR 554 554 554 TYR TYR A . n 
A 1 555 LEU 555 555 555 LEU LEU A . n 
A 1 556 ASP 556 556 556 ASP ASP A . n 
A 1 557 LEU 557 557 557 LEU LEU A . n 
A 1 558 SER 558 558 558 SER SER A . n 
A 1 559 SER 559 559 559 SER SER A . n 
A 1 560 ASN 560 560 560 ASN ASN A . n 
A 1 561 ARG 561 561 561 ARG ARG A . n 
A 1 562 PHE 562 562 562 PHE PHE A . n 
A 1 563 SER 563 563 563 SER SER A . n 
A 1 564 PHE 564 564 564 PHE PHE A . n 
A 1 565 GLU 565 565 565 GLU GLU A . n 
A 1 566 ILE 566 566 566 ILE ILE A . n 
A 1 567 PRO 567 567 567 PRO PRO A . n 
A 1 568 PRO 568 568 568 PRO PRO A . n 
A 1 569 THR 569 569 569 THR THR A . n 
A 1 570 LEU 570 570 570 LEU LEU A . n 
A 1 571 ASN 571 571 571 ASN ASN A . n 
A 1 572 ASN 572 572 572 ASN ASN A . n 
A 1 573 LEU 573 573 573 LEU LEU A . n 
A 1 574 PRO 574 574 574 PRO PRO A . n 
A 1 575 ARG 575 575 575 ARG ARG A . n 
A 1 576 LEU 576 576 576 LEU LEU A . n 
A 1 577 TYR 577 577 577 TYR TYR A . n 
A 1 578 TYR 578 578 578 TYR TYR A . n 
A 1 579 MET 579 579 579 MET MET A . n 
A 1 580 ASN 580 580 580 ASN ASN A . n 
A 1 581 LEU 581 581 581 LEU LEU A . n 
A 1 582 SER 582 582 582 SER SER A . n 
A 1 583 ARG 583 583 583 ARG ARG A . n 
A 1 584 ASN 584 584 584 ASN ASN A . n 
A 1 585 ASP 585 585 585 ASP ASP A . n 
A 1 586 LEU 586 586 586 LEU LEU A . n 
A 1 587 ASP 587 587 587 ASP ASP A . n 
A 1 588 GLN 588 588 588 GLN GLN A . n 
A 1 589 THR 589 589 589 THR THR A . n 
A 1 590 ILE 590 590 590 ILE ILE A . n 
A 1 591 PRO 591 591 591 PRO PRO A . n 
A 1 592 GLU 592 592 592 GLU GLU A . n 
A 1 593 GLY 593 593 593 GLY GLY A . n 
A 1 594 LEU 594 594 594 LEU LEU A . n 
A 1 595 THR 595 595 595 THR THR A . n 
A 1 596 LYS 596 596 596 LYS LYS A . n 
A 1 597 LEU 597 597 597 LEU LEU A . n 
A 1 598 SER 598 598 598 SER SER A . n 
A 1 599 GLN 599 599 599 GLN GLN A . n 
A 1 600 LEU 600 600 600 LEU LEU A . n 
A 1 601 GLN 601 601 601 GLN GLN A . n 
A 1 602 MET 602 602 602 MET MET A . n 
A 1 603 LEU 603 603 603 LEU LEU A . n 
A 1 604 ASP 604 604 604 ASP ASP A . n 
A 1 605 LEU 605 605 605 LEU LEU A . n 
A 1 606 SER 606 606 606 SER SER A . n 
A 1 607 TYR 607 607 607 TYR TYR A . n 
A 1 608 ASN 608 608 608 ASN ASN A . n 
A 1 609 GLN 609 609 609 GLN GLN A . n 
A 1 610 LEU 610 610 610 LEU LEU A . n 
A 1 611 ASP 611 611 611 ASP ASP A . n 
A 1 612 GLY 612 612 612 GLY GLY A . n 
A 1 613 GLU 613 613 613 GLU GLU A . n 
A 1 614 ILE 614 614 614 ILE ILE A . n 
A 1 615 SER 615 615 615 SER SER A . n 
A 1 616 SER 616 616 616 SER SER A . n 
A 1 617 GLN 617 617 617 GLN GLN A . n 
A 1 618 PHE 618 618 618 PHE PHE A . n 
A 1 619 ARG 619 619 619 ARG ARG A . n 
A 1 620 SER 620 620 620 SER SER A . n 
A 1 621 LEU 621 621 621 LEU LEU A . n 
A 1 622 GLN 622 622 622 GLN GLN A . n 
A 1 623 ASN 623 623 623 ASN ASN A . n 
A 1 624 LEU 624 624 624 LEU LEU A . n 
A 1 625 GLU 625 625 625 GLU GLU A . n 
A 1 626 ARG 626 626 626 ARG ARG A . n 
A 1 627 LEU 627 627 627 LEU LEU A . n 
A 1 628 ASP 628 628 628 ASP ASP A . n 
A 1 629 LEU 629 629 629 LEU LEU A . n 
A 1 630 SER 630 630 630 SER SER A . n 
A 1 631 HIS 631 631 631 HIS HIS A . n 
A 1 632 ASN 632 632 632 ASN ASN A . n 
A 1 633 ASN 633 633 633 ASN ASN A . n 
A 1 634 LEU 634 634 634 LEU LEU A . n 
A 1 635 SER 635 635 635 SER SER A . n 
A 1 636 GLY 636 636 636 GLY GLY A . n 
A 1 637 GLN 637 637 637 GLN GLN A . n 
A 1 638 ILE 638 638 638 ILE ILE A . n 
A 1 639 PRO 639 639 639 PRO PRO A . n 
A 1 640 PRO 640 640 640 PRO PRO A . n 
A 1 641 SER 641 641 641 SER SER A . n 
A 1 642 PHE 642 642 642 PHE PHE A . n 
A 1 643 LYS 643 643 643 LYS LYS A . n 
A 1 644 ASP 644 644 644 ASP ASP A . n 
A 1 645 MET 645 645 645 MET MET A . n 
A 1 646 LEU 646 646 646 LEU LEU A . n 
A 1 647 ALA 647 647 647 ALA ALA A . n 
A 1 648 LEU 648 648 648 LEU LEU A . n 
A 1 649 THR 649 649 649 THR THR A . n 
A 1 650 HIS 650 650 650 HIS HIS A . n 
A 1 651 VAL 651 651 651 VAL VAL A . n 
A 1 652 ASP 652 652 652 ASP ASP A . n 
A 1 653 VAL 653 653 653 VAL VAL A . n 
A 1 654 SER 654 654 654 SER SER A . n 
A 1 655 HIS 655 655 655 HIS HIS A . n 
A 1 656 ASN 656 656 656 ASN ASN A . n 
A 1 657 ASN 657 657 657 ASN ASN A . n 
A 1 658 LEU 658 658 658 LEU LEU A . n 
A 1 659 GLN 659 659 659 GLN GLN A . n 
A 1 660 GLY 660 660 660 GLY GLY A . n 
A 1 661 PRO 661 661 661 PRO PRO A . n 
A 1 662 ILE 662 662 662 ILE ILE A . n 
A 1 663 PRO 663 663 663 PRO PRO A . n 
A 1 664 ASP 664 664 664 ASP ASP A . n 
A 1 665 ASN 665 665 665 ASN ASN A . n 
A 1 666 ALA 666 666 666 ALA ALA A . n 
A 1 667 ALA 667 667 667 ALA ALA A . n 
A 1 668 PHE 668 668 668 PHE PHE A . n 
A 1 669 ARG 669 669 669 ARG ARG A . n 
A 1 670 ASN 670 670 670 ASN ASN A . n 
A 1 671 ALA 671 671 671 ALA ALA A . n 
A 1 672 PRO 672 672 672 PRO PRO A . n 
A 1 673 PRO 673 673 673 PRO PRO A . n 
A 1 674 ASP 674 674 674 ASP ASP A . n 
A 1 675 ALA 675 675 675 ALA ALA A . n 
A 1 676 PHE 676 676 676 PHE PHE A . n 
A 1 677 GLU 677 677 677 GLU GLU A . n 
A 1 678 GLY 678 678 678 GLY GLY A . n 
A 1 679 ASN 679 679 679 ASN ASN A . n 
A 1 680 LYS 680 680 680 LYS LYS A . n 
A 1 681 ASP 681 681 681 ASP ASP A . n 
A 1 682 LEU 682 682 682 LEU LEU A . n 
A 1 683 CYS 683 683 683 CYS CYS A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   GLU 2   2   ?   ?   ?   B . n 
B 2 3   ARG 3   3   ?   ?   ?   B . n 
B 2 4   ARG 4   4   ?   ?   ?   B . n 
B 2 5   LEU 5   5   ?   ?   ?   B . n 
B 2 6   MET 6   6   ?   ?   ?   B . n 
B 2 7   ILE 7   7   ?   ?   ?   B . n 
B 2 8   PRO 8   8   ?   ?   ?   B . n 
B 2 9   CYS 9   9   ?   ?   ?   B . n 
B 2 10  PHE 10  10  ?   ?   ?   B . n 
B 2 11  PHE 11  11  ?   ?   ?   B . n 
B 2 12  TRP 12  12  ?   ?   ?   B . n 
B 2 13  LEU 13  13  ?   ?   ?   B . n 
B 2 14  ILE 14  14  ?   ?   ?   B . n 
B 2 15  LEU 15  15  ?   ?   ?   B . n 
B 2 16  VAL 16  16  ?   ?   ?   B . n 
B 2 17  LEU 17  17  ?   ?   ?   B . n 
B 2 18  ASP 18  18  ?   ?   ?   B . n 
B 2 19  LEU 19  19  ?   ?   ?   B . n 
B 2 20  VAL 20  20  ?   ?   ?   B . n 
B 2 21  LEU 21  21  ?   ?   ?   B . n 
B 2 22  ARG 22  22  ?   ?   ?   B . n 
B 2 23  VAL 23  23  ?   ?   ?   B . n 
B 2 24  SER 24  24  ?   ?   ?   B . n 
B 2 25  GLY 25  25  ?   ?   ?   B . n 
B 2 26  ASN 26  26  26  ASN ASN B . n 
B 2 27  ALA 27  27  27  ALA ALA B . n 
B 2 28  GLU 28  28  28  GLU GLU B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  ASP 30  30  30  ASP ASP B . n 
B 2 31  ALA 31  31  31  ALA ALA B . n 
B 2 32  LEU 32  32  32  LEU LEU B . n 
B 2 33  SER 33  33  33  SER SER B . n 
B 2 34  ALA 34  34  34  ALA ALA B . n 
B 2 35  LEU 35  35  35  LEU LEU B . n 
B 2 36  LYS 36  36  36  LYS LYS B . n 
B 2 37  ASN 37  37  37  ASN ASN B . n 
B 2 38  SER 38  38  38  SER SER B . n 
B 2 39  LEU 39  39  39  LEU LEU B . n 
B 2 40  ALA 40  40  40  ALA ALA B . n 
B 2 41  ASP 41  41  41  ASP ASP B . n 
B 2 42  PRO 42  42  42  PRO PRO B . n 
B 2 43  ASN 43  43  43  ASN ASN B . n 
B 2 44  LYS 44  44  44  LYS LYS B . n 
B 2 45  VAL 45  45  45  VAL VAL B . n 
B 2 46  LEU 46  46  46  LEU LEU B . n 
B 2 47  GLN 47  47  47  GLN GLN B . n 
B 2 48  SER 48  48  48  SER SER B . n 
B 2 49  TRP 49  49  49  TRP TRP B . n 
B 2 50  ASP 50  50  50  ASP ASP B . n 
B 2 51  ALA 51  51  51  ALA ALA B . n 
B 2 52  THR 52  52  52  THR THR B . n 
B 2 53  LEU 53  53  53  LEU LEU B . n 
B 2 54  VAL 54  54  54  VAL VAL B . n 
B 2 55  THR 55  55  55  THR THR B . n 
B 2 56  PRO 56  56  56  PRO PRO B . n 
B 2 57  CYS 57  57  57  CYS CYS B . n 
B 2 58  THR 58  58  58  THR THR B . n 
B 2 59  TRP 59  59  59  TRP TRP B . n 
B 2 60  PHE 60  60  60  PHE PHE B . n 
B 2 61  HIS 61  61  61  HIS HIS B . n 
B 2 62  VAL 62  62  62  VAL VAL B . n 
B 2 63  THR 63  63  63  THR THR B . n 
B 2 64  CYS 64  64  64  CYS CYS B . n 
B 2 65  ASN 65  65  65  ASN ASN B . n 
B 2 66  SER 66  66  66  SER SER B . n 
B 2 67  ASP 67  67  67  ASP ASP B . n 
B 2 68  ASN 68  68  68  ASN ASN B . n 
B 2 69  SER 69  69  69  SER SER B . n 
B 2 70  VAL 70  70  70  VAL VAL B . n 
B 2 71  THR 71  71  71  THR THR B . n 
B 2 72  ARG 72  72  72  ARG ARG B . n 
B 2 73  VAL 73  73  73  VAL VAL B . n 
B 2 74  ASP 74  74  74  ASP ASP B . n 
B 2 75  LEU 75  75  75  LEU LEU B . n 
B 2 76  GLY 76  76  76  GLY GLY B . n 
B 2 77  ASN 77  77  77  ASN ASN B . n 
B 2 78  ALA 78  78  78  ALA ALA B . n 
B 2 79  ASN 79  79  79  ASN ASN B . n 
B 2 80  LEU 80  80  80  LEU LEU B . n 
B 2 81  SER 81  81  81  SER SER B . n 
B 2 82  GLY 82  82  82  GLY GLY B . n 
B 2 83  GLN 83  83  83  GLN GLN B . n 
B 2 84  LEU 84  84  84  LEU LEU B . n 
B 2 85  VAL 85  85  85  VAL VAL B . n 
B 2 86  MET 86  86  86  MET MET B . n 
B 2 87  GLN 87  87  87  GLN GLN B . n 
B 2 88  LEU 88  88  88  LEU LEU B . n 
B 2 89  GLY 89  89  89  GLY GLY B . n 
B 2 90  GLN 90  90  90  GLN GLN B . n 
B 2 91  LEU 91  91  91  LEU LEU B . n 
B 2 92  PRO 92  92  92  PRO PRO B . n 
B 2 93  ASN 93  93  93  ASN ASN B . n 
B 2 94  LEU 94  94  94  LEU LEU B . n 
B 2 95  GLN 95  95  95  GLN GLN B . n 
B 2 96  TYR 96  96  96  TYR TYR B . n 
B 2 97  LEU 97  97  97  LEU LEU B . n 
B 2 98  GLU 98  98  98  GLU GLU B . n 
B 2 99  LEU 99  99  99  LEU LEU B . n 
B 2 100 TYR 100 100 100 TYR TYR B . n 
B 2 101 SER 101 101 101 SER SER B . n 
B 2 102 ASN 102 102 102 ASN ASN B . n 
B 2 103 ASN 103 103 103 ASN ASN B . n 
B 2 104 ILE 104 104 104 ILE ILE B . n 
B 2 105 THR 105 105 105 THR THR B . n 
B 2 106 GLY 106 106 106 GLY GLY B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 ILE 108 108 108 ILE ILE B . n 
B 2 109 PRO 109 109 109 PRO PRO B . n 
B 2 110 GLU 110 110 110 GLU GLU B . n 
B 2 111 GLN 111 111 111 GLN GLN B . n 
B 2 112 LEU 112 112 112 LEU LEU B . n 
B 2 113 GLY 113 113 113 GLY GLY B . n 
B 2 114 ASN 114 114 114 ASN ASN B . n 
B 2 115 LEU 115 115 115 LEU LEU B . n 
B 2 116 THR 116 116 116 THR THR B . n 
B 2 117 GLU 117 117 117 GLU GLU B . n 
B 2 118 LEU 118 118 118 LEU LEU B . n 
B 2 119 VAL 119 119 119 VAL VAL B . n 
B 2 120 SER 120 120 120 SER SER B . n 
B 2 121 LEU 121 121 121 LEU LEU B . n 
B 2 122 ASP 122 122 122 ASP ASP B . n 
B 2 123 LEU 123 123 123 LEU LEU B . n 
B 2 124 TYR 124 124 124 TYR TYR B . n 
B 2 125 LEU 125 125 125 LEU LEU B . n 
B 2 126 ASN 126 126 126 ASN ASN B . n 
B 2 127 ASN 127 127 127 ASN ASN B . n 
B 2 128 LEU 128 128 128 LEU LEU B . n 
B 2 129 SER 129 129 129 SER SER B . n 
B 2 130 GLY 130 130 130 GLY GLY B . n 
B 2 131 PRO 131 131 131 PRO PRO B . n 
B 2 132 ILE 132 132 132 ILE ILE B . n 
B 2 133 PRO 133 133 133 PRO PRO B . n 
B 2 134 SER 134 134 134 SER SER B . n 
B 2 135 THR 135 135 135 THR THR B . n 
B 2 136 LEU 136 136 136 LEU LEU B . n 
B 2 137 GLY 137 137 137 GLY GLY B . n 
B 2 138 ARG 138 138 138 ARG ARG B . n 
B 2 139 LEU 139 139 139 LEU LEU B . n 
B 2 140 LYS 140 140 140 LYS LYS B . n 
B 2 141 LYS 141 141 141 LYS LYS B . n 
B 2 142 LEU 142 142 142 LEU LEU B . n 
B 2 143 ARG 143 143 143 ARG ARG B . n 
B 2 144 PHE 144 144 144 PHE PHE B . n 
B 2 145 LEU 145 145 145 LEU LEU B . n 
B 2 146 ARG 146 146 146 ARG ARG B . n 
B 2 147 LEU 147 147 147 LEU LEU B . n 
B 2 148 ASN 148 148 148 ASN ASN B . n 
B 2 149 ASN 149 149 149 ASN ASN B . n 
B 2 150 ASN 150 150 150 ASN ASN B . n 
B 2 151 SER 151 151 151 SER SER B . n 
B 2 152 LEU 152 152 152 LEU LEU B . n 
B 2 153 SER 153 153 153 SER SER B . n 
B 2 154 GLY 154 154 154 GLY GLY B . n 
B 2 155 GLU 155 155 155 GLU GLU B . n 
B 2 156 ILE 156 156 156 ILE ILE B . n 
B 2 157 PRO 157 157 157 PRO PRO B . n 
B 2 158 ARG 158 158 158 ARG ARG B . n 
B 2 159 SER 159 159 159 SER SER B . n 
B 2 160 LEU 160 160 160 LEU LEU B . n 
B 2 161 THR 161 161 161 THR THR B . n 
B 2 162 ALA 162 162 162 ALA ALA B . n 
B 2 163 VAL 163 163 163 VAL VAL B . n 
B 2 164 LEU 164 164 164 LEU LEU B . n 
B 2 165 THR 165 165 165 THR THR B . n 
B 2 166 LEU 166 166 166 LEU LEU B . n 
B 2 167 GLN 167 167 167 GLN GLN B . n 
B 2 168 VAL 168 168 168 VAL VAL B . n 
B 2 169 LEU 169 169 169 LEU LEU B . n 
B 2 170 ASP 170 170 170 ASP ASP B . n 
B 2 171 LEU 171 171 171 LEU LEU B . n 
B 2 172 SER 172 172 172 SER SER B . n 
B 2 173 ASN 173 173 173 ASN ASN B . n 
B 2 174 ASN 174 174 174 ASN ASN B . n 
B 2 175 PRO 175 175 175 PRO PRO B . n 
B 2 176 LEU 176 176 176 LEU LEU B . n 
B 2 177 THR 177 177 177 THR THR B . n 
B 2 178 GLY 178 178 178 GLY GLY B . n 
B 2 179 ASP 179 179 179 ASP ASP B . n 
B 2 180 ILE 180 180 180 ILE ILE B . n 
B 2 181 PRO 181 181 181 PRO PRO B . n 
B 2 182 VAL 182 182 182 VAL VAL B . n 
B 2 183 ASN 183 183 183 ASN ASN B . n 
B 2 184 GLY 184 184 184 GLY GLY B . n 
B 2 185 SER 185 185 185 SER SER B . n 
B 2 186 PHE 186 186 186 PHE PHE B . n 
B 2 187 SER 187 187 187 SER SER B . n 
B 2 188 LEU 188 188 188 LEU LEU B . n 
B 2 189 PHE 189 189 189 PHE PHE B . n 
B 2 190 THR 190 190 190 THR THR B . n 
B 2 191 PRO 191 191 191 PRO PRO B . n 
B 2 192 ILE 192 192 192 ILE ILE B . n 
B 2 193 SER 193 193 193 SER SER B . n 
B 2 194 PHE 194 194 194 PHE PHE B . n 
B 2 195 ALA 195 195 195 ALA ALA B . n 
B 2 196 ASN 196 196 196 ASN ASN B . n 
B 2 197 THR 197 197 197 THR THR B . n 
B 2 198 LYS 198 198 198 LYS LYS B . n 
B 2 199 LEU 199 199 199 LEU LEU B . n 
B 2 200 THR 200 200 200 THR THR B . n 
B 2 201 PRO 201 201 ?   ?   ?   B . n 
B 2 202 LEU 202 202 ?   ?   ?   B . n 
B 2 203 PRO 203 203 ?   ?   ?   B . n 
B 2 204 ALA 204 204 ?   ?   ?   B . n 
B 2 205 SER 205 205 ?   ?   ?   B . n 
B 2 206 PRO 206 206 ?   ?   ?   B . n 
B 2 207 PRO 207 207 ?   ?   ?   B . n 
B 2 208 PRO 208 208 ?   ?   ?   B . n 
B 2 209 PRO 209 209 ?   ?   ?   B . n 
B 2 210 ILE 210 210 ?   ?   ?   B . n 
B 2 211 SER 211 211 ?   ?   ?   B . n 
B 2 212 PRO 212 212 ?   ?   ?   B . n 
B 2 213 THR 213 213 ?   ?   ?   B . n 
B 2 214 PRO 214 214 ?   ?   ?   B . n 
B 2 215 PRO 215 215 ?   ?   ?   B . n 
B 2 216 SER 216 216 ?   ?   ?   B . n 
B 2 217 PRO 217 217 ?   ?   ?   B . n 
B 2 218 ALA 218 218 ?   ?   ?   B . n 
B 2 219 GLY 219 219 ?   ?   ?   B . n 
B 2 220 SER 220 220 ?   ?   ?   B . n 
B 2 221 HIS 221 221 ?   ?   ?   B . n 
B 2 222 HIS 222 222 ?   ?   ?   B . n 
B 2 223 HIS 223 223 ?   ?   ?   B . n 
B 2 224 HIS 224 224 ?   ?   ?   B . n 
B 2 225 HIS 225 225 ?   ?   ?   B . n 
B 2 226 HIS 226 226 ?   ?   ?   B . n 
B 2 227 HIS 227 227 ?   ?   ?   B . n 
B 2 228 HIS 228 228 ?   ?   ?   B . n 
B 2 229 HIS 229 229 ?   ?   ?   B . n 
B 2 230 HIS 230 230 ?   ?   ?   B . n 
C 3 1   GLU 1   1   1   GLU GLU C . n 
C 3 2   SER 2   2   2   SER SER C . n 
C 3 3   SER 3   3   3   SER SER C . n 
C 3 4   SER 4   4   4   SER SER C . n 
C 3 5   SER 5   5   5   SER SER C . n 
C 3 6   HIS 6   6   6   HIS HIS C . n 
C 3 7   SER 7   7   7   SER SER C . n 
C 3 8   GLU 8   8   8   GLU GLU C . n 
C 3 9   ARG 9   9   9   ARG ARG C . n 
C 3 10  ALA 10  10  10  ALA ALA C . n 
C 3 11  GLY 11  11  11  GLY GLY C . n 
C 3 12  GLY 12  12  12  GLY GLY C . n 
C 3 13  ARG 13  13  13  ARG ARG C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   ASN 2   2   ?   ?   ?   D . n 
D 1 3   LYS 3   3   ?   ?   ?   D . n 
D 1 4   THR 4   4   ?   ?   ?   D . n 
D 1 5   ASN 5   5   ?   ?   ?   D . n 
D 1 6   PRO 6   6   ?   ?   ?   D . n 
D 1 7   GLU 7   7   ?   ?   ?   D . n 
D 1 8   ARG 8   8   ?   ?   ?   D . n 
D 1 9   LYS 9   9   ?   ?   ?   D . n 
D 1 10  ILE 10  10  ?   ?   ?   D . n 
D 1 11  SER 11  11  ?   ?   ?   D . n 
D 1 12  LEU 12  12  ?   ?   ?   D . n 
D 1 13  THR 13  13  ?   ?   ?   D . n 
D 1 14  SER 14  14  ?   ?   ?   D . n 
D 1 15  PHE 15  15  ?   ?   ?   D . n 
D 1 16  LYS 16  16  ?   ?   ?   D . n 
D 1 17  GLU 17  17  ?   ?   ?   D . n 
D 1 18  ARG 18  18  ?   ?   ?   D . n 
D 1 19  MET 19  19  ?   ?   ?   D . n 
D 1 20  ALA 20  20  ?   ?   ?   D . n 
D 1 21  CYS 21  21  ?   ?   ?   D . n 
D 1 22  LYS 22  22  ?   ?   ?   D . n 
D 1 23  GLU 23  23  ?   ?   ?   D . n 
D 1 24  LYS 24  24  ?   ?   ?   D . n 
D 1 25  PRO 25  25  ?   ?   ?   D . n 
D 1 26  ARG 26  26  ?   ?   ?   D . n 
D 1 27  ASP 27  27  ?   ?   ?   D . n 
D 1 28  LEU 28  28  ?   ?   ?   D . n 
D 1 29  GLN 29  29  ?   ?   ?   D . n 
D 1 30  VAL 30  30  ?   ?   ?   D . n 
D 1 31  LEU 31  31  ?   ?   ?   D . n 
D 1 32  LEU 32  32  ?   ?   ?   D . n 
D 1 33  ILE 33  33  ?   ?   ?   D . n 
D 1 34  ILE 34  34  ?   ?   ?   D . n 
D 1 35  SER 35  35  ?   ?   ?   D . n 
D 1 36  ILE 36  36  ?   ?   ?   D . n 
D 1 37  VAL 37  37  ?   ?   ?   D . n 
D 1 38  LEU 38  38  ?   ?   ?   D . n 
D 1 39  SER 39  39  ?   ?   ?   D . n 
D 1 40  CYS 40  40  ?   ?   ?   D . n 
D 1 41  SER 41  41  ?   ?   ?   D . n 
D 1 42  PHE 42  42  ?   ?   ?   D . n 
D 1 43  ALA 43  43  ?   ?   ?   D . n 
D 1 44  VAL 44  44  ?   ?   ?   D . n 
D 1 45  SER 45  45  ?   ?   ?   D . n 
D 1 46  ALA 46  46  ?   ?   ?   D . n 
D 1 47  THR 47  47  47  THR THR D . n 
D 1 48  VAL 48  48  48  VAL VAL D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  GLU 50  50  50  GLU GLU D . n 
D 1 51  ALA 51  51  51  ALA ALA D . n 
D 1 52  ASN 52  52  52  ASN ASN D . n 
D 1 53  ALA 53  53  53  ALA ALA D . n 
D 1 54  LEU 54  54  54  LEU LEU D . n 
D 1 55  LEU 55  55  55  LEU LEU D . n 
D 1 56  LYS 56  56  56  LYS LYS D . n 
D 1 57  TRP 57  57  57  TRP TRP D . n 
D 1 58  LYS 58  58  58  LYS LYS D . n 
D 1 59  SER 59  59  59  SER SER D . n 
D 1 60  THR 60  60  60  THR THR D . n 
D 1 61  PHE 61  61  61  PHE PHE D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  GLN 64  64  64  GLN GLN D . n 
D 1 65  THR 65  65  65  THR THR D . n 
D 1 66  SER 66  66  66  SER SER D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  SER 68  68  68  SER SER D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  SER 71  71  71  SER SER D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  TRP 73  73  73  TRP TRP D . n 
D 1 74  VAL 74  74  74  VAL VAL D . n 
D 1 75  ASN 75  75  75  ASN ASN D . n 
D 1 76  PRO 76  76  76  PRO PRO D . n 
D 1 77  ASN 77  77  77  ASN ASN D . n 
D 1 78  THR 78  78  78  THR THR D . n 
D 1 79  SER 79  79  79  SER SER D . n 
D 1 80  SER 80  80  80  SER SER D . n 
D 1 81  PHE 81  81  81  PHE PHE D . n 
D 1 82  CYS 82  82  82  CYS CYS D . n 
D 1 83  THR 83  83  83  THR THR D . n 
D 1 84  SER 84  84  84  SER SER D . n 
D 1 85  TRP 85  85  85  TRP TRP D . n 
D 1 86  TYR 86  86  86  TYR TYR D . n 
D 1 87  GLY 87  87  87  GLY GLY D . n 
D 1 88  VAL 88  88  88  VAL VAL D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  CYS 90  90  90  CYS CYS D . n 
D 1 91  SER 91  91  91  SER SER D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  SER 94  94  94  SER SER D . n 
D 1 95  ILE 95  95  95  ILE ILE D . n 
D 1 96  ILE 96  96  96  ILE ILE D . n 
D 1 97  ARG 97  97  97  ARG ARG D . n 
D 1 98  LEU 98  98  98  LEU LEU D . n 
D 1 99  ASN 99  99  99  ASN ASN D . n 
D 1 100 LEU 100 100 100 LEU LEU D . n 
D 1 101 THR 101 101 101 THR THR D . n 
D 1 102 ASN 102 102 102 ASN ASN D . n 
D 1 103 THR 103 103 103 THR THR D . n 
D 1 104 GLY 104 104 104 GLY GLY D . n 
D 1 105 ILE 105 105 105 ILE ILE D . n 
D 1 106 GLU 106 106 106 GLU GLU D . n 
D 1 107 GLY 107 107 107 GLY GLY D . n 
D 1 108 THR 108 108 108 THR THR D . n 
D 1 109 PHE 109 109 109 PHE PHE D . n 
D 1 110 GLU 110 110 110 GLU GLU D . n 
D 1 111 ASP 111 111 111 ASP ASP D . n 
D 1 112 PHE 112 112 112 PHE PHE D . n 
D 1 113 PRO 113 113 113 PRO PRO D . n 
D 1 114 PHE 114 114 114 PHE PHE D . n 
D 1 115 SER 115 115 115 SER SER D . n 
D 1 116 SER 116 116 116 SER SER D . n 
D 1 117 LEU 117 117 117 LEU LEU D . n 
D 1 118 PRO 118 118 118 PRO PRO D . n 
D 1 119 ASN 119 119 119 ASN ASN D . n 
D 1 120 LEU 120 120 120 LEU LEU D . n 
D 1 121 THR 121 121 121 THR THR D . n 
D 1 122 PHE 122 122 122 PHE PHE D . n 
D 1 123 VAL 123 123 123 VAL VAL D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 SER 126 126 126 SER SER D . n 
D 1 127 MET 127 127 127 MET MET D . n 
D 1 128 ASN 128 128 128 ASN ASN D . n 
D 1 129 ARG 129 129 129 ARG ARG D . n 
D 1 130 PHE 130 130 130 PHE PHE D . n 
D 1 131 SER 131 131 131 SER SER D . n 
D 1 132 GLY 132 132 132 GLY GLY D . n 
D 1 133 THR 133 133 133 THR THR D . n 
D 1 134 ILE 134 134 134 ILE ILE D . n 
D 1 135 SER 135 135 135 SER SER D . n 
D 1 136 PRO 136 136 136 PRO PRO D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 TRP 138 138 138 TRP TRP D . n 
D 1 139 GLY 139 139 139 GLY GLY D . n 
D 1 140 ARG 140 140 140 ARG ARG D . n 
D 1 141 PHE 141 141 141 PHE PHE D . n 
D 1 142 SER 142 142 142 SER SER D . n 
D 1 143 LYS 143 143 143 LYS LYS D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 GLU 145 145 145 GLU GLU D . n 
D 1 146 TYR 146 146 146 TYR TYR D . n 
D 1 147 PHE 147 147 147 PHE PHE D . n 
D 1 148 ASP 148 148 148 ASP ASP D . n 
D 1 149 LEU 149 149 149 LEU LEU D . n 
D 1 150 SER 150 150 150 SER SER D . n 
D 1 151 ILE 151 151 151 ILE ILE D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 GLN 153 153 153 GLN GLN D . n 
D 1 154 LEU 154 154 154 LEU LEU D . n 
D 1 155 VAL 155 155 155 VAL VAL D . n 
D 1 156 GLY 156 156 156 GLY GLY D . n 
D 1 157 GLU 157 157 157 GLU GLU D . n 
D 1 158 ILE 158 158 158 ILE ILE D . n 
D 1 159 PRO 159 159 159 PRO PRO D . n 
D 1 160 PRO 160 160 160 PRO PRO D . n 
D 1 161 GLU 161 161 161 GLU GLU D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 GLY 163 163 163 GLY GLY D . n 
D 1 164 LYS 164 164 164 LYS LYS D . n 
D 1 165 LEU 165 165 165 LEU LEU D . n 
D 1 166 SER 166 166 166 SER SER D . n 
D 1 167 ASN 167 167 167 ASN ASN D . n 
D 1 168 LEU 168 168 168 LEU LEU D . n 
D 1 169 ASP 169 169 169 ASP ASP D . n 
D 1 170 THR 170 170 170 THR THR D . n 
D 1 171 LEU 171 171 171 LEU LEU D . n 
D 1 172 HIS 172 172 172 HIS HIS D . n 
D 1 173 LEU 173 173 173 LEU LEU D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 GLU 175 175 175 GLU GLU D . n 
D 1 176 ASN 176 176 176 ASN ASN D . n 
D 1 177 LYS 177 177 177 LYS LYS D . n 
D 1 178 LEU 178 178 178 LEU LEU D . n 
D 1 179 ASN 179 179 179 ASN ASN D . n 
D 1 180 GLY 180 180 180 GLY GLY D . n 
D 1 181 SER 181 181 181 SER SER D . n 
D 1 182 ILE 182 182 182 ILE ILE D . n 
D 1 183 PRO 183 183 183 PRO PRO D . n 
D 1 184 SER 184 184 184 SER SER D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ILE 186 186 186 ILE ILE D . n 
D 1 187 GLY 187 187 187 GLY GLY D . n 
D 1 188 ARG 188 188 188 ARG ARG D . n 
D 1 189 LEU 189 189 189 LEU LEU D . n 
D 1 190 THR 190 190 190 THR THR D . n 
D 1 191 LYS 191 191 191 LYS LYS D . n 
D 1 192 VAL 192 192 192 VAL VAL D . n 
D 1 193 THR 193 193 193 THR THR D . n 
D 1 194 GLU 194 194 194 GLU GLU D . n 
D 1 195 ILE 195 195 195 ILE ILE D . n 
D 1 196 ALA 196 196 196 ALA ALA D . n 
D 1 197 ILE 197 197 197 ILE ILE D . n 
D 1 198 TYR 198 198 198 TYR TYR D . n 
D 1 199 ASP 199 199 199 ASP ASP D . n 
D 1 200 ASN 200 200 200 ASN ASN D . n 
D 1 201 LEU 201 201 201 LEU LEU D . n 
D 1 202 LEU 202 202 202 LEU LEU D . n 
D 1 203 THR 203 203 203 THR THR D . n 
D 1 204 GLY 204 204 204 GLY GLY D . n 
D 1 205 PRO 205 205 205 PRO PRO D . n 
D 1 206 ILE 206 206 206 ILE ILE D . n 
D 1 207 PRO 207 207 207 PRO PRO D . n 
D 1 208 SER 208 208 208 SER SER D . n 
D 1 209 SER 209 209 209 SER SER D . n 
D 1 210 PHE 210 210 210 PHE PHE D . n 
D 1 211 GLY 211 211 211 GLY GLY D . n 
D 1 212 ASN 212 212 212 ASN ASN D . n 
D 1 213 LEU 213 213 213 LEU LEU D . n 
D 1 214 THR 214 214 214 THR THR D . n 
D 1 215 LYS 215 215 215 LYS LYS D . n 
D 1 216 LEU 216 216 216 LEU LEU D . n 
D 1 217 VAL 217 217 217 VAL VAL D . n 
D 1 218 ASN 218 218 218 ASN ASN D . n 
D 1 219 LEU 219 219 219 LEU LEU D . n 
D 1 220 TYR 220 220 220 TYR TYR D . n 
D 1 221 LEU 221 221 221 LEU LEU D . n 
D 1 222 PHE 222 222 222 PHE PHE D . n 
D 1 223 ILE 223 223 223 ILE ILE D . n 
D 1 224 ASN 224 224 224 ASN ASN D . n 
D 1 225 SER 225 225 225 SER SER D . n 
D 1 226 LEU 226 226 226 LEU LEU D . n 
D 1 227 SER 227 227 227 SER SER D . n 
D 1 228 GLY 228 228 228 GLY GLY D . n 
D 1 229 SER 229 229 229 SER SER D . n 
D 1 230 ILE 230 230 230 ILE ILE D . n 
D 1 231 PRO 231 231 231 PRO PRO D . n 
D 1 232 SER 232 232 232 SER SER D . n 
D 1 233 GLU 233 233 233 GLU GLU D . n 
D 1 234 ILE 234 234 234 ILE ILE D . n 
D 1 235 GLY 235 235 235 GLY GLY D . n 
D 1 236 ASN 236 236 236 ASN ASN D . n 
D 1 237 LEU 237 237 237 LEU LEU D . n 
D 1 238 PRO 238 238 238 PRO PRO D . n 
D 1 239 ASN 239 239 239 ASN ASN D . n 
D 1 240 LEU 240 240 240 LEU LEU D . n 
D 1 241 ARG 241 241 241 ARG ARG D . n 
D 1 242 GLU 242 242 242 GLU GLU D . n 
D 1 243 LEU 243 243 243 LEU LEU D . n 
D 1 244 CYS 244 244 244 CYS CYS D . n 
D 1 245 LEU 245 245 245 LEU LEU D . n 
D 1 246 ASP 246 246 246 ASP ASP D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 ASN 248 248 248 ASN ASN D . n 
D 1 249 ASN 249 249 249 ASN ASN D . n 
D 1 250 LEU 250 250 250 LEU LEU D . n 
D 1 251 THR 251 251 251 THR THR D . n 
D 1 252 GLY 252 252 252 GLY GLY D . n 
D 1 253 LYS 253 253 253 LYS LYS D . n 
D 1 254 ILE 254 254 254 ILE ILE D . n 
D 1 255 PRO 255 255 255 PRO PRO D . n 
D 1 256 SER 256 256 256 SER SER D . n 
D 1 257 SER 257 257 257 SER SER D . n 
D 1 258 PHE 258 258 258 PHE PHE D . n 
D 1 259 GLY 259 259 259 GLY GLY D . n 
D 1 260 ASN 260 260 260 ASN ASN D . n 
D 1 261 LEU 261 261 261 LEU LEU D . n 
D 1 262 LYS 262 262 262 LYS LYS D . n 
D 1 263 ASN 263 263 263 ASN ASN D . n 
D 1 264 VAL 264 264 264 VAL VAL D . n 
D 1 265 THR 265 265 265 THR THR D . n 
D 1 266 LEU 266 266 266 LEU LEU D . n 
D 1 267 LEU 267 267 267 LEU LEU D . n 
D 1 268 ASN 268 268 268 ASN ASN D . n 
D 1 269 MET 269 269 269 MET MET D . n 
D 1 270 PHE 270 270 270 PHE PHE D . n 
D 1 271 GLU 271 271 271 GLU GLU D . n 
D 1 272 ASN 272 272 272 ASN ASN D . n 
D 1 273 GLN 273 273 273 GLN GLN D . n 
D 1 274 LEU 274 274 274 LEU LEU D . n 
D 1 275 SER 275 275 275 SER SER D . n 
D 1 276 GLY 276 276 276 GLY GLY D . n 
D 1 277 GLU 277 277 277 GLU GLU D . n 
D 1 278 ILE 278 278 278 ILE ILE D . n 
D 1 279 PRO 279 279 279 PRO PRO D . n 
D 1 280 PRO 280 280 280 PRO PRO D . n 
D 1 281 GLU 281 281 281 GLU GLU D . n 
D 1 282 ILE 282 282 282 ILE ILE D . n 
D 1 283 GLY 283 283 283 GLY GLY D . n 
D 1 284 ASN 284 284 284 ASN ASN D . n 
D 1 285 MET 285 285 285 MET MET D . n 
D 1 286 THR 286 286 286 THR THR D . n 
D 1 287 ALA 287 287 287 ALA ALA D . n 
D 1 288 LEU 288 288 288 LEU LEU D . n 
D 1 289 ASP 289 289 289 ASP ASP D . n 
D 1 290 THR 290 290 290 THR THR D . n 
D 1 291 LEU 291 291 291 LEU LEU D . n 
D 1 292 SER 292 292 292 SER SER D . n 
D 1 293 LEU 293 293 293 LEU LEU D . n 
D 1 294 HIS 294 294 294 HIS HIS D . n 
D 1 295 THR 295 295 295 THR THR D . n 
D 1 296 ASN 296 296 296 ASN ASN D . n 
D 1 297 LYS 297 297 297 LYS LYS D . n 
D 1 298 LEU 298 298 298 LEU LEU D . n 
D 1 299 THR 299 299 299 THR THR D . n 
D 1 300 GLY 300 300 300 GLY GLY D . n 
D 1 301 PRO 301 301 301 PRO PRO D . n 
D 1 302 ILE 302 302 302 ILE ILE D . n 
D 1 303 PRO 303 303 303 PRO PRO D . n 
D 1 304 SER 304 304 304 SER SER D . n 
D 1 305 THR 305 305 305 THR THR D . n 
D 1 306 LEU 306 306 306 LEU LEU D . n 
D 1 307 GLY 307 307 307 GLY GLY D . n 
D 1 308 ASN 308 308 308 ASN ASN D . n 
D 1 309 ILE 309 309 309 ILE ILE D . n 
D 1 310 LYS 310 310 310 LYS LYS D . n 
D 1 311 THR 311 311 311 THR THR D . n 
D 1 312 LEU 312 312 312 LEU LEU D . n 
D 1 313 ALA 313 313 313 ALA ALA D . n 
D 1 314 VAL 314 314 314 VAL VAL D . n 
D 1 315 LEU 315 315 315 LEU LEU D . n 
D 1 316 HIS 316 316 316 HIS HIS D . n 
D 1 317 LEU 317 317 317 LEU LEU D . n 
D 1 318 TYR 318 318 318 TYR TYR D . n 
D 1 319 LEU 319 319 319 LEU LEU D . n 
D 1 320 ASN 320 320 320 ASN ASN D . n 
D 1 321 GLN 321 321 321 GLN GLN D . n 
D 1 322 LEU 322 322 322 LEU LEU D . n 
D 1 323 ASN 323 323 323 ASN ASN D . n 
D 1 324 GLY 324 324 324 GLY GLY D . n 
D 1 325 SER 325 325 325 SER SER D . n 
D 1 326 ILE 326 326 326 ILE ILE D . n 
D 1 327 PRO 327 327 327 PRO PRO D . n 
D 1 328 PRO 328 328 328 PRO PRO D . n 
D 1 329 GLU 329 329 329 GLU GLU D . n 
D 1 330 LEU 330 330 330 LEU LEU D . n 
D 1 331 GLY 331 331 331 GLY GLY D . n 
D 1 332 GLU 332 332 332 GLU GLU D . n 
D 1 333 MET 333 333 333 MET MET D . n 
D 1 334 GLU 334 334 334 GLU GLU D . n 
D 1 335 SER 335 335 335 SER SER D . n 
D 1 336 MET 336 336 336 MET MET D . n 
D 1 337 ILE 337 337 337 ILE ILE D . n 
D 1 338 ASP 338 338 338 ASP ASP D . n 
D 1 339 LEU 339 339 339 LEU LEU D . n 
D 1 340 GLU 340 340 340 GLU GLU D . n 
D 1 341 ILE 341 341 341 ILE ILE D . n 
D 1 342 SER 342 342 342 SER SER D . n 
D 1 343 GLU 343 343 343 GLU GLU D . n 
D 1 344 ASN 344 344 344 ASN ASN D . n 
D 1 345 LYS 345 345 345 LYS LYS D . n 
D 1 346 LEU 346 346 346 LEU LEU D . n 
D 1 347 THR 347 347 347 THR THR D . n 
D 1 348 GLY 348 348 348 GLY GLY D . n 
D 1 349 PRO 349 349 349 PRO PRO D . n 
D 1 350 VAL 350 350 350 VAL VAL D . n 
D 1 351 PRO 351 351 351 PRO PRO D . n 
D 1 352 ASP 352 352 352 ASP ASP D . n 
D 1 353 SER 353 353 353 SER SER D . n 
D 1 354 PHE 354 354 354 PHE PHE D . n 
D 1 355 GLY 355 355 355 GLY GLY D . n 
D 1 356 LYS 356 356 356 LYS LYS D . n 
D 1 357 LEU 357 357 357 LEU LEU D . n 
D 1 358 THR 358 358 358 THR THR D . n 
D 1 359 ALA 359 359 359 ALA ALA D . n 
D 1 360 LEU 360 360 360 LEU LEU D . n 
D 1 361 GLU 361 361 361 GLU GLU D . n 
D 1 362 TRP 362 362 362 TRP TRP D . n 
D 1 363 LEU 363 363 363 LEU LEU D . n 
D 1 364 PHE 364 364 364 PHE PHE D . n 
D 1 365 LEU 365 365 365 LEU LEU D . n 
D 1 366 ARG 366 366 366 ARG ARG D . n 
D 1 367 ASP 367 367 367 ASP ASP D . n 
D 1 368 ASN 368 368 368 ASN ASN D . n 
D 1 369 GLN 369 369 369 GLN GLN D . n 
D 1 370 LEU 370 370 370 LEU LEU D . n 
D 1 371 SER 371 371 371 SER SER D . n 
D 1 372 GLY 372 372 372 GLY GLY D . n 
D 1 373 PRO 373 373 373 PRO PRO D . n 
D 1 374 ILE 374 374 374 ILE ILE D . n 
D 1 375 PRO 375 375 375 PRO PRO D . n 
D 1 376 PRO 376 376 376 PRO PRO D . n 
D 1 377 GLY 377 377 377 GLY GLY D . n 
D 1 378 ILE 378 378 378 ILE ILE D . n 
D 1 379 ALA 379 379 379 ALA ALA D . n 
D 1 380 ASN 380 380 380 ASN ASN D . n 
D 1 381 SER 381 381 381 SER SER D . n 
D 1 382 THR 382 382 382 THR THR D . n 
D 1 383 GLU 383 383 383 GLU GLU D . n 
D 1 384 LEU 384 384 384 LEU LEU D . n 
D 1 385 THR 385 385 385 THR THR D . n 
D 1 386 VAL 386 386 386 VAL VAL D . n 
D 1 387 LEU 387 387 387 LEU LEU D . n 
D 1 388 GLN 388 388 388 GLN GLN D . n 
D 1 389 LEU 389 389 389 LEU LEU D . n 
D 1 390 ASP 390 390 390 ASP ASP D . n 
D 1 391 THR 391 391 391 THR THR D . n 
D 1 392 ASN 392 392 392 ASN ASN D . n 
D 1 393 ASN 393 393 393 ASN ASN D . n 
D 1 394 PHE 394 394 394 PHE PHE D . n 
D 1 395 THR 395 395 395 THR THR D . n 
D 1 396 GLY 396 396 396 GLY GLY D . n 
D 1 397 PHE 397 397 397 PHE PHE D . n 
D 1 398 LEU 398 398 398 LEU LEU D . n 
D 1 399 PRO 399 399 399 PRO PRO D . n 
D 1 400 ASP 400 400 400 ASP ASP D . n 
D 1 401 THR 401 401 401 THR THR D . n 
D 1 402 ILE 402 402 402 ILE ILE D . n 
D 1 403 CYS 403 403 403 CYS CYS D . n 
D 1 404 ARG 404 404 404 ARG ARG D . n 
D 1 405 GLY 405 405 405 GLY GLY D . n 
D 1 406 GLY 406 406 406 GLY GLY D . n 
D 1 407 LYS 407 407 407 LYS LYS D . n 
D 1 408 LEU 408 408 408 LEU LEU D . n 
D 1 409 GLU 409 409 409 GLU GLU D . n 
D 1 410 ASN 410 410 410 ASN ASN D . n 
D 1 411 LEU 411 411 411 LEU LEU D . n 
D 1 412 THR 412 412 412 THR THR D . n 
D 1 413 LEU 413 413 413 LEU LEU D . n 
D 1 414 ASP 414 414 414 ASP ASP D . n 
D 1 415 ASP 415 415 415 ASP ASP D . n 
D 1 416 ASN 416 416 416 ASN ASN D . n 
D 1 417 HIS 417 417 417 HIS HIS D . n 
D 1 418 PHE 418 418 418 PHE PHE D . n 
D 1 419 GLU 419 419 419 GLU GLU D . n 
D 1 420 GLY 420 420 420 GLY GLY D . n 
D 1 421 PRO 421 421 421 PRO PRO D . n 
D 1 422 VAL 422 422 422 VAL VAL D . n 
D 1 423 PRO 423 423 423 PRO PRO D . n 
D 1 424 LYS 424 424 424 LYS LYS D . n 
D 1 425 SER 425 425 425 SER SER D . n 
D 1 426 LEU 426 426 426 LEU LEU D . n 
D 1 427 ARG 427 427 427 ARG ARG D . n 
D 1 428 ASP 428 428 428 ASP ASP D . n 
D 1 429 CYS 429 429 429 CYS CYS D . n 
D 1 430 LYS 430 430 430 LYS LYS D . n 
D 1 431 SER 431 431 431 SER SER D . n 
D 1 432 LEU 432 432 432 LEU LEU D . n 
D 1 433 ILE 433 433 433 ILE ILE D . n 
D 1 434 ARG 434 434 434 ARG ARG D . n 
D 1 435 VAL 435 435 435 VAL VAL D . n 
D 1 436 ARG 436 436 436 ARG ARG D . n 
D 1 437 PHE 437 437 437 PHE PHE D . n 
D 1 438 LYS 438 438 438 LYS LYS D . n 
D 1 439 GLY 439 439 439 GLY GLY D . n 
D 1 440 ASN 440 440 440 ASN ASN D . n 
D 1 441 SER 441 441 441 SER SER D . n 
D 1 442 PHE 442 442 442 PHE PHE D . n 
D 1 443 SER 443 443 443 SER SER D . n 
D 1 444 GLY 444 444 444 GLY GLY D . n 
D 1 445 ASP 445 445 445 ASP ASP D . n 
D 1 446 ILE 446 446 446 ILE ILE D . n 
D 1 447 SER 447 447 447 SER SER D . n 
D 1 448 GLU 448 448 448 GLU GLU D . n 
D 1 449 ALA 449 449 449 ALA ALA D . n 
D 1 450 PHE 450 450 450 PHE PHE D . n 
D 1 451 GLY 451 451 451 GLY GLY D . n 
D 1 452 VAL 452 452 452 VAL VAL D . n 
D 1 453 TYR 453 453 453 TYR TYR D . n 
D 1 454 PRO 454 454 454 PRO PRO D . n 
D 1 455 THR 455 455 455 THR THR D . n 
D 1 456 LEU 456 456 456 LEU LEU D . n 
D 1 457 ASN 457 457 457 ASN ASN D . n 
D 1 458 PHE 458 458 458 PHE PHE D . n 
D 1 459 ILE 459 459 459 ILE ILE D . n 
D 1 460 ASP 460 460 460 ASP ASP D . n 
D 1 461 LEU 461 461 461 LEU LEU D . n 
D 1 462 SER 462 462 462 SER SER D . n 
D 1 463 ASN 463 463 463 ASN ASN D . n 
D 1 464 ASN 464 464 464 ASN ASN D . n 
D 1 465 ASN 465 465 465 ASN ASN D . n 
D 1 466 PHE 466 466 466 PHE PHE D . n 
D 1 467 HIS 467 467 467 HIS HIS D . n 
D 1 468 GLY 468 468 468 GLY GLY D . n 
D 1 469 GLN 469 469 469 GLN GLN D . n 
D 1 470 LEU 470 470 470 LEU LEU D . n 
D 1 471 SER 471 471 471 SER SER D . n 
D 1 472 ALA 472 472 472 ALA ALA D . n 
D 1 473 ASN 473 473 473 ASN ASN D . n 
D 1 474 TRP 474 474 474 TRP TRP D . n 
D 1 475 GLU 475 475 475 GLU GLU D . n 
D 1 476 GLN 476 476 476 GLN GLN D . n 
D 1 477 SER 477 477 477 SER SER D . n 
D 1 478 GLN 478 478 478 GLN GLN D . n 
D 1 479 LYS 479 479 479 LYS LYS D . n 
D 1 480 LEU 480 480 480 LEU LEU D . n 
D 1 481 VAL 481 481 481 VAL VAL D . n 
D 1 482 ALA 482 482 482 ALA ALA D . n 
D 1 483 PHE 483 483 483 PHE PHE D . n 
D 1 484 ILE 484 484 484 ILE ILE D . n 
D 1 485 LEU 485 485 485 LEU LEU D . n 
D 1 486 SER 486 486 486 SER SER D . n 
D 1 487 ASN 487 487 487 ASN ASN D . n 
D 1 488 ASN 488 488 488 ASN ASN D . n 
D 1 489 SER 489 489 489 SER SER D . n 
D 1 490 ILE 490 490 490 ILE ILE D . n 
D 1 491 THR 491 491 491 THR THR D . n 
D 1 492 GLY 492 492 492 GLY GLY D . n 
D 1 493 ALA 493 493 493 ALA ALA D . n 
D 1 494 ILE 494 494 494 ILE ILE D . n 
D 1 495 PRO 495 495 495 PRO PRO D . n 
D 1 496 PRO 496 496 496 PRO PRO D . n 
D 1 497 GLU 497 497 497 GLU GLU D . n 
D 1 498 ILE 498 498 498 ILE ILE D . n 
D 1 499 TRP 499 499 499 TRP TRP D . n 
D 1 500 ASN 500 500 500 ASN ASN D . n 
D 1 501 MET 501 501 501 MET MET D . n 
D 1 502 THR 502 502 502 THR THR D . n 
D 1 503 GLN 503 503 503 GLN GLN D . n 
D 1 504 LEU 504 504 504 LEU LEU D . n 
D 1 505 SER 505 505 505 SER SER D . n 
D 1 506 GLN 506 506 506 GLN GLN D . n 
D 1 507 LEU 507 507 507 LEU LEU D . n 
D 1 508 ASP 508 508 508 ASP ASP D . n 
D 1 509 LEU 509 509 509 LEU LEU D . n 
D 1 510 SER 510 510 510 SER SER D . n 
D 1 511 SER 511 511 511 SER SER D . n 
D 1 512 ASN 512 512 512 ASN ASN D . n 
D 1 513 ARG 513 513 513 ARG ARG D . n 
D 1 514 ILE 514 514 514 ILE ILE D . n 
D 1 515 THR 515 515 515 THR THR D . n 
D 1 516 GLY 516 516 516 GLY GLY D . n 
D 1 517 GLU 517 517 517 GLU GLU D . n 
D 1 518 LEU 518 518 518 LEU LEU D . n 
D 1 519 PRO 519 519 519 PRO PRO D . n 
D 1 520 GLU 520 520 520 GLU GLU D . n 
D 1 521 SER 521 521 521 SER SER D . n 
D 1 522 ILE 522 522 522 ILE ILE D . n 
D 1 523 SER 523 523 523 SER SER D . n 
D 1 524 ASN 524 524 524 ASN ASN D . n 
D 1 525 ILE 525 525 525 ILE ILE D . n 
D 1 526 ASN 526 526 526 ASN ASN D . n 
D 1 527 ARG 527 527 527 ARG ARG D . n 
D 1 528 ILE 528 528 528 ILE ILE D . n 
D 1 529 SER 529 529 529 SER SER D . n 
D 1 530 LYS 530 530 530 LYS LYS D . n 
D 1 531 LEU 531 531 531 LEU LEU D . n 
D 1 532 GLN 532 532 532 GLN GLN D . n 
D 1 533 LEU 533 533 533 LEU LEU D . n 
D 1 534 ASN 534 534 534 ASN ASN D . n 
D 1 535 GLY 535 535 535 GLY GLY D . n 
D 1 536 ASN 536 536 536 ASN ASN D . n 
D 1 537 ARG 537 537 537 ARG ARG D . n 
D 1 538 LEU 538 538 538 LEU LEU D . n 
D 1 539 SER 539 539 539 SER SER D . n 
D 1 540 GLY 540 540 540 GLY GLY D . n 
D 1 541 LYS 541 541 541 LYS LYS D . n 
D 1 542 ILE 542 542 542 ILE ILE D . n 
D 1 543 PRO 543 543 543 PRO PRO D . n 
D 1 544 SER 544 544 544 SER SER D . n 
D 1 545 GLY 545 545 545 GLY GLY D . n 
D 1 546 ILE 546 546 546 ILE ILE D . n 
D 1 547 ARG 547 547 547 ARG ARG D . n 
D 1 548 LEU 548 548 548 LEU LEU D . n 
D 1 549 LEU 549 549 549 LEU LEU D . n 
D 1 550 THR 550 550 550 THR THR D . n 
D 1 551 ASN 551 551 551 ASN ASN D . n 
D 1 552 LEU 552 552 552 LEU LEU D . n 
D 1 553 GLU 553 553 553 GLU GLU D . n 
D 1 554 TYR 554 554 554 TYR TYR D . n 
D 1 555 LEU 555 555 555 LEU LEU D . n 
D 1 556 ASP 556 556 556 ASP ASP D . n 
D 1 557 LEU 557 557 557 LEU LEU D . n 
D 1 558 SER 558 558 558 SER SER D . n 
D 1 559 SER 559 559 559 SER SER D . n 
D 1 560 ASN 560 560 560 ASN ASN D . n 
D 1 561 ARG 561 561 561 ARG ARG D . n 
D 1 562 PHE 562 562 562 PHE PHE D . n 
D 1 563 SER 563 563 563 SER SER D . n 
D 1 564 PHE 564 564 564 PHE PHE D . n 
D 1 565 GLU 565 565 565 GLU GLU D . n 
D 1 566 ILE 566 566 566 ILE ILE D . n 
D 1 567 PRO 567 567 567 PRO PRO D . n 
D 1 568 PRO 568 568 568 PRO PRO D . n 
D 1 569 THR 569 569 569 THR THR D . n 
D 1 570 LEU 570 570 570 LEU LEU D . n 
D 1 571 ASN 571 571 571 ASN ASN D . n 
D 1 572 ASN 572 572 572 ASN ASN D . n 
D 1 573 LEU 573 573 573 LEU LEU D . n 
D 1 574 PRO 574 574 574 PRO PRO D . n 
D 1 575 ARG 575 575 575 ARG ARG D . n 
D 1 576 LEU 576 576 576 LEU LEU D . n 
D 1 577 TYR 577 577 577 TYR TYR D . n 
D 1 578 TYR 578 578 578 TYR TYR D . n 
D 1 579 MET 579 579 579 MET MET D . n 
D 1 580 ASN 580 580 580 ASN ASN D . n 
D 1 581 LEU 581 581 581 LEU LEU D . n 
D 1 582 SER 582 582 582 SER SER D . n 
D 1 583 ARG 583 583 583 ARG ARG D . n 
D 1 584 ASN 584 584 584 ASN ASN D . n 
D 1 585 ASP 585 585 585 ASP ASP D . n 
D 1 586 LEU 586 586 586 LEU LEU D . n 
D 1 587 ASP 587 587 587 ASP ASP D . n 
D 1 588 GLN 588 588 588 GLN GLN D . n 
D 1 589 THR 589 589 589 THR THR D . n 
D 1 590 ILE 590 590 590 ILE ILE D . n 
D 1 591 PRO 591 591 591 PRO PRO D . n 
D 1 592 GLU 592 592 592 GLU GLU D . n 
D 1 593 GLY 593 593 593 GLY GLY D . n 
D 1 594 LEU 594 594 594 LEU LEU D . n 
D 1 595 THR 595 595 595 THR THR D . n 
D 1 596 LYS 596 596 596 LYS LYS D . n 
D 1 597 LEU 597 597 597 LEU LEU D . n 
D 1 598 SER 598 598 598 SER SER D . n 
D 1 599 GLN 599 599 599 GLN GLN D . n 
D 1 600 LEU 600 600 600 LEU LEU D . n 
D 1 601 GLN 601 601 601 GLN GLN D . n 
D 1 602 MET 602 602 602 MET MET D . n 
D 1 603 LEU 603 603 603 LEU LEU D . n 
D 1 604 ASP 604 604 604 ASP ASP D . n 
D 1 605 LEU 605 605 605 LEU LEU D . n 
D 1 606 SER 606 606 606 SER SER D . n 
D 1 607 TYR 607 607 607 TYR TYR D . n 
D 1 608 ASN 608 608 608 ASN ASN D . n 
D 1 609 GLN 609 609 609 GLN GLN D . n 
D 1 610 LEU 610 610 610 LEU LEU D . n 
D 1 611 ASP 611 611 611 ASP ASP D . n 
D 1 612 GLY 612 612 612 GLY GLY D . n 
D 1 613 GLU 613 613 613 GLU GLU D . n 
D 1 614 ILE 614 614 614 ILE ILE D . n 
D 1 615 SER 615 615 615 SER SER D . n 
D 1 616 SER 616 616 616 SER SER D . n 
D 1 617 GLN 617 617 617 GLN GLN D . n 
D 1 618 PHE 618 618 618 PHE PHE D . n 
D 1 619 ARG 619 619 619 ARG ARG D . n 
D 1 620 SER 620 620 620 SER SER D . n 
D 1 621 LEU 621 621 621 LEU LEU D . n 
D 1 622 GLN 622 622 622 GLN GLN D . n 
D 1 623 ASN 623 623 623 ASN ASN D . n 
D 1 624 LEU 624 624 624 LEU LEU D . n 
D 1 625 GLU 625 625 625 GLU GLU D . n 
D 1 626 ARG 626 626 626 ARG ARG D . n 
D 1 627 LEU 627 627 627 LEU LEU D . n 
D 1 628 ASP 628 628 628 ASP ASP D . n 
D 1 629 LEU 629 629 629 LEU LEU D . n 
D 1 630 SER 630 630 630 SER SER D . n 
D 1 631 HIS 631 631 631 HIS HIS D . n 
D 1 632 ASN 632 632 632 ASN ASN D . n 
D 1 633 ASN 633 633 633 ASN ASN D . n 
D 1 634 LEU 634 634 634 LEU LEU D . n 
D 1 635 SER 635 635 635 SER SER D . n 
D 1 636 GLY 636 636 636 GLY GLY D . n 
D 1 637 GLN 637 637 637 GLN GLN D . n 
D 1 638 ILE 638 638 638 ILE ILE D . n 
D 1 639 PRO 639 639 639 PRO PRO D . n 
D 1 640 PRO 640 640 640 PRO PRO D . n 
D 1 641 SER 641 641 641 SER SER D . n 
D 1 642 PHE 642 642 642 PHE PHE D . n 
D 1 643 LYS 643 643 643 LYS LYS D . n 
D 1 644 ASP 644 644 644 ASP ASP D . n 
D 1 645 MET 645 645 645 MET MET D . n 
D 1 646 LEU 646 646 646 LEU LEU D . n 
D 1 647 ALA 647 647 647 ALA ALA D . n 
D 1 648 LEU 648 648 648 LEU LEU D . n 
D 1 649 THR 649 649 649 THR THR D . n 
D 1 650 HIS 650 650 650 HIS HIS D . n 
D 1 651 VAL 651 651 651 VAL VAL D . n 
D 1 652 ASP 652 652 652 ASP ASP D . n 
D 1 653 VAL 653 653 653 VAL VAL D . n 
D 1 654 SER 654 654 654 SER SER D . n 
D 1 655 HIS 655 655 655 HIS HIS D . n 
D 1 656 ASN 656 656 656 ASN ASN D . n 
D 1 657 ASN 657 657 657 ASN ASN D . n 
D 1 658 LEU 658 658 658 LEU LEU D . n 
D 1 659 GLN 659 659 659 GLN GLN D . n 
D 1 660 GLY 660 660 660 GLY GLY D . n 
D 1 661 PRO 661 661 661 PRO PRO D . n 
D 1 662 ILE 662 662 662 ILE ILE D . n 
D 1 663 PRO 663 663 663 PRO PRO D . n 
D 1 664 ASP 664 664 664 ASP ASP D . n 
D 1 665 ASN 665 665 665 ASN ASN D . n 
D 1 666 ALA 666 666 666 ALA ALA D . n 
D 1 667 ALA 667 667 667 ALA ALA D . n 
D 1 668 PHE 668 668 668 PHE PHE D . n 
D 1 669 ARG 669 669 669 ARG ARG D . n 
D 1 670 ASN 670 670 670 ASN ASN D . n 
D 1 671 ALA 671 671 671 ALA ALA D . n 
D 1 672 PRO 672 672 672 PRO PRO D . n 
D 1 673 PRO 673 673 673 PRO PRO D . n 
D 1 674 ASP 674 674 674 ASP ASP D . n 
D 1 675 ALA 675 675 675 ALA ALA D . n 
D 1 676 PHE 676 676 676 PHE PHE D . n 
D 1 677 GLU 677 677 677 GLU GLU D . n 
D 1 678 GLY 678 678 678 GLY GLY D . n 
D 1 679 ASN 679 679 679 ASN ASN D . n 
D 1 680 LYS 680 680 680 LYS LYS D . n 
D 1 681 ASP 681 681 681 ASP ASP D . n 
D 1 682 LEU 682 682 682 LEU LEU D . n 
D 1 683 CYS 683 683 683 CYS CYS D . n 
E 2 1   MET 1   1   ?   ?   ?   E . n 
E 2 2   GLU 2   2   ?   ?   ?   E . n 
E 2 3   ARG 3   3   ?   ?   ?   E . n 
E 2 4   ARG 4   4   ?   ?   ?   E . n 
E 2 5   LEU 5   5   ?   ?   ?   E . n 
E 2 6   MET 6   6   ?   ?   ?   E . n 
E 2 7   ILE 7   7   ?   ?   ?   E . n 
E 2 8   PRO 8   8   ?   ?   ?   E . n 
E 2 9   CYS 9   9   ?   ?   ?   E . n 
E 2 10  PHE 10  10  ?   ?   ?   E . n 
E 2 11  PHE 11  11  ?   ?   ?   E . n 
E 2 12  TRP 12  12  ?   ?   ?   E . n 
E 2 13  LEU 13  13  ?   ?   ?   E . n 
E 2 14  ILE 14  14  ?   ?   ?   E . n 
E 2 15  LEU 15  15  ?   ?   ?   E . n 
E 2 16  VAL 16  16  ?   ?   ?   E . n 
E 2 17  LEU 17  17  ?   ?   ?   E . n 
E 2 18  ASP 18  18  ?   ?   ?   E . n 
E 2 19  LEU 19  19  ?   ?   ?   E . n 
E 2 20  VAL 20  20  ?   ?   ?   E . n 
E 2 21  LEU 21  21  ?   ?   ?   E . n 
E 2 22  ARG 22  22  ?   ?   ?   E . n 
E 2 23  VAL 23  23  ?   ?   ?   E . n 
E 2 24  SER 24  24  ?   ?   ?   E . n 
E 2 25  GLY 25  25  ?   ?   ?   E . n 
E 2 26  ASN 26  26  26  ASN ASN E . n 
E 2 27  ALA 27  27  27  ALA ALA E . n 
E 2 28  GLU 28  28  28  GLU GLU E . n 
E 2 29  GLY 29  29  29  GLY GLY E . n 
E 2 30  ASP 30  30  30  ASP ASP E . n 
E 2 31  ALA 31  31  31  ALA ALA E . n 
E 2 32  LEU 32  32  32  LEU LEU E . n 
E 2 33  SER 33  33  33  SER SER E . n 
E 2 34  ALA 34  34  34  ALA ALA E . n 
E 2 35  LEU 35  35  35  LEU LEU E . n 
E 2 36  LYS 36  36  36  LYS LYS E . n 
E 2 37  ASN 37  37  37  ASN ASN E . n 
E 2 38  SER 38  38  38  SER SER E . n 
E 2 39  LEU 39  39  39  LEU LEU E . n 
E 2 40  ALA 40  40  40  ALA ALA E . n 
E 2 41  ASP 41  41  41  ASP ASP E . n 
E 2 42  PRO 42  42  42  PRO PRO E . n 
E 2 43  ASN 43  43  43  ASN ASN E . n 
E 2 44  LYS 44  44  44  LYS LYS E . n 
E 2 45  VAL 45  45  45  VAL VAL E . n 
E 2 46  LEU 46  46  46  LEU LEU E . n 
E 2 47  GLN 47  47  47  GLN GLN E . n 
E 2 48  SER 48  48  48  SER SER E . n 
E 2 49  TRP 49  49  49  TRP TRP E . n 
E 2 50  ASP 50  50  50  ASP ASP E . n 
E 2 51  ALA 51  51  51  ALA ALA E . n 
E 2 52  THR 52  52  52  THR THR E . n 
E 2 53  LEU 53  53  53  LEU LEU E . n 
E 2 54  VAL 54  54  54  VAL VAL E . n 
E 2 55  THR 55  55  55  THR THR E . n 
E 2 56  PRO 56  56  56  PRO PRO E . n 
E 2 57  CYS 57  57  57  CYS CYS E . n 
E 2 58  THR 58  58  58  THR THR E . n 
E 2 59  TRP 59  59  59  TRP TRP E . n 
E 2 60  PHE 60  60  60  PHE PHE E . n 
E 2 61  HIS 61  61  61  HIS HIS E . n 
E 2 62  VAL 62  62  62  VAL VAL E . n 
E 2 63  THR 63  63  63  THR THR E . n 
E 2 64  CYS 64  64  64  CYS CYS E . n 
E 2 65  ASN 65  65  65  ASN ASN E . n 
E 2 66  SER 66  66  66  SER SER E . n 
E 2 67  ASP 67  67  67  ASP ASP E . n 
E 2 68  ASN 68  68  68  ASN ASN E . n 
E 2 69  SER 69  69  69  SER SER E . n 
E 2 70  VAL 70  70  70  VAL VAL E . n 
E 2 71  THR 71  71  71  THR THR E . n 
E 2 72  ARG 72  72  72  ARG ARG E . n 
E 2 73  VAL 73  73  73  VAL VAL E . n 
E 2 74  ASP 74  74  74  ASP ASP E . n 
E 2 75  LEU 75  75  75  LEU LEU E . n 
E 2 76  GLY 76  76  76  GLY GLY E . n 
E 2 77  ASN 77  77  77  ASN ASN E . n 
E 2 78  ALA 78  78  78  ALA ALA E . n 
E 2 79  ASN 79  79  79  ASN ASN E . n 
E 2 80  LEU 80  80  80  LEU LEU E . n 
E 2 81  SER 81  81  81  SER SER E . n 
E 2 82  GLY 82  82  82  GLY GLY E . n 
E 2 83  GLN 83  83  83  GLN GLN E . n 
E 2 84  LEU 84  84  84  LEU LEU E . n 
E 2 85  VAL 85  85  85  VAL VAL E . n 
E 2 86  MET 86  86  86  MET MET E . n 
E 2 87  GLN 87  87  87  GLN GLN E . n 
E 2 88  LEU 88  88  88  LEU LEU E . n 
E 2 89  GLY 89  89  89  GLY GLY E . n 
E 2 90  GLN 90  90  90  GLN GLN E . n 
E 2 91  LEU 91  91  91  LEU LEU E . n 
E 2 92  PRO 92  92  92  PRO PRO E . n 
E 2 93  ASN 93  93  93  ASN ASN E . n 
E 2 94  LEU 94  94  94  LEU LEU E . n 
E 2 95  GLN 95  95  95  GLN GLN E . n 
E 2 96  TYR 96  96  96  TYR TYR E . n 
E 2 97  LEU 97  97  97  LEU LEU E . n 
E 2 98  GLU 98  98  98  GLU GLU E . n 
E 2 99  LEU 99  99  99  LEU LEU E . n 
E 2 100 TYR 100 100 100 TYR TYR E . n 
E 2 101 SER 101 101 101 SER SER E . n 
E 2 102 ASN 102 102 102 ASN ASN E . n 
E 2 103 ASN 103 103 103 ASN ASN E . n 
E 2 104 ILE 104 104 104 ILE ILE E . n 
E 2 105 THR 105 105 105 THR THR E . n 
E 2 106 GLY 106 106 106 GLY GLY E . n 
E 2 107 THR 107 107 107 THR THR E . n 
E 2 108 ILE 108 108 108 ILE ILE E . n 
E 2 109 PRO 109 109 109 PRO PRO E . n 
E 2 110 GLU 110 110 110 GLU GLU E . n 
E 2 111 GLN 111 111 111 GLN GLN E . n 
E 2 112 LEU 112 112 112 LEU LEU E . n 
E 2 113 GLY 113 113 113 GLY GLY E . n 
E 2 114 ASN 114 114 114 ASN ASN E . n 
E 2 115 LEU 115 115 115 LEU LEU E . n 
E 2 116 THR 116 116 116 THR THR E . n 
E 2 117 GLU 117 117 117 GLU GLU E . n 
E 2 118 LEU 118 118 118 LEU LEU E . n 
E 2 119 VAL 119 119 119 VAL VAL E . n 
E 2 120 SER 120 120 120 SER SER E . n 
E 2 121 LEU 121 121 121 LEU LEU E . n 
E 2 122 ASP 122 122 122 ASP ASP E . n 
E 2 123 LEU 123 123 123 LEU LEU E . n 
E 2 124 TYR 124 124 124 TYR TYR E . n 
E 2 125 LEU 125 125 125 LEU LEU E . n 
E 2 126 ASN 126 126 126 ASN ASN E . n 
E 2 127 ASN 127 127 127 ASN ASN E . n 
E 2 128 LEU 128 128 128 LEU LEU E . n 
E 2 129 SER 129 129 129 SER SER E . n 
E 2 130 GLY 130 130 130 GLY GLY E . n 
E 2 131 PRO 131 131 131 PRO PRO E . n 
E 2 132 ILE 132 132 132 ILE ILE E . n 
E 2 133 PRO 133 133 133 PRO PRO E . n 
E 2 134 SER 134 134 134 SER SER E . n 
E 2 135 THR 135 135 135 THR THR E . n 
E 2 136 LEU 136 136 136 LEU LEU E . n 
E 2 137 GLY 137 137 137 GLY GLY E . n 
E 2 138 ARG 138 138 138 ARG ARG E . n 
E 2 139 LEU 139 139 139 LEU LEU E . n 
E 2 140 LYS 140 140 140 LYS LYS E . n 
E 2 141 LYS 141 141 141 LYS LYS E . n 
E 2 142 LEU 142 142 142 LEU LEU E . n 
E 2 143 ARG 143 143 143 ARG ARG E . n 
E 2 144 PHE 144 144 144 PHE PHE E . n 
E 2 145 LEU 145 145 145 LEU LEU E . n 
E 2 146 ARG 146 146 146 ARG ARG E . n 
E 2 147 LEU 147 147 147 LEU LEU E . n 
E 2 148 ASN 148 148 148 ASN ASN E . n 
E 2 149 ASN 149 149 149 ASN ASN E . n 
E 2 150 ASN 150 150 150 ASN ASN E . n 
E 2 151 SER 151 151 151 SER SER E . n 
E 2 152 LEU 152 152 152 LEU LEU E . n 
E 2 153 SER 153 153 153 SER SER E . n 
E 2 154 GLY 154 154 154 GLY GLY E . n 
E 2 155 GLU 155 155 155 GLU GLU E . n 
E 2 156 ILE 156 156 156 ILE ILE E . n 
E 2 157 PRO 157 157 157 PRO PRO E . n 
E 2 158 ARG 158 158 158 ARG ARG E . n 
E 2 159 SER 159 159 159 SER SER E . n 
E 2 160 LEU 160 160 160 LEU LEU E . n 
E 2 161 THR 161 161 161 THR THR E . n 
E 2 162 ALA 162 162 162 ALA ALA E . n 
E 2 163 VAL 163 163 163 VAL VAL E . n 
E 2 164 LEU 164 164 164 LEU LEU E . n 
E 2 165 THR 165 165 165 THR THR E . n 
E 2 166 LEU 166 166 166 LEU LEU E . n 
E 2 167 GLN 167 167 167 GLN GLN E . n 
E 2 168 VAL 168 168 168 VAL VAL E . n 
E 2 169 LEU 169 169 169 LEU LEU E . n 
E 2 170 ASP 170 170 170 ASP ASP E . n 
E 2 171 LEU 171 171 171 LEU LEU E . n 
E 2 172 SER 172 172 172 SER SER E . n 
E 2 173 ASN 173 173 173 ASN ASN E . n 
E 2 174 ASN 174 174 174 ASN ASN E . n 
E 2 175 PRO 175 175 175 PRO PRO E . n 
E 2 176 LEU 176 176 176 LEU LEU E . n 
E 2 177 THR 177 177 177 THR THR E . n 
E 2 178 GLY 178 178 178 GLY GLY E . n 
E 2 179 ASP 179 179 179 ASP ASP E . n 
E 2 180 ILE 180 180 180 ILE ILE E . n 
E 2 181 PRO 181 181 181 PRO PRO E . n 
E 2 182 VAL 182 182 182 VAL VAL E . n 
E 2 183 ASN 183 183 183 ASN ASN E . n 
E 2 184 GLY 184 184 184 GLY GLY E . n 
E 2 185 SER 185 185 185 SER SER E . n 
E 2 186 PHE 186 186 186 PHE PHE E . n 
E 2 187 SER 187 187 187 SER SER E . n 
E 2 188 LEU 188 188 188 LEU LEU E . n 
E 2 189 PHE 189 189 189 PHE PHE E . n 
E 2 190 THR 190 190 190 THR THR E . n 
E 2 191 PRO 191 191 191 PRO PRO E . n 
E 2 192 ILE 192 192 192 ILE ILE E . n 
E 2 193 SER 193 193 193 SER SER E . n 
E 2 194 PHE 194 194 194 PHE PHE E . n 
E 2 195 ALA 195 195 195 ALA ALA E . n 
E 2 196 ASN 196 196 196 ASN ASN E . n 
E 2 197 THR 197 197 197 THR THR E . n 
E 2 198 LYS 198 198 198 LYS LYS E . n 
E 2 199 LEU 199 199 199 LEU LEU E . n 
E 2 200 THR 200 200 ?   ?   ?   E . n 
E 2 201 PRO 201 201 ?   ?   ?   E . n 
E 2 202 LEU 202 202 ?   ?   ?   E . n 
E 2 203 PRO 203 203 ?   ?   ?   E . n 
E 2 204 ALA 204 204 ?   ?   ?   E . n 
E 2 205 SER 205 205 ?   ?   ?   E . n 
E 2 206 PRO 206 206 ?   ?   ?   E . n 
E 2 207 PRO 207 207 ?   ?   ?   E . n 
E 2 208 PRO 208 208 ?   ?   ?   E . n 
E 2 209 PRO 209 209 ?   ?   ?   E . n 
E 2 210 ILE 210 210 ?   ?   ?   E . n 
E 2 211 SER 211 211 ?   ?   ?   E . n 
E 2 212 PRO 212 212 ?   ?   ?   E . n 
E 2 213 THR 213 213 ?   ?   ?   E . n 
E 2 214 PRO 214 214 ?   ?   ?   E . n 
E 2 215 PRO 215 215 ?   ?   ?   E . n 
E 2 216 SER 216 216 ?   ?   ?   E . n 
E 2 217 PRO 217 217 ?   ?   ?   E . n 
E 2 218 ALA 218 218 ?   ?   ?   E . n 
E 2 219 GLY 219 219 ?   ?   ?   E . n 
E 2 220 SER 220 220 ?   ?   ?   E . n 
E 2 221 HIS 221 221 ?   ?   ?   E . n 
E 2 222 HIS 222 222 ?   ?   ?   E . n 
E 2 223 HIS 223 223 ?   ?   ?   E . n 
E 2 224 HIS 224 224 ?   ?   ?   E . n 
E 2 225 HIS 225 225 ?   ?   ?   E . n 
E 2 226 HIS 226 226 ?   ?   ?   E . n 
E 2 227 HIS 227 227 ?   ?   ?   E . n 
E 2 228 HIS 228 228 ?   ?   ?   E . n 
E 2 229 HIS 229 229 ?   ?   ?   E . n 
E 2 230 HIS 230 230 ?   ?   ?   E . n 
F 3 1   GLU 1   1   1   GLU GLU F . n 
F 3 2   SER 2   2   2   SER SER F . n 
F 3 3   SER 3   3   3   SER SER F . n 
F 3 4   SER 4   4   4   SER SER F . n 
F 3 5   SER 5   5   5   SER SER F . n 
F 3 6   HIS 6   6   6   HIS HIS F . n 
F 3 7   SER 7   7   7   SER SER F . n 
F 3 8   GLU 8   8   8   GLU GLU F . n 
F 3 9   ARG 9   9   9   ARG ARG F . n 
F 3 10  ALA 10  10  10  ALA ALA F . n 
F 3 11  GLY 11  11  11  GLY GLY F . n 
F 3 12  GLY 12  12  12  GLY GLY F . n 
F 3 13  ARG 13  13  13  ARG ARG F . 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 
G 4 NAG 1 G NAG 1 G NAG 1 n 
G 4 FUC 2 G FUC 2 G FUC 2 n 
G 4 NAG 3 G NAG 3 G NAG 3 n 
G 4 FUC 4 G FUC 4 G FUC 4 n 
H 5 NAG 1 H NAG 1 H NAG 1 n 
H 5 NAG 2 H NAG 2 H NAG 2 n 
I 5 NAG 1 I NAG 1 I NAG 1 n 
I 5 NAG 2 I NAG 2 I NAG 2 n 
J 5 NAG 1 J NAG 1 J NAG 1 n 
J 5 NAG 2 J NAG 2 J NAG 2 n 
K 5 NAG 1 K NAG 1 K NAG 1 n 
K 5 NAG 2 K NAG 2 K NAG 2 n 
L 6 NAG 1 L NAG 1 L NAG 1 n 
L 6 NAG 2 L NAG 2 L NAG 2 n 
L 6 FUC 3 L FUC 3 L FUC 3 n 
M 7 NAG 1 M NAG 1 M NAG 1 n 
M 7 NAG 2 M NAG 2 M NAG 2 n 
M 7 BMA 3 M BMA 3 M BMA 3 n 
N 7 NAG 1 N NAG 1 N NAG 1 n 
N 7 NAG 2 N NAG 2 N NAG 2 n 
N 7 BMA 3 N BMA 3 N BMA 3 n 
O 8 NAG 1 O NAG 1 O NAG 1 n 
O 8 NAG 2 O NAG 2 O NAG 2 n 
O 8 BMA 3 O BMA 3 O BMA 3 n 
O 8 FUC 4 O FUC 4 O FUC 4 n 
P 5 NAG 1 P NAG 1 P NAG 1 n 
P 5 NAG 2 P NAG 2 P NAG 2 n 
Q 5 NAG 1 Q NAG 1 Q NAG 1 n 
Q 5 NAG 2 Q NAG 2 Q NAG 2 n 
R 5 NAG 1 R NAG 1 R NAG 1 n 
R 5 NAG 2 R NAG 2 R NAG 2 n 
S 9 NAG 1 S NAG 1 S NAG 1 n 
S 9 FUC 2 S FUC 2 S FUC 2 n 
T 9 NAG 1 T NAG 1 T NAG 1 n 
T 9 FUC 2 T FUC 2 T FUC 2 n 
U 5 NAG 1 U NAG 1 U NAG 1 n 
U 5 NAG 2 U NAG 2 U NAG 2 n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 BMA ? ? BMA ? ? 'SUBJECT OF INVESTIGATION' ? 
2 NAG ? ? NAG ? ? 'SUBJECT OF INVESTIGATION' ? 
3 FUC ? ? FUC ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
V  10 NAG 1 1601 1601 NAG NAG A . 
W  10 NAG 1 1602 1701 NAG NAG A . 
X  10 NAG 1 1603 1801 NAG NAG A . 
Y  10 NAG 1 1401 1401 NAG NAG D . 
Z  10 NAG 1 1402 1501 NAG NAG D . 
AA 10 NAG 1 1403 1601 NAG NAG D . 
BA 10 NAG 1 1404 1701 NAG NAG D . 
CA 10 NAG 1 1405 2001 NAG NAG D . 
DA 10 NAG 1 1406 2101 NAG NAG D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.11 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8WED 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     72.674 
_cell.length_a_esd                 ? 
_cell.length_b                     178.123 
_cell.length_b_esd                 ? 
_cell.length_c                     142.263 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8WED 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 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                   8WED 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             4.33 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          71.62 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              5.9 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 M MES pH 5.9, 22% PEG200, 7% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'PSI PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-10 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97853 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8WED 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.3 
_reflns.d_resolution_low                               50 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     54443 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.988 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.3 
_reflns_shell.d_res_low                                     3.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1888 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.54 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8WED 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.30 
_refine.ls_d_res_low                             36.34 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     48401 
_refine.ls_number_reflns_R_free                  2371 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.87 
_refine.ls_percent_reflns_R_free                 4.90 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2415 
_refine.ls_R_factor_R_free                       0.2612 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2405 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.25 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.36 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.30 
_refine_hist.d_res_low                        36.34 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               13354 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        12743 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         611 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.003  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.625  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.450 ? 5122 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050  ? 2296 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013  ? 2356 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.30 3.36  . . 39  815  27.00  . . . . 0.3501 . . . . . . . . . . . 0.4276 
'X-RAY DIFFRACTION' 3.36 3.44  . . 69  1442 47.00  . . . . 0.3180 . . . . . . . . . . . 0.3293 
'X-RAY DIFFRACTION' 3.44 3.52  . . 97  2017 66.00  . . . . 0.3005 . . . . . . . . . . . 0.3600 
'X-RAY DIFFRACTION' 3.52 3.61  . . 117 2470 81.00  . . . . 0.2882 . . . . . . . . . . . 0.3201 
'X-RAY DIFFRACTION' 3.61 3.70  . . 158 2807 93.00  . . . . 0.2881 . . . . . . . . . . . 0.3197 
'X-RAY DIFFRACTION' 3.70 3.81  . . 150 3041 99.00  . . . . 0.2626 . . . . . . . . . . . 0.2723 
'X-RAY DIFFRACTION' 3.81 3.93  . . 147 3002 100.00 . . . . 0.2449 . . . . . . . . . . . 0.2461 
'X-RAY DIFFRACTION' 3.93 4.07  . . 148 3074 100.00 . . . . 0.2389 . . . . . . . . . . . 0.2455 
'X-RAY DIFFRACTION' 4.08 4.24  . . 128 3040 100.00 . . . . 0.2243 . . . . . . . . . . . 0.2272 
'X-RAY DIFFRACTION' 4.24 4.43  . . 160 3042 100.00 . . . . 0.2155 . . . . . . . . . . . 0.2164 
'X-RAY DIFFRACTION' 4.43 4.66  . . 160 3031 100.00 . . . . 0.2082 . . . . . . . . . . . 0.2013 
'X-RAY DIFFRACTION' 4.66 4.96  . . 191 3014 100.00 . . . . 0.2170 . . . . . . . . . . . 0.2479 
'X-RAY DIFFRACTION' 4.96 5.34  . . 134 3096 100.00 . . . . 0.2229 . . . . . . . . . . . 0.2037 
'X-RAY DIFFRACTION' 5.34 5.87  . . 180 3006 100.00 . . . . 0.2521 . . . . . . . . . . . 0.3011 
'X-RAY DIFFRACTION' 5.87 6.72  . . 154 3069 100.00 . . . . 0.2238 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 6.72 8.44  . . 170 3051 100.00 . . . . 0.2483 . . . . . . . . . . . 0.2517 
'X-RAY DIFFRACTION' 8.45 36.34 . . 169 3013 97.00  . . . . 0.2172 . . . . . . . . . . . 0.2871 
# 
_struct.entry_id                     8WED 
_struct.title                        
'Crystal structure of Arabidopsis thaliana MIK2 ectodomain in complex with BAK1 ectodomain and Fusarium oxysporum SCOOPL' 
_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        8WED 
_struct_keywords.text            'LRR receptor-like serine/threonine-protein kinase, PLANT PROTEIN' 
_struct_keywords.pdbx_keywords   'PLANT 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 1  ? 
E  N N 2  ? 
F  N N 3  ? 
G  N N 4  ? 
H  N N 5  ? 
I  N N 5  ? 
J  N N 5  ? 
K  N N 5  ? 
L  N N 6  ? 
M  N N 7  ? 
N  N N 7  ? 
O  N N 8  ? 
P  N N 5  ? 
Q  N N 5  ? 
R  N N 5  ? 
S  N N 9  ? 
T  N N 9  ? 
U  N N 5  ? 
V  N N 10 ? 
W  N N 10 ? 
X  N N 10 ? 
Y  N N 10 ? 
Z  N N 10 ? 
AA N N 10 ? 
BA N N 10 ? 
CA N N 10 ? 
DA N N 10 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP MIK2_ARATH Q8VZG8 ? 1 
;MNKTNPERKISLTSFKERMACKEKPRDLQVLLIISIVLSCSFAVSATVEEANALLKWKSTFTNQTSSSKLSSWVNPNTSS
FCTSWYGVACSLGSIIRLNLTNTGIEGTFEDFPFSSLPNLTFVDLSMNRFSGTISPLWGRFSKLEYFDLSINQLVGEIPP
ELGDLSNLDTLHLVENKLNGSIPSEIGRLTKVTEIAIYDNLLTGPIPSSFGNLTKLVNLYLFINSLSGSIPSEIGNLPNL
RELCLDRNNLTGKIPSSFGNLKNVTLLNMFENQLSGEIPPEIGNMTALDTLSLHTNKLTGPIPSTLGNIKTLAVLHLYLN
QLNGSIPPELGEMESMIDLEISENKLTGPVPDSFGKLTALEWLFLRDNQLSGPIPPGIANSTELTVLQLDTNNFTGFLPD
TICRGGKLENLTLDDNHFEGPVPKSLRDCKSLIRVRFKGNSFSGDISEAFGVYPTLNFIDLSNNNFHGQLSANWEQSQKL
VAFILSNNSITGAIPPEIWNMTQLSQLDLSSNRITGELPESISNINRISKLQLNGNRLSGKIPSGIRLLTNLEYLDLSSN
RFSSEIPPTLNNLPRLYYMNLSRNDLDQTIPEGLTKLSQLQMLDLSYNQLDGEISSQFRSLQNLERLDLSHNNLSGQIPP
SFKDMLALTHVDVSHNNLQGPIPDNAAFRNAPPDAFEGNKDLC
;
1 
2 UNP BAK1_ARATH Q94F62 ? 2 
;MERRLMIPCFFWLILVLDLVLRVSGNAEGDALSALKNSLADPNKVLQSWDATLVTPCTWFHVTCNSDNSVTRVDLGNANL
SGQLVMQLGQLPNLQYLELYSNNITGTIPEQLGNLTELVSLDLYLNNLSGPIPSTLGRLKKLRFLRLNNNSLSGEIPRSL
TAVLTLQVLDLSNNPLTGDIPVNGSFSLFTPISFANTKLTPLPASPPPPISPTPPSPAGS
;
1 
3 PDB 8WED       8WED   ? 3 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8WED A 1 ? 683 ? Q8VZG8 1 ? 683 ? 1 683 
2 2 8WED B 1 ? 220 ? Q94F62 1 ? 220 ? 1 220 
3 3 8WED C 1 ? 13  ? 8WED   1 ? 13  ? 1 13  
4 1 8WED D 1 ? 683 ? Q8VZG8 1 ? 683 ? 1 683 
5 2 8WED E 1 ? 220 ? Q94F62 1 ? 220 ? 1 220 
6 3 8WED F 1 ? 13  ? 8WED   1 ? 13  ? 1 13  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8WED GLU A 137 ? UNP Q8VZG8 LEU 137 'engineered mutation' 137 1  
1 8WED LYS A 164 ? UNP Q8VZG8 ASP 164 'engineered mutation' 164 2  
1 8WED PHE A 564 ? UNP Q8VZG8 SER 564 'engineered mutation' 564 3  
2 8WED HIS B 221 ? UNP Q94F62 ?   ?   'expression tag'      221 4  
2 8WED HIS B 222 ? UNP Q94F62 ?   ?   'expression tag'      222 5  
2 8WED HIS B 223 ? UNP Q94F62 ?   ?   'expression tag'      223 6  
2 8WED HIS B 224 ? UNP Q94F62 ?   ?   'expression tag'      224 7  
2 8WED HIS B 225 ? UNP Q94F62 ?   ?   'expression tag'      225 8  
2 8WED HIS B 226 ? UNP Q94F62 ?   ?   'expression tag'      226 9  
2 8WED HIS B 227 ? UNP Q94F62 ?   ?   'expression tag'      227 10 
2 8WED HIS B 228 ? UNP Q94F62 ?   ?   'expression tag'      228 11 
2 8WED HIS B 229 ? UNP Q94F62 ?   ?   'expression tag'      229 12 
2 8WED HIS B 230 ? UNP Q94F62 ?   ?   'expression tag'      230 13 
4 8WED GLU D 137 ? UNP Q8VZG8 LEU 137 'engineered mutation' 137 14 
4 8WED LYS D 164 ? UNP Q8VZG8 ASP 164 'engineered mutation' 164 15 
4 8WED PHE D 564 ? UNP Q8VZG8 SER 564 'engineered mutation' 564 16 
5 8WED HIS E 221 ? UNP Q94F62 ?   ?   'expression tag'      221 17 
5 8WED HIS E 222 ? UNP Q94F62 ?   ?   'expression tag'      222 18 
5 8WED HIS E 223 ? UNP Q94F62 ?   ?   'expression tag'      223 19 
5 8WED HIS E 224 ? UNP Q94F62 ?   ?   'expression tag'      224 20 
5 8WED HIS E 225 ? UNP Q94F62 ?   ?   'expression tag'      225 21 
5 8WED HIS E 226 ? UNP Q94F62 ?   ?   'expression tag'      226 22 
5 8WED HIS E 227 ? UNP Q94F62 ?   ?   'expression tag'      227 23 
5 8WED HIS E 228 ? UNP Q94F62 ?   ?   'expression tag'      228 24 
5 8WED HIS E 229 ? UNP Q94F62 ?   ?   'expression tag'      229 25 
5 8WED HIS E 230 ? UNP Q94F62 ?   ?   'expression tag'      230 26 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? trimeric 3 
2 author_defined_assembly ? trimeric 3 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,G,H,I,J,K,L,M,V,W,X             
2 1 D,E,F,N,O,P,Q,R,S,T,U,Y,Z,AA,BA,CA,DA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 47  ? PHE A 61  ? THR A 47  PHE A 61  1 ? 15 
HELX_P HELX_P2  AA2 SER A 68  ? TRP A 73  ? SER A 68  TRP A 73  5 ? 6  
HELX_P HELX_P3  AA3 ASN A 77  ? TRP A 85  ? ASN A 77  TRP A 85  1 ? 9  
HELX_P HELX_P4  AA4 SER A 135 ? PHE A 141 ? SER A 135 PHE A 141 5 ? 7  
HELX_P HELX_P5  AA5 PRO A 159 ? LEU A 165 ? PRO A 159 LEU A 165 5 ? 7  
HELX_P HELX_P6  AA6 PRO A 183 ? LEU A 189 ? PRO A 183 LEU A 189 5 ? 7  
HELX_P HELX_P7  AA7 PRO A 207 ? LEU A 213 ? PRO A 207 LEU A 213 5 ? 7  
HELX_P HELX_P8  AA8 PRO A 231 ? LEU A 237 ? PRO A 231 LEU A 237 5 ? 7  
HELX_P HELX_P9  AA9 PRO A 255 ? LEU A 261 ? PRO A 255 LEU A 261 5 ? 7  
HELX_P HELX_P10 AB1 PRO A 279 ? MET A 285 ? PRO A 279 MET A 285 5 ? 7  
HELX_P HELX_P11 AB2 PRO A 303 ? ILE A 309 ? PRO A 303 ILE A 309 5 ? 7  
HELX_P HELX_P12 AB3 PRO A 327 ? MET A 333 ? PRO A 327 MET A 333 5 ? 7  
HELX_P HELX_P13 AB4 PRO A 351 ? LEU A 357 ? PRO A 351 LEU A 357 5 ? 7  
HELX_P HELX_P14 AB5 PRO A 375 ? ASN A 380 ? PRO A 375 ASN A 380 5 ? 6  
HELX_P HELX_P15 AB6 PRO A 423 ? ASP A 428 ? PRO A 423 ASP A 428 1 ? 6  
HELX_P HELX_P16 AB7 ILE A 446 ? PHE A 450 ? ILE A 446 PHE A 450 1 ? 5  
HELX_P HELX_P17 AB8 SER A 471 ? SER A 477 ? SER A 471 SER A 477 5 ? 7  
HELX_P HELX_P18 AB9 PRO A 495 ? MET A 501 ? PRO A 495 MET A 501 5 ? 7  
HELX_P HELX_P19 AC1 PRO A 519 ? ASN A 526 ? PRO A 519 ASN A 526 5 ? 8  
HELX_P HELX_P20 AC2 PRO A 543 ? LEU A 549 ? PRO A 543 LEU A 549 5 ? 7  
HELX_P HELX_P21 AC3 PRO A 591 ? LEU A 597 ? PRO A 591 LEU A 597 5 ? 7  
HELX_P HELX_P22 AC4 SER A 615 ? LEU A 621 ? SER A 615 LEU A 621 5 ? 7  
HELX_P HELX_P23 AC5 PRO A 639 ? MET A 645 ? PRO A 639 MET A 645 5 ? 7  
HELX_P HELX_P24 AC6 ASN A 665 ? ASN A 670 ? ASN A 665 ASN A 670 1 ? 6  
HELX_P HELX_P25 AC7 PRO A 672 ? GLU A 677 ? PRO A 672 GLU A 677 5 ? 6  
HELX_P HELX_P26 AC8 ALA B 27  ? SER B 38  ? ALA B 27  SER B 38  1 ? 12 
HELX_P HELX_P27 AC9 LYS B 44  ? TRP B 49  ? LYS B 44  TRP B 49  5 ? 6  
HELX_P HELX_P28 AD1 THR B 55  ? TRP B 59  ? THR B 55  TRP B 59  5 ? 5  
HELX_P HELX_P29 AD2 VAL B 85  ? LEU B 91  ? VAL B 85  LEU B 91  5 ? 7  
HELX_P HELX_P30 AD3 PRO B 109 ? LEU B 115 ? PRO B 109 LEU B 115 5 ? 7  
HELX_P HELX_P31 AD4 PRO B 133 ? LEU B 139 ? PRO B 133 LEU B 139 5 ? 7  
HELX_P HELX_P32 AD5 PRO B 157 ? VAL B 163 ? PRO B 157 VAL B 163 5 ? 7  
HELX_P HELX_P33 AD6 SER B 185 ? PHE B 189 ? SER B 185 PHE B 189 5 ? 5  
HELX_P HELX_P34 AD7 VAL D 48  ? THR D 60  ? VAL D 48  THR D 60  1 ? 13 
HELX_P HELX_P35 AD8 SER D 68  ? TRP D 73  ? SER D 68  TRP D 73  5 ? 6  
HELX_P HELX_P36 AD9 SER D 80  ? TRP D 85  ? SER D 80  TRP D 85  1 ? 6  
HELX_P HELX_P37 AE1 PRO D 113 ? LEU D 117 ? PRO D 113 LEU D 117 5 ? 5  
HELX_P HELX_P38 AE2 SER D 135 ? PHE D 141 ? SER D 135 PHE D 141 5 ? 7  
HELX_P HELX_P39 AE3 PRO D 159 ? LEU D 165 ? PRO D 159 LEU D 165 5 ? 7  
HELX_P HELX_P40 AE4 PRO D 183 ? LEU D 189 ? PRO D 183 LEU D 189 5 ? 7  
HELX_P HELX_P41 AE5 PRO D 207 ? LEU D 213 ? PRO D 207 LEU D 213 5 ? 7  
HELX_P HELX_P42 AE6 PRO D 231 ? LEU D 237 ? PRO D 231 LEU D 237 5 ? 7  
HELX_P HELX_P43 AE7 PRO D 255 ? LEU D 261 ? PRO D 255 LEU D 261 5 ? 7  
HELX_P HELX_P44 AE8 PRO D 279 ? MET D 285 ? PRO D 279 MET D 285 5 ? 7  
HELX_P HELX_P45 AE9 PRO D 303 ? ILE D 309 ? PRO D 303 ILE D 309 5 ? 7  
HELX_P HELX_P46 AF1 PRO D 327 ? MET D 333 ? PRO D 327 MET D 333 5 ? 7  
HELX_P HELX_P47 AF2 PRO D 351 ? LEU D 357 ? PRO D 351 LEU D 357 5 ? 7  
HELX_P HELX_P48 AF3 PRO D 423 ? ASP D 428 ? PRO D 423 ASP D 428 1 ? 6  
HELX_P HELX_P49 AF4 ILE D 446 ? PHE D 450 ? ILE D 446 PHE D 450 1 ? 5  
HELX_P HELX_P50 AF5 SER D 471 ? SER D 477 ? SER D 471 SER D 477 5 ? 7  
HELX_P HELX_P51 AF6 PRO D 495 ? MET D 501 ? PRO D 495 MET D 501 5 ? 7  
HELX_P HELX_P52 AF7 PRO D 519 ? ASN D 526 ? PRO D 519 ASN D 526 5 ? 8  
HELX_P HELX_P53 AF8 PRO D 543 ? LEU D 549 ? PRO D 543 LEU D 549 5 ? 7  
HELX_P HELX_P54 AF9 PRO D 591 ? LEU D 597 ? PRO D 591 LEU D 597 5 ? 7  
HELX_P HELX_P55 AG1 SER D 615 ? LEU D 621 ? SER D 615 LEU D 621 5 ? 7  
HELX_P HELX_P56 AG2 PRO D 639 ? MET D 645 ? PRO D 639 MET D 645 5 ? 7  
HELX_P HELX_P57 AG3 ASN D 665 ? ASN D 670 ? ASN D 665 ASN D 670 1 ? 6  
HELX_P HELX_P58 AG4 PRO D 672 ? GLU D 677 ? PRO D 672 GLU D 677 5 ? 6  
HELX_P HELX_P59 AG5 ALA E 27  ? SER E 38  ? ALA E 27  SER E 38  1 ? 12 
HELX_P HELX_P60 AG6 LYS E 44  ? TRP E 49  ? LYS E 44  TRP E 49  5 ? 6  
HELX_P HELX_P61 AG7 THR E 55  ? TRP E 59  ? THR E 55  TRP E 59  5 ? 5  
HELX_P HELX_P62 AG8 VAL E 85  ? LEU E 91  ? VAL E 85  LEU E 91  5 ? 7  
HELX_P HELX_P63 AG9 PRO E 109 ? LEU E 115 ? PRO E 109 LEU E 115 5 ? 7  
HELX_P HELX_P64 AH1 PRO E 133 ? LEU E 139 ? PRO E 133 LEU E 139 5 ? 7  
HELX_P HELX_P65 AH2 PRO E 157 ? ALA E 162 ? PRO E 157 ALA E 162 5 ? 6  
HELX_P HELX_P66 AH3 SER E 185 ? PHE E 189 ? SER E 185 PHE E 189 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 82  SG  ? ? ? 1_555 A  CYS 90  SG ? ? A CYS 82  A CYS 90   1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf2  disulf ?    ? A CYS 403 SG  ? ? ? 1_555 A  CYS 429 SG ? ? A CYS 403 A CYS 429  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf3  disulf ?    ? B CYS 57  SG  ? ? ? 1_555 B  CYS 64  SG ? ? B CYS 57  B CYS 64   1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf4  disulf ?    ? D CYS 82  SG  ? ? ? 1_555 D  CYS 90  SG ? ? D CYS 82  D CYS 90   1_555 ? ? ? ? ? ? ? 2.030 ? ? 
disulf5  disulf ?    ? D CYS 403 SG  ? ? ? 1_555 D  CYS 429 SG ? ? D CYS 403 D CYS 429  1_555 ? ? ? ? ? ? ? 2.033 ? ? 
disulf6  disulf ?    ? E CYS 57  SG  ? ? ? 1_555 E  CYS 64  SG ? ? E CYS 57  E CYS 64   1_555 ? ? ? ? ? ? ? 2.030 ? ? 
covale1  covale one  ? A ASN 99  ND2 ? ? ? 1_555 J  NAG .   C1 ? ? A ASN 99  J NAG 1    1_555 ? ? ? ? ? ? ? 1.441 ? 
N-Glycosylation 
covale2  covale one  ? A ASN 119 ND2 ? ? ? 1_555 I  NAG .   C1 ? ? A ASN 119 I NAG 1    1_555 ? ? ? ? ? ? ? 1.440 ? 
N-Glycosylation 
covale3  covale one  ? A ASN 179 ND2 ? ? ? 1_555 G  NAG .   C1 ? ? A ASN 179 G NAG 1    1_555 ? ? ? ? ? ? ? 1.441 ? 
N-Glycosylation 
covale4  covale one  ? A ASN 263 ND2 ? ? ? 1_555 W  NAG .   C1 ? ? A ASN 263 A NAG 1602 1_555 ? ? ? ? ? ? ? 1.438 ? 
N-Glycosylation 
covale5  covale one  ? A ASN 284 ND2 ? ? ? 1_555 X  NAG .   C1 ? ? A ASN 284 A NAG 1603 1_555 ? ? ? ? ? ? ? 1.456 ? 
N-Glycosylation 
covale6  covale one  ? A ASN 380 ND2 ? ? ? 1_555 K  NAG .   C1 ? ? A ASN 380 K NAG 1    1_555 ? ? ? ? ? ? ? 1.447 ? 
N-Glycosylation 
covale7  covale one  ? A ASN 410 ND2 ? ? ? 1_555 M  NAG .   C1 ? ? A ASN 410 M NAG 1    1_555 ? ? ? ? ? ? ? 1.444 ? 
N-Glycosylation 
covale8  covale one  ? A ASN 487 ND2 ? ? ? 1_555 V  NAG .   C1 ? ? A ASN 487 A NAG 1601 1_555 ? ? ? ? ? ? ? 1.455 ? 
N-Glycosylation 
covale9  covale one  ? A ASN 500 ND2 ? ? ? 1_555 L  NAG .   C1 ? ? A ASN 500 L NAG 1    1_555 ? ? ? ? ? ? ? 1.449 ? 
N-Glycosylation 
covale10 covale one  ? A ASN 580 ND2 ? ? ? 1_555 H  NAG .   C1 ? ? A ASN 580 H NAG 1    1_555 ? ? ? ? ? ? ? 1.438 ? 
N-Glycosylation 
covale11 covale one  ? D ASN 63  ND2 ? ? ? 1_555 AA NAG .   C1 ? ? D ASN 63  D NAG 1403 1_555 ? ? ? ? ? ? ? 1.444 ? 
N-Glycosylation 
covale12 covale one  ? D ASN 99  ND2 ? ? ? 1_555 Q  NAG .   C1 ? ? D ASN 99  Q NAG 1    1_555 ? ? ? ? ? ? ? 1.440 ? 
N-Glycosylation 
covale13 covale one  ? D ASN 119 ND2 ? ? ? 1_555 Y  NAG .   C1 ? ? D ASN 119 D NAG 1401 1_555 ? ? ? ? ? ? ? 1.447 ? 
N-Glycosylation 
covale14 covale one  ? D ASN 179 ND2 ? ? ? 1_555 O  NAG .   C1 ? ? D ASN 179 O NAG 1    1_555 ? ? ? ? ? ? ? 1.448 ? 
N-Glycosylation 
covale15 covale one  ? D ASN 249 ND2 ? ? ? 1_555 U  NAG .   C1 ? ? D ASN 249 U NAG 1    1_555 ? ? ? ? ? ? ? 1.445 ? 
N-Glycosylation 
covale16 covale one  ? D ASN 263 ND2 ? ? ? 1_555 Z  NAG .   C1 ? ? D ASN 263 D NAG 1402 1_555 ? ? ? ? ? ? ? 1.441 ? 
N-Glycosylation 
covale17 covale one  ? D ASN 284 ND2 ? ? ? 1_555 S  NAG .   C1 ? ? D ASN 284 S NAG 1    1_555 ? ? ? ? ? ? ? 1.446 ? 
N-Glycosylation 
covale18 covale one  ? D ASN 323 ND2 ? ? ? 1_555 CA NAG .   C1 ? ? D ASN 323 D NAG 1405 1_555 ? ? ? ? ? ? ? 1.441 ? 
N-Glycosylation 
covale19 covale one  ? D ASN 380 ND2 ? ? ? 1_555 R  NAG .   C1 ? ? D ASN 380 R NAG 1    1_555 ? ? ? ? ? ? ? 1.442 ? 
N-Glycosylation 
covale20 covale one  ? D ASN 410 ND2 ? ? ? 1_555 N  NAG .   C1 ? ? D ASN 410 N NAG 1    1_555 ? ? ? ? ? ? ? 1.430 ? 
N-Glycosylation 
covale21 covale one  ? D ASN 487 ND2 ? ? ? 1_555 DA NAG .   C1 ? ? D ASN 487 D NAG 1406 1_555 ? ? ? ? ? ? ? 1.443 ? 
N-Glycosylation 
covale22 covale one  ? D ASN 500 ND2 ? ? ? 1_555 T  NAG .   C1 ? ? D ASN 500 T NAG 1    1_555 ? ? ? ? ? ? ? 1.445 ? 
N-Glycosylation 
covale23 covale one  ? D ASN 580 ND2 ? ? ? 1_555 P  NAG .   C1 ? ? D ASN 580 P NAG 1    1_555 ? ? ? ? ? ? ? 1.454 ? 
N-Glycosylation 
covale24 covale one  ? D ASN 633 ND2 ? ? ? 1_555 BA NAG .   C1 ? ? D ASN 633 D NAG 1404 1_555 ? ? ? ? ? ? ? 1.457 ? 
N-Glycosylation 
covale25 covale both ? G NAG .   O3  ? ? ? 1_555 G  FUC .   C1 ? ? G NAG 1   G FUC 2    1_555 ? ? ? ? ? ? ? 1.441 ? ? 
covale26 covale both ? G NAG .   O4  ? ? ? 1_555 G  NAG .   C1 ? ? G NAG 1   G NAG 3    1_555 ? ? ? ? ? ? ? 1.453 ? ? 
covale27 covale both ? G NAG .   O6  ? ? ? 1_555 G  FUC .   C1 ? ? G NAG 1   G FUC 4    1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale28 covale both ? H NAG .   O4  ? ? ? 1_555 H  NAG .   C1 ? ? H NAG 1   H NAG 2    1_555 ? ? ? ? ? ? ? 1.440 ? ? 
covale29 covale both ? I NAG .   O4  ? ? ? 1_555 I  NAG .   C1 ? ? I NAG 1   I NAG 2    1_555 ? ? ? ? ? ? ? 1.443 ? ? 
covale30 covale both ? J NAG .   O4  ? ? ? 1_555 J  NAG .   C1 ? ? J NAG 1   J NAG 2    1_555 ? ? ? ? ? ? ? 1.440 ? ? 
covale31 covale both ? K NAG .   O4  ? ? ? 1_555 K  NAG .   C1 ? ? K NAG 1   K NAG 2    1_555 ? ? ? ? ? ? ? 1.456 ? ? 
covale32 covale both ? L NAG .   O4  ? ? ? 1_555 L  NAG .   C1 ? ? L NAG 1   L NAG 2    1_555 ? ? ? ? ? ? ? 1.451 ? ? 
covale33 covale both ? L NAG .   O6  ? ? ? 1_555 L  FUC .   C1 ? ? L NAG 1   L FUC 3    1_555 ? ? ? ? ? ? ? 1.447 ? ? 
covale34 covale both ? M NAG .   O4  ? ? ? 1_555 M  NAG .   C1 ? ? M NAG 1   M NAG 2    1_555 ? ? ? ? ? ? ? 1.434 ? ? 
covale35 covale both ? M NAG .   O4  ? ? ? 1_555 M  BMA .   C1 ? ? M NAG 2   M BMA 3    1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale36 covale both ? N NAG .   O4  ? ? ? 1_555 N  NAG .   C1 ? ? N NAG 1   N NAG 2    1_555 ? ? ? ? ? ? ? 1.451 ? ? 
covale37 covale both ? N NAG .   O4  ? ? ? 1_555 N  BMA .   C1 ? ? N NAG 2   N BMA 3    1_555 ? ? ? ? ? ? ? 1.430 ? ? 
covale38 covale both ? O NAG .   O4  ? ? ? 1_555 O  NAG .   C1 ? ? O NAG 1   O NAG 2    1_555 ? ? ? ? ? ? ? 1.440 ? ? 
covale39 covale both ? O NAG .   O6  ? ? ? 1_555 O  FUC .   C1 ? ? O NAG 1   O FUC 4    1_555 ? ? ? ? ? ? ? 1.448 ? ? 
covale40 covale both ? O NAG .   O4  ? ? ? 1_555 O  BMA .   C1 ? ? O NAG 2   O BMA 3    1_555 ? ? ? ? ? ? ? 1.435 ? ? 
covale41 covale both ? P NAG .   O4  ? ? ? 1_555 P  NAG .   C1 ? ? P NAG 1   P NAG 2    1_555 ? ? ? ? ? ? ? 1.446 ? ? 
covale42 covale both ? Q NAG .   O4  ? ? ? 1_555 Q  NAG .   C1 ? ? Q NAG 1   Q NAG 2    1_555 ? ? ? ? ? ? ? 1.441 ? ? 
covale43 covale both ? R NAG .   O4  ? ? ? 1_555 R  NAG .   C1 ? ? R NAG 1   R NAG 2    1_555 ? ? ? ? ? ? ? 1.439 ? ? 
covale44 covale both ? S NAG .   O6  ? ? ? 1_555 S  FUC .   C1 ? ? S NAG 1   S FUC 2    1_555 ? ? ? ? ? ? ? 1.440 ? ? 
covale45 covale both ? T NAG .   O6  ? ? ? 1_555 T  FUC .   C1 ? ? T NAG 1   T FUC 2    1_555 ? ? ? ? ? ? ? 1.444 ? ? 
covale46 covale both ? U NAG .   O4  ? ? ? 1_555 U  NAG .   C1 ? ? U NAG 1   U NAG 2    1_555 ? ? ? ? ? ? ? 1.438 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  NAG AA .   ? ASN D 63  ? NAG D 1403 ? 1_555 ASN D 63  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
2  NAG BA .   ? ASN D 633 ? NAG D 1404 ? 1_555 ASN D 633 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
3  NAG CA .   ? ASN D 323 ? NAG D 1405 ? 1_555 ASN D 323 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
4  NAG DA .   ? ASN D 487 ? NAG D 1406 ? 1_555 ASN D 487 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
5  NAG G  .   ? ASN A 179 ? NAG G 1    ? 1_555 ASN A 179 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
6  NAG H  .   ? ASN A 580 ? NAG H 1    ? 1_555 ASN A 580 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
7  NAG I  .   ? ASN A 119 ? NAG I 1    ? 1_555 ASN A 119 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
8  NAG J  .   ? ASN A 99  ? NAG J 1    ? 1_555 ASN A 99  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
9  NAG K  .   ? ASN A 380 ? NAG K 1    ? 1_555 ASN A 380 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
10 NAG L  .   ? ASN A 500 ? NAG L 1    ? 1_555 ASN A 500 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
11 NAG M  .   ? ASN A 410 ? NAG M 1    ? 1_555 ASN A 410 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
12 NAG N  .   ? ASN D 410 ? NAG N 1    ? 1_555 ASN D 410 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
13 NAG O  .   ? ASN D 179 ? NAG O 1    ? 1_555 ASN D 179 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
14 NAG P  .   ? ASN D 580 ? NAG P 1    ? 1_555 ASN D 580 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
15 NAG Q  .   ? ASN D 99  ? NAG Q 1    ? 1_555 ASN D 99  ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
16 NAG R  .   ? ASN D 380 ? NAG R 1    ? 1_555 ASN D 380 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
17 NAG S  .   ? ASN D 284 ? NAG S 1    ? 1_555 ASN D 284 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
18 NAG T  .   ? ASN D 500 ? NAG T 1    ? 1_555 ASN D 500 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
19 NAG U  .   ? ASN D 249 ? NAG U 1    ? 1_555 ASN D 249 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
20 NAG V  .   ? ASN A 487 ? NAG A 1601 ? 1_555 ASN A 487 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
21 NAG W  .   ? ASN A 263 ? NAG A 1602 ? 1_555 ASN A 263 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
22 NAG X  .   ? ASN A 284 ? NAG A 1603 ? 1_555 ASN A 284 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
23 NAG Y  .   ? ASN D 119 ? NAG D 1401 ? 1_555 ASN D 119 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
24 NAG Z  .   ? ASN D 263 ? NAG D 1402 ? 1_555 ASN D 263 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate       
25 CYS A  82  ? CYS A 90  ? CYS A 82   ? 1_555 CYS A 90  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
26 CYS A  403 ? CYS A 429 ? CYS A 403  ? 1_555 CYS A 429 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
27 CYS B  57  ? CYS B 64  ? CYS B 57   ? 1_555 CYS B 64  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
28 CYS D  82  ? CYS D 90  ? CYS D 82   ? 1_555 CYS D 90  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
29 CYS D  403 ? CYS D 429 ? CYS D 403  ? 1_555 CYS D 429 ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
30 CYS E  57  ? CYS E 64  ? CYS E 57   ? 1_555 CYS E 64  ? 1_555 SG SG  .   . .   None            'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 25 ? 
AA2 ? 5  ? 
AA3 ? 2  ? 
AA4 ? 9  ? 
AA5 ? 3  ? 
AA6 ? 3  ? 
AA7 ? 6  ? 
AA8 ? 25 ? 
AA9 ? 5  ? 
AB1 ? 3  ? 
AB2 ? 6  ? 
AB3 ? 3  ? 
AB4 ? 2  ? 
AB5 ? 3  ? 
AB6 ? 2  ? 
AB7 ? 3  ? 
AB8 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? parallel      
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? parallel      
AA1 6  7  ? parallel      
AA1 7  8  ? parallel      
AA1 8  9  ? parallel      
AA1 9  10 ? parallel      
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA1 12 13 ? parallel      
AA1 13 14 ? parallel      
AA1 14 15 ? parallel      
AA1 15 16 ? parallel      
AA1 16 17 ? parallel      
AA1 17 18 ? parallel      
AA1 18 19 ? parallel      
AA1 19 20 ? parallel      
AA1 20 21 ? parallel      
AA1 21 22 ? parallel      
AA1 22 23 ? parallel      
AA1 23 24 ? parallel      
AA1 24 25 ? parallel      
AA2 1  2  ? parallel      
AA2 2  3  ? parallel      
AA2 3  4  ? parallel      
AA2 4  5  ? parallel      
AA3 1  2  ? parallel      
AA4 1  2  ? parallel      
AA4 2  3  ? parallel      
AA4 3  4  ? parallel      
AA4 4  5  ? parallel      
AA4 5  6  ? parallel      
AA4 6  7  ? parallel      
AA4 7  8  ? parallel      
AA4 8  9  ? parallel      
AA5 1  2  ? parallel      
AA5 2  3  ? parallel      
AA6 1  2  ? anti-parallel 
AA6 2  3  ? parallel      
AA7 1  2  ? anti-parallel 
AA7 2  3  ? parallel      
AA7 3  4  ? parallel      
AA7 4  5  ? parallel      
AA7 5  6  ? parallel      
AA8 1  2  ? anti-parallel 
AA8 2  3  ? parallel      
AA8 3  4  ? parallel      
AA8 4  5  ? parallel      
AA8 5  6  ? parallel      
AA8 6  7  ? parallel      
AA8 7  8  ? parallel      
AA8 8  9  ? parallel      
AA8 9  10 ? parallel      
AA8 10 11 ? parallel      
AA8 11 12 ? parallel      
AA8 12 13 ? parallel      
AA8 13 14 ? parallel      
AA8 14 15 ? parallel      
AA8 15 16 ? parallel      
AA8 16 17 ? parallel      
AA8 17 18 ? parallel      
AA8 18 19 ? parallel      
AA8 19 20 ? parallel      
AA8 20 21 ? parallel      
AA8 21 22 ? parallel      
AA8 22 23 ? parallel      
AA8 23 24 ? parallel      
AA8 24 25 ? parallel      
AA9 1  2  ? parallel      
AA9 2  3  ? parallel      
AA9 3  4  ? parallel      
AA9 4  5  ? parallel      
AB1 1  2  ? parallel      
AB1 2  3  ? parallel      
AB2 1  2  ? parallel      
AB2 2  3  ? parallel      
AB2 3  4  ? parallel      
AB2 4  5  ? parallel      
AB2 5  6  ? parallel      
AB3 1  2  ? parallel      
AB3 2  3  ? parallel      
AB4 1  2  ? parallel      
AB5 1  2  ? parallel      
AB5 2  3  ? parallel      
AB6 1  2  ? parallel      
AB7 1  2  ? anti-parallel 
AB7 2  3  ? parallel      
AB8 1  2  ? anti-parallel 
AB8 2  3  ? parallel      
AB8 3  4  ? parallel      
AB8 4  5  ? parallel      
AB8 5  6  ? 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  VAL A 88  ? SER A 91  ? VAL A 88  SER A 91  
AA1 2  SER A 94  ? ASN A 99  ? SER A 94  ASN A 99  
AA1 3  PHE A 122 ? ASP A 124 ? PHE A 122 ASP A 124 
AA1 4  TYR A 146 ? ASP A 148 ? TYR A 146 ASP A 148 
AA1 5  THR A 170 ? HIS A 172 ? THR A 170 HIS A 172 
AA1 6  GLU A 194 ? ALA A 196 ? GLU A 194 ALA A 196 
AA1 7  ASN A 218 ? TYR A 220 ? ASN A 218 TYR A 220 
AA1 8  GLU A 242 ? CYS A 244 ? GLU A 242 CYS A 244 
AA1 9  LEU A 266 ? ASN A 268 ? LEU A 266 ASN A 268 
AA1 10 THR A 290 ? SER A 292 ? THR A 290 SER A 292 
AA1 11 VAL A 314 ? HIS A 316 ? VAL A 314 HIS A 316 
AA1 12 ASP A 338 ? GLU A 340 ? ASP A 338 GLU A 340 
AA1 13 TRP A 362 ? PHE A 364 ? TRP A 362 PHE A 364 
AA1 14 VAL A 386 ? GLN A 388 ? VAL A 386 GLN A 388 
AA1 15 ASN A 410 ? THR A 412 ? ASN A 410 THR A 412 
AA1 16 ARG A 434 ? ARG A 436 ? ARG A 434 ARG A 436 
AA1 17 PHE A 458 ? ASP A 460 ? PHE A 458 ASP A 460 
AA1 18 ALA A 482 ? ILE A 484 ? ALA A 482 ILE A 484 
AA1 19 GLN A 506 ? ASP A 508 ? GLN A 506 ASP A 508 
AA1 20 LYS A 530 ? GLN A 532 ? LYS A 530 GLN A 532 
AA1 21 TYR A 554 ? ASP A 556 ? TYR A 554 ASP A 556 
AA1 22 TYR A 578 ? ASN A 580 ? TYR A 578 ASN A 580 
AA1 23 MET A 602 ? ASP A 604 ? MET A 602 ASP A 604 
AA1 24 ARG A 626 ? ASP A 628 ? ARG A 626 ASP A 628 
AA1 25 HIS A 650 ? ASP A 652 ? HIS A 650 ASP A 652 
AA2 1  GLU A 106 ? GLY A 107 ? GLU A 106 GLY A 107 
AA2 2  ARG A 129 ? GLY A 132 ? ARG A 129 GLY A 132 
AA2 3  GLN A 153 ? GLY A 156 ? GLN A 153 GLY A 156 
AA2 4  LYS A 177 ? SER A 181 ? LYS A 177 SER A 181 
AA2 5  LEU A 201 ? THR A 203 ? LEU A 201 THR A 203 
AA3 1  SER A 227 ? GLY A 228 ? SER A 227 GLY A 228 
AA3 2  ASN A 249 ? LEU A 250 ? ASN A 249 LEU A 250 
AA4 1  THR A 299 ? GLY A 300 ? THR A 299 GLY A 300 
AA4 2  GLN A 321 ? SER A 325 ? GLN A 321 SER A 325 
AA4 3  LYS A 345 ? GLY A 348 ? LYS A 345 GLY A 348 
AA4 4  GLN A 369 ? GLY A 372 ? GLN A 369 GLY A 372 
AA4 5  ASN A 393 ? GLY A 396 ? ASN A 393 GLY A 396 
AA4 6  HIS A 417 ? GLY A 420 ? HIS A 417 GLY A 420 
AA4 7  SER A 441 ? ASP A 445 ? SER A 441 ASP A 445 
AA4 8  ASN A 465 ? GLY A 468 ? ASN A 465 GLY A 468 
AA4 9  SER A 489 ? ILE A 490 ? SER A 489 ILE A 490 
AA5 1  ASP A 611 ? GLU A 613 ? ASP A 611 GLU A 613 
AA5 2  ASN A 633 ? GLN A 637 ? ASN A 633 GLN A 637 
AA5 3  ASN A 657 ? GLN A 659 ? ASN A 657 GLN A 659 
AA6 1  LEU B 39  ? ALA B 40  ? LEU B 39  ALA B 40  
AA6 2  SER B 81  ? GLN B 83  ? SER B 81  GLN B 83  
AA6 3  ASN B 103 ? THR B 105 ? ASN B 103 THR B 105 
AA7 1  VAL B 62  ? CYS B 64  ? VAL B 62  CYS B 64  
AA7 2  VAL B 70  ? ASP B 74  ? VAL B 70  ASP B 74  
AA7 3  TYR B 96  ? GLU B 98  ? TYR B 96  GLU B 98  
AA7 4  SER B 120 ? ASP B 122 ? SER B 120 ASP B 122 
AA7 5  PHE B 144 ? ARG B 146 ? PHE B 144 ARG B 146 
AA7 6  VAL B 168 ? ASP B 170 ? VAL B 168 ASP B 170 
AA8 1  VAL D 88  ? SER D 91  ? VAL D 88  SER D 91  
AA8 2  SER D 94  ? ASN D 99  ? SER D 94  ASN D 99  
AA8 3  PHE D 122 ? ASP D 124 ? PHE D 122 ASP D 124 
AA8 4  TYR D 146 ? ASP D 148 ? TYR D 146 ASP D 148 
AA8 5  THR D 170 ? HIS D 172 ? THR D 170 HIS D 172 
AA8 6  GLU D 194 ? ALA D 196 ? GLU D 194 ALA D 196 
AA8 7  ASN D 218 ? TYR D 220 ? ASN D 218 TYR D 220 
AA8 8  GLU D 242 ? CYS D 244 ? GLU D 242 CYS D 244 
AA8 9  LEU D 266 ? ASN D 268 ? LEU D 266 ASN D 268 
AA8 10 THR D 290 ? SER D 292 ? THR D 290 SER D 292 
AA8 11 VAL D 314 ? HIS D 316 ? VAL D 314 HIS D 316 
AA8 12 ASP D 338 ? GLU D 340 ? ASP D 338 GLU D 340 
AA8 13 TRP D 362 ? PHE D 364 ? TRP D 362 PHE D 364 
AA8 14 VAL D 386 ? GLN D 388 ? VAL D 386 GLN D 388 
AA8 15 ASN D 410 ? THR D 412 ? ASN D 410 THR D 412 
AA8 16 ARG D 434 ? ARG D 436 ? ARG D 434 ARG D 436 
AA8 17 PHE D 458 ? ASP D 460 ? PHE D 458 ASP D 460 
AA8 18 ALA D 482 ? ILE D 484 ? ALA D 482 ILE D 484 
AA8 19 GLN D 506 ? ASP D 508 ? GLN D 506 ASP D 508 
AA8 20 LYS D 530 ? GLN D 532 ? LYS D 530 GLN D 532 
AA8 21 TYR D 554 ? ASP D 556 ? TYR D 554 ASP D 556 
AA8 22 TYR D 578 ? ASN D 580 ? TYR D 578 ASN D 580 
AA8 23 MET D 602 ? ASP D 604 ? MET D 602 ASP D 604 
AA8 24 ARG D 626 ? ASP D 628 ? ARG D 626 ASP D 628 
AA8 25 HIS D 650 ? ASP D 652 ? HIS D 650 ASP D 652 
AA9 1  GLU D 106 ? GLY D 107 ? GLU D 106 GLY D 107 
AA9 2  ARG D 129 ? GLY D 132 ? ARG D 129 GLY D 132 
AA9 3  GLN D 153 ? GLY D 156 ? GLN D 153 GLY D 156 
AA9 4  LYS D 177 ? SER D 181 ? LYS D 177 SER D 181 
AA9 5  LEU D 201 ? THR D 203 ? LEU D 201 THR D 203 
AB1 1  SER D 227 ? GLY D 228 ? SER D 227 GLY D 228 
AB1 2  ASN D 249 ? GLY D 252 ? ASN D 249 GLY D 252 
AB1 3  GLN D 273 ? LEU D 274 ? GLN D 273 LEU D 274 
AB2 1  THR D 299 ? GLY D 300 ? THR D 299 GLY D 300 
AB2 2  GLN D 321 ? GLY D 324 ? GLN D 321 GLY D 324 
AB2 3  LYS D 345 ? GLY D 348 ? LYS D 345 GLY D 348 
AB2 4  GLN D 369 ? GLY D 372 ? GLN D 369 GLY D 372 
AB2 5  ASN D 393 ? GLY D 396 ? ASN D 393 GLY D 396 
AB2 6  HIS D 417 ? PHE D 418 ? HIS D 417 PHE D 418 
AB3 1  SER D 443 ? ASP D 445 ? SER D 443 ASP D 445 
AB3 2  ASN D 465 ? GLY D 468 ? ASN D 465 GLY D 468 
AB3 3  SER D 489 ? ILE D 490 ? SER D 489 ILE D 490 
AB4 1  THR D 515 ? GLU D 517 ? THR D 515 GLU D 517 
AB4 2  ARG D 537 ? SER D 539 ? ARG D 537 SER D 539 
AB5 1  ASP D 587 ? GLN D 588 ? ASP D 587 GLN D 588 
AB5 2  GLN D 609 ? GLU D 613 ? GLN D 609 GLU D 613 
AB5 3  ASN D 633 ? SER D 635 ? ASN D 633 SER D 635 
AB6 1  GLN D 659 ? GLY D 660 ? GLN D 659 GLY D 660 
AB6 2  ASP D 681 ? LEU D 682 ? ASP D 681 LEU D 682 
AB7 1  LEU E 39  ? ALA E 40  ? LEU E 39  ALA E 40  
AB7 2  SER E 81  ? GLN E 83  ? SER E 81  GLN E 83  
AB7 3  ASN E 103 ? THR E 105 ? ASN E 103 THR E 105 
AB8 1  VAL E 62  ? CYS E 64  ? VAL E 62  CYS E 64  
AB8 2  VAL E 70  ? ASP E 74  ? VAL E 70  ASP E 74  
AB8 3  TYR E 96  ? GLU E 98  ? TYR E 96  GLU E 98  
AB8 4  SER E 120 ? ASP E 122 ? SER E 120 ASP E 122 
AB8 5  PHE E 144 ? ARG E 146 ? PHE E 144 ARG E 146 
AB8 6  VAL E 168 ? ASP E 170 ? VAL E 168 ASP E 170 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1  2  N SER A 91  ? N SER A 91  O SER A 94  ? O SER A 94  
AA1 2  3  N LEU A 98  ? N LEU A 98  O PHE A 122 ? O PHE A 122 
AA1 3  4  N VAL A 123 ? N VAL A 123 O TYR A 146 ? O TYR A 146 
AA1 4  5  N PHE A 147 ? N PHE A 147 O HIS A 172 ? O HIS A 172 
AA1 5  6  N LEU A 171 ? N LEU A 171 O ALA A 196 ? O ALA A 196 
AA1 6  7  N ILE A 195 ? N ILE A 195 O TYR A 220 ? O TYR A 220 
AA1 7  8  N LEU A 219 ? N LEU A 219 O GLU A 242 ? O GLU A 242 
AA1 8  9  N LEU A 243 ? N LEU A 243 O ASN A 268 ? O ASN A 268 
AA1 9  10 N LEU A 267 ? N LEU A 267 O THR A 290 ? O THR A 290 
AA1 10 11 N LEU A 291 ? N LEU A 291 O VAL A 314 ? O VAL A 314 
AA1 11 12 N LEU A 315 ? N LEU A 315 O ASP A 338 ? O ASP A 338 
AA1 12 13 N LEU A 339 ? N LEU A 339 O PHE A 364 ? O PHE A 364 
AA1 13 14 N LEU A 363 ? N LEU A 363 O VAL A 386 ? O VAL A 386 
AA1 14 15 N LEU A 387 ? N LEU A 387 O ASN A 410 ? O ASN A 410 
AA1 15 16 N LEU A 411 ? N LEU A 411 O ARG A 434 ? O ARG A 434 
AA1 16 17 N VAL A 435 ? N VAL A 435 O PHE A 458 ? O PHE A 458 
AA1 17 18 N ILE A 459 ? N ILE A 459 O ALA A 482 ? O ALA A 482 
AA1 18 19 N PHE A 483 ? N PHE A 483 O ASP A 508 ? O ASP A 508 
AA1 19 20 N LEU A 507 ? N LEU A 507 O GLN A 532 ? O GLN A 532 
AA1 20 21 N LEU A 531 ? N LEU A 531 O TYR A 554 ? O TYR A 554 
AA1 21 22 N LEU A 555 ? N LEU A 555 O ASN A 580 ? O ASN A 580 
AA1 22 23 N MET A 579 ? N MET A 579 O ASP A 604 ? O ASP A 604 
AA1 23 24 N LEU A 603 ? N LEU A 603 O ASP A 628 ? O ASP A 628 
AA1 24 25 N LEU A 627 ? N LEU A 627 O HIS A 650 ? O HIS A 650 
AA2 1  2  N GLY A 107 ? N GLY A 107 O SER A 131 ? O SER A 131 
AA2 2  3  N GLY A 132 ? N GLY A 132 O VAL A 155 ? O VAL A 155 
AA2 3  4  N LEU A 154 ? N LEU A 154 O LYS A 177 ? O LYS A 177 
AA2 4  5  N GLY A 180 ? N GLY A 180 O THR A 203 ? O THR A 203 
AA3 1  2  N GLY A 228 ? N GLY A 228 O ASN A 249 ? O ASN A 249 
AA4 1  2  N GLY A 300 ? N GLY A 300 O ASN A 323 ? O ASN A 323 
AA4 2  3  N GLY A 324 ? N GLY A 324 O THR A 347 ? O THR A 347 
AA4 3  4  N LEU A 346 ? N LEU A 346 O GLN A 369 ? O GLN A 369 
AA4 4  5  N GLY A 372 ? N GLY A 372 O THR A 395 ? O THR A 395 
AA4 5  6  N GLY A 396 ? N GLY A 396 O GLU A 419 ? O GLU A 419 
AA4 6  7  N PHE A 418 ? N PHE A 418 O SER A 441 ? O SER A 441 
AA4 7  8  N PHE A 442 ? N PHE A 442 O ASN A 465 ? O ASN A 465 
AA4 8  9  N PHE A 466 ? N PHE A 466 O SER A 489 ? O SER A 489 
AA5 1  2  N GLY A 612 ? N GLY A 612 O SER A 635 ? O SER A 635 
AA5 2  3  N LEU A 634 ? N LEU A 634 O ASN A 657 ? O ASN A 657 
AA6 1  2  N ALA B 40  ? N ALA B 40  O SER B 81  ? O SER B 81  
AA6 2  3  N GLY B 82  ? N GLY B 82  O THR B 105 ? O THR B 105 
AA7 1  2  N THR B 63  ? N THR B 63  O THR B 71  ? O THR B 71  
AA7 2  3  N VAL B 73  ? N VAL B 73  O GLU B 98  ? O GLU B 98  
AA7 3  4  N LEU B 97  ? N LEU B 97  O ASP B 122 ? O ASP B 122 
AA7 4  5  N LEU B 121 ? N LEU B 121 O PHE B 144 ? O PHE B 144 
AA7 5  6  N LEU B 145 ? N LEU B 145 O VAL B 168 ? O VAL B 168 
AA8 1  2  N ALA D 89  ? N ALA D 89  O ILE D 96  ? O ILE D 96  
AA8 2  3  N LEU D 98  ? N LEU D 98  O PHE D 122 ? O PHE D 122 
AA8 3  4  N VAL D 123 ? N VAL D 123 O TYR D 146 ? O TYR D 146 
AA8 4  5  N PHE D 147 ? N PHE D 147 O HIS D 172 ? O HIS D 172 
AA8 5  6  N LEU D 171 ? N LEU D 171 O ALA D 196 ? O ALA D 196 
AA8 6  7  N ILE D 195 ? N ILE D 195 O TYR D 220 ? O TYR D 220 
AA8 7  8  N LEU D 219 ? N LEU D 219 O CYS D 244 ? O CYS D 244 
AA8 8  9  N LEU D 243 ? N LEU D 243 O LEU D 266 ? O LEU D 266 
AA8 9  10 N LEU D 267 ? N LEU D 267 O THR D 290 ? O THR D 290 
AA8 10 11 N LEU D 291 ? N LEU D 291 O VAL D 314 ? O VAL D 314 
AA8 11 12 N LEU D 315 ? N LEU D 315 O ASP D 338 ? O ASP D 338 
AA8 12 13 N LEU D 339 ? N LEU D 339 O PHE D 364 ? O PHE D 364 
AA8 13 14 N LEU D 363 ? N LEU D 363 O VAL D 386 ? O VAL D 386 
AA8 14 15 N LEU D 387 ? N LEU D 387 O ASN D 410 ? O ASN D 410 
AA8 15 16 N LEU D 411 ? N LEU D 411 O ARG D 434 ? O ARG D 434 
AA8 16 17 N VAL D 435 ? N VAL D 435 O PHE D 458 ? O PHE D 458 
AA8 17 18 N ILE D 459 ? N ILE D 459 O ILE D 484 ? O ILE D 484 
AA8 18 19 N PHE D 483 ? N PHE D 483 O ASP D 508 ? O ASP D 508 
AA8 19 20 N LEU D 507 ? N LEU D 507 O GLN D 532 ? O GLN D 532 
AA8 20 21 N LEU D 531 ? N LEU D 531 O TYR D 554 ? O TYR D 554 
AA8 21 22 N LEU D 555 ? N LEU D 555 O ASN D 580 ? O ASN D 580 
AA8 22 23 N MET D 579 ? N MET D 579 O ASP D 604 ? O ASP D 604 
AA8 23 24 N LEU D 603 ? N LEU D 603 O ASP D 628 ? O ASP D 628 
AA8 24 25 N LEU D 627 ? N LEU D 627 O HIS D 650 ? O HIS D 650 
AA9 1  2  N GLY D 107 ? N GLY D 107 O SER D 131 ? O SER D 131 
AA9 2  3  N GLY D 132 ? N GLY D 132 O VAL D 155 ? O VAL D 155 
AA9 3  4  N LEU D 154 ? N LEU D 154 O LYS D 177 ? O LYS D 177 
AA9 4  5  N GLY D 180 ? N GLY D 180 O THR D 203 ? O THR D 203 
AB1 1  2  N GLY D 228 ? N GLY D 228 O THR D 251 ? O THR D 251 
AB1 2  3  N LEU D 250 ? N LEU D 250 O GLN D 273 ? O GLN D 273 
AB2 1  2  N GLY D 300 ? N GLY D 300 O ASN D 323 ? O ASN D 323 
AB2 2  3  N GLY D 324 ? N GLY D 324 O THR D 347 ? O THR D 347 
AB2 3  4  N LEU D 346 ? N LEU D 346 O GLN D 369 ? O GLN D 369 
AB2 4  5  N LEU D 370 ? N LEU D 370 O ASN D 393 ? O ASN D 393 
AB2 5  6  N PHE D 394 ? N PHE D 394 O HIS D 417 ? O HIS D 417 
AB3 1  2  N GLY D 444 ? N GLY D 444 O HIS D 467 ? O HIS D 467 
AB3 2  3  N PHE D 466 ? N PHE D 466 O SER D 489 ? O SER D 489 
AB4 1  2  N GLY D 516 ? N GLY D 516 O SER D 539 ? O SER D 539 
AB5 1  2  N GLN D 588 ? N GLN D 588 O ASP D 611 ? O ASP D 611 
AB5 2  3  N LEU D 610 ? N LEU D 610 O ASN D 633 ? O ASN D 633 
AB6 1  2  N GLY D 660 ? N GLY D 660 O ASP D 681 ? O ASP D 681 
AB7 1  2  N ALA E 40  ? N ALA E 40  O SER E 81  ? O SER E 81  
AB7 2  3  N GLY E 82  ? N GLY E 82  O THR E 105 ? O THR E 105 
AB8 1  2  N THR E 63  ? N THR E 63  O THR E 71  ? O THR E 71  
AB8 2  3  N VAL E 73  ? N VAL E 73  O GLU E 98  ? O GLU E 98  
AB8 3  4  N LEU E 97  ? N LEU E 97  O ASP E 122 ? O ASP E 122 
AB8 4  5  N LEU E 121 ? N LEU E 121 O PHE E 144 ? O PHE E 144 
AB8 5  6  N LEU E 145 ? N LEU E 145 O VAL E 168 ? O VAL E 168 
# 
_pdbx_entry_details.entry_id                   8WED 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 OG1 A THR 62  ? ? OE1 A GLU 106 ? ? 2.18 
2 1 O   B LEU 142 ? ? OG1 B THR 165 ? ? 2.19 
# 
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 ILE A 151 ? ? 48.82   78.44   
2  1 ILE A 433 ? ? -123.35 -55.29  
3  1 LYS A 680 ? ? -94.21  -60.64  
4  1 VAL B 119 ? ? -121.20 -53.14  
5  1 LEU B 164 ? ? 64.37   -11.78  
6  1 SER B 185 ? ? 127.61  -45.90  
7  1 PRO B 191 ? ? -56.76  -9.03   
8  1 SER D 79  ? ? 74.16   -5.40   
9  1 ILE D 151 ? ? 53.18   73.05   
10 1 ILE D 223 ? ? 54.90   70.33   
11 1 ILE D 433 ? ? -123.03 -55.95  
12 1 GLN D 588 ? ? 64.31   -165.97 
13 1 SER D 641 ? ? -69.35  0.97    
14 1 PRO E 191 ? ? -57.45  -9.22   
15 1 LYS E 198 ? ? 59.50   -148.16 
16 1 SER F 2   ? ? 62.43   147.20  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 34.0136 -37.1928 117.3066 0.5052  ? 0.1383  ? 0.0282  ? 0.2922  ? 0.0816  ? 0.3711 ? 1.9428 ? 
-0.0300 ? -0.8032 ? 5.2343 ? 2.6188  ? 1.6350 ? -0.1205 ? -0.3533 ? 0.1116  ? 0.5519  ? 0.2932  ? 0.5937  ? -0.0815 ? -0.6456 ? 
-0.1366 ? 
2  'X-RAY DIFFRACTION' ? refined 49.8631 -27.9353 108.4181 0.4089  ? 0.1393  ? -0.1623 ? 0.0591  ? -0.0759 ? 0.3058 ? 0.9309 ? 
0.3816  ? -0.5900 ? 1.6834 ? -0.4984 ? 0.5761 ? 0.0904  ? -0.2117 ? 0.0716  ? 0.2364  ? -0.0711 ? 0.1587  ? -0.2205 ? 0.1042  ? 
0.0084  ? 
3  'X-RAY DIFFRACTION' ? refined 61.4049 -22.4157 81.4075  0.3574  ? 0.2346  ? -0.0059 ? 0.5245  ? 0.0709  ? 0.3879 ? 0.8889 ? 
-0.4145 ? 0.5533  ? 0.9497 ? -0.9654 ? 1.1442 ? 0.1450  ? 0.4580  ? 0.1167  ? -0.1859 ? -0.3516 ? -0.4412 ? 0.3850  ? 1.0113  ? 
0.2118  ? 
4  'X-RAY DIFFRACTION' ? refined 44.1833 -10.9786 57.1492  0.4558  ? 0.1856  ? 0.0326  ? 0.5636  ? 0.1075  ? 0.2369 ? 1.2732 ? 
-1.1961 ? 1.0406  ? 1.4034 ? -0.5450 ? 1.4465 ? 0.2375  ? 0.7990  ? 0.0004  ? -0.3719 ? -0.3096 ? -0.1457 ? 0.5480  ? 0.8529  ? 
0.0663  ? 
5  'X-RAY DIFFRACTION' ? refined 25.4515 9.1280   59.1927  0.3737  ? 0.0242  ? -0.0518 ? 0.1729  ? -0.0199 ? 0.1685 ? 4.3158 ? 
-2.0889 ? 0.1807  ? 4.5894 ? 0.2705  ? 2.6196 ? -0.2167 ? -0.0740 ? -0.0846 ? 0.1661  ? -0.0632 ? 0.1495  ? -0.6565 ? -0.2590 ? 
0.2571  ? 
6  'X-RAY DIFFRACTION' ? refined 28.0287 29.0071  68.4391  1.5542  ? 0.0769  ? -0.3050 ? 0.4877  ? -0.3053 ? 0.6713 ? 1.3607 ? 
0.0605  ? 0.6049  ? 1.4947 ? 0.7717  ? 1.0623 ? -0.4770 ? -0.2700 ? 0.7932  ? 0.6577  ? 0.1938  ? -0.1759 ? -1.0900 ? 0.0580  ? 
0.1928  ? 
7  'X-RAY DIFFRACTION' ? refined 35.9952 -5.4869  83.6657  0.7259  ? 0.2166  ? -0.0027 ? 0.5207  ? 0.0430  ? 0.2915 ? 3.0852 ? 
-0.9926 ? 3.1294  ? 5.1559 ? 2.3464  ? 5.4979 ? -0.3584 ? -0.3239 ? 0.2142  ? 1.4663  ? -0.0153 ? 0.1932  ? -0.2706 ? -0.5793 ? 
0.3709  ? 
8  'X-RAY DIFFRACTION' ? refined 34.4996 -5.4212  75.1783  0.5269  ? 0.0981  ? 0.0607  ? 0.4335  ? 0.1569  ? 0.2436 ? 7.2981 ? 
-1.9938 ? 0.0497  ? 3.4075 ? -0.7266 ? 2.4686 ? 0.1088  ? -0.2047 ? -0.4526 ? 0.7711  ? -0.1456 ? 0.2133  ? -0.7986 ? -0.3242 ? 
-0.0607 ? 
9  'X-RAY DIFFRACTION' ? refined 36.2311 4.7316   76.7078  0.8884  ? 0.1659  ? -0.1377 ? 0.6325  ? -0.0565 ? 0.3090 ? 1.9615 ? 
-0.2097 ? -2.9267 ? 3.9645 ? -1.5036 ? 5.2054 ? -0.1535 ? -0.6786 ? 0.2240  ? 1.0525  ? 0.1110  ? -0.3500 ? -0.9383 ? -0.2565 ? 
-0.0289 ? 
10 'X-RAY DIFFRACTION' ? refined 36.4465 1.6884   87.3620  1.2804  ? 0.2004  ? -0.1650 ? 0.7637  ? -0.0932 ? 0.4069 ? 1.6675 ? 
-0.4518 ? -2.0266 ? 0.5158 ? -0.7205 ? 6.5582 ? -0.2707 ? -0.8530 ? 0.3245  ? 0.7406  ? 0.0333  ? -0.0971 ? -0.9134 ? 0.2518  ? 
0.1896  ? 
11 'X-RAY DIFFRACTION' ? refined 30.6989 5.0526   89.0943  1.7420  ? 0.5076  ? 0.0241  ? 1.0158  ? -0.0469 ? 0.5053 ? 2.0467 ? 
0.3139  ? 1.7442  ? 0.1699 ? -0.4118 ? 5.3039 ? -0.5493 ? -0.8860 ? -0.2111 ? 0.7323  ? 0.3149  ? -0.0958 ? 0.0845  ? -1.1436 ? 
0.2057  ? 
12 'X-RAY DIFFRACTION' ? refined 30.3268 9.3487   89.9976  1.7125  ? 0.3537  ? -0.2117 ? 1.1583  ? -0.2098 ? 0.5340 ? 2.3387 ? 
1.1217  ? 1.2428  ? 0.5664 ? 0.6696  ? 1.3609 ? 0.1407  ? -0.6284 ? 0.0576  ? 0.5221  ? -0.0852 ? -0.0379 ? -0.0305 ? -0.1237 ? 
-0.0454 ? 
13 'X-RAY DIFFRACTION' ? refined 36.6797 15.8468  90.4267  1.5996  ? 0.3245  ? -0.3936 ? 1.0087  ? -0.3502 ? 0.7150 ? 1.4106 ? 
0.5935  ? 0.4193  ? 1.4495 ? 1.7941  ? 3.8891 ? -0.1477 ? -0.0702 ? 0.1026  ? -0.1706 ? 0.1137  ? -0.0193 ? -0.1089 ? -0.0173 ? 
0.0701  ? 
14 'X-RAY DIFFRACTION' ? refined 28.0348 18.0844  96.7286  2.2192  ? 0.2859  ? -0.1329 ? 1.4093  ? -0.4080 ? 0.7617 ? 2.2607 ? 
1.2038  ? -0.1848 ? 1.2200 ? 0.3885  ? 0.4223 ? 0.0911  ? -1.4234 ? 0.8195  ? 0.4600  ? -0.4713 ? 0.3536  ? -0.8062 ? -0.2365 ? 
0.3310  ? 
15 'X-RAY DIFFRACTION' ? refined 22.5848 22.9876  96.2687  2.1832  ? 0.4803  ? 0.0446  ? 1.4470  ? -0.4515 ? 0.9448 ? 6.5501 ? 
-0.6771 ? 0.3659  ? 1.2696 ? 0.7530  ? 1.2542 ? -1.2642 ? -0.9466 ? -0.0864 ? 0.7566  ? 0.6704  ? 0.2326  ? -0.8625 ? 0.1620  ? 
0.5529  ? 
16 'X-RAY DIFFRACTION' ? refined 46.8488 -19.8983 82.4417  0.5407  ? 0.0537  ? 0.0042  ? 0.2685  ? -0.2217 ? 0.5740 ? 3.0137 ? 
0.8398  ? -1.8979 ? 2.5426 ? -3.8391 ? 8.6841 ? -0.2175 ? 0.2719  ? -0.5406 ? -0.3569 ? 0.0356  ? 0.5725  ? 1.1135  ? -0.1554 ? 
0.1538  ? 
17 'X-RAY DIFFRACTION' ? refined 7.9953  15.4961  26.8110  -0.0532 ? 0.2912  ? 0.1543  ? -0.0390 ? -0.2255 ? 0.0788 ? 0.6757 ? 
0.2877  ? 0.3346  ? 1.2510 ? 0.3242  ? 1.0209 ? -0.1225 ? -0.1944 ? 0.0962  ? 0.3097  ? -0.1778 ? -0.0827 ? -0.2804 ? -0.0500 ? 
-0.0764 ? 
18 'X-RAY DIFFRACTION' ? refined -6.7094 -19.3908 -9.3659  0.3648  ? 0.0745  ? -0.1395 ? 0.1606  ? -0.0220 ? 0.3389 ? 1.1199 ? 
0.4915  ? 0.2223  ? 2.2270 ? 1.3655  ? 2.5016 ? 0.1898  ? -0.0928 ? -0.2815 ? -0.0574 ? 0.0212  ? -0.0405 ? 0.5575  ? 0.1526  ? 
-0.1175 ? 
19 'X-RAY DIFFRACTION' ? refined 9.4135  -5.1929  7.9849   0.2341  ? 0.0522  ? -0.1366 ? 0.5530  ? -0.2135 ? 0.3840 ? 1.7017 ? 
-1.5641 ? 1.0208  ? 1.4394 ? -1.0281 ? 3.4812 ? -0.2081 ? 0.2110  ? 0.4433  ? 0.2124  ? 0.1687  ? -0.5208 ? 0.0281  ? 0.5031  ? 
0.0782  ? 
20 'X-RAY DIFFRACTION' ? refined 3.5667  -5.0677  1.6909   0.1482  ? -0.0187 ? -0.0305 ? 0.3697  ? -0.1896 ? 0.3719 ? 1.3469 ? 
-1.8234 ? 0.6902  ? 3.0602 ? 0.4885  ? 3.7838 ? 0.2139  ? 0.2567  ? 0.1346  ? -0.0441 ? -0.0253 ? -0.3495 ? 0.0734  ? 0.5469  ? 
-0.2105 ? 
21 'X-RAY DIFFRACTION' ? refined 3.3587  -15.2314 4.1453   0.3828  ? 0.1604  ? -0.1154 ? 0.5268  ? -0.0536 ? 0.2663 ? 4.0870 ? 
-0.7737 ? 0.0066  ? 4.2467 ? 0.7387  ? 0.6240 ? 0.2668  ? 0.0925  ? -0.4993 ? 0.3152  ? 0.1204  ? -0.0712 ? 0.5583  ? 0.6250  ? 
-0.3961 ? 
22 'X-RAY DIFFRACTION' ? refined 11.7455 -12.2666 10.7674  0.4515  ? 0.2376  ? -0.2572 ? 0.6916  ? -0.1898 ? 0.6159 ? 2.6186 ? 
-1.0073 ? -0.1843 ? 1.0298 ? -0.3207 ? 1.6891 ? 0.0670  ? -0.2873 ? -0.1784 ? 0.2971  ? 0.1596  ? -0.4627 ? 0.2543  ? 0.7779  ? 
-0.1923 ? 
23 'X-RAY DIFFRACTION' ? refined 16.5040 -15.9684 7.4096   0.4141  ? 0.2682  ? -0.1376 ? 0.8784  ? -0.2631 ? 0.6732 ? 1.9677 ? 
0.2023  ? -1.3417 ? 4.2408 ? -1.2448 ? 2.8010 ? -0.0235 ? 0.0271  ? -0.0171 ? 0.4719  ? -0.0945 ? -0.7657 ? 0.1205  ? 0.9238  ? 
0.0519  ? 
24 'X-RAY DIFFRACTION' ? refined 9.6144  -22.8135 10.5810  0.8239  ? 0.3500  ? -0.3511 ? 0.6008  ? -0.2573 ? 0.5593 ? 5.2112 ? 
-0.7265 ? 1.3538  ? 5.5275 ? -0.1287 ? 4.3768 ? -0.0054 ? -0.3677 ? -0.3102 ? 0.5240  ? 0.7118  ? -0.3954 ? 0.5899  ? 0.5262  ? 
-0.5691 ? 
25 'X-RAY DIFFRACTION' ? refined 17.7514 -22.8635 9.6176   0.9089  ? 0.5510  ? -0.3241 ? 0.8967  ? -0.1919 ? 0.7369 ? 1.1330 ? 
-1.2618 ? 0.4427  ? 2.8345 ? -1.3015 ? 1.3013 ? 0.0052  ? -0.0919 ? 0.0028  ? 0.5140  ? 0.2289  ? -0.3690 ? 0.1868  ? 0.3351  ? 
-0.0850 ? 
26 'X-RAY DIFFRACTION' ? refined 21.3782 -28.1320 10.2227  1.1074  ? 0.5865  ? -0.4195 ? 1.1469  ? -0.0780 ? 0.9627 ? 5.4564 ? 
2.4183  ? -1.4688 ? 1.5404 ? -0.2367 ? 0.7601 ? 0.2686  ? -0.5203 ? -0.9045 ? 0.6476  ? -0.2421 ? -0.9808 ? 0.7094  ? 0.8784  ? 
-0.0307 ? 
27 'X-RAY DIFFRACTION' ? refined 27.8965 -30.8522 9.5040   0.6386  ? 0.3268  ? -0.2695 ? 1.3552  ? -0.2124 ? 1.5439 ? 1.9347 ? 
0.6176  ? 1.1786  ? 3.3081 ? -0.8168 ? 4.0648 ? 0.7406  ? -0.3086 ? 0.6557  ? 0.2003  ? -0.4720 ? -1.1412 ? 0.5326  ? 1.1306  ? 
-0.2285 ? 
28 'X-RAY DIFFRACTION' ? refined 26.1362 -34.5327 5.5772   1.1112  ? 0.4861  ? -0.5542 ? 1.2337  ? 0.0106  ? 1.5600 ? 2.6100 ? 
-0.6323 ? 0.7472  ? 0.5026 ? -0.6760 ? 1.0199 ? -0.0545 ? -0.0975 ? 0.0236  ? -0.0345 ? -0.1776 ? -0.0838 ? -0.0450 ? 0.1668  ? 
0.1908  ? 
29 'X-RAY DIFFRACTION' ? refined 2.1372  9.7052   15.6326  0.2641  ? 0.0889  ? 0.0203  ? 0.3638  ? 0.1145  ? 0.5865 ? 2.7498 ? 
-0.8932 ? -0.2883 ? 2.2480 ? 0.7460  ? 2.4406 ? -0.4476 ? 0.4794  ? 1.2386  ? -0.0742 ? 0.5175  ? 0.1990  ? -0.0450 ? 0.8089  ? 
-0.1796 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 47 through 99 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 100 through 212 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 213 through 356 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 357 through 498 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 499 through 591 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 592 through 683 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 26 through 41 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 42 through 61 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 62 through 79 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 80 through 95 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 96 through 114 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 115 through 133 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 134 through 146 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 147 through 185 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 186 through 200 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 1 through 13 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 47 through 395 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 396 through 683 )
;
19 'X-RAY DIFFRACTION' 19 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 26 through 41 )
;
20 'X-RAY DIFFRACTION' 20 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 42 through 61 )
;
21 'X-RAY DIFFRACTION' 21 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 62 through 79 )
;
22 'X-RAY DIFFRACTION' 22 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 80 through 95 )
;
23 'X-RAY DIFFRACTION' 23 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 96 through 114 )
;
24 'X-RAY DIFFRACTION' 24 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 115 through 122 )
;
25 'X-RAY DIFFRACTION' 25 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 123 through 146 )
;
26 'X-RAY DIFFRACTION' 26 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 147 through 170 )
;
27 'X-RAY DIFFRACTION' 27 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 171 through 185 )
;
28 'X-RAY DIFFRACTION' 28 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'E' and (resid 186 through 199 )
;
29 'X-RAY DIFFRACTION' 29 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'F' and (resid 1 through 13 )
;
# 
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 1   ? A MET 1   
2   1 Y 1 A ASN 2   ? A ASN 2   
3   1 Y 1 A LYS 3   ? A LYS 3   
4   1 Y 1 A THR 4   ? A THR 4   
5   1 Y 1 A ASN 5   ? A ASN 5   
6   1 Y 1 A PRO 6   ? A PRO 6   
7   1 Y 1 A GLU 7   ? A GLU 7   
8   1 Y 1 A ARG 8   ? A ARG 8   
9   1 Y 1 A LYS 9   ? A LYS 9   
10  1 Y 1 A ILE 10  ? A ILE 10  
11  1 Y 1 A SER 11  ? A SER 11  
12  1 Y 1 A LEU 12  ? A LEU 12  
13  1 Y 1 A THR 13  ? A THR 13  
14  1 Y 1 A SER 14  ? A SER 14  
15  1 Y 1 A PHE 15  ? A PHE 15  
16  1 Y 1 A LYS 16  ? A LYS 16  
17  1 Y 1 A GLU 17  ? A GLU 17  
18  1 Y 1 A ARG 18  ? A ARG 18  
19  1 Y 1 A MET 19  ? A MET 19  
20  1 Y 1 A ALA 20  ? A ALA 20  
21  1 Y 1 A CYS 21  ? A CYS 21  
22  1 Y 1 A LYS 22  ? A LYS 22  
23  1 Y 1 A GLU 23  ? A GLU 23  
24  1 Y 1 A LYS 24  ? A LYS 24  
25  1 Y 1 A PRO 25  ? A PRO 25  
26  1 Y 1 A ARG 26  ? A ARG 26  
27  1 Y 1 A ASP 27  ? A ASP 27  
28  1 Y 1 A LEU 28  ? A LEU 28  
29  1 Y 1 A GLN 29  ? A GLN 29  
30  1 Y 1 A VAL 30  ? A VAL 30  
31  1 Y 1 A LEU 31  ? A LEU 31  
32  1 Y 1 A LEU 32  ? A LEU 32  
33  1 Y 1 A ILE 33  ? A ILE 33  
34  1 Y 1 A ILE 34  ? A ILE 34  
35  1 Y 1 A SER 35  ? A SER 35  
36  1 Y 1 A ILE 36  ? A ILE 36  
37  1 Y 1 A VAL 37  ? A VAL 37  
38  1 Y 1 A LEU 38  ? A LEU 38  
39  1 Y 1 A SER 39  ? A SER 39  
40  1 Y 1 A CYS 40  ? A CYS 40  
41  1 Y 1 A SER 41  ? A SER 41  
42  1 Y 1 A PHE 42  ? A PHE 42  
43  1 Y 1 A ALA 43  ? A ALA 43  
44  1 Y 1 A VAL 44  ? A VAL 44  
45  1 Y 1 A SER 45  ? A SER 45  
46  1 Y 1 A ALA 46  ? A ALA 46  
47  1 Y 1 B MET 1   ? B MET 1   
48  1 Y 1 B GLU 2   ? B GLU 2   
49  1 Y 1 B ARG 3   ? B ARG 3   
50  1 Y 1 B ARG 4   ? B ARG 4   
51  1 Y 1 B LEU 5   ? B LEU 5   
52  1 Y 1 B MET 6   ? B MET 6   
53  1 Y 1 B ILE 7   ? B ILE 7   
54  1 Y 1 B PRO 8   ? B PRO 8   
55  1 Y 1 B CYS 9   ? B CYS 9   
56  1 Y 1 B PHE 10  ? B PHE 10  
57  1 Y 1 B PHE 11  ? B PHE 11  
58  1 Y 1 B TRP 12  ? B TRP 12  
59  1 Y 1 B LEU 13  ? B LEU 13  
60  1 Y 1 B ILE 14  ? B ILE 14  
61  1 Y 1 B LEU 15  ? B LEU 15  
62  1 Y 1 B VAL 16  ? B VAL 16  
63  1 Y 1 B LEU 17  ? B LEU 17  
64  1 Y 1 B ASP 18  ? B ASP 18  
65  1 Y 1 B LEU 19  ? B LEU 19  
66  1 Y 1 B VAL 20  ? B VAL 20  
67  1 Y 1 B LEU 21  ? B LEU 21  
68  1 Y 1 B ARG 22  ? B ARG 22  
69  1 Y 1 B VAL 23  ? B VAL 23  
70  1 Y 1 B SER 24  ? B SER 24  
71  1 Y 1 B GLY 25  ? B GLY 25  
72  1 Y 1 B PRO 201 ? B PRO 201 
73  1 Y 1 B LEU 202 ? B LEU 202 
74  1 Y 1 B PRO 203 ? B PRO 203 
75  1 Y 1 B ALA 204 ? B ALA 204 
76  1 Y 1 B SER 205 ? B SER 205 
77  1 Y 1 B PRO 206 ? B PRO 206 
78  1 Y 1 B PRO 207 ? B PRO 207 
79  1 Y 1 B PRO 208 ? B PRO 208 
80  1 Y 1 B PRO 209 ? B PRO 209 
81  1 Y 1 B ILE 210 ? B ILE 210 
82  1 Y 1 B SER 211 ? B SER 211 
83  1 Y 1 B PRO 212 ? B PRO 212 
84  1 Y 1 B THR 213 ? B THR 213 
85  1 Y 1 B PRO 214 ? B PRO 214 
86  1 Y 1 B PRO 215 ? B PRO 215 
87  1 Y 1 B SER 216 ? B SER 216 
88  1 Y 1 B PRO 217 ? B PRO 217 
89  1 Y 1 B ALA 218 ? B ALA 218 
90  1 Y 1 B GLY 219 ? B GLY 219 
91  1 Y 1 B SER 220 ? B SER 220 
92  1 Y 1 B HIS 221 ? B HIS 221 
93  1 Y 1 B HIS 222 ? B HIS 222 
94  1 Y 1 B HIS 223 ? B HIS 223 
95  1 Y 1 B HIS 224 ? B HIS 224 
96  1 Y 1 B HIS 225 ? B HIS 225 
97  1 Y 1 B HIS 226 ? B HIS 226 
98  1 Y 1 B HIS 227 ? B HIS 227 
99  1 Y 1 B HIS 228 ? B HIS 228 
100 1 Y 1 B HIS 229 ? B HIS 229 
101 1 Y 1 B HIS 230 ? B HIS 230 
102 1 Y 1 D MET 1   ? D MET 1   
103 1 Y 1 D ASN 2   ? D ASN 2   
104 1 Y 1 D LYS 3   ? D LYS 3   
105 1 Y 1 D THR 4   ? D THR 4   
106 1 Y 1 D ASN 5   ? D ASN 5   
107 1 Y 1 D PRO 6   ? D PRO 6   
108 1 Y 1 D GLU 7   ? D GLU 7   
109 1 Y 1 D ARG 8   ? D ARG 8   
110 1 Y 1 D LYS 9   ? D LYS 9   
111 1 Y 1 D ILE 10  ? D ILE 10  
112 1 Y 1 D SER 11  ? D SER 11  
113 1 Y 1 D LEU 12  ? D LEU 12  
114 1 Y 1 D THR 13  ? D THR 13  
115 1 Y 1 D SER 14  ? D SER 14  
116 1 Y 1 D PHE 15  ? D PHE 15  
117 1 Y 1 D LYS 16  ? D LYS 16  
118 1 Y 1 D GLU 17  ? D GLU 17  
119 1 Y 1 D ARG 18  ? D ARG 18  
120 1 Y 1 D MET 19  ? D MET 19  
121 1 Y 1 D ALA 20  ? D ALA 20  
122 1 Y 1 D CYS 21  ? D CYS 21  
123 1 Y 1 D LYS 22  ? D LYS 22  
124 1 Y 1 D GLU 23  ? D GLU 23  
125 1 Y 1 D LYS 24  ? D LYS 24  
126 1 Y 1 D PRO 25  ? D PRO 25  
127 1 Y 1 D ARG 26  ? D ARG 26  
128 1 Y 1 D ASP 27  ? D ASP 27  
129 1 Y 1 D LEU 28  ? D LEU 28  
130 1 Y 1 D GLN 29  ? D GLN 29  
131 1 Y 1 D VAL 30  ? D VAL 30  
132 1 Y 1 D LEU 31  ? D LEU 31  
133 1 Y 1 D LEU 32  ? D LEU 32  
134 1 Y 1 D ILE 33  ? D ILE 33  
135 1 Y 1 D ILE 34  ? D ILE 34  
136 1 Y 1 D SER 35  ? D SER 35  
137 1 Y 1 D ILE 36  ? D ILE 36  
138 1 Y 1 D VAL 37  ? D VAL 37  
139 1 Y 1 D LEU 38  ? D LEU 38  
140 1 Y 1 D SER 39  ? D SER 39  
141 1 Y 1 D CYS 40  ? D CYS 40  
142 1 Y 1 D SER 41  ? D SER 41  
143 1 Y 1 D PHE 42  ? D PHE 42  
144 1 Y 1 D ALA 43  ? D ALA 43  
145 1 Y 1 D VAL 44  ? D VAL 44  
146 1 Y 1 D SER 45  ? D SER 45  
147 1 Y 1 D ALA 46  ? D ALA 46  
148 1 Y 1 E MET 1   ? E MET 1   
149 1 Y 1 E GLU 2   ? E GLU 2   
150 1 Y 1 E ARG 3   ? E ARG 3   
151 1 Y 1 E ARG 4   ? E ARG 4   
152 1 Y 1 E LEU 5   ? E LEU 5   
153 1 Y 1 E MET 6   ? E MET 6   
154 1 Y 1 E ILE 7   ? E ILE 7   
155 1 Y 1 E PRO 8   ? E PRO 8   
156 1 Y 1 E CYS 9   ? E CYS 9   
157 1 Y 1 E PHE 10  ? E PHE 10  
158 1 Y 1 E PHE 11  ? E PHE 11  
159 1 Y 1 E TRP 12  ? E TRP 12  
160 1 Y 1 E LEU 13  ? E LEU 13  
161 1 Y 1 E ILE 14  ? E ILE 14  
162 1 Y 1 E LEU 15  ? E LEU 15  
163 1 Y 1 E VAL 16  ? E VAL 16  
164 1 Y 1 E LEU 17  ? E LEU 17  
165 1 Y 1 E ASP 18  ? E ASP 18  
166 1 Y 1 E LEU 19  ? E LEU 19  
167 1 Y 1 E VAL 20  ? E VAL 20  
168 1 Y 1 E LEU 21  ? E LEU 21  
169 1 Y 1 E ARG 22  ? E ARG 22  
170 1 Y 1 E VAL 23  ? E VAL 23  
171 1 Y 1 E SER 24  ? E SER 24  
172 1 Y 1 E GLY 25  ? E GLY 25  
173 1 Y 1 E THR 200 ? E THR 200 
174 1 Y 1 E PRO 201 ? E PRO 201 
175 1 Y 1 E LEU 202 ? E LEU 202 
176 1 Y 1 E PRO 203 ? E PRO 203 
177 1 Y 1 E ALA 204 ? E ALA 204 
178 1 Y 1 E SER 205 ? E SER 205 
179 1 Y 1 E PRO 206 ? E PRO 206 
180 1 Y 1 E PRO 207 ? E PRO 207 
181 1 Y 1 E PRO 208 ? E PRO 208 
182 1 Y 1 E PRO 209 ? E PRO 209 
183 1 Y 1 E ILE 210 ? E ILE 210 
184 1 Y 1 E SER 211 ? E SER 211 
185 1 Y 1 E PRO 212 ? E PRO 212 
186 1 Y 1 E THR 213 ? E THR 213 
187 1 Y 1 E PRO 214 ? E PRO 214 
188 1 Y 1 E PRO 215 ? E PRO 215 
189 1 Y 1 E SER 216 ? E SER 216 
190 1 Y 1 E PRO 217 ? E PRO 217 
191 1 Y 1 E ALA 218 ? E ALA 218 
192 1 Y 1 E GLY 219 ? E GLY 219 
193 1 Y 1 E SER 220 ? E SER 220 
194 1 Y 1 E HIS 221 ? E HIS 221 
195 1 Y 1 E HIS 222 ? E HIS 222 
196 1 Y 1 E HIS 223 ? E HIS 223 
197 1 Y 1 E HIS 224 ? E HIS 224 
198 1 Y 1 E HIS 225 ? E HIS 225 
199 1 Y 1 E HIS 226 ? E HIS 226 
200 1 Y 1 E HIS 227 ? E HIS 227 
201 1 Y 1 E HIS 228 ? E HIS 228 
202 1 Y 1 E HIS 229 ? E HIS 229 
203 1 Y 1 E HIS 230 ? E HIS 230 
# 
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 
ILE N    N N N 205 
ILE CA   C N S 206 
ILE C    C N N 207 
ILE O    O N N 208 
ILE CB   C N S 209 
ILE CG1  C N N 210 
ILE CG2  C N N 211 
ILE CD1  C N N 212 
ILE OXT  O N N 213 
ILE H    H N N 214 
ILE H2   H N N 215 
ILE HA   H N N 216 
ILE HB   H N N 217 
ILE HG12 H N N 218 
ILE HG13 H N N 219 
ILE HG21 H N N 220 
ILE HG22 H N N 221 
ILE HG23 H N N 222 
ILE HD11 H N N 223 
ILE HD12 H N N 224 
ILE HD13 H N N 225 
ILE HXT  H N N 226 
LEU N    N N N 227 
LEU CA   C N S 228 
LEU C    C N N 229 
LEU O    O N N 230 
LEU CB   C N N 231 
LEU CG   C N N 232 
LEU CD1  C N N 233 
LEU CD2  C N N 234 
LEU OXT  O N N 235 
LEU H    H N N 236 
LEU H2   H N N 237 
LEU HA   H N N 238 
LEU HB2  H N N 239 
LEU HB3  H N N 240 
LEU HG   H N N 241 
LEU HD11 H N N 242 
LEU HD12 H N N 243 
LEU HD13 H N N 244 
LEU HD21 H N N 245 
LEU HD22 H N N 246 
LEU HD23 H N N 247 
LEU HXT  H N N 248 
LYS N    N N N 249 
LYS CA   C N S 250 
LYS C    C N N 251 
LYS O    O N N 252 
LYS CB   C N N 253 
LYS CG   C N N 254 
LYS CD   C N N 255 
LYS CE   C N N 256 
LYS NZ   N N N 257 
LYS OXT  O N N 258 
LYS H    H N N 259 
LYS H2   H N N 260 
LYS HA   H N N 261 
LYS HB2  H N N 262 
LYS HB3  H N N 263 
LYS HG2  H N N 264 
LYS HG3  H N N 265 
LYS HD2  H N N 266 
LYS HD3  H N N 267 
LYS HE2  H N N 268 
LYS HE3  H N N 269 
LYS HZ1  H N N 270 
LYS HZ2  H N N 271 
LYS HZ3  H N N 272 
LYS HXT  H N N 273 
MET N    N N N 274 
MET CA   C N S 275 
MET C    C N N 276 
MET O    O N N 277 
MET CB   C N N 278 
MET CG   C N N 279 
MET SD   S N N 280 
MET CE   C N N 281 
MET OXT  O N N 282 
MET H    H N N 283 
MET H2   H N N 284 
MET HA   H N N 285 
MET HB2  H N N 286 
MET HB3  H N N 287 
MET HG2  H N N 288 
MET HG3  H N N 289 
MET HE1  H N N 290 
MET HE2  H N N 291 
MET HE3  H N N 292 
MET HXT  H N N 293 
NAG C1   C N R 294 
NAG C2   C N R 295 
NAG C3   C N R 296 
NAG C4   C N S 297 
NAG C5   C N R 298 
NAG C6   C N N 299 
NAG C7   C N N 300 
NAG C8   C N N 301 
NAG N2   N N N 302 
NAG O1   O N N 303 
NAG O3   O N N 304 
NAG O4   O N N 305 
NAG O5   O N N 306 
NAG O6   O N N 307 
NAG O7   O N N 308 
NAG H1   H N N 309 
NAG H2   H N N 310 
NAG H3   H N N 311 
NAG H4   H N N 312 
NAG H5   H N N 313 
NAG H61  H N N 314 
NAG H62  H N N 315 
NAG H81  H N N 316 
NAG H82  H N N 317 
NAG H83  H N N 318 
NAG HN2  H N N 319 
NAG HO1  H N N 320 
NAG HO3  H N N 321 
NAG HO4  H N N 322 
NAG HO6  H N N 323 
PHE N    N N N 324 
PHE CA   C N S 325 
PHE C    C N N 326 
PHE O    O N N 327 
PHE CB   C N N 328 
PHE CG   C Y N 329 
PHE CD1  C Y N 330 
PHE CD2  C Y N 331 
PHE CE1  C Y N 332 
PHE CE2  C Y N 333 
PHE CZ   C Y N 334 
PHE OXT  O N N 335 
PHE H    H N N 336 
PHE H2   H N N 337 
PHE HA   H N N 338 
PHE HB2  H N N 339 
PHE HB3  H N N 340 
PHE HD1  H N N 341 
PHE HD2  H N N 342 
PHE HE1  H N N 343 
PHE HE2  H N N 344 
PHE HZ   H N N 345 
PHE HXT  H N N 346 
PRO N    N N N 347 
PRO CA   C N S 348 
PRO C    C N N 349 
PRO O    O N N 350 
PRO CB   C N N 351 
PRO CG   C N N 352 
PRO CD   C N N 353 
PRO OXT  O N N 354 
PRO H    H N N 355 
PRO HA   H N N 356 
PRO HB2  H N N 357 
PRO HB3  H N N 358 
PRO HG2  H N N 359 
PRO HG3  H N N 360 
PRO HD2  H N N 361 
PRO HD3  H N N 362 
PRO HXT  H N N 363 
SER N    N N N 364 
SER CA   C N S 365 
SER C    C N N 366 
SER O    O N N 367 
SER CB   C N N 368 
SER OG   O N N 369 
SER OXT  O N N 370 
SER H    H N N 371 
SER H2   H N N 372 
SER HA   H N N 373 
SER HB2  H N N 374 
SER HB3  H N N 375 
SER HG   H N N 376 
SER HXT  H N N 377 
THR N    N N N 378 
THR CA   C N S 379 
THR C    C N N 380 
THR O    O N N 381 
THR CB   C N R 382 
THR OG1  O N N 383 
THR CG2  C N N 384 
THR OXT  O N N 385 
THR H    H N N 386 
THR H2   H N N 387 
THR HA   H N N 388 
THR HB   H N N 389 
THR HG1  H N N 390 
THR HG21 H N N 391 
THR HG22 H N N 392 
THR HG23 H N N 393 
THR HXT  H N N 394 
TRP N    N N N 395 
TRP CA   C N S 396 
TRP C    C N N 397 
TRP O    O N N 398 
TRP CB   C N N 399 
TRP CG   C Y N 400 
TRP CD1  C Y N 401 
TRP CD2  C Y N 402 
TRP NE1  N Y N 403 
TRP CE2  C Y N 404 
TRP CE3  C Y N 405 
TRP CZ2  C Y N 406 
TRP CZ3  C Y N 407 
TRP CH2  C Y N 408 
TRP OXT  O N N 409 
TRP H    H N N 410 
TRP H2   H N N 411 
TRP HA   H N N 412 
TRP HB2  H N N 413 
TRP HB3  H N N 414 
TRP HD1  H N N 415 
TRP HE1  H N N 416 
TRP HE3  H N N 417 
TRP HZ2  H N N 418 
TRP HZ3  H N N 419 
TRP HH2  H N N 420 
TRP HXT  H N N 421 
TYR N    N N N 422 
TYR CA   C N S 423 
TYR C    C N N 424 
TYR O    O N N 425 
TYR CB   C N N 426 
TYR CG   C Y N 427 
TYR CD1  C Y N 428 
TYR CD2  C Y N 429 
TYR CE1  C Y N 430 
TYR CE2  C Y N 431 
TYR CZ   C Y N 432 
TYR OH   O N N 433 
TYR OXT  O N N 434 
TYR H    H N N 435 
TYR H2   H N N 436 
TYR HA   H N N 437 
TYR HB2  H N N 438 
TYR HB3  H N N 439 
TYR HD1  H N N 440 
TYR HD2  H N N 441 
TYR HE1  H N N 442 
TYR HE2  H N N 443 
TYR HH   H N N 444 
TYR HXT  H N N 445 
VAL N    N N N 446 
VAL CA   C N S 447 
VAL C    C N N 448 
VAL O    O N N 449 
VAL CB   C N N 450 
VAL CG1  C N N 451 
VAL CG2  C N N 452 
VAL OXT  O N N 453 
VAL H    H N N 454 
VAL H2   H N N 455 
VAL HA   H N N 456 
VAL HB   H N N 457 
VAL HG11 H N N 458 
VAL HG12 H N N 459 
VAL HG13 H N N 460 
VAL HG21 H N N 461 
VAL HG22 H N N 462 
VAL HG23 H N N 463 
VAL HXT  H N N 464 
# 
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 
ILE N   CA   sing N N 197 
ILE N   H    sing N N 198 
ILE N   H2   sing N N 199 
ILE CA  C    sing N N 200 
ILE CA  CB   sing N N 201 
ILE CA  HA   sing N N 202 
ILE C   O    doub N N 203 
ILE C   OXT  sing N N 204 
ILE CB  CG1  sing N N 205 
ILE CB  CG2  sing N N 206 
ILE CB  HB   sing N N 207 
ILE CG1 CD1  sing N N 208 
ILE CG1 HG12 sing N N 209 
ILE CG1 HG13 sing N N 210 
ILE CG2 HG21 sing N N 211 
ILE CG2 HG22 sing N N 212 
ILE CG2 HG23 sing N N 213 
ILE CD1 HD11 sing N N 214 
ILE CD1 HD12 sing N N 215 
ILE CD1 HD13 sing N N 216 
ILE OXT HXT  sing N N 217 
LEU N   CA   sing N N 218 
LEU N   H    sing N N 219 
LEU N   H2   sing N N 220 
LEU CA  C    sing N N 221 
LEU CA  CB   sing N N 222 
LEU CA  HA   sing N N 223 
LEU C   O    doub N N 224 
LEU C   OXT  sing N N 225 
LEU CB  CG   sing N N 226 
LEU CB  HB2  sing N N 227 
LEU CB  HB3  sing N N 228 
LEU CG  CD1  sing N N 229 
LEU CG  CD2  sing N N 230 
LEU CG  HG   sing N N 231 
LEU CD1 HD11 sing N N 232 
LEU CD1 HD12 sing N N 233 
LEU CD1 HD13 sing N N 234 
LEU CD2 HD21 sing N N 235 
LEU CD2 HD22 sing N N 236 
LEU CD2 HD23 sing N N 237 
LEU OXT HXT  sing N N 238 
LYS N   CA   sing N N 239 
LYS N   H    sing N N 240 
LYS N   H2   sing N N 241 
LYS CA  C    sing N N 242 
LYS CA  CB   sing N N 243 
LYS CA  HA   sing N N 244 
LYS C   O    doub N N 245 
LYS C   OXT  sing N N 246 
LYS CB  CG   sing N N 247 
LYS CB  HB2  sing N N 248 
LYS CB  HB3  sing N N 249 
LYS CG  CD   sing N N 250 
LYS CG  HG2  sing N N 251 
LYS CG  HG3  sing N N 252 
LYS CD  CE   sing N N 253 
LYS CD  HD2  sing N N 254 
LYS CD  HD3  sing N N 255 
LYS CE  NZ   sing N N 256 
LYS CE  HE2  sing N N 257 
LYS CE  HE3  sing N N 258 
LYS NZ  HZ1  sing N N 259 
LYS NZ  HZ2  sing N N 260 
LYS NZ  HZ3  sing N N 261 
LYS OXT HXT  sing N N 262 
MET N   CA   sing N N 263 
MET N   H    sing N N 264 
MET N   H2   sing N N 265 
MET CA  C    sing N N 266 
MET CA  CB   sing N N 267 
MET CA  HA   sing N N 268 
MET C   O    doub N N 269 
MET C   OXT  sing N N 270 
MET CB  CG   sing N N 271 
MET CB  HB2  sing N N 272 
MET CB  HB3  sing N N 273 
MET CG  SD   sing N N 274 
MET CG  HG2  sing N N 275 
MET CG  HG3  sing N N 276 
MET SD  CE   sing N N 277 
MET CE  HE1  sing N N 278 
MET CE  HE2  sing N N 279 
MET CE  HE3  sing N N 280 
MET OXT HXT  sing N N 281 
NAG C1  C2   sing N N 282 
NAG C1  O1   sing N N 283 
NAG C1  O5   sing N N 284 
NAG C1  H1   sing N N 285 
NAG C2  C3   sing N N 286 
NAG C2  N2   sing N N 287 
NAG C2  H2   sing N N 288 
NAG C3  C4   sing N N 289 
NAG C3  O3   sing N N 290 
NAG C3  H3   sing N N 291 
NAG C4  C5   sing N N 292 
NAG C4  O4   sing N N 293 
NAG C4  H4   sing N N 294 
NAG C5  C6   sing N N 295 
NAG C5  O5   sing N N 296 
NAG C5  H5   sing N N 297 
NAG C6  O6   sing N N 298 
NAG C6  H61  sing N N 299 
NAG C6  H62  sing N N 300 
NAG C7  C8   sing N N 301 
NAG C7  N2   sing N N 302 
NAG C7  O7   doub N N 303 
NAG C8  H81  sing N N 304 
NAG C8  H82  sing N N 305 
NAG C8  H83  sing N N 306 
NAG N2  HN2  sing N N 307 
NAG O1  HO1  sing N N 308 
NAG O3  HO3  sing N N 309 
NAG O4  HO4  sing N N 310 
NAG O6  HO6  sing N N 311 
PHE N   CA   sing N N 312 
PHE N   H    sing N N 313 
PHE N   H2   sing N N 314 
PHE CA  C    sing N N 315 
PHE CA  CB   sing N N 316 
PHE CA  HA   sing N N 317 
PHE C   O    doub N N 318 
PHE C   OXT  sing N N 319 
PHE CB  CG   sing N N 320 
PHE CB  HB2  sing N N 321 
PHE CB  HB3  sing N N 322 
PHE CG  CD1  doub Y N 323 
PHE CG  CD2  sing Y N 324 
PHE CD1 CE1  sing Y N 325 
PHE CD1 HD1  sing N N 326 
PHE CD2 CE2  doub Y N 327 
PHE CD2 HD2  sing N N 328 
PHE CE1 CZ   doub Y N 329 
PHE CE1 HE1  sing N N 330 
PHE CE2 CZ   sing Y N 331 
PHE CE2 HE2  sing N N 332 
PHE CZ  HZ   sing N N 333 
PHE OXT HXT  sing N N 334 
PRO N   CA   sing N N 335 
PRO N   CD   sing N N 336 
PRO N   H    sing N N 337 
PRO CA  C    sing N N 338 
PRO CA  CB   sing N N 339 
PRO CA  HA   sing N N 340 
PRO C   O    doub N N 341 
PRO C   OXT  sing N N 342 
PRO CB  CG   sing N N 343 
PRO CB  HB2  sing N N 344 
PRO CB  HB3  sing N N 345 
PRO CG  CD   sing N N 346 
PRO CG  HG2  sing N N 347 
PRO CG  HG3  sing N N 348 
PRO CD  HD2  sing N N 349 
PRO CD  HD3  sing N N 350 
PRO OXT HXT  sing N N 351 
SER N   CA   sing N N 352 
SER N   H    sing N N 353 
SER N   H2   sing N N 354 
SER CA  C    sing N N 355 
SER CA  CB   sing N N 356 
SER CA  HA   sing N N 357 
SER C   O    doub N N 358 
SER C   OXT  sing N N 359 
SER CB  OG   sing N N 360 
SER CB  HB2  sing N N 361 
SER CB  HB3  sing N N 362 
SER OG  HG   sing N N 363 
SER OXT HXT  sing N N 364 
THR N   CA   sing N N 365 
THR N   H    sing N N 366 
THR N   H2   sing N N 367 
THR CA  C    sing N N 368 
THR CA  CB   sing N N 369 
THR CA  HA   sing N N 370 
THR C   O    doub N N 371 
THR C   OXT  sing N N 372 
THR CB  OG1  sing N N 373 
THR CB  CG2  sing N N 374 
THR CB  HB   sing N N 375 
THR OG1 HG1  sing N N 376 
THR CG2 HG21 sing N N 377 
THR CG2 HG22 sing N N 378 
THR CG2 HG23 sing N N 379 
THR OXT HXT  sing N N 380 
TRP N   CA   sing N N 381 
TRP N   H    sing N N 382 
TRP N   H2   sing N N 383 
TRP CA  C    sing N N 384 
TRP CA  CB   sing N N 385 
TRP CA  HA   sing N N 386 
TRP C   O    doub N N 387 
TRP C   OXT  sing N N 388 
TRP CB  CG   sing N N 389 
TRP CB  HB2  sing N N 390 
TRP CB  HB3  sing N N 391 
TRP CG  CD1  doub Y N 392 
TRP CG  CD2  sing Y N 393 
TRP CD1 NE1  sing Y N 394 
TRP CD1 HD1  sing N N 395 
TRP CD2 CE2  doub Y N 396 
TRP CD2 CE3  sing Y N 397 
TRP NE1 CE2  sing Y N 398 
TRP NE1 HE1  sing N N 399 
TRP CE2 CZ2  sing Y N 400 
TRP CE3 CZ3  doub Y N 401 
TRP CE3 HE3  sing N N 402 
TRP CZ2 CH2  doub Y N 403 
TRP CZ2 HZ2  sing N N 404 
TRP CZ3 CH2  sing Y N 405 
TRP CZ3 HZ3  sing N N 406 
TRP CH2 HH2  sing N N 407 
TRP OXT HXT  sing N N 408 
TYR N   CA   sing N N 409 
TYR N   H    sing N N 410 
TYR N   H2   sing N N 411 
TYR CA  C    sing N N 412 
TYR CA  CB   sing N N 413 
TYR CA  HA   sing N N 414 
TYR C   O    doub N N 415 
TYR C   OXT  sing N N 416 
TYR CB  CG   sing N N 417 
TYR CB  HB2  sing N N 418 
TYR CB  HB3  sing N N 419 
TYR CG  CD1  doub Y N 420 
TYR CG  CD2  sing Y N 421 
TYR CD1 CE1  sing Y N 422 
TYR CD1 HD1  sing N N 423 
TYR CD2 CE2  doub Y N 424 
TYR CD2 HD2  sing N N 425 
TYR CE1 CZ   doub Y N 426 
TYR CE1 HE1  sing N N 427 
TYR CE2 CZ   sing Y N 428 
TYR CE2 HE2  sing N N 429 
TYR CZ  OH   sing N N 430 
TYR OH  HH   sing N N 431 
TYR OXT HXT  sing N N 432 
VAL N   CA   sing N N 433 
VAL N   H    sing N N 434 
VAL N   H2   sing N N 435 
VAL CA  C    sing N N 436 
VAL CA  CB   sing N N 437 
VAL CA  HA   sing N N 438 
VAL C   O    doub N N 439 
VAL C   OXT  sing N N 440 
VAL CB  CG1  sing N N 441 
VAL CB  CG2  sing N N 442 
VAL CB  HB   sing N N 443 
VAL CG1 HG11 sing N N 444 
VAL CG1 HG12 sing N N 445 
VAL CG1 HG13 sing N N 446 
VAL CG2 HG21 sing N N 447 
VAL CG2 HG22 sing N N 448 
VAL CG2 HG23 sing N N 449 
VAL OXT HXT  sing N N 450 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32000900 
_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 
4 NAG 1 n 
4 FUC 2 n 
4 NAG 3 n 
4 FUC 4 n 
5 NAG 1 n 
5 NAG 2 n 
6 NAG 1 n 
6 NAG 2 n 
6 FUC 3 n 
7 NAG 1 n 
7 NAG 2 n 
7 BMA 3 n 
8 NAG 1 n 
8 NAG 2 n 
8 BMA 3 n 
8 FUC 4 n 
9 NAG 1 n 
9 FUC 2 n 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8WED 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.013760 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000026 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005614 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.007029 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . THR A  1  47  ? 40.202  -44.187 123.448 1.00 50.10  ?  47   THR A N   1 
ATOM   2     C CA  . THR A  1  47  ? 38.933  -43.928 122.780 1.00 49.49  ?  47   THR A CA  1 
ATOM   3     C C   . THR A  1  47  ? 38.109  -42.948 123.596 1.00 52.16  ?  47   THR A C   1 
ATOM   4     O O   . THR A  1  47  ? 37.774  -41.858 123.133 1.00 53.18  ?  47   THR A O   1 
ATOM   5     C CB  . THR A  1  47  ? 38.114  -45.206 122.600 1.00 51.41  ?  47   THR A CB  1 
ATOM   6     O OG1 . THR A  1  47  ? 37.370  -45.461 123.797 1.00 55.31  ?  47   THR A OG1 1 
ATOM   7     C CG2 . THR A  1  47  ? 39.032  -46.379 122.374 1.00 50.81  ?  47   THR A CG2 1 
ATOM   8     N N   . VAL A  1  48  ? 37.790  -43.359 124.824 1.00 46.66  ?  48   VAL A N   1 
ATOM   9     C CA  . VAL A  1  48  ? 36.992  -42.522 125.714 1.00 50.29  ?  48   VAL A CA  1 
ATOM   10    C C   . VAL A  1  48  ? 37.732  -41.229 126.026 1.00 50.68  ?  48   VAL A C   1 
ATOM   11    O O   . VAL A  1  48  ? 37.137  -40.144 126.052 1.00 53.19  ?  48   VAL A O   1 
ATOM   12    C CB  . VAL A  1  48  ? 36.634  -43.303 126.993 1.00 52.49  ?  48   VAL A CB  1 
ATOM   13    C CG1 . VAL A  1  48  ? 36.287  -42.354 128.129 1.00 55.66  ?  48   VAL A CG1 1 
ATOM   14    C CG2 . VAL A  1  48  ? 35.482  -44.262 126.722 1.00 53.71  ?  48   VAL A CG2 1 
ATOM   15    N N   . GLU A  1  49  ? 39.044  -41.319 126.250 1.00 51.74  ?  49   GLU A N   1 
ATOM   16    C CA  . GLU A  1  49  ? 39.841  -40.111 126.424 1.00 51.95  ?  49   GLU A CA  1 
ATOM   17    C C   . GLU A  1  49  ? 39.939  -39.328 125.120 1.00 48.54  ?  49   GLU A C   1 
ATOM   18    O O   . GLU A  1  49  ? 39.923  -38.092 125.130 1.00 48.11  ?  49   GLU A O   1 
ATOM   19    C CB  . GLU A  1  49  ? 41.232  -40.471 126.945 1.00 51.58  ?  49   GLU A CB  1 
ATOM   20    C CG  . GLU A  1  49  ? 41.240  -41.033 128.357 1.00 55.14  ?  49   GLU A CG  1 
ATOM   21    C CD  . GLU A  1  49  ? 41.135  -42.546 128.386 1.00 56.18  ?  49   GLU A CD  1 
ATOM   22    O OE1 . GLU A  1  49  ? 41.836  -43.208 127.592 1.00 54.74  ?  49   GLU A OE1 1 
ATOM   23    O OE2 . GLU A  1  49  ? 40.350  -43.074 129.201 1.00 58.75  -1 49   GLU A OE2 1 
ATOM   24    N N   . GLU A  1  50  ? 40.037  -40.029 123.988 1.00 48.56  ?  50   GLU A N   1 
ATOM   25    C CA  . GLU A  1  50  ? 40.079  -39.352 122.695 1.00 45.05  ?  50   GLU A CA  1 
ATOM   26    C C   . GLU A  1  50  ? 38.736  -38.709 122.365 1.00 46.61  ?  50   GLU A C   1 
ATOM   27    O O   . GLU A  1  50  ? 38.676  -37.535 121.980 1.00 45.47  ?  50   GLU A O   1 
ATOM   28    C CB  . GLU A  1  50  ? 40.485  -40.338 121.597 1.00 43.14  ?  50   GLU A CB  1 
ATOM   29    C CG  . GLU A  1  50  ? 41.885  -40.914 121.749 1.00 43.35  ?  50   GLU A CG  1 
ATOM   30    C CD  . GLU A  1  50  ? 42.201  -41.964 120.699 1.00 42.12  ?  50   GLU A CD  1 
ATOM   31    O OE1 . GLU A  1  50  ? 41.301  -42.766 120.368 1.00 42.46  ?  50   GLU A OE1 1 
ATOM   32    O OE2 . GLU A  1  50  ? 43.345  -41.986 120.198 1.00 40.60  -1 50   GLU A OE2 1 
ATOM   33    N N   . ALA A  1  51  ? 37.645  -39.468 122.504 1.00 43.92  ?  51   ALA A N   1 
ATOM   34    C CA  . ALA A  1  51  ? 36.325  -38.952 122.150 1.00 46.35  ?  51   ALA A CA  1 
ATOM   35    C C   . ALA A  1  51  ? 35.933  -37.769 123.025 1.00 49.04  ?  51   ALA A C   1 
ATOM   36    O O   . ALA A  1  51  ? 35.419  -36.761 122.526 1.00 48.75  ?  51   ALA A O   1 
ATOM   37    C CB  . ALA A  1  51  ? 35.279  -40.061 122.254 1.00 49.66  ?  51   ALA A CB  1 
ATOM   38    N N   . ASN A  1  52  ? 36.156  -37.879 124.337 1.00 45.36  ?  52   ASN A N   1 
ATOM   39    C CA  . ASN A  1  52  ? 35.841  -36.772 125.234 1.00 47.89  ?  52   ASN A CA  1 
ATOM   40    C C   . ASN A  1  52  ? 36.682  -35.543 124.917 1.00 43.84  ?  52   ASN A C   1 
ATOM   41    O O   . ASN A  1  52  ? 36.206  -34.411 125.059 1.00 44.07  ?  52   ASN A O   1 
ATOM   42    C CB  . ASN A  1  52  ? 36.040  -37.201 126.687 1.00 51.71  ?  52   ASN A CB  1 
ATOM   43    C CG  . ASN A  1  52  ? 34.881  -38.025 127.215 1.00 55.44  ?  52   ASN A CG  1 
ATOM   44    O OD1 . ASN A  1  52  ? 33.717  -37.711 126.964 1.00 58.60  ?  52   ASN A OD1 1 
ATOM   45    N ND2 . ASN A  1  52  ? 35.194  -39.088 127.946 1.00 54.65  ?  52   ASN A ND2 1 
ATOM   46    N N   . ALA A  1  53  ? 37.933  -35.744 124.498 1.00 44.13  ?  53   ALA A N   1 
ATOM   47    C CA  . ALA A  1  53  ? 38.775  -34.617 124.114 1.00 43.03  ?  53   ALA A CA  1 
ATOM   48    C C   . ALA A  1  53  ? 38.280  -33.965 122.827 1.00 41.47  ?  53   ALA A C   1 
ATOM   49    O O   . ALA A  1  53  ? 38.280  -32.734 122.711 1.00 41.52  ?  53   ALA A O   1 
ATOM   50    C CB  . ALA A  1  53  ? 40.223  -35.077 123.970 1.00 42.14  ?  53   ALA A CB  1 
ATOM   51    N N   . LEU A  1  54  ? 37.862  -34.772 121.846 1.00 42.18  ?  54   LEU A N   1 
ATOM   52    C CA  . LEU A  1  54  ? 37.247  -34.211 120.645 1.00 41.08  ?  54   LEU A CA  1 
ATOM   53    C C   . LEU A  1  54  ? 35.956  -33.481 120.983 1.00 43.84  ?  54   LEU A C   1 
ATOM   54    O O   . LEU A  1  54  ? 35.709  -32.375 120.485 1.00 42.70  ?  54   LEU A O   1 
ATOM   55    C CB  . LEU A  1  54  ? 36.969  -35.309 119.618 1.00 41.02  ?  54   LEU A CB  1 
ATOM   56    C CG  . LEU A  1  54  ? 38.002  -35.555 118.518 1.00 37.78  ?  54   LEU A CG  1 
ATOM   57    C CD1 . LEU A  1  54  ? 38.287  -34.278 117.742 1.00 37.25  ?  54   LEU A CD1 1 
ATOM   58    C CD2 . LEU A  1  54  ? 39.265  -36.121 119.110 1.00 37.49  ?  54   LEU A CD2 1 
ATOM   59    N N   . LEU A  1  55  ? 35.117  -34.090 121.825 1.00 40.58  ?  55   LEU A N   1 
ATOM   60    C CA  . LEU A  1  55  ? 33.874  -33.448 122.235 1.00 42.47  ?  55   LEU A CA  1 
ATOM   61    C C   . LEU A  1  55  ? 34.138  -32.115 122.920 1.00 43.33  ?  55   LEU A C   1 
ATOM   62    O O   . LEU A  1  55  ? 33.353  -31.172 122.768 1.00 44.25  ?  55   LEU A O   1 
ATOM   63    C CB  . LEU A  1  55  ? 33.089  -34.380 123.158 1.00 44.92  ?  55   LEU A CB  1 
ATOM   64    C CG  . LEU A  1  55  ? 31.976  -35.196 122.498 1.00 46.73  ?  55   LEU A CG  1 
ATOM   65    C CD1 . LEU A  1  55  ? 31.592  -36.384 123.367 1.00 50.41  ?  55   LEU A CD1 1 
ATOM   66    C CD2 . LEU A  1  55  ? 30.765  -34.320 122.210 1.00 48.18  ?  55   LEU A CD2 1 
ATOM   67    N N   . LYS A  1  56  ? 35.236  -32.015 123.673 1.00 42.43  ?  56   LYS A N   1 
ATOM   68    C CA  . LYS A  1  56  ? 35.604  -30.738 124.274 1.00 43.22  ?  56   LYS A CA  1 
ATOM   69    C C   . LYS A  1  56  ? 36.035  -29.736 123.210 1.00 41.77  ?  56   LYS A C   1 
ATOM   70    O O   . LYS A  1  56  ? 35.708  -28.546 123.301 1.00 42.62  ?  56   LYS A O   1 
ATOM   71    C CB  . LYS A  1  56  ? 36.714  -30.946 125.305 1.00 43.78  ?  56   LYS A CB  1 
ATOM   72    C CG  . LYS A  1  56  ? 37.518  -29.697 125.626 1.00 44.00  ?  56   LYS A CG  1 
ATOM   73    C CD  . LYS A  1  56  ? 37.852  -29.625 127.104 1.00 46.18  ?  56   LYS A CD  1 
ATOM   74    C CE  . LYS A  1  56  ? 38.952  -28.615 127.374 1.00 46.29  ?  56   LYS A CE  1 
ATOM   75    N NZ  . LYS A  1  56  ? 38.712  -27.874 128.640 1.00 48.80  ?  56   LYS A NZ  1 
ATOM   76    N N   . TRP A  1  57  ? 36.766  -30.197 122.191 1.00 42.64  ?  57   TRP A N   1 
ATOM   77    C CA  . TRP A  1  57  ? 37.163  -29.304 121.106 1.00 41.57  ?  57   TRP A CA  1 
ATOM   78    C C   . TRP A  1  57  ? 35.955  -28.842 120.300 1.00 42.05  ?  57   TRP A C   1 
ATOM   79    O O   . TRP A  1  57  ? 35.899  -27.686 119.866 1.00 42.41  ?  57   TRP A O   1 
ATOM   80    C CB  . TRP A  1  57  ? 38.179  -29.993 120.198 1.00 39.69  ?  57   TRP A CB  1 
ATOM   81    C CG  . TRP A  1  57  ? 38.610  -29.137 119.045 1.00 38.90  ?  57   TRP A CG  1 
ATOM   82    C CD1 . TRP A  1  57  ? 39.072  -27.854 119.105 1.00 39.45  ?  57   TRP A CD1 1 
ATOM   83    C CD2 . TRP A  1  57  ? 38.616  -29.501 117.660 1.00 37.74  ?  57   TRP A CD2 1 
ATOM   84    N NE1 . TRP A  1  57  ? 39.366  -27.397 117.844 1.00 38.81  ?  57   TRP A NE1 1 
ATOM   85    C CE2 . TRP A  1  57  ? 39.095  -28.390 116.939 1.00 37.79  ?  57   TRP A CE2 1 
ATOM   86    C CE3 . TRP A  1  57  ? 38.264  -30.659 116.960 1.00 36.88  ?  57   TRP A CE3 1 
ATOM   87    C CZ2 . TRP A  1  57  ? 39.231  -28.402 115.553 1.00 37.13  ?  57   TRP A CZ2 1 
ATOM   88    C CZ3 . TRP A  1  57  ? 38.399  -30.669 115.585 1.00 36.10  ?  57   TRP A CZ3 1 
ATOM   89    C CH2 . TRP A  1  57  ? 38.878  -29.549 114.895 1.00 36.30  ?  57   TRP A CH2 1 
ATOM   90    N N   . LYS A  1  58  ? 34.991  -29.738 120.069 1.00 40.63  ?  58   LYS A N   1 
ATOM   91    C CA  . LYS A  1  58  ? 33.767  -29.349 119.375 1.00 41.59  ?  58   LYS A CA  1 
ATOM   92    C C   . LYS A  1  58  ? 33.029  -28.243 120.119 1.00 43.62  ?  58   LYS A C   1 
ATOM   93    O O   . LYS A  1  58  ? 32.391  -27.391 119.489 1.00 44.49  ?  58   LYS A O   1 
ATOM   94    C CB  . LYS A  1  58  ? 32.859  -30.565 119.190 1.00 41.91  ?  58   LYS A CB  1 
ATOM   95    C CG  . LYS A  1  58  ? 31.549  -30.263 118.481 1.00 43.29  ?  58   LYS A CG  1 
ATOM   96    C CD  . LYS A  1  58  ? 30.582  -31.431 118.581 1.00 47.35  ?  58   LYS A CD  1 
ATOM   97    C CE  . LYS A  1  58  ? 29.138  -30.956 118.545 1.00 50.54  ?  58   LYS A CE  1 
ATOM   98    N NZ  . LYS A  1  58  ? 28.186  -32.027 118.951 1.00 55.28  ?  58   LYS A NZ  1 
ATOM   99    N N   . SER A  1  59  ? 33.104  -28.240 121.453 1.00 43.90  ?  59   SER A N   1 
ATOM   100   C CA  . SER A  1  59  ? 32.451  -27.199 122.241 1.00 45.99  ?  59   SER A CA  1 
ATOM   101   C C   . SER A  1  59  ? 32.963  -25.810 121.883 1.00 45.86  ?  59   SER A C   1 
ATOM   102   O O   . SER A  1  59  ? 32.226  -24.824 122.006 1.00 47.52  ?  59   SER A O   1 
ATOM   103   C CB  . SER A  1  59  ? 32.654  -27.474 123.731 1.00 47.17  ?  59   SER A CB  1 
ATOM   104   O OG  . SER A  1  59  ? 32.351  -26.331 124.512 1.00 48.99  ?  59   SER A OG  1 
ATOM   105   N N   . THR A  1  60  ? 34.219  -25.712 121.440 1.00 45.87  ?  60   THR A N   1 
ATOM   106   C CA  . THR A  1  60  ? 34.790  -24.425 121.056 1.00 45.90  ?  60   THR A CA  1 
ATOM   107   C C   . THR A  1  60  ? 34.086  -23.830 119.837 1.00 46.31  ?  60   THR A C   1 
ATOM   108   O O   . THR A  1  60  ? 34.046  -22.602 119.684 1.00 47.35  ?  60   THR A O   1 
ATOM   109   C CB  . THR A  1  60  ? 36.293  -24.600 120.800 1.00 44.20  ?  60   THR A CB  1 
ATOM   110   O OG1 . THR A  1  60  ? 36.989  -24.627 122.053 1.00 44.64  ?  60   THR A OG1 1 
ATOM   111   C CG2 . THR A  1  60  ? 36.868  -23.482 119.933 1.00 44.05  ?  60   THR A CG2 1 
ATOM   112   N N   . PHE A  1  61  ? 33.479  -24.672 118.999 1.00 45.53  ?  61   PHE A N   1 
ATOM   113   C CA  . PHE A  1  61  ? 32.962  -24.219 117.712 1.00 46.02  ?  61   PHE A CA  1 
ATOM   114   C C   . PHE A  1  61  ? 31.859  -23.182 117.895 1.00 48.48  ?  61   PHE A C   1 
ATOM   115   O O   . PHE A  1  61  ? 30.998  -23.308 118.771 1.00 49.86  ?  61   PHE A O   1 
ATOM   116   C CB  . PHE A  1  61  ? 32.435  -25.409 116.908 1.00 45.40  ?  61   PHE A CB  1 
ATOM   117   C CG  . PHE A  1  61  ? 33.486  -26.435 116.582 1.00 43.12  ?  61   PHE A CG  1 
ATOM   118   C CD1 . PHE A  1  61  ? 34.834  -26.127 116.671 1.00 41.89  ?  61   PHE A CD1 1 
ATOM   119   C CD2 . PHE A  1  61  ? 33.122  -27.713 116.193 1.00 42.44  ?  61   PHE A CD2 1 
ATOM   120   C CE1 . PHE A  1  61  ? 35.798  -27.072 116.376 1.00 40.06  ?  61   PHE A CE1 1 
ATOM   121   C CE2 . PHE A  1  61  ? 34.082  -28.661 115.896 1.00 40.49  ?  61   PHE A CE2 1 
ATOM   122   C CZ  . PHE A  1  61  ? 35.420  -28.341 115.988 1.00 39.32  ?  61   PHE A CZ  1 
ATOM   123   N N   . THR A  1  62  ? 31.891  -22.151 117.055 1.00 48.49  ?  62   THR A N   1 
ATOM   124   C CA  . THR A  1  62  ? 30.943  -21.049 117.107 1.00 51.03  ?  62   THR A CA  1 
ATOM   125   C C   . THR A  1  62  ? 30.062  -21.043 115.864 1.00 52.37  ?  62   THR A C   1 
ATOM   126   O O   . THR A  1  62  ? 30.430  -21.571 114.810 1.00 51.29  ?  62   THR A O   1 
ATOM   127   C CB  . THR A  1  62  ? 31.671  -19.706 117.231 1.00 51.54  ?  62   THR A CB  1 
ATOM   128   O OG1 . THR A  1  62  ? 32.114  -19.283 115.936 1.00 51.48  ?  62   THR A OG1 1 
ATOM   129   C CG2 . THR A  1  62  ? 32.874  -19.835 118.150 1.00 49.92  ?  62   THR A CG2 1 
ATOM   130   N N   . ASN A  1  63  ? 28.885  -20.429 116.006 1.00 55.96  ?  63   ASN A N   1 
ATOM   131   C CA  . ASN A  1  63  ? 27.924  -20.281 114.910 1.00 58.01  ?  63   ASN A CA  1 
ATOM   132   C C   . ASN A  1  63  ? 27.584  -21.631 114.284 1.00 57.15  ?  63   ASN A C   1 
ATOM   133   O O   . ASN A  1  63  ? 27.432  -21.759 113.067 1.00 57.67  ?  63   ASN A O   1 
ATOM   134   C CB  . ASN A  1  63  ? 28.439  -19.302 113.852 1.00 58.68  ?  63   ASN A CB  1 
ATOM   135   C CG  . ASN A  1  63  ? 28.446  -17.866 114.339 1.00 60.45  ?  63   ASN A CG  1 
ATOM   136   O OD1 . ASN A  1  63  ? 28.403  -17.605 115.541 1.00 60.50  ?  63   ASN A OD1 1 
ATOM   137   N ND2 . ASN A  1  63  ? 28.499  -16.925 113.403 1.00 62.17  ?  63   ASN A ND2 1 
ATOM   138   N N   . GLN A  1  64  ? 27.464  -22.651 115.128 1.00 63.48  ?  64   GLN A N   1 
ATOM   139   C CA  . GLN A  1  64  ? 27.187  -24.011 114.687 1.00 62.47  ?  64   GLN A CA  1 
ATOM   140   C C   . GLN A  1  64  ? 25.691  -24.283 114.768 1.00 65.09  ?  64   GLN A C   1 
ATOM   141   O O   . GLN A  1  64  ? 25.053  -23.976 115.781 1.00 66.54  ?  64   GLN A O   1 
ATOM   142   C CB  . GLN A  1  64  ? 27.961  -25.022 115.534 1.00 60.30  ?  64   GLN A CB  1 
ATOM   143   C CG  . GLN A  1  64  ? 28.380  -26.274 114.780 1.00 58.86  ?  64   GLN A CG  1 
ATOM   144   C CD  . GLN A  1  64  ? 29.463  -26.002 113.754 1.00 56.72  ?  64   GLN A CD  1 
ATOM   145   O OE1 . GLN A  1  64  ? 30.577  -25.607 114.099 1.00 54.81  ?  64   GLN A OE1 1 
ATOM   146   N NE2 . GLN A  1  64  ? 29.142  -26.215 112.483 1.00 57.31  ?  64   GLN A NE2 1 
ATOM   147   N N   . THR A  1  65  ? 25.139  -24.856 113.704 1.00 64.27  ?  65   THR A N   1 
ATOM   148   C CA  . THR A  1  65  ? 23.721  -25.169 113.615 1.00 67.11  ?  65   THR A CA  1 
ATOM   149   C C   . THR A  1  65  ? 23.469  -26.627 113.984 1.00 65.93  ?  65   THR A C   1 
ATOM   150   O O   . THR A  1  65  ? 24.348  -27.484 113.874 1.00 63.24  ?  65   THR A O   1 
ATOM   151   C CB  . THR A  1  65  ? 23.186  -24.888 112.208 1.00 69.00  ?  65   THR A CB  1 
ATOM   152   O OG1 . THR A  1  65  ? 23.484  -25.996 111.350 1.00 67.93  ?  65   THR A OG1 1 
ATOM   153   C CG2 . THR A  1  65  ? 23.816  -23.625 111.640 1.00 69.58  ?  65   THR A CG2 1 
ATOM   154   N N   . SER A  1  66  ? 22.238  -26.898 114.428 1.00 65.13  ?  66   SER A N   1 
ATOM   155   C CA  . SER A  1  66  ? 21.863  -28.252 114.818 1.00 67.51  ?  66   SER A CA  1 
ATOM   156   C C   . SER A  1  66  ? 21.840  -29.214 113.636 1.00 67.60  ?  66   SER A C   1 
ATOM   157   O O   . SER A  1  66  ? 21.814  -30.431 113.845 1.00 68.79  ?  66   SER A O   1 
ATOM   158   C CB  . SER A  1  66  ? 20.498  -28.240 115.506 1.00 71.30  ?  66   SER A CB  1 
ATOM   159   O OG  . SER A  1  66  ? 19.523  -27.607 114.697 1.00 73.22  ?  66   SER A OG  1 
ATOM   160   N N   . SER A  1  67  ? 21.848  -28.699 112.408 1.00 65.54  ?  67   SER A N   1 
ATOM   161   C CA  . SER A  1  67  ? 21.875  -29.518 111.204 1.00 65.54  ?  67   SER A CA  1 
ATOM   162   C C   . SER A  1  67  ? 23.288  -29.924 110.798 1.00 62.04  ?  67   SER A C   1 
ATOM   163   O O   . SER A  1  67  ? 23.463  -30.529 109.735 1.00 61.75  ?  67   SER A O   1 
ATOM   164   C CB  . SER A  1  67  ? 21.191  -28.779 110.050 1.00 66.83  ?  67   SER A CB  1 
ATOM   165   O OG  . SER A  1  67  ? 21.886  -27.588 109.722 1.00 66.61  ?  67   SER A OG  1 
ATOM   166   N N   . SER A  1  68  ? 24.291  -29.597 111.608 1.00 60.26  ?  68   SER A N   1 
ATOM   167   C CA  . SER A  1  68  ? 25.672  -29.911 111.268 1.00 57.18  ?  68   SER A CA  1 
ATOM   168   C C   . SER A  1  68  ? 25.912  -31.418 111.273 1.00 57.59  ?  68   SER A C   1 
ATOM   169   O O   . SER A  1  68  ? 25.219  -32.181 111.952 1.00 60.76  ?  68   SER A O   1 
ATOM   170   C CB  . SER A  1  68  ? 26.627  -29.230 112.248 1.00 54.03  ?  68   SER A CB  1 
ATOM   171   O OG  . SER A  1  68  ? 27.955  -29.693 112.074 1.00 50.77  ?  68   SER A OG  1 
ATOM   172   N N   . LYS A  1  69  ? 26.915  -31.841 110.499 1.00 52.14  ?  69   LYS A N   1 
ATOM   173   C CA  . LYS A  1  69  ? 27.274  -33.253 110.438 1.00 52.72  ?  69   LYS A CA  1 
ATOM   174   C C   . LYS A  1  69  ? 27.855  -33.768 111.749 1.00 52.22  ?  69   LYS A C   1 
ATOM   175   O O   . LYS A  1  69  ? 27.870  -34.984 111.968 1.00 53.61  ?  69   LYS A O   1 
ATOM   176   C CB  . LYS A  1  69  ? 28.275  -33.496 109.306 1.00 49.41  ?  69   LYS A CB  1 
ATOM   177   C CG  . LYS A  1  69  ? 27.677  -33.432 107.911 1.00 51.20  ?  69   LYS A CG  1 
ATOM   178   C CD  . LYS A  1  69  ? 26.708  -34.578 107.675 1.00 54.91  ?  69   LYS A CD  1 
ATOM   179   C CE  . LYS A  1  69  ? 26.670  -34.976 106.207 1.00 54.58  ?  69   LYS A CE  1 
ATOM   180   N NZ  . LYS A  1  69  ? 27.270  -33.933 105.327 1.00 52.41  ?  69   LYS A NZ  1 
ATOM   181   N N   . LEU A  1  70  ? 28.333  -32.881 112.619 1.00 48.34  ?  70   LEU A N   1 
ATOM   182   C CA  . LEU A  1  70  ? 28.927  -33.287 113.887 1.00 48.28  ?  70   LEU A CA  1 
ATOM   183   C C   . LEU A  1  70  ? 27.890  -33.627 114.951 1.00 52.74  ?  70   LEU A C   1 
ATOM   184   O O   . LEU A  1  70  ? 28.262  -33.818 116.114 1.00 53.24  ?  70   LEU A O   1 
ATOM   185   C CB  . LEU A  1  70  ? 29.873  -32.201 114.406 1.00 44.92  ?  70   LEU A CB  1 
ATOM   186   C CG  . LEU A  1  70  ? 31.339  -32.287 113.960 1.00 40.61  ?  70   LEU A CG  1 
ATOM   187   C CD1 . LEU A  1  70  ? 31.483  -32.605 112.478 1.00 39.53  ?  70   LEU A CD1 1 
ATOM   188   C CD2 . LEU A  1  70  ? 32.076  -31.004 114.301 1.00 39.95  ?  70   LEU A CD2 1 
ATOM   189   N N   . SER A  1  71  ? 26.608  -33.701 114.585 1.00 47.23  ?  71   SER A N   1 
ATOM   190   C CA  . SER A  1  71  ? 25.591  -34.165 115.521 1.00 51.26  ?  71   SER A CA  1 
ATOM   191   C C   . SER A  1  71  ? 25.820  -35.610 115.946 1.00 53.58  ?  71   SER A C   1 
ATOM   192   O O   . SER A  1  71  ? 25.335  -36.016 117.007 1.00 57.17  ?  71   SER A O   1 
ATOM   193   C CB  . SER A  1  71  ? 24.198  -34.016 114.904 1.00 54.09  ?  71   SER A CB  1 
ATOM   194   O OG  . SER A  1  71  ? 24.058  -32.766 114.251 1.00 52.93  ?  71   SER A OG  1 
ATOM   195   N N   . SER A  1  72  ? 26.547  -36.391 115.143 1.00 50.63  ?  72   SER A N   1 
ATOM   196   C CA  . SER A  1  72  ? 26.817  -37.791 115.453 1.00 49.88  ?  72   SER A CA  1 
ATOM   197   C C   . SER A  1  72  ? 27.784  -37.972 116.616 1.00 48.75  ?  72   SER A C   1 
ATOM   198   O O   . SER A  1  72  ? 27.968  -39.106 117.071 1.00 48.63  ?  72   SER A O   1 
ATOM   199   C CB  . SER A  1  72  ? 27.371  -38.496 114.214 1.00 48.04  ?  72   SER A CB  1 
ATOM   200   O OG  . SER A  1  72  ? 28.368  -37.707 113.589 1.00 46.15  ?  72   SER A OG  1 
ATOM   201   N N   . TRP A  1  73  ? 28.412  -36.898 117.095 1.00 48.01  ?  73   TRP A N   1 
ATOM   202   C CA  . TRP A  1  73  ? 29.350  -36.972 118.215 1.00 47.29  ?  73   TRP A CA  1 
ATOM   203   C C   . TRP A  1  73  ? 28.554  -36.894 119.516 1.00 49.85  ?  73   TRP A C   1 
ATOM   204   O O   . TRP A  1  73  ? 28.401  -35.835 120.131 1.00 50.86  ?  73   TRP A O   1 
ATOM   205   C CB  . TRP A  1  73  ? 30.385  -35.856 118.129 1.00 45.79  ?  73   TRP A CB  1 
ATOM   206   C CG  . TRP A  1  73  ? 31.303  -35.934 116.939 1.00 43.50  ?  73   TRP A CG  1 
ATOM   207   C CD1 . TRP A  1  73  ? 31.094  -36.627 115.780 1.00 42.87  ?  73   TRP A CD1 1 
ATOM   208   C CD2 . TRP A  1  73  ? 32.568  -35.277 116.788 1.00 41.85  ?  73   TRP A CD2 1 
ATOM   209   N NE1 . TRP A  1  73  ? 32.153  -36.448 114.924 1.00 40.94  ?  73   TRP A NE1 1 
ATOM   210   C CE2 . TRP A  1  73  ? 33.071  -35.624 115.519 1.00 40.31  ?  73   TRP A CE2 1 
ATOM   211   C CE3 . TRP A  1  73  ? 33.326  -34.433 117.606 1.00 41.74  ?  73   TRP A CE3 1 
ATOM   212   C CZ2 . TRP A  1  73  ? 34.297  -35.156 115.048 1.00 38.77  ?  73   TRP A CZ2 1 
ATOM   213   C CZ3 . TRP A  1  73  ? 34.542  -33.969 117.137 1.00 40.17  ?  73   TRP A CZ3 1 
ATOM   214   C CH2 . TRP A  1  73  ? 35.015  -34.332 115.870 1.00 38.74  ?  73   TRP A CH2 1 
ATOM   215   N N   . VAL A  1  74  ? 28.031  -38.044 119.943 1.00 50.41  ?  74   VAL A N   1 
ATOM   216   C CA  . VAL A  1  74  ? 27.196  -38.072 121.139 1.00 55.04  ?  74   VAL A CA  1 
ATOM   217   C C   . VAL A  1  74  ? 27.815  -38.957 122.213 1.00 56.25  ?  74   VAL A C   1 
ATOM   218   O O   . VAL A  1  74  ? 28.138  -38.485 123.309 1.00 55.58  ?  74   VAL A O   1 
ATOM   219   C CB  . VAL A  1  74  ? 25.770  -38.554 120.809 1.00 58.50  ?  74   VAL A CB  1 
ATOM   220   C CG1 . VAL A  1  74  ? 24.800  -38.120 121.897 1.00 59.99  ?  74   VAL A CG1 1 
ATOM   221   C CG2 . VAL A  1  74  ? 25.325  -38.039 119.452 1.00 57.00  ?  74   VAL A CG2 1 
ATOM   222   N N   . ASN A  1  75  ? 27.997  -40.240 121.905 1.00 64.29  ?  75   ASN A N   1 
ATOM   223   C CA  . ASN A  1  75  ? 28.439  -41.203 122.903 1.00 62.20  ?  75   ASN A CA  1 
ATOM   224   C C   . ASN A  1  75  ? 29.940  -41.410 122.793 1.00 56.78  ?  75   ASN A C   1 
ATOM   225   O O   . ASN A  1  75  ? 30.425  -41.792 121.716 1.00 54.34  ?  75   ASN A O   1 
ATOM   226   C CB  . ASN A  1  75  ? 27.701  -42.526 122.728 1.00 63.05  ?  75   ASN A CB  1 
ATOM   227   C CG  . ASN A  1  75  ? 28.224  -43.620 123.641 1.00 61.12  ?  75   ASN A CG  1 
ATOM   228   O OD1 . ASN A  1  75  ? 28.688  -43.355 124.750 1.00 60.54  ?  75   ASN A OD1 1 
ATOM   229   N ND2 . ASN A  1  75  ? 28.151  -44.862 123.175 1.00 60.04  ?  75   ASN A ND2 1 
ATOM   230   N N   . PRO A  1  76  ? 30.709  -41.179 123.862 1.00 61.55  ?  76   PRO A N   1 
ATOM   231   C CA  . PRO A  1  76  ? 32.166  -41.353 123.782 1.00 56.62  ?  76   PRO A CA  1 
ATOM   232   C C   . PRO A  1  76  ? 32.630  -42.799 123.820 1.00 54.65  ?  76   PRO A C   1 
ATOM   233   O O   . PRO A  1  76  ? 33.825  -43.048 123.606 1.00 50.61  ?  76   PRO A O   1 
ATOM   234   C CB  . PRO A  1  76  ? 32.669  -40.589 125.013 1.00 57.23  ?  76   PRO A CB  1 
ATOM   235   C CG  . PRO A  1  76  ? 31.549  -40.716 125.990 1.00 62.50  ?  76   PRO A CG  1 
ATOM   236   C CD  . PRO A  1  76  ? 30.290  -40.633 125.165 1.00 65.12  ?  76   PRO A CD  1 
ATOM   237   N N   . ASN A  1  77  ? 31.743  -43.753 124.094 1.00 60.63  ?  77   ASN A N   1 
ATOM   238   C CA  . ASN A  1  77  ? 32.140  -45.153 124.089 1.00 58.04  ?  77   ASN A CA  1 
ATOM   239   C C   . ASN A  1  77  ? 32.549  -45.582 122.685 1.00 55.25  ?  77   ASN A C   1 
ATOM   240   O O   . ASN A  1  77  ? 32.014  -45.100 121.682 1.00 55.85  ?  77   ASN A O   1 
ATOM   241   C CB  . ASN A  1  77  ? 31.001  -46.039 124.597 1.00 60.80  ?  77   ASN A CB  1 
ATOM   242   C CG  . ASN A  1  77  ? 30.816  -45.947 126.098 1.00 62.91  ?  77   ASN A CG  1 
ATOM   243   O OD1 . ASN A  1  77  ? 31.697  -45.472 126.816 1.00 61.10  ?  77   ASN A OD1 1 
ATOM   244   N ND2 . ASN A  1  77  ? 29.666  -46.402 126.582 1.00 65.87  ?  77   ASN A ND2 1 
ATOM   245   N N   . THR A  1  78  ? 33.519  -46.497 122.621 1.00 59.94  ?  78   THR A N   1 
ATOM   246   C CA  . THR A  1  78  ? 33.994  -46.993 121.335 1.00 56.80  ?  78   THR A CA  1 
ATOM   247   C C   . THR A  1  78  ? 32.891  -47.689 120.549 1.00 58.51  ?  78   THR A C   1 
ATOM   248   O O   . THR A  1  78  ? 33.012  -47.840 119.329 1.00 56.78  ?  78   THR A O   1 
ATOM   249   C CB  . THR A  1  78  ? 35.171  -47.947 121.544 1.00 53.62  ?  78   THR A CB  1 
ATOM   250   O OG1 . THR A  1  78  ? 35.944  -47.509 122.665 1.00 53.29  ?  78   THR A OG1 1 
ATOM   251   C CG2 . THR A  1  78  ? 36.066  -47.955 120.316 1.00 49.79  ?  78   THR A CG2 1 
ATOM   252   N N   . SER A  1  79  ? 31.815  -48.107 121.222 1.00 53.70  ?  79   SER A N   1 
ATOM   253   C CA  . SER A  1  79  ? 30.677  -48.730 120.559 1.00 56.09  ?  79   SER A CA  1 
ATOM   254   C C   . SER A  1  79  ? 29.910  -47.765 119.664 1.00 59.33  ?  79   SER A C   1 
ATOM   255   O O   . SER A  1  79  ? 28.988  -48.196 118.965 1.00 62.34  ?  79   SER A O   1 
ATOM   256   C CB  . SER A  1  79  ? 29.731  -49.331 121.600 1.00 59.69  ?  79   SER A CB  1 
ATOM   257   O OG  . SER A  1  79  ? 29.381  -48.373 122.583 1.00 61.99  ?  79   SER A OG  1 
ATOM   258   N N   . SER A  1  80  ? 30.207  -46.471 119.722 1.00 54.97  ?  80   SER A N   1 
ATOM   259   C CA  . SER A  1  80  ? 29.738  -45.530 118.714 1.00 56.18  ?  80   SER A CA  1 
ATOM   260   C C   . SER A  1  80  ? 30.818  -44.597 118.192 1.00 51.81  ?  80   SER A C   1 
ATOM   261   O O   . SER A  1  80  ? 30.647  -44.042 117.100 1.00 51.95  ?  80   SER A O   1 
ATOM   262   C CB  . SER A  1  80  ? 28.579  -44.690 119.264 1.00 61.14  ?  80   SER A CB  1 
ATOM   263   O OG  . SER A  1  80  ? 28.906  -44.195 120.544 1.00 61.38  ?  80   SER A OG  1 
ATOM   264   N N   . PHE A  1  81  ? 31.909  -44.392 118.935 1.00 56.16  ?  81   PHE A N   1 
ATOM   265   C CA  . PHE A  1  81  ? 32.942  -43.446 118.521 1.00 52.34  ?  81   PHE A CA  1 
ATOM   266   C C   . PHE A  1  81  ? 33.577  -43.853 117.197 1.00 48.86  ?  81   PHE A C   1 
ATOM   267   O O   . PHE A  1  81  ? 33.650  -43.053 116.258 1.00 48.10  ?  81   PHE A O   1 
ATOM   268   C CB  . PHE A  1  81  ? 34.002  -43.330 119.618 1.00 50.43  ?  81   PHE A CB  1 
ATOM   269   C CG  . PHE A  1  81  ? 35.198  -42.506 119.231 1.00 46.20  ?  81   PHE A CG  1 
ATOM   270   C CD1 . PHE A  1  81  ? 35.062  -41.169 118.904 1.00 46.36  ?  81   PHE A CD1 1 
ATOM   271   C CD2 . PHE A  1  81  ? 36.464  -43.068 119.212 1.00 42.84  ?  81   PHE A CD2 1 
ATOM   272   C CE1 . PHE A  1  81  ? 36.163  -40.408 118.554 1.00 42.64  ?  81   PHE A CE1 1 
ATOM   273   C CE2 . PHE A  1  81  ? 37.569  -42.313 118.863 1.00 39.76  ?  81   PHE A CE2 1 
ATOM   274   C CZ  . PHE A  1  81  ? 37.418  -40.982 118.534 1.00 39.52  ?  81   PHE A CZ  1 
ATOM   275   N N   . CYS A  1  82  ? 34.022  -45.100 117.094 1.00 51.59  ?  82   CYS A N   1 
ATOM   276   C CA  . CYS A  1  82  ? 34.818  -45.540 115.958 1.00 48.29  ?  82   CYS A CA  1 
ATOM   277   C C   . CYS A  1  82  ? 33.979  -45.973 114.763 1.00 49.83  ?  82   CYS A C   1 
ATOM   278   O O   . CYS A  1  82  ? 34.548  -46.319 113.722 1.00 47.62  ?  82   CYS A O   1 
ATOM   279   C CB  . CYS A  1  82  ? 35.736  -46.688 116.388 1.00 46.48  ?  82   CYS A CB  1 
ATOM   280   S SG  . CYS A  1  82  ? 37.137  -46.157 117.399 1.00 43.28  ?  82   CYS A SG  1 
ATOM   281   N N   . THR A  1  83  ? 32.657  -45.973 114.883 1.00 44.68  ?  83   THR A N   1 
ATOM   282   C CA  . THR A  1  83  ? 31.801  -46.438 113.795 1.00 46.11  ?  83   THR A CA  1 
ATOM   283   C C   . THR A  1  83  ? 30.742  -45.433 113.367 1.00 49.73  ?  83   THR A C   1 
ATOM   284   O O   . THR A  1  83  ? 30.423  -45.363 112.177 1.00 50.40  ?  83   THR A O   1 
ATOM   285   C CB  . THR A  1  83  ? 31.124  -47.765 114.184 1.00 48.36  ?  83   THR A CB  1 
ATOM   286   O OG1 . THR A  1  83  ? 29.993  -47.503 115.025 1.00 53.04  ?  83   THR A OG1 1 
ATOM   287   C CG2 . THR A  1  83  ? 32.108  -48.679 114.898 1.00 46.08  ?  83   THR A CG2 1 
ATOM   288   N N   . SER A  1  84  ? 30.186  -44.655 114.298 1.00 45.38  ?  84   SER A N   1 
ATOM   289   C CA  . SER A  1  84  ? 29.069  -43.773 113.989 1.00 46.94  ?  84   SER A CA  1 
ATOM   290   C C   . SER A  1  84  ? 29.408  -42.292 114.073 1.00 46.38  ?  84   SER A C   1 
ATOM   291   O O   . SER A  1  84  ? 28.580  -41.465 113.675 1.00 47.64  ?  84   SER A O   1 
ATOM   292   C CB  . SER A  1  84  ? 27.883  -44.071 114.919 1.00 49.76  ?  84   SER A CB  1 
ATOM   293   O OG  . SER A  1  84  ? 28.145  -43.634 116.241 1.00 50.32  ?  84   SER A OG  1 
ATOM   294   N N   . TRP A  1  85  ? 30.584  -41.931 114.580 1.00 48.78  ?  85   TRP A N   1 
ATOM   295   C CA  . TRP A  1  85  ? 30.997  -40.534 114.625 1.00 46.45  ?  85   TRP A CA  1 
ATOM   296   C C   . TRP A  1  85  ? 31.451  -40.097 113.238 1.00 43.03  ?  85   TRP A C   1 
ATOM   297   O O   . TRP A  1  85  ? 32.382  -40.683 112.674 1.00 40.07  ?  85   TRP A O   1 
ATOM   298   C CB  . TRP A  1  85  ? 32.121  -40.340 115.637 1.00 43.38  ?  85   TRP A CB  1 
ATOM   299   C CG  . TRP A  1  85  ? 31.665  -40.244 117.055 1.00 46.99  ?  85   TRP A CG  1 
ATOM   300   C CD1 . TRP A  1  85  ? 30.644  -40.935 117.639 1.00 52.55  ?  85   TRP A CD1 1 
ATOM   301   C CD2 . TRP A  1  85  ? 32.220  -39.408 118.075 1.00 46.12  ?  85   TRP A CD2 1 
ATOM   302   N NE1 . TRP A  1  85  ? 30.530  -40.581 118.961 1.00 54.65  ?  85   TRP A NE1 1 
ATOM   303   C CE2 . TRP A  1  85  ? 31.486  -39.644 119.253 1.00 50.85  ?  85   TRP A CE2 1 
ATOM   304   C CE3 . TRP A  1  85  ? 33.266  -38.480 118.105 1.00 42.02  ?  85   TRP A CE3 1 
ATOM   305   C CZ2 . TRP A  1  85  ? 31.764  -38.987 120.449 1.00 51.90  ?  85   TRP A CZ2 1 
ATOM   306   C CZ3 . TRP A  1  85  ? 33.542  -37.832 119.292 1.00 42.73  ?  85   TRP A CZ3 1 
ATOM   307   C CH2 . TRP A  1  85  ? 32.794  -38.087 120.448 1.00 47.63  ?  85   TRP A CH2 1 
ATOM   308   N N   . TYR A  1  86  ? 30.797  -39.076 112.688 1.00 48.56  ?  86   TYR A N   1 
ATOM   309   C CA  . TYR A  1  86  ? 31.162  -38.584 111.366 1.00 46.32  ?  86   TYR A CA  1 
ATOM   310   C C   . TYR A  1  86  ? 32.598  -38.075 111.355 1.00 41.32  ?  86   TYR A C   1 
ATOM   311   O O   . TYR A  1  86  ? 33.015  -37.328 112.245 1.00 40.18  ?  86   TYR A O   1 
ATOM   312   C CB  . TYR A  1  86  ? 30.209  -37.471 110.925 1.00 48.21  ?  86   TYR A CB  1 
ATOM   313   C CG  . TYR A  1  86  ? 30.558  -36.871 109.578 1.00 45.79  ?  86   TYR A CG  1 
ATOM   314   C CD1 . TYR A  1  86  ? 30.108  -37.454 108.400 1.00 47.15  ?  86   TYR A CD1 1 
ATOM   315   C CD2 . TYR A  1  86  ? 31.334  -35.721 109.484 1.00 42.43  ?  86   TYR A CD2 1 
ATOM   316   C CE1 . TYR A  1  86  ? 30.424  -36.912 107.167 1.00 45.59  ?  86   TYR A CE1 1 
ATOM   317   C CE2 . TYR A  1  86  ? 31.656  -35.173 108.255 1.00 40.90  ?  86   TYR A CE2 1 
ATOM   318   C CZ  . TYR A  1  86  ? 31.198  -35.773 107.101 1.00 42.52  ?  86   TYR A CZ  1 
ATOM   319   O OH  . TYR A  1  86  ? 31.514  -35.231 105.875 1.00 40.85  ?  86   TYR A OH  1 
ATOM   320   N N   . GLY A  1  87  ? 33.354  -38.488 110.341 1.00 41.73  ?  87   GLY A N   1 
ATOM   321   C CA  . GLY A  1  87  ? 34.673  -37.951 110.094 1.00 37.56  ?  87   GLY A CA  1 
ATOM   322   C C   . GLY A  1  87  ? 35.804  -38.586 110.871 1.00 35.16  ?  87   GLY A C   1 
ATOM   323   O O   . GLY A  1  87  ? 36.947  -38.131 110.742 1.00 33.54  ?  87   GLY A O   1 
ATOM   324   N N   . VAL A  1  88  ? 35.537  -39.612 111.674 1.00 35.89  ?  88   VAL A N   1 
ATOM   325   C CA  . VAL A  1  88  ? 36.581  -40.312 112.410 1.00 34.97  ?  88   VAL A CA  1 
ATOM   326   C C   . VAL A  1  88  ? 36.627  -41.761 111.943 1.00 34.47  ?  88   VAL A C   1 
ATOM   327   O O   . VAL A  1  88  ? 35.596  -42.360 111.618 1.00 35.27  ?  88   VAL A O   1 
ATOM   328   C CB  . VAL A  1  88  ? 36.382  -40.224 113.940 1.00 35.96  ?  88   VAL A CB  1 
ATOM   329   C CG1 . VAL A  1  88  ? 35.970  -38.816 114.347 1.00 36.84  ?  88   VAL A CG1 1 
ATOM   330   C CG2 . VAL A  1  88  ? 35.370  -41.241 114.426 1.00 37.15  ?  88   VAL A CG2 1 
ATOM   331   N N   . ALA A  1  89  ? 37.839  -42.302 111.869 1.00 33.97  ?  89   ALA A N   1 
ATOM   332   C CA  . ALA A  1  89  ? 38.069  -43.705 111.564 1.00 33.29  ?  89   ALA A CA  1 
ATOM   333   C C   . ALA A  1  89  ? 39.218  -44.188 112.433 1.00 32.33  ?  89   ALA A C   1 
ATOM   334   O O   . ALA A  1  89  ? 40.233  -43.500 112.564 1.00 31.81  ?  89   ALA A O   1 
ATOM   335   C CB  . ALA A  1  89  ? 38.384  -43.917 110.080 1.00 31.82  ?  89   ALA A CB  1 
ATOM   336   N N   . CYS A  1  90  ? 39.053  -45.363 113.029 1.00 32.32  ?  90   CYS A N   1 
ATOM   337   C CA  . CYS A  1  90  ? 39.990  -45.863 114.022 1.00 32.60  ?  90   CYS A CA  1 
ATOM   338   C C   . CYS A  1  90  ? 40.807  -47.025 113.476 1.00 31.95  ?  90   CYS A C   1 
ATOM   339   O O   . CYS A  1  90  ? 40.553  -47.557 112.391 1.00 31.41  ?  90   CYS A O   1 
ATOM   340   C CB  . CYS A  1  90  ? 39.260  -46.313 115.292 1.00 34.39  ?  90   CYS A CB  1 
ATOM   341   S SG  . CYS A  1  90  ? 38.276  -45.061 116.125 1.00 36.32  ?  90   CYS A SG  1 
ATOM   342   N N   . SER A  1  91  ? 41.805  -47.408 114.268 1.00 29.94  ?  91   SER A N   1 
ATOM   343   C CA  . SER A  1  91  ? 42.571  -48.627 114.062 1.00 29.89  ?  91   SER A CA  1 
ATOM   344   C C   . SER A  1  91  ? 42.951  -49.149 115.437 1.00 31.57  ?  91   SER A C   1 
ATOM   345   O O   . SER A  1  91  ? 43.453  -48.386 116.269 1.00 32.23  ?  91   SER A O   1 
ATOM   346   C CB  . SER A  1  91  ? 43.823  -48.376 113.216 1.00 28.73  ?  91   SER A CB  1 
ATOM   347   O OG  . SER A  1  91  ? 44.570  -49.567 113.047 1.00 28.89  ?  91   SER A OG  1 
ATOM   348   N N   . LEU A  1  92  ? 42.700  -50.437 115.672 1.00 28.35  ?  92   LEU A N   1 
ATOM   349   C CA  . LEU A  1  92  ? 42.887  -51.049 116.989 1.00 30.49  ?  92   LEU A CA  1 
ATOM   350   C C   . LEU A  1  92  ? 42.184  -50.237 118.075 1.00 31.81  ?  92   LEU A C   1 
ATOM   351   O O   . LEU A  1  92  ? 42.665  -50.114 119.203 1.00 33.49  ?  92   LEU A O   1 
ATOM   352   C CB  . LEU A  1  92  ? 44.372  -51.231 117.310 1.00 30.96  ?  92   LEU A CB  1 
ATOM   353   C CG  . LEU A  1  92  ? 45.176  -52.018 116.274 1.00 29.91  ?  92   LEU A CG  1 
ATOM   354   C CD1 . LEU A  1  92  ? 46.614  -52.203 116.731 1.00 30.94  ?  92   LEU A CD1 1 
ATOM   355   C CD2 . LEU A  1  92  ? 44.518  -53.358 115.993 1.00 30.35  ?  92   LEU A CD2 1 
ATOM   356   N N   . GLY A  1  93  ? 41.034  -49.666 117.719 1.00 36.07  ?  93   GLY A N   1 
ATOM   357   C CA  . GLY A  1  93  ? 40.221  -48.905 118.641 1.00 37.39  ?  93   GLY A CA  1 
ATOM   358   C C   . GLY A  1  93  ? 40.616  -47.457 118.836 1.00 36.78  ?  93   GLY A C   1 
ATOM   359   O O   . GLY A  1  93  ? 39.885  -46.727 119.512 1.00 37.80  ?  93   GLY A O   1 
ATOM   360   N N   . SER A  1  94  ? 41.719  -47.000 118.251 1.00 38.35  ?  94   SER A N   1 
ATOM   361   C CA  . SER A  1  94  ? 42.183  -45.632 118.436 1.00 37.85  ?  94   SER A CA  1 
ATOM   362   C C   . SER A  1  94  ? 42.080  -44.856 117.130 1.00 36.17  ?  94   SER A C   1 
ATOM   363   O O   . SER A  1  94  ? 42.365  -45.389 116.054 1.00 34.85  ?  94   SER A O   1 
ATOM   364   C CB  . SER A  1  94  ? 43.624  -45.596 118.944 1.00 38.38  ?  94   SER A CB  1 
ATOM   365   O OG  . SER A  1  94  ? 44.170  -44.292 118.827 1.00 37.76  ?  94   SER A OG  1 
ATOM   366   N N   . ILE A  1  95  ? 41.681  -43.587 117.239 1.00 34.74  ?  95   ILE A N   1 
ATOM   367   C CA  . ILE A  1  95  ? 41.470  -42.757 116.059 1.00 33.40  ?  95   ILE A CA  1 
ATOM   368   C C   . ILE A  1  95  ? 42.794  -42.545 115.338 1.00 32.32  ?  95   ILE A C   1 
ATOM   369   O O   . ILE A  1  95  ? 43.780  -42.086 115.926 1.00 32.74  ?  95   ILE A O   1 
ATOM   370   C CB  . ILE A  1  95  ? 40.812  -41.424 116.438 1.00 33.95  ?  95   ILE A CB  1 
ATOM   371   C CG1 . ILE A  1  95  ? 40.673  -40.533 115.201 1.00 32.91  ?  95   ILE A CG1 1 
ATOM   372   C CG2 . ILE A  1  95  ? 41.585  -40.720 117.548 1.00 34.82  ?  95   ILE A CG2 1 
ATOM   373   C CD1 . ILE A  1  95  ? 39.847  -39.291 115.430 1.00 33.62  ?  95   ILE A CD1 1 
ATOM   374   N N   . ILE A  1  96  ? 42.828  -42.914 114.060 1.00 31.10  ?  96   ILE A N   1 
ATOM   375   C CA  . ILE A  1  96  ? 43.967  -42.626 113.196 1.00 30.27  ?  96   ILE A CA  1 
ATOM   376   C C   . ILE A  1  96  ? 43.613  -41.678 112.064 1.00 29.69  ?  96   ILE A C   1 
ATOM   377   O O   . ILE A  1  96  ? 44.521  -41.231 111.346 1.00 29.32  ?  96   ILE A O   1 
ATOM   378   C CB  . ILE A  1  96  ? 44.576  -43.922 112.621 1.00 29.80  ?  96   ILE A CB  1 
ATOM   379   C CG1 . ILE A  1  96  ? 43.586  -44.590 111.666 1.00 29.26  ?  96   ILE A CG1 1 
ATOM   380   C CG2 . ILE A  1  96  ? 44.938  -44.879 113.744 1.00 30.74  ?  96   ILE A CG2 1 
ATOM   381   C CD1 . ILE A  1  96  ? 44.194  -45.676 110.805 1.00 28.69  ?  96   ILE A CD1 1 
ATOM   382   N N   . ARG A  1  97  ? 42.336  -41.342 111.890 1.00 34.07  ?  97   ARG A N   1 
ATOM   383   C CA  . ARG A  1  97  ? 41.855  -40.628 110.714 1.00 33.86  ?  97   ARG A CA  1 
ATOM   384   C C   . ARG A  1  97  ? 40.843  -39.583 111.157 1.00 34.72  ?  97   ARG A C   1 
ATOM   385   O O   . ARG A  1  97  ? 39.854  -39.919 111.816 1.00 35.36  ?  97   ARG A O   1 
ATOM   386   C CB  . ARG A  1  97  ? 41.222  -41.600 109.713 1.00 33.59  ?  97   ARG A CB  1 
ATOM   387   C CG  . ARG A  1  97  ? 41.413  -41.233 108.255 1.00 33.65  ?  97   ARG A CG  1 
ATOM   388   C CD  . ARG A  1  97  ? 40.996  -42.379 107.346 1.00 34.09  ?  97   ARG A CD  1 
ATOM   389   N NE  . ARG A  1  97  ? 42.145  -43.053 106.754 1.00 33.16  ?  97   ARG A NE  1 
ATOM   390   C CZ  . ARG A  1  97  ? 42.063  -44.086 105.925 1.00 32.96  ?  97   ARG A CZ  1 
ATOM   391   N NH1 . ARG A  1  97  ? 40.895  -44.587 105.558 1.00 33.27  ?  97   ARG A NH1 1 
ATOM   392   N NH2 . ARG A  1  97  ? 43.181  -44.631 105.455 1.00 32.87  ?  97   ARG A NH2 1 
ATOM   393   N N   . LEU A  1  98  ? 41.093  -38.322 110.809 1.00 31.97  ?  98   LEU A N   1 
ATOM   394   C CA  . LEU A  1  98  ? 40.168  -37.228 111.090 1.00 32.77  ?  98   LEU A CA  1 
ATOM   395   C C   . LEU A  1  98  ? 39.896  -36.493 109.784 1.00 33.14  ?  98   LEU A C   1 
ATOM   396   O O   . LEU A  1  98  ? 40.761  -35.765 109.286 1.00 33.21  ?  98   LEU A O   1 
ATOM   397   C CB  . LEU A  1  98  ? 40.732  -36.278 112.147 1.00 33.17  ?  98   LEU A CB  1 
ATOM   398   C CG  . LEU A  1  98  ? 39.833  -35.108 112.551 1.00 34.29  ?  98   LEU A CG  1 
ATOM   399   C CD1 . LEU A  1  98  ? 38.565  -35.616 113.220 1.00 35.05  ?  98   LEU A CD1 1 
ATOM   400   C CD2 . LEU A  1  98  ? 40.576  -34.146 113.465 1.00 34.68  ?  98   LEU A CD2 1 
ATOM   401   N N   . ASN A  1  99  ? 38.699  -36.681 109.236 1.00 35.16  ?  99   ASN A N   1 
ATOM   402   C CA  . ASN A  1  99  ? 38.312  -36.130 107.938 1.00 35.97  ?  99   ASN A CA  1 
ATOM   403   C C   . ASN A  1  99  ? 37.126  -35.196 108.154 1.00 37.53  ?  99   ASN A C   1 
ATOM   404   O O   . ASN A  1  99  ? 35.986  -35.653 108.284 1.00 38.31  ?  99   ASN A O   1 
ATOM   405   C CB  . ASN A  1  99  ? 37.968  -37.251 106.960 1.00 35.81  ?  99   ASN A CB  1 
ATOM   406   C CG  . ASN A  1  99  ? 37.884  -36.774 105.525 1.00 36.77  ?  99   ASN A CG  1 
ATOM   407   O OD1 . ASN A  1  99  ? 38.175  -35.617 105.222 1.00 37.54  ?  99   ASN A OD1 1 
ATOM   408   N ND2 . ASN A  1  99  ? 37.473  -37.670 104.630 1.00 36.99  ?  99   ASN A ND2 1 
ATOM   409   N N   . LEU A  1  100 ? 37.386  -33.891 108.181 1.00 32.68  ?  100  LEU A N   1 
ATOM   410   C CA  . LEU A  1  100 ? 36.349  -32.890 108.401 1.00 33.46  ?  100  LEU A CA  1 
ATOM   411   C C   . LEU A  1  100 ? 36.372  -31.837 107.304 1.00 33.52  ?  100  LEU A C   1 
ATOM   412   O O   . LEU A  1  100 ? 36.153  -30.647 107.552 1.00 33.97  ?  100  LEU A O   1 
ATOM   413   C CB  . LEU A  1  100 ? 36.495  -32.245 109.777 1.00 33.77  ?  100  LEU A CB  1 
ATOM   414   C CG  . LEU A  1  100 ? 36.134  -33.151 110.955 1.00 34.00  ?  100  LEU A CG  1 
ATOM   415   C CD1 . LEU A  1  100 ? 36.273  -32.406 112.272 1.00 34.42  ?  100  LEU A CD1 1 
ATOM   416   C CD2 . LEU A  1  100 ? 34.726  -33.706 110.790 1.00 34.64  ?  100  LEU A CD2 1 
ATOM   417   N N   . THR A  1  101 ? 36.646  -32.261 106.072 1.00 33.97  ?  101  THR A N   1 
ATOM   418   C CA  . THR A  1  101 ? 36.608  -31.348 104.938 1.00 34.09  ?  101  THR A CA  1 
ATOM   419   C C   . THR A  1  101 ? 35.192  -30.838 104.701 1.00 35.01  ?  101  THR A C   1 
ATOM   420   O O   . THR A  1  101 ? 34.229  -31.611 104.728 1.00 35.40  ?  101  THR A O   1 
ATOM   421   C CB  . THR A  1  101 ? 37.126  -32.046 103.680 1.00 33.57  ?  101  THR A CB  1 
ATOM   422   O OG1 . THR A  1  101 ? 38.404  -32.633 103.947 1.00 32.82  ?  101  THR A OG1 1 
ATOM   423   C CG2 . THR A  1  101 ? 37.244  -31.058 102.525 1.00 33.67  ?  101  THR A CG2 1 
ATOM   424   N N   . ASN A  1  102 ? 35.075  -29.528 104.475 1.00 34.40  ?  102  ASN A N   1 
ATOM   425   C CA  . ASN A  1  102 ? 33.830  -28.911 104.011 1.00 35.35  ?  102  ASN A CA  1 
ATOM   426   C C   . ASN A  1  102 ? 32.680  -29.169 104.983 1.00 36.12  ?  102  ASN A C   1 
ATOM   427   O O   . ASN A  1  102 ? 31.545  -29.423 104.577 1.00 36.81  ?  102  ASN A O   1 
ATOM   428   C CB  . ASN A  1  102 ? 33.477  -29.392 102.601 1.00 35.37  ?  102  ASN A CB  1 
ATOM   429   C CG  . ASN A  1  102 ? 32.566  -28.430 101.867 1.00 36.29  ?  102  ASN A CG  1 
ATOM   430   O OD1 . ASN A  1  102 ? 32.528  -27.239 102.172 1.00 36.73  ?  102  ASN A OD1 1 
ATOM   431   N ND2 . ASN A  1  102 ? 31.829  -28.943 100.887 1.00 36.67  ?  102  ASN A ND2 1 
ATOM   432   N N   . THR A  1  103 ? 32.979  -29.117 106.279 1.00 37.36  ?  103  THR A N   1 
ATOM   433   C CA  . THR A  1  103 ? 31.984  -29.344 107.318 1.00 38.12  ?  103  THR A CA  1 
ATOM   434   C C   . THR A  1  103 ? 31.401  -28.044 107.859 1.00 39.07  ?  103  THR A C   1 
ATOM   435   O O   . THR A  1  103 ? 30.510  -28.080 108.713 1.00 39.88  ?  103  THR A O   1 
ATOM   436   C CB  . THR A  1  103 ? 32.604  -30.166 108.459 1.00 37.60  ?  103  THR A CB  1 
ATOM   437   O OG1 . THR A  1  103 ? 33.431  -31.194 107.904 1.00 36.66  ?  103  THR A OG1 1 
ATOM   438   C CG2 . THR A  1  103 ? 31.529  -30.837 109.302 1.00 38.29  ?  103  THR A CG2 1 
ATOM   439   N N   . GLY A  1  104 ? 31.861  -26.897 107.363 1.00 41.04  ?  104  GLY A N   1 
ATOM   440   C CA  . GLY A  1  104 ? 31.352  -25.624 107.838 1.00 42.37  ?  104  GLY A CA  1 
ATOM   441   C C   . GLY A  1  104 ? 31.662  -25.331 109.286 1.00 42.21  ?  104  GLY A C   1 
ATOM   442   O O   . GLY A  1  104 ? 30.932  -24.571 109.928 1.00 43.26  ?  104  GLY A O   1 
ATOM   443   N N   . ILE A  1  105 ? 32.725  -25.926 109.827 1.00 41.72  ?  105  ILE A N   1 
ATOM   444   C CA  . ILE A  1  105 ? 33.109  -25.667 111.207 1.00 41.85  ?  105  ILE A CA  1 
ATOM   445   C C   . ILE A  1  105 ? 33.723  -24.278 111.312 1.00 42.08  ?  105  ILE A C   1 
ATOM   446   O O   . ILE A  1  105 ? 34.512  -23.859 110.454 1.00 41.59  ?  105  ILE A O   1 
ATOM   447   C CB  . ILE A  1  105 ? 34.083  -26.751 111.702 1.00 40.88  ?  105  ILE A CB  1 
ATOM   448   C CG1 . ILE A  1  105 ? 33.400  -28.119 111.700 1.00 41.26  ?  105  ILE A CG1 1 
ATOM   449   C CG2 . ILE A  1  105 ? 34.600  -26.421 113.089 1.00 41.10  ?  105  ILE A CG2 1 
ATOM   450   C CD1 . ILE A  1  105 ? 34.367  -29.280 111.691 1.00 39.87  ?  105  ILE A CD1 1 
ATOM   451   N N   . GLU A  1  106 ? 33.368  -23.557 112.372 1.00 44.49  ?  106  GLU A N   1 
ATOM   452   C CA  . GLU A  1  106 ? 33.890  -22.222 112.634 1.00 44.91  ?  106  GLU A CA  1 
ATOM   453   C C   . GLU A  1  106 ? 34.500  -22.210 114.028 1.00 45.03  ?  106  GLU A C   1 
ATOM   454   O O   . GLU A  1  106 ? 33.793  -22.410 115.020 1.00 45.81  ?  106  GLU A O   1 
ATOM   455   C CB  . GLU A  1  106 ? 32.785  -21.169 112.509 1.00 46.22  ?  106  GLU A CB  1 
ATOM   456   C CG  . GLU A  1  106 ? 33.288  -19.751 112.284 1.00 46.60  ?  106  GLU A CG  1 
ATOM   457   C CD  . GLU A  1  106 ? 32.288  -18.698 112.720 1.00 48.14  ?  106  GLU A CD  1 
ATOM   458   O OE1 . GLU A  1  106 ? 32.199  -18.425 113.935 1.00 48.88  ?  106  GLU A OE1 1 
ATOM   459   O OE2 . GLU A  1  106 ? 31.590  -18.143 111.846 1.00 48.75  -1 106  GLU A OE2 1 
ATOM   460   N N   . GLY A  1  107 ? 35.806  -21.973 114.099 1.00 40.39  ?  107  GLY A N   1 
ATOM   461   C CA  . GLY A  1  107 ? 36.491  -21.977 115.378 1.00 40.52  ?  107  GLY A CA  1 
ATOM   462   C C   . GLY A  1  107 ? 37.990  -21.850 115.188 1.00 39.74  ?  107  GLY A C   1 
ATOM   463   O O   . GLY A  1  107 ? 38.458  -21.314 114.182 1.00 39.23  ?  107  GLY A O   1 
ATOM   464   N N   . THR A  1  108 ? 38.732  -22.340 116.182 1.00 38.85  ?  108  THR A N   1 
ATOM   465   C CA  . THR A  1  108 ? 40.188  -22.272 116.184 1.00 38.32  ?  108  THR A CA  1 
ATOM   466   C C   . THR A  1  108 ? 40.756  -23.621 116.606 1.00 37.73  ?  108  THR A C   1 
ATOM   467   O O   . THR A  1  108 ? 40.044  -24.488 117.119 1.00 37.91  ?  108  THR A O   1 
ATOM   468   C CB  . THR A  1  108 ? 40.717  -21.178 117.126 1.00 39.41  ?  108  THR A CB  1 
ATOM   469   O OG1 . THR A  1  108 ? 40.700  -21.661 118.474 1.00 40.18  ?  108  THR A OG1 1 
ATOM   470   C CG2 . THR A  1  108 ? 39.874  -19.910 117.037 1.00 40.37  ?  108  THR A CG2 1 
ATOM   471   N N   . PHE A  1  109 ? 42.062  -23.788 116.391 1.00 37.37  ?  109  PHE A N   1 
ATOM   472   C CA  . PHE A  1  109 ? 42.784  -24.973 116.834 1.00 36.94  ?  109  PHE A CA  1 
ATOM   473   C C   . PHE A  1  109 ? 43.457  -24.775 118.187 1.00 37.90  ?  109  PHE A C   1 
ATOM   474   O O   . PHE A  1  109 ? 44.392  -25.513 118.518 1.00 37.65  ?  109  PHE A O   1 
ATOM   475   C CB  . PHE A  1  109 ? 43.835  -25.379 115.798 1.00 35.79  ?  109  PHE A CB  1 
ATOM   476   C CG  . PHE A  1  109 ? 43.272  -25.683 114.443 1.00 34.91  ?  109  PHE A CG  1 
ATOM   477   C CD1 . PHE A  1  109 ? 42.155  -26.489 114.305 1.00 34.80  ?  109  PHE A CD1 1 
ATOM   478   C CD2 . PHE A  1  109 ? 43.872  -25.176 113.303 1.00 34.29  ?  109  PHE A CD2 1 
ATOM   479   C CE1 . PHE A  1  109 ? 41.642  -26.774 113.056 1.00 34.13  ?  109  PHE A CE1 1 
ATOM   480   C CE2 . PHE A  1  109 ? 43.364  -25.457 112.051 1.00 33.61  ?  109  PHE A CE2 1 
ATOM   481   C CZ  . PHE A  1  109 ? 42.247  -26.258 111.928 1.00 33.59  ?  109  PHE A CZ  1 
ATOM   482   N N   . GLU A  1  110 ? 43.003  -23.798 118.975 1.00 43.82  ?  110  GLU A N   1 
ATOM   483   C CA  . GLU A  1  110 ? 43.634  -23.541 120.265 1.00 44.92  ?  110  GLU A CA  1 
ATOM   484   C C   . GLU A  1  110 ? 43.288  -24.626 121.276 1.00 45.35  ?  110  GLU A C   1 
ATOM   485   O O   . GLU A  1  110 ? 44.130  -25.011 122.095 1.00 45.84  ?  110  GLU A O   1 
ATOM   486   C CB  . GLU A  1  110 ? 43.223  -22.166 120.785 1.00 46.22  ?  110  GLU A CB  1 
ATOM   487   C CG  . GLU A  1  110 ? 43.945  -21.744 122.052 1.00 47.56  ?  110  GLU A CG  1 
ATOM   488   C CD  . GLU A  1  110 ? 43.831  -20.258 122.317 1.00 49.41  ?  110  GLU A CD  1 
ATOM   489   O OE1 . GLU A  1  110 ? 42.730  -19.801 122.690 1.00 50.16  ?  110  GLU A OE1 1 
ATOM   490   O OE2 . GLU A  1  110 ? 44.844  -19.548 122.151 1.00 49.50  -1 110  GLU A OE2 1 
ATOM   491   N N   . ASP A  1  111 ? 42.056  -25.132 121.235 1.00 43.71  ?  111  ASP A N   1 
ATOM   492   C CA  . ASP A  1  111 ? 41.631  -26.224 122.100 1.00 44.07  ?  111  ASP A CA  1 
ATOM   493   C C   . ASP A  1  111 ? 41.586  -27.554 121.357 1.00 42.82  ?  111  ASP A C   1 
ATOM   494   O O   . ASP A  1  111 ? 40.752  -28.413 121.659 1.00 42.94  ?  111  ASP A O   1 
ATOM   495   C CB  . ASP A  1  111 ? 40.271  -25.904 122.722 1.00 45.43  ?  111  ASP A CB  1 
ATOM   496   C CG  . ASP A  1  111 ? 40.389  -25.037 123.962 1.00 46.75  ?  111  ASP A CG  1 
ATOM   497   O OD1 . ASP A  1  111 ? 41.461  -25.059 124.601 1.00 47.34  ?  111  ASP A OD1 1 
ATOM   498   O OD2 . ASP A  1  111 ? 39.412  -24.334 124.296 1.00 48.25  -1 111  ASP A OD2 1 
ATOM   499   N N   . PHE A  1  112 ? 42.475  -27.733 120.387 1.00 39.14  ?  112  PHE A N   1 
ATOM   500   C CA  . PHE A  1  112 ? 42.602  -29.001 119.682 1.00 38.03  ?  112  PHE A CA  1 
ATOM   501   C C   . PHE A  1  112 ? 43.349  -29.995 120.563 1.00 38.26  ?  112  PHE A C   1 
ATOM   502   O O   . PHE A  1  112 ? 44.413  -29.663 121.094 1.00 38.69  ?  112  PHE A O   1 
ATOM   503   C CB  . PHE A  1  112 ? 43.337  -28.809 118.358 1.00 36.93  ?  112  PHE A CB  1 
ATOM   504   C CG  . PHE A  1  112 ? 43.257  -29.996 117.441 1.00 35.85  ?  112  PHE A CG  1 
ATOM   505   C CD1 . PHE A  1  112 ? 42.103  -30.251 116.718 1.00 35.52  ?  112  PHE A CD1 1 
ATOM   506   C CD2 . PHE A  1  112 ? 44.335  -30.853 117.297 1.00 35.30  ?  112  PHE A CD2 1 
ATOM   507   C CE1 . PHE A  1  112 ? 42.023  -31.340 115.872 1.00 34.66  ?  112  PHE A CE1 1 
ATOM   508   C CE2 . PHE A  1  112 ? 44.262  -31.946 116.451 1.00 34.41  ?  112  PHE A CE2 1 
ATOM   509   C CZ  . PHE A  1  112 ? 43.103  -32.188 115.738 1.00 34.10  ?  112  PHE A CZ  1 
ATOM   510   N N   . PRO A  1  113 ? 42.828  -31.202 120.754 1.00 37.78  ?  113  PRO A N   1 
ATOM   511   C CA  . PRO A  1  113 ? 43.447  -32.146 121.710 1.00 38.20  ?  113  PRO A CA  1 
ATOM   512   C C   . PRO A  1  113 ? 44.714  -32.793 121.161 1.00 37.40  ?  113  PRO A C   1 
ATOM   513   O O   . PRO A  1  113 ? 44.752  -33.971 120.790 1.00 36.76  ?  113  PRO A O   1 
ATOM   514   C CB  . PRO A  1  113 ? 42.321  -33.156 121.942 1.00 38.26  ?  113  PRO A CB  1 
ATOM   515   C CG  . PRO A  1  113 ? 41.569  -33.171 120.652 1.00 37.32  ?  113  PRO A CG  1 
ATOM   516   C CD  . PRO A  1  113 ? 41.631  -31.767 120.106 1.00 37.30  ?  113  PRO A CD  1 
ATOM   517   N N   . PHE A  1  114 ? 45.790  -32.002 121.102 1.00 36.91  ?  114  PHE A N   1 
ATOM   518   C CA  . PHE A  1  114 ? 47.063  -32.515 120.602 1.00 36.29  ?  114  PHE A CA  1 
ATOM   519   C C   . PHE A  1  114 ? 47.569  -33.667 121.463 1.00 36.75  ?  114  PHE A C   1 
ATOM   520   O O   . PHE A  1  114 ? 47.992  -34.707 120.944 1.00 36.07  ?  114  PHE A O   1 
ATOM   521   C CB  . PHE A  1  114 ? 48.106  -31.396 120.553 1.00 36.57  ?  114  PHE A CB  1 
ATOM   522   C CG  . PHE A  1  114 ? 47.747  -30.262 119.637 1.00 36.12  ?  114  PHE A CG  1 
ATOM   523   C CD1 . PHE A  1  114 ? 47.971  -30.359 118.274 1.00 34.98  ?  114  PHE A CD1 1 
ATOM   524   C CD2 . PHE A  1  114 ? 47.221  -29.085 120.141 1.00 36.96  ?  114  PHE A CD2 1 
ATOM   525   C CE1 . PHE A  1  114 ? 47.653  -29.315 117.429 1.00 34.66  ?  114  PHE A CE1 1 
ATOM   526   C CE2 . PHE A  1  114 ? 46.901  -28.036 119.301 1.00 36.63  ?  114  PHE A CE2 1 
ATOM   527   C CZ  . PHE A  1  114 ? 47.118  -28.151 117.943 1.00 35.48  ?  114  PHE A CZ  1 
ATOM   528   N N   . SER A  1  115 ? 47.538  -33.494 122.786 1.00 39.45  ?  115  SER A N   1 
ATOM   529   C CA  . SER A  1  115 ? 48.057  -34.510 123.695 1.00 40.09  ?  115  SER A CA  1 
ATOM   530   C C   . SER A  1  115 ? 47.203  -35.770 123.720 1.00 39.78  ?  115  SER A C   1 
ATOM   531   O O   . SER A  1  115 ? 47.687  -36.822 124.151 1.00 40.37  ?  115  SER A O   1 
ATOM   532   C CB  . SER A  1  115 ? 48.167  -33.942 125.110 1.00 41.68  ?  115  SER A CB  1 
ATOM   533   O OG  . SER A  1  115 ? 47.096  -33.055 125.385 1.00 42.33  ?  115  SER A OG  1 
ATOM   534   N N   . SER A  1  116 ? 45.952  -35.693 123.270 1.00 37.93  ?  116  SER A N   1 
ATOM   535   C CA  . SER A  1  116 ? 45.009  -36.789 123.424 1.00 37.86  ?  116  SER A CA  1 
ATOM   536   C C   . SER A  1  116 ? 44.902  -37.687 122.199 1.00 36.60  ?  116  SER A C   1 
ATOM   537   O O   . SER A  1  116 ? 44.265  -38.742 122.283 1.00 36.53  ?  116  SER A O   1 
ATOM   538   C CB  . SER A  1  116 ? 43.619  -36.239 123.769 1.00 38.37  ?  116  SER A CB  1 
ATOM   539   O OG  . SER A  1  116 ? 43.711  -35.133 124.650 1.00 39.48  ?  116  SER A OG  1 
ATOM   540   N N   . LEU A  1  117 ? 45.512  -37.314 121.075 1.00 36.99  ?  117  LEU A N   1 
ATOM   541   C CA  . LEU A  1  117 ? 45.347  -38.028 119.807 1.00 35.87  ?  117  LEU A CA  1 
ATOM   542   C C   . LEU A  1  117 ? 46.710  -38.431 119.259 1.00 35.38  ?  117  LEU A C   1 
ATOM   543   O O   . LEU A  1  117 ? 47.147  -37.931 118.216 1.00 34.67  ?  117  LEU A O   1 
ATOM   544   C CB  . LEU A  1  117 ? 44.594  -37.166 118.794 1.00 35.30  ?  117  LEU A CB  1 
ATOM   545   C CG  . LEU A  1  117 ? 43.345  -36.454 119.307 1.00 35.93  ?  117  LEU A CG  1 
ATOM   546   C CD1 . LEU A  1  117 ? 42.682  -35.680 118.182 1.00 35.38  ?  117  LEU A CD1 1 
ATOM   547   C CD2 . LEU A  1  117 ? 42.386  -37.458 119.922 1.00 36.34  ?  117  LEU A CD2 1 
ATOM   548   N N   . PRO A  1  118 ? 47.408  -39.344 119.938 1.00 36.69  ?  118  PRO A N   1 
ATOM   549   C CA  . PRO A  1  118 ? 48.749  -39.728 119.470 1.00 36.37  ?  118  PRO A CA  1 
ATOM   550   C C   . PRO A  1  118 ? 48.764  -40.390 118.102 1.00 35.32  ?  118  PRO A C   1 
ATOM   551   O O   . PRO A  1  118 ? 49.714  -40.178 117.338 1.00 34.89  ?  118  PRO A O   1 
ATOM   552   C CB  . PRO A  1  118 ? 49.235  -40.685 120.566 1.00 37.22  ?  118  PRO A CB  1 
ATOM   553   C CG  . PRO A  1  118 ? 47.988  -41.271 121.122 1.00 37.52  ?  118  PRO A CG  1 
ATOM   554   C CD  . PRO A  1  118 ? 46.959  -40.175 121.070 1.00 37.49  ?  118  PRO A CD  1 
ATOM   555   N N   . ASN A  1  119 ? 47.741  -41.175 117.759 1.00 37.91  ?  119  ASN A N   1 
ATOM   556   C CA  . ASN A  1  119 ? 47.801  -42.067 116.609 1.00 37.14  ?  119  ASN A CA  1 
ATOM   557   C C   . ASN A  1  119 ? 47.259  -41.442 115.328 1.00 36.43  ?  119  ASN A C   1 
ATOM   558   O O   . ASN A  1  119 ? 46.967  -42.174 114.375 1.00 36.28  ?  119  ASN A O   1 
ATOM   559   C CB  . ASN A  1  119 ? 47.036  -43.361 116.897 1.00 37.75  ?  119  ASN A CB  1 
ATOM   560   C CG  . ASN A  1  119 ? 47.653  -44.174 118.015 1.00 38.07  ?  119  ASN A CG  1 
ATOM   561   O OD1 . ASN A  1  119 ? 48.862  -44.134 118.238 1.00 38.31  ?  119  ASN A OD1 1 
ATOM   562   N ND2 . ASN A  1  119 ? 46.815  -44.937 118.713 1.00 38.61  ?  119  ASN A ND2 1 
ATOM   563   N N   . LEU A  1  120 ? 47.121  -40.119 115.275 1.00 32.36  ?  120  LEU A N   1 
ATOM   564   C CA  . LEU A  1  120 ? 46.593  -39.484 114.075 1.00 31.75  ?  120  LEU A CA  1 
ATOM   565   C C   . LEU A  1  120 ? 47.591  -39.602 112.931 1.00 31.13  ?  120  LEU A C   1 
ATOM   566   O O   . LEU A  1  120 ? 48.753  -39.206 113.064 1.00 31.22  ?  120  LEU A O   1 
ATOM   567   C CB  . LEU A  1  120 ? 46.271  -38.013 114.338 1.00 32.01  ?  120  LEU A CB  1 
ATOM   568   C CG  . LEU A  1  120 ? 45.029  -37.690 115.169 1.00 32.61  ?  120  LEU A CG  1 
ATOM   569   C CD1 . LEU A  1  120 ? 44.822  -36.184 115.237 1.00 32.88  ?  120  LEU A CD1 1 
ATOM   570   C CD2 . LEU A  1  120 ? 43.802  -38.384 114.595 1.00 32.38  ?  120  LEU A CD2 1 
ATOM   571   N N   . THR A  1  121 ? 47.138  -40.156 111.806 1.00 28.93  ?  121  THR A N   1 
ATOM   572   C CA  . THR A  1  121 ? 47.948  -40.245 110.599 1.00 28.61  ?  121  THR A CA  1 
ATOM   573   C C   . THR A  1  121 ? 47.355  -39.506 109.407 1.00 28.45  ?  121  THR A C   1 
ATOM   574   O O   . THR A  1  121 ? 48.107  -39.098 108.520 1.00 28.20  ?  121  THR A O   1 
ATOM   575   C CB  . THR A  1  121 ? 48.174  -41.715 110.203 1.00 28.66  ?  121  THR A CB  1 
ATOM   576   O OG1 . THR A  1  121 ? 47.038  -42.197 109.476 1.00 28.72  ?  121  THR A OG1 1 
ATOM   577   C CG2 . THR A  1  121 ? 48.386  -42.579 111.437 1.00 28.97  ?  121  THR A CG2 1 
ATOM   578   N N   . PHE A  1  122 ? 46.038  -39.312 109.369 1.00 31.66  ?  122  PHE A N   1 
ATOM   579   C CA  . PHE A  1  122 ? 45.363  -38.579 108.305 1.00 31.64  ?  122  PHE A CA  1 
ATOM   580   C C   . PHE A  1  122 ? 44.554  -37.461 108.941 1.00 31.94  ?  122  PHE A C   1 
ATOM   581   O O   . PHE A  1  122 ? 43.647  -37.726 109.737 1.00 32.30  ?  122  PHE A O   1 
ATOM   582   C CB  . PHE A  1  122 ? 44.447  -39.495 107.489 1.00 31.77  ?  122  PHE A CB  1 
ATOM   583   C CG  . PHE A  1  122 ? 43.654  -38.778 106.426 1.00 32.03  ?  122  PHE A CG  1 
ATOM   584   C CD1 . PHE A  1  122 ? 44.185  -38.570 105.164 1.00 31.64  ?  122  PHE A CD1 1 
ATOM   585   C CD2 . PHE A  1  122 ? 42.382  -38.293 106.698 1.00 32.40  ?  122  PHE A CD2 1 
ATOM   586   C CE1 . PHE A  1  122 ? 43.455  -37.910 104.189 1.00 31.77  ?  122  PHE A CE1 1 
ATOM   587   C CE2 . PHE A  1  122 ? 41.652  -37.628 105.730 1.00 32.54  ?  122  PHE A CE2 1 
ATOM   588   C CZ  . PHE A  1  122 ? 42.189  -37.435 104.474 1.00 32.48  ?  122  PHE A CZ  1 
ATOM   589   N N   . VAL A  1  123 ? 44.872  -36.219 108.588 1.00 28.53  ?  123  VAL A N   1 
ATOM   590   C CA  . VAL A  1  123 ? 44.164  -35.049 109.093 1.00 28.89  ?  123  VAL A CA  1 
ATOM   591   C C   . VAL A  1  123 ? 43.846  -34.154 107.904 1.00 28.91  ?  123  VAL A C   1 
ATOM   592   O O   . VAL A  1  123 ? 44.759  -33.623 107.258 1.00 28.61  ?  123  VAL A O   1 
ATOM   593   C CB  . VAL A  1  123 ? 44.974  -34.286 110.150 1.00 28.91  ?  123  VAL A CB  1 
ATOM   594   C CG1 . VAL A  1  123 ? 44.371  -32.910 110.394 1.00 29.32  ?  123  VAL A CG1 1 
ATOM   595   C CG2 . VAL A  1  123 ? 45.030  -35.079 111.445 1.00 29.06  ?  123  VAL A CG2 1 
ATOM   596   N N   . ASP A  1  124 ? 42.558  -33.992 107.610 1.00 30.42  ?  124  ASP A N   1 
ATOM   597   C CA  . ASP A  1  124 ? 42.091  -33.096 106.555 1.00 30.59  ?  124  ASP A CA  1 
ATOM   598   C C   . ASP A  1  124 ? 41.007  -32.211 107.164 1.00 31.24  ?  124  ASP A C   1 
ATOM   599   O O   . ASP A  1  124 ? 39.870  -32.652 107.358 1.00 31.67  ?  124  ASP A O   1 
ATOM   600   C CB  . ASP A  1  124 ? 41.571  -33.881 105.353 1.00 30.56  ?  124  ASP A CB  1 
ATOM   601   C CG  . ASP A  1  124 ? 41.360  -33.010 104.129 1.00 30.67  ?  124  ASP A CG  1 
ATOM   602   O OD1 . ASP A  1  124 ? 41.358  -31.768 104.266 1.00 30.89  ?  124  ASP A OD1 1 
ATOM   603   O OD2 . ASP A  1  124 ? 41.194  -33.570 103.025 1.00 30.61  -1 124  ASP A OD2 1 
ATOM   604   N N   . LEU A  1  125 ? 41.364  -30.968 107.473 1.00 29.42  ?  125  LEU A N   1 
ATOM   605   C CA  . LEU A  1  125 ? 40.447  -29.987 108.038 1.00 30.13  ?  125  LEU A CA  1 
ATOM   606   C C   . LEU A  1  125 ? 40.242  -28.829 107.071 1.00 30.38  ?  125  LEU A C   1 
ATOM   607   O O   . LEU A  1  125 ? 40.121  -27.669 107.472 1.00 30.84  ?  125  LEU A O   1 
ATOM   608   C CB  . LEU A  1  125 ? 40.956  -29.482 109.385 1.00 30.29  ?  125  LEU A CB  1 
ATOM   609   C CG  . LEU A  1  125 ? 41.247  -30.575 110.413 1.00 30.10  ?  125  LEU A CG  1 
ATOM   610   C CD1 . LEU A  1  125 ? 41.896  -29.988 111.655 1.00 30.28  ?  125  LEU A CD1 1 
ATOM   611   C CD2 . LEU A  1  125 ? 39.973  -31.323 110.768 1.00 30.56  ?  125  LEU A CD2 1 
ATOM   612   N N   . SER A  1  126 ? 40.201  -29.138 105.779 1.00 32.12  ?  126  SER A N   1 
ATOM   613   C CA  . SER A  1  126 ? 40.143  -28.106 104.760 1.00 32.32  ?  126  SER A CA  1 
ATOM   614   C C   . SER A  1  126 ? 38.706  -27.654 104.517 1.00 33.14  ?  126  SER A C   1 
ATOM   615   O O   . SER A  1  126 ? 37.740  -28.334 104.873 1.00 33.48  ?  126  SER A O   1 
ATOM   616   C CB  . SER A  1  126 ? 40.767  -28.606 103.456 1.00 31.79  ?  126  SER A CB  1 
ATOM   617   O OG  . SER A  1  126 ? 40.057  -29.716 102.940 1.00 31.82  ?  126  SER A OG  1 
ATOM   618   N N   . MET A  1  127 ? 38.581  -26.470 103.914 1.00 34.32  ?  127  MET A N   1 
ATOM   619   C CA  . MET A  1  127 ? 37.294  -25.898 103.514 1.00 35.20  ?  127  MET A CA  1 
ATOM   620   C C   . MET A  1  127 ? 36.377  -25.688 104.722 1.00 35.92  ?  127  MET A C   1 
ATOM   621   O O   . MET A  1  127 ? 35.240  -26.158 104.766 1.00 36.47  ?  127  MET A O   1 
ATOM   622   C CB  . MET A  1  127 ? 36.610  -26.762 102.451 1.00 35.25  ?  127  MET A CB  1 
ATOM   623   C CG  . MET A  1  127 ? 37.475  -27.068 101.247 1.00 34.62  ?  127  MET A CG  1 
ATOM   624   S SD  . MET A  1  127 ? 36.473  -27.675 99.882  1.00 35.04  ?  127  MET A SD  1 
ATOM   625   C CE  . MET A  1  127 ? 35.304  -26.326 99.721  1.00 36.21  ?  127  MET A CE  1 
ATOM   626   N N   . ASN A  1  128 ? 36.891  -24.952 105.701 1.00 37.27  ?  128  ASN A N   1 
ATOM   627   C CA  . ASN A  1  128 ? 36.132  -24.628 106.900 1.00 38.05  ?  128  ASN A CA  1 
ATOM   628   C C   . ASN A  1  128 ? 36.444  -23.184 107.274 1.00 38.53  ?  128  ASN A C   1 
ATOM   629   O O   . ASN A  1  128 ? 37.056  -22.438 106.504 1.00 38.62  ?  128  ASN A O   1 
ATOM   630   C CB  . ASN A  1  128 ? 36.449  -25.612 108.033 1.00 37.67  ?  128  ASN A CB  1 
ATOM   631   C CG  . ASN A  1  128 ? 35.864  -26.991 107.789 1.00 37.46  ?  128  ASN A CG  1 
ATOM   632   O OD1 . ASN A  1  128 ? 34.656  -27.198 107.913 1.00 38.25  ?  128  ASN A OD1 1 
ATOM   633   N ND2 . ASN A  1  128 ? 36.722  -27.944 107.442 1.00 36.57  ?  128  ASN A ND2 1 
ATOM   634   N N   . ARG A  1  129 ? 36.022  -22.789 108.469 1.00 39.69  ?  129  ARG A N   1 
ATOM   635   C CA  . ARG A  1  129 ? 36.180  -21.423 108.947 1.00 40.37  ?  129  ARG A CA  1 
ATOM   636   C C   . ARG A  1  129 ? 37.088  -21.384 110.167 1.00 40.29  ?  129  ARG A C   1 
ATOM   637   O O   . ARG A  1  129 ? 36.829  -20.673 111.141 1.00 41.00  ?  129  ARG A O   1 
ATOM   638   C CB  . ARG A  1  129 ? 34.826  -20.787 109.252 1.00 41.67  ?  129  ARG A CB  1 
ATOM   639   C CG  . ARG A  1  129 ? 33.908  -20.691 108.043 1.00 42.05  ?  129  ARG A CG  1 
ATOM   640   C CD  . ARG A  1  129 ? 32.793  -19.681 108.263 1.00 43.59  ?  129  ARG A CD  1 
ATOM   641   N NE  . ARG A  1  129 ? 33.207  -18.594 109.142 1.00 44.70  ?  129  ARG A NE  1 
ATOM   642   C CZ  . ARG A  1  129 ? 33.606  -17.400 108.722 1.00 44.80  ?  129  ARG A CZ  1 
ATOM   643   N NH1 . ARG A  1  129 ? 33.654  -17.100 107.434 1.00 44.14  ?  129  ARG A NH1 1 
ATOM   644   N NH2 . ARG A  1  129 ? 33.966  -16.485 109.618 1.00 44.90  ?  129  ARG A NH2 1 
ATOM   645   N N   . PHE A  1  130 ? 38.168  -22.159 110.122 1.00 35.73  ?  130  PHE A N   1 
ATOM   646   C CA  . PHE A  1  130 ? 39.156  -22.145 111.189 1.00 35.52  ?  130  PHE A CA  1 
ATOM   647   C C   . PHE A  1  130 ? 40.023  -20.900 111.074 1.00 35.65  ?  130  PHE A C   1 
ATOM   648   O O   . PHE A  1  130 ? 40.587  -20.617 110.012 1.00 35.17  ?  130  PHE A O   1 
ATOM   649   C CB  . PHE A  1  130 ? 40.028  -23.399 111.137 1.00 34.46  ?  130  PHE A CB  1 
ATOM   650   C CG  . PHE A  1  130 ? 39.320  -24.648 111.566 1.00 34.41  ?  130  PHE A CG  1 
ATOM   651   C CD1 . PHE A  1  130 ? 38.888  -24.798 112.873 1.00 34.99  ?  130  PHE A CD1 1 
ATOM   652   C CD2 . PHE A  1  130 ? 39.096  -25.677 110.668 1.00 33.84  ?  130  PHE A CD2 1 
ATOM   653   C CE1 . PHE A  1  130 ? 38.239  -25.949 113.275 1.00 34.98  ?  130  PHE A CE1 1 
ATOM   654   C CE2 . PHE A  1  130 ? 38.448  -26.831 111.063 1.00 33.84  ?  130  PHE A CE2 1 
ATOM   655   C CZ  . PHE A  1  130 ? 38.020  -26.967 112.369 1.00 34.40  ?  130  PHE A CZ  1 
ATOM   656   N N   . SER A  1  131 ? 40.121  -20.155 112.169 1.00 35.58  ?  131  SER A N   1 
ATOM   657   C CA  . SER A  1  131 ? 40.933  -18.952 112.233 1.00 35.88  ?  131  SER A CA  1 
ATOM   658   C C   . SER A  1  131 ? 41.945  -19.086 113.361 1.00 35.97  ?  131  SER A C   1 
ATOM   659   O O   . SER A  1  131 ? 41.737  -19.835 114.319 1.00 36.23  ?  131  SER A O   1 
ATOM   660   C CB  . SER A  1  131 ? 40.064  -17.706 112.444 1.00 37.15  ?  131  SER A CB  1 
ATOM   661   O OG  . SER A  1  131 ? 39.274  -17.828 113.613 1.00 38.00  ?  131  SER A OG  1 
ATOM   662   N N   . GLY A  1  132 ? 43.053  -18.356 113.234 1.00 34.31  ?  132  GLY A N   1 
ATOM   663   C CA  . GLY A  1  132 ? 44.130  -18.415 114.199 1.00 34.59  ?  132  GLY A CA  1 
ATOM   664   C C   . GLY A  1  132 ? 45.446  -18.794 113.543 1.00 33.63  ?  132  GLY A C   1 
ATOM   665   O O   . GLY A  1  132 ? 45.691  -18.475 112.373 1.00 33.01  ?  132  GLY A O   1 
ATOM   666   N N   . THR A  1  133 ? 46.288  -19.478 114.310 1.00 32.60  ?  133  THR A N   1 
ATOM   667   C CA  . THR A  1  133 ? 47.624  -19.853 113.874 1.00 31.90  ?  133  THR A CA  1 
ATOM   668   C C   . THR A  1  133 ? 47.776  -21.369 113.870 1.00 31.12  ?  133  THR A C   1 
ATOM   669   O O   . THR A  1  133 ? 46.936  -22.109 114.389 1.00 31.22  ?  133  THR A O   1 
ATOM   670   C CB  . THR A  1  133 ? 48.693  -19.218 114.770 1.00 32.76  ?  133  THR A CB  1 
ATOM   671   O OG1 . THR A  1  133 ? 48.429  -19.551 116.138 1.00 33.64  ?  133  THR A OG1 1 
ATOM   672   C CG2 . THR A  1  133 ? 48.685  -17.705 114.617 1.00 33.48  ?  133  THR A CG2 1 
ATOM   673   N N   . ILE A  1  134 ? 48.876  -21.822 113.277 1.00 31.53  ?  134  ILE A N   1 
ATOM   674   C CA  . ILE A  1  134 ? 49.223  -23.238 113.241 1.00 30.86  ?  134  ILE A CA  1 
ATOM   675   C C   . ILE A  1  134 ? 50.160  -23.501 114.414 1.00 31.50  ?  134  ILE A C   1 
ATOM   676   O O   . ILE A  1  134 ? 51.319  -23.078 114.403 1.00 31.69  ?  134  ILE A O   1 
ATOM   677   C CB  . ILE A  1  134 ? 49.873  -23.626 111.908 1.00 29.84  ?  134  ILE A CB  1 
ATOM   678   C CG1 . ILE A  1  134 ? 48.875  -23.469 110.761 1.00 29.32  ?  134  ILE A CG1 1 
ATOM   679   C CG2 . ILE A  1  134 ? 50.388  -25.056 111.962 1.00 29.31  ?  134  ILE A CG2 1 
ATOM   680   C CD1 . ILE A  1  134 ? 49.521  -23.429 109.397 1.00 28.59  ?  134  ILE A CD1 1 
ATOM   681   N N   . SER A  1  135 ? 49.648  -24.179 115.436 1.00 32.45  ?  135  SER A N   1 
ATOM   682   C CA  . SER A  1  135 ? 50.420  -24.416 116.644 1.00 33.28  ?  135  SER A CA  1 
ATOM   683   C C   . SER A  1  135 ? 51.619  -25.319 116.356 1.00 32.75  ?  135  SER A C   1 
ATOM   684   O O   . SER A  1  135 ? 51.556  -26.198 115.490 1.00 31.76  ?  135  SER A O   1 
ATOM   685   C CB  . SER A  1  135 ? 49.541  -25.046 117.722 1.00 33.87  ?  135  SER A CB  1 
ATOM   686   O OG  . SER A  1  135 ? 50.236  -25.156 118.953 1.00 34.89  ?  135  SER A OG  1 
ATOM   687   N N   . PRO A  1  136 ? 52.731  -25.119 117.068 1.00 31.23  ?  136  PRO A N   1 
ATOM   688   C CA  . PRO A  1  136 ? 53.851  -26.068 116.962 1.00 30.95  ?  136  PRO A CA  1 
ATOM   689   C C   . PRO A  1  136 ? 53.493  -27.465 117.431 1.00 30.80  ?  136  PRO A C   1 
ATOM   690   O O   . PRO A  1  136 ? 54.199  -28.421 117.084 1.00 30.34  ?  136  PRO A O   1 
ATOM   691   C CB  . PRO A  1  136 ? 54.932  -25.438 117.852 1.00 32.14  ?  136  PRO A CB  1 
ATOM   692   C CG  . PRO A  1  136 ? 54.543  -23.998 117.980 1.00 32.74  ?  136  PRO A CG  1 
ATOM   693   C CD  . PRO A  1  136 ? 53.049  -23.979 117.942 1.00 32.48  ?  136  PRO A CD  1 
ATOM   694   N N   . GLU A  1  137 ? 52.421  -27.613 118.214 1.00 36.68  ?  137  GLU A N   1 
ATOM   695   C CA  . GLU A  1  137 ? 51.989  -28.929 118.667 1.00 36.58  ?  137  GLU A CA  1 
ATOM   696   C C   . GLU A  1  137 ? 51.565  -29.830 117.515 1.00 35.31  ?  137  GLU A C   1 
ATOM   697   O O   . GLU A  1  137 ? 51.472  -31.048 117.701 1.00 35.11  ?  137  GLU A O   1 
ATOM   698   C CB  . GLU A  1  137 ? 50.837  -28.784 119.662 1.00 37.36  ?  137  GLU A CB  1 
ATOM   699   C CG  . GLU A  1  137 ? 51.109  -27.800 120.786 1.00 38.76  ?  137  GLU A CG  1 
ATOM   700   C CD  . GLU A  1  137 ? 51.466  -28.487 122.088 1.00 39.82  ?  137  GLU A CD  1 
ATOM   701   O OE1 . GLU A  1  137 ? 52.492  -29.199 122.123 1.00 39.77  ?  137  GLU A OE1 1 
ATOM   702   O OE2 . GLU A  1  137 ? 50.722  -28.316 123.076 1.00 40.78  -1 137  GLU A OE2 1 
ATOM   703   N N   . TRP A  1  138 ? 51.295  -29.260 116.337 1.00 32.94  ?  138  TRP A N   1 
ATOM   704   C CA  . TRP A  1  138 ? 50.953  -30.076 115.176 1.00 31.86  ?  138  TRP A CA  1 
ATOM   705   C C   . TRP A  1  138 ? 52.069  -31.054 114.829 1.00 31.48  ?  138  TRP A C   1 
ATOM   706   O O   . TRP A  1  138 ? 51.801  -32.144 114.310 1.00 30.87  ?  138  TRP A O   1 
ATOM   707   C CB  . TRP A  1  138 ? 50.630  -29.180 113.980 1.00 31.29  ?  138  TRP A CB  1 
ATOM   708   C CG  . TRP A  1  138 ? 49.239  -28.611 114.021 1.00 31.46  ?  138  TRP A CG  1 
ATOM   709   C CD1 . TRP A  1  138 ? 48.890  -27.309 114.238 1.00 32.03  ?  138  TRP A CD1 1 
ATOM   710   C CD2 . TRP A  1  138 ? 48.012  -29.332 113.853 1.00 31.19  ?  138  TRP A CD2 1 
ATOM   711   N NE1 . TRP A  1  138 ? 47.523  -27.173 114.208 1.00 32.14  ?  138  TRP A NE1 1 
ATOM   712   C CE2 . TRP A  1  138 ? 46.960  -28.401 113.974 1.00 31.63  ?  138  TRP A CE2 1 
ATOM   713   C CE3 . TRP A  1  138 ? 47.700  -30.673 113.610 1.00 30.70  ?  138  TRP A CE3 1 
ATOM   714   C CZ2 . TRP A  1  138 ? 45.620  -28.768 113.859 1.00 31.61  ?  138  TRP A CZ2 1 
ATOM   715   C CZ3 . TRP A  1  138 ? 46.369  -31.036 113.495 1.00 30.65  ?  138  TRP A CZ3 1 
ATOM   716   C CH2 . TRP A  1  138 ? 45.347  -30.087 113.620 1.00 31.11  ?  138  TRP A CH2 1 
ATOM   717   N N   . GLY A  1  139 ? 53.318  -30.690 115.110 1.00 31.09  ?  139  GLY A N   1 
ATOM   718   C CA  . GLY A  1  139 ? 54.439  -31.582 114.883 1.00 30.93  ?  139  GLY A CA  1 
ATOM   719   C C   . GLY A  1  139 ? 54.545  -32.738 115.854 1.00 31.42  ?  139  GLY A C   1 
ATOM   720   O O   . GLY A  1  139 ? 55.421  -33.591 115.681 1.00 31.36  ?  139  GLY A O   1 
ATOM   721   N N   . ARG A  1  140 ? 53.682  -32.791 116.872 1.00 34.22  ?  140  ARG A N   1 
ATOM   722   C CA  . ARG A  1  140 ? 53.720  -33.879 117.842 1.00 34.78  ?  140  ARG A CA  1 
ATOM   723   C C   . ARG A  1  140 ? 53.160  -35.180 117.282 1.00 34.02  ?  140  ARG A C   1 
ATOM   724   O O   . ARG A  1  140 ? 53.413  -36.246 117.854 1.00 34.37  ?  140  ARG A O   1 
ATOM   725   C CB  . ARG A  1  140 ? 52.936  -33.489 119.096 1.00 35.72  ?  140  ARG A CB  1 
ATOM   726   C CG  . ARG A  1  140 ? 53.707  -32.629 120.078 1.00 37.12  ?  140  ARG A CG  1 
ATOM   727   C CD  . ARG A  1  140 ? 52.847  -32.288 121.284 1.00 38.12  ?  140  ARG A CD  1 
ATOM   728   N NE  . ARG A  1  140 ? 52.736  -33.406 122.214 1.00 41.16  ?  140  ARG A NE  1 
ATOM   729   C CZ  . ARG A  1  140 ? 51.885  -33.453 123.230 1.00 41.28  ?  140  ARG A CZ  1 
ATOM   730   N NH1 . ARG A  1  140 ? 51.045  -32.461 123.475 1.00 40.35  ?  140  ARG A NH1 1 
ATOM   731   N NH2 . ARG A  1  140 ? 51.878  -34.522 124.020 1.00 42.65  ?  140  ARG A NH2 1 
ATOM   732   N N   . PHE A  1  141 ? 52.411  -35.119 116.183 1.00 32.66  ?  141  PHE A N   1 
ATOM   733   C CA  . PHE A  1  141 ? 51.739  -36.290 115.621 1.00 32.03  ?  141  PHE A CA  1 
ATOM   734   C C   . PHE A  1  141 ? 52.767  -37.106 114.846 1.00 31.61  ?  141  PHE A C   1 
ATOM   735   O O   . PHE A  1  141 ? 52.925  -36.963 113.633 1.00 30.90  ?  141  PHE A O   1 
ATOM   736   C CB  . PHE A  1  141 ? 50.567  -35.864 114.747 1.00 31.39  ?  141  PHE A CB  1 
ATOM   737   C CG  . PHE A  1  141 ? 49.485  -35.145 115.503 1.00 31.90  ?  141  PHE A CG  1 
ATOM   738   C CD1 . PHE A  1  141 ? 48.748  -35.800 116.475 1.00 32.41  ?  141  PHE A CD1 1 
ATOM   739   C CD2 . PHE A  1  141 ? 49.211  -33.812 115.248 1.00 31.95  ?  141  PHE A CD2 1 
ATOM   740   C CE1 . PHE A  1  141 ? 47.756  -35.138 117.176 1.00 32.98  ?  141  PHE A CE1 1 
ATOM   741   C CE2 . PHE A  1  141 ? 48.219  -33.146 115.945 1.00 32.53  ?  141  PHE A CE2 1 
ATOM   742   C CZ  . PHE A  1  141 ? 47.492  -33.810 116.910 1.00 33.06  ?  141  PHE A CZ  1 
ATOM   743   N N   . SER A  1  142 ? 53.475  -37.979 115.569 1.00 32.44  ?  142  SER A N   1 
ATOM   744   C CA  . SER A  1  142 ? 54.621  -38.681 114.997 1.00 32.29  ?  142  SER A CA  1 
ATOM   745   C C   . SER A  1  142 ? 54.221  -39.544 113.806 1.00 31.45  ?  142  SER A C   1 
ATOM   746   O O   . SER A  1  142 ? 54.953  -39.619 112.811 1.00 31.06  ?  142  SER A O   1 
ATOM   747   C CB  . SER A  1  142 ? 55.293  -39.538 116.069 1.00 33.17  ?  142  SER A CB  1 
ATOM   748   O OG  . SER A  1  142 ? 54.356  -40.410 116.679 1.00 33.33  ?  142  SER A OG  1 
ATOM   749   N N   . LYS A  1  143 ? 53.068  -40.202 113.884 1.00 32.98  ?  143  LYS A N   1 
ATOM   750   C CA  . LYS A  1  143 ? 52.645  -41.108 112.826 1.00 32.30  ?  143  LYS A CA  1 
ATOM   751   C C   . LYS A  1  143 ? 51.931  -40.395 111.685 1.00 31.68  ?  143  LYS A C   1 
ATOM   752   O O   . LYS A  1  143 ? 51.551  -41.053 110.709 1.00 31.27  ?  143  LYS A O   1 
ATOM   753   C CB  . LYS A  1  143 ? 51.746  -42.203 113.411 1.00 32.50  ?  143  LYS A CB  1 
ATOM   754   C CG  . LYS A  1  143 ? 52.467  -43.114 114.398 1.00 33.21  ?  143  LYS A CG  1 
ATOM   755   C CD  . LYS A  1  143 ? 51.826  -44.494 114.482 1.00 33.62  ?  143  LYS A CD  1 
ATOM   756   C CE  . LYS A  1  143 ? 50.491  -44.452 115.211 1.00 34.55  ?  143  LYS A CE  1 
ATOM   757   N NZ  . LYS A  1  143 ? 50.624  -43.922 116.596 1.00 34.26  ?  143  LYS A NZ  1 
ATOM   758   N N   . LEU A  1  144 ? 51.756  -39.077 111.777 1.00 28.86  ?  144  LEU A N   1 
ATOM   759   C CA  . LEU A  1  144 ? 50.985  -38.335 110.787 1.00 28.35  ?  144  LEU A CA  1 
ATOM   760   C C   . LEU A  1  144 ? 51.631  -38.408 109.408 1.00 27.84  ?  144  LEU A C   1 
ATOM   761   O O   . LEU A  1  144 ? 52.832  -38.169 109.254 1.00 27.90  ?  144  LEU A O   1 
ATOM   762   C CB  . LEU A  1  144 ? 50.838  -36.877 111.222 1.00 28.61  ?  144  LEU A CB  1 
ATOM   763   C CG  . LEU A  1  144 ? 49.773  -36.057 110.492 1.00 28.30  ?  144  LEU A CG  1 
ATOM   764   C CD1 . LEU A  1  144 ? 48.383  -36.431 110.978 1.00 28.49  ?  144  LEU A CD1 1 
ATOM   765   C CD2 . LEU A  1  144 ? 50.027  -34.568 110.673 1.00 28.54  ?  144  LEU A CD2 1 
ATOM   766   N N   . GLU A  1  145 ? 50.818  -38.727 108.403 1.00 26.65  ?  145  GLU A N   1 
ATOM   767   C CA  . GLU A  1  145 ? 51.259  -38.846 107.022 1.00 26.47  ?  145  GLU A CA  1 
ATOM   768   C C   . GLU A  1  145 ? 50.612  -37.837 106.087 1.00 26.34  ?  145  GLU A C   1 
ATOM   769   O O   . GLU A  1  145 ? 51.244  -37.430 105.111 1.00 26.21  ?  145  GLU A O   1 
ATOM   770   C CB  . GLU A  1  145 ? 50.975  -40.260 106.492 1.00 26.56  ?  145  GLU A CB  1 
ATOM   771   C CG  . GLU A  1  145 ? 51.666  -41.368 107.270 1.00 26.78  ?  145  GLU A CG  1 
ATOM   772   C CD  . GLU A  1  145 ? 51.135  -42.745 106.918 1.00 26.95  ?  145  GLU A CD  1 
ATOM   773   O OE1 . GLU A  1  145 ? 50.904  -43.007 105.719 1.00 26.88  ?  145  GLU A OE1 1 
ATOM   774   O OE2 . GLU A  1  145 ? 50.947  -43.565 107.841 1.00 27.20  -1 145  GLU A OE2 1 
ATOM   775   N N   . TYR A  1  146 ? 49.378  -37.421 106.363 1.00 25.28  ?  146  TYR A N   1 
ATOM   776   C CA  . TYR A  1  146 ? 48.636  -36.497 105.514 1.00 25.29  ?  146  TYR A CA  1 
ATOM   777   C C   . TYR A  1  146 ? 48.166  -35.334 106.373 1.00 25.46  ?  146  TYR A C   1 
ATOM   778   O O   . TYR A  1  146 ? 47.504  -35.543 107.395 1.00 25.68  ?  146  TYR A O   1 
ATOM   779   C CB  . TYR A  1  146 ? 47.445  -37.200 104.857 1.00 25.44  ?  146  TYR A CB  1 
ATOM   780   C CG  . TYR A  1  146 ? 46.767  -36.419 103.754 1.00 25.52  ?  146  TYR A CG  1 
ATOM   781   C CD1 . TYR A  1  146 ? 45.730  -35.541 104.037 1.00 25.79  ?  146  TYR A CD1 1 
ATOM   782   C CD2 . TYR A  1  146 ? 47.144  -36.582 102.427 1.00 25.41  ?  146  TYR A CD2 1 
ATOM   783   C CE1 . TYR A  1  146 ? 45.097  -34.835 103.032 1.00 25.95  ?  146  TYR A CE1 1 
ATOM   784   C CE2 . TYR A  1  146 ? 46.517  -35.878 101.415 1.00 25.55  ?  146  TYR A CE2 1 
ATOM   785   C CZ  . TYR A  1  146 ? 45.495  -35.006 101.724 1.00 25.82  ?  146  TYR A CZ  1 
ATOM   786   O OH  . TYR A  1  146 ? 44.869  -34.304 100.720 1.00 26.04  ?  146  TYR A OH  1 
ATOM   787   N N   . PHE A  1  147 ? 48.512  -34.114 105.966 1.00 25.22  ?  147  PHE A N   1 
ATOM   788   C CA  . PHE A  1  147 ? 48.204  -32.910 106.732 1.00 25.45  ?  147  PHE A CA  1 
ATOM   789   C C   . PHE A  1  147 ? 47.629  -31.870 105.780 1.00 25.59  ?  147  PHE A C   1 
ATOM   790   O O   . PHE A  1  147 ? 48.341  -31.364 104.907 1.00 25.42  ?  147  PHE A O   1 
ATOM   791   C CB  . PHE A  1  147 ? 49.455  -32.387 107.438 1.00 25.35  ?  147  PHE A CB  1 
ATOM   792   C CG  . PHE A  1  147 ? 49.172  -31.387 108.517 1.00 25.69  ?  147  PHE A CG  1 
ATOM   793   C CD1 . PHE A  1  147 ? 47.983  -31.432 109.227 1.00 26.05  ?  147  PHE A CD1 1 
ATOM   794   C CD2 . PHE A  1  147 ? 50.105  -30.416 108.841 1.00 25.98  ?  147  PHE A CD2 1 
ATOM   795   C CE1 . PHE A  1  147 ? 47.723  -30.516 110.226 1.00 26.69  ?  147  PHE A CE1 1 
ATOM   796   C CE2 . PHE A  1  147 ? 49.852  -29.499 109.841 1.00 26.63  ?  147  PHE A CE2 1 
ATOM   797   C CZ  . PHE A  1  147 ? 48.660  -29.549 110.534 1.00 27.00  ?  147  PHE A CZ  1 
ATOM   798   N N   . ASP A  1  148 ? 46.348  -31.544 105.953 1.00 27.89  ?  148  ASP A N   1 
ATOM   799   C CA  . ASP A  1  148 ? 45.622  -30.671 105.033 1.00 28.15  ?  148  ASP A CA  1 
ATOM   800   C C   . ASP A  1  148 ? 44.821  -29.656 105.837 1.00 28.67  ?  148  ASP A C   1 
ATOM   801   O O   . ASP A  1  148 ? 43.831  -30.013 106.484 1.00 29.00  ?  148  ASP A O   1 
ATOM   802   C CB  . ASP A  1  148 ? 44.705  -31.483 104.116 1.00 28.22  ?  148  ASP A CB  1 
ATOM   803   C CG  . ASP A  1  148 ? 44.234  -30.694 102.906 1.00 28.44  ?  148  ASP A CG  1 
ATOM   804   O OD1 . ASP A  1  148 ? 44.276  -29.446 102.943 1.00 28.66  ?  148  ASP A OD1 1 
ATOM   805   O OD2 . ASP A  1  148 ? 43.822  -31.326 101.912 1.00 28.44  -1 148  ASP A OD2 1 
ATOM   806   N N   . LEU A  1  149 ? 45.248  -28.395 105.793 1.00 26.34  ?  149  LEU A N   1 
ATOM   807   C CA  . LEU A  1  149 ? 44.534  -27.288 106.418 1.00 26.95  ?  149  LEU A CA  1 
ATOM   808   C C   . LEU A  1  149 ? 44.154  -26.230 105.386 1.00 27.25  ?  149  LEU A C   1 
ATOM   809   O O   . LEU A  1  149 ? 44.027  -25.049 105.714 1.00 27.72  ?  149  LEU A O   1 
ATOM   810   C CB  . LEU A  1  149 ? 45.364  -26.668 107.541 1.00 27.02  ?  149  LEU A CB  1 
ATOM   811   C CG  . LEU A  1  149 ? 45.684  -27.568 108.736 1.00 26.89  ?  149  LEU A CG  1 
ATOM   812   C CD1 . LEU A  1  149 ? 46.546  -26.825 109.746 1.00 27.13  ?  149  LEU A CD1 1 
ATOM   813   C CD2 . LEU A  1  149 ? 44.407  -28.080 109.383 1.00 27.30  ?  149  LEU A CD2 1 
ATOM   814   N N   . SER A  1  150 ? 43.981  -26.646 104.134 1.00 29.89  ?  150  SER A N   1 
ATOM   815   C CA  . SER A  1  150 ? 43.768  -25.711 103.040 1.00 30.15  ?  150  SER A CA  1 
ATOM   816   C C   . SER A  1  150 ? 42.408  -25.026 103.151 1.00 30.93  ?  150  SER A C   1 
ATOM   817   O O   . SER A  1  150 ? 41.496  -25.501 103.831 1.00 31.23  ?  150  SER A O   1 
ATOM   818   C CB  . SER A  1  150 ? 43.876  -26.432 101.697 1.00 29.83  ?  150  SER A CB  1 
ATOM   819   O OG  . SER A  1  150 ? 45.086  -27.164 101.608 1.00 29.21  ?  150  SER A OG  1 
ATOM   820   N N   . ILE A  1  151 ? 42.284  -23.893 102.454 1.00 30.25  ?  151  ILE A N   1 
ATOM   821   C CA  . ILE A  1  151 ? 41.062  -23.092 102.402 1.00 31.10  ?  151  ILE A CA  1 
ATOM   822   C C   . ILE A  1  151 ? 40.531  -22.859 103.811 1.00 31.58  ?  151  ILE A C   1 
ATOM   823   O O   . ILE A  1  151 ? 39.596  -23.533 104.261 1.00 31.84  ?  151  ILE A O   1 
ATOM   824   C CB  . ILE A  1  151 ? 39.999  -23.747 101.502 1.00 31.35  ?  151  ILE A CB  1 
ATOM   825   C CG1 . ILE A  1  151 ? 40.559  -23.949 100.097 1.00 30.97  ?  151  ILE A CG1 1 
ATOM   826   C CG2 . ILE A  1  151 ? 38.760  -22.869 101.404 1.00 32.35  ?  151  ILE A CG2 1 
ATOM   827   C CD1 . ILE A  1  151 ? 40.374  -25.341 99.575  1.00 30.60  ?  151  ILE A CD1 1 
ATOM   828   N N   . ASN A  1  152 ? 41.144  -21.920 104.522 1.00 31.68  ?  152  ASN A N   1 
ATOM   829   C CA  . ASN A  1  152 ? 40.746  -21.579 105.877 1.00 32.24  ?  152  ASN A CA  1 
ATOM   830   C C   . ASN A  1  152 ? 41.046  -20.100 106.087 1.00 32.81  ?  152  ASN A C   1 
ATOM   831   O O   . ASN A  1  152 ? 41.297  -19.359 105.131 1.00 32.87  ?  152  ASN A O   1 
ATOM   832   C CB  . ASN A  1  152 ? 41.461  -22.478 106.894 1.00 31.69  ?  152  ASN A CB  1 
ATOM   833   C CG  . ASN A  1  152 ? 40.675  -23.735 107.215 1.00 31.61  ?  152  ASN A CG  1 
ATOM   834   O OD1 . ASN A  1  152 ? 39.487  -23.676 107.529 1.00 32.29  ?  152  ASN A OD1 1 
ATOM   835   N ND2 . ASN A  1  152 ? 41.338  -24.884 107.135 1.00 30.84  ?  152  ASN A ND2 1 
ATOM   836   N N   . GLN A  1  153 ? 41.013  -19.666 107.339 1.00 35.32  ?  153  GLN A N   1 
ATOM   837   C CA  . GLN A  1  153 ? 41.336  -18.293 107.703 1.00 35.97  ?  153  GLN A CA  1 
ATOM   838   C C   . GLN A  1  153 ? 42.506  -18.263 108.677 1.00 35.70  ?  153  GLN A C   1 
ATOM   839   O O   . GLN A  1  153 ? 42.511  -17.514 109.656 1.00 36.44  ?  153  GLN A O   1 
ATOM   840   C CB  . GLN A  1  153 ? 40.113  -17.590 108.284 1.00 37.15  ?  153  GLN A CB  1 
ATOM   841   C CG  . GLN A  1  153 ? 38.918  -17.585 107.345 1.00 37.56  ?  153  GLN A CG  1 
ATOM   842   C CD  . GLN A  1  153 ? 37.614  -17.874 108.059 1.00 38.36  ?  153  GLN A CD  1 
ATOM   843   O OE1 . GLN A  1  153 ? 36.772  -18.620 107.560 1.00 38.34  ?  153  GLN A OE1 1 
ATOM   844   N NE2 . GLN A  1  153 ? 37.442  -17.284 109.237 1.00 39.15  ?  153  GLN A NE2 1 
ATOM   845   N N   . LEU A  1  154 ? 43.519  -19.082 108.404 1.00 33.70  ?  154  LEU A N   1 
ATOM   846   C CA  . LEU A  1  154 ? 44.693  -19.161 109.260 1.00 33.44  ?  154  LEU A CA  1 
ATOM   847   C C   . LEU A  1  154 ? 45.658  -18.022 108.959 1.00 33.60  ?  154  LEU A C   1 
ATOM   848   O O   . LEU A  1  154 ? 45.809  -17.598 107.809 1.00 33.42  ?  154  LEU A O   1 
ATOM   849   C CB  . LEU A  1  154 ? 45.402  -20.504 109.073 1.00 32.45  ?  154  LEU A CB  1 
ATOM   850   C CG  . LEU A  1  154 ? 44.999  -21.702 109.939 1.00 32.29  ?  154  LEU A CG  1 
ATOM   851   C CD1 . LEU A  1  154 ? 43.494  -21.818 110.110 1.00 32.87  ?  154  LEU A CD1 1 
ATOM   852   C CD2 . LEU A  1  154 ? 45.559  -22.982 109.340 1.00 31.35  ?  154  LEU A CD2 1 
ATOM   853   N N   . VAL A  1  155 ? 46.315  -17.531 110.008 1.00 33.80  ?  155  VAL A N   1 
ATOM   854   C CA  . VAL A  1  155 ? 47.310  -16.476 109.904 1.00 34.13  ?  155  VAL A CA  1 
ATOM   855   C C   . VAL A  1  155 ? 48.531  -16.892 110.715 1.00 34.14  ?  155  VAL A C   1 
ATOM   856   O O   . VAL A  1  155 ? 48.538  -17.923 111.387 1.00 33.97  ?  155  VAL A O   1 
ATOM   857   C CB  . VAL A  1  155 ? 46.774  -15.111 110.385 1.00 35.31  ?  155  VAL A CB  1 
ATOM   858   C CG1 . VAL A  1  155 ? 45.832  -14.516 109.349 1.00 35.48  ?  155  VAL A CG1 1 
ATOM   859   C CG2 . VAL A  1  155 ? 46.071  -15.261 111.724 1.00 36.17  ?  155  VAL A CG2 1 
ATOM   860   N N   . GLY A  1  156 ? 49.573  -16.076 110.635 1.00 35.17  ?  156  GLY A N   1 
ATOM   861   C CA  . GLY A  1  156 ? 50.801  -16.365 111.345 1.00 35.34  ?  156  GLY A CA  1 
ATOM   862   C C   . GLY A  1  156 ? 51.813  -17.091 110.485 1.00 34.36  ?  156  GLY A C   1 
ATOM   863   O O   . GLY A  1  156 ? 51.716  -17.159 109.256 1.00 33.62  ?  156  GLY A O   1 
ATOM   864   N N   . GLU A  1  157 ? 52.813  -17.649 111.157 1.00 34.13  ?  157  GLU A N   1 
ATOM   865   C CA  . GLU A  1  157 ? 53.884  -18.366 110.485 1.00 33.39  ?  157  GLU A CA  1 
ATOM   866   C C   . GLU A  1  157 ? 53.646  -19.870 110.533 1.00 32.69  ?  157  GLU A C   1 
ATOM   867   O O   . GLU A  1  157 ? 52.781  -20.374 111.252 1.00 32.86  ?  157  GLU A O   1 
ATOM   868   C CB  . GLU A  1  157 ? 55.239  -18.030 111.116 1.00 34.06  ?  157  GLU A CB  1 
ATOM   869   C CG  . GLU A  1  157 ? 55.472  -16.554 111.359 1.00 35.01  ?  157  GLU A CG  1 
ATOM   870   C CD  . GLU A  1  157 ? 56.910  -16.154 111.104 1.00 35.24  ?  157  GLU A CD  1 
ATOM   871   O OE1 . GLU A  1  157 ? 57.687  -17.005 110.620 1.00 34.61  ?  157  GLU A OE1 1 
ATOM   872   O OE2 . GLU A  1  157 ? 57.266  -14.992 111.389 1.00 36.13  -1 157  GLU A OE2 1 
ATOM   873   N N   . ILE A  1  158 ? 54.440  -20.586 109.746 1.00 27.27  ?  158  ILE A N   1 
ATOM   874   C CA  . ILE A  1  158 ? 54.464  -22.044 109.771 1.00 26.68  ?  158  ILE A CA  1 
ATOM   875   C C   . ILE A  1  158 ? 55.497  -22.469 110.811 1.00 27.25  ?  158  ILE A C   1 
ATOM   876   O O   . ILE A  1  158 ? 56.682  -22.134 110.657 1.00 27.47  ?  158  ILE A O   1 
ATOM   877   C CB  . ILE A  1  158 ? 54.798  -22.625 108.393 1.00 25.76  ?  158  ILE A CB  1 
ATOM   878   C CG1 . ILE A  1  158 ? 53.694  -22.280 107.391 1.00 25.34  ?  158  ILE A CG1 1 
ATOM   879   C CG2 . ILE A  1  158 ? 54.990  -24.130 108.482 1.00 25.31  ?  158  ILE A CG2 1 
ATOM   880   C CD1 . ILE A  1  158 ? 54.105  -22.437 105.944 1.00 24.69  ?  158  ILE A CD1 1 
ATOM   881   N N   . PRO A  1  159 ? 55.101  -23.155 111.876 1.00 28.84  ?  159  PRO A N   1 
ATOM   882   C CA  . PRO A  1  159 ? 56.068  -23.576 112.897 1.00 29.53  ?  159  PRO A CA  1 
ATOM   883   C C   . PRO A  1  159 ? 57.115  -24.504 112.309 1.00 29.02  ?  159  PRO A C   1 
ATOM   884   O O   . PRO A  1  159 ? 56.801  -25.347 111.454 1.00 28.12  ?  159  PRO A O   1 
ATOM   885   C CB  . PRO A  1  159 ? 55.199  -24.301 113.936 1.00 29.84  ?  159  PRO A CB  1 
ATOM   886   C CG  . PRO A  1  159 ? 53.943  -24.659 113.222 1.00 29.02  ?  159  PRO A CG  1 
ATOM   887   C CD  . PRO A  1  159 ? 53.735  -23.617 112.169 1.00 28.69  ?  159  PRO A CD  1 
ATOM   888   N N   . PRO A  1  160 ? 58.375  -24.376 112.732 1.00 32.09  ?  160  PRO A N   1 
ATOM   889   C CA  . PRO A  1  160 ? 59.393  -25.345 112.295 1.00 31.78  ?  160  PRO A CA  1 
ATOM   890   C C   . PRO A  1  160 ? 59.126  -26.748 112.802 1.00 31.64  ?  160  PRO A C   1 
ATOM   891   O O   . PRO A  1  160 ? 59.670  -27.709 112.245 1.00 31.19  ?  160  PRO A O   1 
ATOM   892   C CB  . PRO A  1  160 ? 60.701  -24.778 112.871 1.00 32.81  ?  160  PRO A CB  1 
ATOM   893   C CG  . PRO A  1  160 ? 60.369  -23.394 113.366 1.00 33.52  ?  160  PRO A CG  1 
ATOM   894   C CD  . PRO A  1  160 ? 58.914  -23.402 113.692 1.00 33.29  ?  160  PRO A CD  1 
ATOM   895   N N   . GLU A  1  161 ? 58.299  -26.890 113.841 1.00 31.77  ?  161  GLU A N   1 
ATOM   896   C CA  . GLU A  1  161 ? 57.960  -28.203 114.378 1.00 31.70  ?  161  GLU A CA  1 
ATOM   897   C C   . GLU A  1  161 ? 57.269  -29.086 113.349 1.00 30.56  ?  161  GLU A C   1 
ATOM   898   O O   . GLU A  1  161 ? 57.250  -30.309 113.512 1.00 30.39  ?  161  GLU A O   1 
ATOM   899   C CB  . GLU A  1  161 ? 57.077  -28.045 115.616 1.00 32.42  ?  161  GLU A CB  1 
ATOM   900   C CG  . GLU A  1  161 ? 57.855  -27.770 116.892 1.00 33.77  ?  161  GLU A CG  1 
ATOM   901   C CD  . GLU A  1  161 ? 58.156  -26.296 117.088 1.00 34.49  ?  161  GLU A CD  1 
ATOM   902   O OE1 . GLU A  1  161 ? 57.975  -25.517 116.129 1.00 33.88  ?  161  GLU A OE1 1 
ATOM   903   O OE2 . GLU A  1  161 ? 58.571  -25.916 118.203 1.00 35.75  -1 161  GLU A OE2 1 
ATOM   904   N N   . LEU A  1  162 ? 56.692  -28.498 112.299 1.00 29.51  ?  162  LEU A N   1 
ATOM   905   C CA  . LEU A  1  162 ? 56.158  -29.309 111.213 1.00 28.55  ?  162  LEU A CA  1 
ATOM   906   C C   . LEU A  1  162 ? 57.241  -30.153 110.559 1.00 28.26  ?  162  LEU A C   1 
ATOM   907   O O   . LEU A  1  162 ? 56.935  -31.203 109.983 1.00 27.69  ?  162  LEU A O   1 
ATOM   908   C CB  . LEU A  1  162 ? 55.491  -28.411 110.167 1.00 28.04  ?  162  LEU A CB  1 
ATOM   909   C CG  . LEU A  1  162 ? 54.179  -27.735 110.567 1.00 28.23  ?  162  LEU A CG  1 
ATOM   910   C CD1 . LEU A  1  162 ? 53.369  -27.373 109.330 1.00 27.60  ?  162  LEU A CD1 1 
ATOM   911   C CD2 . LEU A  1  162 ? 53.372  -28.623 111.501 1.00 28.42  ?  162  LEU A CD2 1 
ATOM   912   N N   . GLY A  1  163 ? 58.503  -29.723 110.647 1.00 31.95  ?  163  GLY A N   1 
ATOM   913   C CA  . GLY A  1  163 ? 59.604  -30.476 110.079 1.00 31.84  ?  163  GLY A CA  1 
ATOM   914   C C   . GLY A  1  163 ? 59.882  -31.799 110.761 1.00 32.13  ?  163  GLY A C   1 
ATOM   915   O O   . GLY A  1  163 ? 60.481  -32.685 110.143 1.00 32.21  ?  163  GLY A O   1 
ATOM   916   N N   . LYS A  1  164 ? 59.480  -31.955 112.024 1.00 30.02  ?  164  LYS A N   1 
ATOM   917   C CA  . LYS A  1  164 ? 59.659  -33.219 112.724 1.00 30.37  ?  164  LYS A CA  1 
ATOM   918   C C   . LYS A  1  164 ? 58.496  -34.181 112.495 1.00 29.70  ?  164  LYS A C   1 
ATOM   919   O O   . LYS A  1  164 ? 58.346  -35.154 113.244 1.00 30.03  ?  164  LYS A O   1 
ATOM   920   C CB  . LYS A  1  164 ? 59.887  -32.977 114.221 1.00 31.50  ?  164  LYS A CB  1 
ATOM   921   C CG  . LYS A  1  164 ? 58.680  -32.509 115.010 1.00 31.68  ?  164  LYS A CG  1 
ATOM   922   C CD  . LYS A  1  164 ? 59.124  -31.691 116.214 1.00 32.90  ?  164  LYS A CD  1 
ATOM   923   C CE  . LYS A  1  164 ? 58.100  -31.720 117.334 1.00 33.43  ?  164  LYS A CE  1 
ATOM   924   N NZ  . LYS A  1  164 ? 58.684  -31.204 118.603 1.00 34.85  ?  164  LYS A NZ  1 
ATOM   925   N N   . LEU A  1  165 ? 57.680  -33.931 111.471 1.00 27.92  ?  165  LEU A N   1 
ATOM   926   C CA  . LEU A  1  165 ? 56.664  -34.885 111.025 1.00 27.31  ?  165  LEU A CA  1 
ATOM   927   C C   . LEU A  1  165 ? 57.309  -35.845 110.025 1.00 26.91  ?  165  LEU A C   1 
ATOM   928   O O   . LEU A  1  165 ? 57.061  -35.813 108.819 1.00 26.29  ?  165  LEU A O   1 
ATOM   929   C CB  . LEU A  1  165 ? 55.470  -34.154 110.422 1.00 26.78  ?  165  LEU A CB  1 
ATOM   930   C CG  . LEU A  1  165 ? 54.608  -33.326 111.378 1.00 27.20  ?  165  LEU A CG  1 
ATOM   931   C CD1 . LEU A  1  165 ? 53.661  -32.423 110.602 1.00 26.78  ?  165  LEU A CD1 1 
ATOM   932   C CD2 . LEU A  1  165 ? 53.838  -34.216 112.341 1.00 27.48  ?  165  LEU A CD2 1 
ATOM   933   N N   . SER A  1  166 ? 58.169  -36.712 110.571 1.00 29.54  ?  166  SER A N   1 
ATOM   934   C CA  . SER A  1  166 ? 59.034  -37.556 109.750 1.00 29.43  ?  166  SER A CA  1 
ATOM   935   C C   . SER A  1  166 ? 58.251  -38.424 108.773 1.00 28.74  ?  166  SER A C   1 
ATOM   936   O O   . SER A  1  166 ? 58.740  -38.715 107.674 1.00 28.47  ?  166  SER A O   1 
ATOM   937   C CB  . SER A  1  166 ? 59.902  -38.436 110.649 1.00 30.22  ?  166  SER A CB  1 
ATOM   938   O OG  . SER A  1  166 ? 59.099  -39.266 111.472 1.00 30.36  ?  166  SER A OG  1 
ATOM   939   N N   . ASN A  1  167 ? 57.052  -38.855 109.149 1.00 29.03  ?  167  ASN A N   1 
ATOM   940   C CA  . ASN A  1  167 ? 56.261  -39.759 108.326 1.00 28.53  ?  167  ASN A CA  1 
ATOM   941   C C   . ASN A  1  167 ? 55.358  -39.033 107.337 1.00 28.09  ?  167  ASN A C   1 
ATOM   942   O O   . ASN A  1  167 ? 54.592  -39.689 106.624 1.00 28.01  ?  167  ASN A O   1 
ATOM   943   C CB  . ASN A  1  167 ? 55.422  -40.675 109.220 1.00 28.86  ?  167  ASN A CB  1 
ATOM   944   C CG  . ASN A  1  167 ? 56.170  -41.925 109.630 1.00 29.19  ?  167  ASN A CG  1 
ATOM   945   O OD1 . ASN A  1  167 ? 56.714  -42.640 108.789 1.00 29.41  ?  167  ASN A OD1 1 
ATOM   946   N ND2 . ASN A  1  167 ? 56.212  -42.189 110.931 1.00 29.79  ?  167  ASN A ND2 1 
ATOM   947   N N   . LEU A  1  168 ? 55.430  -37.706 107.274 1.00 27.06  ?  168  LEU A N   1 
ATOM   948   C CA  . LEU A  1  168 ? 54.517  -36.946 106.432 1.00 26.81  ?  168  LEU A CA  1 
ATOM   949   C C   . LEU A  1  168 ? 54.802  -37.201 104.957 1.00 26.71  ?  168  LEU A C   1 
ATOM   950   O O   . LEU A  1  168 ? 55.951  -37.134 104.510 1.00 26.76  ?  168  LEU A O   1 
ATOM   951   C CB  . LEU A  1  168 ? 54.627  -35.454 106.743 1.00 26.76  ?  168  LEU A CB  1 
ATOM   952   C CG  . LEU A  1  168 ? 53.407  -34.604 106.385 1.00 26.67  ?  168  LEU A CG  1 
ATOM   953   C CD1 . LEU A  1  168 ? 52.294  -34.817 107.398 1.00 26.81  ?  168  LEU A CD1 1 
ATOM   954   C CD2 . LEU A  1  168 ? 53.785  -33.135 106.304 1.00 26.67  ?  168  LEU A CD2 1 
ATOM   955   N N   . ASP A  1  169 ? 53.743  -37.494 104.206 1.00 28.95  ?  169  ASP A N   1 
ATOM   956   C CA  . ASP A  1  169 ? 53.798  -37.728 102.769 1.00 28.92  ?  169  ASP A CA  1 
ATOM   957   C C   . ASP A  1  169 ? 53.262  -36.548 101.974 1.00 28.82  ?  169  ASP A C   1 
ATOM   958   O O   . ASP A  1  169 ? 53.828  -36.193 100.935 1.00 28.81  ?  169  ASP A O   1 
ATOM   959   C CB  . ASP A  1  169 ? 53.006  -38.995 102.417 1.00 29.01  ?  169  ASP A CB  1 
ATOM   960   C CG  . ASP A  1  169 ? 52.716  -39.120 100.930 1.00 29.32  ?  169  ASP A CG  1 
ATOM   961   O OD1 . ASP A  1  169 ? 53.615  -38.835 100.110 1.00 29.29  ?  169  ASP A OD1 1 
ATOM   962   O OD2 . ASP A  1  169 ? 51.578  -39.501 100.580 1.00 30.40  -1 169  ASP A OD2 1 
ATOM   963   N N   . THR A  1  170 ? 52.180  -35.934 102.444 1.00 25.77  ?  170  THR A N   1 
ATOM   964   C CA  . THR A  1  170 ? 51.550  -34.804 101.780 1.00 25.79  ?  170  THR A CA  1 
ATOM   965   C C   . THR A  1  170 ? 51.317  -33.690 102.791 1.00 25.84  ?  170  THR A C   1 
ATOM   966   O O   . THR A  1  170 ? 50.891  -33.947 103.922 1.00 25.92  ?  170  THR A O   1 
ATOM   967   C CB  . THR A  1  170 ? 50.223  -35.229 101.133 1.00 25.92  ?  170  THR A CB  1 
ATOM   968   O OG1 . THR A  1  170 ? 50.486  -36.151 100.067 1.00 25.93  ?  170  THR A OG1 1 
ATOM   969   C CG2 . THR A  1  170 ? 49.479  -34.030 100.583 1.00 26.05  ?  170  THR A CG2 1 
ATOM   970   N N   . LEU A  1  171 ? 51.608  -32.453 102.385 1.00 24.65  ?  171  LEU A N   1 
ATOM   971   C CA  . LEU A  1  171 ? 51.415  -31.277 103.227 1.00 24.79  ?  171  LEU A CA  1 
ATOM   972   C C   . LEU A  1  171 ? 50.626  -30.237 102.446 1.00 24.98  ?  171  LEU A C   1 
ATOM   973   O O   . LEU A  1  171 ? 51.101  -29.739 101.420 1.00 24.96  ?  171  LEU A O   1 
ATOM   974   C CB  . LEU A  1  171 ? 52.758  -30.702 103.687 1.00 24.72  ?  171  LEU A CB  1 
ATOM   975   C CG  . LEU A  1  171 ? 52.698  -29.387 104.467 1.00 24.93  ?  171  LEU A CG  1 
ATOM   976   C CD1 . LEU A  1  171 ? 51.935  -29.574 105.768 1.00 25.10  ?  171  LEU A CD1 1 
ATOM   977   C CD2 . LEU A  1  171 ? 54.098  -28.856 104.734 1.00 24.90  ?  171  LEU A CD2 1 
ATOM   978   N N   . HIS A  1  172 ? 49.432  -29.903 102.933 1.00 27.31  ?  172  HIS A N   1 
ATOM   979   C CA  . HIS A  1  172 ? 48.532  -28.967 102.263 1.00 27.62  ?  172  HIS A CA  1 
ATOM   980   C C   . HIS A  1  172 ? 48.164  -27.847 103.230 1.00 27.96  ?  172  HIS A C   1 
ATOM   981   O O   . HIS A  1  172 ? 47.416  -28.067 104.188 1.00 28.17  ?  172  HIS A O   1 
ATOM   982   C CB  . HIS A  1  172 ? 47.280  -29.681 101.755 1.00 27.78  ?  172  HIS A CB  1 
ATOM   983   C CG  . HIS A  1  172 ? 47.518  -30.550 100.559 1.00 27.59  ?  172  HIS A CG  1 
ATOM   984   N ND1 . HIS A  1  172 ? 46.553  -31.394 100.051 1.00 27.72  ?  172  HIS A ND1 1 
ATOM   985   C CD2 . HIS A  1  172 ? 48.604  -30.701 99.765  1.00 27.35  ?  172  HIS A CD2 1 
ATOM   986   C CE1 . HIS A  1  172 ? 47.036  -32.031 99.000  1.00 27.57  ?  172  HIS A CE1 1 
ATOM   987   N NE2 . HIS A  1  172 ? 48.278  -31.626 98.803  1.00 27.35  ?  172  HIS A NE2 1 
ATOM   988   N N   . LEU A  1  173 ? 48.684  -26.649 102.971 1.00 26.74  ?  173  LEU A N   1 
ATOM   989   C CA  . LEU A  1  173 ? 48.407  -25.442 103.749 1.00 27.18  ?  173  LEU A CA  1 
ATOM   990   C C   . LEU A  1  173 ? 47.944  -24.325 102.823 1.00 27.55  ?  173  LEU A C   1 
ATOM   991   O O   . LEU A  1  173 ? 48.401  -23.182 102.892 1.00 27.79  ?  173  LEU A O   1 
ATOM   992   C CB  . LEU A  1  173 ? 49.626  -25.014 104.558 1.00 27.09  ?  173  LEU A CB  1 
ATOM   993   C CG  . LEU A  1  173 ? 50.064  -26.007 105.635 1.00 26.85  ?  173  LEU A CG  1 
ATOM   994   C CD1 . LEU A  1  173 ? 51.486  -25.718 106.086 1.00 26.75  ?  173  LEU A CD1 1 
ATOM   995   C CD2 . LEU A  1  173 ? 49.099  -25.985 106.808 1.00 27.24  ?  173  LEU A CD2 1 
ATOM   996   N N   . VAL A  1  174 ? 47.025  -24.662 101.937 1.00 29.86  ?  174  VAL A N   1 
ATOM   997   C CA  . VAL A  1  174 ? 46.716  -23.872 100.752 1.00 30.15  ?  174  VAL A CA  1 
ATOM   998   C C   . VAL A  1  174 ? 45.620  -22.854 101.040 1.00 30.85  ?  174  VAL A C   1 
ATOM   999   O O   . VAL A  1  174 ? 44.761  -23.050 101.904 1.00 31.14  ?  174  VAL A O   1 
ATOM   1000  C CB  . VAL A  1  174 ? 46.314  -24.805 99.594  1.00 29.99  ?  174  VAL A CB  1 
ATOM   1001  C CG1 . VAL A  1  174 ? 46.312  -24.050 98.316  1.00 30.24  ?  174  VAL A CG1 1 
ATOM   1002  C CG2 . VAL A  1  174 ? 47.267  -25.986 99.507  1.00 29.40  ?  174  VAL A CG2 1 
ATOM   1003  N N   . GLU A  1  175 ? 45.662  -21.745 100.296 1.00 30.13  ?  175  GLU A N   1 
ATOM   1004  C CA  . GLU A  1  175 ? 44.610  -20.727 100.306 1.00 30.92  ?  175  GLU A CA  1 
ATOM   1005  C C   . GLU A  1  175 ? 44.349  -20.213 101.720 1.00 31.30  ?  175  GLU A C   1 
ATOM   1006  O O   . GLU A  1  175 ? 43.215  -20.181 102.204 1.00 31.84  ?  175  GLU A O   1 
ATOM   1007  C CB  . GLU A  1  175 ? 43.330  -21.259 99.656  1.00 31.23  ?  175  GLU A CB  1 
ATOM   1008  C CG  . GLU A  1  175 ? 43.419  -21.329 98.137  1.00 31.18  ?  175  GLU A CG  1 
ATOM   1009  C CD  . GLU A  1  175 ? 42.079  -21.570 97.476  1.00 31.74  ?  175  GLU A CD  1 
ATOM   1010  O OE1 . GLU A  1  175 ? 41.042  -21.254 98.096  1.00 32.34  ?  175  GLU A OE1 1 
ATOM   1011  O OE2 . GLU A  1  175 ? 42.062  -22.077 96.334  1.00 31.64  -1 175  GLU A OE2 1 
ATOM   1012  N N   . ASN A  1  176 ? 45.432  -19.819 102.386 1.00 30.51  ?  176  ASN A N   1 
ATOM   1013  C CA  . ASN A  1  176 ? 45.374  -19.200 103.702 1.00 30.97  ?  176  ASN A CA  1 
ATOM   1014  C C   . ASN A  1  176 ? 46.135  -17.884 103.650 1.00 31.30  ?  176  ASN A C   1 
ATOM   1015  O O   . ASN A  1  176 ? 46.538  -17.442 102.570 1.00 31.22  ?  176  ASN A O   1 
ATOM   1016  C CB  . ASN A  1  176 ? 45.958  -20.126 104.769 1.00 30.50  ?  176  ASN A CB  1 
ATOM   1017  C CG  . ASN A  1  176 ? 44.949  -21.132 105.286 1.00 30.52  ?  176  ASN A CG  1 
ATOM   1018  O OD1 . ASN A  1  176 ? 44.114  -20.811 106.129 1.00 31.14  ?  176  ASN A OD1 1 
ATOM   1019  N ND2 . ASN A  1  176 ? 45.025  -22.359 104.783 1.00 29.92  ?  176  ASN A ND2 1 
ATOM   1020  N N   . LYS A  1  177 ? 46.328  -17.243 104.795 1.00 31.14  ?  177  LYS A N   1 
ATOM   1021  C CA  . LYS A  1  177 ? 47.061  -15.988 104.868 1.00 31.57  ?  177  LYS A CA  1 
ATOM   1022  C C   . LYS A  1  177 ? 48.266  -16.113 105.794 1.00 31.33  ?  177  LYS A C   1 
ATOM   1023  O O   . LYS A  1  177 ? 48.550  -15.225 106.600 1.00 31.97  ?  177  LYS A O   1 
ATOM   1024  C CB  . LYS A  1  177 ? 46.144  -14.850 105.312 1.00 32.64  ?  177  LYS A CB  1 
ATOM   1025  C CG  . LYS A  1  177 ? 45.050  -14.509 104.304 1.00 33.04  ?  177  LYS A CG  1 
ATOM   1026  C CD  . LYS A  1  177 ? 45.632  -13.905 103.032 1.00 32.91  ?  177  LYS A CD  1 
ATOM   1027  C CE  . LYS A  1  177 ? 44.784  -14.220 101.804 1.00 32.90  ?  177  LYS A CE  1 
ATOM   1028  N NZ  . LYS A  1  177 ? 44.609  -15.685 101.586 1.00 32.14  ?  177  LYS A NZ  1 
ATOM   1029  N N   . LEU A  1  178 ? 48.991  -17.225 105.683 1.00 31.39  ?  178  LEU A N   1 
ATOM   1030  C CA  . LEU A  1  178 ? 50.179  -17.428 106.503 1.00 31.19  ?  178  LEU A CA  1 
ATOM   1031  C C   . LEU A  1  178 ? 51.318  -16.538 106.017 1.00 31.28  ?  178  LEU A C   1 
ATOM   1032  O O   . LEU A  1  178 ? 51.680  -16.564 104.838 1.00 30.90  ?  178  LEU A O   1 
ATOM   1033  C CB  . LEU A  1  178 ? 50.606  -18.896 106.468 1.00 30.36  ?  178  LEU A CB  1 
ATOM   1034  C CG  . LEU A  1  178 ? 49.526  -19.958 106.680 1.00 30.17  ?  178  LEU A CG  1 
ATOM   1035  C CD1 . LEU A  1  178 ? 50.091  -21.346 106.431 1.00 29.38  ?  178  LEU A CD1 1 
ATOM   1036  C CD2 . LEU A  1  178 ? 48.940  -19.862 108.079 1.00 30.80  ?  178  LEU A CD2 1 
ATOM   1037  N N   . ASN A  1  179 ? 51.889  -15.759 106.931 1.00 39.68  ?  179  ASN A N   1 
ATOM   1038  C CA  . ASN A  1  179 ? 52.994  -14.863 106.625 1.00 39.97  ?  179  ASN A CA  1 
ATOM   1039  C C   . ASN A  1  179 ? 54.273  -15.349 107.293 1.00 40.03  ?  179  ASN A C   1 
ATOM   1040  O O   . ASN A  1  179 ? 54.247  -16.086 108.282 1.00 40.15  ?  179  ASN A O   1 
ATOM   1041  C CB  . ASN A  1  179 ? 52.690  -13.427 107.066 1.00 41.02  ?  179  ASN A CB  1 
ATOM   1042  C CG  . ASN A  1  179 ? 52.349  -13.330 108.537 1.00 41.87  ?  179  ASN A CG  1 
ATOM   1043  O OD1 . ASN A  1  179 ? 51.974  -14.321 109.162 1.00 41.65  ?  179  ASN A OD1 1 
ATOM   1044  N ND2 . ASN A  1  179 ? 52.479  -12.134 109.101 1.00 42.93  ?  179  ASN A ND2 1 
ATOM   1045  N N   . GLY A  1  180 ? 55.397  -14.924 106.735 1.00 35.64  ?  180  GLY A N   1 
ATOM   1046  C CA  . GLY A  1  180 ? 56.707  -15.305 107.217 1.00 35.80  ?  180  GLY A CA  1 
ATOM   1047  C C   . GLY A  1  180 ? 57.475  -16.092 106.174 1.00 34.96  ?  180  GLY A C   1 
ATOM   1048  O O   . GLY A  1  180 ? 57.023  -16.302 105.049 1.00 34.29  ?  180  GLY A O   1 
ATOM   1049  N N   . SER A  1  181 ? 58.663  -16.527 106.575 1.00 36.15  ?  181  SER A N   1 
ATOM   1050  C CA  . SER A  1  181 ? 59.504  -17.347 105.719 1.00 35.52  ?  181  SER A CA  1 
ATOM   1051  C C   . SER A  1  181 ? 59.245  -18.822 105.990 1.00 34.96  ?  181  SER A C   1 
ATOM   1052  O O   . SER A  1  181 ? 58.872  -19.213 107.100 1.00 35.27  ?  181  SER A O   1 
ATOM   1053  C CB  . SER A  1  181 ? 60.982  -17.025 105.941 1.00 36.12  ?  181  SER A CB  1 
ATOM   1054  O OG  . SER A  1  181 ? 61.299  -15.730 105.460 1.00 36.56  ?  181  SER A OG  1 
ATOM   1055  N N   . ILE A  1  182 ? 59.442  -19.642 104.963 1.00 32.51  ?  182  ILE A N   1 
ATOM   1056  C CA  . ILE A  1  182 ? 59.298  -21.086 105.120 1.00 32.01  ?  182  ILE A CA  1 
ATOM   1057  C C   . ILE A  1  182 ? 60.469  -21.564 105.968 1.00 32.51  ?  182  ILE A C   1 
ATOM   1058  O O   . ILE A  1  182 ? 61.629  -21.293 105.626 1.00 32.78  ?  182  ILE A O   1 
ATOM   1059  C CB  . ILE A  1  182 ? 59.255  -21.808 103.764 1.00 31.24  ?  182  ILE A CB  1 
ATOM   1060  C CG1 . ILE A  1  182 ? 58.023  -21.382 102.964 1.00 30.89  ?  182  ILE A CG1 1 
ATOM   1061  C CG2 . ILE A  1  182 ? 59.256  -23.316 103.967 1.00 30.85  ?  182  ILE A CG2 1 
ATOM   1062  C CD1 . ILE A  1  182 ? 57.943  -22.014 101.588 1.00 30.29  ?  182  ILE A CD1 1 
ATOM   1063  N N   . PRO A  1  183 ? 60.217  -22.249 107.082 1.00 31.68  ?  183  PRO A N   1 
ATOM   1064  C CA  . PRO A  1  183 ? 61.323  -22.686 107.942 1.00 32.32  ?  183  PRO A CA  1 
ATOM   1065  C C   . PRO A  1  183 ? 62.263  -23.626 107.205 1.00 31.97  ?  183  PRO A C   1 
ATOM   1066  O O   . PRO A  1  183 ? 61.842  -24.430 106.370 1.00 31.19  ?  183  PRO A O   1 
ATOM   1067  C CB  . PRO A  1  183 ? 60.615  -23.394 109.104 1.00 32.51  ?  183  PRO A CB  1 
ATOM   1068  C CG  . PRO A  1  183 ? 59.211  -22.909 109.061 1.00 32.24  ?  183  PRO A CG  1 
ATOM   1069  C CD  . PRO A  1  183 ? 58.904  -22.621 107.629 1.00 31.49  ?  183  PRO A CD  1 
ATOM   1070  N N   . SER A  1  184 ? 63.555  -23.509 107.521 1.00 35.22  ?  184  SER A N   1 
ATOM   1071  C CA  . SER A  1  184 ? 64.538  -24.437 106.974 1.00 35.10  ?  184  SER A CA  1 
ATOM   1072  C C   . SER A  1  184 ? 64.228  -25.874 107.367 1.00 34.82  ?  184  SER A C   1 
ATOM   1073  O O   . SER A  1  184 ? 64.582  -26.809 106.639 1.00 34.43  ?  184  SER A O   1 
ATOM   1074  C CB  . SER A  1  184 ? 65.940  -24.050 107.446 1.00 36.11  ?  184  SER A CB  1 
ATOM   1075  O OG  . SER A  1  184 ? 66.074  -22.643 107.547 1.00 37.16  ?  184  SER A OG  1 
ATOM   1076  N N   . GLU A  1  185 ? 63.559  -26.066 108.506 1.00 35.13  ?  185  GLU A N   1 
ATOM   1077  C CA  . GLU A  1  185 ? 63.287  -27.391 109.047 1.00 34.99  ?  185  GLU A CA  1 
ATOM   1078  C C   . GLU A  1  185 ? 62.285  -28.184 108.218 1.00 33.97  ?  185  GLU A C   1 
ATOM   1079  O O   . GLU A  1  185 ? 62.131  -29.386 108.457 1.00 33.83  ?  185  GLU A O   1 
ATOM   1080  C CB  . GLU A  1  185 ? 62.789  -27.267 110.489 1.00 35.66  ?  185  GLU A CB  1 
ATOM   1081  C CG  . GLU A  1  185 ? 63.847  -26.769 111.469 1.00 36.99  ?  185  GLU A CG  1 
ATOM   1082  C CD  . GLU A  1  185 ? 64.056  -25.264 111.401 1.00 37.47  ?  185  GLU A CD  1 
ATOM   1083  O OE1 . GLU A  1  185 ? 63.245  -24.578 110.744 1.00 37.34  ?  185  GLU A OE1 1 
ATOM   1084  O OE2 . GLU A  1  185 ? 65.032  -24.768 112.002 1.00 38.38  -1 185  GLU A OE2 1 
ATOM   1085  N N   . ILE A  1  186 ? 61.604  -27.549 107.260 1.00 33.29  ?  186  ILE A N   1 
ATOM   1086  C CA  . ILE A  1  186 ? 60.716  -28.288 106.367 1.00 32.45  ?  186  ILE A CA  1 
ATOM   1087  C C   . ILE A  1  186 ? 61.511  -29.294 105.546 1.00 32.22  ?  186  ILE A C   1 
ATOM   1088  O O   . ILE A  1  186 ? 60.999  -30.362 105.185 1.00 31.77  ?  186  ILE A O   1 
ATOM   1089  C CB  . ILE A  1  186 ? 59.926  -27.312 105.473 1.00 32.03  ?  186  ILE A CB  1 
ATOM   1090  C CG1 . ILE A  1  186 ? 59.144  -26.318 106.334 1.00 32.38  ?  186  ILE A CG1 1 
ATOM   1091  C CG2 . ILE A  1  186 ? 58.972  -28.066 104.560 1.00 31.30  ?  186  ILE A CG2 1 
ATOM   1092  C CD1 . ILE A  1  186 ? 58.215  -26.971 107.336 1.00 32.44  ?  186  ILE A CD1 1 
ATOM   1093  N N   . GLY A  1  187 ? 62.775  -28.982 105.251 1.00 33.62  ?  187  GLY A N   1 
ATOM   1094  C CA  . GLY A  1  187 ? 63.670  -29.896 104.560 1.00 33.61  ?  187  GLY A CA  1 
ATOM   1095  C C   . GLY A  1  187 ? 63.894  -31.220 105.268 1.00 33.86  ?  187  GLY A C   1 
ATOM   1096  O O   . GLY A  1  187 ? 64.524  -32.112 104.687 1.00 34.04  ?  187  GLY A O   1 
ATOM   1097  N N   . ARG A  1  188 ? 63.417  -31.365 106.504 1.00 34.56  ?  188  ARG A N   1 
ATOM   1098  C CA  . ARG A  1  188 ? 63.540  -32.618 107.237 1.00 34.85  ?  188  ARG A CA  1 
ATOM   1099  C C   . ARG A  1  188 ? 62.515  -33.662 106.815 1.00 34.34  ?  188  ARG A C   1 
ATOM   1100  O O   . ARG A  1  188 ? 62.624  -34.818 107.240 1.00 34.35  ?  188  ARG A O   1 
ATOM   1101  C CB  . ARG A  1  188 ? 63.402  -32.363 108.739 1.00 35.70  ?  188  ARG A CB  1 
ATOM   1102  C CG  . ARG A  1  188 ? 64.529  -31.546 109.335 1.00 36.85  ?  188  ARG A CG  1 
ATOM   1103  C CD  . ARG A  1  188 ? 64.421  -31.499 110.848 1.00 37.32  ?  188  ARG A CD  1 
ATOM   1104  N NE  . ARG A  1  188 ? 65.504  -30.727 111.441 1.00 38.68  ?  188  ARG A NE  1 
ATOM   1105  C CZ  . ARG A  1  188 ? 66.117  -31.046 112.573 1.00 39.48  ?  188  ARG A CZ  1 
ATOM   1106  N NH1 . ARG A  1  188 ? 65.770  -32.116 113.268 1.00 39.65  ?  188  ARG A NH1 1 
ATOM   1107  N NH2 . ARG A  1  188 ? 67.104  -30.273 113.016 1.00 40.52  ?  188  ARG A NH2 1 
ATOM   1108  N N   . LEU A  1  189 ? 61.532  -33.292 105.992 1.00 34.22  ?  189  LEU A N   1 
ATOM   1109  C CA  . LEU A  1  189 ? 60.437  -34.192 105.626 1.00 33.34  ?  189  LEU A CA  1 
ATOM   1110  C C   . LEU A  1  189 ? 60.877  -35.075 104.457 1.00 33.05  ?  189  LEU A C   1 
ATOM   1111  O O   . LEU A  1  189 ? 60.414  -34.952 103.321 1.00 32.88  ?  189  LEU A O   1 
ATOM   1112  C CB  . LEU A  1  189 ? 59.187  -33.392 105.287 1.00 33.11  ?  189  LEU A CB  1 
ATOM   1113  C CG  . LEU A  1  189 ? 58.669  -32.429 106.358 1.00 32.98  ?  189  LEU A CG  1 
ATOM   1114  C CD1 . LEU A  1  189 ? 57.345  -31.818 105.930 1.00 32.71  ?  189  LEU A CD1 1 
ATOM   1115  C CD2 . LEU A  1  189 ? 58.522  -33.140 107.689 1.00 33.41  ?  189  LEU A CD2 1 
ATOM   1116  N N   . THR A  1  190 ? 61.791  -35.998 104.769 1.00 32.56  ?  190  THR A N   1 
ATOM   1117  C CA  . THR A  1  190 ? 62.392  -36.852 103.749 1.00 32.57  ?  190  THR A CA  1 
ATOM   1118  C C   . THR A  1  190 ? 61.372  -37.726 103.029 1.00 32.41  ?  190  THR A C   1 
ATOM   1119  O O   . THR A  1  190 ? 61.620  -38.134 101.889 1.00 32.66  ?  190  THR A O   1 
ATOM   1120  C CB  . THR A  1  190 ? 63.478  -37.727 104.377 1.00 33.46  ?  190  THR A CB  1 
ATOM   1121  O OG1 . THR A  1  190 ? 62.926  -38.462 105.476 1.00 33.50  ?  190  THR A OG1 1 
ATOM   1122  C CG2 . THR A  1  190 ? 64.626  -36.864 104.879 1.00 34.27  ?  190  THR A CG2 1 
ATOM   1123  N N   . LYS A  1  191 ? 60.237  -38.026 103.658 1.00 28.40  ?  191  LYS A N   1 
ATOM   1124  C CA  . LYS A  1  191 ? 59.223  -38.879 103.053 1.00 28.26  ?  191  LYS A CA  1 
ATOM   1125  C C   . LYS A  1  191 ? 58.134  -38.095 102.332 1.00 27.90  ?  191  LYS A C   1 
ATOM   1126  O O   . LYS A  1  191 ? 57.205  -38.708 101.795 1.00 27.83  ?  191  LYS A O   1 
ATOM   1127  C CB  . LYS A  1  191 ? 58.585  -39.778 104.118 1.00 28.36  ?  191  LYS A CB  1 
ATOM   1128  C CG  . LYS A  1  191 ? 59.435  -40.978 104.505 1.00 28.84  ?  191  LYS A CG  1 
ATOM   1129  C CD  . LYS A  1  191 ? 58.675  -41.935 105.409 1.00 28.96  ?  191  LYS A CD  1 
ATOM   1130  C CE  . LYS A  1  191 ? 59.614  -42.941 106.055 1.00 29.55  ?  191  LYS A CE  1 
ATOM   1131  N NZ  . LYS A  1  191 ? 58.913  -43.799 107.050 1.00 29.73  ?  191  LYS A NZ  1 
ATOM   1132  N N   . VAL A  1  192 ? 58.221  -36.764 102.304 1.00 29.08  ?  192  VAL A N   1 
ATOM   1133  C CA  . VAL A  1  192 ? 57.187  -35.964 101.661 1.00 28.85  ?  192  VAL A CA  1 
ATOM   1134  C C   . VAL A  1  192 ? 57.295  -36.099 100.147 1.00 28.89  ?  192  VAL A C   1 
ATOM   1135  O O   . VAL A  1  192 ? 58.393  -36.232 99.587  1.00 29.06  ?  192  VAL A O   1 
ATOM   1136  C CB  . VAL A  1  192 ? 57.274  -34.494 102.110 1.00 28.76  ?  192  VAL A CB  1 
ATOM   1137  C CG1 . VAL A  1  192 ? 58.299  -33.719 101.292 1.00 28.83  ?  192  VAL A CG1 1 
ATOM   1138  C CG2 . VAL A  1  192 ? 55.907  -33.835 102.016 1.00 28.79  ?  192  VAL A CG2 1 
ATOM   1139  N N   . THR A  1  193 ? 56.145  -36.117 99.481  1.00 28.36  ?  193  THR A N   1 
ATOM   1140  C CA  . THR A  1  193 ? 56.078  -36.170 98.028  1.00 28.45  ?  193  THR A CA  1 
ATOM   1141  C C   . THR A  1  193 ? 55.424  -34.948 97.407  1.00 28.40  ?  193  THR A C   1 
ATOM   1142  O O   . THR A  1  193 ? 55.795  -34.569 96.293  1.00 28.52  ?  193  THR A O   1 
ATOM   1143  C CB  . THR A  1  193 ? 55.312  -37.421 97.572  1.00 28.56  ?  193  THR A CB  1 
ATOM   1144  O OG1 . THR A  1  193 ? 54.084  -37.522 98.304  1.00 28.45  ?  193  THR A OG1 1 
ATOM   1145  C CG2 . THR A  1  193 ? 56.141  -38.671 97.818  1.00 28.75  ?  193  THR A CG2 1 
ATOM   1146  N N   . GLU A  1  194 ? 54.471  -34.322 98.093  1.00 28.71  ?  194  GLU A N   1 
ATOM   1147  C CA  . GLU A  1  194 ? 53.800  -33.125 97.605  1.00 28.94  ?  194  GLU A CA  1 
ATOM   1148  C C   . GLU A  1  194 ? 53.747  -32.088 98.716  1.00 29.02  ?  194  GLU A C   1 
ATOM   1149  O O   . GLU A  1  194 ? 53.362  -32.403 99.848  1.00 28.65  ?  194  GLU A O   1 
ATOM   1150  C CB  . GLU A  1  194 ? 52.386  -33.442 97.107  1.00 28.86  ?  194  GLU A CB  1 
ATOM   1151  C CG  . GLU A  1  194 ? 51.585  -32.212 96.717  1.00 29.00  ?  194  GLU A CG  1 
ATOM   1152  C CD  . GLU A  1  194 ? 50.348  -32.550 95.913  1.00 29.44  ?  194  GLU A CD  1 
ATOM   1153  O OE1 . GLU A  1  194 ? 50.488  -32.869 94.713  1.00 29.68  ?  194  GLU A OE1 1 
ATOM   1154  O OE2 . GLU A  1  194 ? 49.236  -32.502 96.481  1.00 29.61  -1 194  GLU A OE2 1 
ATOM   1155  N N   . ILE A  1  195 ? 54.141  -30.859 98.394  1.00 26.74  ?  195  ILE A N   1 
ATOM   1156  C CA  . ILE A  1  195 ? 54.071  -29.731 99.315  1.00 26.78  ?  195  ILE A CA  1 
ATOM   1157  C C   . ILE A  1  195 ? 53.355  -28.604 98.585  1.00 26.99  ?  195  ILE A C   1 
ATOM   1158  O O   . ILE A  1  195 ? 53.882  -28.062 97.605  1.00 27.08  ?  195  ILE A O   1 
ATOM   1159  C CB  . ILE A  1  195 ? 55.458  -29.280 99.794  1.00 26.76  ?  195  ILE A CB  1 
ATOM   1160  C CG1 . ILE A  1  195 ? 56.131  -30.384 100.613 1.00 26.65  ?  195  ILE A CG1 1 
ATOM   1161  C CG2 . ILE A  1  195 ? 55.351  -28.000 100.609 1.00 26.88  ?  195  ILE A CG2 1 
ATOM   1162  C CD1 . ILE A  1  195 ? 57.574  -30.092 100.961 1.00 26.71  ?  195  ILE A CD1 1 
ATOM   1163  N N   . ALA A  1  196 ? 52.158  -28.254 99.050  1.00 26.85  ?  196  ALA A N   1 
ATOM   1164  C CA  . ALA A  1  196 ? 51.359  -27.192 98.447  1.00 27.16  ?  196  ALA A CA  1 
ATOM   1165  C C   . ALA A  1  196 ? 51.056  -26.151 99.517  1.00 27.37  ?  196  ALA A C   1 
ATOM   1166  O O   . ALA A  1  196 ? 50.296  -26.420 100.454 1.00 27.44  ?  196  ALA A O   1 
ATOM   1167  C CB  . ALA A  1  196 ? 50.072  -27.752 97.842  1.00 27.31  ?  196  ALA A CB  1 
ATOM   1168  N N   . ILE A  1  197 ? 51.664  -24.971 99.385  1.00 27.96  ?  197  ILE A N   1 
ATOM   1169  C CA  . ILE A  1  197 ? 51.428  -23.865 100.308 1.00 28.28  ?  197  ILE A CA  1 
ATOM   1170  C C   . ILE A  1  197 ? 51.065  -22.614 99.515  1.00 28.70  ?  197  ILE A C   1 
ATOM   1171  O O   . ILE A  1  197 ? 51.272  -21.488 99.982  1.00 29.02  ?  197  ILE A O   1 
ATOM   1172  C CB  . ILE A  1  197 ? 52.643  -23.608 101.221 1.00 28.18  ?  197  ILE A CB  1 
ATOM   1173  C CG1 . ILE A  1  197 ? 53.347  -24.916 101.580 1.00 27.76  ?  197  ILE A CG1 1 
ATOM   1174  C CG2 . ILE A  1  197 ? 52.204  -22.931 102.514 1.00 28.52  ?  197  ILE A CG2 1 
ATOM   1175  C CD1 . ILE A  1  197 ? 54.713  -24.720 102.205 1.00 27.70  ?  197  ILE A CD1 1 
ATOM   1176  N N   . TYR A  1  198 ? 50.544  -22.793 98.303  1.00 29.89  ?  198  TYR A N   1 
ATOM   1177  C CA  . TYR A  1  198 ? 50.279  -21.640 97.455  1.00 30.33  ?  198  TYR A CA  1 
ATOM   1178  C C   . TYR A  1  198 ? 49.050  -20.877 97.947  1.00 30.87  ?  198  TYR A C   1 
ATOM   1179  O O   . TYR A  1  198 ? 48.298  -21.335 98.813  1.00 30.90  ?  198  TYR A O   1 
ATOM   1180  C CB  . TYR A  1  198 ? 50.096  -22.066 95.997  1.00 30.33  ?  198  TYR A CB  1 
ATOM   1181  C CG  . TYR A  1  198 ? 48.922  -22.983 95.721  1.00 30.37  ?  198  TYR A CG  1 
ATOM   1182  C CD1 . TYR A  1  198 ? 47.666  -22.468 95.414  1.00 30.90  ?  198  TYR A CD1 1 
ATOM   1183  C CD2 . TYR A  1  198 ? 49.076  -24.363 95.740  1.00 29.96  ?  198  TYR A CD2 1 
ATOM   1184  C CE1 . TYR A  1  198 ? 46.598  -23.304 95.132  1.00 31.02  ?  198  TYR A CE1 1 
ATOM   1185  C CE2 . TYR A  1  198 ? 48.013  -25.206 95.473  1.00 30.05  ?  198  TYR A CE2 1 
ATOM   1186  C CZ  . TYR A  1  198 ? 46.777  -24.673 95.168  1.00 30.57  ?  198  TYR A CZ  1 
ATOM   1187  O OH  . TYR A  1  198 ? 45.718  -25.514 94.909  1.00 30.73  ?  198  TYR A OH  1 
ATOM   1188  N N   . ASP A  1  199 ? 48.859  -19.687 97.372  1.00 29.59  ?  199  ASP A N   1 
ATOM   1189  C CA  . ASP A  1  199 ? 47.798  -18.756 97.759  1.00 30.26  ?  199  ASP A CA  1 
ATOM   1190  C C   . ASP A  1  199 ? 47.905  -18.399 99.243  1.00 30.38  ?  199  ASP A C   1 
ATOM   1191  O O   . ASP A  1  199 ? 47.004  -18.648 100.046 1.00 30.60  ?  199  ASP A O   1 
ATOM   1192  C CB  . ASP A  1  199 ? 46.417  -19.325 97.413  1.00 30.51  ?  199  ASP A CB  1 
ATOM   1193  C CG  . ASP A  1  199 ? 45.364  -18.246 97.251  1.00 31.37  ?  199  ASP A CG  1 
ATOM   1194  O OD1 . ASP A  1  199 ? 45.568  -17.127 97.768  1.00 31.77  ?  199  ASP A OD1 1 
ATOM   1195  O OD2 . ASP A  1  199 ? 44.334  -18.516 96.599  1.00 31.71  -1 199  ASP A OD2 1 
ATOM   1196  N N   . ASN A  1  200 ? 49.043  -17.802 99.591  1.00 30.62  ?  200  ASN A N   1 
ATOM   1197  C CA  . ASN A  1  200 ? 49.357  -17.426 100.965 1.00 30.79  ?  200  ASN A CA  1 
ATOM   1198  C C   . ASN A  1  200 ? 50.115  -16.103 100.939 1.00 31.20  ?  200  ASN A C   1 
ATOM   1199  O O   . ASN A  1  200 ? 50.182  -15.421 99.911  1.00 31.43  ?  200  ASN A O   1 
ATOM   1200  C CB  . ASN A  1  200 ? 50.144  -18.541 101.668 1.00 30.16  ?  200  ASN A CB  1 
ATOM   1201  C CG  . ASN A  1  200 ? 49.247  -19.501 102.422 1.00 30.06  ?  200  ASN A CG  1 
ATOM   1202  O OD1 . ASN A  1  200 ? 48.851  -19.233 103.556 1.00 30.42  ?  200  ASN A OD1 1 
ATOM   1203  N ND2 . ASN A  1  200 ? 48.911  -20.620 101.791 1.00 29.64  ?  200  ASN A ND2 1 
ATOM   1204  N N   . LEU A  1  201 ? 50.694  -15.740 102.083 1.00 28.21  ?  201  LEU A N   1 
ATOM   1205  C CA  . LEU A  1  201 ? 51.464  -14.510 102.223 1.00 28.69  ?  201  LEU A CA  1 
ATOM   1206  C C   . LEU A  1  201 ? 52.902  -14.801 102.639 1.00 28.32  ?  201  LEU A C   1 
ATOM   1207  O O   . LEU A  1  201 ? 53.505  -14.035 103.392 1.00 28.77  ?  201  LEU A O   1 
ATOM   1208  C CB  . LEU A  1  201 ? 50.797  -13.569 103.227 1.00 29.55  ?  201  LEU A CB  1 
ATOM   1209  C CG  . LEU A  1  201 ? 49.331  -13.227 102.958 1.00 30.08  ?  201  LEU A CG  1 
ATOM   1210  C CD1 . LEU A  1  201 ? 48.756  -12.434 104.117 1.00 30.98  ?  201  LEU A CD1 1 
ATOM   1211  C CD2 . LEU A  1  201 ? 49.196  -12.457 101.656 1.00 30.34  ?  201  LEU A CD2 1 
ATOM   1212  N N   . LEU A  1  202 ? 53.461  -15.904 102.148 1.00 30.33  ?  202  LEU A N   1 
ATOM   1213  C CA  . LEU A  1  202 ? 54.804  -16.303 102.537 1.00 30.01  ?  202  LEU A CA  1 
ATOM   1214  C C   . LEU A  1  202 ? 55.849  -15.341 101.982 1.00 30.28  ?  202  LEU A C   1 
ATOM   1215  O O   . LEU A  1  202 ? 55.696  -14.771 100.899 1.00 30.42  ?  202  LEU A O   1 
ATOM   1216  C CB  . LEU A  1  202 ? 55.099  -17.726 102.058 1.00 29.26  ?  202  LEU A CB  1 
ATOM   1217  C CG  . LEU A  1  202 ? 54.140  -18.816 102.537 1.00 28.97  ?  202  LEU A CG  1 
ATOM   1218  C CD1 . LEU A  1  202 ? 54.646  -20.184 102.125 1.00 28.33  ?  202  LEU A CD1 1 
ATOM   1219  C CD2 . LEU A  1  202 ? 53.959  -18.747 104.046 1.00 29.29  ?  202  LEU A CD2 1 
ATOM   1220  N N   . THR A  1  203 ? 56.923  -15.161 102.751 1.00 31.85  ?  203  THR A N   1 
ATOM   1221  C CA  . THR A  1  203 ? 58.009  -14.262 102.381 1.00 32.26  ?  203  THR A CA  1 
ATOM   1222  C C   . THR A  1  203 ? 59.346  -14.985 102.477 1.00 32.12  ?  203  THR A C   1 
ATOM   1223  O O   . THR A  1  203 ? 59.388  -16.193 102.731 1.00 31.66  ?  203  THR A O   1 
ATOM   1224  C CB  . THR A  1  203 ? 58.021  -13.020 103.277 1.00 33.24  ?  203  THR A CB  1 
ATOM   1225  O OG1 . THR A  1  203 ? 58.327  -13.406 104.622 1.00 33.63  ?  203  THR A OG1 1 
ATOM   1226  C CG2 . THR A  1  203 ? 56.669  -12.318 103.250 1.00 33.51  ?  203  THR A CG2 1 
ATOM   1227  N N   . GLY A  1  204 ? 60.440  -14.259 102.271 1.00 36.30  ?  204  GLY A N   1 
ATOM   1228  C CA  . GLY A  1  204 ? 61.761  -14.827 102.382 1.00 36.36  ?  204  GLY A CA  1 
ATOM   1229  C C   . GLY A  1  204 ? 62.088  -15.774 101.246 1.00 35.62  ?  204  GLY A C   1 
ATOM   1230  O O   . GLY A  1  204 ? 61.301  -15.960 100.313 1.00 35.32  ?  204  GLY A O   1 
ATOM   1231  N N   . PRO A  1  205 ? 63.263  -16.389 101.302 1.00 34.88  ?  205  PRO A N   1 
ATOM   1232  C CA  . PRO A  1  205 ? 63.690  -17.281 100.221 1.00 34.33  ?  205  PRO A CA  1 
ATOM   1233  C C   . PRO A  1  205 ? 63.104  -18.677 100.379 1.00 33.69  ?  205  PRO A C   1 
ATOM   1234  O O   . PRO A  1  205 ? 62.571  -19.051 101.424 1.00 33.71  ?  205  PRO A O   1 
ATOM   1235  C CB  . PRO A  1  205 ? 65.212  -17.306 100.375 1.00 34.88  ?  205  PRO A CB  1 
ATOM   1236  C CG  . PRO A  1  205 ? 65.426  -17.108 101.838 1.00 35.53  ?  205  PRO A CG  1 
ATOM   1237  C CD  . PRO A  1  205 ? 64.317  -16.202 102.315 1.00 35.66  ?  205  PRO A CD  1 
ATOM   1238  N N   . ILE A  1  206 ? 63.218  -19.451 99.308  1.00 34.15  ?  206  ILE A N   1 
ATOM   1239  C CA  . ILE A  1  206 ? 62.943  -20.887 99.412  1.00 33.65  ?  206  ILE A CA  1 
ATOM   1240  C C   . ILE A  1  206 ? 64.089  -21.545 100.170 1.00 34.01  ?  206  ILE A C   1 
ATOM   1241  O O   . ILE A  1  206 ? 65.264  -21.288 99.851  1.00 34.43  ?  206  ILE A O   1 
ATOM   1242  C CB  . ILE A  1  206 ? 62.774  -21.503 98.021  1.00 33.18  ?  206  ILE A CB  1 
ATOM   1243  C CG1 . ILE A  1  206 ? 61.536  -20.931 97.329  1.00 32.99  ?  206  ILE A CG1 1 
ATOM   1244  C CG2 . ILE A  1  206 ? 62.682  -23.021 98.110  1.00 32.80  ?  206  ILE A CG2 1 
ATOM   1245  C CD1 . ILE A  1  206 ? 61.484  -21.221 95.847  1.00 33.02  ?  206  ILE A CD1 1 
ATOM   1246  N N   . PRO A  1  207 ? 63.815  -22.364 101.183 1.00 35.55  ?  207  PRO A N   1 
ATOM   1247  C CA  . PRO A  1  207 ? 64.907  -22.993 101.941 1.00 36.09  ?  207  PRO A CA  1 
ATOM   1248  C C   . PRO A  1  207 ? 65.733  -23.910 101.053 1.00 35.90  ?  207  PRO A C   1 
ATOM   1249  O O   . PRO A  1  207 ? 65.210  -24.836 100.428 1.00 35.33  ?  207  PRO A O   1 
ATOM   1250  C CB  . PRO A  1  207 ? 64.173  -23.773 103.039 1.00 35.94  ?  207  PRO A CB  1 
ATOM   1251  C CG  . PRO A  1  207 ? 62.826  -23.132 103.133 1.00 35.63  ?  207  PRO A CG  1 
ATOM   1252  C CD  . PRO A  1  207 ? 62.494  -22.694 101.742 1.00 35.31  ?  207  PRO A CD  1 
ATOM   1253  N N   . SER A  1  208 ? 67.040  -23.641 100.996 1.00 37.45  ?  208  SER A N   1 
ATOM   1254  C CA  . SER A  1  208 ? 67.938  -24.495 100.227 1.00 37.51  ?  208  SER A CA  1 
ATOM   1255  C C   . SER A  1  208 ? 68.017  -25.900 100.805 1.00 37.48  ?  208  SER A C   1 
ATOM   1256  O O   . SER A  1  208 ? 68.493  -26.814 100.123 1.00 37.43  ?  208  SER A O   1 
ATOM   1257  C CB  . SER A  1  208 ? 69.334  -23.873 100.162 1.00 38.34  ?  208  SER A CB  1 
ATOM   1258  O OG  . SER A  1  208 ? 69.868  -23.678 101.460 1.00 39.56  ?  208  SER A OG  1 
ATOM   1259  N N   . SER A  1  209 ? 67.557  -26.092 102.042 1.00 36.69  ?  209  SER A N   1 
ATOM   1260  C CA  . SER A  1  209 ? 67.426  -27.421 102.625 1.00 36.62  ?  209  SER A CA  1 
ATOM   1261  C C   . SER A  1  209 ? 66.356  -28.261 101.941 1.00 35.77  ?  209  SER A C   1 
ATOM   1262  O O   . SER A  1  209 ? 66.188  -29.430 102.307 1.00 35.69  ?  209  SER A O   1 
ATOM   1263  C CB  . SER A  1  209 ? 67.119  -27.309 104.120 1.00 37.03  ?  209  SER A CB  1 
ATOM   1264  O OG  . SER A  1  209 ? 65.907  -26.607 104.342 1.00 36.61  ?  209  SER A OG  1 
ATOM   1265  N N   . PHE A  1  210 ? 65.633  -27.701 100.968 1.00 35.11  ?  210  PHE A N   1 
ATOM   1266  C CA  . PHE A  1  210 ? 64.634  -28.470 100.236 1.00 34.43  ?  210  PHE A CA  1 
ATOM   1267  C C   . PHE A  1  210 ? 65.263  -29.534 99.348  1.00 34.48  ?  210  PHE A C   1 
ATOM   1268  O O   . PHE A  1  210 ? 64.562  -30.455 98.917  1.00 34.27  ?  210  PHE A O   1 
ATOM   1269  C CB  . PHE A  1  210 ? 63.766  -27.534 99.392  1.00 34.04  ?  210  PHE A CB  1 
ATOM   1270  C CG  . PHE A  1  210 ? 62.530  -27.052 100.097 1.00 33.90  ?  210  PHE A CG  1 
ATOM   1271  C CD1 . PHE A  1  210 ? 62.481  -27.001 101.480 1.00 34.10  ?  210  PHE A CD1 1 
ATOM   1272  C CD2 . PHE A  1  210 ? 61.421  -26.639 99.376  1.00 33.44  ?  210  PHE A CD2 1 
ATOM   1273  C CE1 . PHE A  1  210 ? 61.346  -26.556 102.132 1.00 33.99  ?  210  PHE A CE1 1 
ATOM   1274  C CE2 . PHE A  1  210 ? 60.283  -26.191 100.023 1.00 33.30  ?  210  PHE A CE2 1 
ATOM   1275  C CZ  . PHE A  1  210 ? 60.246  -26.150 101.403 1.00 33.57  ?  210  PHE A CZ  1 
ATOM   1276  N N   . GLY A  1  211 ? 66.563  -29.424 99.061  1.00 34.58  ?  211  GLY A N   1 
ATOM   1277  C CA  . GLY A  1  211 ? 67.248  -30.492 98.353  1.00 34.77  ?  211  GLY A CA  1 
ATOM   1278  C C   . GLY A  1  211 ? 67.204  -31.815 99.092  1.00 34.84  ?  211  GLY A C   1 
ATOM   1279  O O   . GLY A  1  211 ? 67.305  -32.879 98.476  1.00 34.83  ?  211  GLY A O   1 
ATOM   1280  N N   . ASN A  1  212 ? 67.053  -31.769 100.418 1.00 36.44  ?  212  ASN A N   1 
ATOM   1281  C CA  . ASN A  1  212 ? 66.944  -32.978 101.224 1.00 36.57  ?  212  ASN A CA  1 
ATOM   1282  C C   . ASN A  1  212 ? 65.618  -33.704 101.037 1.00 35.88  ?  212  ASN A C   1 
ATOM   1283  O O   . ASN A  1  212 ? 65.457  -34.805 101.576 1.00 36.43  ?  212  ASN A O   1 
ATOM   1284  C CB  . ASN A  1  212 ? 67.145  -32.642 102.704 1.00 37.06  ?  212  ASN A CB  1 
ATOM   1285  C CG  . ASN A  1  212 ? 68.580  -32.267 103.027 1.00 38.00  ?  212  ASN A CG  1 
ATOM   1286  O OD1 . ASN A  1  212 ? 69.427  -32.186 102.138 1.00 38.78  ?  212  ASN A OD1 1 
ATOM   1287  N ND2 . ASN A  1  212 ? 68.860  -32.042 104.305 1.00 38.62  ?  212  ASN A ND2 1 
ATOM   1288  N N   . LEU A  1  213 ? 64.670  -33.121 100.304 1.00 35.59  ?  213  LEU A N   1 
ATOM   1289  C CA  . LEU A  1  213 ? 63.353  -33.728 100.106 1.00 34.26  ?  213  LEU A CA  1 
ATOM   1290  C C   . LEU A  1  213 ? 63.345  -34.574 98.832  1.00 34.86  ?  213  LEU A C   1 
ATOM   1291  O O   . LEU A  1  213 ? 62.597  -34.327 97.888  1.00 34.18  ?  213  LEU A O   1 
ATOM   1292  C CB  . LEU A  1  213 ? 62.282  -32.645 100.055 1.00 32.72  ?  213  LEU A CB  1 
ATOM   1293  C CG  . LEU A  1  213 ? 62.294  -31.630 101.197 1.00 32.26  ?  213  LEU A CG  1 
ATOM   1294  C CD1 . LEU A  1  213 ? 61.347  -30.477 100.903 1.00 30.99  ?  213  LEU A CD1 1 
ATOM   1295  C CD2 . LEU A  1  213 ? 61.932  -32.305 102.504 1.00 31.83  ?  213  LEU A CD2 1 
ATOM   1296  N N   . THR A  1  214 ? 64.186  -35.614 98.842  1.00 37.20  ?  214  THR A N   1 
ATOM   1297  C CA  . THR A  1  214 ? 64.458  -36.379 97.627  1.00 38.24  ?  214  THR A CA  1 
ATOM   1298  C C   . THR A  1  214 ? 63.198  -37.003 97.036  1.00 37.25  ?  214  THR A C   1 
ATOM   1299  O O   . THR A  1  214 ? 63.101  -37.157 95.812  1.00 37.69  ?  214  THR A O   1 
ATOM   1300  C CB  . THR A  1  214 ? 65.496  -37.465 97.914  1.00 39.87  ?  214  THR A CB  1 
ATOM   1301  O OG1 . THR A  1  214 ? 65.036  -38.302 98.982  1.00 39.31  ?  214  THR A OG1 1 
ATOM   1302  C CG2 . THR A  1  214 ? 66.827  -36.837 98.309  1.00 41.11  ?  214  THR A CG2 1 
ATOM   1303  N N   . LYS A  1  215 ? 62.226  -37.360 97.872  1.00 35.89  ?  215  LYS A N   1 
ATOM   1304  C CA  . LYS A  1  215 ? 61.012  -38.013 97.396  1.00 35.05  ?  215  LYS A CA  1 
ATOM   1305  C C   . LYS A  1  215 ? 59.983  -37.038 96.834  1.00 33.66  ?  215  LYS A C   1 
ATOM   1306  O O   . LYS A  1  215 ? 58.919  -37.481 96.387  1.00 32.94  ?  215  LYS A O   1 
ATOM   1307  C CB  . LYS A  1  215 ? 60.382  -38.833 98.526  1.00 34.41  ?  215  LYS A CB  1 
ATOM   1308  C CG  . LYS A  1  215 ? 61.256  -39.968 99.046  1.00 35.76  ?  215  LYS A CG  1 
ATOM   1309  C CD  . LYS A  1  215 ? 61.454  -41.052 97.995  1.00 36.98  ?  215  LYS A CD  1 
ATOM   1310  C CE  . LYS A  1  215 ? 62.827  -41.695 98.114  1.00 38.81  ?  215  LYS A CE  1 
ATOM   1311  N NZ  . LYS A  1  215 ? 62.749  -43.184 98.099  1.00 39.67  ?  215  LYS A NZ  1 
ATOM   1312  N N   . LEU A  1  216 ? 60.265  -35.737 96.852  1.00 33.32  ?  216  LEU A N   1 
ATOM   1313  C CA  . LEU A  1  216 ? 59.310  -34.738 96.384  1.00 32.02  ?  216  LEU A CA  1 
ATOM   1314  C C   . LEU A  1  216 ? 59.056  -34.887 94.887  1.00 32.34  ?  216  LEU A C   1 
ATOM   1315  O O   . LEU A  1  216 ? 59.996  -35.014 94.098  1.00 33.71  ?  216  LEU A O   1 
ATOM   1316  C CB  . LEU A  1  216 ? 59.834  -33.336 96.691  1.00 31.92  ?  216  LEU A CB  1 
ATOM   1317  C CG  . LEU A  1  216 ? 58.858  -32.164 96.617  1.00 30.48  ?  216  LEU A CG  1 
ATOM   1318  C CD1 . LEU A  1  216 ? 57.823  -32.272 97.724  1.00 29.18  ?  216  LEU A CD1 1 
ATOM   1319  C CD2 . LEU A  1  216 ? 59.613  -30.847 96.708  1.00 30.84  ?  216  LEU A CD2 1 
ATOM   1320  N N   . VAL A  1  217 ? 57.780  -34.868 94.497  1.00 32.25  ?  217  VAL A N   1 
ATOM   1321  C CA  . VAL A  1  217 ? 57.409  -34.938 93.086  1.00 32.45  ?  217  VAL A CA  1 
ATOM   1322  C C   . VAL A  1  217 ? 56.629  -33.694 92.673  1.00 31.22  ?  217  VAL A C   1 
ATOM   1323  O O   . VAL A  1  217 ? 56.632  -33.312 91.497  1.00 31.52  ?  217  VAL A O   1 
ATOM   1324  C CB  . VAL A  1  217 ? 56.601  -36.215 92.786  1.00 32.44  ?  217  VAL A CB  1 
ATOM   1325  C CG1 . VAL A  1  217 ? 57.348  -37.446 93.273  1.00 33.66  ?  217  VAL A CG1 1 
ATOM   1326  C CG2 . VAL A  1  217 ? 55.218  -36.143 93.419  1.00 31.18  ?  217  VAL A CG2 1 
ATOM   1327  N N   . ASN A  1  218 ? 55.964  -33.049 93.632  1.00 29.85  ?  218  ASN A N   1 
ATOM   1328  C CA  . ASN A  1  218 ? 55.086  -31.916 93.357  1.00 28.61  ?  218  ASN A CA  1 
ATOM   1329  C C   . ASN A  1  218 ? 55.393  -30.797 94.340  1.00 28.17  ?  218  ASN A C   1 
ATOM   1330  O O   . ASN A  1  218 ? 55.217  -30.967 95.551  1.00 27.74  ?  218  ASN A O   1 
ATOM   1331  C CB  . ASN A  1  218 ? 53.611  -32.320 93.458  1.00 27.51  ?  218  ASN A CB  1 
ATOM   1332  C CG  . ASN A  1  218 ? 53.149  -33.154 92.278  1.00 28.11  ?  218  ASN A CG  1 
ATOM   1333  O OD1 . ASN A  1  218 ? 53.785  -33.170 91.225  1.00 28.81  ?  218  ASN A OD1 1 
ATOM   1334  N ND2 . ASN A  1  218 ? 52.033  -33.852 92.451  1.00 27.93  ?  218  ASN A ND2 1 
ATOM   1335  N N   . LEU A  1  219 ? 55.851  -29.659 93.822  1.00 27.86  ?  219  LEU A N   1 
ATOM   1336  C CA  . LEU A  1  219 ? 56.107  -28.472 94.633  1.00 27.54  ?  219  LEU A CA  1 
ATOM   1337  C C   . LEU A  1  219 ? 55.224  -27.338 94.127  1.00 26.49  ?  219  LEU A C   1 
ATOM   1338  O O   . LEU A  1  219 ? 55.417  -26.846 93.009  1.00 26.84  ?  219  LEU A O   1 
ATOM   1339  C CB  . LEU A  1  219 ? 57.584  -28.084 94.587  1.00 28.96  ?  219  LEU A CB  1 
ATOM   1340  C CG  . LEU A  1  219 ? 58.017  -27.052 95.627  1.00 28.94  ?  219  LEU A CG  1 
ATOM   1341  C CD1 . LEU A  1  219 ? 57.476  -27.426 96.999  1.00 28.18  ?  219  LEU A CD1 1 
ATOM   1342  C CD2 . LEU A  1  219 ? 59.532  -26.924 95.661  1.00 30.56  ?  219  LEU A CD2 1 
ATOM   1343  N N   . TYR A  1  220 ? 54.262  -26.920 94.949  1.00 28.37  ?  220  TYR A N   1 
ATOM   1344  C CA  . TYR A  1  220 ? 53.322  -25.859 94.599  1.00 27.33  ?  220  TYR A CA  1 
ATOM   1345  C C   . TYR A  1  220 ? 53.446  -24.742 95.628  1.00 27.07  ?  220  TYR A C   1 
ATOM   1346  O O   . TYR A  1  220 ? 53.034  -24.908 96.782  1.00 26.58  ?  220  TYR A O   1 
ATOM   1347  C CB  . TYR A  1  220 ? 51.893  -26.397 94.544  1.00 26.17  ?  220  TYR A CB  1 
ATOM   1348  C CG  . TYR A  1  220 ? 51.722  -27.586 93.625  1.00 26.53  ?  220  TYR A CG  1 
ATOM   1349  C CD1 . TYR A  1  220 ? 52.298  -27.600 92.361  1.00 27.35  ?  220  TYR A CD1 1 
ATOM   1350  C CD2 . TYR A  1  220 ? 50.988  -28.695 94.022  1.00 26.54  ?  220  TYR A CD2 1 
ATOM   1351  C CE1 . TYR A  1  220 ? 52.146  -28.685 91.518  1.00 27.82  ?  220  TYR A CE1 1 
ATOM   1352  C CE2 . TYR A  1  220 ? 50.830  -29.784 93.187  1.00 27.19  ?  220  TYR A CE2 1 
ATOM   1353  C CZ  . TYR A  1  220 ? 51.411  -29.774 91.937  1.00 27.72  ?  220  TYR A CZ  1 
ATOM   1354  O OH  . TYR A  1  220 ? 51.255  -30.857 91.103  1.00 28.50  ?  220  TYR A OH  1 
ATOM   1355  N N   . LEU A  1  221 ? 54.022  -23.608 95.217  1.00 28.59  ?  221  LEU A N   1 
ATOM   1356  C CA  . LEU A  1  221 ? 54.182  -22.465 96.109  1.00 28.53  ?  221  LEU A CA  1 
ATOM   1357  C C   . LEU A  1  221 ? 53.868  -21.146 95.414  1.00 28.22  ?  221  LEU A C   1 
ATOM   1358  O O   . LEU A  1  221 ? 54.456  -20.115 95.759  1.00 28.93  ?  221  LEU A O   1 
ATOM   1359  C CB  . LEU A  1  221 ? 55.607  -22.394 96.666  1.00 29.88  ?  221  LEU A CB  1 
ATOM   1360  C CG  . LEU A  1  221 ? 56.209  -23.608 97.368  1.00 30.49  ?  221  LEU A CG  1 
ATOM   1361  C CD1 . LEU A  1  221 ? 57.727  -23.523 97.341  1.00 32.06  ?  221  LEU A CD1 1 
ATOM   1362  C CD2 . LEU A  1  221 ? 55.701  -23.702 98.793  1.00 29.89  ?  221  LEU A CD2 1 
ATOM   1363  N N   . PHE A  1  222 ? 52.954  -21.137 94.441  1.00 31.72  ?  222  PHE A N   1 
ATOM   1364  C CA  . PHE A  1  222 ? 53.010  -20.042 93.478  1.00 32.54  ?  222  PHE A CA  1 
ATOM   1365  C C   . PHE A  1  222 ? 52.498  -18.717 94.042  1.00 32.02  ?  222  PHE A C   1 
ATOM   1366  O O   . PHE A  1  222 ? 53.256  -17.746 94.121  1.00 34.71  ?  222  PHE A O   1 
ATOM   1367  C CB  . PHE A  1  222 ? 52.296  -20.403 92.164  1.00 31.83  ?  222  PHE A CB  1 
ATOM   1368  C CG  . PHE A  1  222 ? 51.062  -21.247 92.305  1.00 30.18  ?  222  PHE A CG  1 
ATOM   1369  C CD1 . PHE A  1  222 ? 51.157  -22.624 92.436  1.00 30.40  ?  222  PHE A CD1 1 
ATOM   1370  C CD2 . PHE A  1  222 ? 49.804  -20.676 92.208  1.00 29.00  ?  222  PHE A CD2 1 
ATOM   1371  C CE1 . PHE A  1  222 ? 50.027  -23.406 92.526  1.00 29.53  ?  222  PHE A CE1 1 
ATOM   1372  C CE2 . PHE A  1  222 ? 48.668  -21.455 92.296  1.00 28.28  ?  222  PHE A CE2 1 
ATOM   1373  C CZ  . PHE A  1  222 ? 48.782  -22.824 92.448  1.00 28.67  ?  222  PHE A CZ  1 
ATOM   1374  N N   . ILE A  1  223 ? 51.243  -18.648 94.481  1.00 31.72  ?  223  ILE A N   1 
ATOM   1375  C CA  . ILE A  1  223 ? 50.698  -17.343 94.865  1.00 31.05  ?  223  ILE A CA  1 
ATOM   1376  C C   . ILE A  1  223 ? 51.255  -17.012 96.247  1.00 31.70  ?  223  ILE A C   1 
ATOM   1377  O O   . ILE A  1  223 ? 50.740  -17.465 97.271  1.00 31.37  ?  223  ILE A O   1 
ATOM   1378  C CB  . ILE A  1  223 ? 49.167  -17.320 94.844  1.00 29.53  ?  223  ILE A CB  1 
ATOM   1379  C CG1 . ILE A  1  223 ? 48.646  -17.515 93.420  1.00 29.12  ?  223  ILE A CG1 1 
ATOM   1380  C CG2 . ILE A  1  223 ? 48.647  -16.001 95.399  1.00 29.19  ?  223  ILE A CG2 1 
ATOM   1381  C CD1 . ILE A  1  223 ? 47.353  -18.302 93.349  1.00 28.38  ?  223  ILE A CD1 1 
ATOM   1382  N N   . ASN A  1  224 ? 52.311  -16.206 96.271  1.00 29.81  ?  224  ASN A N   1 
ATOM   1383  C CA  . ASN A  1  224 ? 53.059  -15.879 97.481  1.00 30.86  ?  224  ASN A CA  1 
ATOM   1384  C C   . ASN A  1  224 ? 53.973  -14.705 97.153  1.00 34.12  ?  224  ASN A C   1 
ATOM   1385  O O   . ASN A  1  224 ? 53.933  -14.150 96.050  1.00 35.33  ?  224  ASN A O   1 
ATOM   1386  C CB  . ASN A  1  224 ? 53.853  -17.084 97.993  1.00 31.82  ?  224  ASN A CB  1 
ATOM   1387  C CG  . ASN A  1  224 ? 53.091  -17.888 99.022  1.00 30.18  ?  224  ASN A CG  1 
ATOM   1388  O OD1 . ASN A  1  224 ? 52.572  -17.338 99.989  1.00 29.75  ?  224  ASN A OD1 1 
ATOM   1389  N ND2 . ASN A  1  224 ? 53.004  -19.196 98.810  1.00 30.07  ?  224  ASN A ND2 1 
ATOM   1390  N N   . SER A  1  225 ? 54.809  -14.339 98.120  1.00 30.63  ?  225  SER A N   1 
ATOM   1391  C CA  . SER A  1  225 ? 55.784  -13.265 97.964  1.00 32.56  ?  225  SER A CA  1 
ATOM   1392  C C   . SER A  1  225 ? 57.179  -13.752 98.331  1.00 33.82  ?  225  SER A C   1 
ATOM   1393  O O   . SER A  1  225 ? 57.961  -13.036 98.965  1.00 34.70  ?  225  SER A O   1 
ATOM   1394  C CB  . SER A  1  225 ? 55.395  -12.047 98.797  1.00 31.94  ?  225  SER A CB  1 
ATOM   1395  O OG  . SER A  1  225 ? 54.411  -11.272 98.133  1.00 31.08  ?  225  SER A OG  1 
ATOM   1396  N N   . LEU A  1  226 ? 57.505  -14.985 97.945  1.00 32.99  ?  226  LEU A N   1 
ATOM   1397  C CA  . LEU A  1  226 ? 58.841  -15.519 98.175  1.00 34.23  ?  226  LEU A CA  1 
ATOM   1398  C C   . LEU A  1  226 ? 59.878  -14.667 97.450  1.00 35.72  ?  226  LEU A C   1 
ATOM   1399  O O   . LEU A  1  226 ? 59.622  -14.116 96.377  1.00 35.80  ?  226  LEU A O   1 
ATOM   1400  C CB  . LEU A  1  226 ? 58.921  -16.970 97.697  1.00 33.92  ?  226  LEU A CB  1 
ATOM   1401  C CG  . LEU A  1  226 ? 57.970  -17.965 98.365  1.00 32.43  ?  226  LEU A CG  1 
ATOM   1402  C CD1 . LEU A  1  226 ? 58.241  -19.376 97.872  1.00 32.57  ?  226  LEU A CD1 1 
ATOM   1403  C CD2 . LEU A  1  226 ? 58.097  -17.891 99.877  1.00 32.62  ?  226  LEU A CD2 1 
ATOM   1404  N N   . SER A  1  227 ? 61.062  -14.559 98.048  1.00 37.32  ?  227  SER A N   1 
ATOM   1405  C CA  . SER A  1  227 ? 62.078  -13.621 97.590  1.00 38.47  ?  227  SER A CA  1 
ATOM   1406  C C   . SER A  1  227 ? 63.396  -14.351 97.353  1.00 39.47  ?  227  SER A C   1 
ATOM   1407  O O   . SER A  1  227 ? 63.529  -15.551 97.609  1.00 39.38  ?  227  SER A O   1 
ATOM   1408  C CB  . SER A  1  227 ? 62.263  -12.478 98.596  1.00 38.35  ?  227  SER A CB  1 
ATOM   1409  O OG  . SER A  1  227 ? 62.951  -11.386 98.011  1.00 39.98  ?  227  SER A OG  1 
ATOM   1410  N N   . GLY A  1  228 ? 64.370  -13.607 96.839  1.00 41.86  ?  228  GLY A N   1 
ATOM   1411  C CA  . GLY A  1  228 ? 65.706  -14.128 96.621  1.00 42.84  ?  228  GLY A CA  1 
ATOM   1412  C C   . GLY A  1  228 ? 65.785  -15.087 95.445  1.00 42.95  ?  228  GLY A C   1 
ATOM   1413  O O   . GLY A  1  228 ? 64.814  -15.356 94.739  1.00 42.58  ?  228  GLY A O   1 
ATOM   1414  N N   . SER A  1  229 ? 66.988  -15.618 95.250  1.00 43.39  ?  229  SER A N   1 
ATOM   1415  C CA  . SER A  1  229 ? 67.249  -16.523 94.144  1.00 43.75  ?  229  SER A CA  1 
ATOM   1416  C C   . SER A  1  229 ? 66.704  -17.916 94.441  1.00 43.16  ?  229  SER A C   1 
ATOM   1417  O O   . SER A  1  229 ? 66.415  -18.273 95.587  1.00 42.81  ?  229  SER A O   1 
ATOM   1418  C CB  . SER A  1  229 ? 68.748  -16.593 93.850  1.00 46.02  ?  229  SER A CB  1 
ATOM   1419  O OG  . SER A  1  229 ? 69.275  -15.303 93.592  1.00 47.14  ?  229  SER A OG  1 
ATOM   1420  N N   . ILE A  1  230 ? 66.568  -18.704 93.385  1.00 42.11  ?  230  ILE A N   1 
ATOM   1421  C CA  . ILE A  1  230 ? 66.092  -20.081 93.520  1.00 41.47  ?  230  ILE A CA  1 
ATOM   1422  C C   . ILE A  1  230 ? 67.249  -20.954 93.999  1.00 42.76  ?  230  ILE A C   1 
ATOM   1423  O O   . ILE A  1  230 ? 68.338  -20.905 93.405  1.00 44.49  ?  230  ILE A O   1 
ATOM   1424  C CB  . ILE A  1  230 ? 65.533  -20.586 92.195  1.00 41.05  ?  230  ILE A CB  1 
ATOM   1425  C CG1 . ILE A  1  230 ? 64.621  -19.527 91.572  1.00 40.99  ?  230  ILE A CG1 1 
ATOM   1426  C CG2 . ILE A  1  230 ? 64.783  -21.897 92.393  1.00 39.76  ?  230  ILE A CG2 1 
ATOM   1427  C CD1 . ILE A  1  230 ? 63.818  -20.025 90.396  1.00 40.29  ?  230  ILE A CD1 1 
ATOM   1428  N N   . PRO A  1  231 ? 67.065  -21.739 95.060  1.00 40.12  ?  231  PRO A N   1 
ATOM   1429  C CA  . PRO A  1  231 ? 68.150  -22.608 95.535  1.00 41.54  ?  231  PRO A CA  1 
ATOM   1430  C C   . PRO A  1  231 ? 68.587  -23.586 94.455  1.00 42.46  ?  231  PRO A C   1 
ATOM   1431  O O   . PRO A  1  231 ? 67.765  -24.276 93.847  1.00 41.50  ?  231  PRO A O   1 
ATOM   1432  C CB  . PRO A  1  231 ? 67.530  -23.330 96.737  1.00 40.39  ?  231  PRO A CB  1 
ATOM   1433  C CG  . PRO A  1  231 ? 66.355  -22.500 97.133  1.00 38.70  ?  231  PRO A CG  1 
ATOM   1434  C CD  . PRO A  1  231 ? 65.850  -21.862 95.880  1.00 38.26  ?  231  PRO A CD  1 
ATOM   1435  N N   . SER A  1  232 ? 69.901  -23.636 94.215  1.00 44.77  ?  232  SER A N   1 
ATOM   1436  C CA  . SER A  1  232 ? 70.437  -24.549 93.209  1.00 45.96  ?  232  SER A CA  1 
ATOM   1437  C C   . SER A  1  232 ? 70.138  -26.002 93.553  1.00 45.52  ?  232  SER A C   1 
ATOM   1438  O O   . SER A  1  232 ? 70.017  -26.839 92.651  1.00 45.81  ?  232  SER A O   1 
ATOM   1439  C CB  . SER A  1  232 ? 71.944  -24.339 93.058  1.00 48.33  ?  232  SER A CB  1 
ATOM   1440  O OG  . SER A  1  232 ? 72.293  -22.974 93.221  1.00 48.78  ?  232  SER A OG  1 
ATOM   1441  N N   . GLU A  1  233 ? 70.017  -26.320 94.845  1.00 45.27  ?  233  GLU A N   1 
ATOM   1442  C CA  . GLU A  1  233 ? 69.717  -27.686 95.262  1.00 44.87  ?  233  GLU A CA  1 
ATOM   1443  C C   . GLU A  1  233 ? 68.378  -28.176 94.727  1.00 43.21  ?  233  GLU A C   1 
ATOM   1444  O O   . GLU A  1  233 ? 68.176  -29.391 94.620  1.00 43.22  ?  233  GLU A O   1 
ATOM   1445  C CB  . GLU A  1  233 ? 69.728  -27.790 96.790  1.00 44.42  ?  233  GLU A CB  1 
ATOM   1446  C CG  . GLU A  1  233 ? 71.094  -27.614 97.439  1.00 46.20  ?  233  GLU A CG  1 
ATOM   1447  C CD  . GLU A  1  233 ? 71.567  -26.174 97.442  1.00 46.80  ?  233  GLU A CD  1 
ATOM   1448  O OE1 . GLU A  1  233 ? 70.724  -25.270 97.618  1.00 45.46  ?  233  GLU A OE1 1 
ATOM   1449  O OE2 . GLU A  1  233 ? 72.783  -25.947 97.271  1.00 48.70  -1 233  GLU A OE2 1 
ATOM   1450  N N   . ILE A  1  234 ? 67.461  -27.262 94.394  1.00 41.29  ?  234  ILE A N   1 
ATOM   1451  C CA  . ILE A  1  234 ? 66.161  -27.660 93.860  1.00 39.76  ?  234  ILE A CA  1 
ATOM   1452  C C   . ILE A  1  234 ? 66.327  -28.417 92.548  1.00 40.64  ?  234  ILE A C   1 
ATOM   1453  O O   . ILE A  1  234 ? 65.583  -29.365 92.269  1.00 40.00  ?  234  ILE A O   1 
ATOM   1454  C CB  . ILE A  1  234 ? 65.251  -26.423 93.707  1.00 38.38  ?  234  ILE A CB  1 
ATOM   1455  C CG1 . ILE A  1  234 ? 64.623  -26.065 95.057  1.00 37.09  ?  234  ILE A CG1 1 
ATOM   1456  C CG2 . ILE A  1  234 ? 64.164  -26.668 92.672  1.00 37.34  ?  234  ILE A CG2 1 
ATOM   1457  C CD1 . ILE A  1  234 ? 63.478  -25.077 94.966  1.00 35.53  ?  234  ILE A CD1 1 
ATOM   1458  N N   . GLY A  1  235 ? 67.317  -28.038 91.739  1.00 44.20  ?  235  GLY A N   1 
ATOM   1459  C CA  . GLY A  1  235 ? 67.599  -28.746 90.503  1.00 45.33  ?  235  GLY A CA  1 
ATOM   1460  C C   . GLY A  1  235 ? 68.028  -30.188 90.692  1.00 46.27  ?  235  GLY A C   1 
ATOM   1461  O O   . GLY A  1  235 ? 68.072  -30.935 89.707  1.00 47.09  ?  235  GLY A O   1 
ATOM   1462  N N   . ASN A  1  236 ? 68.354  -30.595 91.920  1.00 43.89  ?  236  ASN A N   1 
ATOM   1463  C CA  . ASN A  1  236 ? 68.859  -31.934 92.195  1.00 44.90  ?  236  ASN A CA  1 
ATOM   1464  C C   . ASN A  1  236 ? 67.818  -32.839 92.848  1.00 43.45  ?  236  ASN A C   1 
ATOM   1465  O O   . ASN A  1  236 ? 68.177  -33.870 93.425  1.00 44.06  ?  236  ASN A O   1 
ATOM   1466  C CB  . ASN A  1  236 ? 70.113  -31.856 93.066  1.00 46.27  ?  236  ASN A CB  1 
ATOM   1467  C CG  . ASN A  1  236 ? 71.291  -31.245 92.334  1.00 48.19  ?  236  ASN A CG  1 
ATOM   1468  O OD1 . ASN A  1  236 ? 71.736  -30.144 92.658  1.00 48.40  ?  236  ASN A OD1 1 
ATOM   1469  N ND2 . ASN A  1  236 ? 71.803  -31.960 91.338  1.00 49.71  ?  236  ASN A ND2 1 
ATOM   1470  N N   . LEU A  1  237 ? 66.541  -32.478 92.782  1.00 43.39  ?  237  LEU A N   1 
ATOM   1471  C CA  . LEU A  1  237 ? 65.494  -33.394 93.219  1.00 42.16  ?  237  LEU A CA  1 
ATOM   1472  C C   . LEU A  1  237 ? 65.270  -34.452 92.146  1.00 42.82  ?  237  LEU A C   1 
ATOM   1473  O O   . LEU A  1  237 ? 64.867  -34.110 91.029  1.00 42.71  ?  237  LEU A O   1 
ATOM   1474  C CB  . LEU A  1  237 ? 64.197  -32.650 93.515  1.00 40.09  ?  237  LEU A CB  1 
ATOM   1475  C CG  . LEU A  1  237 ? 64.103  -32.003 94.902  1.00 39.20  ?  237  LEU A CG  1 
ATOM   1476  C CD1 . LEU A  1  237 ? 64.562  -32.986 95.958  1.00 39.73  ?  237  LEU A CD1 1 
ATOM   1477  C CD2 . LEU A  1  237 ? 64.893  -30.718 95.006  1.00 39.76  ?  237  LEU A CD2 1 
ATOM   1478  N N   . PRO A  1  238 ? 65.515  -35.733 92.436  1.00 44.10  ?  238  PRO A N   1 
ATOM   1479  C CA  . PRO A  1  238 ? 65.467  -36.736 91.360  1.00 45.12  ?  238  PRO A CA  1 
ATOM   1480  C C   . PRO A  1  238 ? 64.060  -37.072 90.901  1.00 43.78  ?  238  PRO A C   1 
ATOM   1481  O O   . PRO A  1  238 ? 63.840  -37.281 89.701  1.00 44.33  ?  238  PRO A O   1 
ATOM   1482  C CB  . PRO A  1  238 ? 66.174  -37.950 91.980  1.00 46.35  ?  238  PRO A CB  1 
ATOM   1483  C CG  . PRO A  1  238 ? 66.240  -37.689 93.472  1.00 45.49  ?  238  PRO A CG  1 
ATOM   1484  C CD  . PRO A  1  238 ? 65.643  -36.346 93.767  1.00 43.90  ?  238  PRO A CD  1 
ATOM   1485  N N   . ASN A  1  239 ? 63.099  -37.132 91.819  1.00 45.65  ?  239  ASN A N   1 
ATOM   1486  C CA  . ASN A  1  239 ? 61.744  -37.563 91.506  1.00 44.46  ?  239  ASN A CA  1 
ATOM   1487  C C   . ASN A  1  239 ? 60.794  -36.409 91.215  1.00 42.87  ?  239  ASN A C   1 
ATOM   1488  O O   . ASN A  1  239 ? 59.607  -36.652 90.975  1.00 41.81  ?  239  ASN A O   1 
ATOM   1489  C CB  . ASN A  1  239 ? 61.187  -38.412 92.653  1.00 43.73  ?  239  ASN A CB  1 
ATOM   1490  C CG  . ASN A  1  239 ? 61.970  -39.694 92.857  1.00 45.30  ?  239  ASN A CG  1 
ATOM   1491  O OD1 . ASN A  1  239 ? 62.089  -40.514 91.947  1.00 46.46  ?  239  ASN A OD1 1 
ATOM   1492  N ND2 . ASN A  1  239 ? 62.512  -39.871 94.056  1.00 45.41  ?  239  ASN A ND2 1 
ATOM   1493  N N   . LEU A  1  240 ? 61.277  -35.168 91.246  1.00 39.75  ?  240  LEU A N   1 
ATOM   1494  C CA  . LEU A  1  240 ? 60.408  -34.020 91.012  1.00 38.30  ?  240  LEU A CA  1 
ATOM   1495  C C   . LEU A  1  240 ? 59.761  -34.103 89.635  1.00 38.29  ?  240  LEU A C   1 
ATOM   1496  O O   . LEU A  1  240 ? 60.428  -34.388 88.636  1.00 39.74  ?  240  LEU A O   1 
ATOM   1497  C CB  . LEU A  1  240 ? 61.195  -32.717 91.148  1.00 38.55  ?  240  LEU A CB  1 
ATOM   1498  C CG  . LEU A  1  240 ? 60.322  -31.465 91.262  1.00 36.96  ?  240  LEU A CG  1 
ATOM   1499  C CD1 . LEU A  1  240 ? 59.499  -31.513 92.541  1.00 35.53  ?  240  LEU A CD1 1 
ATOM   1500  C CD2 . LEU A  1  240 ? 61.162  -30.201 91.209  1.00 37.50  ?  240  LEU A CD2 1 
ATOM   1501  N N   . ARG A  1  241 ? 58.455  -33.864 89.590  1.00 41.66  ?  241  ARG A N   1 
ATOM   1502  C CA  . ARG A  1  241 ? 57.695  -33.856 88.347  1.00 41.48  ?  241  ARG A CA  1 
ATOM   1503  C C   . ARG A  1  241 ? 57.078  -32.505 88.026  1.00 40.30  ?  241  ARG A C   1 
ATOM   1504  O O   . ARG A  1  241 ? 57.023  -32.122 86.855  1.00 40.79  ?  241  ARG A O   1 
ATOM   1505  C CB  . ARG A  1  241 ? 56.585  -34.917 88.394  1.00 40.88  ?  241  ARG A CB  1 
ATOM   1506  C CG  . ARG A  1  241 ? 56.710  -35.995 87.329  1.00 43.42  ?  241  ARG A CG  1 
ATOM   1507  C CD  . ARG A  1  241 ? 55.924  -37.240 87.706  1.00 42.78  ?  241  ARG A CD  1 
ATOM   1508  N NE  . ARG A  1  241 ? 56.797  -38.316 88.159  1.00 44.72  ?  241  ARG A NE  1 
ATOM   1509  C CZ  . ARG A  1  241 ? 56.456  -39.237 89.050  1.00 45.17  ?  241  ARG A CZ  1 
ATOM   1510  N NH1 . ARG A  1  241 ? 55.261  -39.242 89.618  1.00 43.73  ?  241  ARG A NH1 1 
ATOM   1511  N NH2 . ARG A  1  241 ? 57.336  -40.178 89.379  1.00 46.27  ?  241  ARG A NH2 1 
ATOM   1512  N N   . GLU A  1  242 ? 56.606  -31.771 89.033  1.00 34.61  ?  242  GLU A N   1 
ATOM   1513  C CA  . GLU A  1  242 ? 55.915  -30.504 88.822  1.00 33.42  ?  242  GLU A CA  1 
ATOM   1514  C C   . GLU A  1  242 ? 56.477  -29.457 89.771  1.00 33.17  ?  242  GLU A C   1 
ATOM   1515  O O   . GLU A  1  242 ? 56.458  -29.647 90.992  1.00 32.74  ?  242  GLU A O   1 
ATOM   1516  C CB  . GLU A  1  242 ? 54.406  -30.658 89.030  1.00 31.88  ?  242  GLU A CB  1 
ATOM   1517  C CG  . GLU A  1  242 ? 53.770  -31.751 88.191  1.00 32.16  ?  242  GLU A CG  1 
ATOM   1518  C CD  . GLU A  1  242 ? 52.298  -31.504 87.945  1.00 30.77  ?  242  GLU A CD  1 
ATOM   1519  O OE1 . GLU A  1  242 ? 51.736  -30.588 88.580  1.00 29.54  ?  242  GLU A OE1 1 
ATOM   1520  O OE2 . GLU A  1  242 ? 51.705  -32.218 87.110  1.00 31.16  -1 242  GLU A OE2 1 
ATOM   1521  N N   . LEU A  1  243 ? 56.962  -28.351 89.209  1.00 30.41  ?  243  LEU A N   1 
ATOM   1522  C CA  . LEU A  1  243 ? 57.527  -27.245 89.977  1.00 30.36  ?  243  LEU A CA  1 
ATOM   1523  C C   . LEU A  1  243 ? 56.791  -25.971 89.585  1.00 29.35  ?  243  LEU A C   1 
ATOM   1524  O O   . LEU A  1  243 ? 56.904  -25.512 88.444  1.00 29.78  ?  243  LEU A O   1 
ATOM   1525  C CB  . LEU A  1  243 ? 59.030  -27.114 89.725  1.00 32.11  ?  243  LEU A CB  1 
ATOM   1526  C CG  . LEU A  1  243 ? 59.782  -26.057 90.535  1.00 32.40  ?  243  LEU A CG  1 
ATOM   1527  C CD1 . LEU A  1  243 ? 59.582  -26.278 92.025  1.00 31.71  ?  243  LEU A CD1 1 
ATOM   1528  C CD2 . LEU A  1  243 ? 61.260  -26.072 90.182  1.00 34.31  ?  243  LEU A CD2 1 
ATOM   1529  N N   . CYS A  1  244 ? 56.039  -25.402 90.525  1.00 30.48  ?  244  CYS A N   1 
ATOM   1530  C CA  . CYS A  1  244 ? 55.213  -24.220 90.282  1.00 29.43  ?  244  CYS A CA  1 
ATOM   1531  C C   . CYS A  1  244 ? 55.632  -23.123 91.258  1.00 29.39  ?  244  CYS A C   1 
ATOM   1532  O O   . CYS A  1  244 ? 55.089  -23.012 92.359  1.00 28.55  ?  244  CYS A O   1 
ATOM   1533  C CB  . CYS A  1  244 ? 53.727  -24.557 90.415  1.00 27.97  ?  244  CYS A CB  1 
ATOM   1534  S SG  . CYS A  1  244 ? 53.138  -25.807 89.248  1.00 28.09  ?  244  CYS A SG  1 
ATOM   1535  N N   . LEU A  1  245 ? 56.611  -22.316 90.845  1.00 29.80  ?  245  LEU A N   1 
ATOM   1536  C CA  . LEU A  1  245 ? 57.092  -21.182 91.626  1.00 30.68  ?  245  LEU A CA  1 
ATOM   1537  C C   . LEU A  1  245 ? 56.611  -19.848 91.063  1.00 31.74  ?  245  LEU A C   1 
ATOM   1538  O O   . LEU A  1  245 ? 57.169  -18.799 91.398  1.00 33.56  ?  245  LEU A O   1 
ATOM   1539  C CB  . LEU A  1  245 ? 58.618  -21.201 91.704  1.00 33.17  ?  245  LEU A CB  1 
ATOM   1540  C CG  . LEU A  1  245 ? 59.238  -22.477 92.272  1.00 32.40  ?  245  LEU A CG  1 
ATOM   1541  C CD1 . LEU A  1  245 ? 60.748  -22.454 92.101  1.00 34.53  ?  245  LEU A CD1 1 
ATOM   1542  C CD2 . LEU A  1  245 ? 58.857  -22.661 93.734  1.00 31.64  ?  245  LEU A CD2 1 
ATOM   1543  N N   . ASP A  1  246 ? 55.585  -19.871 90.217  1.00 34.18  ?  246  ASP A N   1 
ATOM   1544  C CA  . ASP A  1  246 ? 55.142  -18.677 89.515  1.00 35.28  ?  246  ASP A CA  1 
ATOM   1545  C C   . ASP A  1  246 ? 54.522  -17.675 90.487  1.00 34.11  ?  246  ASP A C   1 
ATOM   1546  O O   . ASP A  1  246 ? 54.224  -17.988 91.637  1.00 32.30  ?  246  ASP A O   1 
ATOM   1547  C CB  . ASP A  1  246 ? 54.130  -19.039 88.430  1.00 33.88  ?  246  ASP A CB  1 
ATOM   1548  C CG  . ASP A  1  246 ? 53.036  -19.957 88.938  1.00 29.71  ?  246  ASP A CG  1 
ATOM   1549  O OD1 . ASP A  1  246 ? 53.336  -21.129 89.247  1.00 28.86  ?  246  ASP A OD1 1 
ATOM   1550  O OD2 . ASP A  1  246 ? 51.879  -19.499 89.051  1.00 27.43  -1 246  ASP A OD2 1 
ATOM   1551  N N   . ARG A  1  247 ? 54.359  -16.439 90.012  1.00 36.96  ?  247  ARG A N   1 
ATOM   1552  C CA  . ARG A  1  247 ? 53.641  -15.392 90.741  1.00 35.51  ?  247  ARG A CA  1 
ATOM   1553  C C   . ARG A  1  247 ? 54.256  -15.152 92.123  1.00 35.97  ?  247  ARG A C   1 
ATOM   1554  O O   . ARG A  1  247 ? 53.599  -15.266 93.159  1.00 33.48  ?  247  ARG A O   1 
ATOM   1555  C CB  . ARG A  1  247 ? 52.152  -15.738 90.854  1.00 31.48  ?  247  ARG A CB  1 
ATOM   1556  C CG  . ARG A  1  247 ? 51.338  -15.376 89.625  1.00 30.38  ?  247  ARG A CG  1 
ATOM   1557  C CD  . ARG A  1  247 ? 49.903  -15.858 89.751  1.00 26.33  ?  247  ARG A CD  1 
ATOM   1558  N NE  . ARG A  1  247 ? 49.745  -17.232 89.288  1.00 26.35  ?  247  ARG A NE  1 
ATOM   1559  C CZ  . ARG A  1  247 ? 48.678  -17.983 89.524  1.00 24.56  ?  247  ARG A CZ  1 
ATOM   1560  N NH1 . ARG A  1  247 ? 47.638  -17.513 90.193  1.00 23.22  ?  247  ARG A NH1 1 
ATOM   1561  N NH2 . ARG A  1  247 ? 48.653  -19.235 89.077  1.00 24.43  ?  247  ARG A NH2 1 
ATOM   1562  N N   . ASN A  1  248 ? 55.535  -14.790 92.117  1.00 35.23  ?  248  ASN A N   1 
ATOM   1563  C CA  . ASN A  1  248 ? 56.284  -14.551 93.344  1.00 35.73  ?  248  ASN A CA  1 
ATOM   1564  C C   . ASN A  1  248 ? 57.178  -13.337 93.118  1.00 37.94  ?  248  ASN A C   1 
ATOM   1565  O O   . ASN A  1  248 ? 57.039  -12.613 92.127  1.00 38.65  ?  248  ASN A O   1 
ATOM   1566  C CB  . ASN A  1  248 ? 57.089  -15.795 93.749  1.00 35.76  ?  248  ASN A CB  1 
ATOM   1567  C CG  . ASN A  1  248 ? 56.336  -16.697 94.706  1.00 33.41  ?  248  ASN A CG  1 
ATOM   1568  O OD1 . ASN A  1  248 ? 56.105  -16.341 95.859  1.00 32.68  ?  248  ASN A OD1 1 
ATOM   1569  N ND2 . ASN A  1  248 ? 55.953  -17.877 94.232  1.00 32.03  ?  248  ASN A ND2 1 
ATOM   1570  N N   . ASN A  1  249 ? 58.101  -13.111 94.046  1.00 38.38  ?  249  ASN A N   1 
ATOM   1571  C CA  . ASN A  1  249 ? 59.053  -12.010 93.974  1.00 39.47  ?  249  ASN A CA  1 
ATOM   1572  C C   . ASN A  1  249 ? 60.475  -12.547 93.876  1.00 40.51  ?  249  ASN A C   1 
ATOM   1573  O O   . ASN A  1  249 ? 61.405  -12.029 94.500  1.00 41.26  ?  249  ASN A O   1 
ATOM   1574  C CB  . ASN A  1  249 ? 58.902  -11.080 95.175  1.00 39.04  ?  249  ASN A CB  1 
ATOM   1575  C CG  . ASN A  1  249 ? 57.674  -10.193 95.074  1.00 38.89  ?  249  ASN A CG  1 
ATOM   1576  O OD1 . ASN A  1  249 ? 56.605  -10.534 95.582  1.00 37.56  ?  249  ASN A OD1 1 
ATOM   1577  N ND2 . ASN A  1  249 ? 57.822  -9.049  94.416  1.00 38.69  ?  249  ASN A ND2 1 
ATOM   1578  N N   . LEU A  1  250 ? 60.653  -13.598 93.080  1.00 37.62  ?  250  LEU A N   1 
ATOM   1579  C CA  . LEU A  1  250 ? 61.930  -14.292 92.990  1.00 39.12  ?  250  LEU A CA  1 
ATOM   1580  C C   . LEU A  1  250 ? 62.898  -13.519 92.104  1.00 40.69  ?  250  LEU A C   1 
ATOM   1581  O O   . LEU A  1  250 ? 62.572  -13.172 90.966  1.00 40.51  ?  250  LEU A O   1 
ATOM   1582  C CB  . LEU A  1  250 ? 61.724  -15.703 92.443  1.00 38.69  ?  250  LEU A CB  1 
ATOM   1583  C CG  . LEU A  1  250 ? 61.738  -16.852 93.451  1.00 38.39  ?  250  LEU A CG  1 
ATOM   1584  C CD1 . LEU A  1  250 ? 60.785  -16.570 94.596  1.00 37.08  ?  250  LEU A CD1 1 
ATOM   1585  C CD2 . LEU A  1  250 ? 61.378  -18.161 92.767  1.00 37.93  ?  250  LEU A CD2 1 
ATOM   1586  N N   . THR A  1  251 ? 64.088  -13.252 92.633  1.00 41.93  ?  251  THR A N   1 
ATOM   1587  C CA  . THR A  1  251 ? 65.142  -12.560 91.912  1.00 42.44  ?  251  THR A CA  1 
ATOM   1588  C C   . THR A  1  251 ? 66.221  -13.557 91.486  1.00 43.83  ?  251  THR A C   1 
ATOM   1589  O O   . THR A  1  251 ? 66.156  -14.750 91.786  1.00 43.42  ?  251  THR A O   1 
ATOM   1590  C CB  . THR A  1  251 ? 65.735  -11.446 92.776  1.00 43.49  ?  251  THR A CB  1 
ATOM   1591  O OG1 . THR A  1  251 ? 66.544  -12.023 93.809  1.00 44.36  ?  251  THR A OG1 1 
ATOM   1592  C CG2 . THR A  1  251 ? 64.626  -10.624 93.417  1.00 42.10  ?  251  THR A CG2 1 
ATOM   1593  N N   . GLY A  1  252 ? 67.221  -13.058 90.763  1.00 44.67  ?  252  GLY A N   1 
ATOM   1594  C CA  . GLY A  1  252 ? 68.369  -13.867 90.404  1.00 46.32  ?  252  GLY A CA  1 
ATOM   1595  C C   . GLY A  1  252 ? 68.180  -14.664 89.129  1.00 46.23  ?  252  GLY A C   1 
ATOM   1596  O O   . GLY A  1  252 ? 67.163  -14.586 88.434  1.00 44.90  ?  252  GLY A O   1 
ATOM   1597  N N   . LYS A  1  253 ? 69.204  -15.458 88.823  1.00 48.48  ?  253  LYS A N   1 
ATOM   1598  C CA  . LYS A  1  253 ? 69.222  -16.280 87.624  1.00 48.83  ?  253  LYS A CA  1 
ATOM   1599  C C   . LYS A  1  253 ? 68.467  -17.588 87.849  1.00 47.46  ?  253  LYS A C   1 
ATOM   1600  O O   . LYS A  1  253 ? 68.133  -17.965 88.976  1.00 46.50  ?  253  LYS A O   1 
ATOM   1601  C CB  . LYS A  1  253 ? 70.660  -16.572 87.195  1.00 51.29  ?  253  LYS A CB  1 
ATOM   1602  C CG  . LYS A  1  253 ? 71.449  -15.345 86.773  1.00 52.90  ?  253  LYS A CG  1 
ATOM   1603  C CD  . LYS A  1  253 ? 72.518  -15.693 85.747  1.00 55.12  ?  253  LYS A CD  1 
ATOM   1604  C CE  . LYS A  1  253 ? 73.455  -16.777 86.259  1.00 56.38  ?  253  LYS A CE  1 
ATOM   1605  N NZ  . LYS A  1  253 ? 74.477  -17.155 85.242  1.00 58.64  ?  253  LYS A NZ  1 
ATOM   1606  N N   . ILE A  1  254 ? 68.198  -18.286 86.750  1.00 48.47  ?  254  ILE A N   1 
ATOM   1607  C CA  . ILE A  1  254 ? 67.608  -19.621 86.808  1.00 47.55  ?  254  ILE A CA  1 
ATOM   1608  C C   . ILE A  1  254 ? 68.746  -20.613 87.013  1.00 49.24  ?  254  ILE A C   1 
ATOM   1609  O O   . ILE A  1  254 ? 69.685  -20.646 86.205  1.00 51.09  ?  254  ILE A O   1 
ATOM   1610  C CB  . ILE A  1  254 ? 66.806  -19.940 85.537  1.00 46.95  ?  254  ILE A CB  1 
ATOM   1611  C CG1 . ILE A  1  254 ? 65.636  -18.968 85.382  1.00 45.61  ?  254  ILE A CG1 1 
ATOM   1612  C CG2 . ILE A  1  254 ? 66.311  -21.380 85.563  1.00 46.33  ?  254  ILE A CG2 1 
ATOM   1613  C CD1 . ILE A  1  254 ? 64.865  -19.143 84.093  1.00 45.35  ?  254  ILE A CD1 1 
ATOM   1614  N N   . PRO A  1  255 ? 68.712  -21.420 88.073  1.00 47.76  ?  255  PRO A N   1 
ATOM   1615  C CA  . PRO A  1  255 ? 69.843  -22.311 88.367  1.00 49.44  ?  255  PRO A CA  1 
ATOM   1616  C C   . PRO A  1  255 ? 70.146  -23.249 87.207  1.00 50.57  ?  255  PRO A C   1 
ATOM   1617  O O   . PRO A  1  255 ? 69.265  -23.953 86.707  1.00 49.56  ?  255  PRO A O   1 
ATOM   1618  C CB  . PRO A  1  255 ? 69.375  -23.078 89.610  1.00 48.22  ?  255  PRO A CB  1 
ATOM   1619  C CG  . PRO A  1  255 ? 68.331  -22.201 90.226  1.00 46.33  ?  255  PRO A CG  1 
ATOM   1620  C CD  . PRO A  1  255 ? 67.639  -21.539 89.074  1.00 45.73  ?  255  PRO A CD  1 
ATOM   1621  N N   . SER A  1  256 ? 71.411  -23.249 86.777  1.00 49.98  ?  256  SER A N   1 
ATOM   1622  C CA  . SER A  1  256 ? 71.853  -24.181 85.746  1.00 51.41  ?  256  SER A CA  1 
ATOM   1623  C C   . SER A  1  256 ? 71.701  -25.631 86.183  1.00 51.18  ?  256  SER A C   1 
ATOM   1624  O O   . SER A  1  256 ? 71.647  -26.523 85.329  1.00 51.82  ?  256  SER A O   1 
ATOM   1625  C CB  . SER A  1  256 ? 73.308  -23.898 85.370  1.00 54.01  ?  256  SER A CB  1 
ATOM   1626  O OG  . SER A  1  256 ? 74.137  -23.882 86.520  1.00 54.73  ?  256  SER A OG  1 
ATOM   1627  N N   . SER A  1  257 ? 71.627  -25.882 87.492  1.00 52.76  ?  257  SER A N   1 
ATOM   1628  C CA  . SER A  1  257 ? 71.396  -27.224 88.011  1.00 52.39  ?  257  SER A CA  1 
ATOM   1629  C C   . SER A  1  257 ? 70.059  -27.802 87.569  1.00 50.70  ?  257  SER A C   1 
ATOM   1630  O O   . SER A  1  257 ? 69.854  -29.014 87.704  1.00 50.66  ?  257  SER A O   1 
ATOM   1631  C CB  . SER A  1  257 ? 71.473  -27.214 89.539  1.00 51.69  ?  257  SER A CB  1 
ATOM   1632  O OG  . SER A  1  257 ? 70.443  -26.417 90.096  1.00 49.66  ?  257  SER A OG  1 
ATOM   1633  N N   . PHE A  1  258 ? 69.149  -26.971 87.053  1.00 49.71  ?  258  PHE A N   1 
ATOM   1634  C CA  . PHE A  1  258 ? 67.841  -27.452 86.626  1.00 48.13  ?  258  PHE A CA  1 
ATOM   1635  C C   . PHE A  1  258 ? 67.936  -28.464 85.493  1.00 49.27  ?  258  PHE A C   1 
ATOM   1636  O O   . PHE A  1  258 ? 66.976  -29.207 85.259  1.00 48.27  ?  258  PHE A O   1 
ATOM   1637  C CB  . PHE A  1  258 ? 66.962  -26.275 86.196  1.00 46.77  ?  258  PHE A CB  1 
ATOM   1638  C CG  . PHE A  1  258 ? 66.150  -25.687 87.313  1.00 44.86  ?  258  PHE A CG  1 
ATOM   1639  C CD1 . PHE A  1  258 ? 66.600  -25.745 88.621  1.00 44.87  ?  258  PHE A CD1 1 
ATOM   1640  C CD2 . PHE A  1  258 ? 64.936  -25.072 87.054  1.00 43.15  ?  258  PHE A CD2 1 
ATOM   1641  C CE1 . PHE A  1  258 ? 65.853  -25.204 89.651  1.00 43.24  ?  258  PHE A CE1 1 
ATOM   1642  C CE2 . PHE A  1  258 ? 64.185  -24.529 88.079  1.00 41.52  ?  258  PHE A CE2 1 
ATOM   1643  C CZ  . PHE A  1  258 ? 64.644  -24.595 89.379  1.00 41.59  ?  258  PHE A CZ  1 
ATOM   1644  N N   . GLY A  1  259 ? 69.065  -28.508 84.782  1.00 51.65  ?  259  GLY A N   1 
ATOM   1645  C CA  . GLY A  1  259 ? 69.261  -29.515 83.755  1.00 53.02  ?  259  GLY A CA  1 
ATOM   1646  C C   . GLY A  1  259 ? 69.189  -30.939 84.268  1.00 53.13  ?  259  GLY A C   1 
ATOM   1647  O O   . GLY A  1  259 ? 68.951  -31.861 83.481  1.00 53.76  ?  259  GLY A O   1 
ATOM   1648  N N   . ASN A  1  260 ? 69.389  -31.141 85.572  1.00 52.47  ?  260  ASN A N   1 
ATOM   1649  C CA  . ASN A  1  260 ? 69.349  -32.480 86.146  1.00 52.60  ?  260  ASN A CA  1 
ATOM   1650  C C   . ASN A  1  260 ? 67.933  -33.012 86.320  1.00 50.65  ?  260  ASN A C   1 
ATOM   1651  O O   . ASN A  1  260 ? 67.762  -34.225 86.488  1.00 50.89  ?  260  ASN A O   1 
ATOM   1652  C CB  . ASN A  1  260 ? 70.068  -32.498 87.497  1.00 52.79  ?  260  ASN A CB  1 
ATOM   1653  C CG  . ASN A  1  260 ? 71.534  -32.128 87.383  1.00 54.95  ?  260  ASN A CG  1 
ATOM   1654  O OD1 . ASN A  1  260 ? 72.232  -32.584 86.478  1.00 56.85  ?  260  ASN A OD1 1 
ATOM   1655  N ND2 . ASN A  1  260 ? 72.008  -31.297 88.305  1.00 54.79  ?  260  ASN A ND2 1 
ATOM   1656  N N   . LEU A  1  261 ? 66.917  -32.149 86.279  1.00 50.52  ?  261  LEU A N   1 
ATOM   1657  C CA  . LEU A  1  261 ? 65.538  -32.580 86.505  1.00 48.66  ?  261  LEU A CA  1 
ATOM   1658  C C   . LEU A  1  261 ? 65.033  -33.278 85.246  1.00 49.15  ?  261  LEU A C   1 
ATOM   1659  O O   . LEU A  1  261 ? 64.301  -32.719 84.425  1.00 48.44  ?  261  LEU A O   1 
ATOM   1660  C CB  . LEU A  1  261 ? 64.653  -31.401 86.889  1.00 46.70  ?  261  LEU A CB  1 
ATOM   1661  C CG  . LEU A  1  261 ? 65.026  -30.661 88.174  1.00 46.15  ?  261  LEU A CG  1 
ATOM   1662  C CD1 . LEU A  1  261 ? 64.959  -29.155 87.968  1.00 45.63  ?  261  LEU A CD1 1 
ATOM   1663  C CD2 . LEU A  1  261 ? 64.139  -31.093 89.328  1.00 44.53  ?  261  LEU A CD2 1 
ATOM   1664  N N   . LYS A  1  262 ? 65.442  -34.539 85.100  1.00 52.14  ?  262  LYS A N   1 
ATOM   1665  C CA  . LYS A  1  262 ? 65.044  -35.356 83.963  1.00 52.90  ?  262  LYS A CA  1 
ATOM   1666  C C   . LYS A  1  262 ? 63.638  -35.925 84.102  1.00 51.29  ?  262  LYS A C   1 
ATOM   1667  O O   . LYS A  1  262 ? 63.138  -36.532 83.149  1.00 51.76  ?  262  LYS A O   1 
ATOM   1668  C CB  . LYS A  1  262 ? 66.041  -36.502 83.772  1.00 55.12  ?  262  LYS A CB  1 
ATOM   1669  C CG  . LYS A  1  262 ? 66.862  -36.424 82.495  1.00 57.24  ?  262  LYS A CG  1 
ATOM   1670  C CD  . LYS A  1  262 ? 67.960  -35.377 82.596  1.00 58.08  ?  262  LYS A CD  1 
ATOM   1671  C CE  . LYS A  1  262 ? 68.846  -35.394 81.359  1.00 60.43  ?  262  LYS A CE  1 
ATOM   1672  N NZ  . LYS A  1  262 ? 70.052  -34.536 81.522  1.00 61.61  ?  262  LYS A NZ  1 
ATOM   1673  N N   . ASN A  1  263 ? 62.998  -35.757 85.259  1.00 53.76  ?  263  ASN A N   1 
ATOM   1674  C CA  . ASN A  1  263 ? 61.651  -36.259 85.487  1.00 52.24  ?  263  ASN A CA  1 
ATOM   1675  C C   . ASN A  1  263 ? 60.586  -35.170 85.473  1.00 50.30  ?  263  ASN A C   1 
ATOM   1676  O O   . ASN A  1  263 ? 59.394  -35.496 85.508  1.00 49.09  ?  263  ASN A O   1 
ATOM   1677  C CB  . ASN A  1  263 ? 61.584  -37.005 86.829  1.00 51.73  ?  263  ASN A CB  1 
ATOM   1678  C CG  . ASN A  1  263 ? 61.650  -38.516 86.670  1.00 53.08  ?  263  ASN A CG  1 
ATOM   1679  O OD1 . ASN A  1  263 ? 61.174  -39.071 85.679  1.00 54.22  ?  263  ASN A OD1 1 
ATOM   1680  N ND2 . ASN A  1  263 ? 62.240  -39.187 87.656  1.00 53.41  ?  263  ASN A ND2 1 
ATOM   1681  N N   . VAL A  1  264 ? 60.976  -33.900 85.410  1.00 45.32  ?  264  VAL A N   1 
ATOM   1682  C CA  . VAL A  1  264 ? 60.029  -32.793 85.520  1.00 43.51  ?  264  VAL A CA  1 
ATOM   1683  C C   . VAL A  1  264 ? 59.280  -32.630 84.205  1.00 43.38  ?  264  VAL A C   1 
ATOM   1684  O O   . VAL A  1  264 ? 59.888  -32.563 83.130  1.00 44.78  ?  264  VAL A O   1 
ATOM   1685  C CB  . VAL A  1  264 ? 60.752  -31.495 85.913  1.00 43.49  ?  264  VAL A CB  1 
ATOM   1686  C CG1 . VAL A  1  264 ? 59.927  -30.281 85.512  1.00 42.17  ?  264  VAL A CG1 1 
ATOM   1687  C CG2 . VAL A  1  264 ? 61.025  -31.475 87.407  1.00 42.95  ?  264  VAL A CG2 1 
ATOM   1688  N N   . THR A  1  265 ? 57.948  -32.568 84.289  1.00 40.86  ?  265  THR A N   1 
ATOM   1689  C CA  . THR A  1  265 ? 57.108  -32.338 83.123  1.00 40.54  ?  265  THR A CA  1 
ATOM   1690  C C   . THR A  1  265 ? 56.469  -30.959 83.096  1.00 39.10  ?  265  THR A C   1 
ATOM   1691  O O   . THR A  1  265 ? 56.058  -30.510 82.022  1.00 39.09  ?  265  THR A O   1 
ATOM   1692  C CB  . THR A  1  265 ? 55.992  -33.391 83.050  1.00 40.00  ?  265  THR A CB  1 
ATOM   1693  O OG1 . THR A  1  265 ? 55.188  -33.322 84.235  1.00 38.36  ?  265  THR A OG1 1 
ATOM   1694  C CG2 . THR A  1  265 ? 56.586  -34.785 82.936  1.00 41.60  ?  265  THR A CG2 1 
ATOM   1695  N N   . LEU A  1  266 ? 56.385  -30.273 84.233  1.00 37.87  ?  266  LEU A N   1 
ATOM   1696  C CA  . LEU A  1  266 ? 55.782  -28.949 84.302  1.00 36.51  ?  266  LEU A CA  1 
ATOM   1697  C C   . LEU A  1  266 ? 56.693  -28.023 85.091  1.00 36.66  ?  266  LEU A C   1 
ATOM   1698  O O   . LEU A  1  266 ? 57.076  -28.340 86.222  1.00 36.63  ?  266  LEU A O   1 
ATOM   1699  C CB  . LEU A  1  266 ? 54.395  -29.002 84.949  1.00 34.73  ?  266  LEU A CB  1 
ATOM   1700  C CG  . LEU A  1  266 ? 53.811  -27.647 85.353  1.00 33.33  ?  266  LEU A CG  1 
ATOM   1701  C CD1 . LEU A  1  266 ? 53.525  -26.797 84.123  1.00 33.38  ?  266  LEU A CD1 1 
ATOM   1702  C CD2 . LEU A  1  266 ? 52.559  -27.824 86.197  1.00 31.84  ?  266  LEU A CD2 1 
ATOM   1703  N N   . LEU A  1  267 ? 57.031  -26.880 84.499  1.00 34.08  ?  267  LEU A N   1 
ATOM   1704  C CA  . LEU A  1  267 ? 57.862  -25.868 85.149  1.00 34.34  ?  267  LEU A CA  1 
ATOM   1705  C C   . LEU A  1  267 ? 57.170  -24.519 84.987  1.00 33.21  ?  267  LEU A C   1 
ATOM   1706  O O   . LEU A  1  267 ? 57.306  -23.863 83.950  1.00 33.69  ?  267  LEU A O   1 
ATOM   1707  C CB  . LEU A  1  267 ? 59.271  -25.846 84.565  1.00 36.31  ?  267  LEU A CB  1 
ATOM   1708  C CG  . LEU A  1  267 ? 60.226  -24.809 85.161  1.00 36.86  ?  267  LEU A CG  1 
ATOM   1709  C CD1 . LEU A  1  267 ? 60.335  -24.978 86.669  1.00 36.31  ?  267  LEU A CD1 1 
ATOM   1710  C CD2 . LEU A  1  267 ? 61.598  -24.906 84.511  1.00 38.97  ?  267  LEU A CD2 1 
ATOM   1711  N N   . ASN A  1  268 ? 56.428  -24.110 86.012  1.00 33.39  ?  268  ASN A N   1 
ATOM   1712  C CA  . ASN A  1  268 ? 55.742  -22.824 86.025  1.00 32.31  ?  268  ASN A CA  1 
ATOM   1713  C C   . ASN A  1  268 ? 56.505  -21.883 86.949  1.00 32.60  ?  268  ASN A C   1 
ATOM   1714  O O   . ASN A  1  268 ? 56.517  -22.071 88.169  1.00 32.21  ?  268  ASN A O   1 
ATOM   1715  C CB  . ASN A  1  268 ? 54.291  -22.982 86.471  1.00 30.61  ?  268  ASN A CB  1 
ATOM   1716  C CG  . ASN A  1  268 ? 53.381  -23.433 85.345  1.00 30.23  ?  268  ASN A CG  1 
ATOM   1717  O OD1 . ASN A  1  268 ? 53.744  -23.365 84.171  1.00 31.11  ?  268  ASN A OD1 1 
ATOM   1718  N ND2 . ASN A  1  268 ? 52.191  -23.900 85.699  1.00 29.03  ?  268  ASN A ND2 1 
ATOM   1719  N N   . MET A  1  269 ? 57.142  -20.869 86.360  1.00 32.71  ?  269  MET A N   1 
ATOM   1720  C CA  . MET A  1  269 ? 57.869  -19.869 87.133  1.00 33.16  ?  269  MET A CA  1 
ATOM   1721  C C   . MET A  1  269 ? 57.595  -18.466 86.607  1.00 32.90  ?  269  MET A C   1 
ATOM   1722  O O   . MET A  1  269 ? 58.408  -17.558 86.824  1.00 33.77  ?  269  MET A O   1 
ATOM   1723  C CB  . MET A  1  269 ? 59.373  -20.155 87.124  1.00 35.00  ?  269  MET A CB  1 
ATOM   1724  C CG  . MET A  1  269 ? 59.786  -21.274 88.069  1.00 35.28  ?  269  MET A CG  1 
ATOM   1725  S SD  . MET A  1  269 ? 61.565  -21.569 88.122  1.00 37.53  ?  269  MET A SD  1 
ATOM   1726  C CE  . MET A  1  269 ? 62.048  -21.123 86.458  1.00 38.78  ?  269  MET A CE  1 
ATOM   1727  N N   . PHE A  1  270 ? 56.469  -18.274 85.924  1.00 34.84  ?  270  PHE A N   1 
ATOM   1728  C CA  . PHE A  1  270 ? 56.124  -16.996 85.330  1.00 35.57  ?  270  PHE A CA  1 
ATOM   1729  C C   . PHE A  1  270 ? 55.762  -15.978 86.409  1.00 35.01  ?  270  PHE A C   1 
ATOM   1730  O O   . PHE A  1  270 ? 55.595  -16.306 87.586  1.00 33.87  ?  270  PHE A O   1 
ATOM   1731  C CB  . PHE A  1  270 ? 54.964  -17.163 84.350  1.00 34.42  ?  270  PHE A CB  1 
ATOM   1732  C CG  . PHE A  1  270 ? 53.718  -17.734 84.970  1.00 32.05  ?  270  PHE A CG  1 
ATOM   1733  C CD1 . PHE A  1  270 ? 52.786  -16.906 85.577  1.00 30.80  ?  270  PHE A CD1 1 
ATOM   1734  C CD2 . PHE A  1  270 ? 53.475  -19.096 84.936  1.00 31.96  ?  270  PHE A CD2 1 
ATOM   1735  C CE1 . PHE A  1  270 ? 51.640  -17.428 86.146  1.00 29.50  ?  270  PHE A CE1 1 
ATOM   1736  C CE2 . PHE A  1  270 ? 52.329  -19.623 85.501  1.00 30.65  ?  270  PHE A CE2 1 
ATOM   1737  C CZ  . PHE A  1  270 ? 51.411  -18.788 86.106  1.00 29.42  ?  270  PHE A CZ  1 
ATOM   1738  N N   . GLU A  1  271 ? 55.647  -14.718 85.987  1.00 38.98  ?  271  GLU A N   1 
ATOM   1739  C CA  . GLU A  1  271 ? 55.260  -13.615 86.865  1.00 38.31  ?  271  GLU A CA  1 
ATOM   1740  C C   . GLU A  1  271 ? 56.211  -13.513 88.060  1.00 38.81  ?  271  GLU A C   1 
ATOM   1741  O O   . GLU A  1  271 ? 55.815  -13.602 89.223  1.00 37.58  ?  271  GLU A O   1 
ATOM   1742  C CB  . GLU A  1  271 ? 53.805  -13.759 87.323  1.00 35.54  ?  271  GLU A CB  1 
ATOM   1743  C CG  . GLU A  1  271 ? 52.794  -13.124 86.384  1.00 34.45  ?  271  GLU A CG  1 
ATOM   1744  C CD  . GLU A  1  271 ? 51.372  -13.244 86.894  1.00 30.81  ?  271  GLU A CD  1 
ATOM   1745  O OE1 . GLU A  1  271 ? 51.038  -12.569 87.891  1.00 29.05  ?  271  GLU A OE1 1 
ATOM   1746  O OE2 . GLU A  1  271 ? 50.588  -14.015 86.301  1.00 29.86  -1 271  GLU A OE2 1 
ATOM   1747  N N   . ASN A  1  272 ? 57.489  -13.325 87.743  1.00 39.51  ?  272  ASN A N   1 
ATOM   1748  C CA  . ASN A  1  272 ? 58.533  -13.206 88.747  1.00 39.84  ?  272  ASN A CA  1 
ATOM   1749  C C   . ASN A  1  272 ? 59.490  -12.104 88.319  1.00 40.62  ?  272  ASN A C   1 
ATOM   1750  O O   . ASN A  1  272 ? 59.273  -11.418 87.315  1.00 41.28  ?  272  ASN A O   1 
ATOM   1751  C CB  . ASN A  1  272 ? 59.265  -14.540 88.940  1.00 40.19  ?  272  ASN A CB  1 
ATOM   1752  C CG  . ASN A  1  272 ? 58.663  -15.383 90.044  1.00 39.30  ?  272  ASN A CG  1 
ATOM   1753  O OD1 . ASN A  1  272 ? 58.769  -15.043 91.220  1.00 38.87  ?  272  ASN A OD1 1 
ATOM   1754  N ND2 . ASN A  1  272 ? 58.020  -16.484 89.670  1.00 38.28  ?  272  ASN A ND2 1 
ATOM   1755  N N   . GLN A  1  273 ? 60.563  -11.933 89.090  1.00 44.07  ?  273  GLN A N   1 
ATOM   1756  C CA  . GLN A  1  273 ? 61.621  -10.985 88.767  1.00 44.31  ?  273  GLN A CA  1 
ATOM   1757  C C   . GLN A  1  273 ? 62.917  -11.696 88.392  1.00 44.66  ?  273  GLN A C   1 
ATOM   1758  O O   . GLN A  1  273 ? 64.010  -11.181 88.642  1.00 44.80  ?  273  GLN A O   1 
ATOM   1759  C CB  . GLN A  1  273 ? 61.859  -10.024 89.930  1.00 44.20  ?  273  GLN A CB  1 
ATOM   1760  C CG  . GLN A  1  273 ? 60.595  -9.378  90.466  1.00 42.93  ?  273  GLN A CG  1 
ATOM   1761  C CD  . GLN A  1  273 ? 60.883  -8.162  91.323  1.00 42.81  ?  273  GLN A CD  1 
ATOM   1762  O OE1 . GLN A  1  273 ? 61.545  -7.221  90.883  1.00 42.68  ?  273  GLN A OE1 1 
ATOM   1763  N NE2 . GLN A  1  273 ? 60.390  -8.177  92.556  1.00 41.77  ?  273  GLN A NE2 1 
ATOM   1764  N N   . LEU A  1  274 ? 62.805  -12.885 87.801  1.00 42.53  ?  274  LEU A N   1 
ATOM   1765  C CA  . LEU A  1  274 ? 63.982  -13.628 87.374  1.00 42.83  ?  274  LEU A CA  1 
ATOM   1766  C C   . LEU A  1  274 ? 64.761  -12.830 86.336  1.00 43.08  ?  274  LEU A C   1 
ATOM   1767  O O   . LEU A  1  274 ? 64.188  -12.111 85.513  1.00 43.06  ?  274  LEU A O   1 
ATOM   1768  C CB  . LEU A  1  274 ? 63.581  -14.987 86.798  1.00 42.85  ?  274  LEU A CB  1 
ATOM   1769  C CG  . LEU A  1  274 ? 63.541  -16.198 87.734  1.00 42.53  ?  274  LEU A CG  1 
ATOM   1770  C CD1 . LEU A  1  274 ? 62.875  -15.860 89.058  1.00 42.17  ?  274  LEU A CD1 1 
ATOM   1771  C CD2 . LEU A  1  274 ? 62.818  -17.356 87.064  1.00 41.99  ?  274  LEU A CD2 1 
ATOM   1772  N N   . SER A  1  275 ? 66.083  -12.965 86.379  1.00 42.15  ?  275  SER A N   1 
ATOM   1773  C CA  . SER A  1  275 ? 66.962  -12.155 85.547  1.00 43.93  ?  275  SER A CA  1 
ATOM   1774  C C   . SER A  1  275 ? 68.035  -13.057 84.949  1.00 45.69  ?  275  SER A C   1 
ATOM   1775  O O   . SER A  1  275 ? 67.972  -14.285 85.054  1.00 45.38  ?  275  SER A O   1 
ATOM   1776  C CB  . SER A  1  275 ? 67.568  -11.004 86.360  1.00 44.85  ?  275  SER A CB  1 
ATOM   1777  O OG  . SER A  1  275 ? 68.252  -11.490 87.502  1.00 45.45  ?  275  SER A OG  1 
ATOM   1778  N N   . GLY A  1  276 ? 69.029  -12.442 84.313  1.00 49.99  ?  276  GLY A N   1 
ATOM   1779  C CA  . GLY A  1  276 ? 70.025  -13.222 83.610  1.00 51.82  ?  276  GLY A CA  1 
ATOM   1780  C C   . GLY A  1  276 ? 69.459  -13.815 82.328  1.00 51.42  ?  276  GLY A C   1 
ATOM   1781  O O   . GLY A  1  276 ? 68.460  -13.351 81.771  1.00 50.11  ?  276  GLY A O   1 
ATOM   1782  N N   . GLU A  1  277 ? 70.123  -14.867 81.864  1.00 53.41  ?  277  GLU A N   1 
ATOM   1783  C CA  . GLU A  1  277 ? 69.754  -15.563 80.644  1.00 53.45  ?  277  GLU A CA  1 
ATOM   1784  C C   . GLU A  1  277 ? 69.213  -16.946 80.977  1.00 52.36  ?  277  GLU A C   1 
ATOM   1785  O O   . GLU A  1  277 ? 69.519  -17.521 82.025  1.00 52.27  ?  277  GLU A O   1 
ATOM   1786  C CB  . GLU A  1  277 ? 70.955  -15.683 79.700  1.00 56.04  ?  277  GLU A CB  1 
ATOM   1787  C CG  . GLU A  1  277 ? 71.975  -14.567 79.857  1.00 57.75  ?  277  GLU A CG  1 
ATOM   1788  C CD  . GLU A  1  277 ? 72.828  -14.379 78.619  1.00 60.06  ?  277  GLU A CD  1 
ATOM   1789  O OE1 . GLU A  1  277 ? 72.802  -15.263 77.736  1.00 60.58  ?  277  GLU A OE1 1 
ATOM   1790  O OE2 . GLU A  1  277 ? 73.530  -13.350 78.530  1.00 61.46  -1 277  GLU A OE2 1 
ATOM   1791  N N   . ILE A  1  278 ? 68.392  -17.474 80.075  1.00 51.01  ?  278  ILE A N   1 
ATOM   1792  C CA  . ILE A  1  278 ? 67.868  -18.827 80.240  1.00 50.18  ?  278  ILE A CA  1 
ATOM   1793  C C   . ILE A  1  278 ? 69.037  -19.795 80.110  1.00 52.25  ?  278  ILE A C   1 
ATOM   1794  O O   . ILE A  1  278 ? 69.702  -19.829 79.064  1.00 54.05  ?  278  ILE A O   1 
ATOM   1795  C CB  . ILE A  1  278 ? 66.762  -19.142 79.221  1.00 49.13  ?  278  ILE A CB  1 
ATOM   1796  C CG1 . ILE A  1  278 ? 65.614  -18.142 79.355  1.00 47.15  ?  278  ILE A CG1 1 
ATOM   1797  C CG2 . ILE A  1  278 ? 66.248  -20.561 79.420  1.00 48.44  ?  278  ILE A CG2 1 
ATOM   1798  C CD1 . ILE A  1  278 ? 64.607  -18.211 78.233  1.00 46.36  ?  278  ILE A CD1 1 
ATOM   1799  N N   . PRO A  1  279 ? 69.331  -20.578 81.144  1.00 52.90  ?  279  PRO A N   1 
ATOM   1800  C CA  . PRO A  1  279 ? 70.480  -21.489 81.096  1.00 54.94  ?  279  PRO A CA  1 
ATOM   1801  C C   . PRO A  1  279 ? 70.330  -22.506 79.980  1.00 55.66  ?  279  PRO A C   1 
ATOM   1802  O O   . PRO A  1  279 ? 69.281  -23.156 79.855  1.00 54.19  ?  279  PRO A O   1 
ATOM   1803  C CB  . PRO A  1  279 ? 70.460  -22.164 82.478  1.00 54.12  ?  279  PRO A CB  1 
ATOM   1804  C CG  . PRO A  1  279 ? 69.100  -21.905 83.032  1.00 51.55  ?  279  PRO A CG  1 
ATOM   1805  C CD  . PRO A  1  279 ? 68.640  -20.614 82.443  1.00 51.00  ?  279  PRO A CD  1 
ATOM   1806  N N   . PRO A  1  280 ? 71.356  -22.662 79.138  1.00 57.27  ?  280  PRO A N   1 
ATOM   1807  C CA  . PRO A  1  280 ? 71.274  -23.652 78.051  1.00 58.22  ?  280  PRO A CA  1 
ATOM   1808  C C   . PRO A  1  280 ? 71.091  -25.077 78.540  1.00 57.94  ?  280  PRO A C   1 
ATOM   1809  O O   . PRO A  1  280 ? 70.601  -25.919 77.778  1.00 58.03  ?  280  PRO A O   1 
ATOM   1810  C CB  . PRO A  1  280 ? 72.611  -23.481 77.316  1.00 61.06  ?  280  PRO A CB  1 
ATOM   1811  C CG  . PRO A  1  280 ? 73.067  -22.102 77.664  1.00 61.24  ?  280  PRO A CG  1 
ATOM   1812  C CD  . PRO A  1  280 ? 72.581  -21.849 79.061  1.00 59.25  ?  280  PRO A CD  1 
ATOM   1813  N N   . GLU A  1  281 ? 71.470  -25.377 79.784  1.00 60.27  ?  281  GLU A N   1 
ATOM   1814  C CA  . GLU A  1  281 ? 71.272  -26.709 80.344  1.00 59.93  ?  281  GLU A CA  1 
ATOM   1815  C C   . GLU A  1  281 ? 69.801  -27.070 80.505  1.00 57.55  ?  281  GLU A C   1 
ATOM   1816  O O   . GLU A  1  281 ? 69.499  -28.238 80.774  1.00 57.30  ?  281  GLU A O   1 
ATOM   1817  C CB  . GLU A  1  281 ? 71.982  -26.835 81.697  1.00 60.11  ?  281  GLU A CB  1 
ATOM   1818  C CG  . GLU A  1  281 ? 73.443  -26.377 81.729  1.00 62.41  ?  281  GLU A CG  1 
ATOM   1819  C CD  . GLU A  1  281 ? 73.611  -24.866 81.787  1.00 62.26  ?  281  GLU A CD  1 
ATOM   1820  O OE1 . GLU A  1  281 ? 72.649  -24.136 81.471  1.00 60.67  ?  281  GLU A OE1 1 
ATOM   1821  O OE2 . GLU A  1  281 ? 74.714  -24.409 82.150  1.00 63.81  -1 281  GLU A OE2 1 
ATOM   1822  N N   . ILE A  1  282 ? 68.887  -26.106 80.358  1.00 55.71  ?  282  ILE A N   1 
ATOM   1823  C CA  . ILE A  1  282 ? 67.459  -26.412 80.387  1.00 53.59  ?  282  ILE A CA  1 
ATOM   1824  C C   . ILE A  1  282 ? 67.106  -27.409 79.290  1.00 54.26  ?  282  ILE A C   1 
ATOM   1825  O O   . ILE A  1  282 ? 66.194  -28.230 79.453  1.00 53.12  ?  282  ILE A O   1 
ATOM   1826  C CB  . ILE A  1  282 ? 66.638  -25.108 80.280  1.00 51.99  ?  282  ILE A CB  1 
ATOM   1827  C CG1 . ILE A  1  282 ? 66.470  -24.476 81.665  1.00 50.60  ?  282  ILE A CG1 1 
ATOM   1828  C CG2 . ILE A  1  282 ? 65.276  -25.353 79.636  1.00 50.51  ?  282  ILE A CG2 1 
ATOM   1829  C CD1 . ILE A  1  282 ? 65.488  -23.323 81.706  1.00 48.82  ?  282  ILE A CD1 1 
ATOM   1830  N N   . GLY A  1  283 ? 67.837  -27.375 78.172  1.00 55.23  ?  283  GLY A N   1 
ATOM   1831  C CA  . GLY A  1  283 ? 67.597  -28.322 77.096  1.00 56.18  ?  283  GLY A CA  1 
ATOM   1832  C C   . GLY A  1  283 ? 67.701  -29.770 77.530  1.00 56.67  ?  283  GLY A C   1 
ATOM   1833  O O   . GLY A  1  283 ? 67.056  -30.645 76.946  1.00 56.66  ?  283  GLY A O   1 
ATOM   1834  N N   . ASN A  1  284 ? 68.511  -30.049 78.554  1.00 60.93  ?  284  ASN A N   1 
ATOM   1835  C CA  . ASN A  1  284 ? 68.620  -31.409 79.064  1.00 61.35  ?  284  ASN A CA  1 
ATOM   1836  C C   . ASN A  1  284 ? 67.349  -31.881 79.761  1.00 59.09  ?  284  ASN A C   1 
ATOM   1837  O O   . ASN A  1  284 ? 67.233  -33.077 80.051  1.00 59.34  ?  284  ASN A O   1 
ATOM   1838  C CB  . ASN A  1  284 ? 69.809  -31.530 80.022  1.00 62.44  ?  284  ASN A CB  1 
ATOM   1839  C CG  . ASN A  1  284 ? 71.145  -31.628 79.295  1.00 65.25  ?  284  ASN A CG  1 
ATOM   1840  O OD1 . ASN A  1  284 ? 71.355  -32.530 78.481  1.00 66.80  ?  284  ASN A OD1 1 
ATOM   1841  N ND2 . ASN A  1  284 ? 72.058  -30.704 79.612  1.00 66.01  ?  284  ASN A ND2 1 
ATOM   1842  N N   . MET A  1  285 ? 66.394  -30.986 80.023  1.00 56.74  ?  285  MET A N   1 
ATOM   1843  C CA  . MET A  1  285 ? 65.130  -31.355 80.662  1.00 54.61  ?  285  MET A CA  1 
ATOM   1844  C C   . MET A  1  285 ? 64.242  -32.051 79.629  1.00 54.58  ?  285  MET A C   1 
ATOM   1845  O O   . MET A  1  285 ? 63.232  -31.522 79.164  1.00 53.36  ?  285  MET A O   1 
ATOM   1846  C CB  . MET A  1  285 ? 64.442  -30.126 81.244  1.00 52.59  ?  285  MET A CB  1 
ATOM   1847  C CG  . MET A  1  285 ? 65.150  -29.509 82.441  1.00 52.75  ?  285  MET A CG  1 
ATOM   1848  S SD  . MET A  1  285 ? 64.204  -28.145 83.155  1.00 50.24  ?  285  MET A SD  1 
ATOM   1849  C CE  . MET A  1  285 ? 63.368  -28.969 84.511  1.00 48.47  ?  285  MET A CE  1 
ATOM   1850  N N   . THR A  1  286 ? 64.643  -33.277 79.281  1.00 52.31  ?  286  THR A N   1 
ATOM   1851  C CA  . THR A  1  286 ? 64.061  -33.999 78.155  1.00 52.94  ?  286  THR A CA  1 
ATOM   1852  C C   . THR A  1  286 ? 62.636  -34.472 78.408  1.00 51.11  ?  286  THR A C   1 
ATOM   1853  O O   . THR A  1  286 ? 61.986  -34.938 77.465  1.00 51.42  ?  286  THR A O   1 
ATOM   1854  C CB  . THR A  1  286 ? 64.946  -35.196 77.800  1.00 55.30  ?  286  THR A CB  1 
ATOM   1855  O OG1 . THR A  1  286 ? 65.263  -35.925 78.992  1.00 55.16  ?  286  THR A OG1 1 
ATOM   1856  C CG2 . THR A  1  286 ? 66.238  -34.721 77.150  1.00 57.43  ?  286  THR A CG2 1 
ATOM   1857  N N   . ALA A  1  287 ? 62.132  -34.367 79.636  1.00 48.98  ?  287  ALA A N   1 
ATOM   1858  C CA  . ALA A  1  287 ? 60.765  -34.763 79.953  1.00 47.24  ?  287  ALA A CA  1 
ATOM   1859  C C   . ALA A  1  287 ? 59.827  -33.572 80.087  1.00 45.20  ?  287  ALA A C   1 
ATOM   1860  O O   . ALA A  1  287 ? 58.670  -33.748 80.482  1.00 43.62  ?  287  ALA A O   1 
ATOM   1861  C CB  . ALA A  1  287 ? 60.737  -35.595 81.236  1.00 46.74  ?  287  ALA A CB  1 
ATOM   1862  N N   . LEU A  1  288 ? 60.298  -32.370 79.768  1.00 46.58  ?  288  LEU A N   1 
ATOM   1863  C CA  . LEU A  1  288 ? 59.500  -31.168 79.964  1.00 44.89  ?  288  LEU A CA  1 
ATOM   1864  C C   . LEU A  1  288 ? 58.327  -31.129 78.991  1.00 44.04  ?  288  LEU A C   1 
ATOM   1865  O O   . LEU A  1  288 ? 58.496  -31.326 77.784  1.00 45.31  ?  288  LEU A O   1 
ATOM   1866  C CB  . LEU A  1  288 ? 60.377  -29.929 79.793  1.00 45.58  ?  288  LEU A CB  1 
ATOM   1867  C CG  . LEU A  1  288 ? 59.839  -28.615 80.354  1.00 43.54  ?  288  LEU A CG  1 
ATOM   1868  C CD1 . LEU A  1  288 ? 59.586  -28.736 81.845  1.00 42.27  ?  288  LEU A CD1 1 
ATOM   1869  C CD2 . LEU A  1  288 ? 60.826  -27.500 80.070  1.00 44.49  ?  288  LEU A CD2 1 
ATOM   1870  N N   . ASP A  1  289 ? 57.135  -30.870 79.524  1.00 44.66  ?  289  ASP A N   1 
ATOM   1871  C CA  . ASP A  1  289 ? 55.910  -30.745 78.741  1.00 43.79  ?  289  ASP A CA  1 
ATOM   1872  C C   . ASP A  1  289 ? 55.441  -29.306 78.591  1.00 42.64  ?  289  ASP A C   1 
ATOM   1873  O O   . ASP A  1  289 ? 54.963  -28.925 77.520  1.00 42.60  ?  289  ASP A O   1 
ATOM   1874  C CB  . ASP A  1  289 ? 54.792  -31.582 79.377  1.00 42.60  ?  289  ASP A CB  1 
ATOM   1875  C CG  . ASP A  1  289 ? 53.477  -31.475 78.627  1.00 42.28  ?  289  ASP A CG  1 
ATOM   1876  O OD1 . ASP A  1  289 ? 53.501  -31.329 77.387  1.00 44.02  ?  289  ASP A OD1 1 
ATOM   1877  O OD2 . ASP A  1  289 ? 52.415  -31.535 79.283  1.00 40.62  -1 289  ASP A OD2 1 
ATOM   1878  N N   . THR A  1  290 ? 55.569  -28.497 79.642  1.00 41.90  ?  290  THR A N   1 
ATOM   1879  C CA  . THR A  1  290 ? 55.102  -27.114 79.638  1.00 40.25  ?  290  THR A CA  1 
ATOM   1880  C C   . THR A  1  290 ? 56.119  -26.253 80.371  1.00 40.45  ?  290  THR A C   1 
ATOM   1881  O O   . THR A  1  290 ? 56.403  -26.494 81.548  1.00 40.20  ?  290  THR A O   1 
ATOM   1882  C CB  . THR A  1  290 ? 53.725  -26.993 80.301  1.00 38.19  ?  290  THR A CB  1 
ATOM   1883  O OG1 . THR A  1  290 ? 52.774  -27.797 79.591  1.00 38.27  ?  290  THR A OG1 1 
ATOM   1884  C CG2 . THR A  1  290 ? 53.259  -25.544 80.315  1.00 37.23  ?  290  THR A CG2 1 
ATOM   1885  N N   . LEU A  1  291 ? 56.662  -25.253 79.679  1.00 37.06  ?  291  LEU A N   1 
ATOM   1886  C CA  . LEU A  1  291 ? 57.664  -24.351 80.239  1.00 37.56  ?  291  LEU A CA  1 
ATOM   1887  C C   . LEU A  1  291 ? 57.150  -22.924 80.127  1.00 36.54  ?  291  LEU A C   1 
ATOM   1888  O O   . LEU A  1  291 ? 56.905  -22.435 79.019  1.00 36.77  ?  291  LEU A O   1 
ATOM   1889  C CB  . LEU A  1  291 ? 59.003  -24.502 79.514  1.00 39.73  ?  291  LEU A CB  1 
ATOM   1890  C CG  . LEU A  1  291 ? 60.103  -23.495 79.855  1.00 40.57  ?  291  LEU A CG  1 
ATOM   1891  C CD1 . LEU A  1  291 ? 60.355  -23.469 81.354  1.00 39.96  ?  291  LEU A CD1 1 
ATOM   1892  C CD2 . LEU A  1  291 ? 61.382  -23.830 79.104  1.00 42.86  ?  291  LEU A CD2 1 
ATOM   1893  N N   . SER A  1  292 ? 56.991  -22.258 81.270  1.00 36.19  ?  292  SER A N   1 
ATOM   1894  C CA  . SER A  1  292 ? 56.416  -20.917 81.328  1.00 35.14  ?  292  SER A CA  1 
ATOM   1895  C C   . SER A  1  292 ? 57.300  -20.012 82.173  1.00 35.57  ?  292  SER A C   1 
ATOM   1896  O O   . SER A  1  292 ? 57.307  -20.119 83.404  1.00 35.01  ?  292  SER A O   1 
ATOM   1897  C CB  . SER A  1  292 ? 54.999  -20.952 81.893  1.00 33.22  ?  292  SER A CB  1 
ATOM   1898  O OG  . SER A  1  292 ? 54.440  -19.650 81.904  1.00 32.31  ?  292  SER A OG  1 
ATOM   1899  N N   . LEU A  1  293 ? 58.042  -19.121 81.514  1.00 36.95  ?  293  LEU A N   1 
ATOM   1900  C CA  . LEU A  1  293 ? 58.827  -18.096 82.194  1.00 37.77  ?  293  LEU A CA  1 
ATOM   1901  C C   . LEU A  1  293 ? 58.328  -16.690 81.877  1.00 38.64  ?  293  LEU A C   1 
ATOM   1902  O O   . LEU A  1  293 ? 59.091  -15.726 81.998  1.00 39.63  ?  293  LEU A O   1 
ATOM   1903  C CB  . LEU A  1  293 ? 60.307  -18.226 81.829  1.00 38.65  ?  293  LEU A CB  1 
ATOM   1904  C CG  . LEU A  1  293 ? 60.886  -19.641 81.817  1.00 38.07  ?  293  LEU A CG  1 
ATOM   1905  C CD1 . LEU A  1  293 ? 62.342  -19.623 81.377  1.00 39.53  ?  293  LEU A CD1 1 
ATOM   1906  C CD2 . LEU A  1  293 ? 60.746  -20.284 83.186  1.00 37.15  ?  293  LEU A CD2 1 
ATOM   1907  N N   . HIS A  1  294 ? 57.067  -16.550 81.470  1.00 37.75  ?  294  HIS A N   1 
ATOM   1908  C CA  . HIS A  1  294 ? 56.576  -15.260 81.010  1.00 37.27  ?  294  HIS A CA  1 
ATOM   1909  C C   . HIS A  1  294 ? 56.470  -14.265 82.166  1.00 36.63  ?  294  HIS A C   1 
ATOM   1910  O O   . HIS A  1  294 ? 56.458  -14.633 83.342  1.00 36.16  ?  294  HIS A O   1 
ATOM   1911  C CB  . HIS A  1  294 ? 55.229  -15.415 80.292  1.00 35.99  ?  294  HIS A CB  1 
ATOM   1912  C CG  . HIS A  1  294 ? 54.053  -15.588 81.204  1.00 34.24  ?  294  HIS A CG  1 
ATOM   1913  N ND1 . HIS A  1  294 ? 53.490  -14.542 81.904  1.00 33.26  ?  294  HIS A ND1 1 
ATOM   1914  C CD2 . HIS A  1  294 ? 53.306  -16.679 81.495  1.00 33.38  ?  294  HIS A CD2 1 
ATOM   1915  C CE1 . HIS A  1  294 ? 52.464  -14.987 82.607  1.00 31.89  ?  294  HIS A CE1 1 
ATOM   1916  N NE2 . HIS A  1  294 ? 52.331  -16.280 82.377  1.00 31.92  ?  294  HIS A NE2 1 
ATOM   1917  N N   . THR A  1  295 ? 56.418  -12.981 81.806  1.00 39.30  ?  295  THR A N   1 
ATOM   1918  C CA  . THR A  1  295 ? 56.331  -11.878 82.764  1.00 39.01  ?  295  THR A CA  1 
ATOM   1919  C C   . THR A  1  295 ? 57.502  -11.923 83.751  1.00 39.49  ?  295  THR A C   1 
ATOM   1920  O O   . THR A  1  295 ? 57.332  -12.057 84.964  1.00 38.84  ?  295  THR A O   1 
ATOM   1921  C CB  . THR A  1  295 ? 54.982  -11.883 83.495  1.00 37.65  ?  295  THR A CB  1 
ATOM   1922  O OG1 . THR A  1  295 ? 53.938  -12.204 82.568  1.00 37.44  ?  295  THR A OG1 1 
ATOM   1923  C CG2 . THR A  1  295 ? 54.697  -10.517 84.104  1.00 37.68  ?  295  THR A CG2 1 
ATOM   1924  N N   . ASN A  1  296 ? 58.707  -11.811 83.199  1.00 41.34  ?  296  ASN A N   1 
ATOM   1925  C CA  . ASN A  1  296 ? 59.930  -11.837 83.991  1.00 41.02  ?  296  ASN A CA  1 
ATOM   1926  C C   . ASN A  1  296 ? 60.860  -10.746 83.472  1.00 41.34  ?  296  ASN A C   1 
ATOM   1927  O O   . ASN A  1  296 ? 60.477  -9.918  82.640  1.00 41.33  ?  296  ASN A O   1 
ATOM   1928  C CB  . ASN A  1  296 ? 60.582  -13.225 83.937  1.00 41.53  ?  296  ASN A CB  1 
ATOM   1929  C CG  . ASN A  1  296 ? 60.147  -14.117 85.079  1.00 41.18  ?  296  ASN A CG  1 
ATOM   1930  O OD1 . ASN A  1  296 ? 60.634  -13.985 86.199  1.00 40.94  ?  296  ASN A OD1 1 
ATOM   1931  N ND2 . ASN A  1  296 ? 59.228  -15.036 84.801  1.00 40.52  ?  296  ASN A ND2 1 
ATOM   1932  N N   . LYS A  1  297 ? 62.095  -10.746 83.972  1.00 44.62  ?  297  LYS A N   1 
ATOM   1933  C CA  . LYS A  1  297 ? 63.122  -9.803  83.544  1.00 44.51  ?  297  LYS A CA  1 
ATOM   1934  C C   . LYS A  1  297 ? 64.305  -10.523 82.902  1.00 44.87  ?  297  LYS A C   1 
ATOM   1935  O O   . LYS A  1  297 ? 65.447  -10.068 82.999  1.00 46.11  ?  297  LYS A O   1 
ATOM   1936  C CB  . LYS A  1  297 ? 63.582  -8.938  84.717  1.00 43.87  ?  297  LYS A CB  1 
ATOM   1937  C CG  . LYS A  1  297 ? 62.536  -7.930  85.173  1.00 43.24  ?  297  LYS A CG  1 
ATOM   1938  C CD  . LYS A  1  297 ? 63.017  -7.114  86.361  1.00 43.02  ?  297  LYS A CD  1 
ATOM   1939  C CE  . LYS A  1  297 ? 61.910  -6.212  86.886  1.00 42.21  ?  297  LYS A CE  1 
ATOM   1940  N NZ  . LYS A  1  297 ? 62.238  -5.643  88.222  1.00 42.29  ?  297  LYS A NZ  1 
ATOM   1941  N N   . LEU A  1  298 ? 64.042  -11.656 82.255  1.00 43.33  ?  298  LEU A N   1 
ATOM   1942  C CA  . LEU A  1  298 ? 65.092  -12.413 81.589  1.00 44.52  ?  298  LEU A CA  1 
ATOM   1943  C C   . LEU A  1  298 ? 65.678  -11.619 80.426  1.00 46.07  ?  298  LEU A C   1 
ATOM   1944  O O   . LEU A  1  298 ? 65.003  -10.799 79.798  1.00 45.43  ?  298  LEU A O   1 
ATOM   1945  C CB  . LEU A  1  298 ? 64.544  -13.750 81.089  1.00 43.92  ?  298  LEU A CB  1 
ATOM   1946  C CG  . LEU A  1  298 ? 63.943  -14.673 82.152  1.00 43.72  ?  298  LEU A CG  1 
ATOM   1947  C CD1 . LEU A  1  298 ? 63.780  -16.082 81.614  1.00 43.62  ?  298  LEU A CD1 1 
ATOM   1948  C CD2 . LEU A  1  298 ? 64.813  -14.681 83.395  1.00 43.76  ?  298  LEU A CD2 1 
ATOM   1949  N N   . THR A  1  299 ? 66.954  -11.872 80.141  1.00 47.10  ?  299  THR A N   1 
ATOM   1950  C CA  . THR A  1  299 ? 67.682  -11.205 79.072  1.00 48.93  ?  299  THR A CA  1 
ATOM   1951  C C   . THR A  1  299 ? 68.477  -12.237 78.282  1.00 50.58  ?  299  THR A C   1 
ATOM   1952  O O   . THR A  1  299 ? 68.540  -13.415 78.641  1.00 50.39  ?  299  THR A O   1 
ATOM   1953  C CB  . THR A  1  299 ? 68.615  -10.114 79.621  1.00 50.35  ?  299  THR A CB  1 
ATOM   1954  O OG1 . THR A  1  299 ? 69.416  -10.654 80.679  1.00 51.06  ?  299  THR A OG1 1 
ATOM   1955  C CG2 . THR A  1  299 ? 67.808  -8.937  80.153  1.00 48.97  ?  299  THR A CG2 1 
ATOM   1956  N N   . GLY A  1  300 ? 69.084  -11.785 77.187  1.00 53.08  ?  300  GLY A N   1 
ATOM   1957  C CA  . GLY A  1  300 ? 69.860  -12.655 76.336  1.00 54.90  ?  300  GLY A CA  1 
ATOM   1958  C C   . GLY A  1  300 ? 69.002  -13.416 75.346  1.00 54.08  ?  300  GLY A C   1 
ATOM   1959  O O   . GLY A  1  300 ? 67.776  -13.285 75.325  1.00 52.03  ?  300  GLY A O   1 
ATOM   1960  N N   . PRO A  1  301 ? 69.631  -14.231 74.506  1.00 54.25  ?  301  PRO A N   1 
ATOM   1961  C CA  . PRO A  1  301 ? 68.895  -14.929 73.448  1.00 53.83  ?  301  PRO A CA  1 
ATOM   1962  C C   . PRO A  1  301 ? 68.184  -16.174 73.966  1.00 52.34  ?  301  PRO A C   1 
ATOM   1963  O O   . PRO A  1  301 ? 68.445  -16.670 75.062  1.00 52.00  ?  301  PRO A O   1 
ATOM   1964  C CB  . PRO A  1  301 ? 69.997  -15.303 72.455  1.00 56.56  ?  301  PRO A CB  1 
ATOM   1965  C CG  . PRO A  1  301 ? 71.195  -15.514 73.324  1.00 57.98  ?  301  PRO A CG  1 
ATOM   1966  C CD  . PRO A  1  301 ? 71.075  -14.515 74.454  1.00 56.83  ?  301  PRO A CD  1 
ATOM   1967  N N   . ILE A  1  302 ? 67.263  -16.668 73.142  1.00 54.19  ?  302  ILE A N   1 
ATOM   1968  C CA  . ILE A  1  302 ? 66.638  -17.966 73.424  1.00 53.16  ?  302  ILE A CA  1 
ATOM   1969  C C   . ILE A  1  302 ? 67.708  -19.049 73.337  1.00 55.20  ?  302  ILE A C   1 
ATOM   1970  O O   . ILE A  1  302 ? 68.479  -19.078 72.357  1.00 57.32  ?  302  ILE A O   1 
ATOM   1971  C CB  . ILE A  1  302 ? 65.487  -18.255 72.434  1.00 52.20  ?  302  ILE A CB  1 
ATOM   1972  C CG1 . ILE A  1  302 ? 64.189  -17.508 72.791  1.00 49.73  ?  302  ILE A CG1 1 
ATOM   1973  C CG2 . ILE A  1  302 ? 65.215  -19.753 72.351  1.00 52.21  ?  302  ILE A CG2 1 
ATOM   1974  C CD1 . ILE A  1  302 ? 64.291  -16.005 72.919  1.00 49.52  ?  302  ILE A CD1 1 
ATOM   1975  N N   . PRO A  1  303 ? 67.821  -19.945 74.317  1.00 55.23  ?  303  PRO A N   1 
ATOM   1976  C CA  . PRO A  1  303 ? 68.828  -21.011 74.221  1.00 57.22  ?  303  PRO A CA  1 
ATOM   1977  C C   . PRO A  1  303 ? 68.491  -21.971 73.088  1.00 57.93  ?  303  PRO A C   1 
ATOM   1978  O O   . PRO A  1  303 ? 67.389  -22.521 73.029  1.00 56.37  ?  303  PRO A O   1 
ATOM   1979  C CB  . PRO A  1  303 ? 68.753  -21.700 75.588  1.00 56.14  ?  303  PRO A CB  1 
ATOM   1980  C CG  . PRO A  1  303 ? 67.385  -21.392 76.092  1.00 53.45  ?  303  PRO A CG  1 
ATOM   1981  C CD  . PRO A  1  303 ? 67.030  -20.035 75.556  1.00 52.98  ?  303  PRO A CD  1 
ATOM   1982  N N   . SER A  1  304 ? 69.453  -22.162 72.181  1.00 58.45  ?  304  SER A N   1 
ATOM   1983  C CA  . SER A  1  304 ? 69.253  -23.079 71.064  1.00 59.50  ?  304  SER A CA  1 
ATOM   1984  C C   . SER A  1  304 ? 69.006  -24.506 71.532  1.00 59.19  ?  304  SER A C   1 
ATOM   1985  O O   . SER A  1  304 ? 68.485  -25.319 70.762  1.00 59.46  ?  304  SER A O   1 
ATOM   1986  C CB  . SER A  1  304 ? 70.461  -23.042 70.126  1.00 62.48  ?  304  SER A CB  1 
ATOM   1987  O OG  . SER A  1  304 ? 71.623  -23.541 70.766  1.00 64.06  ?  304  SER A OG  1 
ATOM   1988  N N   . THR A  1  305 ? 69.369  -24.825 72.775  1.00 59.46  ?  305  THR A N   1 
ATOM   1989  C CA  . THR A  1  305 ? 69.174  -26.154 73.338  1.00 59.16  ?  305  THR A CA  1 
ATOM   1990  C C   . THR A  1  305 ? 67.713  -26.481 73.628  1.00 56.68  ?  305  THR A C   1 
ATOM   1991  O O   . THR A  1  305 ? 67.434  -27.592 74.087  1.00 56.33  ?  305  THR A O   1 
ATOM   1992  C CB  . THR A  1  305 ? 69.995  -26.298 74.620  1.00 59.37  ?  305  THR A CB  1 
ATOM   1993  O OG1 . THR A  1  305 ? 69.471  -25.419 75.623  1.00 57.25  ?  305  THR A OG1 1 
ATOM   1994  C CG2 . THR A  1  305 ? 71.452  -25.945 74.360  1.00 61.92  ?  305  THR A CG2 1 
ATOM   1995  N N   . LEU A  1  306 ? 66.776  -25.562 73.382  1.00 57.67  ?  306  LEU A N   1 
ATOM   1996  C CA  . LEU A  1  306 ? 65.367  -25.884 73.574  1.00 55.47  ?  306  LEU A CA  1 
ATOM   1997  C C   . LEU A  1  306 ? 64.876  -26.930 72.582  1.00 56.16  ?  306  LEU A C   1 
ATOM   1998  O O   . LEU A  1  306 ? 63.897  -27.627 72.870  1.00 54.80  ?  306  LEU A O   1 
ATOM   1999  C CB  . LEU A  1  306 ? 64.510  -24.620 73.470  1.00 53.72  ?  306  LEU A CB  1 
ATOM   2000  C CG  . LEU A  1  306 ? 64.676  -23.593 74.592  1.00 52.60  ?  306  LEU A CG  1 
ATOM   2001  C CD1 . LEU A  1  306 ? 63.648  -22.481 74.459  1.00 50.79  ?  306  LEU A CD1 1 
ATOM   2002  C CD2 . LEU A  1  306 ? 64.565  -24.269 75.950  1.00 51.56  ?  306  LEU A CD2 1 
ATOM   2003  N N   . GLY A  1  307 ? 65.530  -27.049 71.425  1.00 56.78  ?  307  GLY A N   1 
ATOM   2004  C CA  . GLY A  1  307 ? 65.129  -28.046 70.447  1.00 57.71  ?  307  GLY A CA  1 
ATOM   2005  C C   . GLY A  1  307 ? 65.228  -29.471 70.955  1.00 58.18  ?  307  GLY A C   1 
ATOM   2006  O O   . GLY A  1  307 ? 64.482  -30.345 70.504  1.00 58.09  ?  307  GLY A O   1 
ATOM   2007  N N   . ASN A  1  308 ? 66.147  -29.730 71.890  1.00 59.77  ?  308  ASN A N   1 
ATOM   2008  C CA  . ASN A  1  308 ? 66.332  -31.092 72.384  1.00 60.38  ?  308  ASN A CA  1 
ATOM   2009  C C   . ASN A  1  308 ? 65.103  -31.612 73.120  1.00 58.12  ?  308  ASN A C   1 
ATOM   2010  O O   . ASN A  1  308 ? 64.883  -32.828 73.163  1.00 58.57  ?  308  ASN A O   1 
ATOM   2011  C CB  . ASN A  1  308 ? 67.559  -31.171 73.294  1.00 61.38  ?  308  ASN A CB  1 
ATOM   2012  C CG  . ASN A  1  308 ? 68.784  -30.520 72.686  1.00 63.55  ?  308  ASN A CG  1 
ATOM   2013  O OD1 . ASN A  1  308 ? 68.850  -29.302 72.537  1.00 63.11  ?  308  ASN A OD1 1 
ATOM   2014  N ND2 . ASN A  1  308 ? 69.770  -31.337 72.338  1.00 66.01  ?  308  ASN A ND2 1 
ATOM   2015  N N   . ILE A  1  309 ? 64.294  -30.729 73.704  1.00 56.70  ?  309  ILE A N   1 
ATOM   2016  C CA  . ILE A  1  309 ? 63.094  -31.175 74.408  1.00 54.59  ?  309  ILE A CA  1 
ATOM   2017  C C   . ILE A  1  309 ? 62.059  -31.516 73.340  1.00 54.41  ?  309  ILE A C   1 
ATOM   2018  O O   . ILE A  1  309 ? 61.393  -30.633 72.796  1.00 53.46  ?  309  ILE A O   1 
ATOM   2019  C CB  . ILE A  1  309 ? 62.571  -30.119 75.384  1.00 52.33  ?  309  ILE A CB  1 
ATOM   2020  C CG1 . ILE A  1  309 ? 63.658  -29.722 76.382  1.00 52.73  ?  309  ILE A CG1 1 
ATOM   2021  C CG2 . ILE A  1  309 ? 61.362  -30.655 76.134  1.00 50.35  ?  309  ILE A CG2 1 
ATOM   2022  C CD1 . ILE A  1  309 ? 63.978  -28.240 76.367  1.00 52.42  ?  309  ILE A CD1 1 
ATOM   2023  N N   . LYS A  1  310 ? 61.918  -32.805 73.038  1.00 52.57  ?  310  LYS A N   1 
ATOM   2024  C CA  . LYS A  1  310 ? 60.957  -33.249 72.037  1.00 52.62  ?  310  LYS A CA  1 
ATOM   2025  C C   . LYS A  1  310 ? 59.552  -33.411 72.598  1.00 50.34  ?  310  LYS A C   1 
ATOM   2026  O O   . LYS A  1  310 ? 58.616  -33.632 71.823  1.00 50.11  ?  310  LYS A O   1 
ATOM   2027  C CB  . LYS A  1  310 ? 61.424  -34.566 71.410  1.00 54.92  ?  310  LYS A CB  1 
ATOM   2028  C CG  . LYS A  1  310 ? 62.847  -34.527 70.861  1.00 57.43  ?  310  LYS A CG  1 
ATOM   2029  C CD  . LYS A  1  310 ? 63.126  -33.233 70.103  1.00 57.66  ?  310  LYS A CD  1 
ATOM   2030  C CE  . LYS A  1  310 ? 64.279  -33.395 69.126  1.00 60.55  ?  310  LYS A CE  1 
ATOM   2031  N NZ  . LYS A  1  310 ? 64.334  -32.279 68.141  1.00 60.91  ?  310  LYS A NZ  1 
ATOM   2032  N N   . THR A  1  311 ? 59.386  -33.325 73.918  1.00 49.68  ?  311  THR A N   1 
ATOM   2033  C CA  . THR A  1  311 ? 58.080  -33.424 74.552  1.00 47.54  ?  311  THR A CA  1 
ATOM   2034  C C   . THR A  1  311 ? 57.437  -32.070 74.824  1.00 45.55  ?  311  THR A C   1 
ATOM   2035  O O   . THR A  1  311 ? 56.272  -32.030 75.237  1.00 43.79  ?  311  THR A O   1 
ATOM   2036  C CB  . THR A  1  311 ? 58.190  -34.200 75.872  1.00 47.03  ?  311  THR A CB  1 
ATOM   2037  O OG1 . THR A  1  311 ? 59.425  -33.873 76.521  1.00 47.71  ?  311  THR A OG1 1 
ATOM   2038  C CG2 . THR A  1  311 ? 58.143  -35.698 75.613  1.00 48.36  ?  311  THR A CG2 1 
ATOM   2039  N N   . LEU A  1  312 ? 58.153  -30.969 74.603  1.00 47.04  ?  312  LEU A N   1 
ATOM   2040  C CA  . LEU A  1  312 ? 57.637  -29.652 74.956  1.00 45.27  ?  312  LEU A CA  1 
ATOM   2041  C C   . LEU A  1  312 ? 56.475  -29.282 74.044  1.00 44.44  ?  312  LEU A C   1 
ATOM   2042  O O   . LEU A  1  312 ? 56.649  -29.142 72.829  1.00 45.64  ?  312  LEU A O   1 
ATOM   2043  C CB  . LEU A  1  312 ? 58.743  -28.604 74.860  1.00 46.11  ?  312  LEU A CB  1 
ATOM   2044  C CG  . LEU A  1  312 ? 58.444  -27.254 75.518  1.00 44.45  ?  312  LEU A CG  1 
ATOM   2045  C CD1 . LEU A  1  312 ? 58.180  -27.433 77.006  1.00 43.04  ?  312  LEU A CD1 1 
ATOM   2046  C CD2 . LEU A  1  312 ? 59.578  -26.267 75.284  1.00 45.60  ?  312  LEU A CD2 1 
ATOM   2047  N N   . ALA A  1  313 ? 55.289  -29.119 74.633  1.00 41.97  ?  313  ALA A N   1 
ATOM   2048  C CA  . ALA A  1  313 ? 54.103  -28.725 73.891  1.00 41.02  ?  313  ALA A CA  1 
ATOM   2049  C C   . ALA A  1  313 ? 53.667  -27.290 74.147  1.00 39.47  ?  313  ALA A C   1 
ATOM   2050  O O   . ALA A  1  313 ? 52.939  -26.730 73.322  1.00 39.02  ?  313  ALA A O   1 
ATOM   2051  C CB  . ALA A  1  313 ? 52.932  -29.664 74.218  1.00 40.06  ?  313  ALA A CB  1 
ATOM   2052  N N   . VAL A  1  314 ? 54.078  -26.689 75.262  1.00 38.90  ?  314  VAL A N   1 
ATOM   2053  C CA  . VAL A  1  314 ? 53.718  -25.317 75.603  1.00 37.55  ?  314  VAL A CA  1 
ATOM   2054  C C   . VAL A  1  314 ? 54.976  -24.581 76.044  1.00 38.31  ?  314  VAL A C   1 
ATOM   2055  O O   . VAL A  1  314 ? 55.614  -24.972 77.029  1.00 38.51  ?  314  VAL A O   1 
ATOM   2056  C CB  . VAL A  1  314 ? 52.645  -25.256 76.704  1.00 35.56  ?  314  VAL A CB  1 
ATOM   2057  C CG1 . VAL A  1  314 ? 52.354  -23.814 77.077  1.00 34.36  ?  314  VAL A CG1 1 
ATOM   2058  C CG2 . VAL A  1  314 ? 51.371  -25.954 76.249  1.00 34.90  ?  314  VAL A CG2 1 
ATOM   2059  N N   . LEU A  1  315 ? 55.329  -23.520 75.320  1.00 36.85  ?  315  LEU A N   1 
ATOM   2060  C CA  . LEU A  1  315 ? 56.447  -22.650 75.665  1.00 37.59  ?  315  LEU A CA  1 
ATOM   2061  C C   . LEU A  1  315 ? 55.941  -21.217 75.745  1.00 38.21  ?  315  LEU A C   1 
ATOM   2062  O O   . LEU A  1  315 ? 55.511  -20.651 74.734  1.00 39.52  ?  315  LEU A O   1 
ATOM   2063  C CB  . LEU A  1  315 ? 57.576  -22.765 74.640  1.00 39.79  ?  315  LEU A CB  1 
ATOM   2064  C CG  . LEU A  1  315 ? 58.870  -22.017 74.969  1.00 40.93  ?  315  LEU A CG  1 
ATOM   2065  C CD1 . LEU A  1  315 ? 59.496  -22.568 76.239  1.00 41.00  ?  315  LEU A CD1 1 
ATOM   2066  C CD2 . LEU A  1  315 ? 59.849  -22.093 73.807  1.00 43.16  ?  315  LEU A CD2 1 
ATOM   2067  N N   . HIS A  1  316 ? 55.992  -20.633 76.940  1.00 37.71  ?  316  HIS A N   1 
ATOM   2068  C CA  . HIS A  1  316 ? 55.550  -19.257 77.168  1.00 36.66  ?  316  HIS A CA  1 
ATOM   2069  C C   . HIS A  1  316 ? 56.736  -18.438 77.668  1.00 37.62  ?  316  HIS A C   1 
ATOM   2070  O O   . HIS A  1  316 ? 57.049  -18.445 78.863  1.00 37.31  ?  316  HIS A O   1 
ATOM   2071  C CB  . HIS A  1  316 ? 54.381  -19.209 78.150  1.00 34.70  ?  316  HIS A CB  1 
ATOM   2072  C CG  . HIS A  1  316 ? 53.115  -19.795 77.608  1.00 33.73  ?  316  HIS A CG  1 
ATOM   2073  N ND1 . HIS A  1  316 ? 51.964  -19.905 78.357  1.00 32.09  ?  316  HIS A ND1 1 
ATOM   2074  C CD2 . HIS A  1  316 ? 52.821  -20.305 76.389  1.00 34.30  ?  316  HIS A CD2 1 
ATOM   2075  C CE1 . HIS A  1  316 ? 51.014  -20.455 77.621  1.00 31.67  ?  316  HIS A CE1 1 
ATOM   2076  N NE2 . HIS A  1  316 ? 51.508  -20.707 76.423  1.00 32.99  ?  316  HIS A NE2 1 
ATOM   2077  N N   . LEU A  1  317 ? 57.388  -17.731 76.746  1.00 37.62  ?  317  LEU A N   1 
ATOM   2078  C CA  . LEU A  1  317 ? 58.531  -16.881 77.051  1.00 38.27  ?  317  LEU A CA  1 
ATOM   2079  C C   . LEU A  1  317 ? 58.201  -15.398 76.936  1.00 38.69  ?  317  LEU A C   1 
ATOM   2080  O O   . LEU A  1  317 ? 59.110  -14.563 77.007  1.00 39.28  ?  317  LEU A O   1 
ATOM   2081  C CB  . LEU A  1  317 ? 59.703  -17.227 76.128  1.00 40.42  ?  317  LEU A CB  1 
ATOM   2082  C CG  . LEU A  1  317 ? 60.367  -18.597 76.288  1.00 41.47  ?  317  LEU A CG  1 
ATOM   2083  C CD1 . LEU A  1  317 ? 61.792  -18.560 75.755  1.00 43.82  ?  317  LEU A CD1 1 
ATOM   2084  C CD2 . LEU A  1  317 ? 60.345  -19.054 77.737  1.00 40.59  ?  317  LEU A CD2 1 
ATOM   2085  N N   . TYR A  1  318 ? 56.928  -15.048 76.769  1.00 39.33  ?  318  TYR A N   1 
ATOM   2086  C CA  . TYR A  1  318 ? 56.555  -13.682 76.438  1.00 39.82  ?  318  TYR A CA  1 
ATOM   2087  C C   . TYR A  1  318 ? 56.729  -12.758 77.644  1.00 39.59  ?  318  TYR A C   1 
ATOM   2088  O O   . TYR A  1  318 ? 56.967  -13.194 78.772  1.00 39.07  ?  318  TYR A O   1 
ATOM   2089  C CB  . TYR A  1  318 ? 55.118  -13.629 75.915  1.00 39.49  ?  318  TYR A CB  1 
ATOM   2090  C CG  . TYR A  1  318 ? 54.050  -14.022 76.915  1.00 38.29  ?  318  TYR A CG  1 
ATOM   2091  C CD1 . TYR A  1  318 ? 53.536  -13.097 77.816  1.00 37.71  ?  318  TYR A CD1 1 
ATOM   2092  C CD2 . TYR A  1  318 ? 53.549  -15.316 76.948  1.00 37.34  ?  318  TYR A CD2 1 
ATOM   2093  C CE1 . TYR A  1  318 ? 52.559  -13.452 78.726  1.00 36.03  ?  318  TYR A CE1 1 
ATOM   2094  C CE2 . TYR A  1  318 ? 52.571  -15.680 77.855  1.00 35.67  ?  318  TYR A CE2 1 
ATOM   2095  C CZ  . TYR A  1  318 ? 52.080  -14.745 78.740  1.00 35.14  ?  318  TYR A CZ  1 
ATOM   2096  O OH  . TYR A  1  318 ? 51.107  -15.102 79.645  1.00 33.19  ?  318  TYR A OH  1 
ATOM   2097  N N   . LEU A  1  319 ? 56.622  -11.454 77.379  1.00 39.62  ?  319  LEU A N   1 
ATOM   2098  C CA  . LEU A  1  319 ? 56.728  -10.412 78.401  1.00 39.32  ?  319  LEU A CA  1 
ATOM   2099  C C   . LEU A  1  319 ? 58.067  -10.495 79.138  1.00 40.72  ?  319  LEU A C   1 
ATOM   2100  O O   . LEU A  1  319 ? 58.137  -10.702 80.351  1.00 40.28  ?  319  LEU A O   1 
ATOM   2101  C CB  . LEU A  1  319 ? 55.550  -10.484 79.379  1.00 37.40  ?  319  LEU A CB  1 
ATOM   2102  C CG  . LEU A  1  319 ? 54.408  -9.505  79.107  1.00 36.20  ?  319  LEU A CG  1 
ATOM   2103  C CD1 . LEU A  1  319 ? 53.395  -9.531  80.240  1.00 34.57  ?  319  LEU A CD1 1 
ATOM   2104  C CD2 . LEU A  1  319 ? 54.946  -8.099  78.894  1.00 37.10  ?  319  LEU A CD2 1 
ATOM   2105  N N   . ASN A  1  320 ? 59.138  -10.322 78.370  1.00 42.73  ?  320  ASN A N   1 
ATOM   2106  C CA  . ASN A  1  320 ? 60.497  -10.402 78.887  1.00 42.09  ?  320  ASN A CA  1 
ATOM   2107  C C   . ASN A  1  320 ? 61.374  -9.453  78.076  1.00 42.13  ?  320  ASN A C   1 
ATOM   2108  O O   . ASN A  1  320 ? 60.875  -8.600  77.336  1.00 41.65  ?  320  ASN A O   1 
ATOM   2109  C CB  . ASN A  1  320 ? 61.011  -11.845 78.838  1.00 42.66  ?  320  ASN A CB  1 
ATOM   2110  C CG  . ASN A  1  320 ? 60.825  -12.577 80.149  1.00 42.54  ?  320  ASN A CG  1 
ATOM   2111  O OD1 . ASN A  1  320 ? 61.615  -12.412 81.077  1.00 42.50  ?  320  ASN A OD1 1 
ATOM   2112  N ND2 . ASN A  1  320 ? 59.785  -13.398 80.230  1.00 42.42  ?  320  ASN A ND2 1 
ATOM   2113  N N   . GLN A  1  321 ? 62.688  -9.598  78.223  1.00 45.74  ?  321  GLN A N   1 
ATOM   2114  C CA  . GLN A  1  321 ? 63.654  -8.747  77.539  1.00 46.62  ?  321  GLN A CA  1 
ATOM   2115  C C   . GLN A  1  321 ? 64.672  -9.578  76.774  1.00 48.50  ?  321  GLN A C   1 
ATOM   2116  O O   . GLN A  1  321 ? 65.849  -9.216  76.685  1.00 50.47  ?  321  GLN A O   1 
ATOM   2117  C CB  . GLN A  1  321 ? 64.367  -7.819  78.519  1.00 47.40  ?  321  GLN A CB  1 
ATOM   2118  C CG  . GLN A  1  321 ? 63.464  -7.120  79.518  1.00 45.72  ?  321  GLN A CG  1 
ATOM   2119  C CD  . GLN A  1  321 ? 64.236  -6.190  80.433  1.00 46.77  ?  321  GLN A CD  1 
ATOM   2120  O OE1 . GLN A  1  321 ? 64.929  -5.284  79.972  1.00 48.64  ?  321  GLN A OE1 1 
ATOM   2121  N NE2 . GLN A  1  321 ? 64.124  -6.415  81.736  1.00 46.04  ?  321  GLN A NE2 1 
ATOM   2122  N N   . LEU A  1  322 ? 64.251  -10.708 76.210  1.00 46.76  ?  322  LEU A N   1 
ATOM   2123  C CA  . LEU A  1  322 ? 65.178  -11.497 75.412  1.00 48.66  ?  322  LEU A CA  1 
ATOM   2124  C C   . LEU A  1  322 ? 65.451  -10.808 74.081  1.00 49.99  ?  322  LEU A C   1 
ATOM   2125  O O   . LEU A  1  322 ? 64.548  -10.250 73.451  1.00 48.99  ?  322  LEU A O   1 
ATOM   2126  C CB  . LEU A  1  322 ? 64.651  -12.913 75.174  1.00 47.96  ?  322  LEU A CB  1 
ATOM   2127  C CG  . LEU A  1  322 ? 64.266  -13.749 76.399  1.00 46.59  ?  322  LEU A CG  1 
ATOM   2128  C CD1 . LEU A  1  322 ? 62.765  -13.779 76.599  1.00 45.73  ?  322  LEU A CD1 1 
ATOM   2129  C CD2 . LEU A  1  322 ? 64.833  -15.155 76.316  1.00 47.58  ?  322  LEU A CD2 1 
ATOM   2130  N N   . ASN A  1  323 ? 66.710  -10.843 73.664  1.00 50.96  ?  323  ASN A N   1 
ATOM   2131  C CA  . ASN A  1  323 ? 67.182  -10.189 72.453  1.00 52.64  ?  323  ASN A CA  1 
ATOM   2132  C C   . ASN A  1  323 ? 67.749  -11.233 71.488  1.00 54.28  ?  323  ASN A C   1 
ATOM   2133  O O   . ASN A  1  323 ? 67.668  -12.442 71.726  1.00 53.98  ?  323  ASN A O   1 
ATOM   2134  C CB  . ASN A  1  323 ? 68.201  -9.100  72.806  1.00 54.21  ?  323  ASN A CB  1 
ATOM   2135  C CG  . ASN A  1  323 ? 69.461  -9.651  73.466  1.00 55.89  ?  323  ASN A CG  1 
ATOM   2136  O OD1 . ASN A  1  323 ? 70.044  -10.637 73.016  1.00 57.16  ?  323  ASN A OD1 1 
ATOM   2137  N ND2 . ASN A  1  323 ? 69.882  -9.006  74.547  1.00 55.97  ?  323  ASN A ND2 1 
ATOM   2138  N N   . GLY A  1  324 ? 68.318  -10.754 70.387  1.00 54.68  ?  324  GLY A N   1 
ATOM   2139  C CA  . GLY A  1  324 ? 68.927  -11.635 69.417  1.00 56.55  ?  324  GLY A CA  1 
ATOM   2140  C C   . GLY A  1  324 ? 67.911  -12.263 68.482  1.00 55.61  ?  324  GLY A C   1 
ATOM   2141  O O   . GLY A  1  324 ? 66.735  -11.892 68.432  1.00 53.60  ?  324  GLY A O   1 
ATOM   2142  N N   . SER A  1  325 ? 68.389  -13.247 67.732  1.00 57.80  ?  325  SER A N   1 
ATOM   2143  C CA  . SER A  1  325 ? 67.588  -13.914 66.719  1.00 57.44  ?  325  SER A CA  1 
ATOM   2144  C C   . SER A  1  325 ? 66.987  -15.203 67.267  1.00 56.12  ?  325  SER A C   1 
ATOM   2145  O O   . SER A  1  325 ? 67.465  -15.775 68.250  1.00 56.12  ?  325  SER A O   1 
ATOM   2146  C CB  . SER A  1  325 ? 68.434  -14.218 65.480  1.00 60.18  ?  325  SER A CB  1 
ATOM   2147  O OG  . SER A  1  325 ? 69.284  -13.129 65.165  1.00 61.83  ?  325  SER A OG  1 
ATOM   2148  N N   . ILE A  1  326 ? 65.920  -15.650 66.614  1.00 58.62  ?  326  ILE A N   1 
ATOM   2149  C CA  . ILE A  1  326 ? 65.267  -16.909 66.962  1.00 57.52  ?  326  ILE A CA  1 
ATOM   2150  C C   . ILE A  1  326 ? 66.154  -18.059 66.501  1.00 59.76  ?  326  ILE A C   1 
ATOM   2151  O O   . ILE A  1  326 ? 66.502  -18.135 65.314  1.00 61.58  ?  326  ILE A O   1 
ATOM   2152  C CB  . ILE A  1  326 ? 63.863  -17.005 66.345  1.00 55.89  ?  326  ILE A CB  1 
ATOM   2153  C CG1 . ILE A  1  326 ? 62.993  -15.835 66.809  1.00 53.76  ?  326  ILE A CG1 1 
ATOM   2154  C CG2 . ILE A  1  326 ? 63.215  -18.335 66.697  1.00 54.94  ?  326  ILE A CG2 1 
ATOM   2155  C CD1 . ILE A  1  326 ? 61.730  -15.651 65.997  1.00 52.60  ?  326  ILE A CD1 1 
ATOM   2156  N N   . PRO A  1  327 ? 66.552  -18.958 67.396  1.00 57.57  ?  327  PRO A N   1 
ATOM   2157  C CA  . PRO A  1  327 ? 67.395  -20.087 66.997  1.00 59.75  ?  327  PRO A CA  1 
ATOM   2158  C C   . PRO A  1  327 ? 66.673  -20.981 66.007  1.00 59.93  ?  327  PRO A C   1 
ATOM   2159  O O   . PRO A  1  327 ? 65.521  -21.378 66.239  1.00 57.96  ?  327  PRO A O   1 
ATOM   2160  C CB  . PRO A  1  327 ? 67.656  -20.821 68.322  1.00 59.10  ?  327  PRO A CB  1 
ATOM   2161  C CG  . PRO A  1  327 ? 67.404  -19.805 69.382  1.00 57.30  ?  327  PRO A CG  1 
ATOM   2162  C CD  . PRO A  1  327 ? 66.318  -18.924 68.848  1.00 55.76  ?  327  PRO A CD  1 
ATOM   2163  N N   . PRO A  1  328 ? 67.313  -21.309 64.882  1.00 60.94  ?  328  PRO A N   1 
ATOM   2164  C CA  . PRO A  1  328 ? 66.692  -22.245 63.930  1.00 61.40  ?  328  PRO A CA  1 
ATOM   2165  C C   . PRO A  1  328 ? 66.393  -23.605 64.531  1.00 60.88  ?  328  PRO A C   1 
ATOM   2166  O O   . PRO A  1  328 ? 65.579  -24.349 63.970  1.00 60.60  ?  328  PRO A O   1 
ATOM   2167  C CB  . PRO A  1  328 ? 67.734  -22.346 62.807  1.00 64.52  ?  328  PRO A CB  1 
ATOM   2168  C CG  . PRO A  1  328 ? 68.523  -21.080 62.909  1.00 65.18  ?  328  PRO A CG  1 
ATOM   2169  C CD  . PRO A  1  328 ? 68.578  -20.754 64.372  1.00 63.44  ?  328  PRO A CD  1 
ATOM   2170  N N   . GLU A  1  329 ? 67.027  -23.955 65.650  1.00 62.87  ?  329  GLU A N   1 
ATOM   2171  C CA  . GLU A  1  329 ? 66.779  -25.230 66.310  1.00 62.38  ?  329  GLU A CA  1 
ATOM   2172  C C   . GLU A  1  329 ? 65.409  -25.298 66.973  1.00 59.48  ?  329  GLU A C   1 
ATOM   2173  O O   . GLU A  1  329 ? 64.987  -26.392 67.360  1.00 59.00  ?  329  GLU A O   1 
ATOM   2174  C CB  . GLU A  1  329 ? 67.874  -25.497 67.345  1.00 63.16  ?  329  GLU A CB  1 
ATOM   2175  C CG  . GLU A  1  329 ? 69.280  -25.549 66.761  1.00 66.21  ?  329  GLU A CG  1 
ATOM   2176  C CD  . GLU A  1  329 ? 69.943  -24.184 66.690  1.00 66.75  ?  329  GLU A CD  1 
ATOM   2177  O OE1 . GLU A  1  329 ? 69.221  -23.169 66.590  1.00 65.14  ?  329  GLU A OE1 1 
ATOM   2178  O OE2 . GLU A  1  329 ? 71.190  -24.127 66.727  1.00 68.88  -1 329  GLU A OE2 1 
ATOM   2179  N N   . LEU A  1  330 ? 64.713  -24.167 67.124  1.00 60.67  ?  330  LEU A N   1 
ATOM   2180  C CA  . LEU A  1  330 ? 63.349  -24.203 67.640  1.00 58.05  ?  330  LEU A CA  1 
ATOM   2181  C C   . LEU A  1  330 ? 62.393  -24.919 66.695  1.00 57.99  ?  330  LEU A C   1 
ATOM   2182  O O   . LEU A  1  330 ? 61.327  -25.362 67.132  1.00 56.22  ?  330  LEU A O   1 
ATOM   2183  C CB  . LEU A  1  330 ? 62.840  -22.788 67.919  1.00 56.32  ?  330  LEU A CB  1 
ATOM   2184  C CG  . LEU A  1  330 ? 63.617  -21.948 68.936  1.00 56.33  ?  330  LEU A CG  1 
ATOM   2185  C CD1 . LEU A  1  330 ? 62.777  -20.771 69.406  1.00 53.94  ?  330  LEU A CD1 1 
ATOM   2186  C CD2 . LEU A  1  330 ? 64.065  -22.796 70.118  1.00 56.01  ?  330  LEU A CD2 1 
ATOM   2187  N N   . GLY A  1  331 ? 62.741  -25.030 65.412  1.00 57.93  ?  331  GLY A N   1 
ATOM   2188  C CA  . GLY A  1  331 ? 61.938  -25.820 64.496  1.00 58.24  ?  331  GLY A CA  1 
ATOM   2189  C C   . GLY A  1  331 ? 61.926  -27.299 64.815  1.00 58.79  ?  331  GLY A C   1 
ATOM   2190  O O   . GLY A  1  331 ? 61.052  -28.022 64.324  1.00 58.59  ?  331  GLY A O   1 
ATOM   2191  N N   . GLU A  1  332 ? 62.874  -27.764 65.625  1.00 59.77  ?  332  GLU A N   1 
ATOM   2192  C CA  . GLU A  1  332 ? 63.000  -29.173 65.971  1.00 60.51  ?  332  GLU A CA  1 
ATOM   2193  C C   . GLU A  1  332 ? 62.190  -29.562 67.201  1.00 58.19  ?  332  GLU A C   1 
ATOM   2194  O O   . GLU A  1  332 ? 62.207  -30.734 67.589  1.00 58.60  ?  332  GLU A O   1 
ATOM   2195  C CB  . GLU A  1  332 ? 64.475  -29.526 66.183  1.00 62.72  ?  332  GLU A CB  1 
ATOM   2196  C CG  . GLU A  1  332 ? 65.408  -28.812 65.222  1.00 64.82  ?  332  GLU A CG  1 
ATOM   2197  C CD  . GLU A  1  332 ? 65.378  -29.413 63.832  1.00 66.90  ?  332  GLU A CD  1 
ATOM   2198  O OE1 . GLU A  1  332 ? 64.986  -30.591 63.701  1.00 67.33  ?  332  GLU A OE1 1 
ATOM   2199  O OE2 . GLU A  1  332 ? 65.739  -28.704 62.869  1.00 68.19  -1 332  GLU A OE2 1 
ATOM   2200  N N   . MET A  1  333 ? 61.489  -28.617 67.822  1.00 59.15  ?  333  MET A N   1 
ATOM   2201  C CA  . MET A  1  333 ? 60.617  -28.911 68.959  1.00 56.87  ?  333  MET A CA  1 
ATOM   2202  C C   . MET A  1  333 ? 59.347  -29.545 68.402  1.00 56.13  ?  333  MET A C   1 
ATOM   2203  O O   . MET A  1  333 ? 58.354  -28.872 68.120  1.00 54.64  ?  333  MET A O   1 
ATOM   2204  C CB  . MET A  1  333 ? 60.340  -27.646 69.761  1.00 54.75  ?  333  MET A CB  1 
ATOM   2205  C CG  . MET A  1  333 ? 61.571  -26.750 69.892  1.00 56.08  ?  333  MET A CG  1 
ATOM   2206  S SD  . MET A  1  333 ? 61.305  -25.168 70.716  1.00 53.94  ?  333  MET A SD  1 
ATOM   2207  C CE  . MET A  1  333 ? 59.848  -25.529 71.679  1.00 51.07  ?  333  MET A CE  1 
ATOM   2208  N N   . GLU A  1  334 ? 59.397  -30.872 68.239  1.00 54.61  ?  334  GLU A N   1 
ATOM   2209  C CA  . GLU A  1  334 ? 58.385  -31.585 67.463  1.00 54.69  ?  334  GLU A CA  1 
ATOM   2210  C C   . GLU A  1  334 ? 56.997  -31.468 68.085  1.00 52.15  ?  334  GLU A C   1 
ATOM   2211  O O   . GLU A  1  334 ? 56.007  -31.261 67.374  1.00 51.54  ?  334  GLU A O   1 
ATOM   2212  C CB  . GLU A  1  334 ? 58.782  -33.054 67.321  1.00 56.54  ?  334  GLU A CB  1 
ATOM   2213  C CG  . GLU A  1  334 ? 60.045  -33.286 66.507  1.00 59.36  ?  334  GLU A CG  1 
ATOM   2214  C CD  . GLU A  1  334 ? 60.781  -34.545 66.924  1.00 60.94  ?  334  GLU A CD  1 
ATOM   2215  O OE1 . GLU A  1  334 ? 60.956  -34.758 68.142  1.00 59.92  ?  334  GLU A OE1 1 
ATOM   2216  O OE2 . GLU A  1  334 ? 61.189  -35.318 66.033  1.00 63.51  -1 334  GLU A OE2 1 
ATOM   2217  N N   . SER A  1  335 ? 56.902  -31.601 69.406  1.00 49.22  ?  335  SER A N   1 
ATOM   2218  C CA  . SER A  1  335 ? 55.613  -31.655 70.083  1.00 47.01  ?  335  SER A CA  1 
ATOM   2219  C C   . SER A  1  335 ? 54.993  -30.283 70.304  1.00 45.04  ?  335  SER A C   1 
ATOM   2220  O O   . SER A  1  335 ? 53.910  -30.203 70.895  1.00 43.17  ?  335  SER A O   1 
ATOM   2221  C CB  . SER A  1  335 ? 55.756  -32.366 71.432  1.00 46.36  ?  335  SER A CB  1 
ATOM   2222  O OG  . SER A  1  335 ? 56.094  -33.731 71.258  1.00 48.00  ?  335  SER A OG  1 
ATOM   2223  N N   . MET A  1  336 ? 55.645  -29.215 69.850  1.00 47.11  ?  336  MET A N   1 
ATOM   2224  C CA  . MET A  1  336 ? 55.218  -27.866 70.197  1.00 45.38  ?  336  MET A CA  1 
ATOM   2225  C C   . MET A  1  336 ? 53.819  -27.569 69.667  1.00 44.05  ?  336  MET A C   1 
ATOM   2226  O O   . MET A  1  336 ? 53.515  -27.802 68.493  1.00 44.99  ?  336  MET A O   1 
ATOM   2227  C CB  . MET A  1  336 ? 56.228  -26.851 69.657  1.00 46.48  ?  336  MET A CB  1 
ATOM   2228  C CG  . MET A  1  336 ? 55.922  -25.402 69.999  1.00 45.07  ?  336  MET A CG  1 
ATOM   2229  S SD  . MET A  1  336 ? 55.177  -25.193 71.627  1.00 42.70  ?  336  MET A SD  1 
ATOM   2230  C CE  . MET A  1  336 ? 56.535  -25.601 72.717  1.00 43.38  ?  336  MET A CE  1 
ATOM   2231  N N   . ILE A  1  337 ? 52.968  -27.050 70.555  1.00 43.05  ?  337  ILE A N   1 
ATOM   2232  C CA  . ILE A  1  337 ? 51.606  -26.660 70.222  1.00 41.76  ?  337  ILE A CA  1 
ATOM   2233  C C   . ILE A  1  337 ? 51.386  -25.166 70.422  1.00 40.88  ?  337  ILE A C   1 
ATOM   2234  O O   . ILE A  1  337 ? 50.766  -24.505 69.580  1.00 40.73  ?  337  ILE A O   1 
ATOM   2235  C CB  . ILE A  1  337 ? 50.581  -27.471 71.048  1.00 40.22  ?  337  ILE A CB  1 
ATOM   2236  C CG1 . ILE A  1  337 ? 50.529  -28.922 70.570  1.00 41.45  ?  337  ILE A CG1 1 
ATOM   2237  C CG2 . ILE A  1  337 ? 49.198  -26.840 70.969  1.00 38.62  ?  337  ILE A CG2 1 
ATOM   2238  C CD1 . ILE A  1  337 ? 49.707  -29.827 71.466  1.00 40.45  ?  337  ILE A CD1 1 
ATOM   2239  N N   . ASP A  1  338 ? 51.897  -24.614 71.520  1.00 39.15  ?  338  ASP A N   1 
ATOM   2240  C CA  . ASP A  1  338 ? 51.669  -23.228 71.918  1.00 37.87  ?  338  ASP A CA  1 
ATOM   2241  C C   . ASP A  1  338 ? 53.031  -22.562 72.096  1.00 38.93  ?  338  ASP A C   1 
ATOM   2242  O O   . ASP A  1  338 ? 53.697  -22.757 73.118  1.00 38.97  ?  338  ASP A O   1 
ATOM   2243  C CB  . ASP A  1  338 ? 50.840  -23.167 73.199  1.00 35.96  ?  338  ASP A CB  1 
ATOM   2244  C CG  . ASP A  1  338 ? 50.504  -21.750 73.612  1.00 34.68  ?  338  ASP A CG  1 
ATOM   2245  O OD1 . ASP A  1  338 ? 50.606  -20.841 72.764  1.00 35.03  ?  338  ASP A OD1 1 
ATOM   2246  O OD2 . ASP A  1  338 ? 50.134  -21.546 74.787  1.00 33.40  -1 338  ASP A OD2 1 
ATOM   2247  N N   . LEU A  1  339 ? 53.442  -21.782 71.099  1.00 37.16  ?  339  LEU A N   1 
ATOM   2248  C CA  . LEU A  1  339 ? 54.741  -21.115 71.080  1.00 38.86  ?  339  LEU A CA  1 
ATOM   2249  C C   . LEU A  1  339 ? 54.512  -19.611 71.182  1.00 39.93  ?  339  LEU A C   1 
ATOM   2250  O O   . LEU A  1  339 ? 53.948  -19.000 70.266  1.00 40.98  ?  339  LEU A O   1 
ATOM   2251  C CB  . LEU A  1  339 ? 55.513  -21.472 69.812  1.00 40.07  ?  339  LEU A CB  1 
ATOM   2252  C CG  . LEU A  1  339 ? 56.920  -20.889 69.677  1.00 41.73  ?  339  LEU A CG  1 
ATOM   2253  C CD1 . LEU A  1  339 ? 57.739  -21.175 70.924  1.00 41.84  ?  339  LEU A CD1 1 
ATOM   2254  C CD2 . LEU A  1  339 ? 57.611  -21.442 68.440  1.00 43.98  ?  339  LEU A CD2 1 
ATOM   2255  N N   . GLU A  1  340 ? 54.946  -19.014 72.293  1.00 39.13  ?  340  GLU A N   1 
ATOM   2256  C CA  . GLU A  1  340 ? 54.688  -17.604 72.580  1.00 39.32  ?  340  GLU A CA  1 
ATOM   2257  C C   . GLU A  1  340 ? 55.980  -16.931 73.020  1.00 40.18  ?  340  GLU A C   1 
ATOM   2258  O O   . GLU A  1  340 ? 56.489  -17.206 74.112  1.00 39.80  ?  340  GLU A O   1 
ATOM   2259  C CB  . GLU A  1  340 ? 53.611  -17.452 73.655  1.00 37.78  ?  340  GLU A CB  1 
ATOM   2260  C CG  . GLU A  1  340 ? 52.494  -18.466 73.551  1.00 36.09  ?  340  GLU A CG  1 
ATOM   2261  C CD  . GLU A  1  340 ? 51.217  -17.994 74.204  1.00 34.39  ?  340  GLU A CD  1 
ATOM   2262  O OE1 . GLU A  1  340 ? 51.230  -17.733 75.425  1.00 33.57  ?  340  GLU A OE1 1 
ATOM   2263  O OE2 . GLU A  1  340 ? 50.201  -17.874 73.491  1.00 33.76  -1 340  GLU A OE2 1 
ATOM   2264  N N   . ILE A  1  341 ? 56.504  -16.047 72.170  1.00 42.72  ?  341  ILE A N   1 
ATOM   2265  C CA  . ILE A  1  341 ? 57.721  -15.296 72.463  1.00 42.98  ?  341  ILE A CA  1 
ATOM   2266  C C   . ILE A  1  341 ? 57.429  -13.807 72.299  1.00 43.55  ?  341  ILE A C   1 
ATOM   2267  O O   . ILE A  1  341 ? 58.325  -13.016 71.983  1.00 43.62  ?  341  ILE A O   1 
ATOM   2268  C CB  . ILE A  1  341 ? 58.883  -15.749 71.558  1.00 43.45  ?  341  ILE A CB  1 
ATOM   2269  C CG1 . ILE A  1  341 ? 58.859  -17.267 71.379  1.00 43.17  ?  341  ILE A CG1 1 
ATOM   2270  C CG2 . ILE A  1  341 ? 60.221  -15.374 72.174  1.00 43.95  ?  341  ILE A CG2 1 
ATOM   2271  C CD1 . ILE A  1  341 ? 59.710  -17.763 70.231  1.00 43.81  ?  341  ILE A CD1 1 
ATOM   2272  N N   . SER A  1  342 ? 56.173  -13.415 72.499  1.00 42.59  ?  342  SER A N   1 
ATOM   2273  C CA  . SER A  1  342 ? 55.756  -12.044 72.233  1.00 42.22  ?  342  SER A CA  1 
ATOM   2274  C C   . SER A  1  342 ? 56.336  -11.076 73.263  1.00 41.71  ?  342  SER A C   1 
ATOM   2275  O O   . SER A  1  342 ? 56.894  -11.469 74.289  1.00 41.69  ?  342  SER A O   1 
ATOM   2276  C CB  . SER A  1  342 ? 54.234  -11.932 72.225  1.00 42.06  ?  342  SER A CB  1 
ATOM   2277  O OG  . SER A  1  342 ? 53.651  -12.986 71.489  1.00 42.76  ?  342  SER A OG  1 
ATOM   2278  N N   . GLU A  1  343 ? 56.187  -9.784  72.965  1.00 44.27  ?  343  GLU A N   1 
ATOM   2279  C CA  . GLU A  1  343 ? 56.584  -8.694  73.858  1.00 43.21  ?  343  GLU A CA  1 
ATOM   2280  C C   . GLU A  1  343 ? 58.026  -8.865  74.333  1.00 43.28  ?  343  GLU A C   1 
ATOM   2281  O O   . GLU A  1  343 ? 58.313  -9.018  75.521  1.00 43.24  ?  343  GLU A O   1 
ATOM   2282  C CB  . GLU A  1  343 ? 55.622  -8.577  75.042  1.00 42.77  ?  343  GLU A CB  1 
ATOM   2283  C CG  . GLU A  1  343 ? 54.181  -8.920  74.708  1.00 43.20  ?  343  GLU A CG  1 
ATOM   2284  C CD  . GLU A  1  343 ? 53.200  -8.298  75.675  1.00 41.76  ?  343  GLU A CD  1 
ATOM   2285  O OE1 . GLU A  1  343 ? 53.421  -7.138  76.081  1.00 39.96  ?  343  GLU A OE1 1 
ATOM   2286  O OE2 . GLU A  1  343 ? 52.208  -8.968  76.031  1.00 42.14  -1 343  GLU A OE2 1 
ATOM   2287  N N   . ASN A  1  344 ? 58.938  -8.846  73.367  1.00 44.31  ?  344  ASN A N   1 
ATOM   2288  C CA  . ASN A  1  344 ? 60.351  -9.055  73.637  1.00 44.18  ?  344  ASN A CA  1 
ATOM   2289  C C   . ASN A  1  344 ? 61.149  -8.097  72.761  1.00 44.46  ?  344  ASN A C   1 
ATOM   2290  O O   . ASN A  1  344 ? 60.598  -7.182  72.143  1.00 44.11  ?  344  ASN A O   1 
ATOM   2291  C CB  . ASN A  1  344 ? 60.733  -10.521 73.393  1.00 45.28  ?  344  ASN A CB  1 
ATOM   2292  C CG  . ASN A  1  344 ? 60.617  -11.364 74.641  1.00 45.79  ?  344  ASN A CG  1 
ATOM   2293  O OD1 . ASN A  1  344 ? 61.374  -11.187 75.592  1.00 46.02  ?  344  ASN A OD1 1 
ATOM   2294  N ND2 . ASN A  1  344 ? 59.665  -12.291 74.644  1.00 46.06  ?  344  ASN A ND2 1 
ATOM   2295  N N   . LYS A  1  345 ? 62.459  -8.310  72.712  1.00 44.29  ?  345  LYS A N   1 
ATOM   2296  C CA  . LYS A  1  345 ? 63.361  -7.516  71.891  1.00 46.31  ?  345  LYS A CA  1 
ATOM   2297  C C   . LYS A  1  345 ? 64.129  -8.413  70.929  1.00 48.12  ?  345  LYS A C   1 
ATOM   2298  O O   . LYS A  1  345 ? 65.308  -8.191  70.642  1.00 50.27  ?  345  LYS A O   1 
ATOM   2299  C CB  . LYS A  1  345 ? 64.314  -6.704  72.764  1.00 47.38  ?  345  LYS A CB  1 
ATOM   2300  C CG  . LYS A  1  345 ? 63.615  -5.649  73.608  1.00 45.93  ?  345  LYS A CG  1 
ATOM   2301  C CD  . LYS A  1  345 ? 64.610  -4.804  74.384  1.00 47.27  ?  345  LYS A CD  1 
ATOM   2302  C CE  . LYS A  1  345 ? 63.898  -3.747  75.212  1.00 45.96  ?  345  LYS A CE  1 
ATOM   2303  N NZ  . LYS A  1  345 ? 62.933  -4.351  76.173  1.00 43.80  ?  345  LYS A NZ  1 
ATOM   2304  N N   . LEU A  1  346 ? 63.458  -9.444  70.424  1.00 48.93  ?  346  LEU A N   1 
ATOM   2305  C CA  . LEU A  1  346 ? 64.060  -10.328 69.439  1.00 50.64  ?  346  LEU A CA  1 
ATOM   2306  C C   . LEU A  1  346 ? 64.247  -9.599  68.115  1.00 51.98  ?  346  LEU A C   1 
ATOM   2307  O O   . LEU A  1  346 ? 63.537  -8.641  67.800  1.00 51.07  ?  346  LEU A O   1 
ATOM   2308  C CB  . LEU A  1  346 ? 63.191  -11.570 69.233  1.00 49.47  ?  346  LEU A CB  1 
ATOM   2309  C CG  . LEU A  1  346 ? 62.986  -12.530 70.406  1.00 48.30  ?  346  LEU A CG  1 
ATOM   2310  C CD1 . LEU A  1  346 ? 62.656  -13.917 69.886  1.00 48.36  ?  346  LEU A CD1 1 
ATOM   2311  C CD2 . LEU A  1  346 ? 64.219  -12.579 71.288  1.00 49.56  ?  346  LEU A CD2 1 
ATOM   2312  N N   . THR A  1  347 ? 65.213  -10.069 67.330  1.00 52.24  ?  347  THR A N   1 
ATOM   2313  C CA  . THR A  1  347 ? 65.546  -9.465  66.049  1.00 53.89  ?  347  THR A CA  1 
ATOM   2314  C C   . THR A  1  347 ? 65.758  -10.574 65.026  1.00 55.24  ?  347  THR A C   1 
ATOM   2315  O O   . THR A  1  347 ? 65.683  -11.764 65.343  1.00 54.94  ?  347  THR A O   1 
ATOM   2316  C CB  . THR A  1  347 ? 66.789  -8.570  66.159  1.00 55.92  ?  347  THR A CB  1 
ATOM   2317  O OG1 . THR A  1  347 ? 67.852  -9.299  66.786  1.00 57.23  ?  347  THR A OG1 1 
ATOM   2318  C CG2 . THR A  1  347 ? 66.487  -7.315  66.970  1.00 54.74  ?  347  THR A CG2 1 
ATOM   2319  N N   . GLY A  1  348 ? 66.014  -10.175 63.783  1.00 59.43  ?  348  GLY A N   1 
ATOM   2320  C CA  . GLY A  1  348 ? 66.319  -11.113 62.732  1.00 61.10  ?  348  GLY A CA  1 
ATOM   2321  C C   . GLY A  1  348 ? 65.092  -11.792 62.161  1.00 59.67  ?  348  GLY A C   1 
ATOM   2322  O O   . GLY A  1  348 ? 63.955  -11.530 62.567  1.00 57.31  ?  348  GLY A O   1 
ATOM   2323  N N   . PRO A  1  349 ? 65.305  -12.683 61.199  1.00 59.59  ?  349  PRO A N   1 
ATOM   2324  C CA  . PRO A  1  349 ? 64.180  -13.344 60.536  1.00 58.56  ?  349  PRO A CA  1 
ATOM   2325  C C   . PRO A  1  349 ? 63.706  -14.570 61.301  1.00 57.27  ?  349  PRO A C   1 
ATOM   2326  O O   . PRO A  1  349 ? 64.409  -15.127 62.147  1.00 57.68  ?  349  PRO A O   1 
ATOM   2327  C CB  . PRO A  1  349 ? 64.766  -13.739 59.178  1.00 61.17  ?  349  PRO A CB  1 
ATOM   2328  C CG  . PRO A  1  349 ? 66.203  -14.014 59.487  1.00 63.37  ?  349  PRO A CG  1 
ATOM   2329  C CD  . PRO A  1  349 ? 66.597  -13.059 60.596  1.00 62.57  ?  349  PRO A CD  1 
ATOM   2330  N N   . VAL A  1  350 ? 62.483  -14.979 60.989  1.00 59.49  ?  350  VAL A N   1 
ATOM   2331  C CA  . VAL A  1  350 ? 61.958  -16.248 61.495  1.00 58.53  ?  350  VAL A CA  1 
ATOM   2332  C C   . VAL A  1  350 ? 62.616  -17.390 60.724  1.00 60.97  ?  350  VAL A C   1 
ATOM   2333  O O   . VAL A  1  350 ? 62.695  -17.325 59.488  1.00 62.70  ?  350  VAL A O   1 
ATOM   2334  C CB  . VAL A  1  350 ? 60.439  -16.295 61.353  1.00 56.44  ?  350  VAL A CB  1 
ATOM   2335  C CG1 . VAL A  1  350 ? 59.896  -17.637 61.831  1.00 55.90  ?  350  VAL A CG1 1 
ATOM   2336  C CG2 . VAL A  1  350 ? 59.796  -15.152 62.128  1.00 54.68  ?  350  VAL A CG2 1 
ATOM   2337  N N   . PRO A  1  351 ? 63.109  -18.424 61.400  1.00 59.51  ?  351  PRO A N   1 
ATOM   2338  C CA  . PRO A  1  351 ? 63.729  -19.543 60.681  1.00 61.83  ?  351  PRO A CA  1 
ATOM   2339  C C   . PRO A  1  351 ? 62.713  -20.320 59.856  1.00 61.56  ?  351  PRO A C   1 
ATOM   2340  O O   . PRO A  1  351 ? 61.586  -20.564 60.294  1.00 59.40  ?  351  PRO A O   1 
ATOM   2341  C CB  . PRO A  1  351 ? 64.314  -20.409 61.804  1.00 61.86  ?  351  PRO A CB  1 
ATOM   2342  C CG  . PRO A  1  351 ? 64.396  -19.499 62.994  1.00 60.23  ?  351  PRO A CG  1 
ATOM   2343  C CD  . PRO A  1  351 ? 63.246  -18.558 62.859  1.00 58.16  ?  351  PRO A CD  1 
ATOM   2344  N N   . ASP A  1  352 ? 63.128  -20.711 58.646  1.00 65.66  ?  352  ASP A N   1 
ATOM   2345  C CA  . ASP A  1  352 ? 62.306  -21.590 57.820  1.00 65.88  ?  352  ASP A CA  1 
ATOM   2346  C C   . ASP A  1  352 ? 62.061  -22.938 58.484  1.00 65.45  ?  352  ASP A C   1 
ATOM   2347  O O   . ASP A  1  352 ? 61.148  -23.663 58.075  1.00 65.03  ?  352  ASP A O   1 
ATOM   2348  C CB  . ASP A  1  352 ? 62.953  -21.801 56.449  1.00 68.83  ?  352  ASP A CB  1 
ATOM   2349  C CG  . ASP A  1  352 ? 63.428  -20.507 55.821  1.00 69.69  ?  352  ASP A CG  1 
ATOM   2350  O OD1 . ASP A  1  352 ? 64.549  -20.062 56.147  1.00 70.87  ?  352  ASP A OD1 1 
ATOM   2351  O OD2 . ASP A  1  352 ? 62.683  -19.935 54.997  1.00 69.25  -1 352  ASP A OD2 1 
ATOM   2352  N N   . SER A  1  353 ? 62.857  -23.287 59.498  1.00 63.45  ?  353  SER A N   1 
ATOM   2353  C CA  . SER A  1  353 ? 62.689  -24.541 60.223  1.00 63.05  ?  353  SER A CA  1 
ATOM   2354  C C   . SER A  1  353 ? 61.352  -24.628 60.945  1.00 60.17  ?  353  SER A C   1 
ATOM   2355  O O   . SER A  1  353 ? 60.966  -25.724 61.366  1.00 59.79  ?  353  SER A O   1 
ATOM   2356  C CB  . SER A  1  353 ? 63.828  -24.716 61.229  1.00 63.69  ?  353  SER A CB  1 
ATOM   2357  O OG  . SER A  1  353 ? 63.827  -23.667 62.182  1.00 61.90  ?  353  SER A OG  1 
ATOM   2358  N N   . PHE A  1  354 ? 60.645  -23.506 61.106  1.00 60.28  ?  354  PHE A N   1 
ATOM   2359  C CA  . PHE A  1  354 ? 59.331  -23.527 61.739  1.00 57.63  ?  354  PHE A CA  1 
ATOM   2360  C C   . PHE A  1  354 ? 58.333  -24.385 60.972  1.00 57.66  ?  354  PHE A C   1 
ATOM   2361  O O   . PHE A  1  354 ? 57.305  -24.773 61.538  1.00 55.82  ?  354  PHE A O   1 
ATOM   2362  C CB  . PHE A  1  354 ? 58.796  -22.101 61.887  1.00 55.87  ?  354  PHE A CB  1 
ATOM   2363  C CG  . PHE A  1  354 ? 59.274  -21.400 63.128  1.00 54.79  ?  354  PHE A CG  1 
ATOM   2364  C CD1 . PHE A  1  354 ? 60.621  -21.369 63.449  1.00 56.38  ?  354  PHE A CD1 1 
ATOM   2365  C CD2 . PHE A  1  354 ? 58.375  -20.774 63.976  1.00 52.29  ?  354  PHE A CD2 1 
ATOM   2366  C CE1 . PHE A  1  354 ? 61.063  -20.729 64.591  1.00 55.50  ?  354  PHE A CE1 1 
ATOM   2367  C CE2 . PHE A  1  354 ? 58.811  -20.131 65.120  1.00 51.43  ?  354  PHE A CE2 1 
ATOM   2368  C CZ  . PHE A  1  354 ? 60.156  -20.108 65.427  1.00 53.03  ?  354  PHE A CZ  1 
ATOM   2369  N N   . GLY A  1  355 ? 58.603  -24.677 59.697  1.00 60.24  ?  355  GLY A N   1 
ATOM   2370  C CA  . GLY A  1  355 ? 57.753  -25.598 58.961  1.00 60.61  ?  355  GLY A CA  1 
ATOM   2371  C C   . GLY A  1  355 ? 57.716  -26.989 59.561  1.00 60.83  ?  355  GLY A C   1 
ATOM   2372  O O   . GLY A  1  355 ? 56.740  -27.723 59.377  1.00 60.31  ?  355  GLY A O   1 
ATOM   2373  N N   . LYS A  1  356 ? 58.765  -27.370 60.294  1.00 56.58  ?  356  LYS A N   1 
ATOM   2374  C CA  . LYS A  1  356 ? 58.813  -28.685 60.920  1.00 56.86  ?  356  LYS A CA  1 
ATOM   2375  C C   . LYS A  1  356 ? 57.909  -28.788 62.140  1.00 54.18  ?  356  LYS A C   1 
ATOM   2376  O O   . LYS A  1  356 ? 57.714  -29.897 62.651  1.00 54.17  ?  356  LYS A O   1 
ATOM   2377  C CB  . LYS A  1  356 ? 60.252  -29.033 61.310  1.00 58.66  ?  356  LYS A CB  1 
ATOM   2378  C CG  . LYS A  1  356 ? 61.076  -29.631 60.178  1.00 61.81  ?  356  LYS A CG  1 
ATOM   2379  C CD  . LYS A  1  356 ? 62.547  -29.731 60.554  1.00 63.57  ?  356  LYS A CD  1 
ATOM   2380  C CE  . LYS A  1  356 ? 63.343  -28.550 60.022  1.00 64.58  ?  356  LYS A CE  1 
ATOM   2381  N NZ  . LYS A  1  356 ? 64.658  -28.408 60.709  1.00 65.62  ?  356  LYS A NZ  1 
ATOM   2382  N N   . LEU A  1  357 ? 57.369  -27.670 62.627  1.00 55.94  ?  357  LEU A N   1 
ATOM   2383  C CA  . LEU A  1  357 ? 56.387  -27.679 63.711  1.00 53.61  ?  357  LEU A CA  1 
ATOM   2384  C C   . LEU A  1  357 ? 55.031  -28.047 63.114  1.00 53.27  ?  357  LEU A C   1 
ATOM   2385  O O   . LEU A  1  357 ? 54.210  -27.193 62.770  1.00 52.03  ?  357  LEU A O   1 
ATOM   2386  C CB  . LEU A  1  357 ? 56.344  -26.328 64.415  1.00 51.55  ?  357  LEU A CB  1 
ATOM   2387  C CG  . LEU A  1  357 ? 57.683  -25.684 64.783  1.00 52.06  ?  357  LEU A CG  1 
ATOM   2388  C CD1 . LEU A  1  357 ? 57.462  -24.331 65.436  1.00 50.04  ?  357  LEU A CD1 1 
ATOM   2389  C CD2 . LEU A  1  357 ? 58.478  -26.596 65.702  1.00 52.71  ?  357  LEU A CD2 1 
ATOM   2390  N N   . THR A  1  358 ? 54.795  -29.355 62.992  1.00 53.48  ?  358  THR A N   1 
ATOM   2391  C CA  . THR A  1  358 ? 53.598  -29.851 62.323  1.00 53.69  ?  358  THR A CA  1 
ATOM   2392  C C   . THR A  1  358 ? 52.359  -29.839 63.210  1.00 51.59  ?  358  THR A C   1 
ATOM   2393  O O   . THR A  1  358 ? 51.250  -30.008 62.691  1.00 51.47  ?  358  THR A O   1 
ATOM   2394  C CB  . THR A  1  358 ? 53.829  -31.274 61.805  1.00 56.12  ?  358  THR A CB  1 
ATOM   2395  O OG1 . THR A  1  358 ? 53.573  -32.216 62.854  1.00 55.76  ?  358  THR A OG1 1 
ATOM   2396  C CG2 . THR A  1  358 ? 55.257  -31.442 61.310  1.00 58.25  ?  358  THR A CG2 1 
ATOM   2397  N N   . ALA A  1  359 ? 52.510  -29.649 64.522  1.00 49.39  ?  359  ALA A N   1 
ATOM   2398  C CA  . ALA A  1  359 ? 51.374  -29.654 65.438  1.00 47.56  ?  359  ALA A CA  1 
ATOM   2399  C C   . ALA A  1  359 ? 51.150  -28.295 66.093  1.00 45.29  ?  359  ALA A C   1 
ATOM   2400  O O   . ALA A  1  359 ? 50.448  -28.208 67.106  1.00 43.74  ?  359  ALA A O   1 
ATOM   2401  C CB  . ALA A  1  359 ? 51.555  -30.732 66.508  1.00 47.85  ?  359  ALA A CB  1 
ATOM   2402  N N   . LEU A  1  360 ? 51.730  -27.232 65.540  1.00 46.75  ?  360  LEU A N   1 
ATOM   2403  C CA  . LEU A  1  360 ? 51.603  -25.911 66.141  1.00 44.79  ?  360  LEU A CA  1 
ATOM   2404  C C   . LEU A  1  360 ? 50.187  -25.369 65.973  1.00 43.32  ?  360  LEU A C   1 
ATOM   2405  O O   . LEU A  1  360 ? 49.559  -25.536 64.924  1.00 43.99  ?  360  LEU A O   1 
ATOM   2406  C CB  . LEU A  1  360 ? 52.613  -24.951 65.514  1.00 45.39  ?  360  LEU A CB  1 
ATOM   2407  C CG  . LEU A  1  360 ? 52.681  -23.536 66.087  1.00 43.71  ?  360  LEU A CG  1 
ATOM   2408  C CD1 . LEU A  1  360 ? 53.351  -23.543 67.452  1.00 43.08  ?  360  LEU A CD1 1 
ATOM   2409  C CD2 . LEU A  1  360 ? 53.415  -22.611 65.130  1.00 44.61  ?  360  LEU A CD2 1 
ATOM   2410  N N   . GLU A  1  361 ? 49.686  -24.713 67.019  1.00 44.79  ?  361  GLU A N   1 
ATOM   2411  C CA  . GLU A  1  361 ? 48.359  -24.107 67.006  1.00 43.30  ?  361  GLU A CA  1 
ATOM   2412  C C   . GLU A  1  361 ? 48.366  -22.621 67.329  1.00 41.74  ?  361  GLU A C   1 
ATOM   2413  O O   . GLU A  1  361 ? 47.595  -21.864 66.732  1.00 41.04  ?  361  GLU A O   1 
ATOM   2414  C CB  . GLU A  1  361 ? 47.444  -24.840 67.998  1.00 42.57  ?  361  GLU A CB  1 
ATOM   2415  C CG  . GLU A  1  361 ? 47.313  -26.330 67.734  1.00 44.17  ?  361  GLU A CG  1 
ATOM   2416  C CD  . GLU A  1  361 ? 46.149  -26.954 68.474  1.00 43.60  ?  361  GLU A CD  1 
ATOM   2417  O OE1 . GLU A  1  361 ? 45.363  -26.203 69.091  1.00 41.97  ?  361  GLU A OE1 1 
ATOM   2418  O OE2 . GLU A  1  361 ? 46.021  -28.196 68.443  1.00 44.92  -1 361  GLU A OE2 1 
ATOM   2419  N N   . TRP A  1  362 ? 49.213  -22.181 68.257  1.00 43.60  ?  362  TRP A N   1 
ATOM   2420  C CA  . TRP A  1  362 ? 49.370  -20.769 68.590  1.00 42.39  ?  362  TRP A CA  1 
ATOM   2421  C C   . TRP A  1  362 ? 50.820  -20.371 68.360  1.00 43.47  ?  362  TRP A C   1 
ATOM   2422  O O   . TRP A  1  362 ? 51.727  -20.942 68.975  1.00 44.16  ?  362  TRP A O   1 
ATOM   2423  C CB  . TRP A  1  362 ? 48.977  -20.479 70.042  1.00 40.83  ?  362  TRP A CB  1 
ATOM   2424  C CG  . TRP A  1  362 ? 47.538  -20.724 70.380  1.00 39.78  ?  362  TRP A CG  1 
ATOM   2425  C CD1 . TRP A  1  362 ? 46.526  -19.811 70.355  1.00 38.46  ?  362  TRP A CD1 1 
ATOM   2426  C CD2 . TRP A  1  362 ? 46.958  -21.953 70.832  1.00 40.08  ?  362  TRP A CD2 1 
ATOM   2427  N NE1 . TRP A  1  362 ? 45.347  -20.399 70.742  1.00 37.96  ?  362  TRP A NE1 1 
ATOM   2428  C CE2 . TRP A  1  362 ? 45.586  -21.714 71.043  1.00 38.97  ?  362  TRP A CE2 1 
ATOM   2429  C CE3 . TRP A  1  362 ? 47.464  -23.234 71.072  1.00 41.30  ?  362  TRP A CE3 1 
ATOM   2430  C CZ2 . TRP A  1  362 ? 44.713  -22.708 71.479  1.00 39.11  ?  362  TRP A CZ2 1 
ATOM   2431  C CZ3 . TRP A  1  362 ? 46.595  -24.220 71.504  1.00 41.40  ?  362  TRP A CZ3 1 
ATOM   2432  C CH2 . TRP A  1  362 ? 45.236  -23.951 71.705  1.00 40.35  ?  362  TRP A CH2 1 
ATOM   2433  N N   . LEU A  1  363 ? 51.036  -19.393 67.487  1.00 39.83  ?  363  LEU A N   1 
ATOM   2434  C CA  . LEU A  1  363 ? 52.360  -18.816 67.264  1.00 40.89  ?  363  LEU A CA  1 
ATOM   2435  C C   . LEU A  1  363 ? 52.283  -17.334 67.616  1.00 39.68  ?  363  LEU A C   1 
ATOM   2436  O O   . LEU A  1  363 ? 51.751  -16.530 66.843  1.00 39.37  ?  363  LEU A O   1 
ATOM   2437  C CB  . LEU A  1  363 ? 52.836  -19.030 65.831  1.00 42.76  ?  363  LEU A CB  1 
ATOM   2438  C CG  . LEU A  1  363 ? 54.257  -18.523 65.577  1.00 44.19  ?  363  LEU A CG  1 
ATOM   2439  C CD1 . LEU A  1  363 ? 55.267  -19.364 66.343  1.00 45.06  ?  363  LEU A CD1 1 
ATOM   2440  C CD2 . LEU A  1  363 ? 54.575  -18.525 64.094  1.00 46.00  ?  363  LEU A CD2 1 
ATOM   2441  N N   . PHE A  1  364 ? 52.812  -16.980 68.782  1.00 39.02  ?  364  PHE A N   1 
ATOM   2442  C CA  . PHE A  1  364 ? 52.787  -15.614 69.295  1.00 37.97  ?  364  PHE A CA  1 
ATOM   2443  C C   . PHE A  1  364 ? 54.182  -15.015 69.131  1.00 39.32  ?  364  PHE A C   1 
ATOM   2444  O O   . PHE A  1  364 ? 55.093  -15.317 69.907  1.00 39.86  ?  364  PHE A O   1 
ATOM   2445  C CB  . PHE A  1  364 ? 52.340  -15.601 70.754  1.00 36.49  ?  364  PHE A CB  1 
ATOM   2446  C CG  . PHE A  1  364 ? 50.858  -15.455 70.939  1.00 34.91  ?  364  PHE A CG  1 
ATOM   2447  C CD1 . PHE A  1  364 ? 50.001  -16.505 70.658  1.00 34.84  ?  364  PHE A CD1 1 
ATOM   2448  C CD2 . PHE A  1  364 ? 50.324  -14.268 71.409  1.00 33.63  ?  364  PHE A CD2 1 
ATOM   2449  C CE1 . PHE A  1  364 ? 48.636  -16.370 70.834  1.00 33.54  ?  364  PHE A CE1 1 
ATOM   2450  C CE2 . PHE A  1  364 ? 48.965  -14.129 71.585  1.00 32.30  ?  364  PHE A CE2 1 
ATOM   2451  C CZ  . PHE A  1  364 ? 48.118  -15.179 71.299  1.00 32.25  ?  364  PHE A CZ  1 
ATOM   2452  N N   . LEU A  1  365 ? 54.343  -14.164 68.116  1.00 43.12  ?  365  LEU A N   1 
ATOM   2453  C CA  . LEU A  1  365 ? 55.599  -13.465 67.865  1.00 44.22  ?  365  LEU A CA  1 
ATOM   2454  C C   . LEU A  1  365 ? 55.438  -11.950 67.888  1.00 43.88  ?  365  LEU A C   1 
ATOM   2455  O O   . LEU A  1  365 ? 56.390  -11.231 67.561  1.00 44.92  ?  365  LEU A O   1 
ATOM   2456  C CB  . LEU A  1  365 ? 56.200  -13.896 66.524  1.00 46.25  ?  365  LEU A CB  1 
ATOM   2457  C CG  . LEU A  1  365 ? 56.549  -15.372 66.338  1.00 47.37  ?  365  LEU A CG  1 
ATOM   2458  C CD1 . LEU A  1  365 ? 56.945  -15.638 64.895  1.00 49.36  ?  365  LEU A CD1 1 
ATOM   2459  C CD2 . LEU A  1  365 ? 57.664  -15.780 67.288  1.00 48.05  ?  365  LEU A CD2 1 
ATOM   2460  N N   . ARG A  1  366 ? 54.265  -11.451 68.268  1.00 44.00  ?  366  ARG A N   1 
ATOM   2461  C CA  . ARG A  1  366 ? 53.965  -10.032 68.172  1.00 43.49  ?  366  ARG A CA  1 
ATOM   2462  C C   . ARG A  1  366 ? 54.825  -9.214  69.133  1.00 42.93  ?  366  ARG A C   1 
ATOM   2463  O O   . ARG A  1  366 ? 55.433  -9.736  70.071  1.00 42.50  ?  366  ARG A O   1 
ATOM   2464  C CB  . ARG A  1  366 ? 52.488  -9.779  68.466  1.00 41.50  ?  366  ARG A CB  1 
ATOM   2465  C CG  . ARG A  1  366 ? 51.985  -10.425 69.745  1.00 39.53  ?  366  ARG A CG  1 
ATOM   2466  C CD  . ARG A  1  366 ? 50.573  -9.966  70.066  1.00 37.42  ?  366  ARG A CD  1 
ATOM   2467  N NE  . ARG A  1  366 ? 50.472  -8.511  70.079  1.00 36.72  ?  366  ARG A NE  1 
ATOM   2468  C CZ  . ARG A  1  366 ? 50.968  -7.729  71.028  1.00 35.99  ?  366  ARG A CZ  1 
ATOM   2469  N NH1 . ARG A  1  366 ? 51.597  -8.230  72.079  1.00 36.13  ?  366  ARG A NH1 1 
ATOM   2470  N NH2 . ARG A  1  366 ? 50.829  -6.411  70.920  1.00 35.79  ?  366  ARG A NH2 1 
ATOM   2471  N N   . ASP A  1  367 ? 54.867  -7.905  68.876  1.00 47.65  ?  367  ASP A N   1 
ATOM   2472  C CA  . ASP A  1  367 ? 55.566  -6.937  69.723  1.00 47.02  ?  367  ASP A CA  1 
ATOM   2473  C C   . ASP A  1  367 ? 57.048  -7.289  69.864  1.00 48.84  ?  367  ASP A C   1 
ATOM   2474  O O   . ASP A  1  367 ? 57.555  -7.563  70.953  1.00 48.74  ?  367  ASP A O   1 
ATOM   2475  C CB  . ASP A  1  367 ? 54.890  -6.824  71.094  1.00 44.96  ?  367  ASP A CB  1 
ATOM   2476  C CG  . ASP A  1  367 ? 55.246  -5.538  71.820  1.00 44.72  ?  367  ASP A CG  1 
ATOM   2477  O OD1 . ASP A  1  367 ? 56.418  -5.109  71.753  1.00 46.23  ?  367  ASP A OD1 1 
ATOM   2478  O OD2 . ASP A  1  367 ? 54.350  -4.959  72.468  1.00 44.24  -1 367  ASP A OD2 1 
ATOM   2479  N N   . ASN A  1  368 ? 57.741  -7.282  68.729  1.00 48.21  ?  368  ASN A N   1 
ATOM   2480  C CA  . ASN A  1  368 ? 59.157  -7.616  68.695  1.00 49.66  ?  368  ASN A CA  1 
ATOM   2481  C C   . ASN A  1  368 ? 59.824  -6.747  67.634  1.00 51.65  ?  368  ASN A C   1 
ATOM   2482  O O   . ASN A  1  368 ? 59.233  -5.787  67.129  1.00 51.65  ?  368  ASN A O   1 
ATOM   2483  C CB  . ASN A  1  368 ? 59.346  -9.116  68.436  1.00 50.51  ?  368  ASN A CB  1 
ATOM   2484  C CG  . ASN A  1  368 ? 59.636  -9.890  69.704  1.00 49.75  ?  368  ASN A CG  1 
ATOM   2485  O OD1 . ASN A  1  368 ? 60.737  -9.820  70.249  1.00 51.03  ?  368  ASN A OD1 1 
ATOM   2486  N ND2 . ASN A  1  368 ? 58.645  -10.632 70.184  1.00 48.06  ?  368  ASN A ND2 1 
ATOM   2487  N N   . GLN A  1  369 ? 61.074  -7.075  67.302  1.00 53.49  ?  369  GLN A N   1 
ATOM   2488  C CA  . GLN A  1  369 ? 61.838  -6.337  66.302  1.00 55.71  ?  369  GLN A CA  1 
ATOM   2489  C C   . GLN A  1  369 ? 62.315  -7.253  65.178  1.00 57.73  ?  369  GLN A C   1 
ATOM   2490  O O   . GLN A  1  369 ? 63.374  -7.027  64.588  1.00 60.63  ?  369  GLN A O   1 
ATOM   2491  C CB  . GLN A  1  369 ? 63.023  -5.617  66.946  1.00 57.22  ?  369  GLN A CB  1 
ATOM   2492  C CG  . GLN A  1  369 ? 62.718  -5.007  68.304  1.00 55.61  ?  369  GLN A CG  1 
ATOM   2493  C CD  . GLN A  1  369 ? 63.346  -3.640  68.486  1.00 57.91  ?  369  GLN A CD  1 
ATOM   2494  O OE1 . GLN A  1  369 ? 62.662  -2.618  68.433  1.00 56.81  ?  369  GLN A OE1 1 
ATOM   2495  N NE2 . GLN A  1  369 ? 64.654  -3.616  68.706  1.00 60.34  ?  369  GLN A NE2 1 
ATOM   2496  N N   . LEU A  1  370 ? 61.543  -8.294  64.879  1.00 54.13  ?  370  LEU A N   1 
ATOM   2497  C CA  . LEU A  1  370 ? 61.880  -9.189  63.784  1.00 55.83  ?  370  LEU A CA  1 
ATOM   2498  C C   . LEU A  1  370 ? 61.713  -8.478  62.443  1.00 57.01  ?  370  LEU A C   1 
ATOM   2499  O O   . LEU A  1  370 ? 61.017  -7.466  62.326  1.00 55.98  ?  370  LEU A O   1 
ATOM   2500  C CB  . LEU A  1  370 ? 61.010  -10.445 63.833  1.00 54.45  ?  370  LEU A CB  1 
ATOM   2501  C CG  . LEU A  1  370 ? 60.738  -11.036 65.217  1.00 52.66  ?  370  LEU A CG  1 
ATOM   2502  C CD1 . LEU A  1  370 ? 59.882  -12.286 65.113  1.00 51.66  ?  370  LEU A CD1 1 
ATOM   2503  C CD2 . LEU A  1  370 ? 62.048  -11.351 65.909  1.00 54.04  ?  370  LEU A CD2 1 
ATOM   2504  N N   . SER A  1  371 ? 62.357  -9.030  61.417  1.00 57.21  ?  371  SER A N   1 
ATOM   2505  C CA  . SER A  1  371 ? 62.408  -8.382  60.113  1.00 58.86  ?  371  SER A CA  1 
ATOM   2506  C C   . SER A  1  371 ? 62.532  -9.443  59.026  1.00 60.49  ?  371  SER A C   1 
ATOM   2507  O O   . SER A  1  371 ? 62.590  -10.645 59.302  1.00 60.34  ?  371  SER A O   1 
ATOM   2508  C CB  . SER A  1  371 ? 63.563  -7.378  60.048  1.00 61.02  ?  371  SER A CB  1 
ATOM   2509  O OG  . SER A  1  371 ? 64.798  -8.004  60.352  1.00 62.88  ?  371  SER A OG  1 
ATOM   2510  N N   . GLY A  1  372 ? 62.574  -8.980  57.778  1.00 64.16  ?  372  GLY A N   1 
ATOM   2511  C CA  . GLY A  1  372 ? 62.698  -9.850  56.634  1.00 66.02  ?  372  GLY A CA  1 
ATOM   2512  C C   . GLY A  1  372 ? 61.367  -10.424 56.193  1.00 64.36  ?  372  GLY A C   1 
ATOM   2513  O O   . GLY A  1  372 ? 60.304  -10.053 56.701  1.00 61.79  ?  372  GLY A O   1 
ATOM   2514  N N   . PRO A  1  373 ? 61.401  -11.341 55.233  1.00 65.72  ?  373  PRO A N   1 
ATOM   2515  C CA  . PRO A  1  373 ? 60.165  -11.946 54.734  1.00 64.49  ?  373  PRO A CA  1 
ATOM   2516  C C   . PRO A  1  373 ? 59.653  -13.031 55.673  1.00 62.61  ?  373  PRO A C   1 
ATOM   2517  O O   . PRO A  1  373 ? 60.354  -13.512 56.564  1.00 62.64  ?  373  PRO A O   1 
ATOM   2518  C CB  . PRO A  1  373 ? 60.583  -12.531 53.383  1.00 67.37  ?  373  PRO A CB  1 
ATOM   2519  C CG  . PRO A  1  373 ? 62.025  -12.873 53.565  1.00 69.68  ?  373  PRO A CG  1 
ATOM   2520  C CD  . PRO A  1  373 ? 62.596  -11.897 54.572  1.00 68.91  ?  373  PRO A CD  1 
ATOM   2521  N N   . ILE A  1  374 ? 58.397  -13.404 55.458  1.00 63.29  ?  374  ILE A N   1 
ATOM   2522  C CA  . ILE A  1  374 ? 57.764  -14.493 56.194  1.00 61.72  ?  374  ILE A CA  1 
ATOM   2523  C C   . ILE A  1  374 ? 58.082  -15.794 55.461  1.00 63.78  ?  374  ILE A C   1 
ATOM   2524  O O   . ILE A  1  374 ? 57.717  -15.928 54.281  1.00 65.00  ?  374  ILE A O   1 
ATOM   2525  C CB  . ILE A  1  374 ? 56.249  -14.291 56.313  1.00 59.27  ?  374  ILE A CB  1 
ATOM   2526  C CG1 . ILE A  1  374 ? 55.918  -13.323 57.446  1.00 57.76  ?  374  ILE A CG1 1 
ATOM   2527  C CG2 . ILE A  1  374 ? 55.570  -15.609 56.618  1.00 58.52  ?  374  ILE A CG2 1 
ATOM   2528  C CD1 . ILE A  1  374 ? 56.514  -13.721 58.764  1.00 58.04  ?  374  ILE A CD1 1 
ATOM   2529  N N   . PRO A  1  375 ? 58.760  -16.746 56.092  1.00 61.54  ?  375  PRO A N   1 
ATOM   2530  C CA  . PRO A  1  375 ? 59.003  -18.037 55.444  1.00 63.50  ?  375  PRO A CA  1 
ATOM   2531  C C   . PRO A  1  375 ? 57.700  -18.788 55.250  1.00 62.31  ?  375  PRO A C   1 
ATOM   2532  O O   . PRO A  1  375 ? 56.806  -18.724 56.107  1.00 59.81  ?  375  PRO A O   1 
ATOM   2533  C CB  . PRO A  1  375 ? 59.928  -18.768 56.432  1.00 63.84  ?  375  PRO A CB  1 
ATOM   2534  C CG  . PRO A  1  375 ? 60.432  -17.711 57.361  1.00 62.75  ?  375  PRO A CG  1 
ATOM   2535  C CD  . PRO A  1  375 ? 59.356  -16.680 57.434  1.00 60.53  ?  375  PRO A CD  1 
ATOM   2536  N N   . PRO A  1  376 ? 57.551  -19.510 54.137  1.00 64.95  ?  376  PRO A N   1 
ATOM   2537  C CA  . PRO A  1  376 ? 56.300  -20.249 53.907  1.00 64.07  ?  376  PRO A CA  1 
ATOM   2538  C C   . PRO A  1  376 ? 56.015  -21.301 54.962  1.00 62.89  ?  376  PRO A C   1 
ATOM   2539  O O   . PRO A  1  376 ? 54.860  -21.723 55.100  1.00 61.55  ?  376  PRO A O   1 
ATOM   2540  C CB  . PRO A  1  376 ? 56.515  -20.887 52.527  1.00 66.93  ?  376  PRO A CB  1 
ATOM   2541  C CG  . PRO A  1  376 ? 57.576  -20.055 51.879  1.00 68.86  ?  376  PRO A CG  1 
ATOM   2542  C CD  . PRO A  1  376 ? 58.474  -19.611 52.994  1.00 68.10  ?  376  PRO A CD  1 
ATOM   2543  N N   . GLY A  1  377 ? 57.025  -21.730 55.718  1.00 64.05  ?  377  GLY A N   1 
ATOM   2544  C CA  . GLY A  1  377 ? 56.844  -22.764 56.720  1.00 63.17  ?  377  GLY A CA  1 
ATOM   2545  C C   . GLY A  1  377 ? 56.136  -22.314 57.980  1.00 60.21  ?  377  GLY A C   1 
ATOM   2546  O O   . GLY A  1  377 ? 55.769  -23.169 58.794  1.00 59.35  ?  377  GLY A O   1 
ATOM   2547  N N   . ILE A  1  378 ? 55.938  -21.007 58.166  1.00 62.33  ?  378  ILE A N   1 
ATOM   2548  C CA  . ILE A  1  378 ? 55.278  -20.521 59.377  1.00 59.63  ?  378  ILE A CA  1 
ATOM   2549  C C   . ILE A  1  378 ? 53.865  -21.082 59.475  1.00 58.26  ?  378  ILE A C   1 
ATOM   2550  O O   . ILE A  1  378 ? 53.443  -21.577 60.528  1.00 56.90  ?  378  ILE A O   1 
ATOM   2551  C CB  . ILE A  1  378 ? 55.275  -18.982 59.410  1.00 58.58  ?  378  ILE A CB  1 
ATOM   2552  C CG1 . ILE A  1  378 ? 56.691  -18.447 59.636  1.00 59.78  ?  378  ILE A CG1 1 
ATOM   2553  C CG2 . ILE A  1  378 ? 54.314  -18.470 60.477  1.00 57.17  ?  378  ILE A CG2 1 
ATOM   2554  C CD1 . ILE A  1  378 ? 56.733  -17.037 60.190  1.00 59.13  ?  378  ILE A CD1 1 
ATOM   2555  N N   . ALA A  1  379 ? 53.114  -21.019 58.377  1.00 60.28  ?  379  ALA A N   1 
ATOM   2556  C CA  . ALA A  1  379 ? 51.746  -21.512 58.336  1.00 59.25  ?  379  ALA A CA  1 
ATOM   2557  C C   . ALA A  1  379 ? 51.647  -22.921 57.757  1.00 61.07  ?  379  ALA A C   1 
ATOM   2558  O O   . ALA A  1  379 ? 50.584  -23.305 57.258  1.00 61.74  ?  379  ALA A O   1 
ATOM   2559  C CB  . ALA A  1  379 ? 50.864  -20.544 57.549  1.00 58.54  ?  379  ALA A CB  1 
ATOM   2560  N N   . ASN A  1  380 ? 52.735  -23.696 57.810  1.00 62.10  ?  380  ASN A N   1 
ATOM   2561  C CA  . ASN A  1  380 ? 52.688  -25.074 57.329  1.00 63.95  ?  380  ASN A CA  1 
ATOM   2562  C C   . ASN A  1  380 ? 51.708  -25.915 58.136  1.00 62.74  ?  380  ASN A C   1 
ATOM   2563  O O   . ASN A  1  380 ? 51.171  -26.904 57.624  1.00 63.92  ?  380  ASN A O   1 
ATOM   2564  C CB  . ASN A  1  380 ? 54.081  -25.707 57.385  1.00 65.96  ?  380  ASN A CB  1 
ATOM   2565  C CG  . ASN A  1  380 ? 54.544  -26.238 56.036  1.00 68.86  ?  380  ASN A CG  1 
ATOM   2566  O OD1 . ASN A  1  380 ? 53.959  -25.923 55.000  1.00 69.40  ?  380  ASN A OD1 1 
ATOM   2567  N ND2 . ASN A  1  380 ? 55.598  -27.056 56.047  1.00 70.85  ?  380  ASN A ND2 1 
ATOM   2568  N N   . SER A  1  381 ? 51.465  -25.542 59.391  1.00 58.16  ?  381  SER A N   1 
ATOM   2569  C CA  . SER A  1  381 ? 50.659  -26.368 60.279  1.00 57.19  ?  381  SER A CA  1 
ATOM   2570  C C   . SER A  1  381 ? 49.195  -26.349 59.857  1.00 56.45  ?  381  SER A C   1 
ATOM   2571  O O   . SER A  1  381 ? 48.602  -25.283 59.669  1.00 55.08  ?  381  SER A O   1 
ATOM   2572  C CB  . SER A  1  381 ? 50.792  -25.877 61.720  1.00 55.15  ?  381  SER A CB  1 
ATOM   2573  O OG  . SER A  1  381 ? 52.151  -25.801 62.113  1.00 55.84  ?  381  SER A OG  1 
ATOM   2574  N N   . THR A  1  382 ? 48.613  -27.541 59.713  1.00 55.94  ?  382  THR A N   1 
ATOM   2575  C CA  . THR A  1  382 ? 47.185  -27.647 59.442  1.00 55.34  ?  382  THR A CA  1 
ATOM   2576  C C   . THR A  1  382 ? 46.345  -27.367 60.681  1.00 53.04  ?  382  THR A C   1 
ATOM   2577  O O   . THR A  1  382 ? 45.143  -27.112 60.556  1.00 52.14  ?  382  THR A O   1 
ATOM   2578  C CB  . THR A  1  382 ? 46.852  -29.031 58.882  1.00 57.42  ?  382  THR A CB  1 
ATOM   2579  O OG1 . THR A  1  382 ? 47.079  -30.026 59.888  1.00 57.61  ?  382  THR A OG1 1 
ATOM   2580  C CG2 . THR A  1  382 ? 47.718  -29.334 57.665  1.00 59.90  ?  382  THR A CG2 1 
ATOM   2581  N N   . GLU A  1  383 ? 46.949  -27.409 61.868  1.00 53.62  ?  383  GLU A N   1 
ATOM   2582  C CA  . GLU A  1  383 ? 46.253  -27.135 63.117  1.00 51.59  ?  383  GLU A CA  1 
ATOM   2583  C C   . GLU A  1  383 ? 46.513  -25.725 63.633  1.00 49.72  ?  383  GLU A C   1 
ATOM   2584  O O   . GLU A  1  383 ? 46.107  -25.402 64.754  1.00 48.09  ?  383  GLU A O   1 
ATOM   2585  C CB  . GLU A  1  383 ? 46.652  -28.162 64.179  1.00 51.95  ?  383  GLU A CB  1 
ATOM   2586  C CG  . GLU A  1  383 ? 45.591  -29.217 64.443  1.00 52.35  ?  383  GLU A CG  1 
ATOM   2587  C CD  . GLU A  1  383 ? 45.652  -30.363 63.453  1.00 54.76  ?  383  GLU A CD  1 
ATOM   2588  O OE1 . GLU A  1  383 ? 46.768  -30.712 63.015  1.00 56.25  ?  383  GLU A OE1 1 
ATOM   2589  O OE2 . GLU A  1  383 ? 44.584  -30.911 63.110  1.00 55.30  -1 383  GLU A OE2 1 
ATOM   2590  N N   . LEU A  1  384 ? 47.191  -24.888 62.849  1.00 45.47  ?  384  LEU A N   1 
ATOM   2591  C CA  . LEU A  1  384 ? 47.384  -23.494 63.229  1.00 43.88  ?  384  LEU A CA  1 
ATOM   2592  C C   . LEU A  1  384 ? 46.039  -22.789 63.354  1.00 42.17  ?  384  LEU A C   1 
ATOM   2593  O O   . LEU A  1  384 ? 45.182  -22.900 62.472  1.00 42.55  ?  384  LEU A O   1 
ATOM   2594  C CB  . LEU A  1  384 ? 48.258  -22.787 62.196  1.00 44.93  ?  384  LEU A CB  1 
ATOM   2595  C CG  . LEU A  1  384 ? 48.671  -21.348 62.511  1.00 43.71  ?  384  LEU A CG  1 
ATOM   2596  C CD1 . LEU A  1  384 ? 49.225  -21.240 63.923  1.00 42.70  ?  384  LEU A CD1 1 
ATOM   2597  C CD2 . LEU A  1  384 ? 49.687  -20.854 61.494  1.00 45.25  ?  384  LEU A CD2 1 
ATOM   2598  N N   . THR A  1  385 ? 45.857  -22.058 64.454  1.00 42.06  ?  385  THR A N   1 
ATOM   2599  C CA  . THR A  1  385 ? 44.594  -21.369 64.690  1.00 40.44  ?  385  THR A CA  1 
ATOM   2600  C C   . THR A  1  385 ? 44.789  -19.888 64.999  1.00 39.05  ?  385  THR A C   1 
ATOM   2601  O O   . THR A  1  385 ? 43.900  -19.075 64.728  1.00 38.05  ?  385  THR A O   1 
ATOM   2602  C CB  . THR A  1  385 ? 43.827  -22.042 65.832  1.00 39.66  ?  385  THR A CB  1 
ATOM   2603  O OG1 . THR A  1  385 ? 44.743  -22.431 66.863  1.00 39.72  ?  385  THR A OG1 1 
ATOM   2604  C CG2 . THR A  1  385 ? 43.089  -23.276 65.326  1.00 40.86  ?  385  THR A CG2 1 
ATOM   2605  N N   . VAL A  1  386 ? 45.941  -19.523 65.561  1.00 38.56  ?  386  VAL A N   1 
ATOM   2606  C CA  . VAL A  1  386 ? 46.219  -18.146 65.961  1.00 37.43  ?  386  VAL A CA  1 
ATOM   2607  C C   . VAL A  1  386 ? 47.621  -17.781 65.496  1.00 38.63  ?  386  VAL A C   1 
ATOM   2608  O O   . VAL A  1  386 ? 48.591  -18.470 65.834  1.00 39.60  ?  386  VAL A O   1 
ATOM   2609  C CB  . VAL A  1  386 ? 46.082  -17.945 67.480  1.00 36.04  ?  386  VAL A CB  1 
ATOM   2610  C CG1 . VAL A  1  386 ? 46.554  -16.559 67.874  1.00 35.20  ?  386  VAL A CG1 1 
ATOM   2611  C CG2 . VAL A  1  386 ? 44.639  -18.155 67.917  1.00 34.92  ?  386  VAL A CG2 1 
ATOM   2612  N N   . LEU A  1  387 ? 47.729  -16.692 64.733  1.00 38.46  ?  387  LEU A N   1 
ATOM   2613  C CA  . LEU A  1  387 ? 48.987  -16.249 64.131  1.00 40.24  ?  387  LEU A CA  1 
ATOM   2614  C C   . LEU A  1  387 ? 49.111  -14.746 64.388  1.00 39.41  ?  387  LEU A C   1 
ATOM   2615  O O   . LEU A  1  387 ? 48.627  -13.934 63.596  1.00 39.72  ?  387  LEU A O   1 
ATOM   2616  C CB  . LEU A  1  387 ? 49.009  -16.594 62.639  1.00 42.48  ?  387  LEU A CB  1 
ATOM   2617  C CG  . LEU A  1  387 ? 50.332  -16.872 61.919  1.00 44.56  ?  387  LEU A CG  1 
ATOM   2618  C CD1 . LEU A  1  387 ? 50.068  -17.349 60.500  1.00 46.22  ?  387  LEU A CD1 1 
ATOM   2619  C CD2 . LEU A  1  387 ? 51.222  -15.657 61.902  1.00 44.83  ?  387  LEU A CD2 1 
ATOM   2620  N N   . GLN A  1  388 ? 49.749  -14.380 65.500  1.00 39.81  ?  388  GLN A N   1 
ATOM   2621  C CA  . GLN A  1  388 ? 49.872  -12.990 65.931  1.00 38.96  ?  388  GLN A CA  1 
ATOM   2622  C C   . GLN A  1  388 ? 51.259  -12.455 65.584  1.00 40.48  ?  388  GLN A C   1 
ATOM   2623  O O   . GLN A  1  388 ? 52.264  -12.955 66.100  1.00 41.31  ?  388  GLN A O   1 
ATOM   2624  C CB  . GLN A  1  388 ? 49.618  -12.870 67.433  1.00 37.50  ?  388  GLN A CB  1 
ATOM   2625  C CG  . GLN A  1  388 ? 48.262  -13.387 67.878  1.00 36.15  ?  388  GLN A CG  1 
ATOM   2626  C CD  . GLN A  1  388 ? 47.269  -12.270 68.129  1.00 34.65  ?  388  GLN A CD  1 
ATOM   2627  O OE1 . GLN A  1  388 ? 47.636  -11.096 68.170  1.00 34.50  ?  388  GLN A OE1 1 
ATOM   2628  N NE2 . GLN A  1  388 ? 46.001  -12.631 68.290  1.00 33.66  ?  388  GLN A NE2 1 
ATOM   2629  N N   . LEU A  1  389 ? 51.312  -11.429 64.723  1.00 41.67  ?  389  LEU A N   1 
ATOM   2630  C CA  . LEU A  1  389 ? 52.580  -10.868 64.267  1.00 42.91  ?  389  LEU A CA  1 
ATOM   2631  C C   . LEU A  1  389 ? 52.665  -9.346  64.353  1.00 42.22  ?  389  LEU A C   1 
ATOM   2632  O O   . LEU A  1  389 ? 53.628  -8.772  63.830  1.00 43.93  ?  389  LEU A O   1 
ATOM   2633  C CB  . LEU A  1  389 ? 52.867  -11.283 62.818  1.00 45.06  ?  389  LEU A CB  1 
ATOM   2634  C CG  . LEU A  1  389 ? 53.011  -12.760 62.471  1.00 46.23  ?  389  LEU A CG  1 
ATOM   2635  C CD1 . LEU A  1  389 ? 53.522  -12.909 61.048  1.00 48.46  ?  389  LEU A CD1 1 
ATOM   2636  C CD2 . LEU A  1  389 ? 53.937  -13.465 63.446  1.00 46.14  ?  389  LEU A CD2 1 
ATOM   2637  N N   . ASP A  1  390 ? 51.702  -8.672  64.982  1.00 45.85  ?  390  ASP A N   1 
ATOM   2638  C CA  . ASP A  1  390 ? 51.696  -7.215  64.942  1.00 45.06  ?  390  ASP A CA  1 
ATOM   2639  C C   . ASP A  1  390 ? 52.911  -6.640  65.669  1.00 45.41  ?  390  ASP A C   1 
ATOM   2640  O O   . ASP A  1  390 ? 53.621  -7.331  66.405  1.00 45.94  ?  390  ASP A O   1 
ATOM   2641  C CB  . ASP A  1  390 ? 50.414  -6.651  65.552  1.00 43.07  ?  390  ASP A CB  1 
ATOM   2642  C CG  . ASP A  1  390 ? 50.288  -6.945  67.034  1.00 41.94  ?  390  ASP A CG  1 
ATOM   2643  O OD1 . ASP A  1  390 ? 50.082  -8.119  67.399  1.00 41.78  ?  390  ASP A OD1 1 
ATOM   2644  O OD2 . ASP A  1  390 ? 50.385  -5.993  67.837  1.00 40.79  -1 390  ASP A OD2 1 
ATOM   2645  N N   . THR A  1  391 ? 53.134  -5.341  65.452  1.00 45.38  ?  391  THR A N   1 
ATOM   2646  C CA  . THR A  1  391 ? 54.219  -4.592  66.085  1.00 46.31  ?  391  THR A CA  1 
ATOM   2647  C C   . THR A  1  391 ? 55.581  -5.222  65.775  1.00 48.42  ?  391  THR A C   1 
ATOM   2648  O O   . THR A  1  391 ? 56.306  -5.684  66.659  1.00 48.68  ?  391  THR A O   1 
ATOM   2649  C CB  . THR A  1  391 ? 53.989  -4.473  67.597  1.00 44.85  ?  391  THR A CB  1 
ATOM   2650  O OG1 . THR A  1  391 ? 52.593  -4.274  67.851  1.00 42.89  ?  391  THR A OG1 1 
ATOM   2651  C CG2 . THR A  1  391 ? 54.768  -3.297  68.166  1.00 45.60  ?  391  THR A CG2 1 
ATOM   2652  N N   . ASN A  1  392 ? 55.913  -5.240  64.484  1.00 50.19  ?  392  ASN A N   1 
ATOM   2653  C CA  . ASN A  1  392 ? 57.163  -5.821  64.016  1.00 51.99  ?  392  ASN A CA  1 
ATOM   2654  C C   . ASN A  1  392 ? 57.600  -5.089  62.751  1.00 54.11  ?  392  ASN A C   1 
ATOM   2655  O O   . ASN A  1  392 ? 56.937  -4.157  62.288  1.00 54.38  ?  392  ASN A O   1 
ATOM   2656  C CB  . ASN A  1  392 ? 57.007  -7.324  63.776  1.00 52.69  ?  392  ASN A CB  1 
ATOM   2657  C CG  . ASN A  1  392 ? 57.447  -8.154  64.967  1.00 52.00  ?  392  ASN A CG  1 
ATOM   2658  O OD1 . ASN A  1  392 ? 58.637  -8.256  65.262  1.00 52.71  ?  392  ASN A OD1 1 
ATOM   2659  N ND2 . ASN A  1  392 ? 56.483  -8.746  65.663  1.00 50.22  ?  392  ASN A ND2 1 
ATOM   2660  N N   . ASN A  1  393 ? 58.730  -5.521  62.192  1.00 56.79  ?  393  ASN A N   1 
ATOM   2661  C CA  . ASN A  1  393 ? 59.361  -4.870  61.047  1.00 58.39  ?  393  ASN A CA  1 
ATOM   2662  C C   . ASN A  1  393 ? 59.500  -5.823  59.862  1.00 60.14  ?  393  ASN A C   1 
ATOM   2663  O O   . ASN A  1  393 ? 60.542  -5.869  59.203  1.00 62.23  ?  393  ASN A O   1 
ATOM   2664  C CB  . ASN A  1  393 ? 60.726  -4.296  61.423  1.00 59.97  ?  393  ASN A CB  1 
ATOM   2665  C CG  . ASN A  1  393 ? 60.638  -3.205  62.475  1.00 59.34  ?  393  ASN A CG  1 
ATOM   2666  O OD1 . ASN A  1  393 ? 59.917  -3.334  63.464  1.00 57.19  ?  393  ASN A OD1 1 
ATOM   2667  N ND2 . ASN A  1  393 ? 61.374  -2.120  62.263  1.00 60.84  ?  393  ASN A ND2 1 
ATOM   2668  N N   . PHE A  1  394 ? 58.455  -6.594  59.570  1.00 58.77  ?  394  PHE A N   1 
ATOM   2669  C CA  . PHE A  1  394 ? 58.537  -7.567  58.492  1.00 59.72  ?  394  PHE A CA  1 
ATOM   2670  C C   . PHE A  1  394 ? 58.335  -6.898  57.134  1.00 60.07  ?  394  PHE A C   1 
ATOM   2671  O O   . PHE A  1  394 ? 57.866  -5.763  57.026  1.00 59.40  ?  394  PHE A O   1 
ATOM   2672  C CB  . PHE A  1  394 ? 57.503  -8.676  58.673  1.00 59.93  ?  394  PHE A CB  1 
ATOM   2673  C CG  . PHE A  1  394 ? 57.848  -9.655  59.752  1.00 59.71  ?  394  PHE A CG  1 
ATOM   2674  C CD1 . PHE A  1  394 ? 57.637  -9.344  61.081  1.00 57.71  ?  394  PHE A CD1 1 
ATOM   2675  C CD2 . PHE A  1  394 ? 58.409  -10.879 59.436  1.00 60.42  ?  394  PHE A CD2 1 
ATOM   2676  C CE1 . PHE A  1  394 ? 57.956  -10.246 62.076  1.00 56.30  ?  394  PHE A CE1 1 
ATOM   2677  C CE2 . PHE A  1  394 ? 58.737  -11.781 60.428  1.00 59.47  ?  394  PHE A CE2 1 
ATOM   2678  C CZ  . PHE A  1  394 ? 58.506  -11.467 61.747  1.00 57.03  ?  394  PHE A CZ  1 
ATOM   2679  N N   . THR A  1  395 ? 58.696  -7.635  56.083  1.00 58.92  ?  395  THR A N   1 
ATOM   2680  C CA  . THR A  1  395 ? 58.616  -7.154  54.712  1.00 60.62  ?  395  THR A CA  1 
ATOM   2681  C C   . THR A  1  395 ? 58.144  -8.284  53.806  1.00 61.23  ?  395  THR A C   1 
ATOM   2682  O O   . THR A  1  395 ? 58.208  -9.462  54.163  1.00 61.03  ?  395  THR A O   1 
ATOM   2683  C CB  . THR A  1  395 ? 59.970  -6.624  54.206  1.00 63.64  ?  395  THR A CB  1 
ATOM   2684  O OG1 . THR A  1  395 ? 60.957  -7.659  54.302  1.00 65.31  ?  395  THR A OG1 1 
ATOM   2685  C CG2 . THR A  1  395 ? 60.425  -5.409  55.010  1.00 63.32  ?  395  THR A CG2 1 
ATOM   2686  N N   . GLY A  1  396 ? 57.658  -7.906  52.630  1.00 61.92  ?  396  GLY A N   1 
ATOM   2687  C CA  . GLY A  1  396 ? 57.348  -8.866  51.588  1.00 63.13  ?  396  GLY A CA  1 
ATOM   2688  C C   . GLY A  1  396 ? 55.907  -9.341  51.590  1.00 60.91  ?  396  GLY A C   1 
ATOM   2689  O O   . GLY A  1  396 ? 55.011  -8.752  52.202  1.00 58.47  ?  396  GLY A O   1 
ATOM   2690  N N   . PHE A  1  397 ? 55.693  -10.448 50.885  1.00 63.77  ?  397  PHE A N   1 
ATOM   2691  C CA  . PHE A  1  397 ? 54.366  -10.998 50.652  1.00 62.29  ?  397  PHE A CA  1 
ATOM   2692  C C   . PHE A  1  397 ? 53.993  -12.008 51.735  1.00 60.50  ?  397  PHE A C   1 
ATOM   2693  O O   . PHE A  1  397 ? 54.842  -12.508 52.477  1.00 60.84  ?  397  PHE A O   1 
ATOM   2694  C CB  . PHE A  1  397 ? 54.283  -11.674 49.278  1.00 64.56  ?  397  PHE A CB  1 
ATOM   2695  C CG  . PHE A  1  397 ? 54.345  -10.724 48.105  1.00 66.17  ?  397  PHE A CG  1 
ATOM   2696  C CD1 . PHE A  1  397 ? 54.804  -9.423  48.248  1.00 66.21  ?  397  PHE A CD1 1 
ATOM   2697  C CD2 . PHE A  1  397 ? 53.938  -11.145 46.849  1.00 67.80  ?  397  PHE A CD2 1 
ATOM   2698  C CE1 . PHE A  1  397 ? 54.857  -8.569  47.163  1.00 67.82  ?  397  PHE A CE1 1 
ATOM   2699  C CE2 . PHE A  1  397 ? 53.987  -10.292 45.762  1.00 69.38  ?  397  PHE A CE2 1 
ATOM   2700  C CZ  . PHE A  1  397 ? 54.446  -9.003  45.920  1.00 69.39  ?  397  PHE A CZ  1 
ATOM   2701  N N   . LEU A  1  398 ? 52.690  -12.301 51.818  1.00 61.34  ?  398  LEU A N   1 
ATOM   2702  C CA  . LEU A  1  398 ? 52.214  -13.379 52.675  1.00 59.97  ?  398  LEU A CA  1 
ATOM   2703  C C   . LEU A  1  398 ? 52.345  -14.718 51.951  1.00 61.89  ?  398  LEU A C   1 
ATOM   2704  O O   . LEU A  1  398 ? 52.132  -14.792 50.737  1.00 63.47  ?  398  LEU A O   1 
ATOM   2705  C CB  . LEU A  1  398 ? 50.758  -13.147 53.078  1.00 57.63  ?  398  LEU A CB  1 
ATOM   2706  C CG  . LEU A  1  398 ? 50.445  -12.024 54.072  1.00 55.46  ?  398  LEU A CG  1 
ATOM   2707  C CD1 . LEU A  1  398 ? 49.239  -12.393 54.922  1.00 53.90  ?  398  LEU A CD1 1 
ATOM   2708  C CD2 . LEU A  1  398 ? 51.645  -11.714 54.954  1.00 56.00  ?  398  LEU A CD2 1 
ATOM   2709  N N   . PRO A  1  399 ? 52.694  -15.787 52.662  1.00 61.61  ?  399  PRO A N   1 
ATOM   2710  C CA  . PRO A  1  399 ? 52.855  -17.085 52.000  1.00 63.59  ?  399  PRO A CA  1 
ATOM   2711  C C   . PRO A  1  399 ? 51.510  -17.699 51.651  1.00 62.85  ?  399  PRO A C   1 
ATOM   2712  O O   . PRO A  1  399 ? 50.501  -17.472 52.323  1.00 60.50  ?  399  PRO A O   1 
ATOM   2713  C CB  . PRO A  1  399 ? 53.598  -17.937 53.036  1.00 63.57  ?  399  PRO A CB  1 
ATOM   2714  C CG  . PRO A  1  399 ? 53.446  -17.240 54.331  1.00 61.07  ?  399  PRO A CG  1 
ATOM   2715  C CD  . PRO A  1  399 ? 52.957  -15.843 54.109  1.00 59.92  ?  399  PRO A CD  1 
ATOM   2716  N N   . ASP A  1  400 ? 51.508  -18.498 50.583  1.00 65.99  ?  400  ASP A N   1 
ATOM   2717  C CA  . ASP A  1  400 ? 50.285  -19.146 50.128  1.00 65.74  ?  400  ASP A CA  1 
ATOM   2718  C C   . ASP A  1  400 ? 49.821  -20.262 51.056  1.00 64.72  ?  400  ASP A C   1 
ATOM   2719  O O   . ASP A  1  400 ? 48.712  -20.774 50.873  1.00 64.26  ?  400  ASP A O   1 
ATOM   2720  C CB  . ASP A  1  400 ? 50.481  -19.694 48.713  1.00 69.09  ?  400  ASP A CB  1 
ATOM   2721  C CG  . ASP A  1  400 ? 50.692  -18.595 47.689  1.00 69.91  ?  400  ASP A CG  1 
ATOM   2722  O OD1 . ASP A  1  400 ? 49.690  -18.094 47.137  1.00 69.50  ?  400  ASP A OD1 1 
ATOM   2723  O OD2 . ASP A  1  400 ? 51.860  -18.231 47.439  1.00 71.56  -1 400  ASP A OD2 1 
ATOM   2724  N N   . THR A  1  401 ? 50.635  -20.654 52.034  1.00 61.78  ?  401  THR A N   1 
ATOM   2725  C CA  . THR A  1  401 ? 50.267  -21.662 53.020  1.00 60.80  ?  401  THR A CA  1 
ATOM   2726  C C   . THR A  1  401 ? 49.457  -21.090 54.181  1.00 57.82  ?  401  THR A C   1 
ATOM   2727  O O   . THR A  1  401 ? 49.305  -21.776 55.197  1.00 56.89  ?  401  THR A O   1 
ATOM   2728  C CB  . THR A  1  401 ? 51.521  -22.355 53.562  1.00 61.98  ?  401  THR A CB  1 
ATOM   2729  O OG1 . THR A  1  401 ? 52.386  -21.382 54.162  1.00 61.25  ?  401  THR A OG1 1 
ATOM   2730  C CG2 . THR A  1  401 ? 52.267  -23.062 52.440  1.00 65.12  ?  401  THR A CG2 1 
ATOM   2731  N N   . ILE A  1  402 ? 48.916  -19.876 54.031  1.00 59.60  ?  402  ILE A N   1 
ATOM   2732  C CA  . ILE A  1  402 ? 48.483  -19.084 55.183  1.00 57.66  ?  402  ILE A CA  1 
ATOM   2733  C C   . ILE A  1  402 ? 47.395  -19.802 55.978  1.00 57.72  ?  402  ILE A C   1 
ATOM   2734  O O   . ILE A  1  402 ? 47.439  -19.843 57.214  1.00 57.91  ?  402  ILE A O   1 
ATOM   2735  C CB  . ILE A  1  402 ? 48.036  -17.679 54.729  1.00 57.82  ?  402  ILE A CB  1 
ATOM   2736  C CG1 . ILE A  1  402 ? 47.634  -16.830 55.937  1.00 56.21  ?  402  ILE A CG1 1 
ATOM   2737  C CG2 . ILE A  1  402 ? 46.920  -17.752 53.687  1.00 58.00  ?  402  ILE A CG2 1 
ATOM   2738  C CD1 . ILE A  1  402 ? 48.797  -16.455 56.830  1.00 56.44  ?  402  ILE A CD1 1 
ATOM   2739  N N   . CYS A  1  403 ? 46.410  -20.378 55.296  1.00 54.37  ?  403  CYS A N   1 
ATOM   2740  C CA  . CYS A  1  403 ? 45.323  -21.110 55.941  1.00 53.65  ?  403  CYS A CA  1 
ATOM   2741  C C   . CYS A  1  403 ? 45.210  -22.504 55.337  1.00 55.05  ?  403  CYS A C   1 
ATOM   2742  O O   . CYS A  1  403 ? 44.127  -22.982 54.993  1.00 55.17  ?  403  CYS A O   1 
ATOM   2743  C CB  . CYS A  1  403 ? 44.000  -20.354 55.838  1.00 54.21  ?  403  CYS A CB  1 
ATOM   2744  S SG  . CYS A  1  403 ? 42.702  -21.000 56.928  1.00 53.31  ?  403  CYS A SG  1 
ATOM   2745  N N   . ARG A  1  404 ? 46.364  -23.162 55.192  1.00 50.58  ?  404  ARG A N   1 
ATOM   2746  C CA  . ARG A  1  404 ? 46.431  -24.463 54.531  1.00 52.86  ?  404  ARG A CA  1 
ATOM   2747  C C   . ARG A  1  404 ? 45.479  -25.469 55.168  1.00 52.39  ?  404  ARG A C   1 
ATOM   2748  O O   . ARG A  1  404 ? 44.749  -26.181 54.470  1.00 53.61  ?  404  ARG A O   1 
ATOM   2749  C CB  . ARG A  1  404 ? 47.866  -24.989 54.565  1.00 54.57  ?  404  ARG A CB  1 
ATOM   2750  C CG  . ARG A  1  404 ? 48.076  -26.260 53.761  1.00 57.27  ?  404  ARG A CG  1 
ATOM   2751  C CD  . ARG A  1  404 ? 49.553  -26.587 53.620  1.00 59.15  ?  404  ARG A CD  1 
ATOM   2752  N NE  . ARG A  1  404 ? 50.035  -27.410 54.723  1.00 58.93  ?  404  ARG A NE  1 
ATOM   2753  C CZ  . ARG A  1  404 ? 51.217  -28.011 54.746  1.00 60.68  ?  404  ARG A CZ  1 
ATOM   2754  N NH1 . ARG A  1  404 ? 52.067  -27.904 53.738  1.00 62.88  ?  404  ARG A NH1 1 
ATOM   2755  N NH2 . ARG A  1  404 ? 51.554  -28.739 55.807  1.00 60.31  ?  404  ARG A NH2 1 
ATOM   2756  N N   . GLY A  1  405 ? 45.476  -25.544 56.498  1.00 49.19  ?  405  GLY A N   1 
ATOM   2757  C CA  . GLY A  1  405 ? 44.613  -26.490 57.179  1.00 48.85  ?  405  GLY A CA  1 
ATOM   2758  C C   . GLY A  1  405 ? 43.164  -26.075 57.289  1.00 47.35  ?  405  GLY A C   1 
ATOM   2759  O O   . GLY A  1  405 ? 42.334  -26.885 57.711  1.00 47.37  ?  405  GLY A O   1 
ATOM   2760  N N   . GLY A  1  406 ? 42.841  -24.836 56.924  1.00 50.34  ?  406  GLY A N   1 
ATOM   2761  C CA  . GLY A  1  406 ? 41.469  -24.373 56.993  1.00 48.96  ?  406  GLY A CA  1 
ATOM   2762  C C   . GLY A  1  406 ? 40.946  -24.157 58.392  1.00 46.88  ?  406  GLY A C   1 
ATOM   2763  O O   . GLY A  1  406 ? 39.728  -24.138 58.592  1.00 46.07  ?  406  GLY A O   1 
ATOM   2764  N N   . LYS A  1  407 ? 41.833  -23.983 59.370  1.00 47.68  ?  407  LYS A N   1 
ATOM   2765  C CA  . LYS A  1  407 ? 41.441  -23.850 60.763  1.00 45.91  ?  407  LYS A CA  1 
ATOM   2766  C C   . LYS A  1  407 ? 41.882  -22.534 61.391  1.00 44.14  ?  407  LYS A C   1 
ATOM   2767  O O   . LYS A  1  407 ? 41.603  -22.311 62.573  1.00 42.68  ?  407  LYS A O   1 
ATOM   2768  C CB  . LYS A  1  407 ? 42.007  -25.017 61.586  1.00 46.66  ?  407  LYS A CB  1 
ATOM   2769  C CG  . LYS A  1  407 ? 41.846  -26.376 60.927  1.00 48.81  ?  407  LYS A CG  1 
ATOM   2770  C CD  . LYS A  1  407 ? 42.085  -27.505 61.916  1.00 49.29  ?  407  LYS A CD  1 
ATOM   2771  C CE  . LYS A  1  407 ? 42.273  -28.831 61.196  1.00 51.75  ?  407  LYS A CE  1 
ATOM   2772  N NZ  . LYS A  1  407 ? 42.756  -29.901 62.110  1.00 52.41  ?  407  LYS A NZ  1 
ATOM   2773  N N   . LEU A  1  408 ? 42.573  -21.671 60.647  1.00 41.72  ?  408  LEU A N   1 
ATOM   2774  C CA  . LEU A  1  408 ? 43.043  -20.407 61.199  1.00 40.28  ?  408  LEU A CA  1 
ATOM   2775  C C   . LEU A  1  408 ? 41.873  -19.543 61.654  1.00 38.38  ?  408  LEU A C   1 
ATOM   2776  O O   . LEU A  1  408 ? 40.926  -19.307 60.897  1.00 38.35  ?  408  LEU A O   1 
ATOM   2777  C CB  . LEU A  1  408 ? 43.882  -19.662 60.163  1.00 41.20  ?  408  LEU A CB  1 
ATOM   2778  C CG  . LEU A  1  408 ? 44.624  -18.424 60.671  1.00 40.19  ?  408  LEU A CG  1 
ATOM   2779  C CD1 . LEU A  1  408 ? 45.775  -18.823 61.578  1.00 40.47  ?  408  LEU A CD1 1 
ATOM   2780  C CD2 . LEU A  1  408 ? 45.124  -17.588 59.504  1.00 41.12  ?  408  LEU A CD2 1 
ATOM   2781  N N   . GLU A  1  409 ? 41.947  -19.068 62.898  1.00 40.27  ?  409  GLU A N   1 
ATOM   2782  C CA  . GLU A  1  409 ? 40.917  -18.230 63.500  1.00 38.09  ?  409  GLU A CA  1 
ATOM   2783  C C   . GLU A  1  409 ? 41.328  -16.770 63.603  1.00 38.12  ?  409  GLU A C   1 
ATOM   2784  O O   . GLU A  1  409 ? 40.600  -15.883 63.145  1.00 38.16  ?  409  GLU A O   1 
ATOM   2785  C CB  . GLU A  1  409 ? 40.559  -18.753 64.898  1.00 36.09  ?  409  GLU A CB  1 
ATOM   2786  C CG  . GLU A  1  409 ? 40.287  -20.241 64.978  1.00 37.21  ?  409  GLU A CG  1 
ATOM   2787  C CD  . GLU A  1  409 ? 39.477  -20.599 66.207  1.00 36.33  ?  409  GLU A CD  1 
ATOM   2788  O OE1 . GLU A  1  409 ? 39.513  -19.824 67.187  1.00 34.98  ?  409  GLU A OE1 1 
ATOM   2789  O OE2 . GLU A  1  409 ? 38.806  -21.651 66.199  1.00 37.12  -1 409  GLU A OE2 1 
ATOM   2790  N N   . ASN A  1  410 ? 42.485  -16.496 64.200  1.00 35.53  ?  410  ASN A N   1 
ATOM   2791  C CA  . ASN A  1  410 ? 42.907  -15.142 64.528  1.00 34.62  ?  410  ASN A CA  1 
ATOM   2792  C C   . ASN A  1  410 ? 44.252  -14.874 63.861  1.00 35.92  ?  410  ASN A C   1 
ATOM   2793  O O   . ASN A  1  410 ? 45.246  -15.542 64.171  1.00 36.82  ?  410  ASN A O   1 
ATOM   2794  C CB  . ASN A  1  410 ? 42.991  -14.955 66.054  1.00 33.42  ?  410  ASN A CB  1 
ATOM   2795  C CG  . ASN A  1  410 ? 41.706  -15.404 66.791  1.00 32.44  ?  410  ASN A CG  1 
ATOM   2796  O OD1 . ASN A  1  410 ? 40.606  -15.285 66.256  1.00 32.12  ?  410  ASN A OD1 1 
ATOM   2797  N ND2 . ASN A  1  410 ? 41.852  -15.914 68.026  1.00 32.07  ?  410  ASN A ND2 1 
ATOM   2798  N N   . LEU A  1  411 ? 44.278  -13.907 62.941  1.00 35.74  ?  411  LEU A N   1 
ATOM   2799  C CA  . LEU A  1  411 ? 45.481  -13.515 62.213  1.00 37.13  ?  411  LEU A CA  1 
ATOM   2800  C C   . LEU A  1  411 ? 45.733  -12.030 62.430  1.00 36.39  ?  411  LEU A C   1 
ATOM   2801  O O   . LEU A  1  411 ? 44.823  -11.211 62.260  1.00 35.37  ?  411  LEU A O   1 
ATOM   2802  C CB  . LEU A  1  411 ? 45.354  -13.811 60.714  1.00 38.58  ?  411  LEU A CB  1 
ATOM   2803  C CG  . LEU A  1  411 ? 46.481  -13.250 59.842  1.00 40.15  ?  411  LEU A CG  1 
ATOM   2804  C CD1 . LEU A  1  411 ? 47.810  -13.921 60.172  1.00 41.44  ?  411  LEU A CD1 1 
ATOM   2805  C CD2 . LEU A  1  411 ? 46.148  -13.400 58.366  1.00 41.47  ?  411  LEU A CD2 1 
ATOM   2806  N N   . THR A  1  412 ? 46.969  -11.687 62.791  1.00 41.50  ?  412  THR A N   1 
ATOM   2807  C CA  . THR A  1  412 ? 47.301  -10.344 63.257  1.00 40.49  ?  412  THR A CA  1 
ATOM   2808  C C   . THR A  1  412 ? 48.600  -9.880  62.610  1.00 42.19  ?  412  THR A C   1 
ATOM   2809  O O   . THR A  1  412 ? 49.639  -10.522 62.787  1.00 43.12  ?  412  THR A O   1 
ATOM   2810  C CB  . THR A  1  412 ? 47.412  -10.331 64.784  1.00 38.59  ?  412  THR A CB  1 
ATOM   2811  O OG1 . THR A  1  412 ? 46.099  -10.391 65.354  1.00 37.30  ?  412  THR A OG1 1 
ATOM   2812  C CG2 . THR A  1  412 ? 48.067  -9.070  65.246  1.00 38.03  ?  412  THR A CG2 1 
ATOM   2813  N N   . LEU A  1  413 ? 48.546  -8.772  61.857  1.00 40.22  ?  413  LEU A N   1 
ATOM   2814  C CA  . LEU A  1  413 ? 49.695  -8.292  61.088  1.00 42.11  ?  413  LEU A CA  1 
ATOM   2815  C C   . LEU A  1  413 ? 49.905  -6.784  61.219  1.00 41.91  ?  413  LEU A C   1 
ATOM   2816  O O   . LEU A  1  413 ? 50.487  -6.164  60.325  1.00 43.40  ?  413  LEU A O   1 
ATOM   2817  C CB  . LEU A  1  413 ? 49.550  -8.659  59.611  1.00 43.53  ?  413  LEU A CB  1 
ATOM   2818  C CG  . LEU A  1  413 ? 49.275  -10.111 59.227  1.00 44.07  ?  413  LEU A CG  1 
ATOM   2819  C CD1 . LEU A  1  413 ? 48.459  -10.167 57.945  1.00 44.56  ?  413  LEU A CD1 1 
ATOM   2820  C CD2 . LEU A  1  413 ? 50.576  -10.877 59.067  1.00 46.02  ?  413  LEU A CD2 1 
ATOM   2821  N N   . ASP A  1  414 ? 49.449  -6.176  62.313  1.00 43.54  ?  414  ASP A N   1 
ATOM   2822  C CA  . ASP A  1  414 ? 49.419  -4.719  62.396  1.00 43.15  ?  414  ASP A CA  1 
ATOM   2823  C C   . ASP A  1  414 ? 50.819  -4.115  62.374  1.00 44.85  ?  414  ASP A C   1 
ATOM   2824  O O   . ASP A  1  414 ? 51.790  -4.718  62.839  1.00 45.69  ?  414  ASP A O   1 
ATOM   2825  C CB  . ASP A  1  414 ? 48.695  -4.262  63.661  1.00 41.19  ?  414  ASP A CB  1 
ATOM   2826  C CG  . ASP A  1  414 ? 47.281  -4.764  63.727  1.00 39.62  ?  414  ASP A CG  1 
ATOM   2827  O OD1 . ASP A  1  414 ? 46.911  -5.561  62.846  1.00 40.06  ?  414  ASP A OD1 1 
ATOM   2828  O OD2 . ASP A  1  414 ? 46.542  -4.355  64.645  1.00 38.10  -1 414  ASP A OD2 1 
ATOM   2829  N N   . ASP A  1  415 ? 50.905  -2.903  61.817  1.00 48.12  ?  415  ASP A N   1 
ATOM   2830  C CA  . ASP A  1  415 ? 52.083  -2.041  61.932  1.00 49.79  ?  415  ASP A CA  1 
ATOM   2831  C C   . ASP A  1  415 ? 53.352  -2.748  61.449  1.00 53.14  ?  415  ASP A C   1 
ATOM   2832  O O   . ASP A  1  415 ? 54.295  -2.992  62.205  1.00 54.08  ?  415  ASP A O   1 
ATOM   2833  C CB  . ASP A  1  415 ? 52.237  -1.521  63.364  1.00 48.40  ?  415  ASP A CB  1 
ATOM   2834  C CG  . ASP A  1  415 ? 51.064  -0.659  63.794  1.00 46.69  ?  415  ASP A CG  1 
ATOM   2835  O OD1 . ASP A  1  415 ? 50.765  0.332   63.092  1.00 46.31  ?  415  ASP A OD1 1 
ATOM   2836  O OD2 . ASP A  1  415 ? 50.437  -0.971  64.829  1.00 45.42  -1 415  ASP A OD2 1 
ATOM   2837  N N   . ASN A  1  416 ? 53.350  -3.080  60.162  1.00 52.01  ?  416  ASN A N   1 
ATOM   2838  C CA  . ASN A  1  416 ? 54.452  -3.786  59.528  1.00 54.54  ?  416  ASN A CA  1 
ATOM   2839  C C   . ASN A  1  416 ? 54.667  -3.171  58.150  1.00 55.09  ?  416  ASN A C   1 
ATOM   2840  O O   . ASN A  1  416 ? 54.127  -2.107  57.831  1.00 55.22  ?  416  ASN A O   1 
ATOM   2841  C CB  . ASN A  1  416 ? 54.160  -5.291  59.452  1.00 55.01  ?  416  ASN A CB  1 
ATOM   2842  C CG  . ASN A  1  416 ? 54.602  -6.035  60.696  1.00 55.34  ?  416  ASN A CG  1 
ATOM   2843  O OD1 . ASN A  1  416 ? 55.746  -6.480  60.792  1.00 57.09  ?  416  ASN A OD1 1 
ATOM   2844  N ND2 . ASN A  1  416 ? 53.695  -6.177  61.655  1.00 53.12  ?  416  ASN A ND2 1 
ATOM   2845  N N   . HIS A  1  417 ? 55.472  -3.837  57.329  1.00 55.81  ?  417  HIS A N   1 
ATOM   2846  C CA  . HIS A  1  417 ? 55.758  -3.390  55.971  1.00 58.36  ?  417  HIS A CA  1 
ATOM   2847  C C   . HIS A  1  417 ? 55.462  -4.507  54.983  1.00 58.79  ?  417  HIS A C   1 
ATOM   2848  O O   . HIS A  1  417 ? 56.235  -4.799  54.069  1.00 62.21  ?  417  HIS A O   1 
ATOM   2849  C CB  . HIS A  1  417 ? 57.199  -2.904  55.846  1.00 61.44  ?  417  HIS A CB  1 
ATOM   2850  C CG  . HIS A  1  417 ? 57.539  -1.787  56.782  1.00 60.59  ?  417  HIS A CG  1 
ATOM   2851  N ND1 . HIS A  1  417 ? 57.047  -0.509  56.623  1.00 59.87  ?  417  HIS A ND1 1 
ATOM   2852  C CD2 . HIS A  1  417 ? 58.318  -1.755  57.889  1.00 60.04  ?  417  HIS A CD2 1 
ATOM   2853  C CE1 . HIS A  1  417 ? 57.509  0.262   57.591  1.00 59.66  ?  417  HIS A CE1 1 
ATOM   2854  N NE2 . HIS A  1  417 ? 58.283  -0.470  58.373  1.00 59.84  ?  417  HIS A NE2 1 
ATOM   2855  N N   . PHE A  1  418 ? 54.314  -5.151  55.173  1.00 55.60  ?  418  PHE A N   1 
ATOM   2856  C CA  . PHE A  1  418 ? 53.845  -6.143  54.222  1.00 56.23  ?  418  PHE A CA  1 
ATOM   2857  C C   . PHE A  1  418 ? 53.313  -5.459  52.970  1.00 57.02  ?  418  PHE A C   1 
ATOM   2858  O O   . PHE A  1  418 ? 52.793  -4.340  53.016  1.00 56.06  ?  418  PHE A O   1 
ATOM   2859  C CB  . PHE A  1  418 ? 52.750  -7.009  54.842  1.00 53.96  ?  418  PHE A CB  1 
ATOM   2860  C CG  . PHE A  1  418 ? 53.259  -8.015  55.831  1.00 53.63  ?  418  PHE A CG  1 
ATOM   2861  C CD1 . PHE A  1  418 ? 54.073  -9.057  55.423  1.00 55.54  ?  418  PHE A CD1 1 
ATOM   2862  C CD2 . PHE A  1  418 ? 52.916  -7.922  57.170  1.00 51.49  ?  418  PHE A CD2 1 
ATOM   2863  C CE1 . PHE A  1  418 ? 54.540  -9.986  56.332  1.00 55.28  ?  418  PHE A CE1 1 
ATOM   2864  C CE2 . PHE A  1  418 ? 53.379  -8.848  58.084  1.00 51.24  ?  418  PHE A CE2 1 
ATOM   2865  C CZ  . PHE A  1  418 ? 54.192  -9.882  57.665  1.00 53.11  ?  418  PHE A CZ  1 
ATOM   2866  N N   . GLU A  1  419 ? 53.455  -6.144  51.841  1.00 59.87  ?  419  GLU A N   1 
ATOM   2867  C CA  . GLU A  1  419 ? 52.997  -5.638  50.559  1.00 60.93  ?  419  GLU A CA  1 
ATOM   2868  C C   . GLU A  1  419 ? 52.499  -6.816  49.730  1.00 61.63  ?  419  GLU A C   1 
ATOM   2869  O O   . GLU A  1  419 ? 52.531  -7.969  50.171  1.00 61.31  ?  419  GLU A O   1 
ATOM   2870  C CB  . GLU A  1  419 ? 54.113  -4.841  49.866  1.00 63.60  ?  419  GLU A CB  1 
ATOM   2871  C CG  . GLU A  1  419 ? 54.992  -5.636  48.917  1.00 66.59  ?  419  GLU A CG  1 
ATOM   2872  C CD  . GLU A  1  419 ? 56.209  -4.856  48.461  1.00 69.28  ?  419  GLU A CD  1 
ATOM   2873  O OE1 . GLU A  1  419 ? 56.495  -3.798  49.059  1.00 68.78  ?  419  GLU A OE1 1 
ATOM   2874  O OE2 . GLU A  1  419 ? 56.879  -5.298  47.503  1.00 72.40  -1 419  GLU A OE2 1 
ATOM   2875  N N   . GLY A  1  420 ? 52.015  -6.521  48.527  1.00 61.65  ?  420  GLY A N   1 
ATOM   2876  C CA  . GLY A  1  420 ? 51.502  -7.543  47.649  1.00 62.52  ?  420  GLY A CA  1 
ATOM   2877  C C   . GLY A  1  420 ? 50.066  -7.900  47.969  1.00 60.07  ?  420  GLY A C   1 
ATOM   2878  O O   . GLY A  1  420 ? 49.428  -7.297  48.837  1.00 57.68  ?  420  GLY A O   1 
ATOM   2879  N N   . PRO A  1  421 ? 49.533  -8.906  47.278  1.00 59.64  ?  421  PRO A N   1 
ATOM   2880  C CA  . PRO A  1  421 ? 48.107  -9.221  47.420  1.00 57.66  ?  421  PRO A CA  1 
ATOM   2881  C C   . PRO A  1  421 ? 47.818  -10.202 48.544  1.00 56.03  ?  421  PRO A C   1 
ATOM   2882  O O   . PRO A  1  421 ? 48.733  -10.699 49.208  1.00 56.42  ?  421  PRO A O   1 
ATOM   2883  C CB  . PRO A  1  421 ? 47.759  -9.823  46.056  1.00 59.63  ?  421  PRO A CB  1 
ATOM   2884  C CG  . PRO A  1  421 ? 49.023  -10.522 45.651  1.00 62.29  ?  421  PRO A CG  1 
ATOM   2885  C CD  . PRO A  1  421 ? 50.176  -9.728  46.237  1.00 62.54  ?  421  PRO A CD  1 
ATOM   2886  N N   . VAL A  1  422 ? 46.540  -10.477 48.760  1.00 56.54  ?  422  VAL A N   1 
ATOM   2887  C CA  . VAL A  1  422 ? 46.128  -11.476 49.748  1.00 55.16  ?  422  VAL A CA  1 
ATOM   2888  C C   . VAL A  1  422 ? 46.168  -12.854 49.094  1.00 56.96  ?  422  VAL A C   1 
ATOM   2889  O O   . VAL A  1  422 ? 45.613  -13.026 47.997  1.00 58.43  ?  422  VAL A O   1 
ATOM   2890  C CB  . VAL A  1  422 ? 44.734  -11.160 50.281  1.00 52.72  ?  422  VAL A CB  1 
ATOM   2891  C CG1 . VAL A  1  422 ? 44.500  -11.868 51.606  1.00 51.09  ?  422  VAL A CG1 1 
ATOM   2892  C CG2 . VAL A  1  422 ? 44.556  -9.657  50.440  1.00 51.52  ?  422  VAL A CG2 1 
ATOM   2893  N N   . PRO A  1  423 ? 46.819  -13.840 49.711  1.00 57.98  ?  423  PRO A N   1 
ATOM   2894  C CA  . PRO A  1  423 ? 46.911  -15.165 49.088  1.00 60.32  ?  423  PRO A CA  1 
ATOM   2895  C C   . PRO A  1  423 ? 45.540  -15.798 48.910  1.00 59.71  ?  423  PRO A C   1 
ATOM   2896  O O   . PRO A  1  423 ? 44.619  -15.576 49.700  1.00 57.30  ?  423  PRO A O   1 
ATOM   2897  C CB  . PRO A  1  423 ? 47.771  -15.965 50.075  1.00 59.98  ?  423  PRO A CB  1 
ATOM   2898  C CG  . PRO A  1  423 ? 48.491  -14.937 50.884  1.00 58.86  ?  423  PRO A CG  1 
ATOM   2899  C CD  . PRO A  1  423 ? 47.559  -13.771 50.981  1.00 56.93  ?  423  PRO A CD  1 
ATOM   2900  N N   . LYS A  1  424 ? 45.412  -16.587 47.839  1.00 60.40  ?  424  LYS A N   1 
ATOM   2901  C CA  . LYS A  1  424 ? 44.145  -17.252 47.546  1.00 60.16  ?  424  LYS A CA  1 
ATOM   2902  C C   . LYS A  1  424 ? 43.708  -18.153 48.694  1.00 58.80  ?  424  LYS A C   1 
ATOM   2903  O O   . LYS A  1  424 ? 42.507  -18.370 48.891  1.00 57.67  ?  424  LYS A O   1 
ATOM   2904  C CB  . LYS A  1  424 ? 44.259  -18.067 46.253  1.00 63.02  ?  424  LYS A CB  1 
ATOM   2905  C CG  . LYS A  1  424 ? 44.838  -17.335 45.035  1.00 64.94  ?  424  LYS A CG  1 
ATOM   2906  C CD  . LYS A  1  424 ? 44.451  -15.861 44.969  1.00 63.40  ?  424  LYS A CD  1 
ATOM   2907  C CE  . LYS A  1  424 ? 44.251  -15.411 43.530  1.00 65.23  ?  424  LYS A CE  1 
ATOM   2908  N NZ  . LYS A  1  424 ? 43.953  -13.957 43.434  1.00 63.93  ?  424  LYS A NZ  1 
ATOM   2909  N N   . SER A  1  425 ? 44.667  -18.686 49.457  1.00 60.99  ?  425  SER A N   1 
ATOM   2910  C CA  . SER A  1  425 ? 44.335  -19.522 50.606  1.00 59.89  ?  425  SER A CA  1 
ATOM   2911  C C   . SER A  1  425 ? 43.642  -18.726 51.705  1.00 56.76  ?  425  SER A C   1 
ATOM   2912  O O   . SER A  1  425 ? 42.827  -19.282 52.449  1.00 56.39  ?  425  SER A O   1 
ATOM   2913  C CB  . SER A  1  425 ? 45.599  -20.185 51.152  1.00 60.58  ?  425  SER A CB  1 
ATOM   2914  O OG  . SER A  1  425 ? 46.309  -20.853 50.124  1.00 64.15  ?  425  SER A OG  1 
ATOM   2915  N N   . LEU A  1  426 ? 43.959  -17.435 51.831  1.00 55.36  ?  426  LEU A N   1 
ATOM   2916  C CA  . LEU A  1  426 ? 43.288  -16.592 52.813  1.00 53.74  ?  426  LEU A CA  1 
ATOM   2917  C C   . LEU A  1  426 ? 41.890  -16.192 52.358  1.00 53.08  ?  426  LEU A C   1 
ATOM   2918  O O   . LEU A  1  426 ? 40.989  -16.052 53.192  1.00 52.26  ?  426  LEU A O   1 
ATOM   2919  C CB  . LEU A  1  426 ? 44.124  -15.344 53.100  1.00 53.11  ?  426  LEU A CB  1 
ATOM   2920  C CG  . LEU A  1  426 ? 43.823  -14.617 54.413  1.00 51.57  ?  426  LEU A CG  1 
ATOM   2921  C CD1 . LEU A  1  426 ? 43.436  -15.603 55.505  1.00 51.69  ?  426  LEU A CD1 1 
ATOM   2922  C CD2 . LEU A  1  426 ? 45.017  -13.782 54.843  1.00 51.35  ?  426  LEU A CD2 1 
ATOM   2923  N N   . ARG A  1  427 ? 41.697  -15.992 51.052  1.00 54.09  ?  427  ARG A N   1 
ATOM   2924  C CA  . ARG A  1  427 ? 40.371  -15.665 50.536  1.00 53.80  ?  427  ARG A CA  1 
ATOM   2925  C C   . ARG A  1  427 ? 39.375  -16.781 50.829  1.00 54.68  ?  427  ARG A C   1 
ATOM   2926  O O   . ARG A  1  427 ? 38.235  -16.517 51.231  1.00 53.95  ?  427  ARG A O   1 
ATOM   2927  C CB  . ARG A  1  427 ? 40.451  -15.389 49.033  1.00 54.58  ?  427  ARG A CB  1 
ATOM   2928  C CG  . ARG A  1  427 ? 39.108  -15.361 48.316  1.00 54.50  ?  427  ARG A CG  1 
ATOM   2929  C CD  . ARG A  1  427 ? 39.288  -15.222 46.809  1.00 56.69  ?  427  ARG A CD  1 
ATOM   2930  N NE  . ARG A  1  427 ? 39.171  -16.500 46.116  1.00 58.97  ?  427  ARG A NE  1 
ATOM   2931  C CZ  . ARG A  1  427 ? 39.936  -16.874 45.100  1.00 61.80  ?  427  ARG A CZ  1 
ATOM   2932  N NH1 . ARG A  1  427 ? 40.890  -16.088 44.627  1.00 62.65  ?  427  ARG A NH1 1 
ATOM   2933  N NH2 . ARG A  1  427 ? 39.741  -18.066 44.543  1.00 63.23  ?  427  ARG A NH2 1 
ATOM   2934  N N   . ASP A  1  428 ? 39.788  -18.033 50.644  1.00 54.14  ?  428  ASP A N   1 
ATOM   2935  C CA  . ASP A  1  428 ? 38.910  -19.181 50.826  1.00 54.56  ?  428  ASP A CA  1 
ATOM   2936  C C   . ASP A  1  428 ? 38.900  -19.712 52.255  1.00 54.63  ?  428  ASP A C   1 
ATOM   2937  O O   . ASP A  1  428 ? 38.127  -20.629 52.552  1.00 55.57  ?  428  ASP A O   1 
ATOM   2938  C CB  . ASP A  1  428 ? 39.314  -20.306 49.866  1.00 56.65  ?  428  ASP A CB  1 
ATOM   2939  C CG  . ASP A  1  428 ? 39.587  -19.805 48.459  1.00 58.30  ?  428  ASP A CG  1 
ATOM   2940  O OD1 . ASP A  1  428 ? 38.994  -18.780 48.062  1.00 57.40  ?  428  ASP A OD1 1 
ATOM   2941  O OD2 . ASP A  1  428 ? 40.394  -20.441 47.749  1.00 60.58  -1 428  ASP A OD2 1 
ATOM   2942  N N   . CYS A  1  429 ? 39.733  -19.170 53.141  1.00 52.70  ?  429  CYS A N   1 
ATOM   2943  C CA  . CYS A  1  429 ? 39.788  -19.612 54.535  1.00 53.00  ?  429  CYS A CA  1 
ATOM   2944  C C   . CYS A  1  429 ? 38.549  -19.111 55.269  1.00 52.26  ?  429  CYS A C   1 
ATOM   2945  O O   . CYS A  1  429 ? 38.477  -17.948 55.670  1.00 51.03  ?  429  CYS A O   1 
ATOM   2946  C CB  . CYS A  1  429 ? 41.065  -19.109 55.198  1.00 52.67  ?  429  CYS A CB  1 
ATOM   2947  S SG  . CYS A  1  429 ? 41.252  -19.575 56.935  1.00 53.45  ?  429  CYS A SG  1 
ATOM   2948  N N   . LYS A  1  430 ? 37.569  -19.996 55.462  1.00 53.21  ?  430  LYS A N   1 
ATOM   2949  C CA  . LYS A  1  430 ? 36.283  -19.617 56.036  1.00 51.92  ?  430  LYS A CA  1 
ATOM   2950  C C   . LYS A  1  430 ? 36.284  -19.560 57.560  1.00 49.40  ?  430  LYS A C   1 
ATOM   2951  O O   . LYS A  1  430 ? 35.299  -19.092 58.141  1.00 47.43  ?  430  LYS A O   1 
ATOM   2952  C CB  . LYS A  1  430 ? 35.195  -20.592 55.574  1.00 50.89  ?  430  LYS A CB  1 
ATOM   2953  C CG  . LYS A  1  430 ? 35.246  -20.938 54.095  1.00 53.00  ?  430  LYS A CG  1 
ATOM   2954  C CD  . LYS A  1  430 ? 34.087  -21.841 53.703  1.00 52.36  ?  430  LYS A CD  1 
ATOM   2955  C CE  . LYS A  1  430 ? 33.209  -21.194 52.645  1.00 53.84  ?  430  LYS A CE  1 
ATOM   2956  N NZ  . LYS A  1  430 ? 32.362  -22.197 51.941  1.00 53.50  ?  430  LYS A NZ  1 
ATOM   2957  N N   . SER A  1  431 ? 37.346  -20.016 58.219  1.00 47.03  ?  431  SER A N   1 
ATOM   2958  C CA  . SER A  1  431 ? 37.360  -20.144 59.671  1.00 44.31  ?  431  SER A CA  1 
ATOM   2959  C C   . SER A  1  431 ? 37.885  -18.902 60.385  1.00 43.81  ?  431  SER A C   1 
ATOM   2960  O O   . SER A  1  431 ? 38.167  -18.970 61.586  1.00 41.54  ?  431  SER A O   1 
ATOM   2961  C CB  . SER A  1  431 ? 38.192  -21.361 60.082  1.00 44.30  ?  431  SER A CB  1 
ATOM   2962  O OG  . SER A  1  431 ? 39.535  -21.234 59.649  1.00 45.66  ?  431  SER A OG  1 
ATOM   2963  N N   . LEU A  1  432 ? 38.021  -17.777 59.686  1.00 40.60  ?  432  LEU A N   1 
ATOM   2964  C CA  . LEU A  1  432 ? 38.576  -16.578 60.299  1.00 39.28  ?  432  LEU A CA  1 
ATOM   2965  C C   . LEU A  1  432 ? 37.620  -16.000 61.338  1.00 37.45  ?  432  LEU A C   1 
ATOM   2966  O O   . LEU A  1  432 ? 36.397  -16.053 61.183  1.00 37.10  ?  432  LEU A O   1 
ATOM   2967  C CB  . LEU A  1  432 ? 38.887  -15.533 59.229  1.00 39.58  ?  432  LEU A CB  1 
ATOM   2968  C CG  . LEU A  1  432 ? 40.068  -15.860 58.313  1.00 41.41  ?  432  LEU A CG  1 
ATOM   2969  C CD1 . LEU A  1  432 ? 40.251  -14.783 57.255  1.00 41.79  ?  432  LEU A CD1 1 
ATOM   2970  C CD2 . LEU A  1  432 ? 41.342  -16.042 59.124  1.00 41.56  ?  432  LEU A CD2 1 
ATOM   2971  N N   . ILE A  1  433 ? 38.192  -15.447 62.408  1.00 35.92  ?  433  ILE A N   1 
ATOM   2972  C CA  . ILE A  1  433 ? 37.418  -14.819 63.475  1.00 33.07  ?  433  ILE A CA  1 
ATOM   2973  C C   . ILE A  1  433 ? 37.872  -13.377 63.660  1.00 34.68  ?  433  ILE A C   1 
ATOM   2974  O O   . ILE A  1  433 ? 37.058  -12.448 63.612  1.00 33.27  ?  433  ILE A O   1 
ATOM   2975  C CB  . ILE A  1  433 ? 37.539  -15.605 64.792  1.00 33.57  ?  433  ILE A CB  1 
ATOM   2976  C CG1 . ILE A  1  433 ? 36.991  -17.024 64.620  1.00 33.81  ?  433  ILE A CG1 1 
ATOM   2977  C CG2 . ILE A  1  433 ? 36.829  -14.872 65.920  1.00 31.35  ?  433  ILE A CG2 1 
ATOM   2978  C CD1 . ILE A  1  433 ? 36.896  -17.803 65.912  1.00 33.46  ?  433  ILE A CD1 1 
ATOM   2979  N N   . ARG A  1  434 ? 39.168  -13.180 63.891  1.00 36.10  ?  434  ARG A N   1 
ATOM   2980  C CA  . ARG A  1  434 ? 39.760  -11.851 63.987  1.00 35.52  ?  434  ARG A CA  1 
ATOM   2981  C C   . ARG A  1  434 ? 40.846  -11.722 62.931  1.00 37.87  ?  434  ARG A C   1 
ATOM   2982  O O   . ARG A  1  434 ? 41.790  -12.520 62.904  1.00 39.42  ?  434  ARG A O   1 
ATOM   2983  C CB  . ARG A  1  434 ? 40.332  -11.588 65.382  1.00 33.73  ?  434  ARG A CB  1 
ATOM   2984  C CG  . ARG A  1  434 ? 39.371  -10.870 66.318  1.00 30.79  ?  434  ARG A CG  1 
ATOM   2985  C CD  . ARG A  1  434 ? 40.010  -10.576 67.668  1.00 29.57  ?  434  ARG A CD  1 
ATOM   2986  N NE  . ARG A  1  434 ? 40.728  -9.306  67.675  1.00 29.43  ?  434  ARG A NE  1 
ATOM   2987  C CZ  . ARG A  1  434 ? 40.238  -8.173  68.160  1.00 28.43  ?  434  ARG A CZ  1 
ATOM   2988  N NH1 . ARG A  1  434 ? 39.016  -8.108  68.664  1.00 27.46  ?  434  ARG A NH1 1 
ATOM   2989  N NH2 . ARG A  1  434 ? 40.991  -7.077  68.137  1.00 28.56  ?  434  ARG A NH2 1 
ATOM   2990  N N   . VAL A  1  435 ? 40.713  -10.718 62.068  1.00 34.96  ?  435  VAL A N   1 
ATOM   2991  C CA  . VAL A  1  435 ? 41.691  -10.418 61.031  1.00 36.38  ?  435  VAL A CA  1 
ATOM   2992  C C   . VAL A  1  435 ? 42.149  -8.981  61.228  1.00 35.90  ?  435  VAL A C   1 
ATOM   2993  O O   . VAL A  1  435 ? 41.321  -8.078  61.393  1.00 34.75  ?  435  VAL A O   1 
ATOM   2994  C CB  . VAL A  1  435 ? 41.110  -10.621 59.620  1.00 37.30  ?  435  VAL A CB  1 
ATOM   2995  C CG1 . VAL A  1  435 ? 42.223  -10.654 58.592  1.00 39.15  ?  435  VAL A CG1 1 
ATOM   2996  C CG2 . VAL A  1  435 ? 40.300  -11.902 59.561  1.00 37.49  ?  435  VAL A CG2 1 
ATOM   2997  N N   . ARG A  1  436 ? 43.463  -8.772  61.230  1.00 39.47  ?  436  ARG A N   1 
ATOM   2998  C CA  . ARG A  1  436 ? 44.028  -7.450  61.495  1.00 38.52  ?  436  ARG A CA  1 
ATOM   2999  C C   . ARG A  1  436 ? 45.160  -7.197  60.504  1.00 40.38  ?  436  ARG A C   1 
ATOM   3000  O O   . ARG A  1  436 ? 46.278  -7.689  60.687  1.00 41.47  ?  436  ARG A O   1 
ATOM   3001  C CB  . ARG A  1  436 ? 44.508  -7.353  62.936  1.00 37.73  ?  436  ARG A CB  1 
ATOM   3002  C CG  . ARG A  1  436 ? 43.396  -7.408  63.966  1.00 35.98  ?  436  ARG A CG  1 
ATOM   3003  C CD  . ARG A  1  436 ? 43.736  -6.575  65.185  1.00 35.17  ?  436  ARG A CD  1 
ATOM   3004  N NE  . ARG A  1  436 ? 44.085  -5.200  64.849  1.00 35.41  ?  436  ARG A NE  1 
ATOM   3005  C CZ  . ARG A  1  436 ? 43.506  -4.132  65.380  1.00 34.36  ?  436  ARG A CZ  1 
ATOM   3006  N NH1 . ARG A  1  436 ? 42.529  -4.243  66.265  1.00 32.99  ?  436  ARG A NH1 1 
ATOM   3007  N NH2 . ARG A  1  436 ? 43.918  -2.921  65.014  1.00 34.83  ?  436  ARG A NH2 1 
ATOM   3008  N N   . PHE A  1  437 ? 44.863  -6.426  59.458  1.00 37.55  ?  437  PHE A N   1 
ATOM   3009  C CA  . PHE A  1  437 ? 45.828  -6.047  58.434  1.00 39.45  ?  437  PHE A CA  1 
ATOM   3010  C C   . PHE A  1  437 ? 46.352  -4.626  58.618  1.00 39.54  ?  437  PHE A C   1 
ATOM   3011  O O   . PHE A  1  437 ? 47.066  -4.125  57.743  1.00 41.17  ?  437  PHE A O   1 
ATOM   3012  C CB  . PHE A  1  437 ? 45.202  -6.186  57.043  1.00 40.26  ?  437  PHE A CB  1 
ATOM   3013  C CG  . PHE A  1  437 ? 45.243  -7.584  56.485  1.00 41.33  ?  437  PHE A CG  1 
ATOM   3014  C CD1 . PHE A  1  437 ? 45.095  -8.687  57.309  1.00 40.69  ?  437  PHE A CD1 1 
ATOM   3015  C CD2 . PHE A  1  437 ? 45.416  -7.791  55.126  1.00 43.11  ?  437  PHE A CD2 1 
ATOM   3016  C CE1 . PHE A  1  437 ? 45.129  -9.968  56.788  1.00 41.82  ?  437  PHE A CE1 1 
ATOM   3017  C CE2 . PHE A  1  437 ? 45.451  -9.068  54.601  1.00 44.26  ?  437  PHE A CE2 1 
ATOM   3018  C CZ  . PHE A  1  437 ? 45.307  -10.158 55.434  1.00 43.61  ?  437  PHE A CZ  1 
ATOM   3019  N N   . LYS A  1  438 ? 46.007  -3.973  59.728  1.00 41.05  ?  438  LYS A N   1 
ATOM   3020  C CA  . LYS A  1  438 ? 46.200  -2.534  59.871  1.00 40.61  ?  438  LYS A CA  1 
ATOM   3021  C C   . LYS A  1  438 ? 47.658  -2.128  59.679  1.00 42.84  ?  438  LYS A C   1 
ATOM   3022  O O   . LYS A  1  438 ? 48.580  -2.843  60.077  1.00 43.72  ?  438  LYS A O   1 
ATOM   3023  C CB  . LYS A  1  438 ? 45.710  -2.080  61.248  1.00 38.85  ?  438  LYS A CB  1 
ATOM   3024  C CG  . LYS A  1  438 ? 45.411  -0.592  61.349  1.00 38.35  ?  438  LYS A CG  1 
ATOM   3025  C CD  . LYS A  1  438 ? 45.156  -0.177  62.790  1.00 36.97  ?  438  LYS A CD  1 
ATOM   3026  C CE  . LYS A  1  438 ? 44.220  1.019   62.866  1.00 36.33  ?  438  LYS A CE  1 
ATOM   3027  N NZ  . LYS A  1  438 ? 44.848  2.262   62.345  1.00 37.68  ?  438  LYS A NZ  1 
ATOM   3028  N N   . GLY A  1  439 ? 47.858  -0.970  59.052  1.00 43.72  ?  439  GLY A N   1 
ATOM   3029  C CA  . GLY A  1  439 ? 49.177  -0.381  58.917  1.00 45.17  ?  439  GLY A CA  1 
ATOM   3030  C C   . GLY A  1  439 ? 50.154  -1.171  58.071  1.00 47.25  ?  439  GLY A C   1 
ATOM   3031  O O   . GLY A  1  439 ? 51.169  -1.657  58.578  1.00 48.04  ?  439  GLY A O   1 
ATOM   3032  N N   . ASN A  1  440 ? 49.865  -1.296  56.780  1.00 47.93  ?  440  ASN A N   1 
ATOM   3033  C CA  . ASN A  1  440 ? 50.723  -2.026  55.855  1.00 50.16  ?  440  ASN A CA  1 
ATOM   3034  C C   . ASN A  1  440 ? 50.600  -1.379  54.480  1.00 51.63  ?  440  ASN A C   1 
ATOM   3035  O O   . ASN A  1  440 ? 50.082  -0.267  54.342  1.00 51.08  ?  440  ASN A O   1 
ATOM   3036  C CB  . ASN A  1  440 ? 50.355  -3.515  55.831  1.00 49.73  ?  440  ASN A CB  1 
ATOM   3037  C CG  . ASN A  1  440 ? 50.947  -4.281  56.996  1.00 49.25  ?  440  ASN A CG  1 
ATOM   3038  O OD1 . ASN A  1  440 ? 52.126  -4.635  56.986  1.00 50.92  ?  440  ASN A OD1 1 
ATOM   3039  N ND2 . ASN A  1  440 ? 50.130  -4.543  58.008  1.00 47.08  ?  440  ASN A ND2 1 
ATOM   3040  N N   . SER A  1  441 ? 51.092  -2.074  53.459  1.00 51.75  ?  441  SER A N   1 
ATOM   3041  C CA  . SER A  1  441 ? 50.984  -1.630  52.074  1.00 53.38  ?  441  SER A CA  1 
ATOM   3042  C C   . SER A  1  441 ? 50.370  -2.723  51.212  1.00 53.68  ?  441  SER A C   1 
ATOM   3043  O O   . SER A  1  441 ? 50.778  -2.946  50.068  1.00 55.89  ?  441  SER A O   1 
ATOM   3044  C CB  . SER A  1  441 ? 52.342  -1.200  51.524  1.00 56.21  ?  441  SER A CB  1 
ATOM   3045  O OG  . SER A  1  441 ? 52.743  0.046   52.069  1.00 56.19  ?  441  SER A OG  1 
ATOM   3046  N N   . PHE A  1  442 ? 49.378  -3.424  51.758  1.00 50.92  ?  442  PHE A N   1 
ATOM   3047  C CA  . PHE A  1  442 ? 48.673  -4.452  51.004  1.00 51.12  ?  442  PHE A CA  1 
ATOM   3048  C C   . PHE A  1  442 ? 47.952  -3.836  49.811  1.00 51.68  ?  442  PHE A C   1 
ATOM   3049  O O   . PHE A  1  442 ? 47.510  -2.685  49.848  1.00 50.84  ?  442  PHE A O   1 
ATOM   3050  C CB  . PHE A  1  442 ? 47.670  -5.176  51.900  1.00 48.76  ?  442  PHE A CB  1 
ATOM   3051  C CG  . PHE A  1  442 ? 48.295  -6.177  52.828  1.00 48.59  ?  442  PHE A CG  1 
ATOM   3052  C CD1 . PHE A  1  442 ? 48.977  -7.274  52.329  1.00 50.42  ?  442  PHE A CD1 1 
ATOM   3053  C CD2 . PHE A  1  442 ? 48.199  -6.021  54.201  1.00 46.71  ?  442  PHE A CD2 1 
ATOM   3054  C CE1 . PHE A  1  442 ? 49.550  -8.199  53.183  1.00 50.31  ?  442  PHE A CE1 1 
ATOM   3055  C CE2 . PHE A  1  442 ? 48.770  -6.941  55.060  1.00 46.60  ?  442  PHE A CE2 1 
ATOM   3056  C CZ  . PHE A  1  442 ? 49.445  -8.031  54.550  1.00 48.37  ?  442  PHE A CZ  1 
ATOM   3057  N N   . SER A  1  443 ? 47.831  -4.620  48.743  1.00 48.28  ?  443  SER A N   1 
ATOM   3058  C CA  . SER A  1  443 ? 47.264  -4.138  47.494  1.00 49.23  ?  443  SER A CA  1 
ATOM   3059  C C   . SER A  1  443 ? 46.312  -5.181  46.928  1.00 49.09  ?  443  SER A C   1 
ATOM   3060  O O   . SER A  1  443 ? 46.247  -6.321  47.396  1.00 48.67  ?  443  SER A O   1 
ATOM   3061  C CB  . SER A  1  443 ? 48.360  -3.808  46.473  1.00 52.22  ?  443  SER A CB  1 
ATOM   3062  O OG  . SER A  1  443 ? 49.304  -4.861  46.387  1.00 53.94  ?  443  SER A OG  1 
ATOM   3063  N N   . GLY A  1  444 ? 45.563  -4.771  45.914  1.00 52.73  ?  444  GLY A N   1 
ATOM   3064  C CA  . GLY A  1  444 ? 44.638  -5.642  45.219  1.00 52.93  ?  444  GLY A CA  1 
ATOM   3065  C C   . GLY A  1  444 ? 43.211  -5.126  45.282  1.00 50.91  ?  444  GLY A C   1 
ATOM   3066  O O   . GLY A  1  444 ? 42.882  -4.186  46.003  1.00 49.12  ?  444  GLY A O   1 
ATOM   3067  N N   . ASP A  1  445 ? 42.360  -5.783  44.498  1.00 54.46  ?  445  ASP A N   1 
ATOM   3068  C CA  . ASP A  1  445 ? 40.946  -5.438  44.446  1.00 52.82  ?  445  ASP A CA  1 
ATOM   3069  C C   . ASP A  1  445 ? 40.255  -5.992  45.685  1.00 50.49  ?  445  ASP A C   1 
ATOM   3070  O O   . ASP A  1  445 ? 40.286  -7.203  45.930  1.00 50.75  ?  445  ASP A O   1 
ATOM   3071  C CB  . ASP A  1  445 ? 40.307  -5.988  43.172  1.00 54.34  ?  445  ASP A CB  1 
ATOM   3072  C CG  . ASP A  1  445 ? 38.971  -5.342  42.861  1.00 53.12  ?  445  ASP A CG  1 
ATOM   3073  O OD1 . ASP A  1  445 ? 37.962  -5.718  43.495  1.00 51.33  ?  445  ASP A OD1 1 
ATOM   3074  O OD2 . ASP A  1  445 ? 38.929  -4.457  41.981  1.00 54.04  -1 445  ASP A OD2 1 
ATOM   3075  N N   . ILE A  1  446 ? 39.637  -5.104  46.469  1.00 51.81  ?  446  ILE A N   1 
ATOM   3076  C CA  . ILE A  1  446 ? 39.058  -5.506  47.748  1.00 49.67  ?  446  ILE A CA  1 
ATOM   3077  C C   . ILE A  1  446 ? 37.966  -6.552  47.555  1.00 49.43  ?  446  ILE A C   1 
ATOM   3078  O O   . ILE A  1  446 ? 37.788  -7.437  48.401  1.00 48.62  ?  446  ILE A O   1 
ATOM   3079  C CB  . ILE A  1  446 ? 38.545  -4.267  48.514  1.00 47.65  ?  446  ILE A CB  1 
ATOM   3080  C CG1 . ILE A  1  446 ? 38.272  -4.614  49.979  1.00 45.69  ?  446  ILE A CG1 1 
ATOM   3081  C CG2 . ILE A  1  446 ? 37.312  -3.672  47.845  1.00 47.15  ?  446  ILE A CG2 1 
ATOM   3082  C CD1 . ILE A  1  446 ? 39.521  -4.692  50.829  1.00 45.82  ?  446  ILE A CD1 1 
ATOM   3083  N N   . SER A  1  447 ? 37.227  -6.483  46.445  1.00 52.63  ?  447  SER A N   1 
ATOM   3084  C CA  . SER A  1  447 ? 36.208  -7.486  46.164  1.00 52.54  ?  447  SER A CA  1 
ATOM   3085  C C   . SER A  1  447 ? 36.800  -8.778  45.620  1.00 54.78  ?  447  SER A C   1 
ATOM   3086  O O   . SER A  1  447 ? 36.151  -9.827  45.707  1.00 54.96  ?  447  SER A O   1 
ATOM   3087  C CB  . SER A  1  447 ? 35.183  -6.932  45.172  1.00 52.62  ?  447  SER A CB  1 
ATOM   3088  O OG  . SER A  1  447 ? 35.725  -6.862  43.864  1.00 56.08  ?  447  SER A OG  1 
ATOM   3089  N N   . GLU A  1  448 ? 38.010  -8.726  45.069  1.00 54.71  ?  448  GLU A N   1 
ATOM   3090  C CA  . GLU A  1  448 ? 38.700  -9.907  44.571  1.00 56.70  ?  448  GLU A CA  1 
ATOM   3091  C C   . GLU A  1  448 ? 39.624  -10.535 45.608  1.00 56.36  ?  448  GLU A C   1 
ATOM   3092  O O   . GLU A  1  448 ? 40.053  -11.678 45.421  1.00 57.83  ?  448  GLU A O   1 
ATOM   3093  C CB  . GLU A  1  448 ? 39.507  -9.551  43.316  1.00 59.12  ?  448  GLU A CB  1 
ATOM   3094  C CG  . GLU A  1  448 ? 39.002  -10.200 42.037  1.00 61.68  ?  448  GLU A CG  1 
ATOM   3095  C CD  . GLU A  1  448 ? 39.567  -9.545  40.789  1.00 63.99  ?  448  GLU A CD  1 
ATOM   3096  O OE1 . GLU A  1  448 ? 40.663  -8.952  40.870  1.00 64.18  ?  448  GLU A OE1 1 
ATOM   3097  O OE2 . GLU A  1  448 ? 38.914  -9.622  39.726  1.00 64.98  -1 448  GLU A OE2 1 
ATOM   3098  N N   . ALA A  1  449 ? 39.936  -9.818  46.688  1.00 50.79  ?  449  ALA A N   1 
ATOM   3099  C CA  . ALA A  1  449 ? 40.901  -10.277 47.680  1.00 50.55  ?  449  ALA A CA  1 
ATOM   3100  C C   . ALA A  1  449 ? 40.287  -11.191 48.734  1.00 49.10  ?  449  ALA A C   1 
ATOM   3101  O O   . ALA A  1  449 ? 40.910  -12.184 49.125  1.00 49.78  ?  449  ALA A O   1 
ATOM   3102  C CB  . ALA A  1  449 ? 41.561  -9.076  48.362  1.00 49.52  ?  449  ALA A CB  1 
ATOM   3103  N N   . PHE A  1  450 ? 39.084  -10.880 49.206  1.00 48.61  ?  450  PHE A N   1 
ATOM   3104  C CA  . PHE A  1  450 ? 38.463  -11.600 50.309  1.00 47.97  ?  450  PHE A CA  1 
ATOM   3105  C C   . PHE A  1  450 ? 37.241  -12.370 49.829  1.00 48.45  ?  450  PHE A C   1 
ATOM   3106  O O   . PHE A  1  450 ? 36.473  -11.882 48.994  1.00 48.41  ?  450  PHE A O   1 
ATOM   3107  C CB  . PHE A  1  450 ? 38.051  -10.641 51.430  1.00 46.09  ?  450  PHE A CB  1 
ATOM   3108  C CG  . PHE A  1  450 ? 39.193  -9.865  52.016  1.00 45.55  ?  450  PHE A CG  1 
ATOM   3109  C CD1 . PHE A  1  450 ? 39.967  -10.404 53.028  1.00 45.55  ?  450  PHE A CD1 1 
ATOM   3110  C CD2 . PHE A  1  450 ? 39.491  -8.595  51.555  1.00 45.11  ?  450  PHE A CD2 1 
ATOM   3111  C CE1 . PHE A  1  450 ? 41.019  -9.691  53.570  1.00 45.17  ?  450  PHE A CE1 1 
ATOM   3112  C CE2 . PHE A  1  450 ? 40.541  -7.877  52.091  1.00 44.74  ?  450  PHE A CE2 1 
ATOM   3113  C CZ  . PHE A  1  450 ? 41.306  -8.426  53.100  1.00 44.79  ?  450  PHE A CZ  1 
ATOM   3114  N N   . GLY A  1  451 ? 37.067  -13.576 50.366  1.00 46.84  ?  451  GLY A N   1 
ATOM   3115  C CA  . GLY A  1  451 ? 35.884  -14.366 50.091  1.00 47.84  ?  451  GLY A CA  1 
ATOM   3116  C C   . GLY A  1  451 ? 34.802  -14.146 51.129  1.00 46.90  ?  451  GLY A C   1 
ATOM   3117  O O   . GLY A  1  451 ? 34.622  -13.026 51.615  1.00 45.80  ?  451  GLY A O   1 
ATOM   3118  N N   . VAL A  1  452 ? 34.075  -15.204 51.478  1.00 46.61  ?  452  VAL A N   1 
ATOM   3119  C CA  . VAL A  1  452 ? 33.040  -15.145 52.504  1.00 44.91  ?  452  VAL A CA  1 
ATOM   3120  C C   . VAL A  1  452 ? 33.582  -15.772 53.780  1.00 44.31  ?  452  VAL A C   1 
ATOM   3121  O O   . VAL A  1  452 ? 34.355  -16.738 53.734  1.00 45.60  ?  452  VAL A O   1 
ATOM   3122  C CB  . VAL A  1  452 ? 31.750  -15.851 52.044  1.00 45.63  ?  452  VAL A CB  1 
ATOM   3123  C CG1 . VAL A  1  452 ? 30.953  -14.945 51.115  1.00 45.52  ?  452  VAL A CG1 1 
ATOM   3124  C CG2 . VAL A  1  452 ? 32.079  -17.171 51.362  1.00 47.89  ?  452  VAL A CG2 1 
ATOM   3125  N N   . TYR A  1  453 ? 33.178  -15.220 54.923  1.00 45.41  ?  453  TYR A N   1 
ATOM   3126  C CA  . TYR A  1  453 ? 33.653  -15.678 56.228  1.00 44.51  ?  453  TYR A CA  1 
ATOM   3127  C C   . TYR A  1  453 ? 32.470  -15.744 57.183  1.00 42.17  ?  453  TYR A C   1 
ATOM   3128  O O   . TYR A  1  453 ? 32.114  -14.747 57.825  1.00 40.54  ?  453  TYR A O   1 
ATOM   3129  C CB  . TYR A  1  453 ? 34.749  -14.762 56.773  1.00 43.42  ?  453  TYR A CB  1 
ATOM   3130  C CG  . TYR A  1  453 ? 35.820  -14.422 55.762  1.00 44.37  ?  453  TYR A CG  1 
ATOM   3131  C CD1 . TYR A  1  453 ? 36.801  -15.344 55.424  1.00 45.78  ?  453  TYR A CD1 1 
ATOM   3132  C CD2 . TYR A  1  453 ? 35.847  -13.180 55.139  1.00 43.21  ?  453  TYR A CD2 1 
ATOM   3133  C CE1 . TYR A  1  453 ? 37.781  -15.041 54.499  1.00 45.84  ?  453  TYR A CE1 1 
ATOM   3134  C CE2 . TYR A  1  453 ? 36.823  -12.867 54.211  1.00 43.67  ?  453  TYR A CE2 1 
ATOM   3135  C CZ  . TYR A  1  453 ? 37.787  -13.802 53.896  1.00 44.93  ?  453  TYR A CZ  1 
ATOM   3136  O OH  . TYR A  1  453 ? 38.762  -13.498 52.974  1.00 45.61  ?  453  TYR A OH  1 
ATOM   3137  N N   . PRO A  1  454 ? 31.830  -16.911 57.301  1.00 45.21  ?  454  PRO A N   1 
ATOM   3138  C CA  . PRO A  1  454 ? 30.630  -17.005 58.150  1.00 42.53  ?  454  PRO A CA  1 
ATOM   3139  C C   . PRO A  1  454 ? 30.904  -16.809 59.631  1.00 39.62  ?  454  PRO A C   1 
ATOM   3140  O O   . PRO A  1  454 ? 29.981  -16.434 60.366  1.00 37.15  ?  454  PRO A O   1 
ATOM   3141  C CB  . PRO A  1  454 ? 30.101  -18.421 57.867  1.00 42.13  ?  454  PRO A CB  1 
ATOM   3142  C CG  . PRO A  1  454 ? 30.894  -18.935 56.691  1.00 45.77  ?  454  PRO A CG  1 
ATOM   3143  C CD  . PRO A  1  454 ? 32.195  -18.207 56.710  1.00 47.16  ?  454  PRO A CD  1 
ATOM   3144  N N   . THR A  1  455 ? 32.132  -17.039 60.094  1.00 39.07  ?  455  THR A N   1 
ATOM   3145  C CA  . THR A  1  455 ? 32.478  -16.908 61.502  1.00 37.92  ?  455  THR A CA  1 
ATOM   3146  C C   . THR A  1  455 ? 33.276  -15.644 61.794  1.00 36.73  ?  455  THR A C   1 
ATOM   3147  O O   . THR A  1  455 ? 33.816  -15.505 62.896  1.00 35.96  ?  455  THR A O   1 
ATOM   3148  C CB  . THR A  1  455 ? 33.260  -18.136 61.975  1.00 38.91  ?  455  THR A CB  1 
ATOM   3149  O OG1 . THR A  1  455 ? 34.365  -18.372 61.093  1.00 40.08  ?  455  THR A OG1 1 
ATOM   3150  C CG2 . THR A  1  455 ? 32.362  -19.363 61.991  1.00 39.99  ?  455  THR A CG2 1 
ATOM   3151  N N   . LEU A  1  456 ? 33.362  -14.725 60.835  1.00 38.73  ?  456  LEU A N   1 
ATOM   3152  C CA  . LEU A  1  456 ? 34.149  -13.515 61.026  1.00 37.71  ?  456  LEU A CA  1 
ATOM   3153  C C   . LEU A  1  456 ? 33.495  -12.616 62.066  1.00 34.15  ?  456  LEU A C   1 
ATOM   3154  O O   . LEU A  1  456 ? 32.283  -12.378 62.028  1.00 32.90  ?  456  LEU A O   1 
ATOM   3155  C CB  . LEU A  1  456 ? 34.307  -12.767 59.703  1.00 39.78  ?  456  LEU A CB  1 
ATOM   3156  C CG  . LEU A  1  456 ? 35.327  -11.628 59.712  1.00 38.87  ?  456  LEU A CG  1 
ATOM   3157  C CD1 . LEU A  1  456 ? 36.703  -12.150 60.095  1.00 39.80  ?  456  LEU A CD1 1 
ATOM   3158  C CD2 . LEU A  1  456 ? 35.369  -10.937 58.359  1.00 40.30  ?  456  LEU A CD2 1 
ATOM   3159  N N   . ASN A  1  457 ? 34.303  -12.119 62.998  1.00 36.97  ?  457  ASN A N   1 
ATOM   3160  C CA  . ASN A  1  457 ? 33.830  -11.279 64.091  1.00 34.04  ?  457  ASN A CA  1 
ATOM   3161  C C   . ASN A  1  457 ? 34.417  -9.879  64.041  1.00 33.43  ?  457  ASN A C   1 
ATOM   3162  O O   . ASN A  1  457 ? 33.680  -8.896  64.187  1.00 32.06  ?  457  ASN A O   1 
ATOM   3163  C CB  . ASN A  1  457 ? 34.161  -11.938 65.440  1.00 33.25  ?  457  ASN A CB  1 
ATOM   3164  C CG  . ASN A  1  457 ? 33.921  -11.011 66.616  1.00 32.11  ?  457  ASN A CG  1 
ATOM   3165  O OD1 . ASN A  1  457 ? 34.831  -10.319 67.073  1.00 31.63  ?  457  ASN A OD1 1 
ATOM   3166  N ND2 . ASN A  1  457 ? 32.691  -10.996 67.116  1.00 31.60  ?  457  ASN A ND2 1 
ATOM   3167  N N   . PHE A  1  458 ? 35.727  -9.758  63.836  1.00 32.36  ?  458  PHE A N   1 
ATOM   3168  C CA  . PHE A  1  458 ? 36.408  -8.472  63.849  1.00 31.89  ?  458  PHE A CA  1 
ATOM   3169  C C   . PHE A  1  458 ? 37.415  -8.452  62.710  1.00 34.67  ?  458  PHE A C   1 
ATOM   3170  O O   . PHE A  1  458 ? 38.193  -9.397  62.553  1.00 36.51  ?  458  PHE A O   1 
ATOM   3171  C CB  . PHE A  1  458 ? 37.111  -8.240  65.195  1.00 30.46  ?  458  PHE A CB  1 
ATOM   3172  C CG  . PHE A  1  458 ? 37.643  -6.843  65.383  1.00 29.76  ?  458  PHE A CG  1 
ATOM   3173  C CD1 . PHE A  1  458 ? 38.780  -6.415  64.716  1.00 31.00  ?  458  PHE A CD1 1 
ATOM   3174  C CD2 . PHE A  1  458 ? 37.017  -5.968  66.254  1.00 28.59  ?  458  PHE A CD2 1 
ATOM   3175  C CE1 . PHE A  1  458 ? 39.266  -5.132  64.896  1.00 30.75  ?  458  PHE A CE1 1 
ATOM   3176  C CE2 . PHE A  1  458 ? 37.498  -4.687  66.441  1.00 28.32  ?  458  PHE A CE2 1 
ATOM   3177  C CZ  . PHE A  1  458 ? 38.624  -4.269  65.762  1.00 29.69  ?  458  PHE A CZ  1 
ATOM   3178  N N   . ILE A  1  459 ? 37.398  -7.384  61.919  1.00 32.41  ?  459  ILE A N   1 
ATOM   3179  C CA  . ILE A  1  459 ? 38.342  -7.212  60.820  1.00 33.77  ?  459  ILE A CA  1 
ATOM   3180  C C   . ILE A  1  459 ? 38.724  -5.740  60.731  1.00 33.53  ?  459  ILE A C   1 
ATOM   3181  O O   . ILE A  1  459 ? 37.876  -4.853  60.882  1.00 32.53  ?  459  ILE A O   1 
ATOM   3182  C CB  . ILE A  1  459 ? 37.769  -7.741  59.484  1.00 34.71  ?  459  ILE A CB  1 
ATOM   3183  C CG1 . ILE A  1  459 ? 38.878  -7.864  58.435  1.00 36.44  ?  459  ILE A CG1 1 
ATOM   3184  C CG2 . ILE A  1  459 ? 36.616  -6.882  58.987  1.00 34.00  ?  459  ILE A CG2 1 
ATOM   3185  C CD1 . ILE A  1  459 ? 38.465  -8.636  57.199  1.00 37.67  ?  459  ILE A CD1 1 
ATOM   3186  N N   . ASP A  1  460 ? 40.016  -5.481  60.526  1.00 38.52  ?  460  ASP A N   1 
ATOM   3187  C CA  . ASP A  1  460 ? 40.537  -4.116  60.444  1.00 37.28  ?  460  ASP A CA  1 
ATOM   3188  C C   . ASP A  1  460 ? 41.605  -4.089  59.353  1.00 39.06  ?  460  ASP A C   1 
ATOM   3189  O O   . ASP A  1  460 ? 42.729  -4.555  59.564  1.00 40.43  ?  460  ASP A O   1 
ATOM   3190  C CB  . ASP A  1  460 ? 41.094  -3.655  61.786  1.00 36.34  ?  460  ASP A CB  1 
ATOM   3191  C CG  . ASP A  1  460 ? 41.400  -2.168  61.814  1.00 36.26  ?  460  ASP A CG  1 
ATOM   3192  O OD1 . ASP A  1  460 ? 41.158  -1.489  60.794  1.00 36.76  ?  460  ASP A OD1 1 
ATOM   3193  O OD2 . ASP A  1  460 ? 41.875  -1.675  62.858  1.00 35.85  -1 460  ASP A OD2 1 
ATOM   3194  N N   . LEU A  1  461 ? 41.245  -3.547  58.189  1.00 36.07  ?  461  LEU A N   1 
ATOM   3195  C CA  . LEU A  1  461 ? 42.140  -3.452  57.043  1.00 37.98  ?  461  LEU A CA  1 
ATOM   3196  C C   . LEU A  1  461 ? 42.661  -2.035  56.834  1.00 38.45  ?  461  LEU A C   1 
ATOM   3197  O O   . LEU A  1  461 ? 43.050  -1.682  55.715  1.00 39.94  ?  461  LEU A O   1 
ATOM   3198  C CB  . LEU A  1  461 ? 41.432  -3.944  55.780  1.00 38.68  ?  461  LEU A CB  1 
ATOM   3199  C CG  . LEU A  1  461 ? 40.630  -5.239  55.907  1.00 38.54  ?  461  LEU A CG  1 
ATOM   3200  C CD1 . LEU A  1  461 ? 39.698  -5.411  54.716  1.00 39.13  ?  461  LEU A CD1 1 
ATOM   3201  C CD2 . LEU A  1  461 ? 41.554  -6.439  56.053  1.00 40.59  ?  461  LEU A CD2 1 
ATOM   3202  N N   . SER A  1  462 ? 42.672  -1.221  57.884  1.00 38.58  ?  462  SER A N   1 
ATOM   3203  C CA  . SER A  1  462 ? 42.968  0.196   57.748  1.00 38.92  ?  462  SER A CA  1 
ATOM   3204  C C   . SER A  1  462 ? 44.427  0.427   57.365  1.00 40.90  ?  462  SER A C   1 
ATOM   3205  O O   . SER A  1  462 ? 45.303  -0.414  57.592  1.00 41.69  ?  462  SER A O   1 
ATOM   3206  C CB  . SER A  1  462 ? 42.651  0.935   59.049  1.00 37.41  ?  462  SER A CB  1 
ATOM   3207  O OG  . SER A  1  462 ? 41.342  0.634   59.498  1.00 35.72  ?  462  SER A OG  1 
ATOM   3208  N N   . ASN A  1  463 ? 44.675  1.595   56.768  1.00 41.74  ?  463  ASN A N   1 
ATOM   3209  C CA  . ASN A  1  463 ? 46.016  2.040   56.389  1.00 43.80  ?  463  ASN A CA  1 
ATOM   3210  C C   . ASN A  1  463 ? 46.687  1.040   55.443  1.00 45.58  ?  463  ASN A C   1 
ATOM   3211  O O   . ASN A  1  463 ? 47.726  0.449   55.745  1.00 46.58  ?  463  ASN A O   1 
ATOM   3212  C CB  . ASN A  1  463 ? 46.874  2.293   57.633  1.00 43.67  ?  463  ASN A CB  1 
ATOM   3213  C CG  . ASN A  1  463 ? 46.214  3.248   58.607  1.00 42.05  ?  463  ASN A CG  1 
ATOM   3214  O OD1 . ASN A  1  463 ? 45.537  4.194   58.206  1.00 41.74  ?  463  ASN A OD1 1 
ATOM   3215  N ND2 . ASN A  1  463 ? 46.402  2.998   59.897  1.00 41.08  ?  463  ASN A ND2 1 
ATOM   3216  N N   . ASN A  1  464 ? 46.065  0.862   54.281  1.00 46.71  ?  464  ASN A N   1 
ATOM   3217  C CA  . ASN A  1  464 ? 46.562  -0.048  53.258  1.00 48.53  ?  464  ASN A CA  1 
ATOM   3218  C C   . ASN A  1  464 ? 46.267  0.570   51.895  1.00 49.79  ?  464  ASN A C   1 
ATOM   3219  O O   . ASN A  1  464 ? 45.817  1.716   51.796  1.00 49.33  ?  464  ASN A O   1 
ATOM   3220  C CB  . ASN A  1  464 ? 45.936  -1.439  53.420  1.00 47.61  ?  464  ASN A CB  1 
ATOM   3221  C CG  . ASN A  1  464 ? 46.703  -2.311  54.391  1.00 47.51  ?  464  ASN A CG  1 
ATOM   3222  O OD1 . ASN A  1  464 ? 47.792  -2.792  54.083  1.00 49.30  ?  464  ASN A OD1 1 
ATOM   3223  N ND2 . ASN A  1  464 ? 46.139  -2.516  55.575  1.00 45.50  ?  464  ASN A ND2 1 
ATOM   3224  N N   . ASN A  1  465 ? 46.525  -0.190  50.833  1.00 52.72  ?  465  ASN A N   1 
ATOM   3225  C CA  . ASN A  1  465 ? 46.357  0.287   49.466  1.00 54.28  ?  465  ASN A CA  1 
ATOM   3226  C C   . ASN A  1  465 ? 45.399  -0.608  48.686  1.00 54.11  ?  465  ASN A C   1 
ATOM   3227  O O   . ASN A  1  465 ? 45.640  -0.945  47.524  1.00 56.24  ?  465  ASN A O   1 
ATOM   3228  C CB  . ASN A  1  465 ? 47.705  0.382   48.754  1.00 57.13  ?  465  ASN A CB  1 
ATOM   3229  C CG  . ASN A  1  465 ? 47.702  1.406   47.634  1.00 59.21  ?  465  ASN A CG  1 
ATOM   3230  O OD1 . ASN A  1  465 ? 47.114  2.480   47.762  1.00 58.13  ?  465  ASN A OD1 1 
ATOM   3231  N ND2 . ASN A  1  465 ? 48.361  1.078   46.528  1.00 62.36  ?  465  ASN A ND2 1 
ATOM   3232  N N   . PHE A  1  466 ? 44.297  -1.002  49.318  1.00 51.24  ?  466  PHE A N   1 
ATOM   3233  C CA  . PHE A  1  466 ? 43.268  -1.776  48.637  1.00 51.02  ?  466  PHE A CA  1 
ATOM   3234  C C   . PHE A  1  466 ? 42.436  -0.863  47.746  1.00 51.07  ?  466  PHE A C   1 
ATOM   3235  O O   . PHE A  1  466 ? 41.946  0.177   48.196  1.00 49.77  ?  466  PHE A O   1 
ATOM   3236  C CB  . PHE A  1  466 ? 42.365  -2.482  49.649  1.00 48.88  ?  466  PHE A CB  1 
ATOM   3237  C CG  . PHE A  1  466 ? 43.019  -3.637  50.353  1.00 48.94  ?  466  PHE A CG  1 
ATOM   3238  C CD1 . PHE A  1  466 ? 43.318  -4.803  49.668  1.00 50.47  ?  466  PHE A CD1 1 
ATOM   3239  C CD2 . PHE A  1  466 ? 43.319  -3.563  51.703  1.00 47.55  ?  466  PHE A CD2 1 
ATOM   3240  C CE1 . PHE A  1  466 ? 43.913  -5.871  50.315  1.00 50.63  ?  466  PHE A CE1 1 
ATOM   3241  C CE2 . PHE A  1  466 ? 43.914  -4.627  52.356  1.00 47.66  ?  466  PHE A CE2 1 
ATOM   3242  C CZ  . PHE A  1  466 ? 44.211  -5.783  51.660  1.00 49.20  ?  466  PHE A CZ  1 
ATOM   3243  N N   . HIS A  1  467 ? 42.281  -1.250  46.485  1.00 50.39  ?  467  HIS A N   1 
ATOM   3244  C CA  . HIS A  1  467 ? 41.441  -0.534  45.538  1.00 50.59  ?  467  HIS A CA  1 
ATOM   3245  C C   . HIS A  1  467 ? 40.194  -1.360  45.230  1.00 49.79  ?  467  HIS A C   1 
ATOM   3246  O O   . HIS A  1  467 ? 40.023  -2.481  45.717  1.00 49.23  ?  467  HIS A O   1 
ATOM   3247  C CB  . HIS A  1  467 ? 42.229  -0.198  44.268  1.00 53.35  ?  467  HIS A CB  1 
ATOM   3248  C CG  . HIS A  1  467 ? 42.550  -1.388  43.416  1.00 55.31  ?  467  HIS A CG  1 
ATOM   3249  N ND1 . HIS A  1  467 ? 43.737  -2.080  43.523  1.00 56.82  ?  467  HIS A ND1 1 
ATOM   3250  C CD2 . HIS A  1  467 ? 41.848  -1.995  42.430  1.00 56.14  ?  467  HIS A CD2 1 
ATOM   3251  C CE1 . HIS A  1  467 ? 43.747  -3.069  42.647  1.00 58.50  ?  467  HIS A CE1 1 
ATOM   3252  N NE2 . HIS A  1  467 ? 42.613  -3.039  41.971  1.00 58.15  ?  467  HIS A NE2 1 
ATOM   3253  N N   . GLY A  1  468 ? 39.308  -0.785  44.424  1.00 50.71  ?  468  GLY A N   1 
ATOM   3254  C CA  . GLY A  1  468 ? 38.101  -1.468  44.000  1.00 50.23  ?  468  GLY A CA  1 
ATOM   3255  C C   . GLY A  1  468 ? 36.892  -1.063  44.821  1.00 47.71  ?  468  GLY A C   1 
ATOM   3256  O O   . GLY A  1  468 ? 36.941  -0.184  45.686  1.00 46.31  ?  468  GLY A O   1 
ATOM   3257  N N   . GLN A  1  469 ? 35.783  -1.739  44.537  1.00 52.93  ?  469  GLN A N   1 
ATOM   3258  C CA  . GLN A  1  469 ? 34.519  -1.502  45.214  1.00 50.63  ?  469  GLN A CA  1 
ATOM   3259  C C   . GLN A  1  469 ? 34.215  -2.651  46.167  1.00 49.59  ?  469  GLN A C   1 
ATOM   3260  O O   . GLN A  1  469 ? 34.683  -3.778  45.978  1.00 50.74  ?  469  GLN A O   1 
ATOM   3261  C CB  . GLN A  1  469 ? 33.375  -1.339  44.208  1.00 51.50  ?  469  GLN A CB  1 
ATOM   3262  C CG  . GLN A  1  469 ? 33.109  -2.573  43.363  1.00 53.05  ?  469  GLN A CG  1 
ATOM   3263  C CD  . GLN A  1  469 ? 31.657  -2.686  42.945  1.00 52.61  ?  469  GLN A CD  1 
ATOM   3264  O OE1 . GLN A  1  469 ? 31.262  -2.191  41.890  1.00 53.48  ?  469  GLN A OE1 1 
ATOM   3265  N NE2 . GLN A  1  469 ? 30.853  -3.343  43.773  1.00 51.22  ?  469  GLN A NE2 1 
ATOM   3266  N N   . LEU A  1  470 ? 33.418  -2.357  47.191  1.00 46.30  ?  470  LEU A N   1 
ATOM   3267  C CA  . LEU A  1  470 ? 33.132  -3.345  48.222  1.00 46.02  ?  470  LEU A CA  1 
ATOM   3268  C C   . LEU A  1  470 ? 32.197  -4.421  47.687  1.00 47.53  ?  470  LEU A C   1 
ATOM   3269  O O   . LEU A  1  470 ? 31.132  -4.121  47.139  1.00 47.50  ?  470  LEU A O   1 
ATOM   3270  C CB  . LEU A  1  470 ? 32.516  -2.675  49.448  1.00 43.95  ?  470  LEU A CB  1 
ATOM   3271  C CG  . LEU A  1  470 ? 33.457  -1.829  50.307  1.00 42.46  ?  470  LEU A CG  1 
ATOM   3272  C CD1 . LEU A  1  470 ? 32.704  -1.217  51.478  1.00 40.49  ?  470  LEU A CD1 1 
ATOM   3273  C CD2 . LEU A  1  470 ? 34.631  -2.663  50.796  1.00 43.18  ?  470  LEU A CD2 1 
ATOM   3274  N N   . SER A  1  471 ? 32.603  -5.677  47.842  1.00 45.01  ?  471  SER A N   1 
ATOM   3275  C CA  . SER A  1  471 ? 31.761  -6.793  47.445  1.00 46.45  ?  471  SER A CA  1 
ATOM   3276  C C   . SER A  1  471 ? 30.601  -6.958  48.419  1.00 45.31  ?  471  SER A C   1 
ATOM   3277  O O   . SER A  1  471 ? 30.723  -6.691  49.617  1.00 44.60  ?  471  SER A O   1 
ATOM   3278  C CB  . SER A  1  471 ? 32.579  -8.083  47.386  1.00 47.28  ?  471  SER A CB  1 
ATOM   3279  O OG  . SER A  1  471 ? 31.741  -9.213  47.223  1.00 48.42  ?  471  SER A OG  1 
ATOM   3280  N N   . ALA A  1  472 ? 29.460  -7.403  47.891  1.00 43.54  ?  472  ALA A N   1 
ATOM   3281  C CA  . ALA A  1  472 ? 28.322  -7.700  48.751  1.00 42.26  ?  472  ALA A CA  1 
ATOM   3282  C C   . ALA A  1  472 ? 28.500  -9.001  49.522  1.00 42.45  ?  472  ALA A C   1 
ATOM   3283  O O   . ALA A  1  472 ? 27.590  -9.396  50.258  1.00 41.64  ?  472  ALA A O   1 
ATOM   3284  C CB  . ALA A  1  472 ? 27.036  -7.755  47.924  1.00 42.78  ?  472  ALA A CB  1 
ATOM   3285  N N   . ASN A  1  473 ? 29.648  -9.666  49.373  1.00 45.06  ?  473  ASN A N   1 
ATOM   3286  C CA  . ASN A  1  473 ? 29.926  -10.884 50.124  1.00 46.17  ?  473  ASN A CA  1 
ATOM   3287  C C   . ASN A  1  473 ? 29.985  -10.639 51.625  1.00 44.96  ?  473  ASN A C   1 
ATOM   3288  O O   . ASN A  1  473 ? 29.754  -11.572 52.401  1.00 45.84  ?  473  ASN A O   1 
ATOM   3289  C CB  . ASN A  1  473 ? 31.245  -11.502 49.655  1.00 47.01  ?  473  ASN A CB  1 
ATOM   3290  C CG  . ASN A  1  473 ? 31.122  -12.193 48.313  1.00 48.27  ?  473  ASN A CG  1 
ATOM   3291  O OD1 . ASN A  1  473 ? 30.020  -12.364 47.792  1.00 48.59  ?  473  ASN A OD1 1 
ATOM   3292  N ND2 . ASN A  1  473 ? 32.254  -12.599 47.749  1.00 49.38  ?  473  ASN A ND2 1 
ATOM   3293  N N   . TRP A  1  474 ? 30.293  -9.410  52.048  1.00 45.91  ?  474  TRP A N   1 
ATOM   3294  C CA  . TRP A  1  474 ? 30.417  -9.117  53.472  1.00 44.48  ?  474  TRP A CA  1 
ATOM   3295  C C   . TRP A  1  474 ? 29.114  -9.359  54.220  1.00 43.57  ?  474  TRP A C   1 
ATOM   3296  O O   . TRP A  1  474 ? 29.138  -9.611  55.430  1.00 41.92  ?  474  TRP A O   1 
ATOM   3297  C CB  . TRP A  1  474 ? 30.875  -7.673  53.673  1.00 42.34  ?  474  TRP A CB  1 
ATOM   3298  C CG  . TRP A  1  474 ? 32.251  -7.398  53.143  1.00 43.10  ?  474  TRP A CG  1 
ATOM   3299  C CD1 . TRP A  1  474 ? 32.577  -6.621  52.070  1.00 43.90  ?  474  TRP A CD1 1 
ATOM   3300  C CD2 . TRP A  1  474 ? 33.487  -7.908  53.659  1.00 43.78  ?  474  TRP A CD2 1 
ATOM   3301  N NE1 . TRP A  1  474 ? 33.939  -6.614  51.887  1.00 44.17  ?  474  TRP A NE1 1 
ATOM   3302  C CE2 . TRP A  1  474 ? 34.521  -7.396  52.850  1.00 44.41  ?  474  TRP A CE2 1 
ATOM   3303  C CE3 . TRP A  1  474 ? 33.819  -8.747  54.726  1.00 43.88  ?  474  TRP A CE3 1 
ATOM   3304  C CZ2 . TRP A  1  474 ? 35.863  -7.695  53.075  1.00 45.05  ?  474  TRP A CZ2 1 
ATOM   3305  C CZ3 . TRP A  1  474 ? 35.150  -9.042  54.948  1.00 44.59  ?  474  TRP A CZ3 1 
ATOM   3306  C CH2 . TRP A  1  474 ? 36.156  -8.518  54.126  1.00 45.08  ?  474  TRP A CH2 1 
ATOM   3307  N N   . GLU A  1  475 ? 27.974  -9.282  53.528  1.00 47.10  ?  475  GLU A N   1 
ATOM   3308  C CA  . GLU A  1  475 ? 26.692  -9.515  54.185  1.00 45.85  ?  475  GLU A CA  1 
ATOM   3309  C C   . GLU A  1  475 ? 26.599  -10.923 54.758  1.00 46.95  ?  475  GLU A C   1 
ATOM   3310  O O   . GLU A  1  475 ? 25.946  -11.132 55.787  1.00 44.73  ?  475  GLU A O   1 
ATOM   3311  C CB  . GLU A  1  475 ? 25.548  -9.265  53.203  1.00 46.78  ?  475  GLU A CB  1 
ATOM   3312  C CG  . GLU A  1  475 ? 24.161  -9.382  53.817  1.00 44.74  ?  475  GLU A CG  1 
ATOM   3313  C CD  . GLU A  1  475 ? 23.189  -10.128 52.925  1.00 47.37  ?  475  GLU A CD  1 
ATOM   3314  O OE1 . GLU A  1  475 ? 23.478  -10.276 51.719  1.00 50.27  ?  475  GLU A OE1 1 
ATOM   3315  O OE2 . GLU A  1  475 ? 22.134  -10.568 53.430  1.00 45.91  -1 475  GLU A OE2 1 
ATOM   3316  N N   . GLN A  1  476 ? 27.253  -11.897 54.119  1.00 45.21  ?  476  GLN A N   1 
ATOM   3317  C CA  . GLN A  1  476 ? 27.214  -13.270 54.611  1.00 45.03  ?  476  GLN A CA  1 
ATOM   3318  C C   . GLN A  1  476 ? 28.012  -13.457 55.893  1.00 43.07  ?  476  GLN A C   1 
ATOM   3319  O O   . GLN A  1  476 ? 27.844  -14.479 56.567  1.00 42.41  ?  476  GLN A O   1 
ATOM   3320  C CB  . GLN A  1  476 ? 27.724  -14.232 53.539  1.00 47.96  ?  476  GLN A CB  1 
ATOM   3321  C CG  . GLN A  1  476 ? 26.885  -14.242 52.276  1.00 49.58  ?  476  GLN A CG  1 
ATOM   3322  C CD  . GLN A  1  476 ? 27.375  -15.251 51.261  1.00 52.25  ?  476  GLN A CD  1 
ATOM   3323  O OE1 . GLN A  1  476 ? 27.954  -16.275 51.620  1.00 53.11  ?  476  GLN A OE1 1 
ATOM   3324  N NE2 . GLN A  1  476 ? 27.147  -14.966 49.983  1.00 52.20  ?  476  GLN A NE2 1 
ATOM   3325  N N   . SER A  1  477 ? 28.874  -12.502 56.246  1.00 44.80  ?  477  SER A N   1 
ATOM   3326  C CA  . SER A  1  477 ? 29.563  -12.521 57.536  1.00 43.32  ?  477  SER A CA  1 
ATOM   3327  C C   . SER A  1  477 ? 28.593  -12.016 58.605  1.00 39.64  ?  477  SER A C   1 
ATOM   3328  O O   . SER A  1  477 ? 28.756  -10.949 59.201  1.00 37.56  ?  477  SER A O   1 
ATOM   3329  C CB  . SER A  1  477 ? 30.835  -11.687 57.483  1.00 43.77  ?  477  SER A CB  1 
ATOM   3330  O OG  . SER A  1  477 ? 31.807  -12.287 56.645  1.00 46.64  ?  477  SER A OG  1 
ATOM   3331  N N   . GLN A  1  478 ? 27.553  -12.821 58.835  1.00 43.26  ?  478  GLN A N   1 
ATOM   3332  C CA  . GLN A  1  478 ? 26.448  -12.417 59.694  1.00 41.23  ?  478  GLN A CA  1 
ATOM   3333  C C   . GLN A  1  478 ? 26.863  -12.232 61.148  1.00 40.29  ?  478  GLN A C   1 
ATOM   3334  O O   . GLN A  1  478 ? 26.108  -11.633 61.920  1.00 39.05  ?  478  GLN A O   1 
ATOM   3335  C CB  . GLN A  1  478 ? 25.316  -13.440 59.596  1.00 41.82  ?  478  GLN A CB  1 
ATOM   3336  C CG  . GLN A  1  478 ? 24.440  -13.262 58.365  1.00 42.58  ?  478  GLN A CG  1 
ATOM   3337  C CD  . GLN A  1  478 ? 23.464  -12.110 58.505  1.00 42.00  ?  478  GLN A CD  1 
ATOM   3338  O OE1 . GLN A  1  478 ? 22.503  -12.185 59.270  1.00 42.10  ?  478  GLN A OE1 1 
ATOM   3339  N NE2 . GLN A  1  478 ? 23.713  -11.031 57.772  1.00 41.14  ?  478  GLN A NE2 1 
ATOM   3340  N N   . LYS A  1  479 ? 28.034  -12.728 61.541  1.00 40.04  ?  479  LYS A N   1 
ATOM   3341  C CA  . LYS A  1  479 ? 28.525  -12.562 62.901  1.00 38.62  ?  479  LYS A CA  1 
ATOM   3342  C C   . LYS A  1  479 ? 29.489  -11.392 63.040  1.00 38.11  ?  479  LYS A C   1 
ATOM   3343  O O   . LYS A  1  479 ? 30.042  -11.186 64.125  1.00 37.06  ?  479  LYS A O   1 
ATOM   3344  C CB  . LYS A  1  479 ? 29.207  -13.850 63.374  1.00 39.41  ?  479  LYS A CB  1 
ATOM   3345  C CG  . LYS A  1  479 ? 28.297  -15.068 63.382  1.00 40.80  ?  479  LYS A CG  1 
ATOM   3346  C CD  . LYS A  1  479 ? 27.006  -14.800 64.137  1.00 40.21  ?  479  LYS A CD  1 
ATOM   3347  C CE  . LYS A  1  479 ? 26.198  -16.077 64.315  1.00 41.39  ?  479  LYS A CE  1 
ATOM   3348  N NZ  . LYS A  1  479 ? 26.856  -17.029 65.252  1.00 41.47  ?  479  LYS A NZ  1 
ATOM   3349  N N   . LEU A  1  480 ? 29.699  -10.622 61.974  1.00 36.05  ?  480  LEU A N   1 
ATOM   3350  C CA  . LEU A  1  480 ? 30.606  -9.484  62.032  1.00 34.74  ?  480  LEU A CA  1 
ATOM   3351  C C   . LEU A  1  480 ? 30.003  -8.361  62.867  1.00 33.33  ?  480  LEU A C   1 
ATOM   3352  O O   . LEU A  1  480 ? 28.843  -7.982  62.677  1.00 33.00  ?  480  LEU A O   1 
ATOM   3353  C CB  . LEU A  1  480 ? 30.924  -8.984  60.624  1.00 36.43  ?  480  LEU A CB  1 
ATOM   3354  C CG  . LEU A  1  480 ? 32.103  -8.015  60.500  1.00 36.81  ?  480  LEU A CG  1 
ATOM   3355  C CD1 . LEU A  1  480 ? 33.412  -8.696  60.862  1.00 38.33  ?  480  LEU A CD1 1 
ATOM   3356  C CD2 . LEU A  1  480 ? 32.171  -7.430  59.097  1.00 38.63  ?  480  LEU A CD2 1 
ATOM   3357  N N   . VAL A  1  481 ? 30.797  -7.832  63.794  1.00 35.71  ?  481  VAL A N   1 
ATOM   3358  C CA  . VAL A  1  481 ? 30.374  -6.706  64.615  1.00 34.79  ?  481  VAL A CA  1 
ATOM   3359  C C   . VAL A  1  481 ? 31.223  -5.462  64.395  1.00 34.57  ?  481  VAL A C   1 
ATOM   3360  O O   . VAL A  1  481 ? 30.775  -4.357  64.744  1.00 33.66  ?  481  VAL A O   1 
ATOM   3361  C CB  . VAL A  1  481 ? 30.364  -7.081  66.112  1.00 33.94  ?  481  VAL A CB  1 
ATOM   3362  C CG1 . VAL A  1  481 ? 29.388  -8.217  66.368  1.00 34.25  ?  481  VAL A CG1 1 
ATOM   3363  C CG2 . VAL A  1  481 ? 31.763  -7.458  66.577  1.00 34.21  ?  481  VAL A CG2 1 
ATOM   3364  N N   . ALA A  1  482 ? 32.426  -5.587  63.835  1.00 32.65  ?  482  ALA A N   1 
ATOM   3365  C CA  . ALA A  1  482 ? 33.298  -4.443  63.587  1.00 32.67  ?  482  ALA A CA  1 
ATOM   3366  C C   . ALA A  1  482 ? 33.887  -4.567  62.188  1.00 34.35  ?  482  ALA A C   1 
ATOM   3367  O O   . ALA A  1  482 ? 34.729  -5.437  61.942  1.00 34.76  ?  482  ALA A O   1 
ATOM   3368  C CB  . ALA A  1  482 ? 34.403  -4.353  64.637  1.00 32.33  ?  482  ALA A CB  1 
ATOM   3369  N N   . PHE A  1  483 ? 33.445  -3.706  61.276  1.00 32.83  ?  483  PHE A N   1 
ATOM   3370  C CA  . PHE A  1  483 ? 34.012  -3.601  59.935  1.00 33.61  ?  483  PHE A CA  1 
ATOM   3371  C C   . PHE A  1  483 ? 34.738  -2.263  59.855  1.00 33.99  ?  483  PHE A C   1 
ATOM   3372  O O   . PHE A  1  483 ? 34.099  -1.205  59.854  1.00 33.53  ?  483  PHE A O   1 
ATOM   3373  C CB  . PHE A  1  483 ? 32.919  -3.712  58.873  1.00 33.94  ?  483  PHE A CB  1 
ATOM   3374  C CG  . PHE A  1  483 ? 33.435  -3.980  57.485  1.00 36.66  ?  483  PHE A CG  1 
ATOM   3375  C CD1 . PHE A  1  483 ? 34.710  -4.483  57.286  1.00 39.01  ?  483  PHE A CD1 1 
ATOM   3376  C CD2 . PHE A  1  483 ? 32.637  -3.735  56.380  1.00 37.81  ?  483  PHE A CD2 1 
ATOM   3377  C CE1 . PHE A  1  483 ? 35.181  -4.732  56.010  1.00 41.08  ?  483  PHE A CE1 1 
ATOM   3378  C CE2 . PHE A  1  483 ? 33.103  -3.981  55.102  1.00 40.55  ?  483  PHE A CE2 1 
ATOM   3379  C CZ  . PHE A  1  483 ? 34.377  -4.480  54.918  1.00 41.57  ?  483  PHE A CZ  1 
ATOM   3380  N N   . ILE A  1  484 ? 36.067  -2.308  59.790  1.00 32.14  ?  484  ILE A N   1 
ATOM   3381  C CA  . ILE A  1  484 ? 36.907  -1.113  59.853  1.00 32.42  ?  484  ILE A CA  1 
ATOM   3382  C C   . ILE A  1  484 ? 37.870  -1.158  58.675  1.00 33.79  ?  484  ILE A C   1 
ATOM   3383  O O   . ILE A  1  484 ? 38.797  -1.978  58.659  1.00 34.73  ?  484  ILE A O   1 
ATOM   3384  C CB  . ILE A  1  484 ? 37.672  -1.019  61.179  1.00 31.59  ?  484  ILE A CB  1 
ATOM   3385  C CG1 . ILE A  1  484 ? 36.713  -1.163  62.364  1.00 30.47  ?  484  ILE A CG1 1 
ATOM   3386  C CG2 . ILE A  1  484 ? 38.432  0.294   61.260  1.00 32.30  ?  484  ILE A CG2 1 
ATOM   3387  C CD1 . ILE A  1  484 ? 37.356  -0.924  63.712  1.00 29.93  ?  484  ILE A CD1 1 
ATOM   3388  N N   . LEU A  1  485 ? 37.657  -0.284  57.692  1.00 34.02  ?  485  LEU A N   1 
ATOM   3389  C CA  . LEU A  1  485 ? 38.444  -0.283  56.462  1.00 35.68  ?  485  LEU A CA  1 
ATOM   3390  C C   . LEU A  1  485 ? 38.866  1.144   56.102  1.00 36.22  ?  485  LEU A C   1 
ATOM   3391  O O   . LEU A  1  485 ? 38.687  1.605   54.974  1.00 37.17  ?  485  LEU A O   1 
ATOM   3392  C CB  . LEU A  1  485 ? 37.656  -0.945  55.335  1.00 36.17  ?  485  LEU A CB  1 
ATOM   3393  C CG  . LEU A  1  485 ? 38.452  -1.726  54.280  1.00 38.12  ?  485  LEU A CG  1 
ATOM   3394  C CD1 . LEU A  1  485 ? 37.514  -2.557  53.408  1.00 38.40  ?  485  LEU A CD1 1 
ATOM   3395  C CD2 . LEU A  1  485 ? 39.395  -0.877  53.438  1.00 39.86  ?  485  LEU A CD2 1 
ATOM   3396  N N   . SER A  1  486 ? 39.378  1.889   57.076  1.00 37.11  ?  486  SER A N   1 
ATOM   3397  C CA  . SER A  1  486 ? 39.685  3.291   56.834  1.00 38.02  ?  486  SER A CA  1 
ATOM   3398  C C   . SER A  1  486 ? 41.019  3.458   56.105  1.00 40.03  ?  486  SER A C   1 
ATOM   3399  O O   . SER A  1  486 ? 41.875  2.569   56.101  1.00 40.53  ?  486  SER A O   1 
ATOM   3400  C CB  . SER A  1  486 ? 39.714  4.070   58.150  1.00 36.75  ?  486  SER A CB  1 
ATOM   3401  O OG  . SER A  1  486 ? 40.784  3.645   58.974  1.00 37.18  ?  486  SER A OG  1 
ATOM   3402  N N   . ASN A  1  487 ? 41.177  4.622   55.469  1.00 44.53  ?  487  ASN A N   1 
ATOM   3403  C CA  . ASN A  1  487 ? 42.421  5.041   54.816  1.00 46.35  ?  487  ASN A CA  1 
ATOM   3404  C C   . ASN A  1  487 ? 42.866  4.036   53.750  1.00 47.98  ?  487  ASN A C   1 
ATOM   3405  O O   . ASN A  1  487 ? 43.977  3.501   53.782  1.00 49.14  ?  487  ASN A O   1 
ATOM   3406  C CB  . ASN A  1  487 ? 43.528  5.266   55.850  1.00 46.69  ?  487  ASN A CB  1 
ATOM   3407  C CG  . ASN A  1  487 ? 44.641  6.166   55.338  1.00 48.79  ?  487  ASN A CG  1 
ATOM   3408  O OD1 . ASN A  1  487 ? 44.395  7.096   54.570  1.00 49.48  ?  487  ASN A OD1 1 
ATOM   3409  N ND2 . ASN A  1  487 ? 45.878  5.877   55.768  1.00 49.91  ?  487  ASN A ND2 1 
ATOM   3410  N N   . ASN A  1  488 ? 41.973  3.789   52.794  1.00 44.69  ?  488  ASN A N   1 
ATOM   3411  C CA  . ASN A  1  488 ? 42.313  2.958   51.646  1.00 46.35  ?  488  ASN A CA  1 
ATOM   3412  C C   . ASN A  1  488 ? 41.939  3.672   50.354  1.00 47.45  ?  488  ASN A C   1 
ATOM   3413  O O   . ASN A  1  488 ? 41.555  4.846   50.378  1.00 47.02  ?  488  ASN A O   1 
ATOM   3414  C CB  . ASN A  1  488 ? 41.625  1.595   51.744  1.00 45.63  ?  488  ASN A CB  1 
ATOM   3415  C CG  . ASN A  1  488 ? 42.483  0.564   52.452  1.00 45.68  ?  488  ASN A CG  1 
ATOM   3416  O OD1 . ASN A  1  488 ? 43.223  -0.187  51.817  1.00 47.34  ?  488  ASN A OD1 1 
ATOM   3417  N ND2 . ASN A  1  488 ? 42.393  0.530   53.776  1.00 44.10  ?  488  ASN A ND2 1 
ATOM   3418  N N   . SER A  1  489 ? 42.053  2.981   49.224  1.00 47.29  ?  489  SER A N   1 
ATOM   3419  C CA  . SER A  1  489 ? 41.757  3.547   47.913  1.00 48.61  ?  489  SER A CA  1 
ATOM   3420  C C   . SER A  1  489 ? 40.501  2.925   47.310  1.00 47.89  ?  489  SER A C   1 
ATOM   3421  O O   . SER A  1  489 ? 40.421  2.698   46.101  1.00 49.43  ?  489  SER A O   1 
ATOM   3422  C CB  . SER A  1  489 ? 42.942  3.374   46.969  1.00 51.37  ?  489  SER A CB  1 
ATOM   3423  O OG  . SER A  1  489 ? 44.156  3.746   47.598  1.00 52.15  ?  489  SER A OG  1 
ATOM   3424  N N   . ILE A  1  490 ? 39.508  2.640   48.146  1.00 46.00  ?  490  ILE A N   1 
ATOM   3425  C CA  . ILE A  1  490 ? 38.295  1.973   47.683  1.00 45.34  ?  490  ILE A CA  1 
ATOM   3426  C C   . ILE A  1  490 ? 37.335  2.993   47.086  1.00 44.97  ?  490  ILE A C   1 
ATOM   3427  O O   . ILE A  1  490 ? 37.049  4.035   47.687  1.00 43.82  ?  490  ILE A O   1 
ATOM   3428  C CB  . ILE A  1  490 ? 37.640  1.174   48.820  1.00 43.38  ?  490  ILE A CB  1 
ATOM   3429  C CG1 . ILE A  1  490 ? 38.275  -0.214  48.895  1.00 44.33  ?  490  ILE A CG1 1 
ATOM   3430  C CG2 . ILE A  1  490 ? 36.132  1.075   48.630  1.00 42.18  ?  490  ILE A CG2 1 
ATOM   3431  C CD1 . ILE A  1  490 ? 38.177  -0.854  50.233  1.00 42.83  ?  490  ILE A CD1 1 
ATOM   3432  N N   . THR A  1  491 ? 36.842  2.685   45.892  1.00 42.74  ?  491  THR A N   1 
ATOM   3433  C CA  . THR A  1  491 ? 35.903  3.488   45.128  1.00 42.67  ?  491  THR A CA  1 
ATOM   3434  C C   . THR A  1  491 ? 34.539  2.802   45.107  1.00 41.48  ?  491  THR A C   1 
ATOM   3435  O O   . THR A  1  491 ? 34.322  1.771   45.751  1.00 40.66  ?  491  THR A O   1 
ATOM   3436  C CB  . THR A  1  491 ? 36.435  3.715   43.712  1.00 45.13  ?  491  THR A CB  1 
ATOM   3437  O OG1 . THR A  1  491 ? 36.295  2.508   42.952  1.00 46.25  ?  491  THR A OG1 1 
ATOM   3438  C CG2 . THR A  1  491 ? 37.904  4.110   43.758  1.00 46.65  ?  491  THR A CG2 1 
ATOM   3439  N N   . GLY A  1  492 ? 33.610  3.391   44.363  1.00 38.89  ?  492  GLY A N   1 
ATOM   3440  C CA  . GLY A  1  492 ? 32.288  2.822   44.229  1.00 38.01  ?  492  GLY A CA  1 
ATOM   3441  C C   . GLY A  1  492 ? 31.387  3.160   45.400  1.00 35.69  ?  492  GLY A C   1 
ATOM   3442  O O   . GLY A  1  492 ? 31.706  3.978   46.264  1.00 34.72  ?  492  GLY A O   1 
ATOM   3443  N N   . ALA A  1  493 ? 30.232  2.505   45.419  1.00 35.23  ?  493  ALA A N   1 
ATOM   3444  C CA  . ALA A  1  493 ? 29.202  2.773   46.409  1.00 33.24  ?  493  ALA A CA  1 
ATOM   3445  C C   . ALA A  1  493 ? 29.162  1.670   47.462  1.00 32.34  ?  493  ALA A C   1 
ATOM   3446  O O   . ALA A  1  493 ? 29.757  0.601   47.310  1.00 33.26  ?  493  ALA A O   1 
ATOM   3447  C CB  . ALA A  1  493 ? 27.835  2.917   45.734  1.00 33.10  ?  493  ALA A CB  1 
ATOM   3448  N N   . ILE A  1  494 ? 28.448  1.951   48.547  1.00 35.12  ?  494  ILE A N   1 
ATOM   3449  C CA  . ILE A  1  494 ? 28.283  0.993   49.636  1.00 34.20  ?  494  ILE A CA  1 
ATOM   3450  C C   . ILE A  1  494 ? 27.198  0.007   49.227  1.00 34.45  ?  494  ILE A C   1 
ATOM   3451  O O   . ILE A  1  494 ? 26.066  0.426   48.944  1.00 34.04  ?  494  ILE A O   1 
ATOM   3452  C CB  . ILE A  1  494 ? 27.917  1.687   50.957  1.00 32.46  ?  494  ILE A CB  1 
ATOM   3453  C CG1 . ILE A  1  494 ? 28.959  2.745   51.323  1.00 32.39  ?  494  ILE A CG1 1 
ATOM   3454  C CG2 . ILE A  1  494 ? 27.789  0.655   52.068  1.00 31.70  ?  494  ILE A CG2 1 
ATOM   3455  C CD1 . ILE A  1  494 ? 28.931  3.159   52.782  1.00 30.94  ?  494  ILE A CD1 1 
ATOM   3456  N N   . PRO A  1  495 ? 27.491  -1.289  49.168  1.00 37.60  ?  495  PRO A N   1 
ATOM   3457  C CA  . PRO A  1  495 ? 26.463  -2.268  48.800  1.00 38.42  ?  495  PRO A CA  1 
ATOM   3458  C C   . PRO A  1  495 ? 25.278  -2.175  49.741  1.00 36.79  ?  495  PRO A C   1 
ATOM   3459  O O   . PRO A  1  495 ? 25.457  -2.075  50.964  1.00 35.73  ?  495  PRO A O   1 
ATOM   3460  C CB  . PRO A  1  495 ? 27.186  -3.616  48.947  1.00 40.82  ?  495  PRO A CB  1 
ATOM   3461  C CG  . PRO A  1  495 ? 28.638  -3.284  48.869  1.00 41.14  ?  495  PRO A CG  1 
ATOM   3462  C CD  . PRO A  1  495 ? 28.782  -1.925  49.476  1.00 38.71  ?  495  PRO A CD  1 
ATOM   3463  N N   . PRO A  1  496 ? 24.052  -2.193  49.214  1.00 37.17  ?  496  PRO A N   1 
ATOM   3464  C CA  . PRO A  1  496 ? 22.879  -2.100  50.098  1.00 35.95  ?  496  PRO A CA  1 
ATOM   3465  C C   . PRO A  1  496 ? 22.790  -3.245  51.086  1.00 35.71  ?  496  PRO A C   1 
ATOM   3466  O O   . PRO A  1  496 ? 22.173  -3.085  52.146  1.00 34.57  ?  496  PRO A O   1 
ATOM   3467  C CB  . PRO A  1  496 ? 21.696  -2.112  49.118  1.00 36.64  ?  496  PRO A CB  1 
ATOM   3468  C CG  . PRO A  1  496 ? 22.285  -1.722  47.795  1.00 37.86  ?  496  PRO A CG  1 
ATOM   3469  C CD  . PRO A  1  496 ? 23.668  -2.291  47.797  1.00 38.58  ?  496  PRO A CD  1 
ATOM   3470  N N   . GLU A  1  497 ? 23.409  -4.386  50.779  1.00 39.73  ?  497  GLU A N   1 
ATOM   3471  C CA  . GLU A  1  497 ? 23.390  -5.533  51.677  1.00 40.39  ?  497  GLU A CA  1 
ATOM   3472  C C   . GLU A  1  497 ? 24.160  -5.275  52.966  1.00 38.42  ?  497  GLU A C   1 
ATOM   3473  O O   . GLU A  1  497 ? 23.949  -5.994  53.948  1.00 38.08  ?  497  GLU A O   1 
ATOM   3474  C CB  . GLU A  1  497 ? 23.959  -6.762  50.964  1.00 43.46  ?  497  GLU A CB  1 
ATOM   3475  C CG  . GLU A  1  497 ? 23.158  -7.220  49.747  1.00 45.19  ?  497  GLU A CG  1 
ATOM   3476  C CD  . GLU A  1  497 ? 23.483  -6.432  48.489  1.00 45.10  ?  497  GLU A CD  1 
ATOM   3477  O OE1 . GLU A  1  497 ? 24.482  -5.682  48.491  1.00 44.25  ?  497  GLU A OE1 1 
ATOM   3478  O OE2 . GLU A  1  497 ? 22.736  -6.564  47.495  1.00 46.08  -1 497  GLU A OE2 1 
ATOM   3479  N N   . ILE A  1  498 ? 25.047  -4.276  52.982  1.00 36.54  ?  498  ILE A N   1 
ATOM   3480  C CA  . ILE A  1  498 ? 25.800  -3.965  54.195  1.00 35.50  ?  498  ILE A CA  1 
ATOM   3481  C C   . ILE A  1  498 ? 24.855  -3.564  55.321  1.00 34.15  ?  498  ILE A C   1 
ATOM   3482  O O   . ILE A  1  498 ? 25.101  -3.862  56.496  1.00 33.49  ?  498  ILE A O   1 
ATOM   3483  C CB  . ILE A  1  498 ? 26.844  -2.868  53.909  1.00 35.46  ?  498  ILE A CB  1 
ATOM   3484  C CG1 . ILE A  1  498 ? 27.839  -3.348  52.852  1.00 37.01  ?  498  ILE A CG1 1 
ATOM   3485  C CG2 . ILE A  1  498 ? 27.580  -2.473  55.181  1.00 34.46  ?  498  ILE A CG2 1 
ATOM   3486  C CD1 . ILE A  1  498 ? 28.775  -4.430  53.345  1.00 37.50  ?  498  ILE A CD1 1 
ATOM   3487  N N   . TRP A  1  499 ? 23.764  -2.876  54.985  1.00 34.41  ?  499  TRP A N   1 
ATOM   3488  C CA  . TRP A  1  499 ? 22.797  -2.500  56.007  1.00 36.40  ?  499  TRP A CA  1 
ATOM   3489  C C   . TRP A  1  499 ? 22.002  -3.691  56.527  1.00 37.68  ?  499  TRP A C   1 
ATOM   3490  O O   . TRP A  1  499 ? 21.503  -3.639  57.655  1.00 39.54  ?  499  TRP A O   1 
ATOM   3491  C CB  . TRP A  1  499 ? 21.863  -1.423  55.458  1.00 37.20  ?  499  TRP A CB  1 
ATOM   3492  C CG  . TRP A  1  499 ? 22.582  -0.422  54.605  1.00 35.36  ?  499  TRP A CG  1 
ATOM   3493  C CD1 . TRP A  1  499 ? 22.281  -0.075  53.321  1.00 34.77  ?  499  TRP A CD1 1 
ATOM   3494  C CD2 . TRP A  1  499 ? 23.738  0.348   54.968  1.00 34.42  ?  499  TRP A CD2 1 
ATOM   3495  N NE1 . TRP A  1  499 ? 23.169  0.869   52.865  1.00 33.68  ?  499  TRP A NE1 1 
ATOM   3496  C CE2 . TRP A  1  499 ? 24.073  1.146   53.857  1.00 33.51  ?  499  TRP A CE2 1 
ATOM   3497  C CE3 . TRP A  1  499 ? 24.519  0.443   56.125  1.00 34.95  ?  499  TRP A CE3 1 
ATOM   3498  C CZ2 . TRP A  1  499 ? 25.151  2.028   53.869  1.00 33.02  ?  499  TRP A CZ2 1 
ATOM   3499  C CZ3 . TRP A  1  499 ? 25.593  1.315   56.133  1.00 34.18  ?  499  TRP A CZ3 1 
ATOM   3500  C CH2 . TRP A  1  499 ? 25.897  2.098   55.013  1.00 33.20  ?  499  TRP A CH2 1 
ATOM   3501  N N   . ASN A  1  500 ? 21.889  -4.766  55.747  1.00 46.27  ?  500  ASN A N   1 
ATOM   3502  C CA  . ASN A  1  500 ? 21.267  -5.988  56.243  1.00 46.82  ?  500  ASN A CA  1 
ATOM   3503  C C   . ASN A  1  500 ? 22.176  -6.765  57.192  1.00 46.59  ?  500  ASN A C   1 
ATOM   3504  O O   . ASN A  1  500 ? 21.808  -7.866  57.613  1.00 48.65  ?  500  ASN A O   1 
ATOM   3505  C CB  . ASN A  1  500 ? 20.829  -6.879  55.072  1.00 48.87  ?  500  ASN A CB  1 
ATOM   3506  C CG  . ASN A  1  500 ? 19.342  -6.734  54.747  1.00 51.02  ?  500  ASN A CG  1 
ATOM   3507  O OD1 . ASN A  1  500 ? 18.585  -6.154  55.526  1.00 51.23  ?  500  ASN A OD1 1 
ATOM   3508  N ND2 . ASN A  1  500 ? 18.919  -7.266  53.597  1.00 52.95  ?  500  ASN A ND2 1 
ATOM   3509  N N   . MET A  1  501 ? 23.348  -6.219  57.533  1.00 40.17  ?  501  MET A N   1 
ATOM   3510  C CA  . MET A  1  501 ? 24.226  -6.790  58.557  1.00 39.93  ?  501  MET A CA  1 
ATOM   3511  C C   . MET A  1  501 ? 23.826  -6.200  59.908  1.00 41.59  ?  501  MET A C   1 
ATOM   3512  O O   . MET A  1  501 ? 24.457  -5.283  60.438  1.00 42.34  ?  501  MET A O   1 
ATOM   3513  C CB  . MET A  1  501 ? 25.690  -6.510  58.235  1.00 38.83  ?  501  MET A CB  1 
ATOM   3514  C CG  . MET A  1  501 ? 26.094  -6.781  56.793  1.00 38.45  ?  501  MET A CG  1 
ATOM   3515  S SD  . MET A  1  501 ? 27.856  -6.517  56.493  1.00 37.82  ?  501  MET A SD  1 
ATOM   3516  C CE  . MET A  1  501 ? 28.546  -6.874  58.106  1.00 37.85  ?  501  MET A CE  1 
ATOM   3517  N N   . THR A  1  502 ? 22.748  -6.751  60.472  1.00 40.70  ?  502  THR A N   1 
ATOM   3518  C CA  . THR A  1  502 ? 22.149  -6.182  61.677  1.00 42.21  ?  502  THR A CA  1 
ATOM   3519  C C   . THR A  1  502 ? 23.082  -6.212  62.882  1.00 42.38  ?  502  THR A C   1 
ATOM   3520  O O   . THR A  1  502 ? 22.921  -5.392  63.793  1.00 43.76  ?  502  THR A O   1 
ATOM   3521  C CB  . THR A  1  502 ? 20.853  -6.918  62.023  1.00 43.47  ?  502  THR A CB  1 
ATOM   3522  O OG1 . THR A  1  502 ? 21.158  -8.254  62.444  1.00 45.33  ?  502  THR A OG1 1 
ATOM   3523  C CG2 . THR A  1  502 ? 19.930  -6.970  60.815  1.00 44.18  ?  502  THR A CG2 1 
ATOM   3524  N N   . GLN A  1  503 ? 24.050  -7.126  62.913  1.00 41.90  ?  503  GLN A N   1 
ATOM   3525  C CA  . GLN A  1  503 ? 24.900  -7.290  64.087  1.00 41.84  ?  503  GLN A CA  1 
ATOM   3526  C C   . GLN A  1  503 ? 26.061  -6.306  64.137  1.00 41.90  ?  503  GLN A C   1 
ATOM   3527  O O   . GLN A  1  503 ? 26.852  -6.360  65.086  1.00 41.50  ?  503  GLN A O   1 
ATOM   3528  C CB  . GLN A  1  503 ? 25.439  -8.722  64.150  1.00 42.52  ?  503  GLN A CB  1 
ATOM   3529  C CG  . GLN A  1  503 ? 24.424  -9.739  64.643  1.00 45.70  ?  503  GLN A CG  1 
ATOM   3530  C CD  . GLN A  1  503 ? 23.738  -9.307  65.925  1.00 47.31  ?  503  GLN A CD  1 
ATOM   3531  O OE1 . GLN A  1  503 ? 22.514  -9.377  66.041  1.00 49.32  ?  503  GLN A OE1 1 
ATOM   3532  N NE2 . GLN A  1  503 ? 24.525  -8.864  66.900  1.00 47.00  ?  503  GLN A NE2 1 
ATOM   3533  N N   . LEU A  1  504 ? 26.181  -5.414  63.159  1.00 38.82  ?  504  LEU A N   1 
ATOM   3534  C CA  . LEU A  1  504 ? 27.277  -4.455  63.148  1.00 38.33  ?  504  LEU A CA  1 
ATOM   3535  C C   . LEU A  1  504 ? 27.116  -3.441  64.274  1.00 39.35  ?  504  LEU A C   1 
ATOM   3536  O O   . LEU A  1  504 ? 26.039  -2.865  64.459  1.00 41.08  ?  504  LEU A O   1 
ATOM   3537  C CB  . LEU A  1  504 ? 27.335  -3.740  61.799  1.00 37.95  ?  504  LEU A CB  1 
ATOM   3538  C CG  . LEU A  1  504 ? 28.716  -3.483  61.196  1.00 36.41  ?  504  LEU A CG  1 
ATOM   3539  C CD1 . LEU A  1  504 ? 29.464  -4.786  60.971  1.00 35.65  ?  504  LEU A CD1 1 
ATOM   3540  C CD2 . LEU A  1  504 ? 28.580  -2.710  59.894  1.00 35.96  ?  504  LEU A CD2 1 
ATOM   3541  N N   . SER A  1  505 ? 28.191  -3.229  65.032  1.00 35.71  ?  505  SER A N   1 
ATOM   3542  C CA  . SER A  1  505 ? 28.227  -2.190  66.051  1.00 37.13  ?  505  SER A CA  1 
ATOM   3543  C C   . SER A  1  505 ? 29.203  -1.069  65.735  1.00 36.89  ?  505  SER A C   1 
ATOM   3544  O O   . SER A  1  505 ? 29.009  0.051   66.212  1.00 37.05  ?  505  SER A O   1 
ATOM   3545  C CB  . SER A  1  505 ? 28.590  -2.790  67.415  1.00 37.11  ?  505  SER A CB  1 
ATOM   3546  O OG  . SER A  1  505 ? 28.266  -1.895  68.465  1.00 37.75  ?  505  SER A OG  1 
ATOM   3547  N N   . GLN A  1  506 ? 30.240  -1.340  64.947  1.00 33.66  ?  506  GLN A N   1 
ATOM   3548  C CA  . GLN A  1  506 ? 31.192  -0.324  64.518  1.00 33.16  ?  506  GLN A CA  1 
ATOM   3549  C C   . GLN A  1  506 ? 31.431  -0.475  63.025  1.00 32.31  ?  506  GLN A C   1 
ATOM   3550  O O   . GLN A  1  506 ? 31.838  -1.547  62.566  1.00 31.65  ?  506  GLN A O   1 
ATOM   3551  C CB  . GLN A  1  506 ? 32.512  -0.436  65.284  1.00 33.76  ?  506  GLN A CB  1 
ATOM   3552  C CG  . GLN A  1  506 ? 33.650  0.367   64.673  1.00 33.78  ?  506  GLN A CG  1 
ATOM   3553  C CD  . GLN A  1  506 ? 34.767  0.636   65.660  1.00 35.06  ?  506  GLN A CD  1 
ATOM   3554  O OE1 . GLN A  1  506 ? 34.909  -0.067  66.661  1.00 35.57  ?  506  GLN A OE1 1 
ATOM   3555  N NE2 . GLN A  1  506 ? 35.566  1.661   65.386  1.00 35.54  ?  506  GLN A NE2 1 
ATOM   3556  N N   . LEU A  1  507 ? 31.188  0.593   62.272  1.00 31.99  ?  507  LEU A N   1 
ATOM   3557  C CA  . LEU A  1  507 ? 31.457  0.619   60.842  1.00 31.16  ?  507  LEU A CA  1 
ATOM   3558  C C   . LEU A  1  507 ? 32.326  1.830   60.545  1.00 30.94  ?  507  LEU A C   1 
ATOM   3559  O O   . LEU A  1  507 ? 31.976  2.954   60.917  1.00 31.04  ?  507  LEU A O   1 
ATOM   3560  C CB  . LEU A  1  507 ? 30.152  0.668   60.036  1.00 30.87  ?  507  LEU A CB  1 
ATOM   3561  C CG  . LEU A  1  507 ? 30.228  0.786   58.512  1.00 30.44  ?  507  LEU A CG  1 
ATOM   3562  C CD1 . LEU A  1  507 ? 31.174  -0.253  57.930  1.00 30.61  ?  507  LEU A CD1 1 
ATOM   3563  C CD2 . LEU A  1  507 ? 28.840  0.646   57.906  1.00 30.67  ?  507  LEU A CD2 1 
ATOM   3564  N N   . ASP A  1  508 ? 33.458  1.599   59.880  1.00 32.75  ?  508  ASP A N   1 
ATOM   3565  C CA  . ASP A  1  508 ? 34.436  2.654   59.614  1.00 32.49  ?  508  ASP A CA  1 
ATOM   3566  C C   . ASP A  1  508 ? 34.951  2.469   58.190  1.00 32.90  ?  508  ASP A C   1 
ATOM   3567  O O   . ASP A  1  508 ? 35.805  1.614   57.938  1.00 34.10  ?  508  ASP A O   1 
ATOM   3568  C CB  . ASP A  1  508 ? 35.576  2.619   60.626  1.00 33.64  ?  508  ASP A CB  1 
ATOM   3569  C CG  . ASP A  1  508 ? 36.507  3.814   60.504  1.00 33.86  ?  508  ASP A CG  1 
ATOM   3570  O OD1 . ASP A  1  508 ? 36.275  4.673   59.628  1.00 32.97  ?  508  ASP A OD1 1 
ATOM   3571  O OD2 . ASP A  1  508 ? 37.477  3.892   61.287  1.00 35.25  -1 508  ASP A OD2 1 
ATOM   3572  N N   . LEU A  1  509 ? 34.428  3.274   57.268  1.00 31.99  ?  509  LEU A N   1 
ATOM   3573  C CA  . LEU A  1  509 ? 34.893  3.309   55.888  1.00 32.44  ?  509  LEU A CA  1 
ATOM   3574  C C   . LEU A  1  509 ? 35.513  4.664   55.561  1.00 33.30  ?  509  LEU A C   1 
ATOM   3575  O O   . LEU A  1  509 ? 35.527  5.091   54.405  1.00 33.94  ?  509  LEU A O   1 
ATOM   3576  C CB  . LEU A  1  509 ? 33.749  2.990   54.927  1.00 32.45  ?  509  LEU A CB  1 
ATOM   3577  C CG  . LEU A  1  509 ? 32.984  1.696   55.209  1.00 31.77  ?  509  LEU A CG  1 
ATOM   3578  C CD1 . LEU A  1  509 ? 31.871  1.499   54.194  1.00 31.98  ?  509  LEU A CD1 1 
ATOM   3579  C CD2 . LEU A  1  509 ? 33.924  0.501   55.217  1.00 33.22  ?  509  LEU A CD2 1 
ATOM   3580  N N   . SER A  1  510 ? 36.036  5.341   56.580  1.00 35.32  ?  510  SER A N   1 
ATOM   3581  C CA  . SER A  1  510 ? 36.492  6.714   56.439  1.00 35.89  ?  510  SER A CA  1 
ATOM   3582  C C   . SER A  1  510 ? 37.768  6.796   55.605  1.00 36.91  ?  510  SER A C   1 
ATOM   3583  O O   . SER A  1  510 ? 38.499  5.817   55.435  1.00 37.91  ?  510  SER A O   1 
ATOM   3584  C CB  . SER A  1  510 ? 36.725  7.343   57.812  1.00 35.22  ?  510  SER A CB  1 
ATOM   3585  O OG  . SER A  1  510 ? 37.676  6.604   58.558  1.00 35.51  ?  510  SER A OG  1 
ATOM   3586  N N   . SER A  1  511 ? 38.018  7.993   55.068  1.00 37.06  ?  511  SER A N   1 
ATOM   3587  C CA  . SER A  1  511 ? 39.241  8.296   54.321  1.00 38.56  ?  511  SER A CA  1 
ATOM   3588  C C   . SER A  1  511 ? 39.370  7.406   53.086  1.00 40.37  ?  511  SER A C   1 
ATOM   3589  O O   . SER A  1  511 ? 40.396  6.763   52.854  1.00 41.36  ?  511  SER A O   1 
ATOM   3590  C CB  . SER A  1  511 ? 40.477  8.181   55.217  1.00 38.58  ?  511  SER A CB  1 
ATOM   3591  O OG  . SER A  1  511 ? 40.486  9.197   56.205  1.00 37.94  ?  511  SER A OG  1 
ATOM   3592  N N   . ASN A  1  512 ? 38.306  7.374   52.288  1.00 39.00  ?  512  ASN A N   1 
ATOM   3593  C CA  . ASN A  1  512 ? 38.250  6.561   51.082  1.00 40.68  ?  512  ASN A CA  1 
ATOM   3594  C C   . ASN A  1  512 ? 37.627  7.404   49.974  1.00 41.89  ?  512  ASN A C   1 
ATOM   3595  O O   . ASN A  1  512 ? 37.440  8.616   50.118  1.00 41.18  ?  512  ASN A O   1 
ATOM   3596  C CB  . ASN A  1  512 ? 37.470  5.264   51.334  1.00 41.06  ?  512  ASN A CB  1 
ATOM   3597  C CG  . ASN A  1  512 ? 38.337  4.164   51.910  1.00 41.16  ?  512  ASN A CG  1 
ATOM   3598  O OD1 . ASN A  1  512 ? 38.967  3.405   51.172  1.00 42.98  ?  512  ASN A OD1 1 
ATOM   3599  N ND2 . ASN A  1  512 ? 38.375  4.070   53.234  1.00 38.77  ?  512  ASN A ND2 1 
ATOM   3600  N N   . ARG A  1  513 ? 37.312  6.758   48.857  1.00 44.73  ?  513  ARG A N   1 
ATOM   3601  C CA  . ARG A  1  513 ? 36.675  7.404   47.718  1.00 45.06  ?  513  ARG A CA  1 
ATOM   3602  C C   . ARG A  1  513 ? 35.336  6.747   47.405  1.00 44.18  ?  513  ARG A C   1 
ATOM   3603  O O   . ARG A  1  513 ? 35.003  6.486   46.246  1.00 44.37  ?  513  ARG A O   1 
ATOM   3604  C CB  . ARG A  1  513 ? 37.592  7.389   46.498  1.00 46.44  ?  513  ARG A CB  1 
ATOM   3605  C CG  . ARG A  1  513 ? 38.852  8.226   46.667  1.00 46.56  ?  513  ARG A CG  1 
ATOM   3606  C CD  . ARG A  1  513 ? 38.509  9.661   47.040  1.00 46.33  ?  513  ARG A CD  1 
ATOM   3607  N NE  . ARG A  1  513 ? 39.262  10.633  46.255  1.00 48.34  ?  513  ARG A NE  1 
ATOM   3608  C CZ  . ARG A  1  513 ? 39.001  11.933  46.224  1.00 48.01  ?  513  ARG A CZ  1 
ATOM   3609  N NH1 . ARG A  1  513 ? 38.008  12.456  46.923  1.00 46.53  ?  513  ARG A NH1 1 
ATOM   3610  N NH2 . ARG A  1  513 ? 39.757  12.728  45.473  1.00 49.72  ?  513  ARG A NH2 1 
ATOM   3611  N N   . ILE A  1  514 ? 34.554  6.469   48.444  1.00 36.61  ?  514  ILE A N   1 
ATOM   3612  C CA  . ILE A  1  514 ? 33.247  5.842   48.278  1.00 35.81  ?  514  ILE A CA  1 
ATOM   3613  C C   . ILE A  1  514 ? 32.241  6.891   47.826  1.00 36.56  ?  514  ILE A C   1 
ATOM   3614  O O   . ILE A  1  514 ? 32.164  7.987   48.395  1.00 36.42  ?  514  ILE A O   1 
ATOM   3615  C CB  . ILE A  1  514 ? 32.795  5.164   49.582  1.00 33.71  ?  514  ILE A CB  1 
ATOM   3616  C CG1 . ILE A  1  514 ? 33.795  4.086   50.004  1.00 33.29  ?  514  ILE A CG1 1 
ATOM   3617  C CG2 . ILE A  1  514 ? 31.400  4.580   49.427  1.00 33.31  ?  514  ILE A CG2 1 
ATOM   3618  C CD1 . ILE A  1  514 ? 34.048  4.038   51.491  1.00 31.92  ?  514  ILE A CD1 1 
ATOM   3619  N N   . THR A  1  515 ? 31.465  6.553   46.802  1.00 33.76  ?  515  THR A N   1 
ATOM   3620  C CA  . THR A  1  515 ? 30.473  7.433   46.205  1.00 33.22  ?  515  THR A CA  1 
ATOM   3621  C C   . THR A  1  515 ? 29.070  6.915   46.512  1.00 32.27  ?  515  THR A C   1 
ATOM   3622  O O   . THR A  1  515 ? 28.885  5.937   47.242  1.00 30.96  ?  515  THR A O   1 
ATOM   3623  C CB  . THR A  1  515 ? 30.705  7.549   44.697  1.00 35.92  ?  515  THR A CB  1 
ATOM   3624  O OG1 . THR A  1  515 ? 30.816  6.238   44.127  1.00 36.34  ?  515  THR A OG1 1 
ATOM   3625  C CG2 . THR A  1  515 ? 31.983  8.326   44.415  1.00 37.35  ?  515  THR A CG2 1 
ATOM   3626  N N   . GLY A  1  516 ? 28.074  7.596   45.957  1.00 35.16  ?  516  GLY A N   1 
ATOM   3627  C CA  . GLY A  1  516 ? 26.690  7.234   46.186  1.00 34.85  ?  516  GLY A CA  1 
ATOM   3628  C C   . GLY A  1  516 ? 26.093  7.994   47.350  1.00 33.55  ?  516  GLY A C   1 
ATOM   3629  O O   . GLY A  1  516 ? 26.703  8.899   47.928  1.00 33.05  ?  516  GLY A O   1 
ATOM   3630  N N   . GLU A  1  517 ? 24.871  7.611   47.707  1.00 35.13  ?  517  GLU A N   1 
ATOM   3631  C CA  . GLU A  1  517 ? 24.169  8.243   48.813  1.00 34.26  ?  517  GLU A CA  1 
ATOM   3632  C C   . GLU A  1  517 ? 23.650  7.190   49.781  1.00 33.03  ?  517  GLU A C   1 
ATOM   3633  O O   . GLU A  1  517 ? 23.344  6.058   49.394  1.00 33.42  ?  517  GLU A O   1 
ATOM   3634  C CB  . GLU A  1  517 ? 23.018  9.140   48.314  1.00 35.98  ?  517  GLU A CB  1 
ATOM   3635  C CG  . GLU A  1  517 ? 22.100  8.542   47.263  1.00 37.81  ?  517  GLU A CG  1 
ATOM   3636  C CD  . GLU A  1  517 ? 21.139  9.578   46.697  1.00 39.88  ?  517  GLU A CD  1 
ATOM   3637  O OE1 . GLU A  1  517 ? 20.092  9.833   47.329  1.00 39.97  ?  517  GLU A OE1 1 
ATOM   3638  O OE2 . GLU A  1  517 ? 21.437  10.147  45.625  1.00 41.69  -1 517  GLU A OE2 1 
ATOM   3639  N N   . LEU A  1  518 ? 23.559  7.580   51.049  1.00 31.31  ?  518  LEU A N   1 
ATOM   3640  C CA  . LEU A  1  518 ? 23.117  6.670   52.098  1.00 30.47  ?  518  LEU A CA  1 
ATOM   3641  C C   . LEU A  1  518 ? 21.611  6.464   52.002  1.00 31.71  ?  518  LEU A C   1 
ATOM   3642  O O   . LEU A  1  518 ? 20.860  7.443   51.963  1.00 32.60  ?  518  LEU A O   1 
ATOM   3643  C CB  . LEU A  1  518 ? 23.480  7.222   53.473  1.00 29.42  ?  518  LEU A CB  1 
ATOM   3644  C CG  . LEU A  1  518 ? 24.712  6.651   54.176  1.00 28.17  ?  518  LEU A CG  1 
ATOM   3645  C CD1 . LEU A  1  518 ? 25.959  6.838   53.332  1.00 28.12  ?  518  LEU A CD1 1 
ATOM   3646  C CD2 . LEU A  1  518 ? 24.884  7.305   55.538  1.00 27.74  ?  518  LEU A CD2 1 
ATOM   3647  N N   . PRO A  1  519 ? 21.137  5.224   51.971  1.00 30.51  ?  519  PRO A N   1 
ATOM   3648  C CA  . PRO A  1  519 ? 19.701  4.983   51.830  1.00 32.17  ?  519  PRO A CA  1 
ATOM   3649  C C   . PRO A  1  519 ? 18.974  5.126   53.157  1.00 32.10  ?  519  PRO A C   1 
ATOM   3650  O O   . PRO A  1  519 ? 19.573  5.140   54.233  1.00 30.81  ?  519  PRO A O   1 
ATOM   3651  C CB  . PRO A  1  519 ? 19.647  3.538   51.329  1.00 32.91  ?  519  PRO A CB  1 
ATOM   3652  C CG  . PRO A  1  519 ? 20.812  2.904   52.006  1.00 31.18  ?  519  PRO A CG  1 
ATOM   3653  C CD  . PRO A  1  519 ? 21.897  3.963   52.052  1.00 29.82  ?  519  PRO A CD  1 
ATOM   3654  N N   . GLU A  1  520 ? 17.648  5.232   53.062  1.00 32.21  ?  520  GLU A N   1 
ATOM   3655  C CA  . GLU A  1  520 ? 16.829  5.194   54.266  1.00 33.71  ?  520  GLU A CA  1 
ATOM   3656  C C   . GLU A  1  520 ? 16.857  3.828   54.936  1.00 34.36  ?  520  GLU A C   1 
ATOM   3657  O O   . GLU A  1  520 ? 16.396  3.702   56.075  1.00 35.34  ?  520  GLU A O   1 
ATOM   3658  C CB  . GLU A  1  520 ? 15.390  5.597   53.941  1.00 36.08  ?  520  GLU A CB  1 
ATOM   3659  C CG  . GLU A  1  520 ? 15.243  7.031   53.439  1.00 35.94  ?  520  GLU A CG  1 
ATOM   3660  C CD  . GLU A  1  520 ? 15.476  8.082   54.517  1.00 35.12  ?  520  GLU A CD  1 
ATOM   3661  O OE1 . GLU A  1  520 ? 15.819  7.722   55.663  1.00 34.61  ?  520  GLU A OE1 1 
ATOM   3662  O OE2 . GLU A  1  520 ? 15.319  9.283   54.210  1.00 35.23  -1 520  GLU A OE2 1 
ATOM   3663  N N   . SER A  1  521 ? 17.400  2.812   54.259  1.00 34.66  ?  521  SER A N   1 
ATOM   3664  C CA  . SER A  1  521 ? 17.652  1.509   54.858  1.00 35.25  ?  521  SER A CA  1 
ATOM   3665  C C   . SER A  1  521 ? 18.762  1.554   55.899  1.00 34.68  ?  521  SER A C   1 
ATOM   3666  O O   . SER A  1  521 ? 19.006  0.540   56.563  1.00 35.56  ?  521  SER A O   1 
ATOM   3667  C CB  . SER A  1  521 ? 18.000  0.493   53.768  1.00 34.05  ?  521  SER A CB  1 
ATOM   3668  O OG  . SER A  1  521 ? 18.223  -0.794  54.317  1.00 34.88  ?  521  SER A OG  1 
ATOM   3669  N N   . ILE A  1  522 ? 19.444  2.696   56.038  1.00 34.98  ?  522  ILE A N   1 
ATOM   3670  C CA  . ILE A  1  522 ? 20.464  2.887   57.069  1.00 34.78  ?  522  ILE A CA  1 
ATOM   3671  C C   . ILE A  1  522 ? 19.943  2.506   58.449  1.00 37.39  ?  522  ILE A C   1 
ATOM   3672  O O   . ILE A  1  522 ? 20.725  2.160   59.343  1.00 37.36  ?  522  ILE A O   1 
ATOM   3673  C CB  . ILE A  1  522 ? 20.962  4.349   57.036  1.00 33.38  ?  522  ILE A CB  1 
ATOM   3674  C CG1 . ILE A  1  522 ? 22.299  4.486   57.758  1.00 31.84  ?  522  ILE A CG1 1 
ATOM   3675  C CG2 . ILE A  1  522 ? 19.925  5.282   57.632  1.00 34.96  ?  522  ILE A CG2 1 
ATOM   3676  C CD1 . ILE A  1  522 ? 23.326  3.505   57.313  1.00 30.85  ?  522  ILE A CD1 1 
ATOM   3677  N N   . SER A  1  523 ? 18.623  2.559   58.648  1.00 37.72  ?  523  SER A N   1 
ATOM   3678  C CA  . SER A  1  523 ? 18.019  2.226   59.933  1.00 38.98  ?  523  SER A CA  1 
ATOM   3679  C C   . SER A  1  523 ? 18.209  0.762   60.316  1.00 39.36  ?  523  SER A C   1 
ATOM   3680  O O   . SER A  1  523 ? 18.032  0.413   61.488  1.00 39.99  ?  523  SER A O   1 
ATOM   3681  C CB  . SER A  1  523 ? 16.528  2.564   59.900  1.00 39.49  ?  523  SER A CB  1 
ATOM   3682  O OG  . SER A  1  523 ? 15.927  2.366   61.165  1.00 40.79  ?  523  SER A OG  1 
ATOM   3683  N N   . ASN A  1  524 ? 18.563  -0.097  59.359  1.00 40.56  ?  524  ASN A N   1 
ATOM   3684  C CA  . ASN A  1  524 ? 18.608  -1.540  59.570  1.00 39.94  ?  524  ASN A CA  1 
ATOM   3685  C C   . ASN A  1  524 ? 19.734  -1.990  60.497  1.00 39.33  ?  524  ASN A C   1 
ATOM   3686  O O   . ASN A  1  524 ? 19.783  -3.176  60.843  1.00 37.87  ?  524  ASN A O   1 
ATOM   3687  C CB  . ASN A  1  524 ? 18.739  -2.250  58.221  1.00 38.26  ?  524  ASN A CB  1 
ATOM   3688  C CG  . ASN A  1  524 ? 17.401  -2.464  57.543  1.00 38.17  ?  524  ASN A CG  1 
ATOM   3689  O OD1 . ASN A  1  524 ? 16.401  -1.844  57.906  1.00 39.53  ?  524  ASN A OD1 1 
ATOM   3690  N ND2 . ASN A  1  524 ? 17.375  -3.346  56.549  1.00 37.94  ?  524  ASN A ND2 1 
ATOM   3691  N N   . ILE A  1  525 ? 20.629  -1.093  60.907  1.00 38.87  ?  525  ILE A N   1 
ATOM   3692  C CA  . ILE A  1  525 ? 21.819  -1.469  61.666  1.00 38.15  ?  525  ILE A CA  1 
ATOM   3693  C C   . ILE A  1  525 ? 21.755  -0.849  63.055  1.00 38.77  ?  525  ILE A C   1 
ATOM   3694  O O   . ILE A  1  525 ? 22.789  -0.507  63.639  1.00 37.92  ?  525  ILE A O   1 
ATOM   3695  C CB  . ILE A  1  525 ? 23.121  -1.063  60.951  1.00 36.04  ?  525  ILE A CB  1 
ATOM   3696  C CG1 . ILE A  1  525 ? 23.055  0.389   60.483  1.00 34.98  ?  525  ILE A CG1 1 
ATOM   3697  C CG2 . ILE A  1  525 ? 23.401  -1.998  59.783  1.00 35.94  ?  525  ILE A CG2 1 
ATOM   3698  C CD1 . ILE A  1  525 ? 24.282  0.835   59.717  1.00 33.40  ?  525  ILE A CD1 1 
ATOM   3699  N N   . ASN A  1  526 ? 20.538  -0.700  63.588  1.00 40.44  ?  526  ASN A N   1 
ATOM   3700  C CA  . ASN A  1  526 ? 20.303  0.064   64.813  1.00 42.01  ?  526  ASN A CA  1 
ATOM   3701  C C   . ASN A  1  526 ? 21.181  -0.373  65.982  1.00 40.87  ?  526  ASN A C   1 
ATOM   3702  O O   . ASN A  1  526 ? 21.292  0.365   66.967  1.00 40.92  ?  526  ASN A O   1 
ATOM   3703  C CB  . ASN A  1  526 ? 18.826  -0.043  65.209  1.00 42.05  ?  526  ASN A CB  1 
ATOM   3704  C CG  . ASN A  1  526 ? 18.414  -1.463  65.555  1.00 40.80  ?  526  ASN A CG  1 
ATOM   3705  O OD1 . ASN A  1  526 ? 19.082  -2.427  65.177  1.00 39.50  ?  526  ASN A OD1 1 
ATOM   3706  N ND2 . ASN A  1  526 ? 17.308  -1.598  66.279  1.00 41.60  ?  526  ASN A ND2 1 
ATOM   3707  N N   . ARG A  1  527 ? 21.807  -1.549  65.903  1.00 43.36  ?  527  ARG A N   1 
ATOM   3708  C CA  . ARG A  1  527 ? 22.762  -1.962  66.925  1.00 42.28  ?  527  ARG A CA  1 
ATOM   3709  C C   . ARG A  1  527 ? 24.074  -1.189  66.857  1.00 41.58  ?  527  ARG A C   1 
ATOM   3710  O O   . ARG A  1  527 ? 24.917  -1.363  67.743  1.00 40.28  ?  527  ARG A O   1 
ATOM   3711  C CB  . ARG A  1  527 ? 23.057  -3.458  66.802  1.00 40.77  ?  527  ARG A CB  1 
ATOM   3712  C CG  . ARG A  1  527 ? 22.008  -4.368  67.417  1.00 41.25  ?  527  ARG A CG  1 
ATOM   3713  C CD  . ARG A  1  527 ? 22.473  -5.816  67.389  1.00 41.51  ?  527  ARG A CD  1 
ATOM   3714  N NE  . ARG A  1  527 ? 21.361  -6.757  67.426  1.00 44.30  ?  527  ARG A NE  1 
ATOM   3715  C CZ  . ARG A  1  527 ? 20.872  -7.292  68.536  1.00 47.51  ?  527  ARG A CZ  1 
ATOM   3716  N NH1 . ARG A  1  527 ? 21.371  -6.994  69.725  1.00 48.39  ?  527  ARG A NH1 1 
ATOM   3717  N NH2 . ARG A  1  527 ? 19.857  -8.146  68.452  1.00 50.28  ?  527  ARG A NH2 1 
ATOM   3718  N N   . ILE A  1  528 ? 24.269  -0.353  65.834  1.00 39.99  ?  528  ILE A N   1 
ATOM   3719  C CA  . ILE A  1  528 ? 25.531  0.358   65.672  1.00 38.18  ?  528  ILE A CA  1 
ATOM   3720  C C   . ILE A  1  528 ? 25.699  1.398   66.776  1.00 37.87  ?  528  ILE A C   1 
ATOM   3721  O O   . ILE A  1  528 ? 24.723  1.937   67.317  1.00 39.17  ?  528  ILE A O   1 
ATOM   3722  C CB  . ILE A  1  528 ? 25.600  1.011   64.277  1.00 38.26  ?  528  ILE A CB  1 
ATOM   3723  C CG1 . ILE A  1  528 ? 27.014  1.514   63.974  1.00 36.06  ?  528  ILE A CG1 1 
ATOM   3724  C CG2 . ILE A  1  528 ? 24.589  2.146   64.161  1.00 40.49  ?  528  ILE A CG2 1 
ATOM   3725  C CD1 . ILE A  1  528 ? 27.495  1.185   62.580  1.00 34.99  ?  528  ILE A CD1 1 
ATOM   3726  N N   . SER A  1  529 ? 26.957  1.672   67.125  1.00 36.93  ?  529  SER A N   1 
ATOM   3727  C CA  . SER A  1  529 ? 27.299  2.752   68.043  1.00 37.86  ?  529  SER A CA  1 
ATOM   3728  C C   . SER A  1  529 ? 28.407  3.661   67.535  1.00 36.68  ?  529  SER A C   1 
ATOM   3729  O O   . SER A  1  529 ? 28.528  4.786   68.036  1.00 37.44  ?  529  SER A O   1 
ATOM   3730  C CB  . SER A  1  529 ? 27.714  2.187   69.410  1.00 40.00  ?  529  SER A CB  1 
ATOM   3731  O OG  . SER A  1  529 ? 28.774  1.256   69.278  1.00 39.66  ?  529  SER A OG  1 
ATOM   3732  N N   . LYS A  1  530 ? 29.215  3.223   66.572  1.00 36.20  ?  530  LYS A N   1 
ATOM   3733  C CA  . LYS A  1  530 ? 30.225  4.064   65.940  1.00 35.05  ?  530  LYS A CA  1 
ATOM   3734  C C   . LYS A  1  530 ? 30.030  3.992   64.434  1.00 34.74  ?  530  LYS A C   1 
ATOM   3735  O O   . LYS A  1  530 ? 30.173  2.919   63.839  1.00 34.88  ?  530  LYS A O   1 
ATOM   3736  C CB  . LYS A  1  530 ? 31.639  3.619   66.326  1.00 35.07  ?  530  LYS A CB  1 
ATOM   3737  C CG  . LYS A  1  530 ? 32.370  4.602   67.226  1.00 34.89  ?  530  LYS A CG  1 
ATOM   3738  C CD  . LYS A  1  530 ? 33.767  4.115   67.571  1.00 36.16  ?  530  LYS A CD  1 
ATOM   3739  C CE  . LYS A  1  530 ? 34.477  5.093   68.494  1.00 36.33  ?  530  LYS A CE  1 
ATOM   3740  N NZ  . LYS A  1  530 ? 35.943  4.843   68.544  1.00 37.29  ?  530  LYS A NZ  1 
ATOM   3741  N N   . LEU A  1  531 ? 29.702  5.127   63.822  1.00 33.68  ?  531  LEU A N   1 
ATOM   3742  C CA  . LEU A  1  531 ? 29.514  5.221   62.378  1.00 32.77  ?  531  LEU A CA  1 
ATOM   3743  C C   . LEU A  1  531 ? 30.497  6.255   61.849  1.00 31.46  ?  531  LEU A C   1 
ATOM   3744  O O   . LEU A  1  531 ? 30.311  7.459   62.058  1.00 32.03  ?  531  LEU A O   1 
ATOM   3745  C CB  . LEU A  1  531 ? 28.072  5.599   62.037  1.00 32.53  ?  531  LEU A CB  1 
ATOM   3746  C CG  . LEU A  1  531 ? 27.650  5.536   60.568  1.00 31.05  ?  531  LEU A CG  1 
ATOM   3747  C CD1 . LEU A  1  531 ? 28.265  4.324   59.886  1.00 30.91  ?  531  LEU A CD1 1 
ATOM   3748  C CD2 . LEU A  1  531 ? 26.134  5.509   60.452  1.00 31.86  ?  531  LEU A CD2 1 
ATOM   3749  N N   . GLN A  1  532 ? 31.543  5.790   61.172  1.00 32.91  ?  532  GLN A N   1 
ATOM   3750  C CA  . GLN A  1  532 ? 32.587  6.655   60.627  1.00 32.27  ?  532  GLN A CA  1 
ATOM   3751  C C   . GLN A  1  532 ? 32.587  6.512   59.107  1.00 32.07  ?  532  GLN A C   1 
ATOM   3752  O O   . GLN A  1  532 ? 33.243  5.627   58.551  1.00 32.40  ?  532  GLN A O   1 
ATOM   3753  C CB  . GLN A  1  532 ? 33.945  6.316   61.232  1.00 33.58  ?  532  GLN A CB  1 
ATOM   3754  C CG  . GLN A  1  532 ? 33.943  6.288   62.752  1.00 35.01  ?  532  GLN A CG  1 
ATOM   3755  C CD  . GLN A  1  532 ? 35.162  5.593   63.325  1.00 37.01  ?  532  GLN A CD  1 
ATOM   3756  O OE1 . GLN A  1  532 ? 35.050  4.558   63.981  1.00 39.08  ?  532  GLN A OE1 1 
ATOM   3757  N NE2 . GLN A  1  532 ? 36.335  6.166   63.086  1.00 37.03  ?  532  GLN A NE2 1 
ATOM   3758  N N   . LEU A  1  533 ? 31.849  7.395   58.437  1.00 31.28  ?  533  LEU A N   1 
ATOM   3759  C CA  . LEU A  1  533 ? 31.780  7.434   56.983  1.00 31.51  ?  533  LEU A CA  1 
ATOM   3760  C C   . LEU A  1  533 ? 32.420  8.693   56.416  1.00 32.45  ?  533  LEU A C   1 
ATOM   3761  O O   . LEU A  1  533 ? 32.231  9.000   55.234  1.00 34.08  ?  533  LEU A O   1 
ATOM   3762  C CB  . LEU A  1  533 ? 30.325  7.330   56.521  1.00 30.79  ?  533  LEU A CB  1 
ATOM   3763  C CG  . LEU A  1  533 ? 29.585  6.055   56.927  1.00 30.49  ?  533  LEU A CG  1 
ATOM   3764  C CD1 . LEU A  1  533 ? 28.163  6.071   56.397  1.00 30.44  ?  533  LEU A CD1 1 
ATOM   3765  C CD2 . LEU A  1  533 ? 30.330  4.820   56.446  1.00 31.85  ?  533  LEU A CD2 1 
ATOM   3766  N N   . ASN A  1  534 ? 33.174  9.423   57.233  1.00 32.67  ?  534  ASN A N   1 
ATOM   3767  C CA  . ASN A  1  534 ? 33.702  10.722  56.851  1.00 34.20  ?  534  ASN A CA  1 
ATOM   3768  C C   . ASN A  1  534 ? 34.832  10.584  55.834  1.00 35.08  ?  534  ASN A C   1 
ATOM   3769  O O   . ASN A  1  534 ? 35.418  9.515   55.652  1.00 34.56  ?  534  ASN A O   1 
ATOM   3770  C CB  . ASN A  1  534 ? 34.207  11.472  58.083  1.00 35.25  ?  534  ASN A CB  1 
ATOM   3771  C CG  . ASN A  1  534 ? 35.184  10.651  58.902  1.00 35.20  ?  534  ASN A CG  1 
ATOM   3772  O OD1 . ASN A  1  534 ? 34.861  9.552   59.354  1.00 33.98  ?  534  ASN A OD1 1 
ATOM   3773  N ND2 . ASN A  1  534 ? 36.388  11.177  59.091  1.00 36.85  ?  534  ASN A ND2 1 
ATOM   3774  N N   . GLY A  1  535 ? 35.134  11.695  55.167  1.00 36.38  ?  535  GLY A N   1 
ATOM   3775  C CA  . GLY A  1  535 ? 36.212  11.725  54.197  1.00 37.61  ?  535  GLY A CA  1 
ATOM   3776  C C   . GLY A  1  535 ? 35.941  10.873  52.976  1.00 38.69  ?  535  GLY A C   1 
ATOM   3777  O O   . GLY A  1  535 ? 36.778  10.052  52.588  1.00 39.60  ?  535  GLY A O   1 
ATOM   3778  N N   . ASN A  1  536 ? 34.774  11.051  52.366  1.00 35.60  ?  536  ASN A N   1 
ATOM   3779  C CA  . ASN A  1  536 ? 34.386  10.268  51.202  1.00 37.01  ?  536  ASN A CA  1 
ATOM   3780  C C   . ASN A  1  536 ? 33.660  11.188  50.227  1.00 37.67  ?  536  ASN A C   1 
ATOM   3781  O O   . ASN A  1  536 ? 33.581  12.404  50.430  1.00 38.05  ?  536  ASN A O   1 
ATOM   3782  C CB  . ASN A  1  536 ? 33.534  9.067   51.631  1.00 36.55  ?  536  ASN A CB  1 
ATOM   3783  C CG  . ASN A  1  536 ? 34.375  7.863   52.000  1.00 36.97  ?  536  ASN A CG  1 
ATOM   3784  O OD1 . ASN A  1  536 ? 34.908  7.177   51.131  1.00 38.68  ?  536  ASN A OD1 1 
ATOM   3785  N ND2 . ASN A  1  536 ? 34.510  7.610   53.296  1.00 35.20  ?  536  ASN A ND2 1 
ATOM   3786  N N   . ARG A  1  537 ? 33.115  10.602  49.161  1.00 39.79  ?  537  ARG A N   1 
ATOM   3787  C CA  . ARG A  1  537 ? 32.338  11.340  48.174  1.00 39.79  ?  537  ARG A CA  1 
ATOM   3788  C C   . ARG A  1  537 ? 30.861  10.962  48.234  1.00 38.35  ?  537  ARG A C   1 
ATOM   3789  O O   . ARG A  1  537 ? 30.180  10.920  47.206  1.00 38.16  ?  537  ARG A O   1 
ATOM   3790  C CB  . ARG A  1  537 ? 32.895  11.120  46.768  1.00 41.71  ?  537  ARG A CB  1 
ATOM   3791  C CG  . ARG A  1  537 ? 34.411  11.158  46.684  1.00 42.93  ?  537  ARG A CG  1 
ATOM   3792  C CD  . ARG A  1  537 ? 34.874  11.898  45.438  1.00 44.08  ?  537  ARG A CD  1 
ATOM   3793  N NE  . ARG A  1  537 ? 34.795  11.074  44.238  1.00 45.09  ?  537  ARG A NE  1 
ATOM   3794  C CZ  . ARG A  1  537 ? 34.756  11.553  43.002  1.00 47.14  ?  537  ARG A CZ  1 
ATOM   3795  N NH1 . ARG A  1  537 ? 34.787  12.854  42.762  1.00 49.31  ?  537  ARG A NH1 1 
ATOM   3796  N NH2 . ARG A  1  537 ? 34.687  10.705  41.979  1.00 48.38  ?  537  ARG A NH2 1 
ATOM   3797  N N   . LEU A  1  538 ? 30.361  10.680  49.434  1.00 34.72  ?  538  LEU A N   1 
ATOM   3798  C CA  . LEU A  1  538 ? 28.942  10.406  49.611  1.00 34.02  ?  538  LEU A CA  1 
ATOM   3799  C C   . LEU A  1  538 ? 28.129  11.665  49.339  1.00 35.39  ?  538  LEU A C   1 
ATOM   3800  O O   . LEU A  1  538 ? 28.466  12.755  49.808  1.00 35.96  ?  538  LEU A O   1 
ATOM   3801  C CB  . LEU A  1  538 ? 28.670  9.884   51.021  1.00 32.09  ?  538  LEU A CB  1 
ATOM   3802  C CG  . LEU A  1  538 ? 29.398  8.586   51.379  1.00 30.90  ?  538  LEU A CG  1 
ATOM   3803  C CD1 . LEU A  1  538 ? 29.315  8.307   52.868  1.00 29.54  ?  538  LEU A CD1 1 
ATOM   3804  C CD2 . LEU A  1  538 ? 28.827  7.424   50.579  1.00 31.00  ?  538  LEU A CD2 1 
ATOM   3805  N N   . SER A  1  539 ? 27.042  11.503  48.588  1.00 33.54  ?  539  SER A N   1 
ATOM   3806  C CA  . SER A  1  539 ? 26.248  12.622  48.101  1.00 35.33  ?  539  SER A CA  1 
ATOM   3807  C C   . SER A  1  539 ? 24.792  12.430  48.499  1.00 34.93  ?  539  SER A C   1 
ATOM   3808  O O   . SER A  1  539 ? 24.475  11.560  49.315  1.00 33.27  ?  539  SER A O   1 
ATOM   3809  C CB  . SER A  1  539 ? 26.390  12.765  46.583  1.00 37.72  ?  539  SER A CB  1 
ATOM   3810  O OG  . SER A  1  539 ? 26.448  11.496  45.956  1.00 37.54  ?  539  SER A OG  1 
ATOM   3811  N N   . GLY A  1  540 ? 23.909  13.271  47.977  1.00 36.79  ?  540  GLY A N   1 
ATOM   3812  C CA  . GLY A  1  540 ? 22.503  13.178  48.313  1.00 36.89  ?  540  GLY A CA  1 
ATOM   3813  C C   . GLY A  1  540 ? 22.243  13.677  49.723  1.00 35.76  ?  540  GLY A C   1 
ATOM   3814  O O   . GLY A  1  540 ? 23.132  14.152  50.426  1.00 35.01  ?  540  GLY A O   1 
ATOM   3815  N N   . LYS A  1  541 ? 20.986  13.562  50.138  1.00 34.96  ?  541  LYS A N   1 
ATOM   3816  C CA  . LYS A  1  541 ? 20.613  14.003  51.473  1.00 34.32  ?  541  LYS A CA  1 
ATOM   3817  C C   . LYS A  1  541 ? 20.983  12.945  52.507  1.00 32.27  ?  541  LYS A C   1 
ATOM   3818  O O   . LYS A  1  541 ? 21.100  11.755  52.199  1.00 31.51  ?  541  LYS A O   1 
ATOM   3819  C CB  . LYS A  1  541 ? 19.115  14.312  51.545  1.00 35.79  ?  541  LYS A CB  1 
ATOM   3820  C CG  . LYS A  1  541 ? 18.246  13.147  52.002  1.00 35.28  ?  541  LYS A CG  1 
ATOM   3821  C CD  . LYS A  1  541 ? 16.766  13.501  51.964  1.00 37.26  ?  541  LYS A CD  1 
ATOM   3822  C CE  . LYS A  1  541 ? 16.203  13.404  50.551  1.00 39.16  ?  541  LYS A CE  1 
ATOM   3823  N NZ  . LYS A  1  541 ? 14.763  13.793  50.492  1.00 41.45  ?  541  LYS A NZ  1 
ATOM   3824  N N   . ILE A  1  542 ? 21.191  13.396  53.740  1.00 34.04  ?  542  ILE A N   1 
ATOM   3825  C CA  . ILE A  1  542 ? 21.413  12.493  54.866  1.00 32.59  ?  542  ILE A CA  1 
ATOM   3826  C C   . ILE A  1  542 ? 20.091  11.805  55.182  1.00 33.04  ?  542  ILE A C   1 
ATOM   3827  O O   . ILE A  1  542 ? 19.085  12.487  55.424  1.00 34.37  ?  542  ILE A O   1 
ATOM   3828  C CB  . ILE A  1  542 ? 21.970  13.238  56.090  1.00 32.45  ?  542  ILE A CB  1 
ATOM   3829  C CG1 . ILE A  1  542 ? 23.414  13.676  55.837  1.00 32.14  ?  542  ILE A CG1 1 
ATOM   3830  C CG2 . ILE A  1  542 ? 21.885  12.365  57.331  1.00 31.61  ?  542  ILE A CG2 1 
ATOM   3831  C CD1 . ILE A  1  542 ? 24.002  14.516  56.950  1.00 32.55  ?  542  ILE A CD1 1 
ATOM   3832  N N   . PRO A  1  543 ? 20.039  10.474  55.177  1.00 32.46  ?  543  PRO A N   1 
ATOM   3833  C CA  . PRO A  1  543 ? 18.757  9.790   55.371  1.00 34.84  ?  543  PRO A CA  1 
ATOM   3834  C C   . PRO A  1  543 ? 18.185  10.058  56.754  1.00 35.64  ?  543  PRO A C   1 
ATOM   3835  O O   . PRO A  1  543 ? 18.910  10.111  57.749  1.00 34.94  ?  543  PRO A O   1 
ATOM   3836  C CB  . PRO A  1  543 ? 19.115  8.311   55.187  1.00 35.11  ?  543  PRO A CB  1 
ATOM   3837  C CG  . PRO A  1  543 ? 20.566  8.233   55.536  1.00 32.63  ?  543  PRO A CG  1 
ATOM   3838  C CD  . PRO A  1  543 ? 21.166  9.531   55.080  1.00 30.96  ?  543  PRO A CD  1 
ATOM   3839  N N   . SER A  1  544 ? 16.863  10.229  56.809  1.00 36.60  ?  544  SER A N   1 
ATOM   3840  C CA  . SER A  1  544 ? 16.191  10.394  58.091  1.00 37.93  ?  544  SER A CA  1 
ATOM   3841  C C   . SER A  1  544 ? 16.202  9.116   58.917  1.00 39.71  ?  544  SER A C   1 
ATOM   3842  O O   . SER A  1  544 ? 15.847  9.160   60.100  1.00 41.07  ?  544  SER A O   1 
ATOM   3843  C CB  . SER A  1  544 ? 14.753  10.872  57.881  1.00 39.11  ?  544  SER A CB  1 
ATOM   3844  O OG  . SER A  1  544 ? 13.921  9.818   57.431  1.00 41.86  ?  544  SER A OG  1 
ATOM   3845  N N   . GLY A  1  545 ? 16.596  7.987   58.326  1.00 37.71  ?  545  GLY A N   1 
ATOM   3846  C CA  . GLY A  1  545 ? 16.711  6.737   59.054  1.00 39.68  ?  545  GLY A CA  1 
ATOM   3847  C C   . GLY A  1  545 ? 17.806  6.719   60.100  1.00 39.05  ?  545  GLY A C   1 
ATOM   3848  O O   . GLY A  1  545 ? 17.874  5.761   60.877  1.00 41.08  ?  545  GLY A O   1 
ATOM   3849  N N   . ILE A  1  546 ? 18.664  7.743   60.132  1.00 40.40  ?  546  ILE A N   1 
ATOM   3850  C CA  . ILE A  1  546 ? 19.630  7.878   61.216  1.00 40.03  ?  546  ILE A CA  1 
ATOM   3851  C C   . ILE A  1  546 ? 18.924  8.110   62.544  1.00 41.72  ?  546  ILE A C   1 
ATOM   3852  O O   . ILE A  1  546 ? 19.488  7.821   63.606  1.00 41.79  ?  546  ILE A O   1 
ATOM   3853  C CB  . ILE A  1  546 ? 20.628  9.017   60.905  1.00 36.53  ?  546  ILE A CB  1 
ATOM   3854  C CG1 . ILE A  1  546 ? 21.232  8.838   59.512  1.00 34.91  ?  546  ILE A CG1 1 
ATOM   3855  C CG2 . ILE A  1  546 ? 21.742  9.065   61.941  1.00 35.52  ?  546  ILE A CG2 1 
ATOM   3856  C CD1 . ILE A  1  546 ? 22.162  7.658   59.403  1.00 34.74  ?  546  ILE A CD1 1 
ATOM   3857  N N   . ARG A  1  547 ? 17.687  8.617   62.507  1.00 42.22  ?  547  ARG A N   1 
ATOM   3858  C CA  . ARG A  1  547 ? 16.914  8.814   63.731  1.00 43.50  ?  547  ARG A CA  1 
ATOM   3859  C C   . ARG A  1  547 ? 16.797  7.526   64.534  1.00 45.45  ?  547  ARG A C   1 
ATOM   3860  O O   . ARG A  1  547 ? 16.883  7.543   65.768  1.00 45.98  ?  547  ARG A O   1 
ATOM   3861  C CB  . ARG A  1  547 ? 15.520  9.345   63.389  1.00 44.35  ?  547  ARG A CB  1 
ATOM   3862  C CG  . ARG A  1  547 ? 14.451  8.975   64.412  1.00 47.11  ?  547  ARG A CG  1 
ATOM   3863  C CD  . ARG A  1  547 ? 13.054  9.280   63.904  1.00 48.16  ?  547  ARG A CD  1 
ATOM   3864  N NE  . ARG A  1  547 ? 12.971  9.183   62.451  1.00 48.45  ?  547  ARG A NE  1 
ATOM   3865  C CZ  . ARG A  1  547 ? 12.402  8.179   61.798  1.00 49.25  ?  547  ARG A CZ  1 
ATOM   3866  N NH1 . ARG A  1  547 ? 11.823  7.177   62.438  1.00 50.39  ?  547  ARG A NH1 1 
ATOM   3867  N NH2 . ARG A  1  547 ? 12.411  8.183   60.468  1.00 47.91  ?  547  ARG A NH2 1 
ATOM   3868  N N   . LEU A  1  548 ? 16.622  6.399   63.853  1.00 40.02  ?  548  LEU A N   1 
ATOM   3869  C CA  . LEU A  1  548 ? 16.298  5.139   64.506  1.00 41.37  ?  548  LEU A CA  1 
ATOM   3870  C C   . LEU A  1  548 ? 17.526  4.364   64.968  1.00 40.19  ?  548  LEU A C   1 
ATOM   3871  O O   . LEU A  1  548 ? 17.378  3.252   65.484  1.00 41.40  ?  548  LEU A O   1 
ATOM   3872  C CB  . LEU A  1  548 ? 15.458  4.269   63.568  1.00 42.12  ?  548  LEU A CB  1 
ATOM   3873  C CG  . LEU A  1  548 ? 14.068  4.829   63.257  1.00 44.11  ?  548  LEU A CG  1 
ATOM   3874  C CD1 . LEU A  1  548 ? 13.342  3.969   62.234  1.00 45.04  ?  548  LEU A CD1 1 
ATOM   3875  C CD2 . LEU A  1  548 ? 13.252  4.954   64.532  1.00 46.82  ?  548  LEU A CD2 1 
ATOM   3876  N N   . LEU A  1  549 ? 18.729  4.913   64.795  1.00 41.58  ?  549  LEU A N   1 
ATOM   3877  C CA  . LEU A  1  549 ? 19.941  4.295   65.333  1.00 41.72  ?  549  LEU A CA  1 
ATOM   3878  C C   . LEU A  1  549 ? 20.171  4.864   66.731  1.00 41.62  ?  549  LEU A C   1 
ATOM   3879  O O   . LEU A  1  549 ? 21.024  5.723   66.960  1.00 40.20  ?  549  LEU A O   1 
ATOM   3880  C CB  . LEU A  1  549 ? 21.128  4.545   64.411  1.00 40.23  ?  549  LEU A CB  1 
ATOM   3881  C CG  . LEU A  1  549 ? 20.884  4.398   62.906  1.00 39.98  ?  549  LEU A CG  1 
ATOM   3882  C CD1 . LEU A  1  549 ? 22.068  4.927   62.110  1.00 37.04  ?  549  LEU A CD1 1 
ATOM   3883  C CD2 . LEU A  1  549 ? 20.598  2.952   62.540  1.00 40.84  ?  549  LEU A CD2 1 
ATOM   3884  N N   . THR A  1  550 ? 19.382  4.366   67.687  1.00 40.71  ?  550  THR A N   1 
ATOM   3885  C CA  . THR A  1  550 ? 19.368  4.954   69.024  1.00 42.70  ?  550  THR A CA  1 
ATOM   3886  C C   . THR A  1  550 ? 20.600  4.592   69.844  1.00 42.72  ?  550  THR A C   1 
ATOM   3887  O O   . THR A  1  550 ? 20.991  5.358   70.731  1.00 43.81  ?  550  THR A O   1 
ATOM   3888  C CB  . THR A  1  550 ? 18.106  4.526   69.775  1.00 45.76  ?  550  THR A CB  1 
ATOM   3889  O OG1 . THR A  1  550 ? 18.100  3.101   69.930  1.00 46.56  ?  550  THR A OG1 1 
ATOM   3890  C CG2 . THR A  1  550 ? 16.861  4.956   69.013  1.00 46.17  ?  550  THR A CG2 1 
ATOM   3891  N N   . ASN A  1  551 ? 21.220  3.445   69.576  1.00 46.78  ?  551  ASN A N   1 
ATOM   3892  C CA  . ASN A  1  551 ? 22.427  3.047   70.291  1.00 46.01  ?  551  ASN A CA  1 
ATOM   3893  C C   . ASN A  1  551 ? 23.668  3.780   69.802  1.00 44.28  ?  551  ASN A C   1 
ATOM   3894  O O   . ASN A  1  551 ? 24.762  3.536   70.322  1.00 42.68  ?  551  ASN A O   1 
ATOM   3895  C CB  . ASN A  1  551 ? 22.631  1.535   70.179  1.00 46.00  ?  551  ASN A CB  1 
ATOM   3896  C CG  . ASN A  1  551 ? 21.904  0.771   71.267  1.00 46.73  ?  551  ASN A CG  1 
ATOM   3897  O OD1 . ASN A  1  551 ? 20.746  0.385   71.102  1.00 47.36  ?  551  ASN A OD1 1 
ATOM   3898  N ND2 . ASN A  1  551 ? 22.577  0.556   72.391  1.00 46.34  ?  551  ASN A ND2 1 
ATOM   3899  N N   . LEU A  1  552 ? 23.516  4.653   68.811  1.00 41.91  ?  552  LEU A N   1 
ATOM   3900  C CA  . LEU A  1  552 ? 24.635  5.377   68.228  1.00 40.19  ?  552  LEU A CA  1 
ATOM   3901  C C   . LEU A  1  552 ? 25.305  6.284   69.256  1.00 41.55  ?  552  LEU A C   1 
ATOM   3902  O O   . LEU A  1  552 ? 24.636  7.038   69.969  1.00 43.28  ?  552  LEU A O   1 
ATOM   3903  C CB  . LEU A  1  552 ? 24.126  6.191   67.039  1.00 38.87  ?  552  LEU A CB  1 
ATOM   3904  C CG  . LEU A  1  552 ? 25.042  7.017   66.147  1.00 37.33  ?  552  LEU A CG  1 
ATOM   3905  C CD1 . LEU A  1  552 ? 26.058  6.137   65.452  1.00 35.85  ?  552  LEU A CD1 1 
ATOM   3906  C CD2 . LEU A  1  552 ? 24.168  7.732   65.137  1.00 36.85  ?  552  LEU A CD2 1 
ATOM   3907  N N   . GLU A  1  553 ? 26.633  6.202   69.332  1.00 46.86  ?  553  GLU A N   1 
ATOM   3908  C CA  . GLU A  1  553 ? 27.447  7.048   70.201  1.00 45.65  ?  553  GLU A CA  1 
ATOM   3909  C C   . GLU A  1  553 ? 28.267  8.079   69.445  1.00 44.35  ?  553  GLU A C   1 
ATOM   3910  O O   . GLU A  1  553 ? 28.444  9.197   69.932  1.00 43.64  ?  553  GLU A O   1 
ATOM   3911  C CB  . GLU A  1  553 ? 28.411  6.200   71.038  1.00 45.84  ?  553  GLU A CB  1 
ATOM   3912  C CG  . GLU A  1  553 ? 27.775  5.284   72.059  1.00 47.80  ?  553  GLU A CG  1 
ATOM   3913  C CD  . GLU A  1  553 ? 28.803  4.398   72.737  1.00 48.54  ?  553  GLU A CD  1 
ATOM   3914  O OE1 . GLU A  1  553 ? 29.973  4.823   72.846  1.00 47.37  ?  553  GLU A OE1 1 
ATOM   3915  O OE2 . GLU A  1  553 ? 28.446  3.281   73.162  1.00 49.78  -1 553  GLU A OE2 1 
ATOM   3916  N N   . TYR A  1  554 ? 28.776  7.726   68.267  1.00 41.61  ?  554  TYR A N   1 
ATOM   3917  C CA  . TYR A  1  554 ? 29.773  8.530   67.571  1.00 40.28  ?  554  TYR A CA  1 
ATOM   3918  C C   . TYR A  1  554 ? 29.413  8.557   66.095  1.00 39.78  ?  554  TYR A C   1 
ATOM   3919  O O   . TYR A  1  554 ? 29.414  7.514   65.436  1.00 40.58  ?  554  TYR A O   1 
ATOM   3920  C CB  . TYR A  1  554 ? 31.173  7.940   67.787  1.00 40.71  ?  554  TYR A CB  1 
ATOM   3921  C CG  . TYR A  1  554 ? 32.325  8.695   67.158  1.00 40.87  ?  554  TYR A CG  1 
ATOM   3922  C CD1 . TYR A  1  554 ? 32.632  8.546   65.811  1.00 41.00  ?  554  TYR A CD1 1 
ATOM   3923  C CD2 . TYR A  1  554 ? 33.132  9.526   67.924  1.00 40.64  ?  554  TYR A CD2 1 
ATOM   3924  C CE1 . TYR A  1  554 ? 33.692  9.226   65.240  1.00 40.63  ?  554  TYR A CE1 1 
ATOM   3925  C CE2 . TYR A  1  554 ? 34.194  10.207  67.363  1.00 40.80  ?  554  TYR A CE2 1 
ATOM   3926  C CZ  . TYR A  1  554 ? 34.470  10.054  66.021  1.00 41.03  ?  554  TYR A CZ  1 
ATOM   3927  O OH  . TYR A  1  554 ? 35.527  10.732  65.458  1.00 40.94  ?  554  TYR A OH  1 
ATOM   3928  N N   . LEU A  1  555 ? 29.108  9.746   65.581  1.00 37.27  ?  555  LEU A N   1 
ATOM   3929  C CA  . LEU A  1  555 ? 28.747  9.943   64.183  1.00 35.97  ?  555  LEU A CA  1 
ATOM   3930  C C   . LEU A  1  555 ? 29.777  10.835  63.514  1.00 36.18  ?  555  LEU A C   1 
ATOM   3931  O O   . LEU A  1  555 ? 30.069  11.930  64.005  1.00 37.65  ?  555  LEU A O   1 
ATOM   3932  C CB  . LEU A  1  555 ? 27.357  10.568  64.041  1.00 36.36  ?  555  LEU A CB  1 
ATOM   3933  C CG  . LEU A  1  555 ? 26.208  9.607   63.743  1.00 35.70  ?  555  LEU A CG  1 
ATOM   3934  C CD1 . LEU A  1  555 ? 24.909  10.374  63.554  1.00 36.45  ?  555  LEU A CD1 1 
ATOM   3935  C CD2 . LEU A  1  555 ? 26.512  8.749   62.525  1.00 35.10  ?  555  LEU A CD2 1 
ATOM   3936  N N   . ASP A  1  556 ? 30.321  10.370  62.393  1.00 35.28  ?  556  ASP A N   1 
ATOM   3937  C CA  . ASP A  1  556 ? 31.257  11.165  61.602  1.00 35.52  ?  556  ASP A CA  1 
ATOM   3938  C C   . ASP A  1  556 ? 30.853  11.032  60.138  1.00 34.93  ?  556  ASP A C   1 
ATOM   3939  O O   . ASP A  1  556 ? 31.151  10.022  59.492  1.00 34.53  ?  556  ASP A O   1 
ATOM   3940  C CB  . ASP A  1  556 ? 32.696  10.722  61.832  1.00 36.14  ?  556  ASP A CB  1 
ATOM   3941  C CG  . ASP A  1  556 ? 33.688  11.851  61.638  1.00 37.36  ?  556  ASP A CG  1 
ATOM   3942  O OD1 . ASP A  1  556 ? 33.330  12.850  60.981  1.00 37.95  ?  556  ASP A OD1 1 
ATOM   3943  O OD2 . ASP A  1  556 ? 34.822  11.743  62.149  1.00 38.35  -1 556  ASP A OD2 1 
ATOM   3944  N N   . LEU A  1  557 ? 30.165  12.053  59.625  1.00 34.25  ?  557  LEU A N   1 
ATOM   3945  C CA  . LEU A  1  557 ? 29.753  12.117  58.228  1.00 34.78  ?  557  LEU A CA  1 
ATOM   3946  C C   . LEU A  1  557 ? 30.439  13.263  57.493  1.00 36.32  ?  557  LEU A C   1 
ATOM   3947  O O   . LEU A  1  557 ? 29.988  13.665  56.416  1.00 37.61  ?  557  LEU A O   1 
ATOM   3948  C CB  . LEU A  1  557 ? 28.232  12.252  58.122  1.00 33.87  ?  557  LEU A CB  1 
ATOM   3949  C CG  . LEU A  1  557 ? 27.394  11.170  58.805  1.00 32.74  ?  557  LEU A CG  1 
ATOM   3950  C CD1 . LEU A  1  557 ? 25.917  11.532  58.761  1.00 32.67  ?  557  LEU A CD1 1 
ATOM   3951  C CD2 . LEU A  1  557 ? 27.635  9.813   58.163  1.00 32.87  ?  557  LEU A CD2 1 
ATOM   3952  N N   . SER A  1  558 ? 31.524  13.792  58.053  1.00 39.87  ?  558  SER A N   1 
ATOM   3953  C CA  . SER A  1  558 ? 32.135  15.010  57.551  1.00 41.00  ?  558  SER A CA  1 
ATOM   3954  C C   . SER A  1  558 ? 32.980  14.733  56.308  1.00 41.63  ?  558  SER A C   1 
ATOM   3955  O O   . SER A  1  558 ? 33.205  13.586  55.916  1.00 41.67  ?  558  SER A O   1 
ATOM   3956  C CB  . SER A  1  558 ? 32.991  15.659  58.638  1.00 40.64  ?  558  SER A CB  1 
ATOM   3957  O OG  . SER A  1  558 ? 34.111  14.849  58.954  1.00 40.58  ?  558  SER A OG  1 
ATOM   3958  N N   . SER A  1  559 ? 33.457  15.814  55.691  1.00 41.30  ?  559  SER A N   1 
ATOM   3959  C CA  . SER A  1  559 ? 34.261  15.756  54.470  1.00 42.75  ?  559  SER A CA  1 
ATOM   3960  C C   . SER A  1  559 ? 33.599  14.860  53.421  1.00 43.44  ?  559  SER A C   1 
ATOM   3961  O O   . SER A  1  559 ? 34.144  13.844  52.986  1.00 43.72  ?  559  SER A O   1 
ATOM   3962  C CB  . SER A  1  559 ? 35.686  15.291  54.776  1.00 42.78  ?  559  SER A CB  1 
ATOM   3963  O OG  . SER A  1  559 ? 36.405  16.283  55.488  1.00 43.83  ?  559  SER A OG  1 
ATOM   3964  N N   . ASN A  1  560 ? 32.395  15.260  53.026  1.00 38.97  ?  560  ASN A N   1 
ATOM   3965  C CA  . ASN A  1  560 ? 31.581  14.498  52.091  1.00 39.11  ?  560  ASN A CA  1 
ATOM   3966  C C   . ASN A  1  560 ? 30.851  15.490  51.193  1.00 39.88  ?  560  ASN A C   1 
ATOM   3967  O O   . ASN A  1  560 ? 31.171  16.683  51.165  1.00 40.55  ?  560  ASN A O   1 
ATOM   3968  C CB  . ASN A  1  560 ? 30.627  13.561  52.845  1.00 38.32  ?  560  ASN A CB  1 
ATOM   3969  C CG  . ASN A  1  560 ? 31.232  12.193  53.096  1.00 38.42  ?  560  ASN A CG  1 
ATOM   3970  O OD1 . ASN A  1  560 ? 31.311  11.362  52.194  1.00 39.02  ?  560  ASN A OD1 1 
ATOM   3971  N ND2 . ASN A  1  560 ? 31.666  11.955  54.328  1.00 37.65  ?  560  ASN A ND2 1 
ATOM   3972  N N   . ARG A  1  561 ? 29.869  14.997  50.441  1.00 37.41  ?  561  ARG A N   1 
ATOM   3973  C CA  . ARG A  1  561 ? 29.101  15.828  49.523  1.00 38.46  ?  561  ARG A CA  1 
ATOM   3974  C C   . ARG A  1  561 ? 27.602  15.746  49.800  1.00 37.70  ?  561  ARG A C   1 
ATOM   3975  O O   . ARG A  1  561 ? 26.790  15.858  48.879  1.00 38.92  ?  561  ARG A O   1 
ATOM   3976  C CB  . ARG A  1  561 ? 29.399  15.446  48.072  1.00 39.90  ?  561  ARG A CB  1 
ATOM   3977  C CG  . ARG A  1  561 ? 30.881  15.325  47.746  1.00 40.80  ?  561  ARG A CG  1 
ATOM   3978  C CD  . ARG A  1  561 ? 31.113  15.282  46.243  1.00 43.21  ?  561  ARG A CD  1 
ATOM   3979  N NE  . ARG A  1  561 ? 30.602  14.051  45.653  1.00 42.28  ?  561  ARG A NE  1 
ATOM   3980  C CZ  . ARG A  1  561 ? 31.087  13.487  44.555  1.00 43.77  ?  561  ARG A CZ  1 
ATOM   3981  N NH1 . ARG A  1  561 ? 32.091  14.029  43.885  1.00 46.33  ?  561  ARG A NH1 1 
ATOM   3982  N NH2 . ARG A  1  561 ? 30.552  12.351  44.118  1.00 43.04  ?  561  ARG A NH2 1 
ATOM   3983  N N   . PHE A  1  562 ? 27.220  15.538  51.061  1.00 38.10  ?  562  PHE A N   1 
ATOM   3984  C CA  . PHE A  1  562 ? 25.816  15.659  51.437  1.00 37.93  ?  562  PHE A CA  1 
ATOM   3985  C C   . PHE A  1  562 ? 25.330  17.068  51.118  1.00 40.20  ?  562  PHE A C   1 
ATOM   3986  O O   . PHE A  1  562 ? 26.020  18.053  51.388  1.00 41.40  ?  562  PHE A O   1 
ATOM   3987  C CB  . PHE A  1  562 ? 25.627  15.350  52.923  1.00 36.35  ?  562  PHE A CB  1 
ATOM   3988  C CG  . PHE A  1  562 ? 25.973  13.934  53.301  1.00 34.38  ?  562  PHE A CG  1 
ATOM   3989  C CD1 . PHE A  1  562 ? 25.238  12.869  52.804  1.00 33.76  ?  562  PHE A CD1 1 
ATOM   3990  C CD2 . PHE A  1  562 ? 27.026  13.669  54.164  1.00 34.28  ?  562  PHE A CD2 1 
ATOM   3991  C CE1 . PHE A  1  562 ? 25.552  11.566  53.152  1.00 32.28  ?  562  PHE A CE1 1 
ATOM   3992  C CE2 . PHE A  1  562 ? 27.344  12.368  54.517  1.00 32.89  ?  562  PHE A CE2 1 
ATOM   3993  C CZ  . PHE A  1  562 ? 26.606  11.316  54.010  1.00 31.83  ?  562  PHE A CZ  1 
ATOM   3994  N N   . SER A  1  563 ? 24.127  17.167  50.547  1.00 37.28  ?  563  SER A N   1 
ATOM   3995  C CA  . SER A  1  563 ? 23.751  18.366  49.812  1.00 39.95  ?  563  SER A CA  1 
ATOM   3996  C C   . SER A  1  563 ? 22.469  19.046  50.270  1.00 40.87  ?  563  SER A C   1 
ATOM   3997  O O   . SER A  1  563 ? 22.289  20.230  49.966  1.00 43.20  ?  563  SER A O   1 
ATOM   3998  C CB  . SER A  1  563 ? 23.613  18.043  48.316  1.00 41.38  ?  563  SER A CB  1 
ATOM   3999  O OG  . SER A  1  563 ? 24.884  17.867  47.715  1.00 41.72  ?  563  SER A OG  1 
ATOM   4000  N N   . PHE A  1  564 ? 21.573  18.356  50.960  1.00 38.15  ?  564  PHE A N   1 
ATOM   4001  C CA  . PHE A  1  564 ? 20.308  18.963  51.349  1.00 39.37  ?  564  PHE A CA  1 
ATOM   4002  C C   . PHE A  1  564 ? 20.237  19.112  52.867  1.00 38.39  ?  564  PHE A C   1 
ATOM   4003  O O   . PHE A  1  564 ? 21.184  18.806  53.596  1.00 36.91  ?  564  PHE A O   1 
ATOM   4004  C CB  . PHE A  1  564 ? 19.137  18.159  50.782  1.00 39.60  ?  564  PHE A CB  1 
ATOM   4005  C CG  . PHE A  1  564 ? 18.980  18.304  49.291  1.00 41.57  ?  564  PHE A CG  1 
ATOM   4006  C CD1 . PHE A  1  564 ? 18.274  19.369  48.752  1.00 44.33  ?  564  PHE A CD1 1 
ATOM   4007  C CD2 . PHE A  1  564 ? 19.563  17.390  48.429  1.00 41.00  ?  564  PHE A CD2 1 
ATOM   4008  C CE1 . PHE A  1  564 ? 18.140  19.508  47.380  1.00 46.56  ?  564  PHE A CE1 1 
ATOM   4009  C CE2 . PHE A  1  564 ? 19.432  17.524  47.058  1.00 43.24  ?  564  PHE A CE2 1 
ATOM   4010  C CZ  . PHE A  1  564 ? 18.721  18.584  46.534  1.00 46.05  ?  564  PHE A CZ  1 
ATOM   4011  N N   . GLU A  1  565 ? 19.089  19.597  53.336  1.00 44.15  ?  565  GLU A N   1 
ATOM   4012  C CA  . GLU A  1  565 ? 18.953  20.054  54.712  1.00 44.19  ?  565  GLU A CA  1 
ATOM   4013  C C   . GLU A  1  565 ? 19.074  18.905  55.712  1.00 42.03  ?  565  GLU A C   1 
ATOM   4014  O O   . GLU A  1  565 ? 18.755  17.751  55.415  1.00 40.83  ?  565  GLU A O   1 
ATOM   4015  C CB  . GLU A  1  565 ? 17.615  20.771  54.897  1.00 46.32  ?  565  GLU A CB  1 
ATOM   4016  C CG  . GLU A  1  565 ? 16.428  20.034  54.297  1.00 46.62  ?  565  GLU A CG  1 
ATOM   4017  C CD  . GLU A  1  565 ? 16.083  20.526  52.904  1.00 48.54  ?  565  GLU A CD  1 
ATOM   4018  O OE1 . GLU A  1  565 ? 16.968  21.108  52.241  1.00 49.06  ?  565  GLU A OE1 1 
ATOM   4019  O OE2 . GLU A  1  565 ? 14.930  20.325  52.468  1.00 50.13  -1 565  GLU A OE2 1 
ATOM   4020  N N   . ILE A  1  566 ? 19.554  19.246  56.907  1.00 44.42  ?  566  ILE A N   1 
ATOM   4021  C CA  . ILE A  1  566 ? 19.690  18.279  58.003  1.00 42.91  ?  566  ILE A CA  1 
ATOM   4022  C C   . ILE A  1  566 ? 18.315  17.726  58.354  1.00 43.64  ?  566  ILE A C   1 
ATOM   4023  O O   . ILE A  1  566 ? 17.330  18.493  58.379  1.00 45.99  ?  566  ILE A O   1 
ATOM   4024  C CB  . ILE A  1  566 ? 20.347  18.943  59.229  1.00 43.52  ?  566  ILE A CB  1 
ATOM   4025  C CG1 . ILE A  1  566 ? 21.793  19.336  58.927  1.00 43.27  ?  566  ILE A CG1 1 
ATOM   4026  C CG2 . ILE A  1  566 ? 20.298  18.033  60.448  1.00 42.64  ?  566  ILE A CG2 1 
ATOM   4027  C CD1 . ILE A  1  566 ? 22.543  19.891  60.122  1.00 44.12  ?  566  ILE A CD1 1 
ATOM   4028  N N   . PRO A  1  567 ? 18.174  16.429  58.619  1.00 43.28  ?  567  PRO A N   1 
ATOM   4029  C CA  . PRO A  1  567 ? 16.871  15.888  59.017  1.00 44.38  ?  567  PRO A CA  1 
ATOM   4030  C C   . PRO A  1  567 ? 16.360  16.559  60.278  1.00 45.67  ?  567  PRO A C   1 
ATOM   4031  O O   . PRO A  1  567 ? 17.018  16.513  61.329  1.00 45.33  ?  567  PRO A O   1 
ATOM   4032  C CB  . PRO A  1  567 ? 17.164  14.399  59.261  1.00 43.73  ?  567  PRO A CB  1 
ATOM   4033  C CG  . PRO A  1  567 ? 18.383  14.117  58.454  1.00 42.05  ?  567  PRO A CG  1 
ATOM   4034  C CD  . PRO A  1  567 ? 19.196  15.374  58.492  1.00 41.44  ?  567  PRO A CD  1 
ATOM   4035  N N   . PRO A  1  568 ? 15.184  17.193  60.217  1.00 46.97  ?  568  PRO A N   1 
ATOM   4036  C CA  . PRO A  1  568 ? 14.602  17.778  61.433  1.00 48.93  ?  568  PRO A CA  1 
ATOM   4037  C C   . PRO A  1  568 ? 14.092  16.737  62.411  1.00 49.24  ?  568  PRO A C   1 
ATOM   4038  O O   . PRO A  1  568 ? 13.695  17.100  63.526  1.00 51.20  ?  568  PRO A O   1 
ATOM   4039  C CB  . PRO A  1  568 ? 13.458  18.652  60.897  1.00 51.26  ?  568  PRO A CB  1 
ATOM   4040  C CG  . PRO A  1  568 ? 13.226  18.214  59.468  1.00 50.68  ?  568  PRO A CG  1 
ATOM   4041  C CD  . PRO A  1  568 ? 14.218  17.146  59.108  1.00 47.91  ?  568  PRO A CD  1 
ATOM   4042  N N   . THR A  1  569 ? 14.089  15.465  62.026  1.00 49.95  ?  569  THR A N   1 
ATOM   4043  C CA  . THR A  1  569 ? 13.637  14.372  62.872  1.00 50.78  ?  569  THR A CA  1 
ATOM   4044  C C   . THR A  1  569 ? 14.765  13.746  63.689  1.00 50.26  ?  569  THR A C   1 
ATOM   4045  O O   . THR A  1  569 ? 14.543  12.724  64.346  1.00 51.83  ?  569  THR A O   1 
ATOM   4046  C CB  . THR A  1  569 ? 12.955  13.303  62.014  1.00 52.18  ?  569  THR A CB  1 
ATOM   4047  O OG1 . THR A  1  569 ? 12.758  12.118  62.791  1.00 54.60  ?  569  THR A OG1 1 
ATOM   4048  C CG2 . THR A  1  569 ? 13.809  12.970  60.796  1.00 50.56  ?  569  THR A CG2 1 
ATOM   4049  N N   . LEU A  1  570 ? 15.966  14.330  63.662  1.00 50.68  ?  570  LEU A N   1 
ATOM   4050  C CA  . LEU A  1  570 ? 17.102  13.809  64.426  1.00 49.96  ?  570  LEU A CA  1 
ATOM   4051  C C   . LEU A  1  570 ? 17.059  14.399  65.832  1.00 51.09  ?  570  LEU A C   1 
ATOM   4052  O O   . LEU A  1  570 ? 17.787  15.332  66.179  1.00 51.20  ?  570  LEU A O   1 
ATOM   4053  C CB  . LEU A  1  570 ? 18.417  14.132  63.726  1.00 47.36  ?  570  LEU A CB  1 
ATOM   4054  C CG  . LEU A  1  570 ? 18.922  13.167  62.653  1.00 47.32  ?  570  LEU A CG  1 
ATOM   4055  C CD1 . LEU A  1  570 ? 20.239  13.662  62.075  1.00 44.37  ?  570  LEU A CD1 1 
ATOM   4056  C CD2 . LEU A  1  570 ? 19.079  11.772  63.227  1.00 48.65  ?  570  LEU A CD2 1 
ATOM   4057  N N   . ASN A  1  571 ? 16.183  13.825  66.663  1.00 51.18  ?  571  ASN A N   1 
ATOM   4058  C CA  . ASN A  1  571 ? 16.049  14.283  68.041  1.00 53.21  ?  571  ASN A CA  1 
ATOM   4059  C C   . ASN A  1  571 ? 15.927  13.129  69.035  1.00 54.58  ?  571  ASN A C   1 
ATOM   4060  O O   . ASN A  1  571 ? 15.408  13.331  70.140  1.00 57.08  ?  571  ASN A O   1 
ATOM   4061  C CB  . ASN A  1  571 ? 14.841  15.216  68.178  1.00 55.79  ?  571  ASN A CB  1 
ATOM   4062  C CG  . ASN A  1  571 ? 13.602  14.673  67.493  1.00 56.63  ?  571  ASN A CG  1 
ATOM   4063  O OD1 . ASN A  1  571 ? 13.382  13.462  67.446  1.00 55.88  ?  571  ASN A OD1 1 
ATOM   4064  N ND2 . ASN A  1  571 ? 12.784  15.570  66.957  1.00 58.18  ?  571  ASN A ND2 1 
ATOM   4065  N N   . ASN A  1  572 ? 16.396  11.931  68.685  1.00 54.26  ?  572  ASN A N   1 
ATOM   4066  C CA  . ASN A  1  572 ? 16.198  10.750  69.522  1.00 55.45  ?  572  ASN A CA  1 
ATOM   4067  C C   . ASN A  1  572 ? 17.480  9.930   69.633  1.00 54.65  ?  572  ASN A C   1 
ATOM   4068  O O   . ASN A  1  572 ? 17.463  8.701   69.503  1.00 55.66  ?  572  ASN A O   1 
ATOM   4069  C CB  . ASN A  1  572 ? 15.044  9.892   69.000  1.00 57.56  ?  572  ASN A CB  1 
ATOM   4070  C CG  . ASN A  1  572 ? 14.556  8.888   70.027  1.00 59.12  ?  572  ASN A CG  1 
ATOM   4071  O OD1 . ASN A  1  572 ? 14.114  9.262   71.114  1.00 59.97  ?  572  ASN A OD1 1 
ATOM   4072  N ND2 . ASN A  1  572 ? 14.634  7.604   69.688  1.00 59.36  ?  572  ASN A ND2 1 
ATOM   4073  N N   . LEU A  1  573 ? 18.614  10.593  69.854  1.00 51.15  ?  573  LEU A N   1 
ATOM   4074  C CA  . LEU A  1  573 ? 19.876  9.884   70.039  1.00 50.23  ?  573  LEU A CA  1 
ATOM   4075  C C   . LEU A  1  573 ? 20.361  10.055  71.475  1.00 50.95  ?  573  LEU A C   1 
ATOM   4076  O O   . LEU A  1  573 ? 21.223  10.901  71.745  1.00 51.11  ?  573  LEU A O   1 
ATOM   4077  C CB  . LEU A  1  573 ? 20.934  10.383  69.054  1.00 47.66  ?  573  LEU A CB  1 
ATOM   4078  C CG  . LEU A  1  573 ? 20.589  10.271  67.568  1.00 47.43  ?  573  LEU A CG  1 
ATOM   4079  C CD1 . LEU A  1  573 ? 21.782  10.659  66.709  1.00 45.00  ?  573  LEU A CD1 1 
ATOM   4080  C CD2 . LEU A  1  573 ? 20.119  8.865   67.233  1.00 49.80  ?  573  LEU A CD2 1 
ATOM   4081  N N   . PRO A  1  574 ? 19.839  9.263   72.418  1.00 51.00  ?  574  PRO A N   1 
ATOM   4082  C CA  . PRO A  1  574 ? 20.124  9.515   73.840  1.00 53.68  ?  574  PRO A CA  1 
ATOM   4083  C C   . PRO A  1  574 ? 21.549  9.197   74.266  1.00 53.19  ?  574  PRO A C   1 
ATOM   4084  O O   . PRO A  1  574 ? 21.910  9.510   75.408  1.00 55.76  ?  574  PRO A O   1 
ATOM   4085  C CB  . PRO A  1  574 ? 19.123  8.602   74.556  1.00 56.15  ?  574  PRO A CB  1 
ATOM   4086  C CG  . PRO A  1  574 ? 18.938  7.462   73.609  1.00 53.98  ?  574  PRO A CG  1 
ATOM   4087  C CD  . PRO A  1  574 ? 19.010  8.060   72.224  1.00 52.02  ?  574  PRO A CD  1 
ATOM   4088  N N   . ARG A  1  575 ? 22.367  8.593   73.406  1.00 54.56  ?  575  ARG A N   1 
ATOM   4089  C CA  . ARG A  1  575 ? 23.740  8.259   73.759  1.00 54.40  ?  575  ARG A CA  1 
ATOM   4090  C C   . ARG A  1  575 ? 24.772  8.945   72.877  1.00 52.24  ?  575  ARG A C   1 
ATOM   4091  O O   . ARG A  1  575 ? 25.974  8.746   73.089  1.00 51.61  ?  575  ARG A O   1 
ATOM   4092  C CB  . ARG A  1  575 ? 23.953  6.740   73.709  1.00 53.69  ?  575  ARG A CB  1 
ATOM   4093  C CG  . ARG A  1  575 ? 23.108  5.969   74.708  1.00 56.40  ?  575  ARG A CG  1 
ATOM   4094  C CD  . ARG A  1  575 ? 23.337  4.473   74.589  1.00 56.36  ?  575  ARG A CD  1 
ATOM   4095  N NE  . ARG A  1  575 ? 22.277  3.709   75.235  1.00 59.59  ?  575  ARG A NE  1 
ATOM   4096  C CZ  . ARG A  1  575 ? 21.146  3.348   74.643  1.00 59.49  ?  575  ARG A CZ  1 
ATOM   4097  N NH1 . ARG A  1  575 ? 20.899  3.655   73.380  1.00 57.90  ?  575  ARG A NH1 1 
ATOM   4098  N NH2 . ARG A  1  575 ? 20.242  2.661   75.335  1.00 61.96  ?  575  ARG A NH2 1 
ATOM   4099  N N   . LEU A  1  576 ? 24.345  9.739   71.900  1.00 51.41  ?  576  LEU A N   1 
ATOM   4100  C CA  . LEU A  1  576 ? 25.281  10.413  71.010  1.00 49.42  ?  576  LEU A CA  1 
ATOM   4101  C C   . LEU A  1  576 ? 26.015  11.519  71.758  1.00 51.36  ?  576  LEU A C   1 
ATOM   4102  O O   . LEU A  1  576 ? 25.388  12.437  72.296  1.00 53.06  ?  576  LEU A O   1 
ATOM   4103  C CB  . LEU A  1  576 ? 24.539  10.985  69.806  1.00 47.51  ?  576  LEU A CB  1 
ATOM   4104  C CG  . LEU A  1  576 ? 25.426  11.430  68.643  1.00 45.52  ?  576  LEU A CG  1 
ATOM   4105  C CD1 . LEU A  1  576 ? 25.788  10.242  67.767  1.00 44.96  ?  576  LEU A CD1 1 
ATOM   4106  C CD2 . LEU A  1  576 ? 24.748  12.520  67.830  1.00 45.85  ?  576  LEU A CD2 1 
ATOM   4107  N N   . TYR A  1  577 ? 27.344  11.425  71.802  1.00 49.06  ?  577  TYR A N   1 
ATOM   4108  C CA  . TYR A  1  577 ? 28.176  12.487  72.346  1.00 51.04  ?  577  TYR A CA  1 
ATOM   4109  C C   . TYR A  1  577 ? 29.076  13.126  71.298  1.00 49.65  ?  577  TYR A C   1 
ATOM   4110  O O   . TYR A  1  577 ? 29.818  14.059  71.625  1.00 51.46  ?  577  TYR A O   1 
ATOM   4111  C CB  . TYR A  1  577 ? 29.022  11.963  73.519  1.00 53.14  ?  577  TYR A CB  1 
ATOM   4112  C CG  . TYR A  1  577 ? 30.112  10.974  73.152  1.00 51.62  ?  577  TYR A CG  1 
ATOM   4113  C CD1 . TYR A  1  577 ? 31.367  11.408  72.739  1.00 51.44  ?  577  TYR A CD1 1 
ATOM   4114  C CD2 . TYR A  1  577 ? 29.891  9.605   73.237  1.00 50.75  ?  577  TYR A CD2 1 
ATOM   4115  C CE1 . TYR A  1  577 ? 32.365  10.508  72.410  1.00 50.34  ?  577  TYR A CE1 1 
ATOM   4116  C CE2 . TYR A  1  577 ? 30.883  8.698   72.911  1.00 49.62  ?  577  TYR A CE2 1 
ATOM   4117  C CZ  . TYR A  1  577 ? 32.117  9.155   72.499  1.00 49.38  ?  577  TYR A CZ  1 
ATOM   4118  O OH  . TYR A  1  577 ? 33.106  8.256   72.174  1.00 48.51  ?  577  TYR A OH  1 
ATOM   4119  N N   . TYR A  1  578 ? 29.029  12.656  70.053  1.00 46.75  ?  578  TYR A N   1 
ATOM   4120  C CA  . TYR A  1  578 ? 29.850  13.182  68.974  1.00 45.65  ?  578  TYR A CA  1 
ATOM   4121  C C   . TYR A  1  578 ? 29.027  13.225  67.697  1.00 43.71  ?  578  TYR A C   1 
ATOM   4122  O O   . TYR A  1  578 ? 28.304  12.275  67.384  1.00 42.32  ?  578  TYR A O   1 
ATOM   4123  C CB  . TYR A  1  578 ? 31.104  12.319  68.764  1.00 44.78  ?  578  TYR A CB  1 
ATOM   4124  C CG  . TYR A  1  578 ? 32.104  12.876  67.772  1.00 44.33  ?  578  TYR A CG  1 
ATOM   4125  C CD1 . TYR A  1  578 ? 31.979  12.620  66.412  1.00 42.21  ?  578  TYR A CD1 1 
ATOM   4126  C CD2 . TYR A  1  578 ? 33.188  13.633  68.198  1.00 46.46  ?  578  TYR A CD2 1 
ATOM   4127  C CE1 . TYR A  1  578 ? 32.893  13.118  65.503  1.00 42.22  ?  578  TYR A CE1 1 
ATOM   4128  C CE2 . TYR A  1  578 ? 34.109  14.134  67.295  1.00 46.50  ?  578  TYR A CE2 1 
ATOM   4129  C CZ  . TYR A  1  578 ? 33.956  13.872  65.949  1.00 44.37  ?  578  TYR A CZ  1 
ATOM   4130  O OH  . TYR A  1  578 ? 34.869  14.367  65.045  1.00 44.81  ?  578  TYR A OH  1 
ATOM   4131  N N   . MET A  1  579 ? 29.147  14.325  66.957  1.00 44.98  ?  579  MET A N   1 
ATOM   4132  C CA  . MET A  1  579 ? 28.480  14.454  65.663  1.00 43.47  ?  579  MET A CA  1 
ATOM   4133  C C   . MET A  1  579 ? 29.264  15.457  64.831  1.00 44.27  ?  579  MET A C   1 
ATOM   4134  O O   . MET A  1  579 ? 29.278  16.651  65.148  1.00 46.90  ?  579  MET A O   1 
ATOM   4135  C CB  . MET A  1  579 ? 27.025  14.891  65.825  1.00 44.31  ?  579  MET A CB  1 
ATOM   4136  C CG  . MET A  1  579 ? 26.334  15.217  64.509  1.00 43.16  ?  579  MET A CG  1 
ATOM   4137  S SD  . MET A  1  579 ? 24.637  15.791  64.711  1.00 44.46  ?  579  MET A SD  1 
ATOM   4138  C CE  . MET A  1  579 ? 23.752  14.236  64.782  1.00 43.20  ?  579  MET A CE  1 
ATOM   4139  N N   . ASN A  1  580 ? 29.923  14.971  63.782  1.00 44.10  ?  580  ASN A N   1 
ATOM   4140  C CA  . ASN A  1  580 ? 30.686  15.808  62.866  1.00 44.82  ?  580  ASN A CA  1 
ATOM   4141  C C   . ASN A  1  580 ? 30.040  15.744  61.489  1.00 43.99  ?  580  ASN A C   1 
ATOM   4142  O O   . ASN A  1  580 ? 30.018  14.681  60.858  1.00 42.73  ?  580  ASN A O   1 
ATOM   4143  C CB  . ASN A  1  580 ? 32.149  15.360  62.812  1.00 44.91  ?  580  ASN A CB  1 
ATOM   4144  C CG  . ASN A  1  580 ? 33.057  16.408  62.212  1.00 46.95  ?  580  ASN A CG  1 
ATOM   4145  O OD1 . ASN A  1  580 ? 32.595  17.372  61.603  1.00 48.54  ?  580  ASN A OD1 1 
ATOM   4146  N ND2 . ASN A  1  580 ? 34.361  16.230  62.387  1.00 47.58  ?  580  ASN A ND2 1 
ATOM   4147  N N   . LEU A  1  581 ? 29.513  16.880  61.027  1.00 41.94  ?  581  LEU A N   1 
ATOM   4148  C CA  . LEU A  1  581 ? 28.872  16.992  59.721  1.00 41.46  ?  581  LEU A CA  1 
ATOM   4149  C C   . LEU A  1  581 ? 29.562  18.039  58.851  1.00 43.19  ?  581  LEU A C   1 
ATOM   4150  O O   . LEU A  1  581 ? 28.949  18.608  57.946  1.00 43.86  ?  581  LEU A O   1 
ATOM   4151  C CB  . LEU A  1  581 ? 27.388  17.327  59.870  1.00 41.70  ?  581  LEU A CB  1 
ATOM   4152  C CG  . LEU A  1  581 ? 26.550  16.537  60.876  1.00 40.87  ?  581  LEU A CG  1 
ATOM   4153  C CD1 . LEU A  1  581 ? 25.092  16.963  60.789  1.00 41.54  ?  581  LEU A CD1 1 
ATOM   4154  C CD2 . LEU A  1  581 ? 26.686  15.044  60.642  1.00 38.83  ?  581  LEU A CD2 1 
ATOM   4155  N N   . SER A  1  582 ? 30.839  18.297  59.113  1.00 46.48  ?  582  SER A N   1 
ATOM   4156  C CA  . SER A  1  582 ? 31.548  19.409  58.500  1.00 48.86  ?  582  SER A CA  1 
ATOM   4157  C C   . SER A  1  582 ? 31.926  19.099  57.053  1.00 48.61  ?  582  SER A C   1 
ATOM   4158  O O   . SER A  1  582 ? 31.948  17.945  56.619  1.00 46.62  ?  582  SER A O   1 
ATOM   4159  C CB  . SER A  1  582 ? 32.799  19.751  59.310  1.00 50.55  ?  582  SER A CB  1 
ATOM   4160  O OG  . SER A  1  582 ? 33.839  20.225  58.475  1.00 52.43  ?  582  SER A OG  1 
ATOM   4161  N N   . ARG A  1  583 ? 32.225  20.163  56.303  1.00 50.66  ?  583  ARG A N   1 
ATOM   4162  C CA  . ARG A  1  583 ? 32.692  20.066  54.919  1.00 51.33  ?  583  ARG A CA  1 
ATOM   4163  C C   . ARG A  1  583 ? 31.683  19.325  54.036  1.00 49.15  ?  583  ARG A C   1 
ATOM   4164  O O   . ARG A  1  583 ? 31.958  18.262  53.473  1.00 47.70  ?  583  ARG A O   1 
ATOM   4165  C CB  . ARG A  1  583 ? 34.079  19.415  54.866  1.00 51.10  ?  583  ARG A CB  1 
ATOM   4166  C CG  . ARG A  1  583 ? 35.150  20.255  55.543  1.00 53.44  ?  583  ARG A CG  1 
ATOM   4167  C CD  . ARG A  1  583 ? 36.405  19.452  55.849  1.00 53.05  ?  583  ARG A CD  1 
ATOM   4168  N NE  . ARG A  1  583 ? 37.467  20.274  56.421  1.00 56.63  ?  583  ARG A NE  1 
ATOM   4169  C CZ  . ARG A  1  583 ? 37.403  20.892  57.595  1.00 57.09  ?  583  ARG A CZ  1 
ATOM   4170  N NH1 . ARG A  1  583 ? 36.351  20.771  58.388  1.00 55.39  ?  583  ARG A NH1 1 
ATOM   4171  N NH2 . ARG A  1  583 ? 38.428  21.644  57.987  1.00 60.30  ?  583  ARG A NH2 1 
ATOM   4172  N N   . ASN A  1  584 ? 30.498  19.918  53.929  1.00 47.32  ?  584  ASN A N   1 
ATOM   4173  C CA  . ASN A  1  584 ? 29.396  19.363  53.155  1.00 46.25  ?  584  ASN A CA  1 
ATOM   4174  C C   . ASN A  1  584 ? 28.609  20.524  52.551  1.00 48.83  ?  584  ASN A C   1 
ATOM   4175  O O   . ASN A  1  584 ? 29.059  21.674  52.571  1.00 51.81  ?  584  ASN A O   1 
ATOM   4176  C CB  . ASN A  1  584 ? 28.524  18.460  54.034  1.00 44.78  ?  584  ASN A CB  1 
ATOM   4177  C CG  . ASN A  1  584 ? 29.114  17.078  54.219  1.00 43.94  ?  584  ASN A CG  1 
ATOM   4178  O OD1 . ASN A  1  584 ? 28.905  16.188  53.396  1.00 44.27  ?  584  ASN A OD1 1 
ATOM   4179  N ND2 . ASN A  1  584 ? 29.855  16.891  55.304  1.00 43.06  ?  584  ASN A ND2 1 
ATOM   4180  N N   . ASP A  1  585 ? 27.427  20.225  52.007  1.00 49.17  ?  585  ASP A N   1 
ATOM   4181  C CA  . ASP A  1  585 ? 26.631  21.211  51.283  1.00 51.64  ?  585  ASP A CA  1 
ATOM   4182  C C   . ASP A  1  585 ? 25.222  21.349  51.851  1.00 51.43  ?  585  ASP A C   1 
ATOM   4183  O O   . ASP A  1  585 ? 24.285  21.660  51.113  1.00 53.31  ?  585  ASP A O   1 
ATOM   4184  C CB  . ASP A  1  585 ? 26.558  20.864  49.796  1.00 52.51  ?  585  ASP A CB  1 
ATOM   4185  C CG  . ASP A  1  585 ? 27.693  21.470  48.993  1.00 55.76  ?  585  ASP A CG  1 
ATOM   4186  O OD1 . ASP A  1  585 ? 28.760  21.750  49.578  1.00 56.34  ?  585  ASP A OD1 1 
ATOM   4187  O OD2 . ASP A  1  585 ? 27.516  21.667  47.771  1.00 58.58  -1 585  ASP A OD2 1 
ATOM   4188  N N   . LEU A  1  586 ? 25.050  21.141  53.156  1.00 49.67  ?  586  LEU A N   1 
ATOM   4189  C CA  . LEU A  1  586 ? 23.722  21.265  53.747  1.00 49.63  ?  586  LEU A CA  1 
ATOM   4190  C C   . LEU A  1  586 ? 23.285  22.726  53.720  1.00 52.51  ?  586  LEU A C   1 
ATOM   4191  O O   . LEU A  1  586 ? 24.060  23.625  54.060  1.00 54.08  ?  586  LEU A O   1 
ATOM   4192  C CB  . LEU A  1  586 ? 23.710  20.705  55.168  1.00 47.90  ?  586  LEU A CB  1 
ATOM   4193  C CG  . LEU A  1  586 ? 24.346  19.313  55.278  1.00 46.07  ?  586  LEU A CG  1 
ATOM   4194  C CD1 . LEU A  1  586 ? 25.754  19.391  55.832  1.00 45.48  ?  586  LEU A CD1 1 
ATOM   4195  C CD2 . LEU A  1  586 ? 23.500  18.349  56.083  1.00 44.43  ?  586  LEU A CD2 1 
ATOM   4196  N N   . ASP A  1  587 ? 22.031  22.959  53.317  1.00 54.09  ?  587  ASP A N   1 
ATOM   4197  C CA  . ASP A  1  587 ? 21.649  24.215  52.681  1.00 57.22  ?  587  ASP A CA  1 
ATOM   4198  C C   . ASP A  1  587 ? 20.483  24.935  53.355  1.00 58.68  ?  587  ASP A C   1 
ATOM   4199  O O   . ASP A  1  587 ? 19.802  25.728  52.698  1.00 62.18  ?  587  ASP A O   1 
ATOM   4200  C CB  . ASP A  1  587 ? 21.314  23.963  51.209  1.00 58.47  ?  587  ASP A CB  1 
ATOM   4201  C CG  . ASP A  1  587 ? 20.230  22.913  51.033  1.00 56.92  ?  587  ASP A CG  1 
ATOM   4202  O OD1 . ASP A  1  587 ? 19.910  22.218  52.020  1.00 54.56  ?  587  ASP A OD1 1 
ATOM   4203  O OD2 . ASP A  1  587 ? 19.703  22.780  49.909  1.00 58.40  -1 587  ASP A OD2 1 
ATOM   4204  N N   . GLN A  1  588 ? 20.224  24.694  54.636  1.00 57.66  ?  588  GLN A N   1 
ATOM   4205  C CA  . GLN A  1  588 ? 19.105  25.371  55.285  1.00 59.44  ?  588  GLN A CA  1 
ATOM   4206  C C   . GLN A  1  588 ? 19.435  25.587  56.758  1.00 59.82  ?  588  GLN A C   1 
ATOM   4207  O O   . GLN A  1  588 ? 20.585  25.448  57.184  1.00 58.94  ?  588  GLN A O   1 
ATOM   4208  C CB  . GLN A  1  588 ? 17.804  24.584  55.080  1.00 58.75  ?  588  GLN A CB  1 
ATOM   4209  C CG  . GLN A  1  588 ? 16.843  25.254  54.107  1.00 61.33  ?  588  GLN A CG  1 
ATOM   4210  C CD  . GLN A  1  588 ? 15.698  24.353  53.688  1.00 61.01  ?  588  GLN A CD  1 
ATOM   4211  O OE1 . GLN A  1  588 ? 15.756  23.701  52.645  1.00 60.34  ?  588  GLN A OE1 1 
ATOM   4212  N NE2 . GLN A  1  588 ? 14.644  24.322  54.495  1.00 61.55  ?  588  GLN A NE2 1 
ATOM   4213  N N   . THR A  1  589 ? 18.417  25.946  57.535  1.00 57.50  ?  589  THR A N   1 
ATOM   4214  C CA  . THR A  1  589 ? 18.608  26.297  58.933  1.00 58.19  ?  589  THR A CA  1 
ATOM   4215  C C   . THR A  1  589 ? 18.808  25.050  59.785  1.00 55.57  ?  589  THR A C   1 
ATOM   4216  O O   . THR A  1  589 ? 18.259  23.981  59.502  1.00 53.72  ?  589  THR A O   1 
ATOM   4217  C CB  . THR A  1  589 ? 17.411  27.090  59.459  1.00 60.82  ?  589  THR A CB  1 
ATOM   4218  O OG1 . THR A  1  589 ? 16.297  26.209  59.647  1.00 59.81  ?  589  THR A OG1 1 
ATOM   4219  C CG2 . THR A  1  589 ? 17.024  28.183  58.475  1.00 63.49  ?  589  THR A CG2 1 
ATOM   4220  N N   . ILE A  1  590 ? 19.615  25.198  60.832  1.00 55.49  ?  590  ILE A N   1 
ATOM   4221  C CA  . ILE A  1  590 ? 19.856  24.121  61.788  1.00 53.60  ?  590  ILE A CA  1 
ATOM   4222  C C   . ILE A  1  590 ? 18.531  23.748  62.442  1.00 54.07  ?  590  ILE A C   1 
ATOM   4223  O O   . ILE A  1  590 ? 17.850  24.619  63.001  1.00 56.63  ?  590  ILE A O   1 
ATOM   4224  C CB  . ILE A  1  590 ? 20.901  24.530  62.838  1.00 54.60  ?  590  ILE A CB  1 
ATOM   4225  C CG1 . ILE A  1  590 ? 22.157  25.078  62.156  1.00 54.93  ?  590  ILE A CG1 1 
ATOM   4226  C CG2 . ILE A  1  590 ? 21.245  23.353  63.739  1.00 52.77  ?  590  ILE A CG2 1 
ATOM   4227  C CD1 . ILE A  1  590 ? 23.123  25.756  63.104  1.00 56.90  ?  590  ILE A CD1 1 
ATOM   4228  N N   . PRO A  1  591 ? 18.127  22.481  62.396  1.00 55.96  ?  591  PRO A N   1 
ATOM   4229  C CA  . PRO A  1  591 ? 16.832  22.101  62.969  1.00 56.82  ?  591  PRO A CA  1 
ATOM   4230  C C   . PRO A  1  591 ? 16.844  22.166  64.487  1.00 58.19  ?  591  PRO A C   1 
ATOM   4231  O O   . PRO A  1  591 ? 17.859  21.909  65.139  1.00 57.50  ?  591  PRO A O   1 
ATOM   4232  C CB  . PRO A  1  591 ? 16.635  20.664  62.477  1.00 54.41  ?  591  PRO A CB  1 
ATOM   4233  C CG  . PRO A  1  591 ? 18.018  20.154  62.266  1.00 52.19  ?  591  PRO A CG  1 
ATOM   4234  C CD  . PRO A  1  591 ? 18.835  21.331  61.808  1.00 53.11  ?  591  PRO A CD  1 
ATOM   4235  N N   . GLU A  1  592 ? 15.684  22.514  65.049  1.00 66.62  ?  592  GLU A N   1 
ATOM   4236  C CA  . GLU A  1  592 ? 15.552  22.603  66.498  1.00 68.13  ?  592  GLU A CA  1 
ATOM   4237  C C   . GLU A  1  592 ? 15.676  21.243  67.173  1.00 66.74  ?  592  GLU A C   1 
ATOM   4238  O O   . GLU A  1  592 ? 15.978  21.184  68.370  1.00 67.82  ?  592  GLU A O   1 
ATOM   4239  C CB  . GLU A  1  592 ? 14.214  23.252  66.863  1.00 69.88  ?  592  GLU A CB  1 
ATOM   4240  C CG  . GLU A  1  592 ? 14.120  23.732  68.305  1.00 72.12  ?  592  GLU A CG  1 
ATOM   4241  C CD  . GLU A  1  592 ? 12.749  23.506  68.912  1.00 72.94  ?  592  GLU A CD  1 
ATOM   4242  O OE1 . GLU A  1  592 ? 11.927  22.805  68.285  1.00 71.55  ?  592  GLU A OE1 1 
ATOM   4243  O OE2 . GLU A  1  592 ? 12.494  24.030  70.017  1.00 75.08  -1 592  GLU A OE2 1 
ATOM   4244  N N   . GLY A  1  593 ? 15.455  20.152  66.435  1.00 60.76  ?  593  GLY A N   1 
ATOM   4245  C CA  . GLY A  1  593 ? 15.552  18.824  67.015  1.00 59.47  ?  593  GLY A CA  1 
ATOM   4246  C C   . GLY A  1  593 ? 16.952  18.424  67.430  1.00 59.01  ?  593  GLY A C   1 
ATOM   4247  O O   . GLY A  1  593 ? 17.108  17.479  68.210  1.00 58.56  ?  593  GLY A O   1 
ATOM   4248  N N   . LEU A  1  594 ? 17.976  19.119  66.928  1.00 58.35  ?  594  LEU A N   1 
ATOM   4249  C CA  . LEU A  1  594 ? 19.343  18.817  67.343  1.00 58.15  ?  594  LEU A CA  1 
ATOM   4250  C C   . LEU A  1  594 ? 19.563  19.163  68.810  1.00 60.12  ?  594  LEU A C   1 
ATOM   4251  O O   . LEU A  1  594 ? 20.285  18.452  69.519  1.00 59.87  ?  594  LEU A O   1 
ATOM   4252  C CB  . LEU A  1  594 ? 20.344  19.560  66.461  1.00 58.21  ?  594  LEU A CB  1 
ATOM   4253  C CG  . LEU A  1  594 ? 21.040  18.720  65.387  1.00 56.01  ?  594  LEU A CG  1 
ATOM   4254  C CD1 . LEU A  1  594 ? 20.029  17.951  64.547  1.00 54.26  ?  594  LEU A CD1 1 
ATOM   4255  C CD2 . LEU A  1  594 ? 21.929  19.588  64.507  1.00 56.44  ?  594  LEU A CD2 1 
ATOM   4256  N N   . THR A  1  595 ? 18.952  20.250  69.282  1.00 63.44  ?  595  THR A N   1 
ATOM   4257  C CA  . THR A  1  595 ? 19.092  20.653  70.676  1.00 65.53  ?  595  THR A CA  1 
ATOM   4258  C C   . THR A  1  595 ? 18.445  19.671  71.645  1.00 65.45  ?  595  THR A C   1 
ATOM   4259  O O   . THR A  1  595 ? 18.694  19.767  72.852  1.00 67.02  ?  595  THR A O   1 
ATOM   4260  C CB  . THR A  1  595 ? 18.498  22.047  70.886  1.00 67.84  ?  595  THR A CB  1 
ATOM   4261  O OG1 . THR A  1  595 ? 17.068  21.963  70.916  1.00 68.08  ?  595  THR A OG1 1 
ATOM   4262  C CG2 . THR A  1  595 ? 18.920  22.978  69.761  1.00 67.88  ?  595  THR A CG2 1 
ATOM   4263  N N   . LYS A  1  596 ? 17.627  18.737  71.156  1.00 63.61  ?  596  LYS A N   1 
ATOM   4264  C CA  . LYS A  1  596 ? 16.989  17.764  72.033  1.00 63.60  ?  596  LYS A CA  1 
ATOM   4265  C C   . LYS A  1  596 ? 17.872  16.558  72.326  1.00 62.27  ?  596  LYS A C   1 
ATOM   4266  O O   . LYS A  1  596 ? 17.500  15.732  73.167  1.00 62.48  ?  596  LYS A O   1 
ATOM   4267  C CB  . LYS A  1  596 ? 15.668  17.287  71.423  1.00 62.61  ?  596  LYS A CB  1 
ATOM   4268  C CG  . LYS A  1  596 ? 14.738  18.402  70.975  1.00 63.78  ?  596  LYS A CG  1 
ATOM   4269  C CD  . LYS A  1  596 ? 13.454  17.834  70.386  1.00 62.80  ?  596  LYS A CD  1 
ATOM   4270  C CE  . LYS A  1  596 ? 12.720  18.865  69.544  1.00 63.44  ?  596  LYS A CE  1 
ATOM   4271  N NZ  . LYS A  1  596 ? 11.535  18.276  68.860  1.00 62.37  ?  596  LYS A NZ  1 
ATOM   4272  N N   . LEU A  1  597 ? 19.020  16.434  71.664  1.00 60.77  ?  597  LEU A N   1 
ATOM   4273  C CA  . LEU A  1  597 ? 20.006  15.410  72.007  1.00 59.83  ?  597  LEU A CA  1 
ATOM   4274  C C   . LEU A  1  597 ? 20.843  15.944  73.162  1.00 61.83  ?  597  LEU A C   1 
ATOM   4275  O O   . LEU A  1  597 ? 21.797  16.695  72.959  1.00 62.37  ?  597  LEU A O   1 
ATOM   4276  C CB  . LEU A  1  597 ? 20.877  15.065  70.805  1.00 57.85  ?  597  LEU A CB  1 
ATOM   4277  C CG  . LEU A  1  597 ? 20.275  14.890  69.414  1.00 56.06  ?  597  LEU A CG  1 
ATOM   4278  C CD1 . LEU A  1  597 ? 21.364  14.535  68.418  1.00 54.45  ?  597  LEU A CD1 1 
ATOM   4279  C CD2 . LEU A  1  597 ? 19.240  13.798  69.452  1.00 54.97  ?  597  LEU A CD2 1 
ATOM   4280  N N   . SER A  1  598 ? 20.487  15.558  74.386  1.00 62.73  ?  598  SER A N   1 
ATOM   4281  C CA  . SER A  1  598 ? 21.079  16.175  75.568  1.00 65.00  ?  598  SER A CA  1 
ATOM   4282  C C   . SER A  1  598 ? 22.565  15.860  75.738  1.00 64.73  ?  598  SER A C   1 
ATOM   4283  O O   . SER A  1  598 ? 23.277  16.635  76.384  1.00 66.49  ?  598  SER A O   1 
ATOM   4284  C CB  . SER A  1  598 ? 20.308  15.741  76.817  1.00 66.42  ?  598  SER A CB  1 
ATOM   4285  O OG  . SER A  1  598 ? 20.229  14.329  76.899  1.00 65.01  ?  598  SER A OG  1 
ATOM   4286  N N   . GLN A  1  599 ? 23.051  14.749  75.185  1.00 63.84  ?  599  GLN A N   1 
ATOM   4287  C CA  . GLN A  1  599 ? 24.348  14.203  75.569  1.00 63.77  ?  599  GLN A CA  1 
ATOM   4288  C C   . GLN A  1  599 ? 25.503  14.578  74.641  1.00 62.95  ?  599  GLN A C   1 
ATOM   4289  O O   . GLN A  1  599 ? 26.594  14.018  74.794  1.00 62.64  ?  599  GLN A O   1 
ATOM   4290  C CB  . GLN A  1  599 ? 24.266  12.680  75.685  1.00 62.35  ?  599  GLN A CB  1 
ATOM   4291  C CG  . GLN A  1  599 ? 23.982  12.177  77.091  1.00 63.90  ?  599  GLN A CG  1 
ATOM   4292  C CD  . GLN A  1  599 ? 22.618  12.588  77.602  1.00 65.14  ?  599  GLN A CD  1 
ATOM   4293  O OE1 . GLN A  1  599 ? 21.591  12.240  77.019  1.00 64.01  ?  599  GLN A OE1 1 
ATOM   4294  N NE2 . GLN A  1  599 ? 22.599  13.330  78.704  1.00 67.59  ?  599  GLN A NE2 1 
ATOM   4295  N N   . LEU A  1  600 ? 25.315  15.491  73.686  1.00 61.32  ?  600  LEU A N   1 
ATOM   4296  C CA  . LEU A  1  600 ? 26.448  15.871  72.846  1.00 60.81  ?  600  LEU A CA  1 
ATOM   4297  C C   . LEU A  1  600 ? 27.549  16.526  73.669  1.00 62.75  ?  600  LEU A C   1 
ATOM   4298  O O   . LEU A  1  600 ? 27.289  17.328  74.570  1.00 64.81  ?  600  LEU A O   1 
ATOM   4299  C CB  . LEU A  1  600 ? 26.052  16.826  71.717  1.00 60.54  ?  600  LEU A CB  1 
ATOM   4300  C CG  . LEU A  1  600 ? 25.251  16.366  70.502  1.00 58.50  ?  600  LEU A CG  1 
ATOM   4301  C CD1 . LEU A  1  600 ? 23.804  16.680  70.684  1.00 59.00  ?  600  LEU A CD1 1 
ATOM   4302  C CD2 . LEU A  1  600 ? 25.778  17.004  69.228  1.00 57.96  ?  600  LEU A CD2 1 
ATOM   4303  N N   . GLN A  1  601 ? 28.788  16.172  73.344  1.00 61.16  ?  601  GLN A N   1 
ATOM   4304  C CA  . GLN A  1  601 ? 29.975  16.875  73.808  1.00 62.83  ?  601  GLN A CA  1 
ATOM   4305  C C   . GLN A  1  601 ? 30.629  17.698  72.712  1.00 62.70  ?  601  GLN A C   1 
ATOM   4306  O O   . GLN A  1  601 ? 31.109  18.804  72.974  1.00 64.53  ?  601  GLN A O   1 
ATOM   4307  C CB  . GLN A  1  601 ? 30.996  15.878  74.373  1.00 62.65  ?  601  GLN A CB  1 
ATOM   4308  C CG  . GLN A  1  601 ? 32.446  16.313  74.223  1.00 63.43  ?  601  GLN A CG  1 
ATOM   4309  C CD  . GLN A  1  601 ? 33.389  15.541  75.120  1.00 64.02  ?  601  GLN A CD  1 
ATOM   4310  O OE1 . GLN A  1  601 ? 32.997  14.566  75.758  1.00 63.63  ?  601  GLN A OE1 1 
ATOM   4311  N NE2 . GLN A  1  601 ? 34.644  15.972  75.170  1.00 65.08  ?  601  GLN A NE2 1 
ATOM   4312  N N   . MET A  1  602 ? 30.632  17.192  71.481  1.00 62.53  ?  602  MET A N   1 
ATOM   4313  C CA  . MET A  1  602 ? 31.218  17.878  70.341  1.00 62.35  ?  602  MET A CA  1 
ATOM   4314  C C   . MET A  1  602 ? 30.220  17.880  69.193  1.00 60.85  ?  602  MET A C   1 
ATOM   4315  O O   . MET A  1  602 ? 29.571  16.866  68.920  1.00 59.10  ?  602  MET A O   1 
ATOM   4316  C CB  . MET A  1  602 ? 32.527  17.204  69.912  1.00 61.54  ?  602  MET A CB  1 
ATOM   4317  C CG  . MET A  1  602 ? 33.661  17.392  70.909  1.00 63.28  ?  602  MET A CG  1 
ATOM   4318  S SD  . MET A  1  602 ? 34.906  16.091  70.829  1.00 62.18  ?  602  MET A SD  1 
ATOM   4319  C CE  . MET A  1  602 ? 35.962  16.707  69.519  1.00 62.14  ?  602  MET A CE  1 
ATOM   4320  N N   . LEU A  1  603 ? 30.100  19.026  68.526  1.00 57.16  ?  603  LEU A N   1 
ATOM   4321  C CA  . LEU A  1  603 ? 29.137  19.191  67.439  1.00 56.08  ?  603  LEU A CA  1 
ATOM   4322  C C   . LEU A  1  603 ? 29.739  20.144  66.418  1.00 56.67  ?  603  LEU A C   1 
ATOM   4323  O O   . LEU A  1  603 ? 29.805  21.353  66.661  1.00 58.63  ?  603  LEU A O   1 
ATOM   4324  C CB  . LEU A  1  603 ? 27.801  19.713  67.960  1.00 56.95  ?  603  LEU A CB  1 
ATOM   4325  C CG  . LEU A  1  603 ? 26.773  20.142  66.911  1.00 56.36  ?  603  LEU A CG  1 
ATOM   4326  C CD1 . LEU A  1  603 ? 26.213  18.938  66.172  1.00 53.93  ?  603  LEU A CD1 1 
ATOM   4327  C CD2 . LEU A  1  603 ? 25.652  20.942  67.560  1.00 57.91  ?  603  LEU A CD2 1 
ATOM   4328  N N   . ASP A  1  604 ? 30.187  19.601  65.292  1.00 54.68  ?  604  ASP A N   1 
ATOM   4329  C CA  . ASP A  1  604 ? 30.832  20.375  64.239  1.00 55.20  ?  604  ASP A CA  1 
ATOM   4330  C C   . ASP A  1  604 ? 29.895  20.457  63.039  1.00 54.12  ?  604  ASP A C   1 
ATOM   4331  O O   . ASP A  1  604 ? 29.587  19.434  62.419  1.00 52.10  ?  604  ASP A O   1 
ATOM   4332  C CB  . ASP A  1  604 ? 32.167  19.739  63.847  1.00 54.55  ?  604  ASP A CB  1 
ATOM   4333  C CG  . ASP A  1  604 ? 33.022  20.650  62.989  1.00 55.67  ?  604  ASP A CG  1 
ATOM   4334  O OD1 . ASP A  1  604 ? 32.525  21.708  62.553  1.00 56.73  ?  604  ASP A OD1 1 
ATOM   4335  O OD2 . ASP A  1  604 ? 34.199  20.304  62.752  1.00 55.60  -1 604  ASP A OD2 1 
ATOM   4336  N N   . LEU A  1  605 ? 29.440  21.672  62.723  1.00 55.55  ?  605  LEU A N   1 
ATOM   4337  C CA  . LEU A  1  605 ? 28.619  21.923  61.543  1.00 54.91  ?  605  LEU A CA  1 
ATOM   4338  C C   . LEU A  1  605 ? 29.308  22.867  60.562  1.00 56.04  ?  605  LEU A C   1 
ATOM   4339  O O   . LEU A  1  605 ? 28.635  23.526  59.763  1.00 56.44  ?  605  LEU A O   1 
ATOM   4340  C CB  . LEU A  1  605 ? 27.257  22.492  61.949  1.00 55.66  ?  605  LEU A CB  1 
ATOM   4341  C CG  . LEU A  1  605 ? 26.421  21.684  62.941  1.00 54.90  ?  605  LEU A CG  1 
ATOM   4342  C CD1 . LEU A  1  605 ? 25.091  22.375  63.203  1.00 55.90  ?  605  LEU A CD1 1 
ATOM   4343  C CD2 . LEU A  1  605 ? 26.201  20.271  62.428  1.00 52.38  ?  605  LEU A CD2 1 
ATOM   4344  N N   . SER A  1  606 ? 30.636  22.934  60.598  1.00 57.41  ?  606  SER A N   1 
ATOM   4345  C CA  . SER A  1  606 ? 31.379  23.941  59.857  1.00 58.96  ?  606  SER A CA  1 
ATOM   4346  C C   . SER A  1  606 ? 31.428  23.615  58.365  1.00 57.77  ?  606  SER A C   1 
ATOM   4347  O O   . SER A  1  606 ? 31.099  22.510  57.925  1.00 55.64  ?  606  SER A O   1 
ATOM   4348  C CB  . SER A  1  606 ? 32.797  24.070  60.411  1.00 60.11  ?  606  SER A CB  1 
ATOM   4349  O OG  . SER A  1  606 ? 33.505  22.848  60.286  1.00 58.44  ?  606  SER A OG  1 
ATOM   4350  N N   . TYR A  1  607 ? 31.846  24.615  57.584  1.00 63.71  ?  607  TYR A N   1 
ATOM   4351  C CA  . TYR A  1  607 ? 32.139  24.465  56.157  1.00 63.12  ?  607  TYR A CA  1 
ATOM   4352  C C   . TYR A  1  607 ? 30.924  23.928  55.397  1.00 61.39  ?  607  TYR A C   1 
ATOM   4353  O O   . TYR A  1  607 ? 30.950  22.850  54.800  1.00 59.43  ?  607  TYR A O   1 
ATOM   4354  C CB  . TYR A  1  607 ? 33.372  23.580  55.946  1.00 62.22  ?  607  TYR A CB  1 
ATOM   4355  C CG  . TYR A  1  607 ? 34.671  24.271  56.301  1.00 64.25  ?  607  TYR A CG  1 
ATOM   4356  C CD1 . TYR A  1  607 ? 34.954  24.629  57.613  1.00 65.44  ?  607  TYR A CD1 1 
ATOM   4357  C CD2 . TYR A  1  607 ? 35.607  24.577  55.323  1.00 65.11  ?  607  TYR A CD2 1 
ATOM   4358  C CE1 . TYR A  1  607 ? 36.134  25.265  57.943  1.00 67.38  ?  607  TYR A CE1 1 
ATOM   4359  C CE2 . TYR A  1  607 ? 36.792  25.213  55.644  1.00 67.08  ?  607  TYR A CE2 1 
ATOM   4360  C CZ  . TYR A  1  607 ? 37.050  25.554  56.955  1.00 68.19  ?  607  TYR A CZ  1 
ATOM   4361  O OH  . TYR A  1  607 ? 38.227  26.188  57.278  1.00 70.23  ?  607  TYR A OH  1 
ATOM   4362  N N   . ASN A  1  608 ? 29.850  24.712  55.430  1.00 62.08  ?  608  ASN A N   1 
ATOM   4363  C CA  . ASN A  1  608 ? 28.562  24.280  54.910  1.00 60.67  ?  608  ASN A CA  1 
ATOM   4364  C C   . ASN A  1  608 ? 27.906  25.459  54.199  1.00 62.30  ?  608  ASN A C   1 
ATOM   4365  O O   . ASN A  1  608 ? 28.532  26.497  53.961  1.00 64.33  ?  608  ASN A O   1 
ATOM   4366  C CB  . ASN A  1  608 ? 27.697  23.742  56.056  1.00 59.82  ?  608  ASN A CB  1 
ATOM   4367  C CG  . ASN A  1  608 ? 27.846  22.251  56.249  1.00 57.49  ?  608  ASN A CG  1 
ATOM   4368  O OD1 . ASN A  1  608 ? 28.521  21.574  55.474  1.00 56.35  ?  608  ASN A OD1 1 
ATOM   4369  N ND2 . ASN A  1  608 ? 27.248  21.736  57.315  1.00 56.91  ?  608  ASN A ND2 1 
ATOM   4370  N N   . GLN A  1  609 ? 26.628  25.294  53.860  1.00 62.25  ?  609  GLN A N   1 
ATOM   4371  C CA  . GLN A  1  609 ? 25.805  26.358  53.297  1.00 63.80  ?  609  GLN A CA  1 
ATOM   4372  C C   . GLN A  1  609 ? 24.618  26.656  54.206  1.00 64.26  ?  609  GLN A C   1 
ATOM   4373  O O   . GLN A  1  609 ? 23.536  27.015  53.737  1.00 64.59  ?  609  GLN A O   1 
ATOM   4374  C CB  . GLN A  1  609 ? 25.331  25.995  51.889  1.00 62.75  ?  609  GLN A CB  1 
ATOM   4375  C CG  . GLN A  1  609 ? 26.402  26.121  50.815  1.00 63.16  ?  609  GLN A CG  1 
ATOM   4376  C CD  . GLN A  1  609 ? 26.065  25.337  49.559  1.00 62.34  ?  609  GLN A CD  1 
ATOM   4377  O OE1 . GLN A  1  609 ? 24.922  25.333  49.104  1.00 62.45  ?  609  GLN A OE1 1 
ATOM   4378  N NE2 . GLN A  1  609 ? 27.064  24.668  48.994  1.00 62.08  ?  609  GLN A NE2 1 
ATOM   4379  N N   . LEU A  1  610 ? 24.818  26.504  55.513  1.00 61.62  ?  610  LEU A N   1 
ATOM   4380  C CA  . LEU A  1  610 ? 23.747  26.701  56.478  1.00 62.11  ?  610  LEU A CA  1 
ATOM   4381  C C   . LEU A  1  610 ? 23.430  28.185  56.616  1.00 64.82  ?  610  LEU A C   1 
ATOM   4382  O O   . LEU A  1  610 ? 24.335  29.014  56.746  1.00 66.55  ?  610  LEU A O   1 
ATOM   4383  C CB  . LEU A  1  610 ? 24.147  26.119  57.833  1.00 61.69  ?  610  LEU A CB  1 
ATOM   4384  C CG  . LEU A  1  610 ? 24.393  24.609  57.921  1.00 59.17  ?  610  LEU A CG  1 
ATOM   4385  C CD1 . LEU A  1  610 ? 24.563  24.175  59.369  1.00 59.19  ?  610  LEU A CD1 1 
ATOM   4386  C CD2 . LEU A  1  610 ? 23.278  23.823  57.252  1.00 57.38  ?  610  LEU A CD2 1 
ATOM   4387  N N   . ASP A  1  611 ? 22.146  28.518  56.588  1.00 68.70  ?  611  ASP A N   1 
ATOM   4388  C CA  . ASP A  1  611 ? 21.688  29.890  56.760  1.00 71.32  ?  611  ASP A CA  1 
ATOM   4389  C C   . ASP A  1  611 ? 20.686  29.938  57.912  1.00 71.83  ?  611  ASP A C   1 
ATOM   4390  O O   . ASP A  1  611 ? 20.457  28.943  58.606  1.00 70.27  ?  611  ASP A O   1 
ATOM   4391  C CB  . ASP A  1  611 ? 21.092  30.434  55.459  1.00 71.89  ?  611  ASP A CB  1 
ATOM   4392  C CG  . ASP A  1  611 ? 19.769  29.785  55.103  1.00 70.48  ?  611  ASP A CG  1 
ATOM   4393  O OD1 . ASP A  1  611 ? 19.594  28.582  55.391  1.00 68.28  ?  611  ASP A OD1 1 
ATOM   4394  O OD2 . ASP A  1  611 ? 18.901  30.480  54.536  1.00 71.68  -1 611  ASP A OD2 1 
ATOM   4395  N N   . GLY A  1  612 ? 20.096  31.107  58.121  1.00 75.00  ?  612  GLY A N   1 
ATOM   4396  C CA  . GLY A  1  612 ? 19.163  31.283  59.212  1.00 75.88  ?  612  GLY A CA  1 
ATOM   4397  C C   . GLY A  1  612 ? 19.847  31.711  60.494  1.00 77.33  ?  612  GLY A C   1 
ATOM   4398  O O   . GLY A  1  612 ? 21.054  31.965  60.552  1.00 77.83  ?  612  GLY A O   1 
ATOM   4399  N N   . GLU A  1  613 ? 19.044  31.779  61.550  1.00 82.90  ?  613  GLU A N   1 
ATOM   4400  C CA  . GLU A  1  613 ? 19.493  32.260  62.849  1.00 84.77  ?  613  GLU A CA  1 
ATOM   4401  C C   . GLU A  1  613 ? 19.822  31.088  63.762  1.00 82.90  ?  613  GLU A C   1 
ATOM   4402  O O   . GLU A  1  613 ? 19.152  30.051  63.726  1.00 81.01  ?  613  GLU A O   1 
ATOM   4403  C CB  . GLU A  1  613 ? 18.425  33.141  63.500  1.00 86.81  ?  613  GLU A CB  1 
ATOM   4404  C CG  . GLU A  1  613 ? 18.131  34.425  62.742  1.00 88.92  ?  613  GLU A CG  1 
ATOM   4405  C CD  . GLU A  1  613 ? 17.379  35.436  63.584  1.00 91.89  ?  613  GLU A CD  1 
ATOM   4406  O OE1 . GLU A  1  613 ? 16.320  35.076  64.140  1.00 92.08  ?  613  GLU A OE1 1 
ATOM   4407  O OE2 . GLU A  1  613 ? 17.847  36.589  63.693  1.00 94.60  -1 613  GLU A OE2 1 
ATOM   4408  N N   . ILE A  1  614 ? 20.863  31.257  64.574  1.00 80.92  ?  614  ILE A N   1 
ATOM   4409  C CA  . ILE A  1  614 ? 21.250  30.238  65.546  1.00 79.74  ?  614  ILE A CA  1 
ATOM   4410  C C   . ILE A  1  614 ? 20.165  30.176  66.615  1.00 80.56  ?  614  ILE A C   1 
ATOM   4411  O O   . ILE A  1  614 ? 19.992  31.121  67.390  1.00 82.94  ?  614  ILE A O   1 
ATOM   4412  C CB  . ILE A  1  614 ? 22.620  30.537  66.164  1.00 80.75  ?  614  ILE A CB  1 
ATOM   4413  C CG1 . ILE A  1  614 ? 23.600  31.025  65.094  1.00 80.88  ?  614  ILE A CG1 1 
ATOM   4414  C CG2 . ILE A  1  614 ? 23.161  29.305  66.874  1.00 79.12  ?  614  ILE A CG2 1 
ATOM   4415  C CD1 . ILE A  1  614 ? 25.004  31.258  65.615  1.00 81.82  ?  614  ILE A CD1 1 
ATOM   4416  N N   . SER A  1  615 ? 19.419  29.073  66.644  1.00 81.28  ?  615  SER A N   1 
ATOM   4417  C CA  . SER A  1  615 ? 18.347  28.914  67.618  1.00 82.02  ?  615  SER A CA  1 
ATOM   4418  C C   . SER A  1  615 ? 18.885  29.037  69.038  1.00 83.47  ?  615  SER A C   1 
ATOM   4419  O O   . SER A  1  615 ? 19.918  28.454  69.378  1.00 82.65  ?  615  SER A O   1 
ATOM   4420  C CB  . SER A  1  615 ? 17.660  27.562  67.428  1.00 79.64  ?  615  SER A CB  1 
ATOM   4421  O OG  . SER A  1  615 ? 16.741  27.306  68.476  1.00 80.42  ?  615  SER A OG  1 
ATOM   4422  N N   . SER A  1  616 ? 18.175  29.803  69.868  1.00 84.22  ?  616  SER A N   1 
ATOM   4423  C CA  . SER A  1  616 ? 18.562  29.971  71.263  1.00 85.91  ?  616  SER A CA  1 
ATOM   4424  C C   . SER A  1  616 ? 18.377  28.702  72.083  1.00 84.63  ?  616  SER A C   1 
ATOM   4425  O O   . SER A  1  616 ? 18.890  28.630  73.205  1.00 85.68  ?  616  SER A O   1 
ATOM   4426  C CB  . SER A  1  616 ? 17.764  31.113  71.893  1.00 88.74  ?  616  SER A CB  1 
ATOM   4427  O OG  . SER A  1  616 ? 18.510  31.759  72.910  1.00 91.06  ?  616  SER A OG  1 
ATOM   4428  N N   . GLN A  1  617 ? 17.662  27.706  71.554  1.00 85.22  ?  617  GLN A N   1 
ATOM   4429  C CA  . GLN A  1  617 ? 17.428  26.463  72.277  1.00 84.09  ?  617  GLN A CA  1 
ATOM   4430  C C   . GLN A  1  617 ? 18.685  25.616  72.430  1.00 82.83  ?  617  GLN A C   1 
ATOM   4431  O O   . GLN A  1  617 ? 18.632  24.582  73.106  1.00 81.86  ?  617  GLN A O   1 
ATOM   4432  C CB  . GLN A  1  617 ? 16.330  25.654  71.582  1.00 82.30  ?  617  GLN A CB  1 
ATOM   4433  C CG  . GLN A  1  617 ? 14.942  26.303  71.609  1.00 84.05  ?  617  GLN A CG  1 
ATOM   4434  C CD  . GLN A  1  617 ? 14.397  26.560  73.014  1.00 86.44  ?  617  GLN A CD  1 
ATOM   4435  O OE1 . GLN A  1  617 ? 14.992  26.169  74.019  1.00 86.77  ?  617  GLN A OE1 1 
ATOM   4436  N NE2 . GLN A  1  617 ? 13.253  27.232  73.080  1.00 88.44  ?  617  GLN A NE2 1 
ATOM   4437  N N   . PHE A  1  618 ? 19.805  26.016  71.821  1.00 81.39  ?  618  PHE A N   1 
ATOM   4438  C CA  . PHE A  1  618 ? 21.065  25.316  72.046  1.00 80.16  ?  618  PHE A CA  1 
ATOM   4439  C C   . PHE A  1  618 ? 21.518  25.408  73.496  1.00 81.82  ?  618  PHE A C   1 
ATOM   4440  O O   . PHE A  1  618 ? 22.408  24.655  73.907  1.00 81.10  ?  618  PHE A O   1 
ATOM   4441  C CB  . PHE A  1  618 ? 22.153  25.869  71.125  1.00 79.81  ?  618  PHE A CB  1 
ATOM   4442  C CG  . PHE A  1  618 ? 22.218  25.187  69.790  1.00 77.34  ?  618  PHE A CG  1 
ATOM   4443  C CD1 . PHE A  1  618 ? 21.275  25.455  68.812  1.00 76.90  ?  618  PHE A CD1 1 
ATOM   4444  C CD2 . PHE A  1  618 ? 23.219  24.270  69.516  1.00 75.62  ?  618  PHE A CD2 1 
ATOM   4445  C CE1 . PHE A  1  618 ? 21.333  24.826  67.583  1.00 75.06  ?  618  PHE A CE1 1 
ATOM   4446  C CE2 . PHE A  1  618 ? 23.282  23.638  68.290  1.00 73.45  ?  618  PHE A CE2 1 
ATOM   4447  C CZ  . PHE A  1  618 ? 22.339  23.916  67.323  1.00 72.96  ?  618  PHE A CZ  1 
ATOM   4448  N N   . ARG A  1  619 ? 20.936  26.325  74.273  1.00 85.63  ?  619  ARG A N   1 
ATOM   4449  C CA  . ARG A  1  619 ? 21.200  26.398  75.705  1.00 87.54  ?  619  ARG A CA  1 
ATOM   4450  C C   . ARG A  1  619 ? 20.827  25.105  76.422  1.00 86.14  ?  619  ARG A C   1 
ATOM   4451  O O   . ARG A  1  619 ? 21.339  24.843  77.516  1.00 87.18  ?  619  ARG A O   1 
ATOM   4452  C CB  . ARG A  1  619 ? 20.438  27.588  76.296  1.00 90.31  ?  619  ARG A CB  1 
ATOM   4453  C CG  . ARG A  1  619 ? 20.771  27.936  77.736  1.00 92.57  ?  619  ARG A CG  1 
ATOM   4454  C CD  . ARG A  1  619 ? 19.607  28.676  78.380  1.00 94.73  ?  619  ARG A CD  1 
ATOM   4455  N NE  . ARG A  1  619 ? 19.912  29.119  79.735  1.00 97.65  ?  619  ARG A NE  1 
ATOM   4456  C CZ  . ARG A  1  619 ? 19.051  29.095  80.743  1.00 98.96  ?  619  ARG A CZ  1 
ATOM   4457  N NH1 . ARG A  1  619 ? 17.814  28.652  80.585  1.00 98.56  ?  619  ARG A NH1 1 
ATOM   4458  N NH2 . ARG A  1  619 ? 19.438  29.530  81.938  1.00 101.20 ?  619  ARG A NH2 1 
ATOM   4459  N N   . SER A  1  620 ? 19.957  24.287  75.823  1.00 83.60  ?  620  SER A N   1 
ATOM   4460  C CA  . SER A  1  620 ? 19.560  23.021  76.428  1.00 82.68  ?  620  SER A CA  1 
ATOM   4461  C C   . SER A  1  620 ? 20.693  22.001  76.453  1.00 81.14  ?  620  SER A C   1 
ATOM   4462  O O   . SER A  1  620 ? 20.659  21.081  77.277  1.00 81.12  ?  620  SER A O   1 
ATOM   4463  C CB  . SER A  1  620 ? 18.358  22.436  75.683  1.00 81.11  ?  620  SER A CB  1 
ATOM   4464  O OG  . SER A  1  620 ? 17.273  23.348  75.663  1.00 82.90  ?  620  SER A OG  1 
ATOM   4465  N N   . LEU A  1  621 ? 21.692  22.140  75.579  1.00 77.20  ?  621  LEU A N   1 
ATOM   4466  C CA  . LEU A  1  621 ? 22.795  21.180  75.508  1.00 75.70  ?  621  LEU A CA  1 
ATOM   4467  C C   . LEU A  1  621 ? 23.730  21.448  76.684  1.00 77.60  ?  621  LEU A C   1 
ATOM   4468  O O   . LEU A  1  621 ? 24.735  22.157  76.583  1.00 78.41  ?  621  LEU A O   1 
ATOM   4469  C CB  . LEU A  1  621 ? 23.523  21.290  74.174  1.00 74.10  ?  621  LEU A CB  1 
ATOM   4470  C CG  . LEU A  1  621 ? 22.692  21.131  72.899  1.00 72.34  ?  621  LEU A CG  1 
ATOM   4471  C CD1 . LEU A  1  621 ? 23.576  21.221  71.663  1.00 71.00  ?  621  LEU A CD1 1 
ATOM   4472  C CD2 . LEU A  1  621 ? 21.927  19.824  72.914  1.00 70.64  ?  621  LEU A CD2 1 
ATOM   4473  N N   . GLN A  1  622 ? 23.382  20.856  77.830  1.00 79.63  ?  622  GLN A N   1 
ATOM   4474  C CA  . GLN A  1  622 ? 24.093  21.140  79.072  1.00 81.77  ?  622  GLN A CA  1 
ATOM   4475  C C   . GLN A  1  622 ? 25.477  20.505  79.126  1.00 81.01  ?  622  GLN A C   1 
ATOM   4476  O O   . GLN A  1  622 ? 26.311  20.942  79.927  1.00 82.78  ?  622  GLN A O   1 
ATOM   4477  C CB  . GLN A  1  622 ? 23.257  20.670  80.263  1.00 83.02  ?  622  GLN A CB  1 
ATOM   4478  C CG  . GLN A  1  622 ? 22.004  21.497  80.498  1.00 84.58  ?  622  GLN A CG  1 
ATOM   4479  C CD  . GLN A  1  622 ? 21.208  21.025  81.698  1.00 86.14  ?  622  GLN A CD  1 
ATOM   4480  O OE1 . GLN A  1  622 ? 21.716  20.290  82.545  1.00 86.41  ?  622  GLN A OE1 1 
ATOM   4481  N NE2 . GLN A  1  622 ? 19.951  21.447  81.776  1.00 86.95  ?  622  GLN A NE2 1 
ATOM   4482  N N   . ASN A  1  623 ? 25.743  19.491  78.305  1.00 75.52  ?  623  ASN A N   1 
ATOM   4483  C CA  . ASN A  1  623 ? 27.037  18.820  78.293  1.00 74.76  ?  623  ASN A CA  1 
ATOM   4484  C C   . ASN A  1  623 ? 27.910  19.229  77.115  1.00 73.71  ?  623  ASN A C   1 
ATOM   4485  O O   . ASN A  1  623 ? 29.009  18.688  76.959  1.00 73.00  ?  623  ASN A O   1 
ATOM   4486  C CB  . ASN A  1  623 ? 26.842  17.300  78.289  1.00 72.94  ?  623  ASN A CB  1 
ATOM   4487  C CG  . ASN A  1  623 ? 25.817  16.841  79.308  1.00 73.88  ?  623  ASN A CG  1 
ATOM   4488  O OD1 . ASN A  1  623 ? 24.629  17.146  79.193  1.00 74.04  ?  623  ASN A OD1 1 
ATOM   4489  N ND2 . ASN A  1  623 ? 26.273  16.107  80.316  1.00 74.64  ?  623  ASN A ND2 1 
ATOM   4490  N N   . LEU A  1  624 ? 27.450  20.165  76.289  1.00 72.34  ?  624  LEU A N   1 
ATOM   4491  C CA  . LEU A  1  624 ? 28.187  20.557  75.095  1.00 71.41  ?  624  LEU A CA  1 
ATOM   4492  C C   . LEU A  1  624 ? 29.510  21.217  75.467  1.00 73.01  ?  624  LEU A C   1 
ATOM   4493  O O   . LEU A  1  624 ? 29.541  22.187  76.231  1.00 75.30  ?  624  LEU A O   1 
ATOM   4494  C CB  . LEU A  1  624 ? 27.341  21.504  74.246  1.00 71.50  ?  624  LEU A CB  1 
ATOM   4495  C CG  . LEU A  1  624 ? 27.849  21.807  72.838  1.00 70.34  ?  624  LEU A CG  1 
ATOM   4496  C CD1 . LEU A  1  624 ? 28.018  20.522  72.043  1.00 67.70  ?  624  LEU A CD1 1 
ATOM   4497  C CD2 . LEU A  1  624 ? 26.897  22.755  72.134  1.00 70.74  ?  624  LEU A CD2 1 
ATOM   4498  N N   . GLU A  1  625 ? 30.606  20.687  74.924  1.00 68.64  ?  625  GLU A N   1 
ATOM   4499  C CA  . GLU A  1  625 ? 31.937  21.231  75.162  1.00 70.05  ?  625  GLU A CA  1 
ATOM   4500  C C   . GLU A  1  625 ? 32.541  21.928  73.954  1.00 69.77  ?  625  GLU A C   1 
ATOM   4501  O O   . GLU A  1  625 ? 33.349  22.842  74.128  1.00 71.54  ?  625  GLU A O   1 
ATOM   4502  C CB  . GLU A  1  625 ? 32.895  20.123  75.615  1.00 69.47  ?  625  GLU A CB  1 
ATOM   4503  C CG  . GLU A  1  625 ? 32.912  19.885  77.114  1.00 71.09  ?  625  GLU A CG  1 
ATOM   4504  C CD  . GLU A  1  625 ? 33.534  18.553  77.482  1.00 70.15  ?  625  GLU A CD  1 
ATOM   4505  O OE1 . GLU A  1  625 ? 34.721  18.341  77.157  1.00 69.92  ?  625  GLU A OE1 1 
ATOM   4506  O OE2 . GLU A  1  625 ? 32.836  17.719  78.097  1.00 69.76  -1 625  GLU A OE2 1 
ATOM   4507  N N   . ARG A  1  626 ? 32.180  21.518  72.740  1.00 71.78  ?  626  ARG A N   1 
ATOM   4508  C CA  . ARG A  1  626 ? 32.742  22.094  71.527  1.00 71.50  ?  626  ARG A CA  1 
ATOM   4509  C C   . ARG A  1  626 ? 31.630  22.464  70.558  1.00 70.64  ?  626  ARG A C   1 
ATOM   4510  O O   . ARG A  1  626 ? 30.645  21.733  70.415  1.00 69.12  ?  626  ARG A O   1 
ATOM   4511  C CB  . ARG A  1  626 ? 33.719  21.128  70.852  1.00 69.85  ?  626  ARG A CB  1 
ATOM   4512  C CG  . ARG A  1  626 ? 34.984  20.886  71.649  1.00 70.91  ?  626  ARG A CG  1 
ATOM   4513  C CD  . ARG A  1  626 ? 36.135  20.495  70.746  1.00 70.04  ?  626  ARG A CD  1 
ATOM   4514  N NE  . ARG A  1  626 ? 37.407  20.990  71.256  1.00 71.93  ?  626  ARG A NE  1 
ATOM   4515  C CZ  . ARG A  1  626 ? 38.568  20.366  71.109  1.00 71.64  ?  626  ARG A CZ  1 
ATOM   4516  N NH1 . ARG A  1  626 ? 38.656  19.213  70.468  1.00 69.54  ?  626  ARG A NH1 1 
ATOM   4517  N NH2 . ARG A  1  626 ? 39.667  20.914  71.620  1.00 73.60  ?  626  ARG A NH2 1 
ATOM   4518  N N   . LEU A  1  627 ? 31.802  23.603  69.891  1.00 68.18  ?  627  LEU A N   1 
ATOM   4519  C CA  . LEU A  1  627 ? 30.861  24.084  68.890  1.00 67.66  ?  627  LEU A CA  1 
ATOM   4520  C C   . LEU A  1  627 ? 31.642  24.744  67.767  1.00 67.97  ?  627  LEU A C   1 
ATOM   4521  O O   . LEU A  1  627 ? 32.469  25.626  68.020  1.00 69.90  ?  627  LEU A O   1 
ATOM   4522  C CB  . LEU A  1  627 ? 29.861  25.079  69.492  1.00 69.44  ?  627  LEU A CB  1 
ATOM   4523  C CG  . LEU A  1  627 ? 28.385  24.679  69.464  1.00 68.42  ?  627  LEU A CG  1 
ATOM   4524  C CD1 . LEU A  1  627 ? 27.498  25.882  69.751  1.00 70.40  ?  627  LEU A CD1 1 
ATOM   4525  C CD2 . LEU A  1  627 ? 28.017  24.041  68.133  1.00 66.12  ?  627  LEU A CD2 1 
ATOM   4526  N N   . ASP A  1  628 ? 31.385  24.316  66.533  1.00 63.10  ?  628  ASP A N   1 
ATOM   4527  C CA  . ASP A  1  628 ? 32.028  24.890  65.356  1.00 63.37  ?  628  ASP A CA  1 
ATOM   4528  C C   . ASP A  1  628 ? 30.957  25.122  64.300  1.00 62.58  ?  628  ASP A C   1 
ATOM   4529  O O   . ASP A  1  628 ? 30.471  24.169  63.683  1.00 60.44  ?  628  ASP A O   1 
ATOM   4530  C CB  . ASP A  1  628 ? 33.136  23.977  64.828  1.00 62.03  ?  628  ASP A CB  1 
ATOM   4531  C CG  . ASP A  1  628 ? 34.041  24.673  63.828  1.00 62.91  ?  628  ASP A CG  1 
ATOM   4532  O OD1 . ASP A  1  628 ? 33.734  25.819  63.437  1.00 64.39  ?  628  ASP A OD1 1 
ATOM   4533  O OD2 . ASP A  1  628 ? 35.063  24.073  63.432  1.00 62.25  -1 628  ASP A OD2 1 
ATOM   4534  N N   . LEU A  1  629 ? 30.596  26.390  64.094  1.00 64.40  ?  629  LEU A N   1 
ATOM   4535  C CA  . LEU A  1  629 ? 29.609  26.786  63.097  1.00 64.09  ?  629  LEU A CA  1 
ATOM   4536  C C   . LEU A  1  629 ? 30.228  27.672  62.022  1.00 65.21  ?  629  LEU A C   1 
ATOM   4537  O O   . LEU A  1  629 ? 29.515  28.427  61.354  1.00 65.94  ?  629  LEU A O   1 
ATOM   4538  C CB  . LEU A  1  629 ? 28.434  27.510  63.761  1.00 65.40  ?  629  LEU A CB  1 
ATOM   4539  C CG  . LEU A  1  629 ? 27.608  26.823  64.855  1.00 64.76  ?  629  LEU A CG  1 
ATOM   4540  C CD1 . LEU A  1  629 ? 26.190  27.365  64.851  1.00 65.39  ?  629  LEU A CD1 1 
ATOM   4541  C CD2 . LEU A  1  629 ? 27.586  25.312  64.686  1.00 62.12  ?  629  LEU A CD2 1 
ATOM   4542  N N   . SER A  1  630 ? 31.543  27.589  61.842  1.00 68.00  ?  630  SER A N   1 
ATOM   4543  C CA  . SER A  1  630 ? 32.248  28.495  60.951  1.00 69.47  ?  630  SER A CA  1 
ATOM   4544  C C   . SER A  1  630 ? 31.960  28.163  59.489  1.00 68.09  ?  630  SER A C   1 
ATOM   4545  O O   . SER A  1  630 ? 31.485  27.076  59.149  1.00 65.79  ?  630  SER A O   1 
ATOM   4546  C CB  . SER A  1  630 ? 33.753  28.439  61.214  1.00 70.24  ?  630  SER A CB  1 
ATOM   4547  O OG  . SER A  1  630 ? 34.285  27.170  60.874  1.00 68.11  ?  630  SER A OG  1 
ATOM   4548  N N   . HIS A  1  631 ? 32.261  29.131  58.622  1.00 73.39  ?  631  HIS A N   1 
ATOM   4549  C CA  . HIS A  1  631 ? 32.115  28.993  57.172  1.00 72.59  ?  631  HIS A CA  1 
ATOM   4550  C C   . HIS A  1  631 ? 30.675  28.636  56.797  1.00 71.15  ?  631  HIS A C   1 
ATOM   4551  O O   . HIS A  1  631 ? 30.387  27.583  56.225  1.00 68.92  ?  631  HIS A O   1 
ATOM   4552  C CB  . HIS A  1  631 ? 33.110  27.967  56.618  1.00 71.05  ?  631  HIS A CB  1 
ATOM   4553  C CG  . HIS A  1  631 ? 34.543  28.361  56.798  1.00 72.63  ?  631  HIS A CG  1 
ATOM   4554  N ND1 . HIS A  1  631 ? 35.074  28.704  58.023  1.00 73.94  ?  631  HIS A ND1 1 
ATOM   4555  C CD2 . HIS A  1  631 ? 35.557  28.471  55.906  1.00 73.25  ?  631  HIS A CD2 1 
ATOM   4556  C CE1 . HIS A  1  631 ? 36.352  29.006  57.879  1.00 75.26  ?  631  HIS A CE1 1 
ATOM   4557  N NE2 . HIS A  1  631 ? 36.670  28.872  56.604  1.00 74.89  ?  631  HIS A NE2 1 
ATOM   4558  N N   . ASN A  1  632 ? 29.765  29.544  57.146  1.00 70.73  ?  632  ASN A N   1 
ATOM   4559  C CA  . ASN A  1  632 ? 28.343  29.371  56.897  1.00 69.80  ?  632  ASN A CA  1 
ATOM   4560  C C   . ASN A  1  632 ? 27.748  30.724  56.527  1.00 72.09  ?  632  ASN A C   1 
ATOM   4561  O O   . ASN A  1  632 ? 28.460  31.723  56.390  1.00 74.25  ?  632  ASN A O   1 
ATOM   4562  C CB  . ASN A  1  632 ? 27.650  28.764  58.121  1.00 68.88  ?  632  ASN A CB  1 
ATOM   4563  C CG  . ASN A  1  632 ? 27.897  27.275  58.249  1.00 66.30  ?  632  ASN A CG  1 
ATOM   4564  O OD1 . ASN A  1  632 ? 27.329  26.475  57.509  1.00 64.41  ?  632  ASN A OD1 1 
ATOM   4565  N ND2 . ASN A  1  632 ? 28.759  26.897  59.186  1.00 66.31  ?  632  ASN A ND2 1 
ATOM   4566  N N   . ASN A  1  633 ? 26.428  30.757  56.365  1.00 72.14  ?  633  ASN A N   1 
ATOM   4567  C CA  . ASN A  1  633 ? 25.694  31.985  56.086  1.00 74.30  ?  633  ASN A CA  1 
ATOM   4568  C C   . ASN A  1  633 ? 24.656  32.243  57.171  1.00 74.92  ?  633  ASN A C   1 
ATOM   4569  O O   . ASN A  1  633 ? 23.553  32.726  56.907  1.00 75.63  ?  633  ASN A O   1 
ATOM   4570  C CB  . ASN A  1  633 ? 25.041  31.933  54.706  1.00 73.71  ?  633  ASN A CB  1 
ATOM   4571  C CG  . ASN A  1  633 ? 24.749  33.313  54.144  1.00 76.36  ?  633  ASN A CG  1 
ATOM   4572  O OD1 . ASN A  1  633 ? 25.337  34.308  54.570  1.00 78.65  ?  633  ASN A OD1 1 
ATOM   4573  N ND2 . ASN A  1  633 ? 23.839  33.379  53.178  1.00 76.16  ?  633  ASN A ND2 1 
ATOM   4574  N N   . LEU A  1  634 ? 25.008  31.916  58.412  1.00 75.34  ?  634  LEU A N   1 
ATOM   4575  C CA  . LEU A  1  634 ? 24.115  32.157  59.537  1.00 76.14  ?  634  LEU A CA  1 
ATOM   4576  C C   . LEU A  1  634 ? 24.021  33.650  59.822  1.00 79.23  ?  634  LEU A C   1 
ATOM   4577  O O   . LEU A  1  634 ? 25.038  34.349  59.875  1.00 80.82  ?  634  LEU A O   1 
ATOM   4578  C CB  . LEU A  1  634 ? 24.600  31.410  60.778  1.00 75.34  ?  634  LEU A CB  1 
ATOM   4579  C CG  . LEU A  1  634 ? 24.899  29.917  60.626  1.00 72.49  ?  634  LEU A CG  1 
ATOM   4580  C CD1 . LEU A  1  634 ? 26.120  29.528  61.445  1.00 72.42  ?  634  LEU A CD1 1 
ATOM   4581  C CD2 . LEU A  1  634 ? 23.692  29.085  61.027  1.00 71.00  ?  634  LEU A CD2 1 
ATOM   4582  N N   . SER A  1  635 ? 22.802  34.136  60.009  1.00 81.44  ?  635  SER A N   1 
ATOM   4583  C CA  . SER A  1  635 ? 22.540  35.546  60.256  1.00 84.45  ?  635  SER A CA  1 
ATOM   4584  C C   . SER A  1  635 ? 21.893  35.712  61.628  1.00 85.43  ?  635  SER A C   1 
ATOM   4585  O O   . SER A  1  635 ? 21.742  34.755  62.390  1.00 83.87  ?  635  SER A O   1 
ATOM   4586  C CB  . SER A  1  635 ? 21.655  36.136  59.152  1.00 85.18  ?  635  SER A CB  1 
ATOM   4587  O OG  . SER A  1  635 ? 20.416  35.454  59.075  1.00 83.69  ?  635  SER A OG  1 
ATOM   4588  N N   . GLY A  1  636 ? 21.508  36.947  61.938  1.00 87.56  ?  636  GLY A N   1 
ATOM   4589  C CA  . GLY A  1  636 ? 20.989  37.261  63.251  1.00 88.96  ?  636  GLY A CA  1 
ATOM   4590  C C   . GLY A  1  636 ? 22.103  37.460  64.259  1.00 89.97  ?  636  GLY A C   1 
ATOM   4591  O O   . GLY A  1  636 ? 23.291  37.461  63.939  1.00 89.82  ?  636  GLY A O   1 
ATOM   4592  N N   . GLN A  1  637 ? 21.700  37.648  65.509  1.00 93.82  ?  637  GLN A N   1 
ATOM   4593  C CA  . GLN A  1  637 ? 22.638  37.812  66.609  1.00 94.92  ?  637  GLN A CA  1 
ATOM   4594  C C   . GLN A  1  637 ? 22.841  36.493  67.343  1.00 92.73  ?  637  GLN A C   1 
ATOM   4595  O O   . GLN A  1  637 ? 21.922  35.678  67.459  1.00 91.18  ?  637  GLN A O   1 
ATOM   4596  C CB  . GLN A  1  637 ? 22.157  38.888  67.586  1.00 97.91  ?  637  GLN A CB  1 
ATOM   4597  C CG  . GLN A  1  637 ? 21.703  40.173  66.913  1.00 100.21 ?  637  GLN A CG  1 
ATOM   4598  C CD  . GLN A  1  637 ? 21.624  41.343  67.874  1.00 103.49 ?  637  GLN A CD  1 
ATOM   4599  O OE1 . GLN A  1  637 ? 21.812  41.185  69.080  1.00 104.05 ?  637  GLN A OE1 1 
ATOM   4600  N NE2 . GLN A  1  637 ? 21.344  42.527  67.342  1.00 105.79 ?  637  GLN A NE2 1 
ATOM   4601  N N   . ILE A  1  638 ? 24.065  36.284  67.822  1.00 94.50  ?  638  ILE A N   1 
ATOM   4602  C CA  . ILE A  1  638 ? 24.381  35.126  68.655  1.00 92.40  ?  638  ILE A CA  1 
ATOM   4603  C C   . ILE A  1  638 ? 23.518  35.209  69.908  1.00 93.74  ?  638  ILE A C   1 
ATOM   4604  O O   . ILE A  1  638 ? 23.559  36.225  70.618  1.00 96.54  ?  638  ILE A O   1 
ATOM   4605  C CB  . ILE A  1  638 ? 25.876  35.068  69.009  1.00 92.70  ?  638  ILE A CB  1 
ATOM   4606  C CG1 . ILE A  1  638 ? 26.725  34.950  67.742  1.00 91.59  ?  638  ILE A CG1 1 
ATOM   4607  C CG2 . ILE A  1  638 ? 26.157  33.905  69.950  1.00 91.29  ?  638  ILE A CG2 1 
ATOM   4608  C CD1 . ILE A  1  638 ? 28.216  34.928  68.008  1.00 92.03  ?  638  ILE A CD1 1 
ATOM   4609  N N   . PRO A  1  639 ? 22.722  34.186  70.210  1.00 94.09  ?  639  PRO A N   1 
ATOM   4610  C CA  . PRO A  1  639 ? 21.770  34.279  71.324  1.00 95.37  ?  639  PRO A CA  1 
ATOM   4611  C C   . PRO A  1  639 ? 22.484  34.518  72.641  1.00 97.10  ?  639  PRO A C   1 
ATOM   4612  O O   . PRO A  1  639 ? 23.358  33.732  73.037  1.00 95.99  ?  639  PRO A O   1 
ATOM   4613  C CB  . PRO A  1  639 ? 21.070  32.910  71.309  1.00 92.84  ?  639  PRO A CB  1 
ATOM   4614  C CG  . PRO A  1  639 ? 21.989  32.013  70.542  1.00 90.36  ?  639  PRO A CG  1 
ATOM   4615  C CD  . PRO A  1  639 ? 22.645  32.887  69.523  1.00 91.00  ?  639  PRO A CD  1 
ATOM   4616  N N   . PRO A  1  640 ? 22.142  35.600  73.347  1.00 97.62  ?  640  PRO A N   1 
ATOM   4617  C CA  . PRO A  1  640 ? 22.822  35.901  74.618  1.00 99.52  ?  640  PRO A CA  1 
ATOM   4618  C C   . PRO A  1  640 ? 22.612  34.848  75.694  1.00 98.75  ?  640  PRO A C   1 
ATOM   4619  O O   . PRO A  1  640 ? 23.308  34.893  76.717  1.00 100.00 ?  640  PRO A O   1 
ATOM   4620  C CB  . PRO A  1  640 ? 22.212  37.247  75.034  1.00 102.65 ?  640  PRO A CB  1 
ATOM   4621  C CG  . PRO A  1  640 ? 21.688  37.839  73.761  1.00 102.51 ?  640  PRO A CG  1 
ATOM   4622  C CD  . PRO A  1  640 ? 21.211  36.670  72.953  1.00 99.39  ?  640  PRO A CD  1 
ATOM   4623  N N   . SER A  1  641 ? 21.683  33.909  75.504  1.00 99.58  ?  641  SER A N   1 
ATOM   4624  C CA  . SER A  1  641 ? 21.502  32.820  76.457  1.00 98.78  ?  641  SER A CA  1 
ATOM   4625  C C   . SER A  1  641 ? 22.638  31.806  76.424  1.00 96.91  ?  641  SER A C   1 
ATOM   4626  O O   . SER A  1  641 ? 22.575  30.814  77.158  1.00 96.05  ?  641  SER A O   1 
ATOM   4627  C CB  . SER A  1  641 ? 20.172  32.111  76.196  1.00 97.42  ?  641  SER A CB  1 
ATOM   4628  O OG  . SER A  1  641 ? 20.177  31.468  74.933  1.00 94.74  ?  641  SER A OG  1 
ATOM   4629  N N   . PHE A  1  642 ? 23.667  32.024  75.603  1.00 100.01 ?  642  PHE A N   1 
ATOM   4630  C CA  . PHE A  1  642 ? 24.816  31.130  75.566  1.00 98.50  ?  642  PHE A CA  1 
ATOM   4631  C C   . PHE A  1  642 ? 25.788  31.370  76.712  1.00 100.06 ?  642  PHE A C   1 
ATOM   4632  O O   . PHE A  1  642 ? 26.693  30.553  76.915  1.00 98.74  ?  642  PHE A O   1 
ATOM   4633  C CB  . PHE A  1  642 ? 25.552  31.272  74.231  1.00 96.94  ?  642  PHE A CB  1 
ATOM   4634  C CG  . PHE A  1  642 ? 24.957  30.456  73.120  1.00 93.98  ?  642  PHE A CG  1 
ATOM   4635  C CD1 . PHE A  1  642 ? 23.696  29.897  73.247  1.00 93.32  ?  642  PHE A CD1 1 
ATOM   4636  C CD2 . PHE A  1  642 ? 25.662  30.247  71.946  1.00 92.35  ?  642  PHE A CD2 1 
ATOM   4637  C CE1 . PHE A  1  642 ? 23.149  29.144  72.225  1.00 91.04  ?  642  PHE A CE1 1 
ATOM   4638  C CE2 . PHE A  1  642 ? 25.120  29.496  70.920  1.00 89.99  ?  642  PHE A CE2 1 
ATOM   4639  C CZ  . PHE A  1  642 ? 23.863  28.944  71.060  1.00 89.13  ?  642  PHE A CZ  1 
ATOM   4640  N N   . LYS A  1  643 ? 25.629  32.467  77.457  1.00 98.67  ?  643  LYS A N   1 
ATOM   4641  C CA  . LYS A  1  643 ? 26.474  32.712  78.618  1.00 100.80 ?  643  LYS A CA  1 
ATOM   4642  C C   . LYS A  1  643 ? 26.258  31.682  79.720  1.00 100.16 ?  643  LYS A C   1 
ATOM   4643  O O   . LYS A  1  643 ? 27.138  31.507  80.569  1.00 101.06 ?  643  LYS A O   1 
ATOM   4644  C CB  . LYS A  1  643 ? 26.219  34.120  79.162  1.00 103.67 ?  643  LYS A CB  1 
ATOM   4645  C CG  . LYS A  1  643 ? 24.852  34.305  79.800  1.00 104.84 ?  643  LYS A CG  1 
ATOM   4646  C CD  . LYS A  1  643 ? 24.632  35.745  80.234  1.00 108.06 ?  643  LYS A CD  1 
ATOM   4647  C CE  . LYS A  1  643 ? 23.294  35.909  80.937  1.00 109.42 ?  643  LYS A CE  1 
ATOM   4648  N NZ  . LYS A  1  643 ? 23.179  35.026  82.131  1.00 109.52 ?  643  LYS A NZ  1 
ATOM   4649  N N   . ASP A  1  644 ? 25.113  31.001  79.724  1.00 100.61 ?  644  ASP A N   1 
ATOM   4650  C CA  . ASP A  1  644 ? 24.770  30.036  80.759  1.00 100.48 ?  644  ASP A CA  1 
ATOM   4651  C C   . ASP A  1  644 ? 25.238  28.621  80.440  1.00 97.92  ?  644  ASP A C   1 
ATOM   4652  O O   . ASP A  1  644 ? 24.866  27.686  81.155  1.00 97.36  ?  644  ASP A O   1 
ATOM   4653  C CB  . ASP A  1  644 ? 23.258  30.036  80.994  1.00 100.94 ?  644  ASP A CB  1 
ATOM   4654  C CG  . ASP A  1  644 ? 22.728  31.402  81.373  1.00 103.79 ?  644  ASP A CG  1 
ATOM   4655  O OD1 . ASP A  1  644 ? 23.508  32.214  81.912  1.00 105.87 ?  644  ASP A OD1 1 
ATOM   4656  O OD2 . ASP A  1  644 ? 21.532  31.665  81.129  1.00 104.06 -1 644  ASP A OD2 1 
ATOM   4657  N N   . MET A  1  645 ? 26.027  28.438  79.385  1.00 97.27  ?  645  MET A N   1 
ATOM   4658  C CA  . MET A  1  645 ? 26.545  27.120  79.018  1.00 94.81  ?  645  MET A CA  1 
ATOM   4659  C C   . MET A  1  645 ? 27.939  26.986  79.625  1.00 95.14  ?  645  MET A C   1 
ATOM   4660  O O   . MET A  1  645 ? 28.941  27.389  79.031  1.00 95.07  ?  645  MET A O   1 
ATOM   4661  C CB  . MET A  1  645 ? 26.540  26.938  77.505  1.00 92.59  ?  645  MET A CB  1 
ATOM   4662  C CG  . MET A  1  645 ? 25.139  26.715  76.942  1.00 90.95  ?  645  MET A CG  1 
ATOM   4663  S SD  . MET A  1  645 ? 25.026  26.692  75.143  1.00 88.65  ?  645  MET A SD  1 
ATOM   4664  C CE  . MET A  1  645 ? 26.753  26.643  74.686  1.00 88.14  ?  645  MET A CE  1 
ATOM   4665  N N   . LEU A  1  646 ? 27.995  26.409  80.828  1.00 91.85  ?  646  LEU A N   1 
ATOM   4666  C CA  . LEU A  1  646 ? 29.251  26.345  81.570  1.00 92.99  ?  646  LEU A CA  1 
ATOM   4667  C C   . LEU A  1  646 ? 30.200  25.300  80.996  1.00 90.79  ?  646  LEU A C   1 
ATOM   4668  O O   . LEU A  1  646 ? 31.422  25.449  81.107  1.00 91.42  ?  646  LEU A O   1 
ATOM   4669  C CB  . LEU A  1  646 ? 28.984  26.047  83.048  1.00 94.76  ?  646  LEU A CB  1 
ATOM   4670  C CG  . LEU A  1  646 ? 28.062  26.965  83.859  1.00 97.27  ?  646  LEU A CG  1 
ATOM   4671  C CD1 . LEU A  1  646 ? 26.591  26.610  83.666  1.00 96.39  ?  646  LEU A CD1 1 
ATOM   4672  C CD2 . LEU A  1  646 ? 28.434  26.919  85.333  1.00 99.61  ?  646  LEU A CD2 1 
ATOM   4673  N N   . ALA A  1  647 ? 29.665  24.240  80.388  1.00 86.62  ?  647  ALA A N   1 
ATOM   4674  C CA  . ALA A  1  647 ? 30.514  23.180  79.859  1.00 84.56  ?  647  ALA A CA  1 
ATOM   4675  C C   . ALA A  1  647 ? 31.259  23.603  78.600  1.00 83.57  ?  647  ALA A C   1 
ATOM   4676  O O   . ALA A  1  647 ? 32.311  23.031  78.299  1.00 82.66  ?  647  ALA A O   1 
ATOM   4677  C CB  . ALA A  1  647 ? 29.680  21.931  79.572  1.00 82.31  ?  647  ALA A CB  1 
ATOM   4678  N N   . LEU A  1  648 ? 30.733  24.578  77.861  1.00 85.19  ?  648  LEU A N   1 
ATOM   4679  C CA  . LEU A  1  648 ? 31.351  25.010  76.614  1.00 84.38  ?  648  LEU A CA  1 
ATOM   4680  C C   . LEU A  1  648 ? 32.757  25.550  76.856  1.00 85.90  ?  648  LEU A C   1 
ATOM   4681  O O   . LEU A  1  648 ? 32.979  26.354  77.765  1.00 88.32  ?  648  LEU A O   1 
ATOM   4682  C CB  . LEU A  1  648 ? 30.477  26.080  75.961  1.00 84.95  ?  648  LEU A CB  1 
ATOM   4683  C CG  . LEU A  1  648 ? 30.801  26.538  74.541  1.00 84.07  ?  648  LEU A CG  1 
ATOM   4684  C CD1 . LEU A  1  648 ? 30.452  25.462  73.525  1.00 81.19  ?  648  LEU A CD1 1 
ATOM   4685  C CD2 . LEU A  1  648 ? 30.056  27.828  74.247  1.00 85.59  ?  648  LEU A CD2 1 
ATOM   4686  N N   . THR A  1  649 ? 33.710  25.100  76.037  1.00 83.65  ?  649  THR A N   1 
ATOM   4687  C CA  . THR A  1  649 ? 35.089  25.572  76.114  1.00 85.00  ?  649  THR A CA  1 
ATOM   4688  C C   . THR A  1  649 ? 35.608  26.154  74.809  1.00 84.62  ?  649  THR A C   1 
ATOM   4689  O O   . THR A  1  649 ? 36.349  27.140  74.835  1.00 86.54  ?  649  THR A O   1 
ATOM   4690  C CB  . THR A  1  649 ? 36.030  24.436  76.553  1.00 84.28  ?  649  THR A CB  1 
ATOM   4691  O OG1 . THR A  1  649 ? 36.474  23.707  75.401  1.00 82.08  ?  649  THR A OG1 1 
ATOM   4692  C CG2 . THR A  1  649 ? 35.333  23.485  77.510  1.00 83.79  ?  649  THR A CG2 1 
ATOM   4693  N N   . HIS A  1  650 ? 35.241  25.578  73.665  1.00 85.19  ?  650  HIS A N   1 
ATOM   4694  C CA  . HIS A  1  650 ? 35.748  26.010  72.368  1.00 84.76  ?  650  HIS A CA  1 
ATOM   4695  C C   . HIS A  1  650 ? 34.589  26.431  71.477  1.00 84.20  ?  650  HIS A C   1 
ATOM   4696  O O   . HIS A  1  650 ? 33.588  25.715  71.372  1.00 82.33  ?  650  HIS A O   1 
ATOM   4697  C CB  . HIS A  1  650 ? 36.549  24.894  71.686  1.00 82.64  ?  650  HIS A CB  1 
ATOM   4698  C CG  . HIS A  1  650 ? 37.845  24.570  72.363  1.00 83.55  ?  650  HIS A CG  1 
ATOM   4699  N ND1 . HIS A  1  650 ? 37.980  24.509  73.733  1.00 84.96  ?  650  HIS A ND1 1 
ATOM   4700  C CD2 . HIS A  1  650 ? 39.068  24.286  71.853  1.00 83.47  ?  650  HIS A CD2 1 
ATOM   4701  C CE1 . HIS A  1  650 ? 39.228  24.204  74.039  1.00 85.56  ?  650  HIS A CE1 1 
ATOM   4702  N NE2 . HIS A  1  650 ? 39.909  24.062  72.916  1.00 84.82  ?  650  HIS A NE2 1 
ATOM   4703  N N   . VAL A  1  651 ? 34.727  27.594  70.839  1.00 83.13  ?  651  VAL A N   1 
ATOM   4704  C CA  . VAL A  1  651 ? 33.743  28.098  69.890  1.00 82.67  ?  651  VAL A CA  1 
ATOM   4705  C C   . VAL A  1  651 ? 34.475  28.589  68.651  1.00 82.79  ?  651  VAL A C   1 
ATOM   4706  O O   . VAL A  1  651 ? 35.601  29.091  68.733  1.00 84.28  ?  651  VAL A O   1 
ATOM   4707  C CB  . VAL A  1  651 ? 32.885  29.236  70.494  1.00 84.77  ?  651  VAL A CB  1 
ATOM   4708  C CG1 . VAL A  1  651 ? 31.732  29.588  69.575  1.00 84.14  ?  651  VAL A CG1 1 
ATOM   4709  C CG2 . VAL A  1  651 ? 32.371  28.858  71.861  1.00 85.21  ?  651  VAL A CG2 1 
ATOM   4710  N N   . ASP A  1  652 ? 33.834  28.439  67.493  1.00 76.42  ?  652  ASP A N   1 
ATOM   4711  C CA  . ASP A  1  652 ? 34.320  29.040  66.253  1.00 76.80  ?  652  ASP A CA  1 
ATOM   4712  C C   . ASP A  1  652 ? 33.109  29.485  65.443  1.00 76.46  ?  652  ASP A C   1 
ATOM   4713  O O   . ASP A  1  652 ? 32.333  28.646  64.976  1.00 74.33  ?  652  ASP A O   1 
ATOM   4714  C CB  . ASP A  1  652 ? 35.186  28.062  65.459  1.00 75.01  ?  652  ASP A CB  1 
ATOM   4715  C CG  . ASP A  1  652 ? 36.071  28.757  64.441  1.00 76.08  ?  652  ASP A CG  1 
ATOM   4716  O OD1 . ASP A  1  652 ? 35.711  29.867  63.993  1.00 77.59  ?  652  ASP A OD1 1 
ATOM   4717  O OD2 . ASP A  1  652 ? 37.129  28.195  64.091  1.00 75.53  -1 652  ASP A OD2 1 
ATOM   4718  N N   . VAL A  1  653 ? 32.945  30.797  65.282  1.00 73.87  ?  653  VAL A N   1 
ATOM   4719  C CA  . VAL A  1  653 ? 31.820  31.370  64.556  1.00 74.00  ?  653  VAL A CA  1 
ATOM   4720  C C   . VAL A  1  653 ? 32.303  32.180  63.349  1.00 75.04  ?  653  VAL A C   1 
ATOM   4721  O O   . VAL A  1  653 ? 31.552  32.958  62.771  1.00 75.92  ?  653  VAL A O   1 
ATOM   4722  C CB  . VAL A  1  653 ? 30.940  32.216  65.500  1.00 75.84  ?  653  VAL A CB  1 
ATOM   4723  C CG1 . VAL A  1  653 ? 29.589  32.521  64.887  1.00 75.58  ?  653  VAL A CG1 1 
ATOM   4724  C CG2 . VAL A  1  653 ? 30.755  31.518  66.831  1.00 75.39  ?  653  VAL A CG2 1 
ATOM   4725  N N   . SER A  1  654 ? 33.562  31.995  62.961  1.00 79.25  ?  654  SER A N   1 
ATOM   4726  C CA  . SER A  1  654 ? 34.162  32.815  61.919  1.00 80.64  ?  654  SER A CA  1 
ATOM   4727  C C   . SER A  1  654 ? 33.479  32.593  60.570  1.00 79.28  ?  654  SER A C   1 
ATOM   4728  O O   . SER A  1  654 ? 32.825  31.575  60.331  1.00 76.88  ?  654  SER A O   1 
ATOM   4729  C CB  . SER A  1  654 ? 35.655  32.512  61.798  1.00 80.83  ?  654  SER A CB  1 
ATOM   4730  O OG  . SER A  1  654 ? 35.876  31.160  61.433  1.00 78.21  ?  654  SER A OG  1 
ATOM   4731  N N   . HIS A  1  655 ? 33.646  33.575  59.681  1.00 83.15  ?  655  HIS A N   1 
ATOM   4732  C CA  . HIS A  1  655 ? 33.167  33.502  58.300  1.00 82.32  ?  655  HIS A CA  1 
ATOM   4733  C C   . HIS A  1  655 ? 31.655  33.263  58.241  1.00 81.08  ?  655  HIS A C   1 
ATOM   4734  O O   . HIS A  1  655 ? 31.175  32.244  57.739  1.00 78.67  ?  655  HIS A O   1 
ATOM   4735  C CB  . HIS A  1  655 ? 33.932  32.431  57.515  1.00 80.37  ?  655  HIS A CB  1 
ATOM   4736  C CG  . HIS A  1  655 ? 35.398  32.706  57.393  1.00 81.75  ?  655  HIS A CG  1 
ATOM   4737  N ND1 . HIS A  1  655 ? 36.262  32.621  58.463  1.00 82.40  ?  655  HIS A ND1 1 
ATOM   4738  C CD2 . HIS A  1  655 ? 36.153  33.066  56.328  1.00 82.75  ?  655  HIS A CD2 1 
ATOM   4739  C CE1 . HIS A  1  655 ? 37.486  32.917  58.063  1.00 83.71  ?  655  HIS A CE1 1 
ATOM   4740  N NE2 . HIS A  1  655 ? 37.447  33.190  56.772  1.00 83.97  ?  655  HIS A NE2 1 
ATOM   4741  N N   . ASN A  1  656 ? 30.908  34.226  58.774  1.00 81.49  ?  656  ASN A N   1 
ATOM   4742  C CA  . ASN A  1  656 ? 29.455  34.131  58.840  1.00 80.74  ?  656  ASN A CA  1 
ATOM   4743  C C   . ASN A  1  656 ? 28.868  35.523  58.627  1.00 83.36  ?  656  ASN A C   1 
ATOM   4744  O O   . ASN A  1  656 ? 29.565  36.458  58.220  1.00 85.47  ?  656  ASN A O   1 
ATOM   4745  C CB  . ASN A  1  656 ? 29.018  33.507  60.171  1.00 79.82  ?  656  ASN A CB  1 
ATOM   4746  C CG  . ASN A  1  656 ? 28.678  32.039  60.038  1.00 76.75  ?  656  ASN A CG  1 
ATOM   4747  O OD1 . ASN A  1  656 ? 27.589  31.681  59.591  1.00 75.54  ?  656  ASN A OD1 1 
ATOM   4748  N ND2 . ASN A  1  656 ? 29.609  31.178  60.430  1.00 75.57  ?  656  ASN A ND2 1 
ATOM   4749  N N   . ASN A  1  657 ? 27.570  35.660  58.893  1.00 86.27  ?  657  ASN A N   1 
ATOM   4750  C CA  . ASN A  1  657 ? 26.828  36.893  58.646  1.00 88.62  ?  657  ASN A CA  1 
ATOM   4751  C C   . ASN A  1  657 ? 26.063  37.320  59.892  1.00 89.80  ?  657  ASN A C   1 
ATOM   4752  O O   . ASN A  1  657 ? 24.925  37.792  59.819  1.00 90.59  ?  657  ASN A O   1 
ATOM   4753  C CB  . ASN A  1  657 ? 25.879  36.728  57.460  1.00 87.69  ?  657  ASN A CB  1 
ATOM   4754  C CG  . ASN A  1  657 ? 25.456  38.056  56.858  1.00 90.36  ?  657  ASN A CG  1 
ATOM   4755  O OD1 . ASN A  1  657 ? 26.292  38.857  56.442  1.00 92.26  ?  657  ASN A OD1 1 
ATOM   4756  N ND2 . ASN A  1  657 ? 24.149  38.293  56.807  1.00 90.63  ?  657  ASN A ND2 1 
ATOM   4757  N N   . LEU A  1  658 ? 26.679  37.158  61.058  1.00 90.11  ?  658  LEU A N   1 
ATOM   4758  C CA  . LEU A  1  658 ? 26.058  37.498  62.328  1.00 91.29  ?  658  LEU A CA  1 
ATOM   4759  C C   . LEU A  1  658 ? 26.495  38.883  62.798  1.00 94.60  ?  658  LEU A C   1 
ATOM   4760  O O   . LEU A  1  658 ? 27.397  39.509  62.236  1.00 95.91  ?  658  LEU A O   1 
ATOM   4761  C CB  . LEU A  1  658 ? 26.391  36.436  63.378  1.00 89.65  ?  658  LEU A CB  1 
ATOM   4762  C CG  . LEU A  1  658 ? 25.891  35.037  63.012  1.00 86.48  ?  658  LEU A CG  1 
ATOM   4763  C CD1 . LEU A  1  658 ? 26.993  34.024  63.172  1.00 84.75  ?  658  LEU A CD1 1 
ATOM   4764  C CD2 . LEU A  1  658 ? 24.698  34.648  63.868  1.00 86.02  ?  658  LEU A CD2 1 
ATOM   4765  N N   . GLN A  1  659 ? 25.832  39.359  63.851  1.00 93.94  ?  659  GLN A N   1 
ATOM   4766  C CA  . GLN A  1  659 ? 26.063  40.699  64.368  1.00 97.22  ?  659  GLN A CA  1 
ATOM   4767  C C   . GLN A  1  659 ? 25.723  40.733  65.851  1.00 98.10  ?  659  GLN A C   1 
ATOM   4768  O O   . GLN A  1  659 ? 25.078  39.826  66.382  1.00 96.37  ?  659  GLN A O   1 
ATOM   4769  C CB  . GLN A  1  659 ? 25.238  41.740  63.603  1.00 99.06  ?  659  GLN A CB  1 
ATOM   4770  C CG  . GLN A  1  659 ? 23.736  41.609  63.790  1.00 98.70  ?  659  GLN A CG  1 
ATOM   4771  C CD  . GLN A  1  659 ? 22.951  42.402  62.764  1.00 99.96  ?  659  GLN A CD  1 
ATOM   4772  O OE1 . GLN A  1  659 ? 23.524  42.982  61.840  1.00 100.95 ?  659  GLN A OE1 1 
ATOM   4773  N NE2 . GLN A  1  659 ? 21.633  42.433  62.920  1.00 100.08 ?  659  GLN A NE2 1 
ATOM   4774  N N   . GLY A  1  660 ? 26.175  41.792  66.518  1.00 101.56 ?  660  GLY A N   1 
ATOM   4775  C CA  . GLY A  1  660 ? 25.833  42.025  67.901  1.00 102.95 ?  660  GLY A CA  1 
ATOM   4776  C C   . GLY A  1  660 ? 26.932  41.625  68.863  1.00 102.88 ?  660  GLY A C   1 
ATOM   4777  O O   . GLY A  1  660 ? 27.873  40.907  68.508  1.00 101.21 ?  660  GLY A O   1 
ATOM   4778  N N   . PRO A  1  661 ? 26.832  42.085  70.110  1.00 103.07 ?  661  PRO A N   1 
ATOM   4779  C CA  . PRO A  1  661 ? 27.834  41.706  71.114  1.00 103.19 ?  661  PRO A CA  1 
ATOM   4780  C C   . PRO A  1  661 ? 27.661  40.256  71.538  1.00 100.39 ?  661  PRO A C   1 
ATOM   4781  O O   . PRO A  1  661 ? 26.542  39.773  71.725  1.00 99.37  ?  661  PRO A O   1 
ATOM   4782  C CB  . PRO A  1  661 ? 27.551  42.667  72.274  1.00 106.24 ?  661  PRO A CB  1 
ATOM   4783  C CG  . PRO A  1  661 ? 26.106  43.004  72.127  1.00 106.69 ?  661  PRO A CG  1 
ATOM   4784  C CD  . PRO A  1  661 ? 25.841  43.033  70.646  1.00 105.50 ?  661  PRO A CD  1 
ATOM   4785  N N   . ILE A  1  662 ? 28.786  39.564  71.687  1.00 101.17 ?  662  ILE A N   1 
ATOM   4786  C CA  . ILE A  1  662 ? 28.776  38.146  72.035  1.00 98.54  ?  662  ILE A CA  1 
ATOM   4787  C C   . ILE A  1  662 ? 28.378  37.990  73.498  1.00 99.51  ?  662  ILE A C   1 
ATOM   4788  O O   . ILE A  1  662 ? 28.721  38.845  74.326  1.00 102.12 ?  662  ILE A O   1 
ATOM   4789  C CB  . ILE A  1  662 ? 30.143  37.497  71.763  1.00 97.30  ?  662  ILE A CB  1 
ATOM   4790  C CG1 . ILE A  1  662 ? 31.242  38.205  72.558  1.00 99.74  ?  662  ILE A CG1 1 
ATOM   4791  C CG2 . ILE A  1  662 ? 30.461  37.530  70.277  1.00 96.20  ?  662  ILE A CG2 1 
ATOM   4792  C CD1 . ILE A  1  662 ? 32.609  37.553  72.426  1.00 98.75  ?  662  ILE A CD1 1 
ATOM   4793  N N   . PRO A  1  663 ? 27.643  36.940  73.858  1.00 103.16 ?  663  PRO A N   1 
ATOM   4794  C CA  . PRO A  1  663 ? 27.424  36.648  75.278  1.00 104.10 ?  663  PRO A CA  1 
ATOM   4795  C C   . PRO A  1  663 ? 28.731  36.277  75.958  1.00 104.32 ?  663  PRO A C   1 
ATOM   4796  O O   . PRO A  1  663 ? 29.674  35.792  75.326  1.00 102.81 ?  663  PRO A O   1 
ATOM   4797  C CB  . PRO A  1  663 ? 26.448  35.464  75.254  1.00 101.64 ?  663  PRO A CB  1 
ATOM   4798  C CG  . PRO A  1  663 ? 26.518  34.931  73.845  1.00 99.37  ?  663  PRO A CG  1 
ATOM   4799  C CD  . PRO A  1  663 ? 26.775  36.125  72.995  1.00 100.68 ?  663  PRO A CD  1 
ATOM   4800  N N   . ASP A  1  664 ? 28.779  36.507  77.267  1.00 102.82 ?  664  ASP A N   1 
ATOM   4801  C CA  . ASP A  1  664 ? 30.003  36.350  78.045  1.00 103.64 ?  664  ASP A CA  1 
ATOM   4802  C C   . ASP A  1  664 ? 29.984  35.000  78.755  1.00 101.98 ?  664  ASP A C   1 
ATOM   4803  O O   . ASP A  1  664 ? 29.230  34.805  79.713  1.00 102.70 ?  664  ASP A O   1 
ATOM   4804  C CB  . ASP A  1  664 ? 30.149  37.495  79.046  1.00 107.06 ?  664  ASP A CB  1 
ATOM   4805  C CG  . ASP A  1  664 ? 31.180  37.206  80.122  1.00 108.04 ?  664  ASP A CG  1 
ATOM   4806  O OD1 . ASP A  1  664 ? 32.249  36.650  79.795  1.00 106.85 ?  664  ASP A OD1 1 
ATOM   4807  O OD2 . ASP A  1  664 ? 30.920  37.537  81.298  1.00 110.12 -1 664  ASP A OD2 1 
ATOM   4808  N N   . ASN A  1  665 ? 30.827  34.078  78.292  1.00 104.64 ?  665  ASN A N   1 
ATOM   4809  C CA  . ASN A  1  665 ? 31.076  32.823  78.986  1.00 103.34 ?  665  ASN A CA  1 
ATOM   4810  C C   . ASN A  1  665 ? 32.561  32.501  78.869  1.00 103.02 ?  665  ASN A C   1 
ATOM   4811  O O   . ASN A  1  665 ? 33.324  33.224  78.220  1.00 103.74 ?  665  ASN A O   1 
ATOM   4812  C CB  . ASN A  1  665 ? 30.191  31.688  78.446  1.00 100.50 ?  665  ASN A CB  1 
ATOM   4813  C CG  . ASN A  1  665 ? 30.355  31.460  76.950  1.00 98.32  ?  665  ASN A CG  1 
ATOM   4814  O OD1 . ASN A  1  665 ? 31.457  31.529  76.408  1.00 98.08  ?  665  ASN A OD1 1 
ATOM   4815  N ND2 . ASN A  1  665 ? 29.246  31.171  76.278  1.00 96.80  ?  665  ASN A ND2 1 
ATOM   4816  N N   . ALA A  1  666 ? 32.973  31.405  79.511  1.00 101.84 ?  666  ALA A N   1 
ATOM   4817  C CA  . ALA A  1  666 ? 34.385  31.033  79.512  1.00 101.69 ?  666  ALA A CA  1 
ATOM   4818  C C   . ALA A  1  666 ? 34.905  30.760  78.107  1.00 99.70  ?  666  ALA A C   1 
ATOM   4819  O O   . ALA A  1  666 ? 36.074  31.034  77.815  1.00 100.31 ?  666  ALA A O   1 
ATOM   4820  C CB  . ALA A  1  666 ? 34.604  29.811  80.404  1.00 100.93 ?  666  ALA A CB  1 
ATOM   4821  N N   . ALA A  1  667 ? 34.058  30.224  77.225  1.00 97.91  ?  667  ALA A N   1 
ATOM   4822  C CA  . ALA A  1  667 ? 34.521  29.851  75.892  1.00 95.93  ?  667  ALA A CA  1 
ATOM   4823  C C   . ALA A  1  667 ? 34.768  31.076  75.018  1.00 97.16  ?  667  ALA A C   1 
ATOM   4824  O O   . ALA A  1  667 ? 35.771  31.137  74.298  1.00 96.97  ?  667  ALA A O   1 
ATOM   4825  C CB  . ALA A  1  667 ? 33.510  28.915  75.235  1.00 93.25  ?  667  ALA A CB  1 
ATOM   4826  N N   . PHE A  1  668 ? 33.865  32.058  75.063  1.00 99.63  ?  668  PHE A N   1 
ATOM   4827  C CA  . PHE A  1  668 ? 34.009  33.235  74.211  1.00 100.84 ?  668  PHE A CA  1 
ATOM   4828  C C   . PHE A  1  668 ? 35.190  34.102  74.631  1.00 103.34 ?  668  PHE A C   1 
ATOM   4829  O O   . PHE A  1  668 ? 35.822  34.737  73.780  1.00 103.98 ?  668  PHE A O   1 
ATOM   4830  C CB  . PHE A  1  668 ? 32.718  34.055  74.222  1.00 102.24 ?  668  PHE A CB  1 
ATOM   4831  C CG  . PHE A  1  668 ? 31.652  33.518  73.309  1.00 100.09 ?  668  PHE A CG  1 
ATOM   4832  C CD1 . PHE A  1  668 ? 31.840  33.503  71.936  1.00 98.73  ?  668  PHE A CD1 1 
ATOM   4833  C CD2 . PHE A  1  668 ? 30.461  33.031  73.822  1.00 99.24  ?  668  PHE A CD2 1 
ATOM   4834  C CE1 . PHE A  1  668 ? 30.861  33.010  71.093  1.00 96.55  ?  668  PHE A CE1 1 
ATOM   4835  C CE2 . PHE A  1  668 ? 29.478  32.537  72.985  1.00 96.96  ?  668  PHE A CE2 1 
ATOM   4836  C CZ  . PHE A  1  668 ? 29.679  32.526  71.619  1.00 95.84  ?  668  PHE A CZ  1 
ATOM   4837  N N   . ARG A  1  669 ? 35.496  34.148  75.930  1.00 98.20  ?  669  ARG A N   1 
ATOM   4838  C CA  . ARG A  1  669 ? 36.580  34.998  76.413  1.00 100.78 ?  669  ARG A CA  1 
ATOM   4839  C C   . ARG A  1  669 ? 37.928  34.541  75.866  1.00 100.06 ?  669  ARG A C   1 
ATOM   4840  O O   . ARG A  1  669 ? 38.681  35.337  75.293  1.00 101.38 ?  669  ARG A O   1 
ATOM   4841  C CB  . ARG A  1  669 ? 36.592  35.005  77.942  1.00 102.47 ?  669  ARG A CB  1 
ATOM   4842  C CG  . ARG A  1  669 ? 35.415  35.734  78.565  1.00 104.02 ?  669  ARG A CG  1 
ATOM   4843  C CD  . ARG A  1  669 ? 35.626  35.951  80.053  1.00 106.28 ?  669  ARG A CD  1 
ATOM   4844  N NE  . ARG A  1  669 ? 34.497  35.465  80.836  1.00 105.94 ?  669  ARG A NE  1 
ATOM   4845  C CZ  . ARG A  1  669 ? 34.588  34.558  81.799  1.00 105.60 ?  669  ARG A CZ  1 
ATOM   4846  N NH1 . ARG A  1  669 ? 35.749  34.015  82.128  1.00 105.51 ?  669  ARG A NH1 1 
ATOM   4847  N NH2 . ARG A  1  669 ? 33.488  34.186  82.446  1.00 105.46 ?  669  ARG A NH2 1 
ATOM   4848  N N   . ASN A  1  670 ? 38.247  33.259  76.031  1.00 101.94 ?  670  ASN A N   1 
ATOM   4849  C CA  . ASN A  1  670 ? 39.524  32.719  75.581  1.00 101.26 ?  670  ASN A CA  1 
ATOM   4850  C C   . ASN A  1  670 ? 39.564  32.446  74.083  1.00 99.32  ?  670  ASN A C   1 
ATOM   4851  O O   . ASN A  1  670 ? 40.556  31.890  73.599  1.00 98.68  ?  670  ASN A O   1 
ATOM   4852  C CB  . ASN A  1  670 ? 39.848  31.433  76.346  1.00 100.02 ?  670  ASN A CB  1 
ATOM   4853  C CG  . ASN A  1  670 ? 39.640  31.577  77.839  1.00 101.78 ?  670  ASN A CG  1 
ATOM   4854  O OD1 . ASN A  1  670 ? 38.600  32.056  78.289  1.00 102.52 ?  670  ASN A OD1 1 
ATOM   4855  N ND2 . ASN A  1  670 ? 40.630  31.157  78.617  1.00 102.58 ?  670  ASN A ND2 1 
ATOM   4856  N N   . ALA A  1  671 ? 38.521  32.806  73.349  1.00 95.07  ?  671  ALA A N   1 
ATOM   4857  C CA  . ALA A  1  671 ? 38.510  32.589  71.909  1.00 93.38  ?  671  ALA A CA  1 
ATOM   4858  C C   . ALA A  1  671 ? 39.553  33.475  71.235  1.00 95.10  ?  671  ALA A C   1 
ATOM   4859  O O   . ALA A  1  671 ? 39.612  34.679  71.513  1.00 97.63  ?  671  ALA A O   1 
ATOM   4860  C CB  . ALA A  1  671 ? 37.124  32.871  71.337  1.00 92.60  ?  671  ALA A CB  1 
ATOM   4861  N N   . PRO A  1  672 ? 40.388  32.926  70.358  1.00 95.69  ?  672  PRO A N   1 
ATOM   4862  C CA  . PRO A  1  672 ? 41.380  33.745  69.653  1.00 97.41  ?  672  PRO A CA  1 
ATOM   4863  C C   . PRO A  1  672 ? 40.713  34.607  68.596  1.00 97.84  ?  672  PRO A C   1 
ATOM   4864  O O   . PRO A  1  672 ? 39.514  34.443  68.321  1.00 96.49  ?  672  PRO A O   1 
ATOM   4865  C CB  . PRO A  1  672 ? 42.322  32.706  69.022  1.00 95.75  ?  672  PRO A CB  1 
ATOM   4866  C CG  . PRO A  1  672 ? 41.589  31.408  69.044  1.00 92.82  ?  672  PRO A CG  1 
ATOM   4867  C CD  . PRO A  1  672 ? 40.359  31.531  69.889  1.00 92.77  ?  672  PRO A CD  1 
ATOM   4868  N N   . PRO A  1  673 ? 41.446  35.544  67.986  1.00 98.32  ?  673  PRO A N   1 
ATOM   4869  C CA  . PRO A  1  673 ? 40.833  36.386  66.943  1.00 98.92  ?  673  PRO A CA  1 
ATOM   4870  C C   . PRO A  1  673 ? 40.317  35.605  65.747  1.00 96.31  ?  673  PRO A C   1 
ATOM   4871  O O   . PRO A  1  673 ? 39.465  36.121  65.014  1.00 96.36  ?  673  PRO A O   1 
ATOM   4872  C CB  . PRO A  1  673 ? 41.973  37.331  66.542  1.00 101.51 ?  673  PRO A CB  1 
ATOM   4873  C CG  . PRO A  1  673 ? 42.840  37.398  67.748  1.00 103.01 ?  673  PRO A CG  1 
ATOM   4874  C CD  . PRO A  1  673 ? 42.791  36.024  68.353  1.00 100.56 ?  673  PRO A CD  1 
ATOM   4875  N N   . ASP A  1  674 ? 40.804  34.382  65.521  1.00 99.47  ?  674  ASP A N   1 
ATOM   4876  C CA  . ASP A  1  674 ? 40.310  33.578  64.410  1.00 97.09  ?  674  ASP A CA  1 
ATOM   4877  C C   . ASP A  1  674 ? 38.871  33.124  64.614  1.00 95.51  ?  674  ASP A C   1 
ATOM   4878  O O   . ASP A  1  674 ? 38.178  32.849  63.630  1.00 93.97  ?  674  ASP A O   1 
ATOM   4879  C CB  . ASP A  1  674 ? 41.206  32.356  64.199  1.00 95.18  ?  674  ASP A CB  1 
ATOM   4880  C CG  . ASP A  1  674 ? 42.680  32.705  64.206  1.00 97.26  ?  674  ASP A CG  1 
ATOM   4881  O OD1 . ASP A  1  674 ? 43.051  33.741  63.617  1.00 100.10 ?  674  ASP A OD1 1 
ATOM   4882  O OD2 . ASP A  1  674 ? 43.469  31.940  64.800  1.00 96.92  -1 674  ASP A OD2 1 
ATOM   4883  N N   . ALA A  1  675 ? 38.408  33.036  65.861  1.00 89.37  ?  675  ALA A N   1 
ATOM   4884  C CA  . ALA A  1  675 ? 37.071  32.535  66.157  1.00 87.75  ?  675  ALA A CA  1 
ATOM   4885  C C   . ALA A  1  675 ? 35.962  33.533  65.845  1.00 88.82  ?  675  ALA A C   1 
ATOM   4886  O O   . ALA A  1  675 ? 34.794  33.231  66.112  1.00 87.78  ?  675  ALA A O   1 
ATOM   4887  C CB  . ALA A  1  675 ? 36.984  32.119  67.628  1.00 87.88  ?  675  ALA A CB  1 
ATOM   4888  N N   . PHE A  1  676 ? 36.285  34.711  65.300  1.00 83.52  ?  676  PHE A N   1 
ATOM   4889  C CA  . PHE A  1  676 ? 35.256  35.683  64.952  1.00 84.71  ?  676  PHE A CA  1 
ATOM   4890  C C   . PHE A  1  676 ? 35.499  36.344  63.600  1.00 85.51  ?  676  PHE A C   1 
ATOM   4891  O O   . PHE A  1  676 ? 34.849  37.354  63.298  1.00 87.13  ?  676  PHE A O   1 
ATOM   4892  C CB  . PHE A  1  676 ? 35.143  36.760  66.037  1.00 87.45  ?  676  PHE A CB  1 
ATOM   4893  C CG  . PHE A  1  676 ? 34.943  36.209  67.418  1.00 87.07  ?  676  PHE A CG  1 
ATOM   4894  C CD1 . PHE A  1  676 ? 33.676  35.885  67.874  1.00 86.13  ?  676  PHE A CD1 1 
ATOM   4895  C CD2 . PHE A  1  676 ? 36.023  36.014  68.262  1.00 87.80  ?  676  PHE A CD2 1 
ATOM   4896  C CE1 . PHE A  1  676 ? 33.491  35.376  69.144  1.00 85.95  ?  676  PHE A CE1 1 
ATOM   4897  C CE2 . PHE A  1  676 ? 35.844  35.508  69.531  1.00 87.61  ?  676  PHE A CE2 1 
ATOM   4898  C CZ  . PHE A  1  676 ? 34.577  35.188  69.974  1.00 86.70  ?  676  PHE A CZ  1 
ATOM   4899  N N   . GLU A  1  677 ? 36.408  35.816  62.786  1.00 89.19  ?  677  GLU A N   1 
ATOM   4900  C CA  . GLU A  1  677 ? 36.751  36.442  61.518  1.00 90.20  ?  677  GLU A CA  1 
ATOM   4901  C C   . GLU A  1  677 ? 35.571  36.423  60.550  1.00 89.11  ?  677  GLU A C   1 
ATOM   4902  O O   . GLU A  1  677 ? 34.683  35.571  60.629  1.00 86.84  ?  677  GLU A O   1 
ATOM   4903  C CB  . GLU A  1  677 ? 37.947  35.728  60.890  1.00 89.29  ?  677  GLU A CB  1 
ATOM   4904  C CG  . GLU A  1  677 ? 39.297  36.238  61.363  1.00 91.47  ?  677  GLU A CG  1 
ATOM   4905  C CD  . GLU A  1  677 ? 40.360  36.155  60.286  1.00 91.78  ?  677  GLU A CD  1 
ATOM   4906  O OE1 . GLU A  1  677 ? 40.396  35.134  59.566  1.00 89.50  ?  677  GLU A OE1 1 
ATOM   4907  O OE2 . GLU A  1  677 ? 41.159  37.106  60.160  1.00 94.41  -1 677  GLU A OE2 1 
ATOM   4908  N N   . GLY A  1  678 ? 35.572  37.381  59.628  1.00 90.45  ?  678  GLY A N   1 
ATOM   4909  C CA  . GLY A  1  678 ? 34.630  37.377  58.518  1.00 89.61  ?  678  GLY A CA  1 
ATOM   4910  C C   . GLY A  1  678 ? 33.165  37.393  58.897  1.00 88.94  ?  678  GLY A C   1 
ATOM   4911  O O   . GLY A  1  678 ? 32.367  36.660  58.300  1.00 86.81  ?  678  GLY A O   1 
ATOM   4912  N N   . ASN A  1  679 ? 32.789  38.206  59.878  1.00 90.42  ?  679  ASN A N   1 
ATOM   4913  C CA  . ASN A  1  679 ? 31.390  38.434  60.210  1.00 90.39  ?  679  ASN A CA  1 
ATOM   4914  C C   . ASN A  1  679 ? 30.999  39.851  59.799  1.00 93.25  ?  679  ASN A C   1 
ATOM   4915  O O   . ASN A  1  679 ? 31.807  40.609  59.255  1.00 95.17  ?  679  ASN A O   1 
ATOM   4916  C CB  . ASN A  1  679 ? 31.142  38.183  61.697  1.00 90.28  ?  679  ASN A CB  1 
ATOM   4917  C CG  . ASN A  1  679 ? 30.652  36.775  61.973  1.00 87.20  ?  679  ASN A CG  1 
ATOM   4918  O OD1 . ASN A  1  679 ? 29.476  36.465  61.781  1.00 86.04  ?  679  ASN A OD1 1 
ATOM   4919  N ND2 . ASN A  1  679 ? 31.557  35.909  62.416  1.00 85.94  ?  679  ASN A ND2 1 
ATOM   4920  N N   . LYS A  1  680 ? 29.739  40.211  60.051  1.00 96.33  ?  680  LYS A N   1 
ATOM   4921  C CA  . LYS A  1  680 ? 29.257  41.503  59.570  1.00 98.99  ?  680  LYS A CA  1 
ATOM   4922  C C   . LYS A  1  680 ? 29.376  42.617  60.610  1.00 101.94 ?  680  LYS A C   1 
ATOM   4923  O O   . LYS A  1  680 ? 30.071  43.612  60.381  1.00 104.48 ?  680  LYS A O   1 
ATOM   4924  C CB  . LYS A  1  680 ? 27.799  41.368  59.113  1.00 98.09  ?  680  LYS A CB  1 
ATOM   4925  C CG  . LYS A  1  680 ? 27.526  41.900  57.717  1.00 98.93  ?  680  LYS A CG  1 
ATOM   4926  C CD  . LYS A  1  680 ? 26.047  42.195  57.530  1.00 99.21  ?  680  LYS A CD  1 
ATOM   4927  C CE  . LYS A  1  680 ? 25.720  42.500  56.078  1.00 99.61  ?  680  LYS A CE  1 
ATOM   4928  N NZ  . LYS A  1  680 ? 24.254  42.630  55.856  1.00 99.60  ?  680  LYS A NZ  1 
ATOM   4929  N N   . ASP A  1  681 ? 28.708  42.468  61.754  1.00 100.10 ?  681  ASP A N   1 
ATOM   4930  C CA  . ASP A  1  681 ? 28.636  43.554  62.731  1.00 103.01 ?  681  ASP A CA  1 
ATOM   4931  C C   . ASP A  1  681 ? 28.802  43.041  64.158  1.00 102.48 ?  681  ASP A C   1 
ATOM   4932  O O   . ASP A  1  681 ? 28.066  43.444  65.063  1.00 103.68 ?  681  ASP A O   1 
ATOM   4933  C CB  . ASP A  1  681 ? 27.332  44.337  62.585  1.00 104.48 ?  681  ASP A CB  1 
ATOM   4934  C CG  . ASP A  1  681 ? 27.518  45.823  62.817  1.00 108.22 ?  681  ASP A CG  1 
ATOM   4935  O OD1 . ASP A  1  681 ? 28.448  46.405  62.220  1.00 109.67 ?  681  ASP A OD1 1 
ATOM   4936  O OD2 . ASP A  1  681 ? 26.737  46.410  63.596  1.00 109.82 -1 681  ASP A OD2 1 
ATOM   4937  N N   . LEU A  1  682 ? 29.757  42.145  64.390  1.00 100.48 ?  682  LEU A N   1 
ATOM   4938  C CA  . LEU A  1  682 ? 29.927  41.581  65.728  1.00 99.95  ?  682  LEU A CA  1 
ATOM   4939  C C   . LEU A  1  682 ? 30.571  42.612  66.648  1.00 103.01 ?  682  LEU A C   1 
ATOM   4940  O O   . LEU A  1  682 ? 31.735  42.981  66.466  1.00 104.15 ?  682  LEU A O   1 
ATOM   4941  C CB  . LEU A  1  682 ? 30.765  40.308  65.676  1.00 97.36  ?  682  LEU A CB  1 
ATOM   4942  C CG  . LEU A  1  682 ? 30.055  39.025  65.244  1.00 94.09  ?  682  LEU A CG  1 
ATOM   4943  C CD1 . LEU A  1  682 ? 31.015  37.847  65.291  1.00 91.93  ?  682  LEU A CD1 1 
ATOM   4944  C CD2 . LEU A  1  682 ? 28.840  38.763  66.121  1.00 93.69  ?  682  LEU A CD2 1 
ATOM   4945  N N   . CYS A  1  683 ? 29.814  43.073  67.641  1.00 103.99 ?  683  CYS A N   1 
ATOM   4946  C CA  . CYS A  1  683 ? 30.318  44.025  68.623  1.00 106.94 ?  683  CYS A CA  1 
ATOM   4947  C C   . CYS A  1  683 ? 31.268  43.349  69.605  1.00 106.35 ?  683  CYS A C   1 
ATOM   4948  O O   . CYS A  1  683 ? 32.487  43.403  69.441  1.00 106.79 ?  683  CYS A O   1 
ATOM   4949  C CB  . CYS A  1  683 ? 29.158  44.677  69.378  1.00 108.65 ?  683  CYS A CB  1 
ATOM   4950  S SG  . CYS A  1  683 ? 29.649  45.623  70.841  1.00 112.03 ?  683  CYS A SG  1 
ATOM   4951  N N   . ASN B  2  26  ? 45.977  -6.114  79.310  1.00 47.49  ?  26   ASN B N   1 
ATOM   4952  C CA  . ASN B  2  26  ? 46.962  -5.493  80.187  1.00 49.72  ?  26   ASN B CA  1 
ATOM   4953  C C   . ASN B  2  26  ? 46.330  -5.056  81.505  1.00 50.22  ?  26   ASN B C   1 
ATOM   4954  O O   . ASN B  2  26  ? 45.258  -5.535  81.876  1.00 49.07  ?  26   ASN B O   1 
ATOM   4955  C CB  . ASN B  2  26  ? 47.622  -4.300  79.492  1.00 51.29  ?  26   ASN B CB  1 
ATOM   4956  C CG  . ASN B  2  26  ? 46.629  -3.211  79.136  1.00 50.82  ?  26   ASN B CG  1 
ATOM   4957  O OD1 . ASN B  2  26  ? 45.421  -3.444  79.096  1.00 49.02  ?  26   ASN B OD1 1 
ATOM   4958  N ND2 . ASN B  2  26  ? 47.136  -2.012  78.872  1.00 52.87  ?  26   ASN B ND2 1 
ATOM   4959  N N   . ALA B  2  27  ? 47.005  -4.142  82.206  1.00 47.36  ?  27   ALA B N   1 
ATOM   4960  C CA  . ALA B  2  27  ? 46.508  -3.676  83.498  1.00 48.38  ?  27   ALA B CA  1 
ATOM   4961  C C   . ALA B  2  27  ? 45.144  -3.012  83.357  1.00 47.45  ?  27   ALA B C   1 
ATOM   4962  O O   . ALA B  2  27  ? 44.201  -3.342  84.087  1.00 47.21  ?  27   ALA B O   1 
ATOM   4963  C CB  . ALA B  2  27  ? 47.515  -2.714  84.129  1.00 51.13  ?  27   ALA B CB  1 
ATOM   4964  N N   . GLU B  2  28  ? 45.023  -2.067  82.422  1.00 52.99  ?  28   GLU B N   1 
ATOM   4965  C CA  . GLU B  2  28  ? 43.751  -1.381  82.219  1.00 52.51  ?  28   GLU B CA  1 
ATOM   4966  C C   . GLU B  2  28  ? 42.664  -2.349  81.764  1.00 50.28  ?  28   GLU B C   1 
ATOM   4967  O O   . GLU B  2  28  ? 41.507  -2.238  82.189  1.00 50.28  ?  28   GLU B O   1 
ATOM   4968  C CB  . GLU B  2  28  ? 43.926  -0.248  81.207  1.00 53.28  ?  28   GLU B CB  1 
ATOM   4969  C CG  . GLU B  2  28  ? 44.786  0.900   81.714  1.00 56.11  ?  28   GLU B CG  1 
ATOM   4970  C CD  . GLU B  2  28  ? 44.965  1.997   80.684  1.00 57.46  ?  28   GLU B CD  1 
ATOM   4971  O OE1 . GLU B  2  28  ? 44.143  2.077   79.748  1.00 56.29  ?  28   GLU B OE1 1 
ATOM   4972  O OE2 . GLU B  2  28  ? 45.929  2.782   80.811  1.00 60.06  -1 28   GLU B OE2 1 
ATOM   4973  N N   . GLY B  2  29  ? 43.016  -3.304  80.901  1.00 50.86  ?  29   GLY B N   1 
ATOM   4974  C CA  . GLY B  2  29  ? 42.027  -4.259  80.427  1.00 49.02  ?  29   GLY B CA  1 
ATOM   4975  C C   . GLY B  2  29  ? 41.554  -5.207  81.513  1.00 49.16  ?  29   GLY B C   1 
ATOM   4976  O O   . GLY B  2  29  ? 40.369  -5.547  81.577  1.00 48.73  ?  29   GLY B O   1 
ATOM   4977  N N   . ASP B  2  30  ? 42.470  -5.653  82.377  1.00 47.55  ?  30   ASP B N   1 
ATOM   4978  C CA  . ASP B  2  30  ? 42.065  -6.479  83.511  1.00 48.41  ?  30   ASP B CA  1 
ATOM   4979  C C   . ASP B  2  30  ? 41.186  -5.693  84.475  1.00 49.94  ?  30   ASP B C   1 
ATOM   4980  O O   . ASP B  2  30  ? 40.243  -6.243  85.057  1.00 50.59  ?  30   ASP B O   1 
ATOM   4981  C CB  . ASP B  2  30  ? 43.294  -7.030  84.236  1.00 49.71  ?  30   ASP B CB  1 
ATOM   4982  C CG  . ASP B  2  30  ? 44.056  -8.046  83.407  1.00 48.73  ?  30   ASP B CG  1 
ATOM   4983  O OD1 . ASP B  2  30  ? 43.411  -8.928  82.802  1.00 47.41  ?  30   ASP B OD1 1 
ATOM   4984  O OD2 . ASP B  2  30  ? 45.302  -7.968  83.367  1.00 49.63  -1 30   ASP B OD2 1 
ATOM   4985  N N   . ALA B  2  31  ? 41.488  -4.406  84.668  1.00 48.96  ?  31   ALA B N   1 
ATOM   4986  C CA  . ALA B  2  31  ? 40.667  -3.566  85.536  1.00 50.77  ?  31   ALA B CA  1 
ATOM   4987  C C   . ALA B  2  31  ? 39.238  -3.465  85.014  1.00 50.13  ?  31   ALA B C   1 
ATOM   4988  O O   . ALA B  2  31  ? 38.274  -3.640  85.769  1.00 51.55  ?  31   ALA B O   1 
ATOM   4989  C CB  . ALA B  2  31  ? 41.295  -2.178  85.667  1.00 52.15  ?  31   ALA B CB  1 
ATOM   4990  N N   . LEU B  2  32  ? 39.083  -3.169  83.720  1.00 50.75  ?  32   LEU B N   1 
ATOM   4991  C CA  . LEU B  2  32  ? 37.750  -3.117  83.128  1.00 50.29  ?  32   LEU B CA  1 
ATOM   4992  C C   . LEU B  2  32  ? 37.081  -4.485  83.130  1.00 49.59  ?  32   LEU B C   1 
ATOM   4993  O O   . LEU B  2  32  ? 35.848  -4.569  83.186  1.00 50.35  ?  32   LEU B O   1 
ATOM   4994  C CB  . LEU B  2  32  ? 37.829  -2.561  81.706  1.00 48.93  ?  32   LEU B CB  1 
ATOM   4995  C CG  . LEU B  2  32  ? 37.949  -1.039  81.601  1.00 50.39  ?  32   LEU B CG  1 
ATOM   4996  C CD1 . LEU B  2  32  ? 38.395  -0.625  80.207  1.00 49.46  ?  32   LEU B CD1 1 
ATOM   4997  C CD2 . LEU B  2  32  ? 36.633  -0.370  81.965  1.00 52.03  ?  32   LEU B CD2 1 
ATOM   4998  N N   . SER B  2  33  ? 37.870  -5.561  83.069  1.00 49.71  ?  33   SER B N   1 
ATOM   4999  C CA  . SER B  2  33  ? 37.299  -6.900  83.150  1.00 49.55  ?  33   SER B CA  1 
ATOM   5000  C C   . SER B  2  33  ? 36.704  -7.173  84.525  1.00 52.13  ?  33   SER B C   1 
ATOM   5001  O O   . SER B  2  33  ? 35.730  -7.926  84.637  1.00 52.97  ?  33   SER B O   1 
ATOM   5002  C CB  . SER B  2  33  ? 38.362  -7.947  82.814  1.00 48.38  ?  33   SER B CB  1 
ATOM   5003  O OG  . SER B  2  33  ? 38.815  -7.805  81.479  1.00 46.43  ?  33   SER B OG  1 
ATOM   5004  N N   . ALA B  2  34  ? 37.274  -6.580  85.578  1.00 51.72  ?  34   ALA B N   1 
ATOM   5005  C CA  . ALA B  2  34  ? 36.674  -6.692  86.903  1.00 54.73  ?  34   ALA B CA  1 
ATOM   5006  C C   . ALA B  2  34  ? 35.278  -6.083  86.924  1.00 56.14  ?  34   ALA B C   1 
ATOM   5007  O O   . ALA B  2  34  ? 34.350  -6.652  87.511  1.00 58.36  ?  34   ALA B O   1 
ATOM   5008  C CB  . ALA B  2  34  ? 37.569  -6.023  87.946  1.00 56.43  ?  34   ALA B CB  1 
ATOM   5009  N N   . LEU B  2  35  ? 35.116  -4.917  86.295  1.00 54.79  ?  35   LEU B N   1 
ATOM   5010  C CA  . LEU B  2  35  ? 33.797  -4.305  86.173  1.00 56.73  ?  35   LEU B CA  1 
ATOM   5011  C C   . LEU B  2  35  ? 32.835  -5.226  85.433  1.00 57.02  ?  35   LEU B C   1 
ATOM   5012  O O   . LEU B  2  35  ? 31.676  -5.380  85.836  1.00 59.03  ?  35   LEU B O   1 
ATOM   5013  C CB  . LEU B  2  35  ? 33.924  -2.958  85.454  1.00 57.44  ?  35   LEU B CB  1 
ATOM   5014  C CG  . LEU B  2  35  ? 32.872  -1.853  85.604  1.00 62.02  ?  35   LEU B CG  1 
ATOM   5015  C CD1 . LEU B  2  35  ? 33.348  -0.598  84.901  1.00 62.29  ?  35   LEU B CD1 1 
ATOM   5016  C CD2 . LEU B  2  35  ? 31.531  -2.257  85.044  1.00 63.04  ?  35   LEU B CD2 1 
ATOM   5017  N N   . LYS B  2  36  ? 33.306  -5.850  84.350  1.00 54.58  ?  36   LYS B N   1 
ATOM   5018  C CA  . LYS B  2  36  ? 32.439  -6.666  83.505  1.00 53.88  ?  36   LYS B CA  1 
ATOM   5019  C C   . LYS B  2  36  ? 31.835  -7.837  84.270  1.00 56.05  ?  36   LYS B C   1 
ATOM   5020  O O   . LYS B  2  36  ? 30.709  -8.255  83.976  1.00 57.23  ?  36   LYS B O   1 
ATOM   5021  C CB  . LYS B  2  36  ? 33.233  -7.164  82.295  1.00 50.66  ?  36   LYS B CB  1 
ATOM   5022  C CG  . LYS B  2  36  ? 32.521  -8.186  81.425  1.00 49.91  ?  36   LYS B CG  1 
ATOM   5023  C CD  . LYS B  2  36  ? 33.497  -8.844  80.461  1.00 47.26  ?  36   LYS B CD  1 
ATOM   5024  C CE  . LYS B  2  36  ? 32.817  -9.901  79.609  1.00 46.75  ?  36   LYS B CE  1 
ATOM   5025  N NZ  . LYS B  2  36  ? 32.037  -9.295  78.495  1.00 46.12  ?  36   LYS B NZ  1 
ATOM   5026  N N   . ASN B  2  37  ? 32.549  -8.366  85.263  1.00 60.26  ?  37   ASN B N   1 
ATOM   5027  C CA  . ASN B  2  37  ? 32.073  -9.527  86.002  1.00 62.17  ?  37   ASN B CA  1 
ATOM   5028  C C   . ASN B  2  37  ? 31.171  -9.172  87.176  1.00 65.22  ?  37   ASN B C   1 
ATOM   5029  O O   . ASN B  2  37  ? 30.401  -10.029 87.626  1.00 67.46  ?  37   ASN B O   1 
ATOM   5030  C CB  . ASN B  2  37  ? 33.258  -10.352 86.513  1.00 60.06  ?  37   ASN B CB  1 
ATOM   5031  C CG  . ASN B  2  37  ? 34.105  -10.916 85.388  1.00 57.45  ?  37   ASN B CG  1 
ATOM   5032  O OD1 . ASN B  2  37  ? 34.005  -12.097 85.054  1.00 58.50  ?  37   ASN B OD1 1 
ATOM   5033  N ND2 . ASN B  2  37  ? 34.945  -10.074 84.799  1.00 55.00  ?  37   ASN B ND2 1 
ATOM   5034  N N   . SER B  2  38  ? 31.243  -7.945  87.686  1.00 63.59  ?  38   SER B N   1 
ATOM   5035  C CA  . SER B  2  38  ? 30.393  -7.528  88.793  1.00 68.00  ?  38   SER B CA  1 
ATOM   5036  C C   . SER B  2  38  ? 29.089  -6.887  88.339  1.00 69.41  ?  38   SER B C   1 
ATOM   5037  O O   . SER B  2  38  ? 28.259  -6.544  89.187  1.00 73.57  ?  38   SER B O   1 
ATOM   5038  C CB  . SER B  2  38  ? 31.149  -6.559  89.704  1.00 68.96  ?  38   SER B CB  1 
ATOM   5039  O OG  . SER B  2  38  ? 30.254  -5.745  90.442  1.00 72.78  ?  38   SER B OG  1 
ATOM   5040  N N   . LEU B  2  39  ? 28.888  -6.709  87.037  1.00 66.62  ?  39   LEU B N   1 
ATOM   5041  C CA  . LEU B  2  39  ? 27.648  -6.164  86.506  1.00 68.08  ?  39   LEU B CA  1 
ATOM   5042  C C   . LEU B  2  39  ? 26.863  -7.245  85.779  1.00 68.08  ?  39   LEU B C   1 
ATOM   5043  O O   . LEU B  2  39  ? 27.432  -8.040  85.025  1.00 64.99  ?  39   LEU B O   1 
ATOM   5044  C CB  . LEU B  2  39  ? 27.903  -4.996  85.549  1.00 65.49  ?  39   LEU B CB  1 
ATOM   5045  C CG  . LEU B  2  39  ? 28.287  -3.640  86.140  1.00 66.55  ?  39   LEU B CG  1 
ATOM   5046  C CD1 . LEU B  2  39  ? 28.066  -2.547  85.107  1.00 65.37  ?  39   LEU B CD1 1 
ATOM   5047  C CD2 . LEU B  2  39  ? 27.510  -3.345  87.410  1.00 71.44  ?  39   LEU B CD2 1 
ATOM   5048  N N   . ALA B  2  40  ? 25.554  -7.265  86.011  1.00 71.09  ?  40   ALA B N   1 
ATOM   5049  C CA  . ALA B  2  40  ? 24.653  -8.078  85.208  1.00 71.58  ?  40   ALA B CA  1 
ATOM   5050  C C   . ALA B  2  40  ? 24.308  -7.319  83.935  1.00 69.38  ?  40   ALA B C   1 
ATOM   5051  O O   . ALA B  2  40  ? 23.914  -6.150  83.986  1.00 70.68  ?  40   ALA B O   1 
ATOM   5052  C CB  . ALA B  2  40  ? 23.386  -8.414  85.994  1.00 77.36  ?  40   ALA B CB  1 
ATOM   5053  N N   . ASP B  2  41  ? 24.462  -7.981  82.788  1.00 68.18  ?  41   ASP B N   1 
ATOM   5054  C CA  . ASP B  2  41  ? 24.333  -7.346  81.478  1.00 65.77  ?  41   ASP B CA  1 
ATOM   5055  C C   . ASP B  2  41  ? 23.254  -8.087  80.699  1.00 67.10  ?  41   ASP B C   1 
ATOM   5056  O O   . ASP B  2  41  ? 23.555  -8.996  79.910  1.00 64.78  ?  41   ASP B O   1 
ATOM   5057  C CB  . ASP B  2  41  ? 25.668  -7.355  80.733  1.00 61.37  ?  41   ASP B CB  1 
ATOM   5058  C CG  . ASP B  2  41  ? 25.659  -6.477  79.492  1.00 59.06  ?  41   ASP B CG  1 
ATOM   5059  O OD1 . ASP B  2  41  ? 24.578  -6.247  78.912  1.00 60.73  ?  41   ASP B OD1 1 
ATOM   5060  O OD2 . ASP B  2  41  ? 26.747  -6.013  79.094  1.00 57.65  -1 41   ASP B OD2 1 
ATOM   5061  N N   . PRO B  2  42  ? 21.983  -7.725  80.892  1.00 63.87  ?  42   PRO B N   1 
ATOM   5062  C CA  . PRO B  2  42  ? 20.919  -8.389  80.128  1.00 64.72  ?  42   PRO B CA  1 
ATOM   5063  C C   . PRO B  2  42  ? 20.909  -8.008  78.660  1.00 62.21  ?  42   PRO B C   1 
ATOM   5064  O O   . PRO B  2  42  ? 20.463  -8.808  77.828  1.00 62.33  ?  42   PRO B O   1 
ATOM   5065  C CB  . PRO B  2  42  ? 19.642  -7.926  80.840  1.00 68.22  ?  42   PRO B CB  1 
ATOM   5066  C CG  . PRO B  2  42  ? 20.002  -6.584  81.390  1.00 68.08  ?  42   PRO B CG  1 
ATOM   5067  C CD  . PRO B  2  42  ? 21.465  -6.644  81.750  1.00 66.12  ?  42   PRO B CD  1 
ATOM   5068  N N   . ASN B  2  43  ? 21.393  -6.818  78.315  1.00 62.03  ?  43   ASN B N   1 
ATOM   5069  C CA  . ASN B  2  43  ? 21.352  -6.321  76.948  1.00 60.34  ?  43   ASN B CA  1 
ATOM   5070  C C   . ASN B  2  43  ? 22.623  -6.635  76.168  1.00 59.45  ?  43   ASN B C   1 
ATOM   5071  O O   . ASN B  2  43  ? 22.771  -6.163  75.035  1.00 57.76  ?  43   ASN B O   1 
ATOM   5072  C CB  . ASN B  2  43  ? 21.099  -4.811  76.952  1.00 60.46  ?  43   ASN B CB  1 
ATOM   5073  C CG  . ASN B  2  43  ? 19.624  -4.467  77.042  1.00 63.23  ?  43   ASN B CG  1 
ATOM   5074  O OD1 . ASN B  2  43  ? 19.115  -4.153  78.118  1.00 65.74  ?  43   ASN B OD1 1 
ATOM   5075  N ND2 . ASN B  2  43  ? 18.928  -4.528  75.912  1.00 63.28  ?  43   ASN B ND2 1 
ATOM   5076  N N   . LYS B  2  44  ? 23.537  -7.416  76.749  1.00 56.88  ?  44   LYS B N   1 
ATOM   5077  C CA  . LYS B  2  44  ? 24.780  -7.832  76.094  1.00 56.62  ?  44   LYS B CA  1 
ATOM   5078  C C   . LYS B  2  44  ? 25.610  -6.635  75.636  1.00 54.28  ?  44   LYS B C   1 
ATOM   5079  O O   . LYS B  2  44  ? 26.278  -6.687  74.601  1.00 53.81  ?  44   LYS B O   1 
ATOM   5080  C CB  . LYS B  2  44  ? 24.500  -8.774  74.918  1.00 55.48  ?  44   LYS B CB  1 
ATOM   5081  C CG  . LYS B  2  44  ? 23.864  -10.100 75.317  1.00 56.56  ?  44   LYS B CG  1 
ATOM   5082  C CD  . LYS B  2  44  ? 24.372  -10.583 76.669  1.00 59.29  ?  44   LYS B CD  1 
ATOM   5083  C CE  . LYS B  2  44  ? 23.556  -11.758 77.182  1.00 60.62  ?  44   LYS B CE  1 
ATOM   5084  N NZ  . LYS B  2  44  ? 24.361  -13.008 77.249  1.00 61.24  ?  44   LYS B NZ  1 
ATOM   5085  N N   . VAL B  2  45  ? 25.576  -5.549  76.410  1.00 52.09  ?  45   VAL B N   1 
ATOM   5086  C CA  . VAL B  2  45  ? 26.314  -4.345  76.041  1.00 50.89  ?  45   VAL B CA  1 
ATOM   5087  C C   . VAL B  2  45  ? 27.816  -4.580  76.154  1.00 49.21  ?  45   VAL B C   1 
ATOM   5088  O O   . VAL B  2  45  ? 28.590  -4.175  75.277  1.00 47.63  ?  45   VAL B O   1 
ATOM   5089  C CB  . VAL B  2  45  ? 25.851  -3.157  76.906  1.00 52.84  ?  45   VAL B CB  1 
ATOM   5090  C CG1 . VAL B  2  45  ? 26.955  -2.121  77.038  1.00 52.25  ?  45   VAL B CG1 1 
ATOM   5091  C CG2 . VAL B  2  45  ? 24.593  -2.532  76.319  1.00 54.04  ?  45   VAL B CG2 1 
ATOM   5092  N N   . LEU B  2  46  ? 28.251  -5.245  77.223  1.00 49.63  ?  46   LEU B N   1 
ATOM   5093  C CA  . LEU B  2  46  ? 29.662  -5.490  77.493  1.00 48.50  ?  46   LEU B CA  1 
ATOM   5094  C C   . LEU B  2  46  ? 30.213  -6.698  76.743  1.00 48.98  ?  46   LEU B C   1 
ATOM   5095  O O   . LEU B  2  46  ? 31.290  -7.192  77.100  1.00 47.81  ?  46   LEU B O   1 
ATOM   5096  C CB  . LEU B  2  46  ? 29.883  -5.668  78.998  1.00 50.40  ?  46   LEU B CB  1 
ATOM   5097  C CG  . LEU B  2  46  ? 29.700  -4.420  79.864  1.00 52.33  ?  46   LEU B CG  1 
ATOM   5098  C CD1 . LEU B  2  46  ? 30.520  -4.522  81.140  1.00 53.90  ?  46   LEU B CD1 1 
ATOM   5099  C CD2 . LEU B  2  46  ? 30.065  -3.165  79.089  1.00 51.32  ?  46   LEU B CD2 1 
ATOM   5100  N N   . GLN B  2  47  ? 29.499  -7.182  75.723  1.00 47.36  ?  47   GLN B N   1 
ATOM   5101  C CA  . GLN B  2  47  ? 29.897  -8.410  75.040  1.00 51.38  ?  47   GLN B CA  1 
ATOM   5102  C C   . GLN B  2  47  ? 31.275  -8.279  74.402  1.00 49.18  ?  47   GLN B C   1 
ATOM   5103  O O   . GLN B  2  47  ? 32.090  -9.207  74.471  1.00 50.06  ?  47   GLN B O   1 
ATOM   5104  C CB  . GLN B  2  47  ? 28.851  -8.781  73.988  1.00 52.90  ?  47   GLN B CB  1 
ATOM   5105  C CG  . GLN B  2  47  ? 29.373  -9.666  72.869  1.00 51.49  ?  47   GLN B CG  1 
ATOM   5106  C CD  . GLN B  2  47  ? 28.428  -10.802 72.539  1.00 50.62  ?  47   GLN B CD  1 
ATOM   5107  O OE1 . GLN B  2  47  ? 27.212  -10.616 72.483  1.00 50.04  ?  47   GLN B OE1 1 
ATOM   5108  N NE2 . GLN B  2  47  ? 28.982  -11.990 72.320  1.00 50.66  ?  47   GLN B NE2 1 
ATOM   5109  N N   . SER B  2  48  ? 31.563  -7.129  73.791  1.00 41.95  ?  48   SER B N   1 
ATOM   5110  C CA  . SER B  2  48  ? 32.821  -6.942  73.078  1.00 40.57  ?  48   SER B CA  1 
ATOM   5111  C C   . SER B  2  48  ? 34.034  -6.937  73.998  1.00 40.34  ?  48   SER B C   1 
ATOM   5112  O O   . SER B  2  48  ? 35.164  -6.989  73.500  1.00 39.42  ?  48   SER B O   1 
ATOM   5113  C CB  . SER B  2  48  ? 32.786  -5.639  72.279  1.00 40.36  ?  48   SER B CB  1 
ATOM   5114  O OG  . SER B  2  48  ? 32.313  -4.565  73.072  1.00 41.34  ?  48   SER B OG  1 
ATOM   5115  N N   . TRP B  2  49  ? 33.835  -6.877  75.314  1.00 41.63  ?  49   TRP B N   1 
ATOM   5116  C CA  . TRP B  2  49  ? 34.936  -6.735  76.266  1.00 41.34  ?  49   TRP B CA  1 
ATOM   5117  C C   . TRP B  2  49  ? 35.639  -8.084  76.405  1.00 41.22  ?  49   TRP B C   1 
ATOM   5118  O O   . TRP B  2  49  ? 35.370  -8.882  77.306  1.00 42.34  ?  49   TRP B O   1 
ATOM   5119  C CB  . TRP B  2  49  ? 34.420  -6.224  77.606  1.00 43.28  ?  49   TRP B CB  1 
ATOM   5120  C CG  . TRP B  2  49  ? 33.955  -4.795  77.568  1.00 43.94  ?  49   TRP B CG  1 
ATOM   5121  C CD1 . TRP B  2  49  ? 33.520  -4.100  76.476  1.00 43.16  ?  49   TRP B CD1 1 
ATOM   5122  C CD2 . TRP B  2  49  ? 33.900  -3.880  78.670  1.00 45.99  ?  49   TRP B CD2 1 
ATOM   5123  N NE1 . TRP B  2  49  ? 33.188  -2.816  76.831  1.00 44.53  ?  49   TRP B NE1 1 
ATOM   5124  C CE2 . TRP B  2  49  ? 33.414  -2.655  78.173  1.00 46.31  ?  49   TRP B CE2 1 
ATOM   5125  C CE3 . TRP B  2  49  ? 34.212  -3.980  80.029  1.00 47.99  ?  49   TRP B CE3 1 
ATOM   5126  C CZ2 . TRP B  2  49  ? 33.232  -1.539  78.986  1.00 48.58  ?  49   TRP B CZ2 1 
ATOM   5127  C CZ3 . TRP B  2  49  ? 34.030  -2.871  80.835  1.00 50.30  ?  49   TRP B CZ3 1 
ATOM   5128  C CH2 . TRP B  2  49  ? 33.544  -1.666  80.310  1.00 50.57  ?  49   TRP B CH2 1 
ATOM   5129  N N   . ASP B  2  50  ? 36.572  -8.331  75.485  1.00 37.39  ?  50   ASP B N   1 
ATOM   5130  C CA  . ASP B  2  50  ? 37.304  -9.593  75.423  1.00 37.88  ?  50   ASP B CA  1 
ATOM   5131  C C   . ASP B  2  50  ? 38.571  -9.463  76.261  1.00 37.65  ?  50   ASP B C   1 
ATOM   5132  O O   . ASP B  2  50  ? 39.484  -8.709  75.909  1.00 37.05  ?  50   ASP B O   1 
ATOM   5133  C CB  . ASP B  2  50  ? 37.627  -9.952  73.973  1.00 41.12  ?  50   ASP B CB  1 
ATOM   5134  C CG  . ASP B  2  50  ? 38.313  -11.301 73.838  1.00 43.26  ?  50   ASP B CG  1 
ATOM   5135  O OD1 . ASP B  2  50  ? 38.418  -12.030 74.847  1.00 43.21  ?  50   ASP B OD1 1 
ATOM   5136  O OD2 . ASP B  2  50  ? 38.738  -11.639 72.714  1.00 44.18  -1 50   ASP B OD2 1 
ATOM   5137  N N   . ALA B  2  51  ? 38.632  -10.217 77.362  1.00 38.82  ?  51   ALA B N   1 
ATOM   5138  C CA  . ALA B  2  51  ? 39.730  -10.094 78.314  1.00 39.80  ?  51   ALA B CA  1 
ATOM   5139  C C   . ALA B  2  51  ? 41.069  -10.541 77.741  1.00 39.01  ?  51   ALA B C   1 
ATOM   5140  O O   . ALA B  2  51  ? 42.114  -10.095 78.226  1.00 39.58  ?  51   ALA B O   1 
ATOM   5141  C CB  . ALA B  2  51  ? 39.418  -10.892 79.580  1.00 41.94  ?  51   ALA B CB  1 
ATOM   5142  N N   . THR B  2  52  ? 41.069  -11.408 76.731  1.00 39.01  ?  52   THR B N   1 
ATOM   5143  C CA  . THR B  2  52  ? 42.304  -11.972 76.199  1.00 38.67  ?  52   THR B CA  1 
ATOM   5144  C C   . THR B  2  52  ? 43.001  -11.056 75.197  1.00 37.48  ?  52   THR B C   1 
ATOM   5145  O O   . THR B  2  52  ? 43.948  -11.496 74.537  1.00 38.70  ?  52   THR B O   1 
ATOM   5146  C CB  . THR B  2  52  ? 42.021  -13.327 75.546  1.00 41.32  ?  52   THR B CB  1 
ATOM   5147  O OG1 . THR B  2  52  ? 41.269  -13.130 74.342  1.00 44.60  ?  52   THR B OG1 1 
ATOM   5148  C CG2 . THR B  2  52  ? 41.229  -14.215 76.491  1.00 41.73  ?  52   THR B CG2 1 
ATOM   5149  N N   . LEU B  2  53  ? 42.569  -9.806  75.077  1.00 37.63  ?  53   LEU B N   1 
ATOM   5150  C CA  . LEU B  2  53  ? 43.213  -8.839  74.201  1.00 37.05  ?  53   LEU B CA  1 
ATOM   5151  C C   . LEU B  2  53  ? 44.253  -8.044  74.983  1.00 38.04  ?  53   LEU B C   1 
ATOM   5152  O O   . LEU B  2  53  ? 44.151  -7.890  76.203  1.00 39.17  ?  53   LEU B O   1 
ATOM   5153  C CB  . LEU B  2  53  ? 42.179  -7.896  73.584  1.00 36.56  ?  53   LEU B CB  1 
ATOM   5154  C CG  . LEU B  2  53  ? 41.575  -8.276  72.227  1.00 35.81  ?  53   LEU B CG  1 
ATOM   5155  C CD1 . LEU B  2  53  ? 41.284  -9.765  72.136  1.00 35.86  ?  53   LEU B CD1 1 
ATOM   5156  C CD2 . LEU B  2  53  ? 40.308  -7.477  71.970  1.00 35.76  ?  53   LEU B CD2 1 
ATOM   5157  N N   . VAL B  2  54  ? 45.270  -7.552  74.268  1.00 37.37  ?  54   VAL B N   1 
ATOM   5158  C CA  . VAL B  2  54  ? 46.359  -6.829  74.925  1.00 38.72  ?  54   VAL B CA  1 
ATOM   5159  C C   . VAL B  2  54  ? 45.816  -5.613  75.666  1.00 39.76  ?  54   VAL B C   1 
ATOM   5160  O O   . VAL B  2  54  ? 46.035  -5.449  76.872  1.00 41.29  ?  54   VAL B O   1 
ATOM   5161  C CB  . VAL B  2  54  ? 47.438  -6.428  73.902  1.00 38.85  ?  54   VAL B CB  1 
ATOM   5162  C CG1 . VAL B  2  54  ? 48.320  -5.327  74.464  1.00 40.65  ?  54   VAL B CG1 1 
ATOM   5163  C CG2 . VAL B  2  54  ? 48.290  -7.624  73.528  1.00 38.66  ?  54   VAL B CG2 1 
ATOM   5164  N N   . THR B  2  55  ? 45.095  -4.752  74.962  1.00 42.66  ?  55   THR B N   1 
ATOM   5165  C CA  . THR B  2  55  ? 44.443  -3.589  75.538  1.00 43.83  ?  55   THR B CA  1 
ATOM   5166  C C   . THR B  2  55  ? 42.951  -3.622  75.233  1.00 42.87  ?  55   THR B C   1 
ATOM   5167  O O   . THR B  2  55  ? 42.517  -4.271  74.274  1.00 41.40  ?  55   THR B O   1 
ATOM   5168  C CB  . THR B  2  55  ? 45.048  -2.279  75.005  1.00 45.02  ?  55   THR B CB  1 
ATOM   5169  O OG1 . THR B  2  55  ? 44.692  -2.101  73.628  1.00 44.07  ?  55   THR B OG1 1 
ATOM   5170  C CG2 . THR B  2  55  ? 46.563  -2.273  75.157  1.00 46.24  ?  55   THR B CG2 1 
ATOM   5171  N N   . PRO B  2  56  ? 42.136  -2.933  76.032  1.00 43.68  ?  56   PRO B N   1 
ATOM   5172  C CA  . PRO B  2  56  ? 40.700  -2.842  75.746  1.00 43.12  ?  56   PRO B CA  1 
ATOM   5173  C C   . PRO B  2  56  ? 40.333  -1.784  74.719  1.00 43.15  ?  56   PRO B C   1 
ATOM   5174  O O   . PRO B  2  56  ? 39.152  -1.442  74.603  1.00 43.28  ?  56   PRO B O   1 
ATOM   5175  C CB  . PRO B  2  56  ? 40.113  -2.488  77.120  1.00 44.94  ?  56   PRO B CB  1 
ATOM   5176  C CG  . PRO B  2  56  ? 41.182  -1.714  77.782  1.00 46.83  ?  56   PRO B CG  1 
ATOM   5177  C CD  . PRO B  2  56  ? 42.475  -2.336  77.338  1.00 45.94  ?  56   PRO B CD  1 
ATOM   5178  N N   . CYS B  2  57  ? 41.315  -1.257  73.985  1.00 43.42  ?  57   CYS B N   1 
ATOM   5179  C CA  . CYS B  2  57  ? 41.078  -0.147  73.073  1.00 44.13  ?  57   CYS B CA  1 
ATOM   5180  C C   . CYS B  2  57  ? 40.228  -0.536  71.869  1.00 42.84  ?  57   CYS B C   1 
ATOM   5181  O O   . CYS B  2  57  ? 39.603  0.341   71.263  1.00 43.64  ?  57   CYS B O   1 
ATOM   5182  C CB  . CYS B  2  57  ? 42.419  0.427   72.617  1.00 45.17  ?  57   CYS B CB  1 
ATOM   5183  S SG  . CYS B  2  57  ? 43.386  1.137   73.971  1.00 49.93  ?  57   CYS B SG  1 
ATOM   5184  N N   . THR B  2  58  ? 40.188  -1.817  71.507  1.00 38.43  ?  58   THR B N   1 
ATOM   5185  C CA  . THR B  2  58  ? 39.330  -2.279  70.424  1.00 37.66  ?  58   THR B CA  1 
ATOM   5186  C C   . THR B  2  58  ? 37.939  -2.677  70.901  1.00 37.40  ?  58   THR B C   1 
ATOM   5187  O O   . THR B  2  58  ? 37.137  -3.158  70.094  1.00 37.05  ?  58   THR B O   1 
ATOM   5188  C CB  . THR B  2  58  ? 39.976  -3.462  69.695  1.00 36.71  ?  58   THR B CB  1 
ATOM   5189  O OG1 . THR B  2  58  ? 40.077  -4.578  70.586  1.00 36.03  ?  58   THR B OG1 1 
ATOM   5190  C CG2 . THR B  2  58  ? 41.363  -3.090  69.200  1.00 37.26  ?  58   THR B CG2 1 
ATOM   5191  N N   . TRP B  2  59  ? 37.636  -2.486  72.182  1.00 38.46  ?  59   TRP B N   1 
ATOM   5192  C CA  . TRP B  2  59  ? 36.311  -2.771  72.703  1.00 38.70  ?  59   TRP B CA  1 
ATOM   5193  C C   . TRP B  2  59  ? 35.349  -1.641  72.353  1.00 39.72  ?  59   TRP B C   1 
ATOM   5194  O O   . TRP B  2  59  ? 35.752  -0.504  72.091  1.00 40.64  ?  59   TRP B O   1 
ATOM   5195  C CB  . TRP B  2  59  ? 36.340  -2.954  74.222  1.00 39.51  ?  59   TRP B CB  1 
ATOM   5196  C CG  . TRP B  2  59  ? 37.239  -4.047  74.720  1.00 38.96  ?  59   TRP B CG  1 
ATOM   5197  C CD1 . TRP B  2  59  ? 37.980  -4.916  73.972  1.00 37.79  ?  59   TRP B CD1 1 
ATOM   5198  C CD2 . TRP B  2  59  ? 37.486  -4.386  76.090  1.00 40.01  ?  59   TRP B CD2 1 
ATOM   5199  N NE1 . TRP B  2  59  ? 38.675  -5.772  74.793  1.00 37.94  ?  59   TRP B NE1 1 
ATOM   5200  C CE2 . TRP B  2  59  ? 38.388  -5.467  76.097  1.00 39.32  ?  59   TRP B CE2 1 
ATOM   5201  C CE3 . TRP B  2  59  ? 37.032  -3.878  77.310  1.00 41.85  ?  59   TRP B CE3 1 
ATOM   5202  C CZ2 . TRP B  2  59  ? 38.845  -6.048  77.278  1.00 40.38  ?  59   TRP B CZ2 1 
ATOM   5203  C CZ3 . TRP B  2  59  ? 37.485  -4.457  78.481  1.00 43.00  ?  59   TRP B CZ3 1 
ATOM   5204  C CH2 . TRP B  2  59  ? 38.382  -5.531  78.456  1.00 42.25  ?  59   TRP B CH2 1 
ATOM   5205  N N   . PHE B  2  60  ? 34.061  -1.968  72.348  1.00 40.08  ?  60   PHE B N   1 
ATOM   5206  C CA  . PHE B  2  60  ? 33.041  -0.952  72.153  1.00 41.35  ?  60   PHE B CA  1 
ATOM   5207  C C   . PHE B  2  60  ? 32.747  -0.249  73.472  1.00 42.91  ?  60   PHE B C   1 
ATOM   5208  O O   . PHE B  2  60  ? 32.967  -0.799  74.556  1.00 43.06  ?  60   PHE B O   1 
ATOM   5209  C CB  . PHE B  2  60  ? 31.764  -1.568  71.580  1.00 41.31  ?  60   PHE B CB  1 
ATOM   5210  C CG  . PHE B  2  60  ? 31.974  -2.288  70.280  1.00 40.38  ?  60   PHE B CG  1 
ATOM   5211  C CD1 . PHE B  2  60  ? 32.786  -1.747  69.298  1.00 40.28  ?  60   PHE B CD1 1 
ATOM   5212  C CD2 . PHE B  2  60  ? 31.355  -3.501  70.035  1.00 40.10  ?  60   PHE B CD2 1 
ATOM   5213  C CE1 . PHE B  2  60  ? 32.984  -2.407  68.101  1.00 39.92  ?  60   PHE B CE1 1 
ATOM   5214  C CE2 . PHE B  2  60  ? 31.548  -4.166  68.841  1.00 40.96  ?  60   PHE B CE2 1 
ATOM   5215  C CZ  . PHE B  2  60  ? 32.362  -3.618  67.871  1.00 39.68  ?  60   PHE B CZ  1 
ATOM   5216  N N   . HIS B  2  61  ? 32.266  0.990   73.367  1.00 44.70  ?  61   HIS B N   1 
ATOM   5217  C CA  . HIS B  2  61  ? 31.971  1.896   74.474  1.00 46.87  ?  61   HIS B CA  1 
ATOM   5218  C C   . HIS B  2  61  ? 33.229  2.327   75.220  1.00 47.64  ?  61   HIS B C   1 
ATOM   5219  O O   . HIS B  2  61  ? 33.125  3.059   76.211  1.00 49.89  ?  61   HIS B O   1 
ATOM   5220  C CB  . HIS B  2  61  ? 30.972  1.295   75.475  1.00 47.58  ?  61   HIS B CB  1 
ATOM   5221  C CG  . HIS B  2  61  ? 29.839  0.561   74.827  1.00 46.85  ?  61   HIS B CG  1 
ATOM   5222  N ND1 . HIS B  2  61  ? 28.903  1.188   74.033  1.00 47.61  ?  61   HIS B ND1 1 
ATOM   5223  C CD2 . HIS B  2  61  ? 29.497  -0.749  74.848  1.00 45.83  ?  61   HIS B CD2 1 
ATOM   5224  C CE1 . HIS B  2  61  ? 28.031  0.297   73.596  1.00 47.09  ?  61   HIS B CE1 1 
ATOM   5225  N NE2 . HIS B  2  61  ? 28.368  -0.886  74.076  1.00 46.06  ?  61   HIS B NE2 1 
ATOM   5226  N N   . VAL B  2  62  ? 34.411  1.901   74.778  1.00 47.01  ?  62   VAL B N   1 
ATOM   5227  C CA  . VAL B  2  62  ? 35.685  2.296   75.365  1.00 47.78  ?  62   VAL B CA  1 
ATOM   5228  C C   . VAL B  2  62  ? 36.519  2.957   74.277  1.00 48.10  ?  62   VAL B C   1 
ATOM   5229  O O   . VAL B  2  62  ? 36.653  2.410   73.176  1.00 47.67  ?  62   VAL B O   1 
ATOM   5230  C CB  . VAL B  2  62  ? 36.429  1.089   75.967  1.00 47.96  ?  62   VAL B CB  1 
ATOM   5231  C CG1 . VAL B  2  62  ? 37.859  1.463   76.329  1.00 49.16  ?  62   VAL B CG1 1 
ATOM   5232  C CG2 . VAL B  2  62  ? 35.684  0.555   77.182  1.00 49.15  ?  62   VAL B CG2 1 
ATOM   5233  N N   . THR B  2  63  ? 37.073  4.130   74.578  1.00 50.84  ?  63   THR B N   1 
ATOM   5234  C CA  . THR B  2  63  ? 37.936  4.848   73.651  1.00 52.24  ?  63   THR B CA  1 
ATOM   5235  C C   . THR B  2  63  ? 39.273  5.148   74.315  1.00 54.60  ?  63   THR B C   1 
ATOM   5236  O O   . THR B  2  63  ? 39.325  5.504   75.497  1.00 54.86  ?  63   THR B O   1 
ATOM   5237  C CB  . THR B  2  63  ? 37.292  6.156   73.167  1.00 53.48  ?  63   THR B CB  1 
ATOM   5238  O OG1 . THR B  2  63  ? 37.536  7.196   74.122  1.00 55.88  ?  63   THR B OG1 1 
ATOM   5239  C CG2 . THR B  2  63  ? 35.791  5.985   72.975  1.00 52.00  ?  63   THR B CG2 1 
ATOM   5240  N N   . CYS B  2  64  ? 40.349  4.991   73.552  1.00 54.62  ?  64   CYS B N   1 
ATOM   5241  C CA  . CYS B  2  64  ? 41.704  5.248   74.012  1.00 56.82  ?  64   CYS B CA  1 
ATOM   5242  C C   . CYS B  2  64  ? 42.296  6.442   73.274  1.00 59.80  ?  64   CYS B C   1 
ATOM   5243  O O   . CYS B  2  64  ? 41.765  6.914   72.265  1.00 60.63  ?  64   CYS B O   1 
ATOM   5244  C CB  . CYS B  2  64  ? 42.597  4.021   73.802  1.00 56.97  ?  64   CYS B CB  1 
ATOM   5245  S SG  . CYS B  2  64  ? 42.171  2.559   74.762  1.00 55.34  ?  64   CYS B SG  1 
ATOM   5246  N N   . ASN B  2  65  ? 43.419  6.927   73.798  1.00 58.47  ?  65   ASN B N   1 
ATOM   5247  C CA  . ASN B  2  65  ? 44.212  7.943   73.125  1.00 62.20  ?  65   ASN B CA  1 
ATOM   5248  C C   . ASN B  2  65  ? 45.326  7.262   72.325  1.00 62.94  ?  65   ASN B C   1 
ATOM   5249  O O   . ASN B  2  65  ? 45.391  6.034   72.234  1.00 61.32  ?  65   ASN B O   1 
ATOM   5250  C CB  . ASN B  2  65  ? 44.742  8.961   74.135  1.00 63.64  ?  65   ASN B CB  1 
ATOM   5251  C CG  . ASN B  2  65  ? 45.523  8.318   75.269  1.00 63.32  ?  65   ASN B CG  1 
ATOM   5252  O OD1 . ASN B  2  65  ? 46.037  7.207   75.140  1.00 62.85  ?  65   ASN B OD1 1 
ATOM   5253  N ND2 . ASN B  2  65  ? 45.624  9.026   76.388  1.00 64.09  ?  65   ASN B ND2 1 
ATOM   5254  N N   . SER B  2  66  ? 46.218  8.061   71.734  1.00 61.50  ?  66   SER B N   1 
ATOM   5255  C CA  . SER B  2  66  ? 47.274  7.511   70.889  1.00 62.88  ?  66   SER B CA  1 
ATOM   5256  C C   . SER B  2  66  ? 48.234  6.610   71.657  1.00 62.84  ?  66   SER B C   1 
ATOM   5257  O O   . SER B  2  66  ? 48.988  5.855   71.033  1.00 63.58  ?  66   SER B O   1 
ATOM   5258  C CB  . SER B  2  66  ? 48.050  8.646   70.220  1.00 65.21  ?  66   SER B CB  1 
ATOM   5259  O OG  . SER B  2  66  ? 48.315  9.690   71.141  1.00 66.18  ?  66   SER B OG  1 
ATOM   5260  N N   . ASP B  2  67  ? 48.225  6.668   72.986  1.00 65.55  ?  67   ASP B N   1 
ATOM   5261  C CA  . ASP B  2  67  ? 49.078  5.823   73.812  1.00 65.21  ?  67   ASP B CA  1 
ATOM   5262  C C   . ASP B  2  67  ? 48.412  4.512   74.206  1.00 62.55  ?  67   ASP B C   1 
ATOM   5263  O O   . ASP B  2  67  ? 49.005  3.740   74.968  1.00 62.88  ?  67   ASP B O   1 
ATOM   5264  C CB  . ASP B  2  67  ? 49.505  6.579   75.074  1.00 66.07  ?  67   ASP B CB  1 
ATOM   5265  C CG  . ASP B  2  67  ? 50.422  7.746   74.772  1.00 68.82  ?  67   ASP B CG  1 
ATOM   5266  O OD1 . ASP B  2  67  ? 50.994  7.784   73.662  1.00 70.60  ?  67   ASP B OD1 1 
ATOM   5267  O OD2 . ASP B  2  67  ? 50.569  8.627   75.645  1.00 70.30  -1 67   ASP B OD2 1 
ATOM   5268  N N   . ASN B  2  68  ? 47.193  4.257   73.721  1.00 62.86  ?  68   ASN B N   1 
ATOM   5269  C CA  . ASN B  2  68  ? 46.422  3.056   74.053  1.00 60.53  ?  68   ASN B CA  1 
ATOM   5270  C C   . ASN B  2  68  ? 46.055  3.009   75.534  1.00 59.19  ?  68   ASN B C   1 
ATOM   5271  O O   . ASN B  2  68  ? 45.907  1.931   76.115  1.00 58.70  ?  68   ASN B O   1 
ATOM   5272  C CB  . ASN B  2  68  ? 47.155  1.776   73.638  1.00 60.70  ?  68   ASN B CB  1 
ATOM   5273  C CG  . ASN B  2  68  ? 47.457  1.734   72.154  1.00 61.76  ?  68   ASN B CG  1 
ATOM   5274  O OD1 . ASN B  2  68  ? 48.436  2.318   71.691  1.00 64.01  ?  68   ASN B OD1 1 
ATOM   5275  N ND2 . ASN B  2  68  ? 46.611  1.042   71.399  1.00 60.39  ?  68   ASN B ND2 1 
ATOM   5276  N N   . SER B  2  69  ? 45.912  4.176   76.155  1.00 62.59  ?  69   SER B N   1 
ATOM   5277  C CA  . SER B  2  69  ? 45.394  4.285   77.511  1.00 61.71  ?  69   SER B CA  1 
ATOM   5278  C C   . SER B  2  69  ? 43.920  4.662   77.444  1.00 59.97  ?  69   SER B C   1 
ATOM   5279  O O   . SER B  2  69  ? 43.538  5.548   76.672  1.00 60.73  ?  69   SER B O   1 
ATOM   5280  C CB  . SER B  2  69  ? 46.175  5.323   78.318  1.00 63.89  ?  69   SER B CB  1 
ATOM   5281  O OG  . SER B  2  69  ? 45.728  5.360   79.662  1.00 65.82  ?  69   SER B OG  1 
ATOM   5282  N N   . VAL B  2  70  ? 43.098  3.985   78.245  1.00 61.40  ?  70   VAL B N   1 
ATOM   5283  C CA  . VAL B  2  70  ? 41.662  4.233   78.224  1.00 59.65  ?  70   VAL B CA  1 
ATOM   5284  C C   . VAL B  2  70  ? 41.379  5.630   78.757  1.00 60.96  ?  70   VAL B C   1 
ATOM   5285  O O   . VAL B  2  70  ? 41.818  5.995   79.855  1.00 63.57  ?  70   VAL B O   1 
ATOM   5286  C CB  . VAL B  2  70  ? 40.920  3.164   79.037  1.00 58.31  ?  70   VAL B CB  1 
ATOM   5287  C CG1 . VAL B  2  70  ? 39.470  3.571   79.257  1.00 57.50  ?  70   VAL B CG1 1 
ATOM   5288  C CG2 . VAL B  2  70  ? 40.999  1.822   78.335  1.00 57.37  ?  70   VAL B CG2 1 
ATOM   5289  N N   . THR B  2  71  ? 40.641  6.421   77.976  1.00 60.54  ?  71   THR B N   1 
ATOM   5290  C CA  . THR B  2  71  ? 40.286  7.778   78.358  1.00 62.91  ?  71   THR B CA  1 
ATOM   5291  C C   . THR B  2  71  ? 38.787  8.010   78.475  1.00 62.49  ?  71   THR B C   1 
ATOM   5292  O O   . THR B  2  71  ? 38.384  9.060   78.988  1.00 64.93  ?  71   THR B O   1 
ATOM   5293  C CB  . THR B  2  71  ? 40.861  8.791   77.354  1.00 62.90  ?  71   THR B CB  1 
ATOM   5294  O OG1 . THR B  2  71  ? 40.214  8.628   76.086  1.00 60.07  ?  71   THR B OG1 1 
ATOM   5295  C CG2 . THR B  2  71  ? 42.359  8.590   77.186  1.00 63.63  ?  71   THR B CG2 1 
ATOM   5296  N N   . ARG B  2  72  ? 37.955  7.077   78.019  1.00 58.76  ?  72   ARG B N   1 
ATOM   5297  C CA  . ARG B  2  72  ? 36.514  7.269   78.052  1.00 58.07  ?  72   ARG B CA  1 
ATOM   5298  C C   . ARG B  2  72  ? 35.818  5.926   78.221  1.00 56.32  ?  72   ARG B C   1 
ATOM   5299  O O   . ARG B  2  72  ? 36.252  4.919   77.656  1.00 54.61  ?  72   ARG B O   1 
ATOM   5300  C CB  . ARG B  2  72  ? 36.029  7.956   76.771  1.00 58.71  ?  72   ARG B CB  1 
ATOM   5301  C CG  . ARG B  2  72  ? 34.591  8.421   76.808  1.00 58.86  ?  72   ARG B CG  1 
ATOM   5302  C CD  . ARG B  2  72  ? 34.267  9.283   75.599  1.00 60.10  ?  72   ARG B CD  1 
ATOM   5303  N NE  . ARG B  2  72  ? 33.247  10.276  75.905  1.00 61.63  ?  72   ARG B NE  1 
ATOM   5304  C CZ  . ARG B  2  72  ? 33.457  11.584  75.926  1.00 63.90  ?  72   ARG B CZ  1 
ATOM   5305  N NH1 . ARG B  2  72  ? 34.642  12.099  75.639  1.00 65.30  ?  72   ARG B NH1 1 
ATOM   5306  N NH2 . ARG B  2  72  ? 32.453  12.398  76.239  1.00 64.97  ?  72   ARG B NH2 1 
ATOM   5307  N N   . VAL B  2  73  ? 34.737  5.926   79.001  1.00 55.77  ?  73   VAL B N   1 
ATOM   5308  C CA  . VAL B  2  73  ? 33.863  4.767   79.154  1.00 54.73  ?  73   VAL B CA  1 
ATOM   5309  C C   . VAL B  2  73  ? 32.418  5.243   79.071  1.00 55.51  ?  73   VAL B C   1 
ATOM   5310  O O   . VAL B  2  73  ? 31.885  5.813   80.031  1.00 58.02  ?  73   VAL B O   1 
ATOM   5311  C CB  . VAL B  2  73  ? 34.126  4.021   80.476  1.00 56.23  ?  73   VAL B CB  1 
ATOM   5312  C CG1 . VAL B  2  73  ? 33.165  2.852   80.621  1.00 55.44  ?  73   VAL B CG1 1 
ATOM   5313  C CG2 . VAL B  2  73  ? 35.566  3.535   80.548  1.00 55.94  ?  73   VAL B CG2 1 
ATOM   5314  N N   . ASP B  2  74  ? 31.776  5.018   77.927  1.00 58.53  ?  74   ASP B N   1 
ATOM   5315  C CA  . ASP B  2  74  ? 30.428  5.524   77.665  1.00 59.59  ?  74   ASP B CA  1 
ATOM   5316  C C   . ASP B  2  74  ? 29.435  4.385   77.871  1.00 59.20  ?  74   ASP B C   1 
ATOM   5317  O O   . ASP B  2  74  ? 29.044  3.698   76.927  1.00 59.10  ?  74   ASP B O   1 
ATOM   5318  C CB  . ASP B  2  74  ? 30.333  6.098   76.257  1.00 60.24  ?  74   ASP B CB  1 
ATOM   5319  C CG  . ASP B  2  74  ? 31.420  7.109   75.968  1.00 60.91  ?  74   ASP B CG  1 
ATOM   5320  O OD1 . ASP B  2  74  ? 31.303  8.263   76.433  1.00 62.52  ?  74   ASP B OD1 1 
ATOM   5321  O OD2 . ASP B  2  74  ? 32.392  6.745   75.273  1.00 59.84  -1 74   ASP B OD2 1 
ATOM   5322  N N   . LEU B  2  75  ? 29.020  4.188   79.122  1.00 61.65  ?  75   LEU B N   1 
ATOM   5323  C CA  . LEU B  2  75  ? 28.085  3.128   79.479  1.00 62.00  ?  75   LEU B CA  1 
ATOM   5324  C C   . LEU B  2  75  ? 26.742  3.684   79.948  1.00 64.64  ?  75   LEU B C   1 
ATOM   5325  O O   . LEU B  2  75  ? 26.035  3.040   80.727  1.00 65.99  ?  75   LEU B O   1 
ATOM   5326  C CB  . LEU B  2  75  ? 28.693  2.226   80.550  1.00 62.23  ?  75   LEU B CB  1 
ATOM   5327  C CG  . LEU B  2  75  ? 29.581  1.104   80.011  1.00 59.83  ?  75   LEU B CG  1 
ATOM   5328  C CD1 . LEU B  2  75  ? 30.178  0.286   81.146  1.00 60.64  ?  75   LEU B CD1 1 
ATOM   5329  C CD2 . LEU B  2  75  ? 28.792  0.224   79.062  1.00 58.56  ?  75   LEU B CD2 1 
ATOM   5330  N N   . GLY B  2  76  ? 26.386  4.879   79.488  1.00 66.88  ?  76   GLY B N   1 
ATOM   5331  C CA  . GLY B  2  76  ? 25.107  5.459   79.859  1.00 69.75  ?  76   GLY B CA  1 
ATOM   5332  C C   . GLY B  2  76  ? 23.947  4.741   79.189  1.00 69.79  ?  76   GLY B C   1 
ATOM   5333  O O   . GLY B  2  76  ? 24.023  4.342   78.026  1.00 68.39  ?  76   GLY B O   1 
ATOM   5334  N N   . ASN B  2  77  ? 22.857  4.579   79.945  1.00 71.36  ?  77   ASN B N   1 
ATOM   5335  C CA  . ASN B  2  77  ? 21.611  3.998   79.436  1.00 72.55  ?  77   ASN B CA  1 
ATOM   5336  C C   . ASN B  2  77  ? 21.843  2.602   78.857  1.00 70.96  ?  77   ASN B C   1 
ATOM   5337  O O   . ASN B  2  77  ? 21.414  2.284   77.746  1.00 71.62  ?  77   ASN B O   1 
ATOM   5338  C CB  . ASN B  2  77  ? 20.959  4.922   78.404  1.00 73.83  ?  77   ASN B CB  1 
ATOM   5339  C CG  . ASN B  2  77  ? 19.450  4.975   78.539  1.00 77.22  ?  77   ASN B CG  1 
ATOM   5340  O OD1 . ASN B  2  77  ? 18.917  5.657   79.414  1.00 79.58  ?  77   ASN B OD1 1 
ATOM   5341  N ND2 . ASN B  2  77  ? 18.753  4.256   77.666  1.00 77.96  ?  77   ASN B ND2 1 
ATOM   5342  N N   . ALA B  2  78  ? 22.530  1.761   79.628  1.00 72.27  ?  78   ALA B N   1 
ATOM   5343  C CA  . ALA B  2  78  ? 22.896  0.422   79.190  1.00 71.10  ?  78   ALA B CA  1 
ATOM   5344  C C   . ALA B  2  78  ? 22.118  -0.679  79.898  1.00 72.20  ?  78   ALA B C   1 
ATOM   5345  O O   . ALA B  2  78  ? 22.365  -1.859  79.627  1.00 71.47  ?  78   ALA B O   1 
ATOM   5346  C CB  . ALA B  2  78  ? 24.399  0.196   79.386  1.00 68.72  ?  78   ALA B CB  1 
ATOM   5347  N N   . ASN B  2  79  ? 21.191  -0.328  80.794  1.00 73.84  ?  79   ASN B N   1 
ATOM   5348  C CA  . ASN B  2  79  ? 20.416  -1.302  81.567  1.00 75.30  ?  79   ASN B CA  1 
ATOM   5349  C C   . ASN B  2  79  ? 21.317  -2.237  82.369  1.00 74.20  ?  79   ASN B C   1 
ATOM   5350  O O   . ASN B  2  79  ? 20.992  -3.409  82.572  1.00 74.52  ?  79   ASN B O   1 
ATOM   5351  C CB  . ASN B  2  79  ? 19.476  -2.113  80.668  1.00 76.19  ?  79   ASN B CB  1 
ATOM   5352  C CG  . ASN B  2  79  ? 18.291  -1.304  80.182  1.00 78.60  ?  79   ASN B CG  1 
ATOM   5353  O OD1 . ASN B  2  79  ? 17.883  -0.332  80.819  1.00 80.24  ?  79   ASN B OD1 1 
ATOM   5354  N ND2 . ASN B  2  79  ? 17.729  -1.702  79.046  1.00 79.14  ?  79   ASN B ND2 1 
ATOM   5355  N N   . LEU B  2  80  ? 22.454  -1.725  82.833  1.00 77.00  ?  80   LEU B N   1 
ATOM   5356  C CA  . LEU B  2  80  ? 23.411  -2.513  83.599  1.00 76.63  ?  80   LEU B CA  1 
ATOM   5357  C C   . LEU B  2  80  ? 23.009  -2.518  85.068  1.00 77.36  ?  80   LEU B C   1 
ATOM   5358  O O   . LEU B  2  80  ? 22.865  -1.455  85.682  1.00 78.20  ?  80   LEU B O   1 
ATOM   5359  C CB  . LEU B  2  80  ? 24.825  -1.957  83.437  1.00 75.21  ?  80   LEU B CB  1 
ATOM   5360  C CG  . LEU B  2  80  ? 25.459  -2.074  82.051  1.00 74.84  ?  80   LEU B CG  1 
ATOM   5361  C CD1 . LEU B  2  80  ? 26.698  -1.197  81.955  1.00 74.22  ?  80   LEU B CD1 1 
ATOM   5362  C CD2 . LEU B  2  80  ? 25.795  -3.522  81.739  1.00 74.98  ?  80   LEU B CD2 1 
ATOM   5363  N N   . SER B  2  81  ? 22.825  -3.710  85.625  1.00 77.51  ?  81   SER B N   1 
ATOM   5364  C CA  . SER B  2  81  ? 22.578  -3.885  87.047  1.00 78.52  ?  81   SER B CA  1 
ATOM   5365  C C   . SER B  2  81  ? 23.781  -4.559  87.694  1.00 77.67  ?  81   SER B C   1 
ATOM   5366  O O   . SER B  2  81  ? 24.457  -5.385  87.075  1.00 76.72  ?  81   SER B O   1 
ATOM   5367  C CB  . SER B  2  81  ? 21.316  -4.716  87.292  1.00 80.24  ?  81   SER B CB  1 
ATOM   5368  O OG  . SER B  2  81  ? 21.065  -4.865  88.679  1.00 81.76  ?  81   SER B OG  1 
ATOM   5369  N N   . GLY B  2  82  ? 24.043  -4.197  88.939  1.00 78.10  ?  82   GLY B N   1 
ATOM   5370  C CA  . GLY B  2  82  ? 25.160  -4.753  89.671  1.00 77.62  ?  82   GLY B CA  1 
ATOM   5371  C C   . GLY B  2  82  ? 25.735  -3.720  90.620  1.00 78.51  ?  82   GLY B C   1 
ATOM   5372  O O   . GLY B  2  82  ? 25.056  -2.777  91.015  1.00 79.98  ?  82   GLY B O   1 
ATOM   5373  N N   . GLN B  2  83  ? 27.002  -3.925  90.975  1.00 76.37  ?  83   GLN B N   1 
ATOM   5374  C CA  . GLN B  2  83  ? 27.706  -3.057  91.905  1.00 77.48  ?  83   GLN B CA  1 
ATOM   5375  C C   . GLN B  2  83  ? 29.015  -2.581  91.291  1.00 76.29  ?  83   GLN B C   1 
ATOM   5376  O O   . GLN B  2  83  ? 29.656  -3.298  90.517  1.00 74.73  ?  83   GLN B O   1 
ATOM   5377  C CB  . GLN B  2  83  ? 27.992  -3.768  93.237  1.00 78.75  ?  83   GLN B CB  1 
ATOM   5378  C CG  . GLN B  2  83  ? 26.929  -4.768  93.656  1.00 79.52  ?  83   GLN B CG  1 
ATOM   5379  C CD  . GLN B  2  83  ? 26.848  -4.927  95.160  1.00 81.51  ?  83   GLN B CD  1 
ATOM   5380  O OE1 . GLN B  2  83  ? 27.831  -4.720  95.871  1.00 82.07  ?  83   GLN B OE1 1 
ATOM   5381  N NE2 . GLN B  2  83  ? 25.671  -5.292  95.655  1.00 82.91  ?  83   GLN B NE2 1 
ATOM   5382  N N   . LEU B  2  84  ? 29.402  -1.358  91.649  1.00 73.71  ?  84   LEU B N   1 
ATOM   5383  C CA  . LEU B  2  84  ? 30.661  -0.788  91.194  1.00 73.16  ?  84   LEU B CA  1 
ATOM   5384  C C   . LEU B  2  84  ? 31.846  -1.603  91.716  1.00 73.08  ?  84   LEU B C   1 
ATOM   5385  O O   . LEU B  2  84  ? 31.714  -2.481  92.572  1.00 73.74  ?  84   LEU B O   1 
ATOM   5386  C CB  . LEU B  2  84  ? 30.783  0.669   91.636  1.00 75.08  ?  84   LEU B CB  1 
ATOM   5387  C CG  . LEU B  2  84  ? 30.639  1.721   90.534  1.00 74.70  ?  84   LEU B CG  1 
ATOM   5388  C CD1 . LEU B  2  84  ? 29.311  1.579   89.808  1.00 73.98  ?  84   LEU B CD1 1 
ATOM   5389  C CD2 . LEU B  2  84  ? 30.796  3.124   91.099  1.00 77.19  ?  84   LEU B CD2 1 
ATOM   5390  N N   . VAL B  2  85  ? 33.023  -1.292  91.180  1.00 69.40  ?  85   VAL B N   1 
ATOM   5391  C CA  . VAL B  2  85  ? 34.232  -2.074  91.400  1.00 69.28  ?  85   VAL B CA  1 
ATOM   5392  C C   . VAL B  2  85  ? 35.381  -1.123  91.707  1.00 70.74  ?  85   VAL B C   1 
ATOM   5393  O O   . VAL B  2  85  ? 35.544  -0.097  91.037  1.00 70.65  ?  85   VAL B O   1 
ATOM   5394  C CB  . VAL B  2  85  ? 34.547  -2.949  90.167  1.00 66.99  ?  85   VAL B CB  1 
ATOM   5395  C CG1 . VAL B  2  85  ? 35.962  -3.463  90.208  1.00 67.13  ?  85   VAL B CG1 1 
ATOM   5396  C CG2 . VAL B  2  85  ? 33.575  -4.106  90.085  1.00 66.24  ?  85   VAL B CG2 1 
ATOM   5397  N N   . MET B  2  86  ? 36.174  -1.459  92.729  1.00 73.13  ?  86   MET B N   1 
ATOM   5398  C CA  . MET B  2  86  ? 37.280  -0.594  93.130  1.00 75.09  ?  86   MET B CA  1 
ATOM   5399  C C   . MET B  2  86  ? 38.401  -0.557  92.098  1.00 74.11  ?  86   MET B C   1 
ATOM   5400  O O   . MET B  2  86  ? 39.232  0.356   92.140  1.00 75.68  ?  86   MET B O   1 
ATOM   5401  C CB  . MET B  2  86  ? 37.810  -1.019  94.509  1.00 77.39  ?  86   MET B CB  1 
ATOM   5402  C CG  . MET B  2  86  ? 38.543  -2.368  94.594  1.00 77.01  ?  86   MET B CG  1 
ATOM   5403  S SD  . MET B  2  86  ? 40.209  -2.489  93.892  1.00 77.10  ?  86   MET B SD  1 
ATOM   5404  C CE  . MET B  2  86  ? 40.987  -1.020  94.545  1.00 80.21  ?  86   MET B CE  1 
ATOM   5405  N N   . GLN B  2  87  ? 38.443  -1.517  91.169  1.00 70.56  ?  87   GLN B N   1 
ATOM   5406  C CA  . GLN B  2  87  ? 39.427  -1.471  90.091  1.00 69.52  ?  87   GLN B CA  1 
ATOM   5407  C C   . GLN B  2  87  ? 39.227  -0.292  89.146  1.00 68.86  ?  87   GLN B C   1 
ATOM   5408  O O   . GLN B  2  87  ? 40.056  -0.099  88.251  1.00 68.21  ?  87   GLN B O   1 
ATOM   5409  C CB  . GLN B  2  87  ? 39.414  -2.772  89.280  1.00 67.33  ?  87   GLN B CB  1 
ATOM   5410  C CG  . GLN B  2  87  ? 40.028  -3.997  89.961  1.00 68.23  ?  87   GLN B CG  1 
ATOM   5411  C CD  . GLN B  2  87  ? 39.154  -4.607  91.043  1.00 69.07  ?  87   GLN B CD  1 
ATOM   5412  O OE1 . GLN B  2  87  ? 38.513  -3.903  91.819  1.00 70.19  ?  87   GLN B OE1 1 
ATOM   5413  N NE2 . GLN B  2  87  ? 39.125  -5.932  91.094  1.00 68.76  ?  87   GLN B NE2 1 
ATOM   5414  N N   . LEU B  2  88  ? 38.160  0.495   89.313  1.00 75.34  ?  88   LEU B N   1 
ATOM   5415  C CA  . LEU B  2  88  ? 37.948  1.664   88.467  1.00 75.17  ?  88   LEU B CA  1 
ATOM   5416  C C   . LEU B  2  88  ? 39.009  2.738   88.656  1.00 77.42  ?  88   LEU B C   1 
ATOM   5417  O O   . LEU B  2  88  ? 39.085  3.654   87.832  1.00 77.92  ?  88   LEU B O   1 
ATOM   5418  C CB  . LEU B  2  88  ? 36.563  2.262   88.724  1.00 75.65  ?  88   LEU B CB  1 
ATOM   5419  C CG  . LEU B  2  88  ? 35.399  1.478   88.126  1.00 73.55  ?  88   LEU B CG  1 
ATOM   5420  C CD1 . LEU B  2  88  ? 34.066  1.989   88.647  1.00 74.76  ?  88   LEU B CD1 1 
ATOM   5421  C CD2 . LEU B  2  88  ? 35.464  1.594   86.618  1.00 72.30  ?  88   LEU B CD2 1 
ATOM   5422  N N   . GLY B  2  89  ? 39.823  2.651   89.703  1.00 74.83  ?  89   GLY B N   1 
ATOM   5423  C CA  . GLY B  2  89  ? 40.901  3.589   89.922  1.00 77.42  ?  89   GLY B CA  1 
ATOM   5424  C C   . GLY B  2  89  ? 42.197  3.242   89.229  1.00 77.00  ?  89   GLY B C   1 
ATOM   5425  O O   . GLY B  2  89  ? 43.194  3.950   89.406  1.00 79.45  ?  89   GLY B O   1 
ATOM   5426  N N   . GLN B  2  90  ? 42.216  2.167   88.444  1.00 75.36  ?  90   GLN B N   1 
ATOM   5427  C CA  . GLN B  2  90  ? 43.395  1.743   87.701  1.00 74.84  ?  90   GLN B CA  1 
ATOM   5428  C C   . GLN B  2  90  ? 43.485  2.377   86.319  1.00 73.39  ?  90   GLN B C   1 
ATOM   5429  O O   . GLN B  2  90  ? 44.304  1.942   85.504  1.00 72.42  ?  90   GLN B O   1 
ATOM   5430  C CB  . GLN B  2  90  ? 43.416  0.218   87.567  1.00 72.96  ?  90   GLN B CB  1 
ATOM   5431  C CG  . GLN B  2  90  ? 43.146  -0.527  88.862  1.00 74.14  ?  90   GLN B CG  1 
ATOM   5432  C CD  . GLN B  2  90  ? 44.418  -0.913  89.583  1.00 76.57  ?  90   GLN B CD  1 
ATOM   5433  O OE1 . GLN B  2  90  ? 45.011  -1.955  89.305  1.00 76.01  ?  90   GLN B OE1 1 
ATOM   5434  N NE2 . GLN B  2  90  ? 44.850  -0.070  90.515  1.00 79.61  ?  90   GLN B NE2 1 
ATOM   5435  N N   . LEU B  2  91  ? 42.659  3.381   86.033  1.00 74.12  ?  91   LEU B N   1 
ATOM   5436  C CA  . LEU B  2  91  ? 42.651  4.010   84.719  1.00 72.88  ?  91   LEU B CA  1 
ATOM   5437  C C   . LEU B  2  91  ? 43.204  5.426   84.836  1.00 75.82  ?  91   LEU B C   1 
ATOM   5438  O O   . LEU B  2  91  ? 42.431  6.388   84.922  1.00 76.84  ?  91   LEU B O   1 
ATOM   5439  C CB  . LEU B  2  91  ? 41.236  4.033   84.136  1.00 70.77  ?  91   LEU B CB  1 
ATOM   5440  C CG  . LEU B  2  91  ? 40.613  2.743   83.584  1.00 68.22  ?  91   LEU B CG  1 
ATOM   5441  C CD1 . LEU B  2  91  ? 41.459  2.176   82.456  1.00 67.49  ?  91   LEU B CD1 1 
ATOM   5442  C CD2 . LEU B  2  91  ? 40.359  1.693   84.663  1.00 67.92  ?  91   LEU B CD2 1 
ATOM   5443  N N   . PRO B  2  92  ? 44.531  5.592   84.832  1.00 73.92  ?  92   PRO B N   1 
ATOM   5444  C CA  . PRO B  2  92  ? 45.103  6.923   85.109  1.00 77.46  ?  92   PRO B CA  1 
ATOM   5445  C C   . PRO B  2  92  ? 44.658  8.006   84.142  1.00 77.34  ?  92   PRO B C   1 
ATOM   5446  O O   . PRO B  2  92  ? 44.421  9.145   84.564  1.00 80.14  ?  92   PRO B O   1 
ATOM   5447  C CB  . PRO B  2  92  ? 46.615  6.671   85.024  1.00 78.88  ?  92   PRO B CB  1 
ATOM   5448  C CG  . PRO B  2  92  ? 46.750  5.479   84.134  1.00 75.42  ?  92   PRO B CG  1 
ATOM   5449  C CD  . PRO B  2  92  ? 45.559  4.616   84.429  1.00 72.93  ?  92   PRO B CD  1 
ATOM   5450  N N   . ASN B  2  93  ? 44.536  7.688   82.856  1.00 74.35  ?  93   ASN B N   1 
ATOM   5451  C CA  . ASN B  2  93  ? 44.208  8.681   81.842  1.00 74.32  ?  93   ASN B CA  1 
ATOM   5452  C C   . ASN B  2  93  ? 42.715  8.783   81.559  1.00 72.61  ?  93   ASN B C   1 
ATOM   5453  O O   . ASN B  2  93  ? 42.317  9.596   80.718  1.00 72.69  ?  93   ASN B O   1 
ATOM   5454  C CB  . ASN B  2  93  ? 44.958  8.373   80.542  1.00 72.45  ?  93   ASN B CB  1 
ATOM   5455  C CG  . ASN B  2  93  ? 46.448  8.630   80.657  1.00 74.94  ?  93   ASN B CG  1 
ATOM   5456  O OD1 . ASN B  2  93  ? 46.883  9.772   80.806  1.00 78.19  ?  93   ASN B OD1 1 
ATOM   5457  N ND2 . ASN B  2  93  ? 47.238  7.565   80.594  1.00 73.78  ?  93   ASN B ND2 1 
ATOM   5458  N N   . LEU B  2  94  ? 41.887  7.978   82.225  1.00 73.17  ?  94   LEU B N   1 
ATOM   5459  C CA  . LEU B  2  94  ? 40.444  8.002   82.008  1.00 71.83  ?  94   LEU B CA  1 
ATOM   5460  C C   . LEU B  2  94  ? 39.867  9.380   82.304  1.00 74.71  ?  94   LEU B C   1 
ATOM   5461  O O   . LEU B  2  94  ? 39.879  9.832   83.453  1.00 77.42  ?  94   LEU B O   1 
ATOM   5462  C CB  . LEU B  2  94  ? 39.765  6.940   82.872  1.00 70.70  ?  94   LEU B CB  1 
ATOM   5463  C CG  . LEU B  2  94  ? 38.254  7.019   83.085  1.00 70.39  ?  94   LEU B CG  1 
ATOM   5464  C CD1 . LEU B  2  94  ? 37.509  6.559   81.844  1.00 67.65  ?  94   LEU B CD1 1 
ATOM   5465  C CD2 . LEU B  2  94  ? 37.870  6.177   84.286  1.00 70.49  ?  94   LEU B CD2 1 
ATOM   5466  N N   . GLN B  2  95  ? 39.346  10.049  81.276  1.00 72.41  ?  95   GLN B N   1 
ATOM   5467  C CA  . GLN B  2  95  ? 38.860  11.417  81.400  1.00 75.47  ?  95   GLN B CA  1 
ATOM   5468  C C   . GLN B  2  95  ? 37.355  11.503  81.614  1.00 75.40  ?  95   GLN B C   1 
ATOM   5469  O O   . GLN B  2  95  ? 36.896  12.341  82.396  1.00 78.40  ?  95   GLN B O   1 
ATOM   5470  C CB  . GLN B  2  95  ? 39.241  12.228  80.156  1.00 75.83  ?  95   GLN B CB  1 
ATOM   5471  C CG  . GLN B  2  95  ? 40.727  12.211  79.834  1.00 76.15  ?  95   GLN B CG  1 
ATOM   5472  C CD  . GLN B  2  95  ? 41.046  12.843  78.493  1.00 76.00  ?  95   GLN B CD  1 
ATOM   5473  O OE1 . GLN B  2  95  ? 40.210  13.524  77.900  1.00 76.43  ?  95   GLN B OE1 1 
ATOM   5474  N NE2 . GLN B  2  95  ? 42.264  12.625  78.011  1.00 75.60  ?  95   GLN B NE2 1 
ATOM   5475  N N   . TYR B  2  96  ? 36.576  10.660  80.940  1.00 72.00  ?  96   TYR B N   1 
ATOM   5476  C CA  . TYR B  2  96  ? 35.120  10.708  81.013  1.00 72.55  ?  96   TYR B CA  1 
ATOM   5477  C C   . TYR B  2  96  ? 34.594  9.341   81.426  1.00 72.90  ?  96   TYR B C   1 
ATOM   5478  O O   . TYR B  2  96  ? 34.871  8.339   80.758  1.00 71.94  ?  96   TYR B O   1 
ATOM   5479  C CB  . TYR B  2  96  ? 34.514  11.143  79.675  1.00 71.46  ?  96   TYR B CB  1 
ATOM   5480  C CG  . TYR B  2  96  ? 34.897  12.550  79.266  1.00 71.50  ?  96   TYR B CG  1 
ATOM   5481  C CD1 . TYR B  2  96  ? 36.127  12.815  78.678  1.00 70.67  ?  96   TYR B CD1 1 
ATOM   5482  C CD2 . TYR B  2  96  ? 34.029  13.614  79.474  1.00 72.71  ?  96   TYR B CD2 1 
ATOM   5483  C CE1 . TYR B  2  96  ? 36.482  14.099  78.308  1.00 71.02  ?  96   TYR B CE1 1 
ATOM   5484  C CE2 . TYR B  2  96  ? 34.374  14.902  79.106  1.00 73.10  ?  96   TYR B CE2 1 
ATOM   5485  C CZ  . TYR B  2  96  ? 35.602  15.138  78.524  1.00 72.24  ?  96   TYR B CZ  1 
ATOM   5486  O OH  . TYR B  2  96  ? 35.952  16.417  78.155  1.00 72.91  ?  96   TYR B OH  1 
ATOM   5487  N N   . LEU B  2  97  ? 33.837  9.307   82.521  1.00 74.52  ?  97   LEU B N   1 
ATOM   5488  C CA  . LEU B  2  97  ? 33.255  8.085   83.068  1.00 75.38  ?  97   LEU B CA  1 
ATOM   5489  C C   . LEU B  2  97  ? 31.738  8.235   83.057  1.00 76.37  ?  97   LEU B C   1 
ATOM   5490  O O   . LEU B  2  97  ? 31.177  8.963   83.882  1.00 77.93  ?  97   LEU B O   1 
ATOM   5491  C CB  . LEU B  2  97  ? 33.778  7.820   84.480  1.00 76.82  ?  97   LEU B CB  1 
ATOM   5492  C CG  . LEU B  2  97  ? 33.720  6.385   85.006  1.00 77.62  ?  97   LEU B CG  1 
ATOM   5493  C CD1 . LEU B  2  97  ? 34.780  6.160   86.068  1.00 78.42  ?  97   LEU B CD1 1 
ATOM   5494  C CD2 . LEU B  2  97  ? 32.348  6.097   85.570  1.00 79.30  ?  97   LEU B CD2 1 
ATOM   5495  N N   . GLU B  2  98  ? 31.078  7.551   82.126  1.00 75.67  ?  98   GLU B N   1 
ATOM   5496  C CA  . GLU B  2  98  ? 29.636  7.672   81.914  1.00 76.56  ?  98   GLU B CA  1 
ATOM   5497  C C   . GLU B  2  98  ? 28.956  6.355   82.290  1.00 77.77  ?  98   GLU B C   1 
ATOM   5498  O O   . GLU B  2  98  ? 28.820  5.454   81.461  1.00 77.01  ?  98   GLU B O   1 
ATOM   5499  C CB  . GLU B  2  98  ? 29.339  8.056   80.465  1.00 75.00  ?  98   GLU B CB  1 
ATOM   5500  C CG  . GLU B  2  98  ? 30.240  9.151   79.915  1.00 73.70  ?  98   GLU B CG  1 
ATOM   5501  C CD  . GLU B  2  98  ? 30.111  10.450  80.685  1.00 75.05  ?  98   GLU B CD  1 
ATOM   5502  O OE1 . GLU B  2  98  ? 28.971  10.824  81.034  1.00 76.60  ?  98   GLU B OE1 1 
ATOM   5503  O OE2 . GLU B  2  98  ? 31.148  11.097  80.942  1.00 74.79  -1 98   GLU B OE2 1 
ATOM   5504  N N   . LEU B  2  99  ? 28.533  6.245   83.551  1.00 79.87  ?  99   LEU B N   1 
ATOM   5505  C CA  . LEU B  2  99  ? 27.744  5.108   84.017  1.00 81.58  ?  99   LEU B CA  1 
ATOM   5506  C C   . LEU B  2  99  ? 26.306  5.496   84.351  1.00 83.61  ?  99   LEU B C   1 
ATOM   5507  O O   . LEU B  2  99  ? 25.603  4.734   85.021  1.00 85.68  ?  99   LEU B O   1 
ATOM   5508  C CB  . LEU B  2  99  ? 28.400  4.452   85.233  1.00 82.80  ?  99   LEU B CB  1 
ATOM   5509  C CG  . LEU B  2  99  ? 29.446  3.363   84.982  1.00 81.86  ?  99   LEU B CG  1 
ATOM   5510  C CD1 . LEU B  2  99  ? 30.404  3.246   86.160  1.00 82.65  ?  99   LEU B CD1 1 
ATOM   5511  C CD2 . LEU B  2  99  ? 28.780  2.027   84.698  1.00 82.88  ?  99   LEU B CD2 1 
ATOM   5512  N N   . TYR B  2  100 ? 25.859  6.666   83.903  1.00 83.33  ?  100  TYR B N   1 
ATOM   5513  C CA  . TYR B  2  100 ? 24.550  7.182   84.276  1.00 85.57  ?  100  TYR B CA  1 
ATOM   5514  C C   . TYR B  2  100 ? 23.424  6.331   83.689  1.00 86.34  ?  100  TYR B C   1 
ATOM   5515  O O   . TYR B  2  100 ? 23.614  5.558   82.746  1.00 84.80  ?  100  TYR B O   1 
ATOM   5516  C CB  . TYR B  2  100 ? 24.401  8.637   83.823  1.00 85.19  ?  100  TYR B CB  1 
ATOM   5517  C CG  . TYR B  2  100 ? 24.496  8.842   82.325  1.00 82.88  ?  100  TYR B CG  1 
ATOM   5518  C CD1 . TYR B  2  100 ? 23.372  8.733   81.514  1.00 83.24  ?  100  TYR B CD1 1 
ATOM   5519  C CD2 . TYR B  2  100 ? 25.709  9.147   81.723  1.00 80.53  ?  100  TYR B CD2 1 
ATOM   5520  C CE1 . TYR B  2  100 ? 23.454  8.918   80.148  1.00 81.21  ?  100  TYR B CE1 1 
ATOM   5521  C CE2 . TYR B  2  100 ? 25.801  9.335   80.357  1.00 78.60  ?  100  TYR B CE2 1 
ATOM   5522  C CZ  . TYR B  2  100 ? 24.671  9.220   79.576  1.00 78.89  ?  100  TYR B CZ  1 
ATOM   5523  O OH  . TYR B  2  100 ? 24.761  9.404   78.217  1.00 77.02  ?  100  TYR B OH  1 
ATOM   5524  N N   . SER B  2  101 ? 22.234  6.489   84.275  1.00 89.03  ?  101  SER B N   1 
ATOM   5525  C CA  . SER B  2  101 ? 20.995  5.882   83.782  1.00 90.34  ?  101  SER B CA  1 
ATOM   5526  C C   . SER B  2  101 ? 21.096  4.356   83.703  1.00 90.43  ?  101  SER B C   1 
ATOM   5527  O O   . SER B  2  101 ? 20.987  3.750   82.635  1.00 89.20  ?  101  SER B O   1 
ATOM   5528  C CB  . SER B  2  101 ? 20.604  6.479   82.426  1.00 88.81  ?  101  SER B CB  1 
ATOM   5529  O OG  . SER B  2  101 ? 19.617  5.689   81.788  1.00 89.62  ?  101  SER B OG  1 
ATOM   5530  N N   . ASN B  2  102 ? 21.305  3.739   84.866  1.00 92.15  ?  102  ASN B N   1 
ATOM   5531  C CA  . ASN B  2  102 ? 21.303  2.288   84.993  1.00 93.07  ?  102  ASN B CA  1 
ATOM   5532  C C   . ASN B  2  102 ? 20.704  1.913   86.344  1.00 96.50  ?  102  ASN B C   1 
ATOM   5533  O O   . ASN B  2  102 ? 20.292  2.776   87.125  1.00 98.05  ?  102  ASN B O   1 
ATOM   5534  C CB  . ASN B  2  102 ? 22.716  1.715   84.829  1.00 90.92  ?  102  ASN B CB  1 
ATOM   5535  C CG  . ASN B  2  102 ? 23.189  1.729   83.388  1.00 88.04  ?  102  ASN B CG  1 
ATOM   5536  O OD1 . ASN B  2  102 ? 22.660  1.007   82.542  1.00 88.08  ?  102  ASN B OD1 1 
ATOM   5537  N ND2 . ASN B  2  102 ? 24.191  2.551   83.102  1.00 85.71  ?  102  ASN B ND2 1 
ATOM   5538  N N   . ASN B  2  103 ? 20.648  0.610   86.615  1.00 97.93  ?  103  ASN B N   1 
ATOM   5539  C CA  . ASN B  2  103 ? 20.126  0.073   87.870  1.00 101.40 ?  103  ASN B CA  1 
ATOM   5540  C C   . ASN B  2  103 ? 21.258  -0.421  88.769  1.00 101.32 ?  103  ASN B C   1 
ATOM   5541  O O   . ASN B  2  103 ? 21.123  -1.415  89.485  1.00 103.70 ?  103  ASN B O   1 
ATOM   5542  C CB  . ASN B  2  103 ? 19.117  -1.042  87.604  1.00 103.81 ?  103  ASN B CB  1 
ATOM   5543  C CG  . ASN B  2  103 ? 18.296  -1.395  88.834  1.00 107.91 ?  103  ASN B CG  1 
ATOM   5544  O OD1 . ASN B  2  103 ? 17.800  -0.515  89.538  1.00 109.38 ?  103  ASN B OD1 1 
ATOM   5545  N ND2 . ASN B  2  103 ? 18.152  -2.689  89.100  1.00 110.02 ?  103  ASN B ND2 1 
ATOM   5546  N N   . ILE B  2  104 ? 22.395  0.274   88.734  1.00 98.74  ?  104  ILE B N   1 
ATOM   5547  C CA  . ILE B  2  104 ? 23.557  -0.144  89.507  1.00 98.50  ?  104  ILE B CA  1 
ATOM   5548  C C   . ILE B  2  104 ? 23.339  0.177   90.979  1.00 101.08 ?  104  ILE B C   1 
ATOM   5549  O O   . ILE B  2  104 ? 22.865  1.264   91.337  1.00 101.70 ?  104  ILE B O   1 
ATOM   5550  C CB  . ILE B  2  104 ? 24.828  0.533   88.969  1.00 95.14  ?  104  ILE B CB  1 
ATOM   5551  C CG1 . ILE B  2  104 ? 24.926  0.344   87.454  1.00 92.74  ?  104  ILE B CG1 1 
ATOM   5552  C CG2 . ILE B  2  104 ? 26.063  -0.021  89.657  1.00 94.96  ?  104  ILE B CG2 1 
ATOM   5553  C CD1 . ILE B  2  104 ? 25.894  1.289   86.783  1.00 89.69  ?  104  ILE B CD1 1 
ATOM   5554  N N   . THR B  2  105 ? 23.671  -0.778  91.841  1.00 102.85 ?  105  THR B N   1 
ATOM   5555  C CA  . THR B  2  105 ? 23.529  -0.643  93.283  1.00 105.51 ?  105  THR B CA  1 
ATOM   5556  C C   . THR B  2  105 ? 24.908  -0.613  93.938  1.00 104.41 ?  105  THR B C   1 
ATOM   5557  O O   . THR B  2  105 ? 25.945  -0.633  93.269  1.00 101.68 ?  105  THR B O   1 
ATOM   5558  C CB  . THR B  2  105 ? 22.682  -1.784  93.854  1.00 109.09 ?  105  THR B CB  1 
ATOM   5559  O OG1 . THR B  2  105 ? 23.529  -2.891  94.185  1.00 109.41 ?  105  THR B OG1 1 
ATOM   5560  C CG2 . THR B  2  105 ? 21.639  -2.236  92.841  1.00 109.57 ?  105  THR B CG2 1 
ATOM   5561  N N   . GLY B  2  106 ? 24.909  -0.557  95.264  1.00 106.76 ?  106  GLY B N   1 
ATOM   5562  C CA  . GLY B  2  106 ? 26.144  -0.565  96.020  1.00 106.21 ?  106  GLY B CA  1 
ATOM   5563  C C   . GLY B  2  106 ? 26.659  0.824   96.332  1.00 104.91 ?  106  GLY B C   1 
ATOM   5564  O O   . GLY B  2  106 ? 25.990  1.844   96.142  1.00 104.93 ?  106  GLY B O   1 
ATOM   5565  N N   . THR B  2  107 ? 27.892  0.852   96.825  1.00 104.00 ?  107  THR B N   1 
ATOM   5566  C CA  . THR B  2  107 ? 28.549  2.083   97.234  1.00 103.06 ?  107  THR B CA  1 
ATOM   5567  C C   . THR B  2  107 ? 29.496  2.580   96.147  1.00 99.61  ?  107  THR B C   1 
ATOM   5568  O O   . THR B  2  107 ? 29.770  1.899   95.157  1.00 97.94  ?  107  THR B O   1 
ATOM   5569  C CB  . THR B  2  107 ? 29.319  1.876   98.542  1.00 104.53 ?  107  THR B CB  1 
ATOM   5570  O OG1 . THR B  2  107 ? 29.840  3.131   98.996  1.00 104.05 ?  107  THR B OG1 1 
ATOM   5571  C CG2 . THR B  2  107 ? 30.472  0.905   98.330  1.00 103.29 ?  107  THR B CG2 1 
ATOM   5572  N N   . ILE B  2  108 ? 29.997  3.793   96.350  1.00 98.81  ?  108  ILE B N   1 
ATOM   5573  C CA  . ILE B  2  108 ? 31.027  4.372   95.494  1.00 95.94  ?  108  ILE B CA  1 
ATOM   5574  C C   . ILE B  2  108 ? 32.381  4.053   96.120  1.00 95.67  ?  108  ILE B C   1 
ATOM   5575  O O   . ILE B  2  108 ? 32.652  4.510   97.242  1.00 97.16  ?  108  ILE B O   1 
ATOM   5576  C CB  . ILE B  2  108 ? 30.842  5.886   95.333  1.00 95.53  ?  108  ILE B CB  1 
ATOM   5577  C CG1 . ILE B  2  108 ? 29.500  6.193   94.667  1.00 95.94  ?  108  ILE B CG1 1 
ATOM   5578  C CG2 . ILE B  2  108 ? 31.983  6.478   94.521  1.00 92.89  ?  108  ILE B CG2 1 
ATOM   5579  C CD1 . ILE B  2  108 ? 29.186  7.671   94.586  1.00 96.18  ?  108  ILE B CD1 1 
ATOM   5580  N N   . PRO B  2  109 ? 33.245  3.292   95.450  1.00 94.91  ?  109  PRO B N   1 
ATOM   5581  C CA  . PRO B  2  109 ? 34.544  2.955   96.049  1.00 94.93  ?  109  PRO B CA  1 
ATOM   5582  C C   . PRO B  2  109 ? 35.480  4.155   96.021  1.00 93.65  ?  109  PRO B C   1 
ATOM   5583  O O   . PRO B  2  109 ? 35.702  4.762   94.974  1.00 91.65  ?  109  PRO B O   1 
ATOM   5584  C CB  . PRO B  2  109 ? 35.059  1.812   95.167  1.00 93.78  ?  109  PRO B CB  1 
ATOM   5585  C CG  . PRO B  2  109 ? 34.377  2.008   93.854  1.00 92.13  ?  109  PRO B CG  1 
ATOM   5586  C CD  . PRO B  2  109 ? 33.047  2.655   94.137  1.00 93.29  ?  109  PRO B CD  1 
ATOM   5587  N N   . GLU B  2  110 ? 36.034  4.488   97.188  1.00 96.33  ?  110  GLU B N   1 
ATOM   5588  C CA  . GLU B  2  110 ? 36.904  5.653   97.315  1.00 95.65  ?  110  GLU B CA  1 
ATOM   5589  C C   . GLU B  2  110 ? 38.098  5.616   96.368  1.00 93.47  ?  110  GLU B C   1 
ATOM   5590  O O   . GLU B  2  110 ? 38.758  6.646   96.190  1.00 92.73  ?  110  GLU B O   1 
ATOM   5591  C CB  . GLU B  2  110 ? 37.390  5.784   98.759  1.00 97.67  ?  110  GLU B CB  1 
ATOM   5592  C CG  . GLU B  2  110 ? 38.413  4.743   99.170  1.00 97.95  ?  110  GLU B CG  1 
ATOM   5593  C CD  . GLU B  2  110 ? 38.748  4.813   100.645 1.00 100.17 ?  110  GLU B CD  1 
ATOM   5594  O OE1 . GLU B  2  110 ? 38.966  5.934   101.151 1.00 100.67 ?  110  GLU B OE1 1 
ATOM   5595  O OE2 . GLU B  2  110 ? 38.788  3.750   101.299 1.00 101.59 -1 110  GLU B OE2 1 
ATOM   5596  N N   . GLN B  2  111 ? 38.394  4.465   95.762  1.00 93.32  ?  111  GLN B N   1 
ATOM   5597  C CA  . GLN B  2  111 ? 39.551  4.336   94.886  1.00 91.60  ?  111  GLN B CA  1 
ATOM   5598  C C   . GLN B  2  111 ? 39.397  5.071   93.559  1.00 89.53  ?  111  GLN B C   1 
ATOM   5599  O O   . GLN B  2  111 ? 40.380  5.165   92.817  1.00 88.21  ?  111  GLN B O   1 
ATOM   5600  C CB  . GLN B  2  111 ? 39.845  2.858   94.635  1.00 91.81  ?  111  GLN B CB  1 
ATOM   5601  C CG  . GLN B  2  111 ? 40.347  2.138   95.872  1.00 93.85  ?  111  GLN B CG  1 
ATOM   5602  C CD  . GLN B  2  111 ? 41.346  2.966   96.658  1.00 94.25  ?  111  GLN B CD  1 
ATOM   5603  O OE1 . GLN B  2  111 ? 41.046  3.452   97.748  1.00 95.69  ?  111  GLN B OE1 1 
ATOM   5604  N NE2 . GLN B  2  111 ? 42.542  3.132   96.104  1.00 93.17  ?  111  GLN B NE2 1 
ATOM   5605  N N   . LEU B  2  112 ? 38.208  5.592   93.232  1.00 90.98  ?  112  LEU B N   1 
ATOM   5606  C CA  . LEU B  2  112 ? 38.117  6.441   92.047  1.00 89.27  ?  112  LEU B CA  1 
ATOM   5607  C C   . LEU B  2  112 ? 38.871  7.754   92.212  1.00 88.89  ?  112  LEU B C   1 
ATOM   5608  O O   . LEU B  2  112 ? 39.040  8.476   91.224  1.00 87.52  ?  112  LEU B O   1 
ATOM   5609  C CB  . LEU B  2  112 ? 36.663  6.737   91.661  1.00 89.19  ?  112  LEU B CB  1 
ATOM   5610  C CG  . LEU B  2  112 ? 35.746  5.593   91.210  1.00 89.68  ?  112  LEU B CG  1 
ATOM   5611  C CD1 . LEU B  2  112 ? 34.655  5.294   92.221  1.00 91.56  ?  112  LEU B CD1 1 
ATOM   5612  C CD2 . LEU B  2  112 ? 35.143  5.893   89.844  1.00 88.59  ?  112  LEU B CD2 1 
ATOM   5613  N N   . GLY B  2  113 ? 39.317  8.085   93.424  1.00 91.04  ?  113  GLY B N   1 
ATOM   5614  C CA  . GLY B  2  113 ? 40.191  9.230   93.609  1.00 91.19  ?  113  GLY B CA  1 
ATOM   5615  C C   . GLY B  2  113 ? 41.580  9.055   93.029  1.00 90.07  ?  113  GLY B C   1 
ATOM   5616  O O   . GLY B  2  113 ? 42.338  10.030  92.979  1.00 90.14  ?  113  GLY B O   1 
ATOM   5617  N N   . ASN B  2  114 ? 41.925  7.847   92.586  1.00 91.40  ?  114  ASN B N   1 
ATOM   5618  C CA  . ASN B  2  114 ? 43.216  7.576   91.967  1.00 90.75  ?  114  ASN B CA  1 
ATOM   5619  C C   . ASN B  2  114 ? 43.265  7.985   90.501  1.00 89.33  ?  114  ASN B C   1 
ATOM   5620  O O   . ASN B  2  114 ? 44.331  7.891   89.884  1.00 89.08  ?  114  ASN B O   1 
ATOM   5621  C CB  . ASN B  2  114 ? 43.560  6.089   92.094  1.00 91.72  ?  114  ASN B CB  1 
ATOM   5622  C CG  . ASN B  2  114 ? 44.034  5.716   93.486  1.00 93.80  ?  114  ASN B CG  1 
ATOM   5623  O OD1 . ASN B  2  114 ? 44.282  6.583   94.324  1.00 94.35  ?  114  ASN B OD1 1 
ATOM   5624  N ND2 . ASN B  2  114 ? 44.164  4.419   93.738  1.00 94.44  ?  114  ASN B ND2 1 
ATOM   5625  N N   . LEU B  2  115 ? 42.146  8.429   89.934  1.00 90.93  ?  115  LEU B N   1 
ATOM   5626  C CA  . LEU B  2  115 ? 42.076  8.836   88.532  1.00 89.73  ?  115  LEU B CA  1 
ATOM   5627  C C   . LEU B  2  115 ? 42.713  10.215  88.410  1.00 89.69  ?  115  LEU B C   1 
ATOM   5628  O O   . LEU B  2  115 ? 42.040  11.243  88.491  1.00 89.51  ?  115  LEU B O   1 
ATOM   5629  C CB  . LEU B  2  115 ? 40.631  8.839   88.048  1.00 88.92  ?  115  LEU B CB  1 
ATOM   5630  C CG  . LEU B  2  115 ? 39.875  7.519   88.220  1.00 89.03  ?  115  LEU B CG  1 
ATOM   5631  C CD1 . LEU B  2  115 ? 38.388  7.699   87.952  1.00 88.39  ?  115  LEU B CD1 1 
ATOM   5632  C CD2 . LEU B  2  115 ? 40.460  6.442   87.329  1.00 88.74  ?  115  LEU B CD2 1 
ATOM   5633  N N   . THR B  2  116 ? 44.036  10.229  88.221  1.00 90.01  ?  116  THR B N   1 
ATOM   5634  C CA  . THR B  2  116 ? 44.788  11.482  88.236  1.00 90.21  ?  116  THR B CA  1 
ATOM   5635  C C   . THR B  2  116 ? 44.259  12.464  87.196  1.00 89.36  ?  116  THR B C   1 
ATOM   5636  O O   . THR B  2  116 ? 43.904  13.602  87.524  1.00 89.54  ?  116  THR B O   1 
ATOM   5637  C CB  . THR B  2  116 ? 46.273  11.203  88.003  1.00 90.66  ?  116  THR B CB  1 
ATOM   5638  O OG1 . THR B  2  116 ? 46.788  10.417  89.085  1.00 91.67  ?  116  THR B OG1 1 
ATOM   5639  C CG2 . THR B  2  116 ? 47.052  12.505  87.916  1.00 90.88  ?  116  THR B CG2 1 
ATOM   5640  N N   . GLU B  2  117 ? 44.193  12.041  85.937  1.00 88.58  ?  117  GLU B N   1 
ATOM   5641  C CA  . GLU B  2  117 ? 43.541  12.829  84.904  1.00 87.83  ?  117  GLU B CA  1 
ATOM   5642  C C   . GLU B  2  117 ? 42.072  12.434  84.875  1.00 87.26  ?  117  GLU B C   1 
ATOM   5643  O O   . GLU B  2  117 ? 41.747  11.244  84.828  1.00 87.04  ?  117  GLU B O   1 
ATOM   5644  C CB  . GLU B  2  117 ? 44.194  12.598  83.539  1.00 87.41  ?  117  GLU B CB  1 
ATOM   5645  C CG  . GLU B  2  117 ? 44.273  13.834  82.633  1.00 87.23  ?  117  GLU B CG  1 
ATOM   5646  C CD  . GLU B  2  117 ? 42.918  14.363  82.178  1.00 86.63  ?  117  GLU B CD  1 
ATOM   5647  O OE1 . GLU B  2  117 ? 41.903  13.651  82.314  1.00 86.15  ?  117  GLU B OE1 1 
ATOM   5648  O OE2 . GLU B  2  117 ? 42.871  15.507  81.679  1.00 86.74  -1 117  GLU B OE2 1 
ATOM   5649  N N   . LEU B  2  118 ? 41.191  13.430  84.907  1.00 87.15  ?  118  LEU B N   1 
ATOM   5650  C CA  . LEU B  2  118 ? 39.768  13.166  85.057  1.00 86.82  ?  118  LEU B CA  1 
ATOM   5651  C C   . LEU B  2  118 ? 38.998  14.442  84.757  1.00 86.77  ?  118  LEU B C   1 
ATOM   5652  O O   . LEU B  2  118 ? 39.392  15.518  85.203  1.00 87.44  ?  118  LEU B O   1 
ATOM   5653  C CB  . LEU B  2  118 ? 39.460  12.663  86.475  1.00 87.56  ?  118  LEU B CB  1 
ATOM   5654  C CG  . LEU B  2  118 ? 38.053  12.155  86.772  1.00 87.42  ?  118  LEU B CG  1 
ATOM   5655  C CD1 . LEU B  2  118 ? 37.122  13.305  87.150  1.00 87.78  ?  118  LEU B CD1 1 
ATOM   5656  C CD2 . LEU B  2  118 ? 37.534  11.390  85.562  1.00 86.37  ?  118  LEU B CD2 1 
ATOM   5657  N N   . VAL B  2  119 ? 37.896  14.320  84.016  1.00 86.09  ?  119  VAL B N   1 
ATOM   5658  C CA  . VAL B  2  119 ? 37.064  15.462  83.660  1.00 86.15  ?  119  VAL B CA  1 
ATOM   5659  C C   . VAL B  2  119 ? 35.631  15.294  84.158  1.00 86.20  ?  119  VAL B C   1 
ATOM   5660  O O   . VAL B  2  119 ? 35.096  16.169  84.846  1.00 86.97  ?  119  VAL B O   1 
ATOM   5661  C CB  . VAL B  2  119 ? 37.087  15.724  82.137  1.00 85.46  ?  119  VAL B CB  1 
ATOM   5662  C CG1 . VAL B  2  119 ? 35.936  16.633  81.735  1.00 85.51  ?  119  VAL B CG1 1 
ATOM   5663  C CG2 . VAL B  2  119 ? 38.421  16.333  81.726  1.00 85.79  ?  119  VAL B CG2 1 
ATOM   5664  N N   . SER B  2  120 ? 34.993  14.173  83.823  1.00 85.51  ?  120  SER B N   1 
ATOM   5665  C CA  . SER B  2  120 ? 33.563  13.999  84.056  1.00 85.49  ?  120  SER B CA  1 
ATOM   5666  C C   . SER B  2  120 ? 33.279  12.716  84.826  1.00 85.59  ?  120  SER B C   1 
ATOM   5667  O O   . SER B  2  120 ? 33.782  11.646  84.467  1.00 85.11  ?  120  SER B O   1 
ATOM   5668  C CB  . SER B  2  120 ? 32.795  13.990  82.729  1.00 84.59  ?  120  SER B CB  1 
ATOM   5669  O OG  . SER B  2  120 ? 31.415  14.241  82.933  1.00 84.77  ?  120  SER B OG  1 
ATOM   5670  N N   . LEU B  2  121 ? 32.465  12.832  85.878  1.00 86.39  ?  121  LEU B N   1 
ATOM   5671  C CA  . LEU B  2  121 ? 31.887  11.700  86.607  1.00 86.69  ?  121  LEU B CA  1 
ATOM   5672  C C   . LEU B  2  121 ? 30.368  11.819  86.536  1.00 86.70  ?  121  LEU B C   1 
ATOM   5673  O O   . LEU B  2  121 ? 29.767  12.629  87.248  1.00 87.61  ?  121  LEU B O   1 
ATOM   5674  C CB  . LEU B  2  121 ? 32.360  11.658  88.062  1.00 87.94  ?  121  LEU B CB  1 
ATOM   5675  C CG  . LEU B  2  121 ? 33.569  10.812  88.469  1.00 88.18  ?  121  LEU B CG  1 
ATOM   5676  C CD1 . LEU B  2  121 ? 33.175  9.364   88.631  1.00 88.19  ?  121  LEU B CD1 1 
ATOM   5677  C CD2 . LEU B  2  121 ? 34.651  10.914  87.445  1.00 87.35  ?  121  LEU B CD2 1 
ATOM   5678  N N   . ASP B  2  122 ? 29.746  11.012  85.683  1.00 87.73  ?  122  ASP B N   1 
ATOM   5679  C CA  . ASP B  2  122 ? 28.296  11.014  85.507  1.00 87.67  ?  122  ASP B CA  1 
ATOM   5680  C C   . ASP B  2  122 ? 27.753  9.683   86.025  1.00 87.88  ?  122  ASP B C   1 
ATOM   5681  O O   . ASP B  2  122 ? 27.691  8.691   85.296  1.00 87.06  ?  122  ASP B O   1 
ATOM   5682  C CB  . ASP B  2  122 ? 27.923  11.244  84.046  1.00 86.54  ?  122  ASP B CB  1 
ATOM   5683  C CG  . ASP B  2  122 ? 28.227  12.657  83.582  1.00 86.64  ?  122  ASP B CG  1 
ATOM   5684  O OD1 . ASP B  2  122 ? 29.420  13.028  83.536  1.00 86.67  ?  122  ASP B OD1 1 
ATOM   5685  O OD2 . ASP B  2  122 ? 27.272  13.399  83.268  1.00 86.80  -1 122  ASP B OD2 1 
ATOM   5686  N N   . LEU B  2  123 ? 27.363  9.671   87.300  1.00 88.93  ?  123  LEU B N   1 
ATOM   5687  C CA  . LEU B  2  123 ? 26.785  8.499   87.947  1.00 89.49  ?  123  LEU B CA  1 
ATOM   5688  C C   . LEU B  2  123 ? 25.309  8.683   88.277  1.00 90.10  ?  123  LEU B C   1 
ATOM   5689  O O   . LEU B  2  123 ? 24.735  7.850   88.986  1.00 90.89  ?  123  LEU B O   1 
ATOM   5690  C CB  . LEU B  2  123 ? 27.562  8.150   89.220  1.00 90.71  ?  123  LEU B CB  1 
ATOM   5691  C CG  . LEU B  2  123 ? 28.885  7.379   89.125  1.00 90.45  ?  123  LEU B CG  1 
ATOM   5692  C CD1 . LEU B  2  123 ? 28.645  5.966   88.614  1.00 89.97  ?  123  LEU B CD1 1 
ATOM   5693  C CD2 . LEU B  2  123 ? 29.911  8.090   88.261  1.00 89.52  ?  123  LEU B CD2 1 
ATOM   5694  N N   . TYR B  2  124 ? 24.687  9.753   87.789  1.00 90.16  ?  124  TYR B N   1 
ATOM   5695  C CA  . TYR B  2  124 ? 23.314  10.073  88.145  1.00 90.96  ?  124  TYR B CA  1 
ATOM   5696  C C   . TYR B  2  124 ? 22.348  9.005   87.628  1.00 90.38  ?  124  TYR B C   1 
ATOM   5697  O O   . TYR B  2  124 ? 22.696  8.147   86.811  1.00 89.23  ?  124  TYR B O   1 
ATOM   5698  C CB  . TYR B  2  124 ? 22.929  11.448  87.600  1.00 90.91  ?  124  TYR B CB  1 
ATOM   5699  C CG  . TYR B  2  124 ? 23.108  11.604  86.105  1.00 89.38  ?  124  TYR B CG  1 
ATOM   5700  C CD1 . TYR B  2  124 ? 24.311  12.048  85.571  1.00 88.74  ?  124  TYR B CD1 1 
ATOM   5701  C CD2 . TYR B  2  124 ? 22.069  11.321  85.229  1.00 88.68  ?  124  TYR B CD2 1 
ATOM   5702  C CE1 . TYR B  2  124 ? 24.476  12.196  84.206  1.00 87.53  ?  124  TYR B CE1 1 
ATOM   5703  C CE2 . TYR B  2  124 ? 22.224  11.466  83.863  1.00 87.41  ?  124  TYR B CE2 1 
ATOM   5704  C CZ  . TYR B  2  124 ? 23.429  11.904  83.357  1.00 86.88  ?  124  TYR B CZ  1 
ATOM   5705  O OH  . TYR B  2  124 ? 23.589  12.050  81.998  1.00 85.79  ?  124  TYR B OH  1 
ATOM   5706  N N   . LEU B  2  125 ? 21.112  9.071   88.129  1.00 93.47  ?  125  LEU B N   1 
ATOM   5707  C CA  . LEU B  2  125 ? 20.026  8.174   87.728  1.00 93.15  ?  125  LEU B CA  1 
ATOM   5708  C C   . LEU B  2  125 ? 20.401  6.707   87.959  1.00 93.05  ?  125  LEU B C   1 
ATOM   5709  O O   . LEU B  2  125 ? 20.469  5.897   87.033  1.00 91.86  ?  125  LEU B O   1 
ATOM   5710  C CB  . LEU B  2  125 ? 19.622  8.419   86.269  1.00 91.68  ?  125  LEU B CB  1 
ATOM   5711  C CG  . LEU B  2  125 ? 18.884  9.725   85.964  1.00 91.99  ?  125  LEU B CG  1 
ATOM   5712  C CD1 . LEU B  2  125 ? 18.877  9.999   84.469  1.00 90.51  ?  125  LEU B CD1 1 
ATOM   5713  C CD2 . LEU B  2  125 ? 17.465  9.675   86.505  1.00 93.12  ?  125  LEU B CD2 1 
ATOM   5714  N N   . ASN B  2  126 ? 20.642  6.378   89.226  1.00 94.16  ?  126  ASN B N   1 
ATOM   5715  C CA  . ASN B  2  126 ? 21.010  5.023   89.618  1.00 94.49  ?  126  ASN B CA  1 
ATOM   5716  C C   . ASN B  2  126 ? 20.388  4.727   90.979  1.00 96.47  ?  126  ASN B C   1 
ATOM   5717  O O   . ASN B  2  126 ? 19.548  5.479   91.481  1.00 97.45  ?  126  ASN B O   1 
ATOM   5718  C CB  . ASN B  2  126 ? 22.536  4.858   89.633  1.00 94.12  ?  126  ASN B CB  1 
ATOM   5719  C CG  . ASN B  2  126 ? 23.061  4.180   88.387  1.00 92.54  ?  126  ASN B CG  1 
ATOM   5720  O OD1 . ASN B  2  126 ? 22.867  2.980   88.192  1.00 92.48  ?  126  ASN B OD1 1 
ATOM   5721  N ND2 . ASN B  2  126 ? 23.729  4.944   87.533  1.00 91.41  ?  126  ASN B ND2 1 
ATOM   5722  N N   . ASN B  2  127 ? 20.809  3.614   91.580  1.00 96.22  ?  127  ASN B N   1 
ATOM   5723  C CA  . ASN B  2  127 ? 20.335  3.187   92.891  1.00 98.29  ?  127  ASN B CA  1 
ATOM   5724  C C   . ASN B  2  127 ? 21.514  3.072   93.856  1.00 99.34  ?  127  ASN B C   1 
ATOM   5725  O O   . ASN B  2  127 ? 21.520  2.241   94.763  1.00 100.87 ?  127  ASN B O   1 
ATOM   5726  C CB  . ASN B  2  127 ? 19.558  1.871   92.765  1.00 98.58  ?  127  ASN B CB  1 
ATOM   5727  C CG  . ASN B  2  127 ? 18.806  1.485   94.036  1.00 100.86 ?  127  ASN B CG  1 
ATOM   5728  O OD1 . ASN B  2  127 ? 19.361  0.892   94.961  1.00 102.26 ?  127  ASN B OD1 1 
ATOM   5729  N ND2 . ASN B  2  127 ? 17.524  1.823   94.076  1.00 101.36 ?  127  ASN B ND2 1 
ATOM   5730  N N   . LEU B  2  128 ? 22.530  3.907   93.654  1.00 101.53 ?  128  LEU B N   1 
ATOM   5731  C CA  . LEU B  2  128 ? 23.702  3.890   94.516  1.00 102.45 ?  128  LEU B CA  1 
ATOM   5732  C C   . LEU B  2  128 ? 23.342  4.353   95.923  1.00 104.58 ?  128  LEU B C   1 
ATOM   5733  O O   . LEU B  2  128 ? 22.420  5.148   96.125  1.00 105.12 ?  128  LEU B O   1 
ATOM   5734  C CB  . LEU B  2  128 ? 24.806  4.782   93.943  1.00 101.21 ?  128  LEU B CB  1 
ATOM   5735  C CG  . LEU B  2  128 ? 25.840  4.180   92.986  1.00 99.77  ?  128  LEU B CG  1 
ATOM   5736  C CD1 . LEU B  2  128 ? 25.184  3.393   91.863  1.00 98.54  ?  128  LEU B CD1 1 
ATOM   5737  C CD2 . LEU B  2  128 ? 26.735  5.273   92.420  1.00 98.71  ?  128  LEU B CD2 1 
ATOM   5738  N N   . SER B  2  129 ? 24.085  3.845   96.904  1.00 102.23 ?  129  SER B N   1 
ATOM   5739  C CA  . SER B  2  129 ? 23.864  4.220   98.295  1.00 104.44 ?  129  SER B CA  1 
ATOM   5740  C C   . SER B  2  129 ? 25.191  4.512   98.982  1.00 105.05 ?  129  SER B C   1 
ATOM   5741  O O   . SER B  2  129 ? 26.241  4.544   98.333  1.00 103.68 ?  129  SER B O   1 
ATOM   5742  C CB  . SER B  2  129 ? 23.108  3.117   99.039  1.00 106.20 ?  129  SER B CB  1 
ATOM   5743  O OG  . SER B  2  129 ? 23.913  1.962   99.194  1.00 106.52 ?  129  SER B OG  1 
ATOM   5744  N N   . GLY B  2  130 ? 25.153  4.725   100.294 1.00 108.87 ?  130  GLY B N   1 
ATOM   5745  C CA  . GLY B  2  130 ? 26.344  5.032   101.046 1.00 109.65 ?  130  GLY B CA  1 
ATOM   5746  C C   . GLY B  2  130 ? 26.758  6.481   100.900 1.00 109.00 ?  130  GLY B C   1 
ATOM   5747  O O   . GLY B  2  130 ? 26.052  7.299   100.303 1.00 108.18 ?  130  GLY B O   1 
ATOM   5748  N N   . PRO B  2  131 ? 27.919  6.824   101.440 1.00 106.91 ?  131  PRO B N   1 
ATOM   5749  C CA  . PRO B  2  131 ? 28.375  8.216   101.441 1.00 106.60 ?  131  PRO B CA  1 
ATOM   5750  C C   . PRO B  2  131 ? 29.042  8.587   100.120 1.00 104.24 ?  131  PRO B C   1 
ATOM   5751  O O   . PRO B  2  131 ? 29.162  7.780   99.200  1.00 102.84 ?  131  PRO B O   1 
ATOM   5752  C CB  . PRO B  2  131 ? 29.373  8.243   102.598 1.00 108.17 ?  131  PRO B CB  1 
ATOM   5753  C CG  . PRO B  2  131 ? 29.964  6.874   102.584 1.00 108.16 ?  131  PRO B CG  1 
ATOM   5754  C CD  . PRO B  2  131 ? 28.853  5.939   102.160 1.00 107.98 ?  131  PRO B CD  1 
ATOM   5755  N N   . ILE B  2  132 ? 29.473  9.843   100.046 1.00 102.83 ?  132  ILE B N   1 
ATOM   5756  C CA  . ILE B  2  132 ? 30.252  10.354  98.922  1.00 100.93 ?  132  ILE B CA  1 
ATOM   5757  C C   . ILE B  2  132 ? 31.714  10.368  99.363  1.00 101.20 ?  132  ILE B C   1 
ATOM   5758  O O   . ILE B  2  132 ? 32.065  11.137  100.274 1.00 102.47 ?  132  ILE B O   1 
ATOM   5759  C CB  . ILE B  2  132 ? 29.785  11.751  98.492  1.00 100.58 ?  132  ILE B CB  1 
ATOM   5760  C CG1 . ILE B  2  132 ? 28.512  11.668  97.641  1.00 99.75  ?  132  ILE B CG1 1 
ATOM   5761  C CG2 . ILE B  2  132 ? 30.877  12.470  97.714  1.00 99.28  ?  132  ILE B CG2 1 
ATOM   5762  C CD1 . ILE B  2  132 ? 27.244  11.479  98.444  1.00 101.34 ?  132  ILE B CD1 1 
ATOM   5763  N N   . PRO B  2  133 ? 32.574  9.520   98.799  1.00 100.22 ?  133  PRO B N   1 
ATOM   5764  C CA  . PRO B  2  133 ? 33.954  9.430   99.291  1.00 100.68 ?  133  PRO B CA  1 
ATOM   5765  C C   . PRO B  2  133 ? 34.664  10.775  99.254  1.00 100.46 ?  133  PRO B C   1 
ATOM   5766  O O   . PRO B  2  133 ? 34.548  11.536  98.292  1.00 99.18  ?  133  PRO B O   1 
ATOM   5767  C CB  . PRO B  2  133 ? 34.615  8.430   98.333  1.00 99.38  ?  133  PRO B CB  1 
ATOM   5768  C CG  . PRO B  2  133 ? 33.506  7.801   97.539  1.00 98.49  ?  133  PRO B CG  1 
ATOM   5769  C CD  . PRO B  2  133 ? 32.193  8.348   97.996  1.00 99.23  ?  133  PRO B CD  1 
ATOM   5770  N N   . SER B  2  134 ? 35.403  11.061  100.327 1.00 100.00 ?  134  SER B N   1 
ATOM   5771  C CA  . SER B  2  134 ? 36.209  12.273  100.404 1.00 99.43  ?  134  SER B CA  1 
ATOM   5772  C C   . SER B  2  134 ? 37.419  12.231  99.480  1.00 99.01  ?  134  SER B C   1 
ATOM   5773  O O   . SER B  2  134 ? 38.096  13.253  99.327  1.00 98.65  ?  134  SER B O   1 
ATOM   5774  C CB  . SER B  2  134 ? 36.664  12.506  101.845 1.00 100.03 ?  134  SER B CB  1 
ATOM   5775  O OG  . SER B  2  134 ? 37.506  11.455  102.287 1.00 100.76 ?  134  SER B OG  1 
ATOM   5776  N N   . THR B  2  135 ? 37.706  11.080  98.871  1.00 95.96  ?  135  THR B N   1 
ATOM   5777  C CA  . THR B  2  135 ? 38.861  10.938  97.996  1.00 95.82  ?  135  THR B CA  1 
ATOM   5778  C C   . THR B  2  135 ? 38.669  11.608  96.642  1.00 95.05  ?  135  THR B C   1 
ATOM   5779  O O   . THR B  2  135 ? 39.649  11.755  95.904  1.00 95.00  ?  135  THR B O   1 
ATOM   5780  C CB  . THR B  2  135 ? 39.181  9.458   97.788  1.00 96.58  ?  135  THR B CB  1 
ATOM   5781  O OG1 . THR B  2  135 ? 37.961  8.730   97.607  1.00 96.73  ?  135  THR B OG1 1 
ATOM   5782  C CG2 . THR B  2  135 ? 39.925  8.901   98.992  1.00 97.66  ?  135  THR B CG2 1 
ATOM   5783  N N   . LEU B  2  136 ? 37.444  12.008  96.291  1.00 96.15  ?  136  LEU B N   1 
ATOM   5784  C CA  . LEU B  2  136 ? 37.230  12.704  95.027  1.00 95.65  ?  136  LEU B CA  1 
ATOM   5785  C C   . LEU B  2  136 ? 37.876  14.082  94.998  1.00 95.47  ?  136  LEU B C   1 
ATOM   5786  O O   . LEU B  2  136 ? 37.947  14.688  93.924  1.00 95.31  ?  136  LEU B O   1 
ATOM   5787  C CB  . LEU B  2  136 ? 35.735  12.836  94.730  1.00 95.58  ?  136  LEU B CB  1 
ATOM   5788  C CG  . LEU B  2  136 ? 34.817  11.679  95.124  1.00 96.04  ?  136  LEU B CG  1 
ATOM   5789  C CD1 . LEU B  2  136 ? 33.371  12.140  95.134  1.00 96.24  ?  136  LEU B CD1 1 
ATOM   5790  C CD2 . LEU B  2  136 ? 34.999  10.502  94.182  1.00 96.15  ?  136  LEU B CD2 1 
ATOM   5791  N N   . GLY B  2  137 ? 38.342  14.590  96.139  1.00 95.07  ?  137  GLY B N   1 
ATOM   5792  C CA  . GLY B  2  137 ? 39.047  15.857  96.153  1.00 95.12  ?  137  GLY B CA  1 
ATOM   5793  C C   . GLY B  2  137 ? 40.429  15.812  95.535  1.00 95.35  ?  137  GLY B C   1 
ATOM   5794  O O   . GLY B  2  137 ? 41.019  16.873  95.310  1.00 95.57  ?  137  GLY B O   1 
ATOM   5795  N N   . ARG B  2  138 ? 40.955  14.617  95.259  1.00 93.97  ?  138  ARG B N   1 
ATOM   5796  C CA  . ARG B  2  138 ? 42.221  14.493  94.548  1.00 94.40  ?  138  ARG B CA  1 
ATOM   5797  C C   . ARG B  2  138 ? 42.068  14.689  93.046  1.00 94.23  ?  138  ARG B C   1 
ATOM   5798  O O   . ARG B  2  138 ? 43.069  14.922  92.360  1.00 94.73  ?  138  ARG B O   1 
ATOM   5799  C CB  . ARG B  2  138 ? 42.856  13.128  94.828  1.00 94.97  ?  138  ARG B CB  1 
ATOM   5800  C CG  . ARG B  2  138 ? 42.649  12.626  96.248  1.00 95.26  ?  138  ARG B CG  1 
ATOM   5801  C CD  . ARG B  2  138 ? 43.926  12.027  96.813  1.00 96.32  ?  138  ARG B CD  1 
ATOM   5802  N NE  . ARG B  2  138 ? 44.242  10.744  96.196  1.00 96.91  ?  138  ARG B NE  1 
ATOM   5803  C CZ  . ARG B  2  138 ? 45.357  10.490  95.524  1.00 97.65  ?  138  ARG B CZ  1 
ATOM   5804  N NH1 . ARG B  2  138 ? 46.291  11.412  95.360  1.00 97.94  ?  138  ARG B NH1 1 
ATOM   5805  N NH2 . ARG B  2  138 ? 45.538  9.280   95.002  1.00 98.31  ?  138  ARG B NH2 1 
ATOM   5806  N N   . LEU B  2  139 ? 40.842  14.605  92.526  1.00 94.64  ?  139  LEU B N   1 
ATOM   5807  C CA  . LEU B  2  139 ? 40.581  14.793  91.098  1.00 94.59  ?  139  LEU B CA  1 
ATOM   5808  C C   . LEU B  2  139 ? 40.490  16.291  90.809  1.00 94.76  ?  139  LEU B C   1 
ATOM   5809  O O   . LEU B  2  139 ? 39.426  16.852  90.535  1.00 94.62  ?  139  LEU B O   1 
ATOM   5810  C CB  . LEU B  2  139 ? 39.309  14.065  90.683  1.00 94.22  ?  139  LEU B CB  1 
ATOM   5811  C CG  . LEU B  2  139 ? 39.007  12.741  91.383  1.00 94.21  ?  139  LEU B CG  1 
ATOM   5812  C CD1 . LEU B  2  139 ? 37.584  12.298  91.092  1.00 94.02  ?  139  LEU B CD1 1 
ATOM   5813  C CD2 . LEU B  2  139 ? 39.999  11.680  90.947  1.00 94.64  ?  139  LEU B CD2 1 
ATOM   5814  N N   . LYS B  2  140 ? 41.651  16.947  90.876  1.00 96.07  ?  140  LYS B N   1 
ATOM   5815  C CA  . LYS B  2  140 ? 41.693  18.392  90.693  1.00 96.54  ?  140  LYS B CA  1 
ATOM   5816  C C   . LYS B  2  140 ? 41.330  18.818  89.276  1.00 96.89  ?  140  LYS B C   1 
ATOM   5817  O O   . LYS B  2  140 ? 41.056  20.001  89.058  1.00 97.43  ?  140  LYS B O   1 
ATOM   5818  C CB  . LYS B  2  140 ? 43.079  18.936  91.050  1.00 97.31  ?  140  LYS B CB  1 
ATOM   5819  C CG  . LYS B  2  140 ? 43.617  18.503  92.401  1.00 97.24  ?  140  LYS B CG  1 
ATOM   5820  C CD  . LYS B  2  140 ? 42.776  19.060  93.537  1.00 96.86  ?  140  LYS B CD  1 
ATOM   5821  C CE  . LYS B  2  140 ? 43.456  18.837  94.878  1.00 97.06  ?  140  LYS B CE  1 
ATOM   5822  N NZ  . LYS B  2  140 ? 44.800  19.478  94.930  1.00 98.02  ?  140  LYS B NZ  1 
ATOM   5823  N N   . LYS B  2  141 ? 41.324  17.900  88.310  1.00 90.98  ?  141  LYS B N   1 
ATOM   5824  C CA  . LYS B  2  141 ? 40.927  18.244  86.950  1.00 91.40  ?  141  LYS B CA  1 
ATOM   5825  C C   . LYS B  2  141 ? 39.423  18.132  86.724  1.00 90.97  ?  141  LYS B C   1 
ATOM   5826  O O   . LYS B  2  141 ? 38.952  18.470  85.632  1.00 91.45  ?  141  LYS B O   1 
ATOM   5827  C CB  . LYS B  2  141 ? 41.650  17.361  85.918  1.00 91.69  ?  141  LYS B CB  1 
ATOM   5828  C CG  . LYS B  2  141 ? 43.154  17.090  86.090  1.00 92.28  ?  141  LYS B CG  1 
ATOM   5829  C CD  . LYS B  2  141 ? 43.982  18.292  86.530  1.00 93.10  ?  141  LYS B CD  1 
ATOM   5830  C CE  . LYS B  2  141 ? 44.441  18.153  87.970  1.00 92.82  ?  141  LYS B CE  1 
ATOM   5831  N NZ  . LYS B  2  141 ? 45.466  19.163  88.347  1.00 93.84  ?  141  LYS B NZ  1 
ATOM   5832  N N   . LEU B  2  142 ? 38.671  17.653  87.716  1.00 92.20  ?  142  LEU B N   1 
ATOM   5833  C CA  . LEU B  2  142 ? 37.237  17.420  87.564  1.00 91.99  ?  142  LEU B CA  1 
ATOM   5834  C C   . LEU B  2  142 ? 36.496  18.704  87.202  1.00 92.68  ?  142  LEU B C   1 
ATOM   5835  O O   . LEU B  2  142 ? 36.707  19.752  87.818  1.00 93.07  ?  142  LEU B O   1 
ATOM   5836  C CB  . LEU B  2  142 ? 36.676  16.833  88.861  1.00 91.45  ?  142  LEU B CB  1 
ATOM   5837  C CG  . LEU B  2  142 ? 35.182  16.965  89.169  1.00 91.54  ?  142  LEU B CG  1 
ATOM   5838  C CD1 . LEU B  2  142 ? 34.344  16.248  88.126  1.00 91.62  ?  142  LEU B CD1 1 
ATOM   5839  C CD2 . LEU B  2  142 ? 34.872  16.445  90.563  1.00 91.24  ?  142  LEU B CD2 1 
ATOM   5840  N N   . ARG B  2  143 ? 35.618  18.614  86.202  1.00 93.56  ?  143  ARG B N   1 
ATOM   5841  C CA  . ARG B  2  143 ? 34.766  19.729  85.797  1.00 94.51  ?  143  ARG B CA  1 
ATOM   5842  C C   . ARG B  2  143 ? 33.287  19.500  86.066  1.00 94.59  ?  143  ARG B C   1 
ATOM   5843  O O   . ARG B  2  143 ? 32.589  20.435  86.464  1.00 95.33  ?  143  ARG B O   1 
ATOM   5844  C CB  . ARG B  2  143 ? 34.942  20.029  84.304  1.00 95.35  ?  143  ARG B CB  1 
ATOM   5845  C CG  . ARG B  2  143 ? 36.361  20.315  83.852  1.00 95.68  ?  143  ARG B CG  1 
ATOM   5846  C CD  . ARG B  2  143 ? 36.331  21.120  82.561  1.00 97.06  ?  143  ARG B CD  1 
ATOM   5847  N NE  . ARG B  2  143 ? 37.587  21.060  81.825  1.00 97.51  ?  143  ARG B NE  1 
ATOM   5848  C CZ  . ARG B  2  143 ? 37.855  21.781  80.746  1.00 98.93  ?  143  ARG B CZ  1 
ATOM   5849  N NH1 . ARG B  2  143 ? 36.980  22.645  80.257  1.00 100.10 ?  143  ARG B NH1 1 
ATOM   5850  N NH2 . ARG B  2  143 ? 39.031  21.634  80.142  1.00 99.42  ?  143  ARG B NH2 1 
ATOM   5851  N N   . PHE B  2  144 ? 32.786  18.284  85.855  1.00 93.05  ?  144  PHE B N   1 
ATOM   5852  C CA  . PHE B  2  144 ? 31.357  17.999  85.926  1.00 93.41  ?  144  PHE B CA  1 
ATOM   5853  C C   . PHE B  2  144 ? 31.132  16.778  86.803  1.00 92.66  ?  144  PHE B C   1 
ATOM   5854  O O   . PHE B  2  144 ? 31.672  15.703  86.523  1.00 92.08  ?  144  PHE B O   1 
ATOM   5855  C CB  . PHE B  2  144 ? 30.772  17.760  84.530  1.00 94.04  ?  144  PHE B CB  1 
ATOM   5856  C CG  . PHE B  2  144 ? 31.350  18.647  83.465  1.00 94.78  ?  144  PHE B CG  1 
ATOM   5857  C CD1 . PHE B  2  144 ? 31.056  20.000  83.434  1.00 95.93  ?  144  PHE B CD1 1 
ATOM   5858  C CD2 . PHE B  2  144 ? 32.184  18.125  82.490  1.00 94.56  ?  144  PHE B CD2 1 
ATOM   5859  C CE1 . PHE B  2  144 ? 31.586  20.816  82.452  1.00 96.91  ?  144  PHE B CE1 1 
ATOM   5860  C CE2 . PHE B  2  144 ? 32.717  18.935  81.506  1.00 95.48  ?  144  PHE B CE2 1 
ATOM   5861  C CZ  . PHE B  2  144 ? 32.417  20.283  81.487  1.00 96.68  ?  144  PHE B CZ  1 
ATOM   5862  N N   . LEU B  2  145 ? 30.324  16.938  87.850  1.00 95.48  ?  145  LEU B N   1 
ATOM   5863  C CA  . LEU B  2  145 ? 29.984  15.848  88.761  1.00 95.12  ?  145  LEU B CA  1 
ATOM   5864  C C   . LEU B  2  145 ? 28.477  15.860  88.983  1.00 96.04  ?  145  LEU B C   1 
ATOM   5865  O O   . LEU B  2  145 ? 27.948  16.774  89.624  1.00 96.68  ?  145  LEU B O   1 
ATOM   5866  C CB  . LEU B  2  145 ? 30.740  15.983  90.084  1.00 94.63  ?  145  LEU B CB  1 
ATOM   5867  C CG  . LEU B  2  145 ? 30.576  14.864  91.115  1.00 94.44  ?  145  LEU B CG  1 
ATOM   5868  C CD1 . LEU B  2  145 ? 31.908  14.547  91.770  1.00 93.81  ?  145  LEU B CD1 1 
ATOM   5869  C CD2 . LEU B  2  145 ? 29.549  15.243  92.167  1.00 95.12  ?  145  LEU B CD2 1 
ATOM   5870  N N   . ARG B  2  146 ? 27.790  14.846  88.457  1.00 95.39  ?  146  ARG B N   1 
ATOM   5871  C CA  . ARG B  2  146 ? 26.336  14.738  88.553  1.00 96.52  ?  146  ARG B CA  1 
ATOM   5872  C C   . ARG B  2  146 ? 25.985  13.390  89.169  1.00 96.54  ?  146  ARG B C   1 
ATOM   5873  O O   . ARG B  2  146 ? 26.217  12.344  88.553  1.00 96.26  ?  146  ARG B O   1 
ATOM   5874  C CB  . ARG B  2  146 ? 25.682  14.898  87.180  1.00 97.29  ?  146  ARG B CB  1 
ATOM   5875  C CG  . ARG B  2  146 ? 25.999  16.215  86.489  1.00 97.62  ?  146  ARG B CG  1 
ATOM   5876  C CD  . ARG B  2  146 ? 25.648  16.157  85.012  1.00 98.27  ?  146  ARG B CD  1 
ATOM   5877  N NE  . ARG B  2  146 ? 26.274  17.235  84.256  1.00 98.53  ?  146  ARG B NE  1 
ATOM   5878  C CZ  . ARG B  2  146 ? 27.425  17.127  83.607  1.00 97.77  ?  146  ARG B CZ  1 
ATOM   5879  N NH1 . ARG B  2  146 ? 28.117  16.000  83.609  1.00 96.66  ?  146  ARG B NH1 1 
ATOM   5880  N NH2 . ARG B  2  146 ? 27.892  18.177  82.937  1.00 98.37  ?  146  ARG B NH2 1 
ATOM   5881  N N   . LEU B  2  147 ? 25.424  13.414  90.380  1.00 100.31 ?  147  LEU B N   1 
ATOM   5882  C CA  . LEU B  2  147 ? 25.058  12.201  91.105  1.00 99.89  ?  147  LEU B CA  1 
ATOM   5883  C C   . LEU B  2  147 ? 23.581  12.176  91.484  1.00 101.21 ?  147  LEU B C   1 
ATOM   5884  O O   . LEU B  2  147 ? 23.191  11.427  92.385  1.00 101.76 ?  147  LEU B O   1 
ATOM   5885  C CB  . LEU B  2  147 ? 25.919  12.044  92.360  1.00 101.11 ?  147  LEU B CB  1 
ATOM   5886  C CG  . LEU B  2  147 ? 27.412  12.351  92.242  1.00 100.61 ?  147  LEU B CG  1 
ATOM   5887  C CD1 . LEU B  2  147 ? 28.101  12.155  93.582  1.00 102.13 ?  147  LEU B CD1 1 
ATOM   5888  C CD2 . LEU B  2  147 ? 28.062  11.483  91.177  1.00 97.64  ?  147  LEU B CD2 1 
ATOM   5889  N N   . ASN B  2  148 ? 22.750  12.974  90.818  1.00 104.34 ?  148  ASN B N   1 
ATOM   5890  C CA  . ASN B  2  148 ? 21.371  13.137  91.251  1.00 106.04 ?  148  ASN B CA  1 
ATOM   5891  C C   . ASN B  2  148 ? 20.554  11.870  90.986  1.00 104.38 ?  148  ASN B C   1 
ATOM   5892  O O   . ASN B  2  148 ? 21.007  10.921  90.338  1.00 101.87 ?  148  ASN B O   1 
ATOM   5893  C CB  . ASN B  2  148 ? 20.731  14.337  90.554  1.00 107.25 ?  148  ASN B CB  1 
ATOM   5894  C CG  . ASN B  2  148 ? 20.824  14.254  89.045  1.00 105.03 ?  148  ASN B CG  1 
ATOM   5895  O OD1 . ASN B  2  148 ? 21.908  14.368  88.472  1.00 103.74 ?  148  ASN B OD1 1 
ATOM   5896  N ND2 . ASN B  2  148 ? 19.686  14.053  88.390  1.00 104.68 ?  148  ASN B ND2 1 
ATOM   5897  N N   . ASN B  2  149 ? 19.324  11.879  91.500  1.00 105.33 ?  149  ASN B N   1 
ATOM   5898  C CA  . ASN B  2  149 ? 18.379  10.766  91.386  1.00 104.23 ?  149  ASN B CA  1 
ATOM   5899  C C   . ASN B  2  149 ? 19.020  9.446   91.820  1.00 102.65 ?  149  ASN B C   1 
ATOM   5900  O O   . ASN B  2  149 ? 19.134  8.489   91.052  1.00 100.20 ?  149  ASN B O   1 
ATOM   5901  C CB  . ASN B  2  149 ? 17.820  10.669  89.965  1.00 102.47 ?  149  ASN B CB  1 
ATOM   5902  C CG  . ASN B  2  149 ? 16.631  11.584  89.743  1.00 104.34 ?  149  ASN B CG  1 
ATOM   5903  O OD1 . ASN B  2  149 ? 16.667  12.765  90.091  1.00 106.55 ?  149  ASN B OD1 1 
ATOM   5904  N ND2 . ASN B  2  149 ? 15.567  11.041  89.163  1.00 103.56 ?  149  ASN B ND2 1 
ATOM   5905  N N   . ASN B  2  150 ? 19.440  9.414   93.082  1.00 106.48 ?  150  ASN B N   1 
ATOM   5906  C CA  . ASN B  2  150 ? 20.082  8.242   93.663  1.00 105.52 ?  150  ASN B CA  1 
ATOM   5907  C C   . ASN B  2  150 ? 19.595  8.091   95.101  1.00 107.97 ?  150  ASN B C   1 
ATOM   5908  O O   . ASN B  2  150 ? 18.692  8.802   95.553  1.00 110.16 ?  150  ASN B O   1 
ATOM   5909  C CB  . ASN B  2  150 ? 21.609  8.364   93.571  1.00 104.68 ?  150  ASN B CB  1 
ATOM   5910  C CG  . ASN B  2  150 ? 22.173  7.702   92.334  1.00 101.65 ?  150  ASN B CG  1 
ATOM   5911  O OD1 . ASN B  2  150 ? 22.491  6.514   92.344  1.00 100.14 ?  150  ASN B OD1 1 
ATOM   5912  N ND2 . ASN B  2  150 ? 22.299  8.468   91.256  1.00 100.90 ?  150  ASN B ND2 1 
ATOM   5913  N N   . SER B  2  151 ? 20.201  7.149   95.825  1.00 107.65 ?  151  SER B N   1 
ATOM   5914  C CA  . SER B  2  151 ? 19.909  6.913   97.234  1.00 110.02 ?  151  SER B CA  1 
ATOM   5915  C C   . SER B  2  151 ? 21.097  7.264   98.128  1.00 111.44 ?  151  SER B C   1 
ATOM   5916  O O   . SER B  2  151 ? 21.316  6.624   99.159  1.00 112.55 ?  151  SER B O   1 
ATOM   5917  C CB  . SER B  2  151 ? 19.484  5.462   97.455  1.00 108.99 ?  151  SER B CB  1 
ATOM   5918  O OG  . SER B  2  151 ? 18.955  5.277   98.756  1.00 111.49 ?  151  SER B OG  1 
ATOM   5919  N N   . LEU B  2  152 ? 21.870  8.276   97.742  1.00 111.93 ?  152  LEU B N   1 
ATOM   5920  C CA  . LEU B  2  152 ? 23.070  8.639   98.483  1.00 113.13 ?  152  LEU B CA  1 
ATOM   5921  C C   . LEU B  2  152 ? 22.711  9.314   99.803  1.00 116.63 ?  152  LEU B C   1 
ATOM   5922  O O   . LEU B  2  152 ? 21.714  10.032  99.911  1.00 118.24 ?  152  LEU B O   1 
ATOM   5923  C CB  . LEU B  2  152 ? 23.951  9.565   97.642  1.00 112.25 ?  152  LEU B CB  1 
ATOM   5924  C CG  . LEU B  2  152 ? 25.046  8.934   96.773  1.00 109.44 ?  152  LEU B CG  1 
ATOM   5925  C CD1 . LEU B  2  152 ? 24.565  7.658   96.108  1.00 107.02 ?  152  LEU B CD1 1 
ATOM   5926  C CD2 . LEU B  2  152 ? 25.523  9.923   95.720  1.00 108.54 ?  152  LEU B CD2 1 
ATOM   5927  N N   . SER B  2  153 ? 23.545  9.082   100.816 1.00 115.48 ?  153  SER B N   1 
ATOM   5928  C CA  . SER B  2  153 ? 23.311  9.610   102.153 1.00 118.94 ?  153  SER B CA  1 
ATOM   5929  C C   . SER B  2  153 ? 24.637  9.966   102.807 1.00 120.10 ?  153  SER B C   1 
ATOM   5930  O O   . SER B  2  153 ? 25.605  9.205   102.717 1.00 118.62 ?  153  SER B O   1 
ATOM   5931  C CB  . SER B  2  153 ? 22.550  8.602   103.024 1.00 119.96 ?  153  SER B CB  1 
ATOM   5932  O OG  . SER B  2  153 ? 23.194  7.340   103.023 1.00 118.24 ?  153  SER B OG  1 
ATOM   5933  N N   . GLY B  2  154 ? 24.672  11.111  103.465 1.00 124.48 ?  154  GLY B N   1 
ATOM   5934  C CA  . GLY B  2  154 ? 25.875  11.598  104.113 1.00 125.91 ?  154  GLY B CA  1 
ATOM   5935  C C   . GLY B  2  154 ? 25.927  13.117  104.063 1.00 127.67 ?  154  GLY B C   1 
ATOM   5936  O O   . GLY B  2  154 ? 24.895  13.784  104.113 1.00 129.16 ?  154  GLY B O   1 
ATOM   5937  N N   . GLU B  2  155 ? 27.149  13.639  103.969 1.00 124.63 ?  155  GLU B N   1 
ATOM   5938  C CA  . GLU B  2  155 ? 27.383  15.074  103.891 1.00 126.23 ?  155  GLU B CA  1 
ATOM   5939  C C   . GLU B  2  155 ? 28.446  15.345  102.835 1.00 123.85 ?  155  GLU B C   1 
ATOM   5940  O O   . GLU B  2  155 ? 29.296  14.494  102.559 1.00 121.79 ?  155  GLU B O   1 
ATOM   5941  C CB  . GLU B  2  155 ? 27.809  15.645  105.254 1.00 129.76 ?  155  GLU B CB  1 
ATOM   5942  C CG  . GLU B  2  155 ? 27.919  17.164  105.306 1.00 131.91 ?  155  GLU B CG  1 
ATOM   5943  C CD  . GLU B  2  155 ? 28.217  17.683  106.700 1.00 135.63 ?  155  GLU B CD  1 
ATOM   5944  O OE1 . GLU B  2  155 ? 29.102  17.113  107.373 1.00 135.96 ?  155  GLU B OE1 1 
ATOM   5945  O OE2 . GLU B  2  155 ? 27.567  18.662  107.122 1.00 138.34 -1 155  GLU B OE2 1 
ATOM   5946  N N   . ILE B  2  156 ? 28.390  16.537  102.246 1.00 123.75 ?  156  ILE B N   1 
ATOM   5947  C CA  . ILE B  2  156 ? 29.308  16.926  101.177 1.00 121.69 ?  156  ILE B CA  1 
ATOM   5948  C C   . ILE B  2  156 ? 30.691  17.184  101.765 1.00 122.60 ?  156  ILE B C   1 
ATOM   5949  O O   . ILE B  2  156 ? 30.839  18.040  102.650 1.00 125.53 ?  156  ILE B O   1 
ATOM   5950  C CB  . ILE B  2  156 ? 28.796  18.161  100.417 1.00 122.21 ?  156  ILE B CB  1 
ATOM   5951  C CG1 . ILE B  2  156 ? 27.472  17.854  99.712  1.00 121.11 ?  156  ILE B CG1 1 
ATOM   5952  C CG2 . ILE B  2  156 ? 29.838  18.638  99.417  1.00 120.48 ?  156  ILE B CG2 1 
ATOM   5953  C CD1 . ILE B  2  156 ? 26.245  18.202  100.525 1.00 123.88 ?  156  ILE B CD1 1 
ATOM   5954  N N   . PRO B  2  157 ? 31.721  16.466  101.316 1.00 120.10 ?  157  PRO B N   1 
ATOM   5955  C CA  . PRO B  2  157 ? 33.068  16.684  101.860 1.00 120.97 ?  157  PRO B CA  1 
ATOM   5956  C C   . PRO B  2  157 ? 33.579  18.089  101.573 1.00 122.07 ?  157  PRO B C   1 
ATOM   5957  O O   . PRO B  2  157 ? 33.293  18.680  100.529 1.00 120.92 ?  157  PRO B O   1 
ATOM   5958  C CB  . PRO B  2  157 ? 33.927  15.632  101.147 1.00 117.89 ?  157  PRO B CB  1 
ATOM   5959  C CG  . PRO B  2  157 ? 32.994  14.687  100.497 1.00 115.73 ?  157  PRO B CG  1 
ATOM   5960  C CD  . PRO B  2  157 ? 31.629  15.284  100.444 1.00 116.87 ?  157  PRO B CD  1 
ATOM   5961  N N   . ARG B  2  158 ? 34.346  18.622  102.528 1.00 124.46 ?  158  ARG B N   1 
ATOM   5962  C CA  . ARG B  2  158 ? 35.035  19.891  102.311 1.00 125.50 ?  158  ARG B CA  1 
ATOM   5963  C C   . ARG B  2  158 ? 36.049  19.784  101.178 1.00 122.69 ?  158  ARG B C   1 
ATOM   5964  O O   . ARG B  2  158 ? 36.352  20.785  100.517 1.00 122.69 ?  158  ARG B O   1 
ATOM   5965  C CB  . ARG B  2  158 ? 35.712  20.340  103.612 1.00 128.60 ?  158  ARG B CB  1 
ATOM   5966  C CG  . ARG B  2  158 ? 36.642  21.546  103.491 1.00 129.71 ?  158  ARG B CG  1 
ATOM   5967  C CD  . ARG B  2  158 ? 38.103  21.121  103.391 1.00 128.41 ?  158  ARG B CD  1 
ATOM   5968  N NE  . ARG B  2  158 ? 38.929  22.134  102.744 1.00 128.21 ?  158  ARG B NE  1 
ATOM   5969  C CZ  . ARG B  2  158 ? 40.170  21.930  102.322 1.00 126.69 ?  158  ARG B CZ  1 
ATOM   5970  N NH1 . ARG B  2  158 ? 40.761  20.754  102.456 1.00 125.21 ?  158  ARG B NH1 1 
ATOM   5971  N NH2 . ARG B  2  158 ? 40.833  22.931  101.750 1.00 126.74 ?  158  ARG B NH2 1 
ATOM   5972  N N   . SER B  2  159 ? 36.574  18.579  100.934 1.00 120.40 ?  159  SER B N   1 
ATOM   5973  C CA  . SER B  2  159 ? 37.598  18.393  99.910  1.00 117.84 ?  159  SER B CA  1 
ATOM   5974  C C   . SER B  2  159 ? 37.097  18.781  98.525  1.00 115.88 ?  159  SER B C   1 
ATOM   5975  O O   . SER B  2  159 ? 37.880  19.261  97.696  1.00 114.77 ?  159  SER B O   1 
ATOM   5976  C CB  . SER B  2  159 ? 38.080  16.942  99.912  1.00 115.88 ?  159  SER B CB  1 
ATOM   5977  O OG  . SER B  2  159 ? 37.021  16.053  99.600  1.00 114.46 ?  159  SER B OG  1 
ATOM   5978  N N   . LEU B  2  160 ? 35.805  18.587  98.252  1.00 119.00 ?  160  LEU B N   1 
ATOM   5979  C CA  . LEU B  2  160 ? 35.246  18.927  96.948  1.00 117.32 ?  160  LEU B CA  1 
ATOM   5980  C C   . LEU B  2  160 ? 35.287  20.421  96.656  1.00 118.92 ?  160  LEU B C   1 
ATOM   5981  O O   . LEU B  2  160 ? 35.060  20.814  95.507  1.00 117.64 ?  160  LEU B O   1 
ATOM   5982  C CB  . LEU B  2  160 ? 33.806  18.422  96.840  1.00 116.98 ?  160  LEU B CB  1 
ATOM   5983  C CG  . LEU B  2  160 ? 33.610  16.904  96.832  1.00 114.97 ?  160  LEU B CG  1 
ATOM   5984  C CD1 . LEU B  2  160 ? 32.131  16.553  96.869  1.00 115.14 ?  160  LEU B CD1 1 
ATOM   5985  C CD2 . LEU B  2  160 ? 34.282  16.285  95.615  1.00 111.81 ?  160  LEU B CD2 1 
ATOM   5986  N N   . THR B  2  161 ? 35.554  21.259  97.657  1.00 119.44 ?  161  THR B N   1 
ATOM   5987  C CA  . THR B  2  161 ? 35.665  22.695  97.440  1.00 121.18 ?  161  THR B CA  1 
ATOM   5988  C C   . THR B  2  161 ? 37.054  23.125  96.981  1.00 120.46 ?  161  THR B C   1 
ATOM   5989  O O   . THR B  2  161 ? 37.222  24.280  96.578  1.00 121.50 ?  161  THR B O   1 
ATOM   5990  C CB  . THR B  2  161 ? 35.295  23.451  98.719  1.00 124.81 ?  161  THR B CB  1 
ATOM   5991  O OG1 . THR B  2  161 ? 36.313  23.250  99.707  1.00 125.90 ?  161  THR B OG1 1 
ATOM   5992  C CG2 . THR B  2  161 ? 33.965  22.953  99.264  1.00 125.65 ?  161  THR B CG2 1 
ATOM   5993  N N   . ALA B  2  162 ? 38.045  22.237  97.035  1.00 117.74 ?  162  ALA B N   1 
ATOM   5994  C CA  . ALA B  2  162 ? 39.418  22.574  96.682  1.00 117.15 ?  162  ALA B CA  1 
ATOM   5995  C C   . ALA B  2  162 ? 39.774  22.237  95.239  1.00 114.10 ?  162  ALA B C   1 
ATOM   5996  O O   . ALA B  2  162 ? 40.930  22.421  94.845  1.00 113.37 ?  162  ALA B O   1 
ATOM   5997  C CB  . ALA B  2  162 ? 40.392  21.863  97.628  1.00 117.50 ?  162  ALA B CB  1 
ATOM   5998  N N   . VAL B  2  163 ? 38.820  21.745  94.446  1.00 113.59 ?  163  VAL B N   1 
ATOM   5999  C CA  . VAL B  2  163 ? 39.129  21.338  93.078  1.00 110.74 ?  163  VAL B CA  1 
ATOM   6000  C C   . VAL B  2  163 ? 39.406  22.553  92.196  1.00 111.10 ?  163  VAL B C   1 
ATOM   6001  O O   . VAL B  2  163 ? 40.294  22.518  91.337  1.00 109.50 ?  163  VAL B O   1 
ATOM   6002  C CB  . VAL B  2  163 ? 37.991  20.463  92.517  1.00 109.01 ?  163  VAL B CB  1 
ATOM   6003  C CG1 . VAL B  2  163 ? 36.639  21.120  92.752  1.00 110.81 ?  163  VAL B CG1 1 
ATOM   6004  C CG2 . VAL B  2  163 ? 38.204  20.175  91.036  1.00 106.35 ?  163  VAL B CG2 1 
ATOM   6005  N N   . LEU B  2  164 ? 38.648  23.636  92.433  1.00 113.77 ?  164  LEU B N   1 
ATOM   6006  C CA  . LEU B  2  164 ? 38.701  24.955  91.728  1.00 114.81 ?  164  LEU B CA  1 
ATOM   6007  C C   . LEU B  2  164 ? 38.312  24.852  90.241  1.00 112.72 ?  164  LEU B C   1 
ATOM   6008  O O   . LEU B  2  164 ? 38.097  25.916  89.627  1.00 113.76 ?  164  LEU B O   1 
ATOM   6009  C CB  . LEU B  2  164 ? 40.049  25.657  91.946  1.00 115.72 ?  164  LEU B CB  1 
ATOM   6010  C CG  . LEU B  2  164 ? 41.040  25.596  90.783  1.00 113.60 ?  164  LEU B CG  1 
ATOM   6011  C CD1 . LEU B  2  164 ? 40.701  26.634  89.725  1.00 113.99 ?  164  LEU B CD1 1 
ATOM   6012  C CD2 . LEU B  2  164 ? 42.464  25.795  91.278  1.00 114.12 ?  164  LEU B CD2 1 
ATOM   6013  N N   . THR B  2  165 ? 38.213  23.639  89.685  1.00 108.49 ?  165  THR B N   1 
ATOM   6014  C CA  . THR B  2  165 ? 37.824  23.463  88.292  1.00 106.57 ?  165  THR B CA  1 
ATOM   6015  C C   . THR B  2  165 ? 36.399  22.960  88.117  1.00 106.16 ?  165  THR B C   1 
ATOM   6016  O O   . THR B  2  165 ? 35.922  22.902  86.977  1.00 104.90 ?  165  THR B O   1 
ATOM   6017  C CB  . THR B  2  165 ? 38.796  22.517  87.569  1.00 103.81 ?  165  THR B CB  1 
ATOM   6018  O OG1 . THR B  2  165 ? 38.387  21.156  87.751  1.00 102.13 ?  165  THR B OG1 1 
ATOM   6019  C CG2 . THR B  2  165 ? 40.220  22.728  88.066  1.00 104.25 ?  165  THR B CG2 1 
ATOM   6020  N N   . LEU B  2  166 ? 35.723  22.579  89.197  1.00 107.23 ?  166  LEU B N   1 
ATOM   6021  C CA  . LEU B  2  166 ? 34.344  22.116  89.118  1.00 107.03 ?  166  LEU B CA  1 
ATOM   6022  C C   . LEU B  2  166 ? 33.450  23.215  88.558  1.00 108.54 ?  166  LEU B C   1 
ATOM   6023  O O   . LEU B  2  166 ? 33.313  24.283  89.161  1.00 111.18 ?  166  LEU B O   1 
ATOM   6024  C CB  . LEU B  2  166 ? 33.871  21.694  90.508  1.00 108.44 ?  166  LEU B CB  1 
ATOM   6025  C CG  . LEU B  2  166 ? 32.396  21.363  90.741  1.00 108.97 ?  166  LEU B CG  1 
ATOM   6026  C CD1 . LEU B  2  166 ? 31.877  20.432  89.666  1.00 106.30 ?  166  LEU B CD1 1 
ATOM   6027  C CD2 . LEU B  2  166 ? 32.190  20.764  92.124  1.00 110.11 ?  166  LEU B CD2 1 
ATOM   6028  N N   . GLN B  2  167 ? 32.847  22.951  87.399  1.00 107.00 ?  167  GLN B N   1 
ATOM   6029  C CA  . GLN B  2  167 ? 31.950  23.897  86.746  1.00 108.35 ?  167  GLN B CA  1 
ATOM   6030  C C   . GLN B  2  167 ? 30.480  23.557  86.966  1.00 108.89 ?  167  GLN B C   1 
ATOM   6031  O O   . GLN B  2  167 ? 29.686  24.437  87.309  1.00 111.34 ?  167  GLN B O   1 
ATOM   6032  C CB  . GLN B  2  167 ? 32.247  23.954  85.242  1.00 106.61 ?  167  GLN B CB  1 
ATOM   6033  C CG  . GLN B  2  167 ? 33.610  24.526  84.887  1.00 106.46 ?  167  GLN B CG  1 
ATOM   6034  C CD  . GLN B  2  167 ? 33.530  25.962  84.401  1.00 108.54 ?  167  GLN B CD  1 
ATOM   6035  O OE1 . GLN B  2  167 ? 33.211  26.873  85.165  1.00 111.18 ?  167  GLN B OE1 1 
ATOM   6036  N NE2 . GLN B  2  167 ? 33.818  26.169  83.121  1.00 107.50 ?  167  GLN B NE2 1 
ATOM   6037  N N   . VAL B  2  168 ? 30.102  22.295  86.776  1.00 106.73 ?  168  VAL B N   1 
ATOM   6038  C CA  . VAL B  2  168 ? 28.716  21.853  86.883  1.00 106.95 ?  168  VAL B CA  1 
ATOM   6039  C C   . VAL B  2  168 ? 28.620  20.816  87.992  1.00 106.59 ?  168  VAL B C   1 
ATOM   6040  O O   . VAL B  2  168 ? 29.342  19.812  87.975  1.00 104.51 ?  168  VAL B O   1 
ATOM   6041  C CB  . VAL B  2  168 ? 28.198  21.278  85.552  1.00 104.80 ?  168  VAL B CB  1 
ATOM   6042  C CG1 . VAL B  2  168 ? 26.726  20.914  85.667  1.00 105.26 ?  168  VAL B CG1 1 
ATOM   6043  C CG2 . VAL B  2  168 ? 28.420  22.272  84.421  1.00 105.18 ?  168  VAL B CG2 1 
ATOM   6044  N N   . LEU B  2  169 ? 27.706  21.043  88.934  1.00 108.71 ?  169  LEU B N   1 
ATOM   6045  C CA  . LEU B  2  169 ? 27.528  20.193  90.102  1.00 108.95 ?  169  LEU B CA  1 
ATOM   6046  C C   . LEU B  2  169 ? 26.042  19.934  90.298  1.00 109.73 ?  169  LEU B C   1 
ATOM   6047  O O   . LEU B  2  169 ? 25.215  20.820  90.061  1.00 111.45 ?  169  LEU B O   1 
ATOM   6048  C CB  . LEU B  2  169 ? 28.143  20.856  91.351  1.00 111.38 ?  169  LEU B CB  1 
ATOM   6049  C CG  . LEU B  2  169 ? 28.378  20.110  92.670  1.00 111.95 ?  169  LEU B CG  1 
ATOM   6050  C CD1 . LEU B  2  169 ? 27.090  19.903  93.456  1.00 113.57 ?  169  LEU B CD1 1 
ATOM   6051  C CD2 . LEU B  2  169 ? 29.071  18.786  92.413  1.00 109.10 ?  169  LEU B CD2 1 
ATOM   6052  N N   . ASP B  2  170 ? 25.703  18.717  90.721  1.00 109.04 ?  170  ASP B N   1 
ATOM   6053  C CA  . ASP B  2  170 ? 24.300  18.351  90.911  1.00 109.62 ?  170  ASP B CA  1 
ATOM   6054  C C   . ASP B  2  170 ? 24.213  17.162  91.854  1.00 109.14 ?  170  ASP B C   1 
ATOM   6055  O O   . ASP B  2  170 ? 24.736  16.088  91.542  1.00 106.72 ?  170  ASP B O   1 
ATOM   6056  C CB  . ASP B  2  170 ? 23.643  18.024  89.568  1.00 107.72 ?  170  ASP B CB  1 
ATOM   6057  C CG  . ASP B  2  170 ? 22.137  17.897  89.672  1.00 108.69 ?  170  ASP B CG  1 
ATOM   6058  O OD1 . ASP B  2  170 ? 21.568  18.371  90.677  1.00 111.24 ?  170  ASP B OD1 1 
ATOM   6059  O OD2 . ASP B  2  170 ? 21.522  17.326  88.746  1.00 107.00 -1 170  ASP B OD2 1 
ATOM   6060  N N   . LEU B  2  171 ? 23.549  17.350  93.000  1.00 111.06 ?  171  LEU B N   1 
ATOM   6061  C CA  . LEU B  2  171 ? 23.287  16.279  93.957  1.00 111.05 ?  171  LEU B CA  1 
ATOM   6062  C C   . LEU B  2  171 ? 21.803  16.199  94.302  1.00 112.45 ?  171  LEU B C   1 
ATOM   6063  O O   . LEU B  2  171 ? 21.439  15.845  95.426  1.00 113.97 ?  171  LEU B O   1 
ATOM   6064  C CB  . LEU B  2  171 ? 24.113  16.460  95.233  1.00 112.86 ?  171  LEU B CB  1 
ATOM   6065  C CG  . LEU B  2  171 ? 25.537  15.899  95.330  1.00 111.34 ?  171  LEU B CG  1 
ATOM   6066  C CD1 . LEU B  2  171 ? 25.512  14.378  95.275  1.00 109.10 ?  171  LEU B CD1 1 
ATOM   6067  C CD2 . LEU B  2  171 ? 26.471  16.463  94.271  1.00 109.92 ?  171  LEU B CD2 1 
ATOM   6068  N N   . SER B  2  172 ? 20.938  16.523  93.345  1.00 114.27 ?  172  SER B N   1 
ATOM   6069  C CA  . SER B  2  172 ? 19.504  16.564  93.592  1.00 115.76 ?  172  SER B CA  1 
ATOM   6070  C C   . SER B  2  172 ? 18.945  15.166  93.855  1.00 114.36 ?  172  SER B C   1 
ATOM   6071  O O   . SER B  2  172 ? 19.583  14.147  93.577  1.00 111.91 ?  172  SER B O   1 
ATOM   6072  C CB  . SER B  2  172 ? 18.776  17.202  92.409  1.00 115.58 ?  172  SER B CB  1 
ATOM   6073  O OG  . SER B  2  172 ? 17.376  17.215  92.624  1.00 117.04 ?  172  SER B OG  1 
ATOM   6074  N N   . ASN B  2  173 ? 17.736  15.135  94.425  1.00 119.23 ?  173  ASN B N   1 
ATOM   6075  C CA  . ASN B  2  173 ? 16.978  13.896  94.618  1.00 118.18 ?  173  ASN B CA  1 
ATOM   6076  C C   . ASN B  2  173 ? 17.769  12.871  95.429  1.00 117.38 ?  173  ASN B C   1 
ATOM   6077  O O   . ASN B  2  173 ? 17.822  11.689  95.088  1.00 115.06 ?  173  ASN B O   1 
ATOM   6078  C CB  . ASN B  2  173 ? 16.545  13.302  93.275  1.00 115.49 ?  173  ASN B CB  1 
ATOM   6079  C CG  . ASN B  2  173 ? 15.053  13.048  93.201  1.00 116.15 ?  173  ASN B CG  1 
ATOM   6080  O OD1 . ASN B  2  173 ? 14.429  12.655  94.186  1.00 117.58 ?  173  ASN B OD1 1 
ATOM   6081  N ND2 . ASN B  2  173 ? 14.474  13.264  92.025  1.00 115.20 ?  173  ASN B ND2 1 
ATOM   6082  N N   . ASN B  2  174 ? 18.395  13.329  96.514  1.00 118.62 ?  174  ASN B N   1 
ATOM   6083  C CA  . ASN B  2  174 ? 19.241  12.471  97.327  1.00 118.22 ?  174  ASN B CA  1 
ATOM   6084  C C   . ASN B  2  174 ? 19.129  12.857  98.799  1.00 121.52 ?  174  ASN B C   1 
ATOM   6085  O O   . ASN B  2  174 ? 19.223  14.051  99.134  1.00 123.81 ?  174  ASN B O   1 
ATOM   6086  C CB  . ASN B  2  174 ? 20.696  12.558  96.858  1.00 116.58 ?  174  ASN B CB  1 
ATOM   6087  C CG  . ASN B  2  174 ? 20.984  11.669  95.671  1.00 113.13 ?  174  ASN B CG  1 
ATOM   6088  O OD1 . ASN B  2  174 ? 21.253  10.481  95.830  1.00 111.66 ?  174  ASN B OD1 1 
ATOM   6089  N ND2 . ASN B  2  174 ? 20.928  12.237  94.471  1.00 111.97 ?  174  ASN B ND2 1 
ATOM   6090  N N   . PRO B  2  175 ? 18.947  11.889  99.694  1.00 119.66 ?  175  PRO B N   1 
ATOM   6091  C CA  . PRO B  2  175 ? 18.837  12.185  101.140 1.00 122.96 ?  175  PRO B CA  1 
ATOM   6092  C C   . PRO B  2  175 ? 20.179  12.388  101.844 1.00 123.79 ?  175  PRO B C   1 
ATOM   6093  O O   . PRO B  2  175 ? 20.699  11.529  102.556 1.00 123.78 ?  175  PRO B O   1 
ATOM   6094  C CB  . PRO B  2  175 ? 18.094  10.958  101.672 1.00 122.83 ?  175  PRO B CB  1 
ATOM   6095  C CG  . PRO B  2  175 ? 18.514  9.854   100.754 1.00 119.26 ?  175  PRO B CG  1 
ATOM   6096  C CD  . PRO B  2  175 ? 18.641  10.480  99.391  1.00 117.37 ?  175  PRO B CD  1 
ATOM   6097  N N   . LEU B  2  176 ? 20.769  13.568  101.647 1.00 124.70 ?  176  LEU B N   1 
ATOM   6098  C CA  . LEU B  2  176 ? 21.951  13.957  102.401 1.00 126.04 ?  176  LEU B CA  1 
ATOM   6099  C C   . LEU B  2  176 ? 21.548  14.785  103.621 1.00 130.01 ?  176  LEU B C   1 
ATOM   6100  O O   . LEU B  2  176 ? 20.376  15.102  103.837 1.00 131.69 ?  176  LEU B O   1 
ATOM   6101  C CB  . LEU B  2  176 ? 22.938  14.743  101.534 1.00 124.80 ?  176  LEU B CB  1 
ATOM   6102  C CG  . LEU B  2  176 ? 23.708  14.121  100.363 1.00 121.16 ?  176  LEU B CG  1 
ATOM   6103  C CD1 . LEU B  2  176 ? 24.389  12.829  100.772 1.00 119.85 ?  176  LEU B CD1 1 
ATOM   6104  C CD2 . LEU B  2  176 ? 22.829  13.898  99.158  1.00 119.06 ?  176  LEU B CD2 1 
ATOM   6105  N N   . THR B  2  177 ? 22.544  15.142  104.430 1.00 131.61 ?  177  THR B N   1 
ATOM   6106  C CA  . THR B  2  177 ? 22.335  15.941  105.628 1.00 135.52 ?  177  THR B CA  1 
ATOM   6107  C C   . THR B  2  177 ? 23.483  16.930  105.775 1.00 136.58 ?  177  THR B C   1 
ATOM   6108  O O   . THR B  2  177 ? 24.555  16.761  105.189 1.00 134.40 ?  177  THR B O   1 
ATOM   6109  C CB  . THR B  2  177 ? 22.226  15.066  106.886 1.00 137.17 ?  177  THR B CB  1 
ATOM   6110  O OG1 . THR B  2  177 ? 23.207  14.021  106.832 1.00 135.03 ?  177  THR B OG1 1 
ATOM   6111  C CG2 . THR B  2  177 ? 20.837  14.450  106.996 1.00 137.42 ?  177  THR B CG2 1 
ATOM   6112  N N   . GLY B  2  178 ? 23.244  17.968  106.571 1.00 141.56 ?  178  GLY B N   1 
ATOM   6113  C CA  . GLY B  2  178 ? 24.229  19.007  106.806 1.00 143.06 ?  178  GLY B CA  1 
ATOM   6114  C C   . GLY B  2  178 ? 23.953  20.250  105.983 1.00 143.35 ?  178  GLY B C   1 
ATOM   6115  O O   . GLY B  2  178 ? 23.031  20.312  105.165 1.00 142.28 ?  178  GLY B O   1 
ATOM   6116  N N   . ASP B  2  179 ? 24.785  21.261  106.206 1.00 142.19 ?  179  ASP B N   1 
ATOM   6117  C CA  . ASP B  2  179 ? 24.637  22.539  105.527 1.00 142.92 ?  179  ASP B CA  1 
ATOM   6118  C C   . ASP B  2  179 ? 25.443  22.555  104.234 1.00 139.62 ?  179  ASP B C   1 
ATOM   6119  O O   . ASP B  2  179 ? 26.429  21.828  104.085 1.00 137.44 ?  179  ASP B O   1 
ATOM   6120  C CB  . ASP B  2  179 ? 25.077  23.687  106.436 1.00 146.58 ?  179  ASP B CB  1 
ATOM   6121  C CG  . ASP B  2  179 ? 24.330  23.701  107.756 1.00 150.12 ?  179  ASP B CG  1 
ATOM   6122  O OD1 . ASP B  2  179 ? 23.144  24.092  107.766 1.00 151.71 ?  179  ASP B OD1 1 
ATOM   6123  O OD2 . ASP B  2  179 ? 24.928  23.316  108.783 1.00 151.44 -1 179  ASP B OD2 1 
ATOM   6124  N N   . ILE B  2  180 ? 25.011  23.395  103.297 1.00 139.21 ?  180  ILE B N   1 
ATOM   6125  C CA  . ILE B  2  180 ? 25.673  23.519  101.999 1.00 136.34 ?  180  ILE B CA  1 
ATOM   6126  C C   . ILE B  2  180 ? 27.032  24.171  102.223 1.00 137.00 ?  180  ILE B C   1 
ATOM   6127  O O   . ILE B  2  180 ? 27.095  25.349  102.604 1.00 139.80 ?  180  ILE B O   1 
ATOM   6128  C CB  . ILE B  2  180 ? 24.826  24.335  101.007 1.00 136.46 ?  180  ILE B CB  1 
ATOM   6129  C CG1 . ILE B  2  180 ? 23.622  23.526  100.517 1.00 134.97 ?  180  ILE B CG1 1 
ATOM   6130  C CG2 . ILE B  2  180 ? 25.669  24.780  99.821  1.00 134.41 ?  180  ILE B CG2 1 
ATOM   6131  C CD1 . ILE B  2  180 ? 22.407  23.609  101.422 1.00 137.78 ?  180  ILE B CD1 1 
ATOM   6132  N N   . PRO B  2  181 ? 28.141  23.458  102.013 1.00 135.20 ?  181  PRO B N   1 
ATOM   6133  C CA  . PRO B  2  181 ? 29.461  24.053  102.256 1.00 135.88 ?  181  PRO B CA  1 
ATOM   6134  C C   . PRO B  2  181 ? 29.876  24.974  101.120 1.00 134.96 ?  181  PRO B C   1 
ATOM   6135  O O   . PRO B  2  181 ? 30.223  24.521  100.024 1.00 131.88 ?  181  PRO B O   1 
ATOM   6136  C CB  . PRO B  2  181 ? 30.375  22.824  102.362 1.00 133.54 ?  181  PRO B CB  1 
ATOM   6137  C CG  . PRO B  2  181 ? 29.729  21.814  101.464 1.00 130.48 ?  181  PRO B CG  1 
ATOM   6138  C CD  . PRO B  2  181 ? 28.237  22.072  101.517 1.00 131.86 ?  181  PRO B CD  1 
ATOM   6139  N N   . VAL B  2  182 ? 29.840  26.277  101.378 1.00 136.44 ?  182  VAL B N   1 
ATOM   6140  C CA  . VAL B  2  182 ? 30.475  27.263  100.508 1.00 136.14 ?  182  VAL B CA  1 
ATOM   6141  C C   . VAL B  2  182 ? 31.832  27.556  101.139 1.00 137.02 ?  182  VAL B C   1 
ATOM   6142  O O   . VAL B  2  182 ? 31.976  28.454  101.971 1.00 140.19 ?  182  VAL B O   1 
ATOM   6143  C CB  . VAL B  2  182 ? 29.620  28.518  100.340 1.00 138.72 ?  182  VAL B CB  1 
ATOM   6144  C CG1 . VAL B  2  182 ? 30.335  29.538  99.465  1.00 138.56 ?  182  VAL B CG1 1 
ATOM   6145  C CG2 . VAL B  2  182 ? 28.265  28.156  99.744  1.00 137.89 ?  182  VAL B CG2 1 
ATOM   6146  N N   . ASN B  2  183 ? 32.841  26.783  100.749 1.00 134.30 ?  183  ASN B N   1 
ATOM   6147  C CA  . ASN B  2  183 ? 34.203  26.984  101.224 1.00 134.81 ?  183  ASN B CA  1 
ATOM   6148  C C   . ASN B  2  183 ? 35.066  27.735  100.221 1.00 133.74 ?  183  ASN B C   1 
ATOM   6149  O O   . ASN B  2  183 ? 36.240  27.993  100.501 1.00 134.11 ?  183  ASN B O   1 
ATOM   6150  C CB  . ASN B  2  183 ? 34.847  25.635  101.563 1.00 132.86 ?  183  ASN B CB  1 
ATOM   6151  C CG  . ASN B  2  183 ? 35.948  25.758  102.596 1.00 134.61 ?  183  ASN B CG  1 
ATOM   6152  O OD1 . ASN B  2  183 ? 37.087  25.358  102.357 1.00 132.97 ?  183  ASN B OD1 1 
ATOM   6153  N ND2 . ASN B  2  183 ? 35.611  26.308  103.756 1.00 138.06 ?  183  ASN B ND2 1 
ATOM   6154  N N   . GLY B  2  184 ? 34.510  28.090  99.067  1.00 133.01 ?  184  GLY B N   1 
ATOM   6155  C CA  . GLY B  2  184 ? 35.251  28.729  97.999  1.00 131.83 ?  184  GLY B CA  1 
ATOM   6156  C C   . GLY B  2  184 ? 35.445  27.783  96.834  1.00 128.02 ?  184  GLY B C   1 
ATOM   6157  O O   . GLY B  2  184 ? 36.346  26.939  96.865  1.00 126.15 ?  184  GLY B O   1 
ATOM   6158  N N   . SER B  2  185 ? 34.623  27.981  95.793  1.00 133.54 ?  185  SER B N   1 
ATOM   6159  C CA  . SER B  2  185 ? 34.411  27.153  94.601  1.00 130.26 ?  185  SER B CA  1 
ATOM   6160  C C   . SER B  2  185 ? 32.916  26.898  94.474  1.00 130.47 ?  185  SER B C   1 
ATOM   6161  O O   . SER B  2  185 ? 32.343  27.025  93.388  1.00 129.37 ?  185  SER B O   1 
ATOM   6162  C CB  . SER B  2  185 ? 35.155  25.815  94.631  1.00 127.59 ?  185  SER B CB  1 
ATOM   6163  O OG  . SER B  2  185 ? 36.509  25.975  94.245  1.00 126.58 ?  185  SER B OG  1 
ATOM   6164  N N   . PHE B  2  186 ? 32.281  26.539  95.590  1.00 130.53 ?  186  PHE B N   1 
ATOM   6165  C CA  . PHE B  2  186 ? 30.837  26.357  95.654  1.00 130.07 ?  186  PHE B CA  1 
ATOM   6166  C C   . PHE B  2  186 ? 30.083  27.678  95.722  1.00 130.64 ?  186  PHE B C   1 
ATOM   6167  O O   . PHE B  2  186 ? 28.847  27.669  95.725  1.00 130.37 ?  186  PHE B O   1 
ATOM   6168  C CB  . PHE B  2  186 ? 30.465  25.486  96.860  1.00 130.78 ?  186  PHE B CB  1 
ATOM   6169  C CG  . PHE B  2  186 ? 30.751  24.019  96.668  1.00 131.17 ?  186  PHE B CG  1 
ATOM   6170  C CD1 . PHE B  2  186 ? 32.020  23.578  96.324  1.00 131.56 ?  186  PHE B CD1 1 
ATOM   6171  C CD2 . PHE B  2  186 ? 29.747  23.080  96.836  1.00 131.69 ?  186  PHE B CD2 1 
ATOM   6172  C CE1 . PHE B  2  186 ? 32.279  22.231  96.149  1.00 132.62 ?  186  PHE B CE1 1 
ATOM   6173  C CE2 . PHE B  2  186 ? 30.001  21.732  96.664  1.00 132.81 ?  186  PHE B CE2 1 
ATOM   6174  C CZ  . PHE B  2  186 ? 31.268  21.307  96.320  1.00 133.37 ?  186  PHE B CZ  1 
ATOM   6175  N N   . SER B  2  187 ? 30.796  28.806  95.781  1.00 127.65 ?  187  SER B N   1 
ATOM   6176  C CA  . SER B  2  187 ? 30.144  30.110  95.836  1.00 129.62 ?  187  SER B CA  1 
ATOM   6177  C C   . SER B  2  187 ? 29.403  30.429  94.545  1.00 128.26 ?  187  SER B C   1 
ATOM   6178  O O   . SER B  2  187 ? 28.436  31.198  94.561  1.00 129.37 ?  187  SER B O   1 
ATOM   6179  C CB  . SER B  2  187 ? 31.177  31.196  96.135  1.00 132.31 ?  187  SER B CB  1 
ATOM   6180  O OG  . SER B  2  187 ? 32.290  31.093  95.262  1.00 131.39 ?  187  SER B OG  1 
ATOM   6181  N N   . LEU B  2  188 ? 29.838  29.855  93.424  1.00 126.57 ?  188  LEU B N   1 
ATOM   6182  C CA  . LEU B  2  188 ? 29.255  30.164  92.126  1.00 125.61 ?  188  LEU B CA  1 
ATOM   6183  C C   . LEU B  2  188 ? 28.008  29.345  91.818  1.00 123.61 ?  188  LEU B C   1 
ATOM   6184  O O   . LEU B  2  188 ? 27.356  29.606  90.802  1.00 123.04 ?  188  LEU B O   1 
ATOM   6185  C CB  . LEU B  2  188 ? 30.285  29.945  91.010  1.00 124.63 ?  188  LEU B CB  1 
ATOM   6186  C CG  . LEU B  2  188 ? 31.625  30.689  91.047  1.00 126.50 ?  188  LEU B CG  1 
ATOM   6187  C CD1 . LEU B  2  188 ? 32.648  29.986  91.933  1.00 126.41 ?  188  LEU B CD1 1 
ATOM   6188  C CD2 . LEU B  2  188 ? 32.171  30.867  89.637  1.00 126.12 ?  188  LEU B CD2 1 
ATOM   6189  N N   . PHE B  2  189 ? 27.660  28.374  92.655  1.00 123.73 ?  189  PHE B N   1 
ATOM   6190  C CA  . PHE B  2  189 ? 26.589  27.446  92.328  1.00 121.87 ?  189  PHE B CA  1 
ATOM   6191  C C   . PHE B  2  189 ? 25.245  27.920  92.877  1.00 122.90 ?  189  PHE B C   1 
ATOM   6192  O O   . PHE B  2  189 ? 25.166  28.728  93.805  1.00 125.09 ?  189  PHE B O   1 
ATOM   6193  C CB  . PHE B  2  189 ? 26.918  26.046  92.844  1.00 120.93 ?  189  PHE B CB  1 
ATOM   6194  C CG  . PHE B  2  189 ? 28.082  25.409  92.141  1.00 120.45 ?  189  PHE B CG  1 
ATOM   6195  C CD1 . PHE B  2  189 ? 29.380  25.640  92.566  1.00 120.97 ?  189  PHE B CD1 1 
ATOM   6196  C CD2 . PHE B  2  189 ? 27.880  24.605  91.033  1.00 119.66 ?  189  PHE B CD2 1 
ATOM   6197  C CE1 . PHE B  2  189 ? 30.452  25.060  91.912  1.00 120.66 ?  189  PHE B CE1 1 
ATOM   6198  C CE2 . PHE B  2  189 ? 28.948  24.028  90.373  1.00 119.43 ?  189  PHE B CE2 1 
ATOM   6199  C CZ  . PHE B  2  189 ? 30.235  24.255  90.814  1.00 119.91 ?  189  PHE B CZ  1 
ATOM   6200  N N   . THR B  2  190 ? 24.175  27.386  92.276  1.00 128.12 ?  190  THR B N   1 
ATOM   6201  C CA  . THR B  2  190 ? 22.768  27.738  92.384  1.00 128.41 ?  190  THR B CA  1 
ATOM   6202  C C   . THR B  2  190 ? 22.004  26.661  93.156  1.00 127.79 ?  190  THR B C   1 
ATOM   6203  O O   . THR B  2  190 ? 22.354  25.479  93.084  1.00 127.39 ?  190  THR B O   1 
ATOM   6204  C CB  . THR B  2  190 ? 22.180  27.897  90.971  1.00 129.01 ?  190  THR B CB  1 
ATOM   6205  O OG1 . THR B  2  190 ? 22.858  28.961  90.290  1.00 130.31 ?  190  THR B OG1 1 
ATOM   6206  C CG2 . THR B  2  190 ? 20.687  28.201  90.992  1.00 129.49 ?  190  THR B CG2 1 
ATOM   6207  N N   . PRO B  2  191 ? 20.969  27.034  93.919  1.00 125.06 ?  191  PRO B N   1 
ATOM   6208  C CA  . PRO B  2  191 ? 20.210  26.028  94.685  1.00 124.91 ?  191  PRO B CA  1 
ATOM   6209  C C   . PRO B  2  191 ? 19.613  24.895  93.854  1.00 123.96 ?  191  PRO B C   1 
ATOM   6210  O O   . PRO B  2  191 ? 19.105  23.934  94.446  1.00 124.09 ?  191  PRO B O   1 
ATOM   6211  C CB  . PRO B  2  191 ? 19.103  26.858  95.359  1.00 125.92 ?  191  PRO B CB  1 
ATOM   6212  C CG  . PRO B  2  191 ? 19.222  28.257  94.775  1.00 126.63 ?  191  PRO B CG  1 
ATOM   6213  C CD  . PRO B  2  191 ? 20.653  28.392  94.385  1.00 126.41 ?  191  PRO B CD  1 
ATOM   6214  N N   . ILE B  2  192 ? 19.645  24.969  92.521  1.00 123.00 ?  192  ILE B N   1 
ATOM   6215  C CA  . ILE B  2  192 ? 19.195  23.831  91.723  1.00 122.84 ?  192  ILE B CA  1 
ATOM   6216  C C   . ILE B  2  192 ? 20.165  22.663  91.868  1.00 122.80 ?  192  ILE B C   1 
ATOM   6217  O O   . ILE B  2  192 ? 19.768  21.497  91.753  1.00 123.00 ?  192  ILE B O   1 
ATOM   6218  C CB  . ILE B  2  192 ? 19.018  24.246  90.250  1.00 123.19 ?  192  ILE B CB  1 
ATOM   6219  C CG1 . ILE B  2  192 ? 18.046  25.423  90.141  1.00 123.88 ?  192  ILE B CG1 1 
ATOM   6220  C CG2 . ILE B  2  192 ? 18.516  23.079  89.410  1.00 123.21 ?  192  ILE B CG2 1 
ATOM   6221  C CD1 . ILE B  2  192 ? 17.709  25.806  88.717  1.00 124.96 ?  192  ILE B CD1 1 
ATOM   6222  N N   . SER B  2  193 ? 21.439  22.950  92.144  1.00 120.45 ?  193  SER B N   1 
ATOM   6223  C CA  . SER B  2  193 ? 22.418  21.895  92.379  1.00 120.49 ?  193  SER B CA  1 
ATOM   6224  C C   . SER B  2  193 ? 22.141  21.119  93.660  1.00 121.46 ?  193  SER B C   1 
ATOM   6225  O O   . SER B  2  193 ? 22.558  19.962  93.772  1.00 121.93 ?  193  SER B O   1 
ATOM   6226  C CB  . SER B  2  193 ? 23.827  22.486  92.428  1.00 120.55 ?  193  SER B CB  1 
ATOM   6227  O OG  . SER B  2  193 ? 24.137  23.165  91.224  1.00 120.07 ?  193  SER B OG  1 
ATOM   6228  N N   . PHE B  2  194 ? 21.449  21.729  94.625  1.00 122.78 ?  194  PHE B N   1 
ATOM   6229  C CA  . PHE B  2  194 ? 21.206  21.118  95.927  1.00 124.19 ?  194  PHE B CA  1 
ATOM   6230  C C   . PHE B  2  194 ? 19.717  20.965  96.223  1.00 124.52 ?  194  PHE B C   1 
ATOM   6231  O O   . PHE B  2  194 ? 19.332  20.844  97.390  1.00 125.94 ?  194  PHE B O   1 
ATOM   6232  C CB  . PHE B  2  194 ? 21.875  21.933  97.037  1.00 125.23 ?  194  PHE B CB  1 
ATOM   6233  C CG  . PHE B  2  194 ? 23.362  22.087  96.875  1.00 125.10 ?  194  PHE B CG  1 
ATOM   6234  C CD1 . PHE B  2  194 ? 23.889  23.120  96.115  1.00 124.12 ?  194  PHE B CD1 1 
ATOM   6235  C CD2 . PHE B  2  194 ? 24.234  21.207  97.494  1.00 126.30 ?  194  PHE B CD2 1 
ATOM   6236  C CE1 . PHE B  2  194 ? 25.255  23.266  95.969  1.00 124.08 ?  194  PHE B CE1 1 
ATOM   6237  C CE2 . PHE B  2  194 ? 25.603  21.349  97.352  1.00 126.26 ?  194  PHE B CE2 1 
ATOM   6238  C CZ  . PHE B  2  194 ? 26.113  22.380  96.589  1.00 125.02 ?  194  PHE B CZ  1 
ATOM   6239  N N   . ALA B  2  195 ? 18.872  20.970  95.196  1.00 125.38 ?  195  ALA B N   1 
ATOM   6240  C CA  . ALA B  2  195 ? 17.437  20.844  95.406  1.00 125.39 ?  195  ALA B CA  1 
ATOM   6241  C C   . ALA B  2  195 ? 17.065  19.419  95.802  1.00 126.45 ?  195  ALA B C   1 
ATOM   6242  O O   . ALA B  2  195 ? 17.711  18.449  95.399  1.00 126.94 ?  195  ALA B O   1 
ATOM   6243  C CB  . ALA B  2  195 ? 16.675  21.251  94.145  1.00 124.46 ?  195  ALA B CB  1 
ATOM   6244  N N   . ASN B  2  196 ? 16.005  19.304  96.609  1.00 123.06 ?  196  ASN B N   1 
ATOM   6245  C CA  . ASN B  2  196 ? 15.462  18.013  97.042  1.00 124.26 ?  196  ASN B CA  1 
ATOM   6246  C C   . ASN B  2  196 ? 16.512  17.161  97.749  1.00 125.80 ?  196  ASN B C   1 
ATOM   6247  O O   . ASN B  2  196 ? 16.502  15.931  97.648  1.00 126.56 ?  196  ASN B O   1 
ATOM   6248  C CB  . ASN B  2  196 ? 14.851  17.242  95.868  1.00 123.24 ?  196  ASN B CB  1 
ATOM   6249  C CG  . ASN B  2  196 ? 13.785  16.257  96.309  1.00 124.41 ?  196  ASN B CG  1 
ATOM   6250  O OD1 . ASN B  2  196 ? 13.058  16.501  97.272  1.00 125.57 ?  196  ASN B OD1 1 
ATOM   6251  N ND2 . ASN B  2  196 ? 13.689  15.135  95.606  1.00 124.29 ?  196  ASN B ND2 1 
ATOM   6252  N N   . THR B  2  197 ? 17.428  17.805  98.471  1.00 125.99 ?  197  THR B N   1 
ATOM   6253  C CA  . THR B  2  197 ? 18.545  17.117  99.097  1.00 127.63 ?  197  THR B CA  1 
ATOM   6254  C C   . THR B  2  197 ? 18.388  16.950  100.603 1.00 130.43 ?  197  THR B C   1 
ATOM   6255  O O   . THR B  2  197 ? 19.154  16.188  101.206 1.00 132.46 ?  197  THR B O   1 
ATOM   6256  C CB  . THR B  2  197 ? 19.853  17.867  98.791  1.00 126.69 ?  197  THR B CB  1 
ATOM   6257  O OG1 . THR B  2  197 ? 19.837  18.303  97.428  1.00 124.31 ?  197  THR B OG1 1 
ATOM   6258  C CG2 . THR B  2  197 ? 21.058  16.967  98.982  1.00 127.99 ?  197  THR B CG2 1 
ATOM   6259  N N   . LYS B  2  198 ? 17.411  17.618  101.219 1.00 129.32 ?  198  LYS B N   1 
ATOM   6260  C CA  . LYS B  2  198 ? 17.183  17.545  102.664 1.00 132.84 ?  198  LYS B CA  1 
ATOM   6261  C C   . LYS B  2  198 ? 18.413  17.993  103.449 1.00 134.34 ?  198  LYS B C   1 
ATOM   6262  O O   . LYS B  2  198 ? 18.673  17.507  104.553 1.00 137.18 ?  198  LYS B O   1 
ATOM   6263  C CB  . LYS B  2  198 ? 16.751  16.140  103.097 1.00 134.37 ?  198  LYS B CB  1 
ATOM   6264  C CG  . LYS B  2  198 ? 15.646  15.542  102.241 1.00 132.92 ?  198  LYS B CG  1 
ATOM   6265  C CD  . LYS B  2  198 ? 15.475  14.055  102.509 1.00 134.35 ?  198  LYS B CD  1 
ATOM   6266  C CE  . LYS B  2  198 ? 14.527  13.422  101.503 1.00 132.75 ?  198  LYS B CE  1 
ATOM   6267  N NZ  . LYS B  2  198 ? 14.372  11.958  101.726 1.00 134.43 ?  198  LYS B NZ  1 
ATOM   6268  N N   . LEU B  2  199 ? 19.182  18.921  102.878 1.00 134.71 ?  199  LEU B N   1 
ATOM   6269  C CA  . LEU B  2  199 ? 20.370  19.434  103.550 1.00 135.76 ?  199  LEU B CA  1 
ATOM   6270  C C   . LEU B  2  199 ? 19.996  20.397  104.672 1.00 137.84 ?  199  LEU B C   1 
ATOM   6271  O O   . LEU B  2  199 ? 20.327  20.166  105.841 1.00 140.90 ?  199  LEU B O   1 
ATOM   6272  C CB  . LEU B  2  199 ? 21.288  20.116  102.533 1.00 133.23 ?  199  LEU B CB  1 
ATOM   6273  C CG  . LEU B  2  199 ? 22.151  19.192  101.673 1.00 132.50 ?  199  LEU B CG  1 
ATOM   6274  C CD1 . LEU B  2  199 ? 23.109  19.997  100.817 1.00 130.42 ?  199  LEU B CD1 1 
ATOM   6275  C CD2 . LEU B  2  199 ? 22.914  18.215  102.549 1.00 135.34 ?  199  LEU B CD2 1 
ATOM   6276  N N   . THR B  2  200 ? 19.298  21.475  104.335 1.00 137.36 ?  200  THR B N   1 
ATOM   6277  C CA  . THR B  2  200 ? 18.898  22.468  105.324 1.00 140.55 ?  200  THR B CA  1 
ATOM   6278  C C   . THR B  2  200 ? 17.412  22.785  105.201 1.00 140.83 ?  200  THR B C   1 
ATOM   6279  O O   . THR B  2  200 ? 16.636  21.976  104.692 1.00 139.34 ?  200  THR B O   1 
ATOM   6280  C CB  . THR B  2  200 ? 19.709  23.770  105.181 1.00 140.73 ?  200  THR B CB  1 
ATOM   6281  O OG1 . THR B  2  200 ? 21.109  23.477  105.272 1.00 140.50 ?  200  THR B OG1 1 
ATOM   6282  C CG2 . THR B  2  200 ? 19.331  24.756  106.275 1.00 144.54 ?  200  THR B CG2 1 
ATOM   6283  N N   . GLU C  3  1   ? 43.413  -28.791 99.446  1.00 52.25  ?  1    GLU C N   1 
ATOM   6284  C CA  . GLU C  3  1   ? 43.369  -29.316 98.086  1.00 53.15  ?  1    GLU C CA  1 
ATOM   6285  C C   . GLU C  3  1   ? 44.695  -29.061 97.379  1.00 51.70  ?  1    GLU C C   1 
ATOM   6286  O O   . GLU C  3  1   ? 45.632  -28.532 97.977  1.00 50.26  ?  1    GLU C O   1 
ATOM   6287  C CB  . GLU C  3  1   ? 42.219  -28.684 97.298  1.00 52.59  ?  1    GLU C CB  1 
ATOM   6288  C CG  . GLU C  3  1   ? 40.950  -28.447 98.105  1.00 53.47  ?  1    GLU C CG  1 
ATOM   6289  C CD  . GLU C  3  1   ? 40.529  -29.654 98.922  1.00 56.66  ?  1    GLU C CD  1 
ATOM   6290  O OE1 . GLU C  3  1   ? 39.966  -30.602 98.337  1.00 59.56  ?  1    GLU C OE1 1 
ATOM   6291  O OE2 . GLU C  3  1   ? 40.761  -29.654 100.150 1.00 56.59  -1 1    GLU C OE2 1 
ATOM   6292  N N   . SER C  3  2   ? 44.769  -29.437 96.105  1.00 52.48  ?  2    SER C N   1 
ATOM   6293  C CA  . SER C  3  2   ? 45.976  -29.210 95.325  1.00 51.45  ?  2    SER C CA  1 
ATOM   6294  C C   . SER C  3  2   ? 45.622  -29.186 93.848  1.00 51.67  ?  2    SER C C   1 
ATOM   6295  O O   . SER C  3  2   ? 44.715  -29.890 93.398  1.00 54.07  ?  2    SER C O   1 
ATOM   6296  C CB  . SER C  3  2   ? 47.036  -30.284 95.592  1.00 53.98  ?  2    SER C CB  1 
ATOM   6297  O OG  . SER C  3  2   ? 47.713  -30.044 96.812  1.00 53.38  ?  2    SER C OG  1 
ATOM   6298  N N   . SER C  3  3   ? 46.359  -28.367 93.104  1.00 49.48  ?  3    SER C N   1 
ATOM   6299  C CA  . SER C  3  3   ? 46.233  -28.280 91.658  1.00 49.64  ?  3    SER C CA  1 
ATOM   6300  C C   . SER C  3  3   ? 47.431  -27.508 91.133  1.00 47.53  ?  3    SER C C   1 
ATOM   6301  O O   . SER C  3  3   ? 48.079  -26.759 91.870  1.00 45.55  ?  3    SER C O   1 
ATOM   6302  C CB  . SER C  3  3   ? 44.923  -27.603 91.235  1.00 48.78  ?  3    SER C CB  1 
ATOM   6303  O OG  . SER C  3  3   ? 44.740  -26.371 91.911  1.00 45.94  ?  3    SER C OG  1 
ATOM   6304  N N   . SER C  3  4   ? 47.715  -27.698 89.851  1.00 48.34  ?  4    SER C N   1 
ATOM   6305  C CA  . SER C  3  4   ? 48.809  -26.977 89.228  1.00 46.66  ?  4    SER C CA  1 
ATOM   6306  C C   . SER C  3  4   ? 48.347  -25.586 88.809  1.00 43.58  ?  4    SER C C   1 
ATOM   6307  O O   . SER C  3  4   ? 47.166  -25.235 88.898  1.00 43.07  ?  4    SER C O   1 
ATOM   6308  C CB  . SER C  3  4   ? 49.342  -27.746 88.021  1.00 49.15  ?  4    SER C CB  1 
ATOM   6309  O OG  . SER C  3  4   ? 48.338  -27.909 87.035  1.00 50.19  ?  4    SER C OG  1 
ATOM   6310  N N   . SER C  3  5   ? 49.300  -24.783 88.355  1.00 41.93  ?  5    SER C N   1 
ATOM   6311  C CA  . SER C  3  5   ? 49.010  -23.463 87.823  1.00 39.44  ?  5    SER C CA  1 
ATOM   6312  C C   . SER C  3  5   ? 49.064  -23.521 86.305  1.00 40.04  ?  5    SER C C   1 
ATOM   6313  O O   . SER C  3  5   ? 49.925  -24.191 85.731  1.00 41.65  ?  5    SER C O   1 
ATOM   6314  C CB  . SER C  3  5   ? 50.008  -22.430 88.348  1.00 37.53  ?  5    SER C CB  1 
ATOM   6315  O OG  . SER C  3  5   ? 51.345  -22.861 88.152  1.00 38.61  ?  5    SER C OG  1 
ATOM   6316  N N   . HIS C  3  6   ? 48.138  -22.825 85.659  1.00 39.36  ?  6    HIS C N   1 
ATOM   6317  C CA  . HIS C  3  6   ? 48.036  -22.831 84.206  1.00 40.13  ?  6    HIS C CA  1 
ATOM   6318  C C   . HIS C  3  6   ? 48.578  -21.507 83.693  1.00 37.75  ?  6    HIS C C   1 
ATOM   6319  O O   . HIS C  3  6   ? 48.009  -20.447 83.974  1.00 36.06  ?  6    HIS C O   1 
ATOM   6320  C CB  . HIS C  3  6   ? 46.596  -23.056 83.748  1.00 41.58  ?  6    HIS C CB  1 
ATOM   6321  C CG  . HIS C  3  6   ? 46.463  -23.300 82.277  1.00 43.27  ?  6    HIS C CG  1 
ATOM   6322  N ND1 . HIS C  3  6   ? 46.655  -22.310 81.337  1.00 41.83  ?  6    HIS C ND1 1 
ATOM   6323  C CD2 . HIS C  3  6   ? 46.172  -24.425 81.583  1.00 46.66  ?  6    HIS C CD2 1 
ATOM   6324  C CE1 . HIS C  3  6   ? 46.477  -22.812 80.128  1.00 44.11  ?  6    HIS C CE1 1 
ATOM   6325  N NE2 . HIS C  3  6   ? 46.185  -24.095 80.249  1.00 47.19  ?  6    HIS C NE2 1 
ATOM   6326  N N   . SER C  3  7   ? 49.685  -21.570 82.958  1.00 37.80  ?  7    SER C N   1 
ATOM   6327  C CA  . SER C  3  7   ? 50.193  -20.394 82.272  1.00 36.06  ?  7    SER C CA  1 
ATOM   6328  C C   . SER C  3  7   ? 49.174  -19.940 81.240  1.00 36.08  ?  7    SER C C   1 
ATOM   6329  O O   . SER C  3  7   ? 48.933  -20.638 80.249  1.00 38.04  ?  7    SER C O   1 
ATOM   6330  C CB  . SER C  3  7   ? 51.532  -20.693 81.603  1.00 37.00  ?  7    SER C CB  1 
ATOM   6331  O OG  . SER C  3  7   ? 52.109  -19.514 81.068  1.00 35.40  ?  7    SER C OG  1 
ATOM   6332  N N   . GLU C  3  8   ? 48.572  -18.778 81.460  1.00 36.20  ?  8    GLU C N   1 
ATOM   6333  C CA  . GLU C  3  8   ? 47.543  -18.293 80.557  1.00 36.97  ?  8    GLU C CA  1 
ATOM   6334  C C   . GLU C  3  8   ? 48.184  -17.702 79.312  1.00 36.66  ?  8    GLU C C   1 
ATOM   6335  O O   . GLU C  3  8   ? 49.250  -17.082 79.377  1.00 35.46  ?  8    GLU C O   1 
ATOM   6336  C CB  . GLU C  3  8   ? 46.658  -17.259 81.253  1.00 36.66  ?  8    GLU C CB  1 
ATOM   6337  C CG  . GLU C  3  8   ? 45.972  -17.766 82.520  1.00 37.40  ?  8    GLU C CG  1 
ATOM   6338  C CD  . GLU C  3  8   ? 44.966  -18.879 82.258  1.00 40.47  ?  8    GLU C CD  1 
ATOM   6339  O OE1 . GLU C  3  8   ? 45.380  -20.009 81.920  1.00 41.10  ?  8    GLU C OE1 1 
ATOM   6340  O OE2 . GLU C  3  8   ? 43.751  -18.623 82.398  1.00 43.22  -1 8    GLU C OE2 1 
ATOM   6341  N N   . ARG C  3  9   ? 47.531  -17.918 78.171  1.00 36.65  ?  9    ARG C N   1 
ATOM   6342  C CA  . ARG C  3  9   ? 48.025  -17.455 76.881  1.00 36.76  ?  9    ARG C CA  1 
ATOM   6343  C C   . ARG C  3  9   ? 48.296  -15.958 76.902  1.00 34.71  ?  9    ARG C C   1 
ATOM   6344  O O   . ARG C  3  9   ? 47.744  -15.227 77.731  1.00 34.20  ?  9    ARG C O   1 
ATOM   6345  C CB  . ARG C  3  9   ? 47.028  -17.802 75.772  1.00 39.10  ?  9    ARG C CB  1 
ATOM   6346  C CG  . ARG C  3  9   ? 47.528  -18.852 74.794  1.00 41.52  ?  9    ARG C CG  1 
ATOM   6347  C CD  . ARG C  3  9   ? 46.384  -19.628 74.165  1.00 44.80  ?  9    ARG C CD  1 
ATOM   6348  N NE  . ARG C  3  9   ? 45.874  -20.665 75.054  1.00 46.27  ?  9    ARG C NE  1 
ATOM   6349  C CZ  . ARG C  3  9   ? 44.696  -21.257 74.914  1.00 49.11  ?  9    ARG C CZ  1 
ATOM   6350  N NH1 . ARG C  3  9   ? 43.870  -20.928 73.934  1.00 50.92  ?  9    ARG C NH1 1 
ATOM   6351  N NH2 . ARG C  3  9   ? 44.337  -22.201 75.778  1.00 50.51  ?  9    ARG C NH2 1 
ATOM   6352  N N   . ALA C  3  10  ? 49.136  -15.493 75.988  1.00 36.60  ?  10   ALA C N   1 
ATOM   6353  C CA  . ALA C  3  10  ? 49.490  -14.083 75.926  1.00 36.13  ?  10   ALA C CA  1 
ATOM   6354  C C   . ALA C  3  10  ? 48.304  -13.323 75.340  1.00 37.90  ?  10   ALA C C   1 
ATOM   6355  O O   . ALA C  3  10  ? 47.218  -13.872 75.130  1.00 39.31  ?  10   ALA C O   1 
ATOM   6356  C CB  . ALA C  3  10  ? 50.768  -13.889 75.116  1.00 37.03  ?  10   ALA C CB  1 
ATOM   6357  N N   . GLY C  3  11  ? 48.491  -12.038 75.073  1.00 35.07  ?  11   GLY C N   1 
ATOM   6358  C CA  . GLY C  3  11  ? 47.356  -11.208 74.736  1.00 37.21  ?  11   GLY C CA  1 
ATOM   6359  C C   . GLY C  3  11  ? 46.978  -11.343 73.279  1.00 37.94  ?  11   GLY C C   1 
ATOM   6360  O O   . GLY C  3  11  ? 46.832  -12.458 72.772  1.00 38.23  ?  11   GLY C O   1 
ATOM   6361  N N   . GLY C  3  12  ? 46.783  -10.228 72.604  1.00 38.07  ?  12   GLY C N   1 
ATOM   6362  C CA  . GLY C  3  12  ? 46.397  -10.251 71.212  1.00 39.63  ?  12   GLY C CA  1 
ATOM   6363  C C   . GLY C  3  12  ? 45.812  -8.927  70.798  1.00 40.43  ?  12   GLY C C   1 
ATOM   6364  O O   . GLY C  3  12  ? 45.321  -8.144  71.613  1.00 40.92  ?  12   GLY C O   1 
ATOM   6365  N N   . ARG C  3  13  ? 45.874  -8.673  69.500  1.00 42.95  ?  13   ARG C N   1 
ATOM   6366  C CA  . ARG C  3  13  ? 45.479  -7.379  68.978  1.00 43.96  ?  13   ARG C CA  1 
ATOM   6367  C C   . ARG C  3  13  ? 44.097  -7.458  68.344  1.00 46.90  ?  13   ARG C C   1 
ATOM   6368  O O   . ARG C  3  13  ? 43.221  -6.645  68.637  1.00 48.24  ?  13   ARG C O   1 
ATOM   6369  C CB  . ARG C  3  13  ? 46.510  -6.879  67.969  1.00 43.58  ?  13   ARG C CB  1 
ATOM   6370  C CG  . ARG C  3  13  ? 46.334  -5.432  67.569  1.00 44.47  ?  13   ARG C CG  1 
ATOM   6371  C CD  . ARG C  3  13  ? 46.800  -4.500  68.673  1.00 44.84  ?  13   ARG C CD  1 
ATOM   6372  N NE  . ARG C  3  13  ? 47.017  -3.146  68.180  1.00 46.68  ?  13   ARG C NE  1 
ATOM   6373  C CZ  . ARG C  3  13  ? 48.164  -2.711  67.677  1.00 45.70  ?  13   ARG C CZ  1 
ATOM   6374  N NH1 . ARG C  3  13  ? 49.231  -3.491  67.612  1.00 42.61  ?  13   ARG C NH1 1 
ATOM   6375  N NH2 . ARG C  3  13  ? 48.243  -1.463  67.225  1.00 48.09  ?  13   ARG C NH2 1 
ATOM   6376  N N   . THR D  1  47  ? 38.624  33.407  32.370  1.00 33.73  ?  47   THR D N   1 
ATOM   6377  C CA  . THR D  1  47  ? 39.836  33.555  33.165  1.00 35.41  ?  47   THR D CA  1 
ATOM   6378  C C   . THR D  1  47  ? 40.899  32.555  32.728  1.00 35.77  ?  47   THR D C   1 
ATOM   6379  O O   . THR D  1  47  ? 40.611  31.613  31.990  1.00 34.59  ?  47   THR D O   1 
ATOM   6380  C CB  . THR D  1  47  ? 39.556  33.362  34.667  1.00 35.62  ?  47   THR D CB  1 
ATOM   6381  O OG1 . THR D  1  47  ? 39.573  31.965  34.982  1.00 34.91  ?  47   THR D OG1 1 
ATOM   6382  C CG2 . THR D  1  47  ? 38.200  33.941  35.034  1.00 34.77  ?  47   THR D CG2 1 
ATOM   6383  N N   . VAL D  1  48  ? 42.134  32.773  33.182  1.00 36.78  ?  48   VAL D N   1 
ATOM   6384  C CA  . VAL D  1  48  ? 43.209  31.835  32.879  1.00 37.36  ?  48   VAL D CA  1 
ATOM   6385  C C   . VAL D  1  48  ? 43.012  30.532  33.643  1.00 36.67  ?  48   VAL D C   1 
ATOM   6386  O O   . VAL D  1  48  ? 43.287  29.444  33.124  1.00 36.20  ?  48   VAL D O   1 
ATOM   6387  C CB  . VAL D  1  48  ? 44.576  32.474  33.185  1.00 39.54  ?  48   VAL D CB  1 
ATOM   6388  C CG1 . VAL D  1  48  ? 45.698  31.632  32.600  1.00 40.25  ?  48   VAL D CG1 1 
ATOM   6389  C CG2 . VAL D  1  48  ? 44.629  33.896  32.643  1.00 40.30  ?  48   VAL D CG2 1 
ATOM   6390  N N   . GLU D  1  49  ? 42.532  30.620  34.886  1.00 40.16  ?  49   GLU D N   1 
ATOM   6391  C CA  . GLU D  1  49  ? 42.299  29.416  35.678  1.00 39.61  ?  49   GLU D CA  1 
ATOM   6392  C C   . GLU D  1  49  ? 41.142  28.599  35.117  1.00 37.59  ?  49   GLU D C   1 
ATOM   6393  O O   . GLU D  1  49  ? 41.166  27.364  35.164  1.00 37.03  ?  49   GLU D O   1 
ATOM   6394  C CB  . GLU D  1  49  ? 42.040  29.790  37.138  1.00 40.24  ?  49   GLU D CB  1 
ATOM   6395  C CG  . GLU D  1  49  ? 43.107  30.687  37.753  1.00 42.28  ?  49   GLU D CG  1 
ATOM   6396  C CD  . GLU D  1  49  ? 42.809  32.165  37.580  1.00 42.67  ?  49   GLU D CD  1 
ATOM   6397  O OE1 . GLU D  1  49  ? 41.620  32.545  37.625  1.00 41.56  ?  49   GLU D OE1 1 
ATOM   6398  O OE2 . GLU D  1  49  ? 43.767  32.948  37.401  1.00 44.17  -1 49   GLU D OE2 1 
ATOM   6399  N N   . GLU D  1  50  ? 40.119  29.272  34.583  1.00 35.70  ?  50   GLU D N   1 
ATOM   6400  C CA  . GLU D  1  50  ? 39.022  28.564  33.930  1.00 34.01  ?  50   GLU D CA  1 
ATOM   6401  C C   . GLU D  1  50  ? 39.512  27.835  32.686  1.00 33.46  ?  50   GLU D C   1 
ATOM   6402  O O   . GLU D  1  50  ? 39.215  26.652  32.484  1.00 32.48  ?  50   GLU D O   1 
ATOM   6403  C CB  . GLU D  1  50  ? 37.908  29.546  33.567  1.00 33.80  ?  50   GLU D CB  1 
ATOM   6404  C CG  . GLU D  1  50  ? 37.018  29.956  34.724  1.00 33.25  ?  50   GLU D CG  1 
ATOM   6405  C CD  . GLU D  1  50  ? 36.108  31.116  34.370  1.00 32.56  ?  50   GLU D CD  1 
ATOM   6406  O OE1 . GLU D  1  50  ? 36.358  31.774  33.338  1.00 32.74  ?  50   GLU D OE1 1 
ATOM   6407  O OE2 . GLU D  1  50  ? 35.140  31.368  35.119  1.00 32.18  -1 50   GLU D OE2 1 
ATOM   6408  N N   . ALA D  1  51  ? 40.262  28.538  31.834  1.00 34.75  ?  51   ALA D N   1 
ATOM   6409  C CA  . ALA D  1  51  ? 40.722  27.955  30.578  1.00 34.42  ?  51   ALA D CA  1 
ATOM   6410  C C   . ALA D  1  51  ? 41.645  26.766  30.812  1.00 34.99  ?  51   ALA D C   1 
ATOM   6411  O O   . ALA D  1  51  ? 41.539  25.745  30.122  1.00 34.15  ?  51   ALA D O   1 
ATOM   6412  C CB  . ALA D  1  51  ? 41.418  29.021  29.737  1.00 35.52  ?  51   ALA D CB  1 
ATOM   6413  N N   . ASN D  1  52  ? 42.566  26.881  31.773  1.00 33.23  ?  52   ASN D N   1 
ATOM   6414  C CA  . ASN D  1  52  ? 43.448  25.759  32.083  1.00 33.92  ?  52   ASN D CA  1 
ATOM   6415  C C   . ASN D  1  52  ? 42.652  24.561  32.583  1.00 32.63  ?  52   ASN D C   1 
ATOM   6416  O O   . ASN D  1  52  ? 43.006  23.409  32.303  1.00 32.51  ?  52   ASN D O   1 
ATOM   6417  C CB  . ASN D  1  52  ? 44.490  26.176  33.122  1.00 35.82  ?  52   ASN D CB  1 
ATOM   6418  C CG  . ASN D  1  52  ? 45.684  26.878  32.505  1.00 37.44  ?  52   ASN D CG  1 
ATOM   6419  O OD1 . ASN D  1  52  ? 46.421  26.290  31.713  1.00 37.88  ?  52   ASN D OD1 1 
ATOM   6420  N ND2 . ASN D  1  52  ? 45.885  28.140  32.871  1.00 38.44  ?  52   ASN D ND2 1 
ATOM   6421  N N   . ALA D  1  53  ? 41.573  24.814  33.324  1.00 32.10  ?  53   ALA D N   1 
ATOM   6422  C CA  . ALA D  1  53  ? 40.750  23.723  33.836  1.00 30.94  ?  53   ALA D CA  1 
ATOM   6423  C C   . ALA D  1  53  ? 40.002  23.013  32.712  1.00 29.32  ?  53   ALA D C   1 
ATOM   6424  O O   . ALA D  1  53  ? 39.900  21.781  32.712  1.00 28.77  ?  53   ALA D O   1 
ATOM   6425  C CB  . ALA D  1  53  ? 39.780  24.260  34.883  1.00 30.56  ?  53   ALA D CB  1 
ATOM   6426  N N   . LEU D  1  54  ? 39.469  23.771  31.749  1.00 29.78  ?  54   LEU D N   1 
ATOM   6427  C CA  . LEU D  1  54  ? 38.866  23.151  30.572  1.00 28.41  ?  54   LEU D CA  1 
ATOM   6428  C C   . LEU D  1  54  ? 39.912  22.409  29.755  1.00 29.00  ?  54   LEU D C   1 
ATOM   6429  O O   . LEU D  1  54  ? 39.665  21.295  29.277  1.00 28.21  ?  54   LEU D O   1 
ATOM   6430  C CB  . LEU D  1  54  ? 38.177  24.203  29.700  1.00 27.78  ?  54   LEU D CB  1 
ATOM   6431  C CG  . LEU D  1  54  ? 36.711  24.551  29.962  1.00 26.49  ?  54   LEU D CG  1 
ATOM   6432  C CD1 . LEU D  1  54  ? 35.804  23.352  29.721  1.00 24.98  ?  54   LEU D CD1 1 
ATOM   6433  C CD2 . LEU D  1  54  ? 36.545  25.081  31.362  1.00 27.09  ?  54   LEU D CD2 1 
ATOM   6434  N N   . LEU D  1  55  ? 41.086  23.020  29.578  1.00 29.40  ?  55   LEU D N   1 
ATOM   6435  C CA  . LEU D  1  55  ? 42.145  22.404  28.787  1.00 30.20  ?  55   LEU D CA  1 
ATOM   6436  C C   . LEU D  1  55  ? 42.592  21.077  29.386  1.00 30.48  ?  55   LEU D C   1 
ATOM   6437  O O   . LEU D  1  55  ? 42.967  20.158  28.649  1.00 30.69  ?  55   LEU D O   1 
ATOM   6438  C CB  . LEU D  1  55  ? 43.324  23.371  28.673  1.00 32.00  ?  55   LEU D CB  1 
ATOM   6439  C CG  . LEU D  1  55  ? 44.077  23.424  27.346  1.00 32.64  ?  55   LEU D CG  1 
ATOM   6440  C CD1 . LEU D  1  55  ? 43.102  23.636  26.203  1.00 31.20  ?  55   LEU D CD1 1 
ATOM   6441  C CD2 . LEU D  1  55  ? 45.111  24.538  27.380  1.00 34.46  ?  55   LEU D CD2 1 
ATOM   6442  N N   . LYS D  1  56  ? 42.561  20.958  30.717  1.00 30.43  ?  56   LYS D N   1 
ATOM   6443  C CA  . LYS D  1  56  ? 42.880  19.685  31.354  1.00 30.70  ?  56   LYS D CA  1 
ATOM   6444  C C   . LYS D  1  56  ? 41.804  18.644  31.072  1.00 29.49  ?  56   LYS D C   1 
ATOM   6445  O O   . LYS D  1  56  ? 42.113  17.472  30.828  1.00 29.95  ?  56   LYS D O   1 
ATOM   6446  C CB  . LYS D  1  56  ? 43.053  19.877  32.861  1.00 31.60  ?  56   LYS D CB  1 
ATOM   6447  C CG  . LYS D  1  56  ? 44.075  18.944  33.487  1.00 32.94  ?  56   LYS D CG  1 
ATOM   6448  C CD  . LYS D  1  56  ? 43.969  18.946  35.002  1.00 33.54  ?  56   LYS D CD  1 
ATOM   6449  C CE  . LYS D  1  56  ? 43.247  17.704  35.500  1.00 32.61  ?  56   LYS D CE  1 
ATOM   6450  N NZ  . LYS D  1  56  ? 43.541  17.436  36.934  1.00 33.72  ?  56   LYS D NZ  1 
ATOM   6451  N N   . TRP D  1  57  ? 40.535  19.054  31.109  1.00 29.11  ?  57   TRP D N   1 
ATOM   6452  C CA  . TRP D  1  57  ? 39.442  18.130  30.820  1.00 28.05  ?  57   TRP D CA  1 
ATOM   6453  C C   . TRP D  1  57  ? 39.497  17.648  29.376  1.00 27.92  ?  57   TRP D C   1 
ATOM   6454  O O   . TRP D  1  57  ? 39.256  16.468  29.096  1.00 27.83  ?  57   TRP D O   1 
ATOM   6455  C CB  . TRP D  1  57  ? 38.103  18.806  31.112  1.00 26.76  ?  57   TRP D CB  1 
ATOM   6456  C CG  . TRP D  1  57  ? 36.911  17.969  30.772  1.00 25.74  ?  57   TRP D CG  1 
ATOM   6457  C CD1 . TRP D  1  57  ? 36.672  16.684  31.161  1.00 25.77  ?  57   TRP D CD1 1 
ATOM   6458  C CD2 . TRP D  1  57  ? 35.792  18.359  29.967  1.00 24.63  ?  57   TRP D CD2 1 
ATOM   6459  N NE1 . TRP D  1  57  ? 35.472  16.250  30.651  1.00 24.75  ?  57   TRP D NE1 1 
ATOM   6460  C CE2 . TRP D  1  57  ? 34.912  17.259  29.913  1.00 24.07  ?  57   TRP D CE2 1 
ATOM   6461  C CE3 . TRP D  1  57  ? 35.448  19.531  29.287  1.00 24.14  ?  57   TRP D CE3 1 
ATOM   6462  C CZ2 . TRP D  1  57  ? 33.712  17.297  29.207  1.00 23.09  ?  57   TRP D CZ2 1 
ATOM   6463  C CZ3 . TRP D  1  57  ? 34.255  19.567  28.586  1.00 23.17  ?  57   TRP D CZ3 1 
ATOM   6464  C CH2 . TRP D  1  57  ? 33.402  18.457  28.552  1.00 22.68  ?  57   TRP D CH2 1 
ATOM   6465  N N   . LYS D  1  58  ? 39.808  18.554  28.444  1.00 27.53  ?  58   LYS D N   1 
ATOM   6466  C CA  . LYS D  1  58  ? 39.855  18.193  27.031  1.00 27.46  ?  58   LYS D CA  1 
ATOM   6467  C C   . LYS D  1  58  ? 40.903  17.119  26.763  1.00 28.71  ?  58   LYS D C   1 
ATOM   6468  O O   . LYS D  1  58  ? 40.707  16.252  25.902  1.00 28.59  ?  58   LYS D O   1 
ATOM   6469  C CB  . LYS D  1  58  ? 40.127  19.441  26.188  1.00 27.50  ?  58   LYS D CB  1 
ATOM   6470  C CG  . LYS D  1  58  ? 40.142  19.215  24.685  1.00 27.45  ?  58   LYS D CG  1 
ATOM   6471  C CD  . LYS D  1  58  ? 41.564  19.128  24.155  1.00 28.99  ?  58   LYS D CD  1 
ATOM   6472  C CE  . LYS D  1  58  ? 41.602  19.224  22.639  1.00 29.03  ?  58   LYS D CE  1 
ATOM   6473  N NZ  . LYS D  1  58  ? 41.548  20.636  22.170  1.00 28.80  ?  58   LYS D NZ  1 
ATOM   6474  N N   . SER D  1  59  ? 42.028  17.162  27.487  1.00 29.02  ?  59   SER D N   1 
ATOM   6475  C CA  . SER D  1  59  ? 43.090  16.180  27.286  1.00 30.40  ?  59   SER D CA  1 
ATOM   6476  C C   . SER D  1  59  ? 42.620  14.750  27.530  1.00 30.15  ?  59   SER D C   1 
ATOM   6477  O O   . SER D  1  59  ? 43.218  13.812  26.990  1.00 31.02  ?  59   SER D O   1 
ATOM   6478  C CB  . SER D  1  59  ? 44.280  16.503  28.194  1.00 31.89  ?  59   SER D CB  1 
ATOM   6479  O OG  . SER D  1  59  ? 44.016  16.122  29.533  1.00 31.80  ?  59   SER D OG  1 
ATOM   6480  N N   . THR D  1  60  ? 41.576  14.562  28.338  1.00 29.48  ?  60   THR D N   1 
ATOM   6481  C CA  . THR D  1  60  ? 41.047  13.236  28.628  1.00 29.22  ?  60   THR D CA  1 
ATOM   6482  C C   . THR D  1  60  ? 40.187  12.662  27.507  1.00 28.31  ?  60   THR D C   1 
ATOM   6483  O O   . THR D  1  60  ? 39.850  11.474  27.561  1.00 28.25  ?  60   THR D O   1 
ATOM   6484  C CB  . THR D  1  60  ? 40.232  13.266  29.925  1.00 28.51  ?  60   THR D CB  1 
ATOM   6485  O OG1 . THR D  1  60  ? 38.914  13.757  29.652  1.00 27.03  ?  60   THR D OG1 1 
ATOM   6486  C CG2 . THR D  1  60  ? 40.902  14.162  30.954  1.00 29.21  ?  60   THR D CG2 1 
ATOM   6487  N N   . PHE D  1  61  ? 39.821  13.462  26.508  1.00 29.90  ?  61   PHE D N   1 
ATOM   6488  C CA  . PHE D  1  61  ? 38.905  13.003  25.470  1.00 29.02  ?  61   PHE D CA  1 
ATOM   6489  C C   . PHE D  1  61  ? 39.504  11.844  24.678  1.00 29.87  ?  61   PHE D C   1 
ATOM   6490  O O   . PHE D  1  61  ? 40.713  11.781  24.438  1.00 31.17  ?  61   PHE D O   1 
ATOM   6491  C CB  . PHE D  1  61  ? 38.548  14.155  24.529  1.00 28.38  ?  61   PHE D CB  1 
ATOM   6492  C CG  . PHE D  1  61  ? 37.730  15.240  25.176  1.00 27.41  ?  61   PHE D CG  1 
ATOM   6493  C CD1 . PHE D  1  61  ? 37.057  15.005  26.365  1.00 26.92  ?  61   PHE D CD1 1 
ATOM   6494  C CD2 . PHE D  1  61  ? 37.638  16.496  24.599  1.00 27.07  ?  61   PHE D CD2 1 
ATOM   6495  C CE1 . PHE D  1  61  ? 36.305  16.000  26.964  1.00 26.15  ?  61   PHE D CE1 1 
ATOM   6496  C CE2 . PHE D  1  61  ? 36.887  17.496  25.194  1.00 26.27  ?  61   PHE D CE2 1 
ATOM   6497  C CZ  . PHE D  1  61  ? 36.221  17.246  26.378  1.00 25.84  ?  61   PHE D CZ  1 
ATOM   6498  N N   . THR D  1  62  ? 38.637  10.919  24.273  1.00 35.01  ?  62   THR D N   1 
ATOM   6499  C CA  . THR D  1  62  ? 39.037  9.711   23.566  1.00 35.73  ?  62   THR D CA  1 
ATOM   6500  C C   . THR D  1  62  ? 38.687  9.821   22.087  1.00 35.37  ?  62   THR D C   1 
ATOM   6501  O O   . THR D  1  62  ? 37.748  10.525  21.704  1.00 34.26  ?  62   THR D O   1 
ATOM   6502  C CB  . THR D  1  62  ? 38.349  8.479   24.163  1.00 35.39  ?  62   THR D CB  1 
ATOM   6503  O OG1 . THR D  1  62  ? 38.233  8.633   25.583  1.00 35.26  ?  62   THR D OG1 1 
ATOM   6504  C CG2 . THR D  1  62  ? 39.148  7.219   23.863  1.00 36.58  ?  62   THR D CG2 1 
ATOM   6505  N N   . ASN D  1  63  ? 39.456  9.108   21.259  1.00 42.07  ?  63   ASN D N   1 
ATOM   6506  C CA  . ASN D  1  63  ? 39.216  9.027   19.817  1.00 41.94  ?  63   ASN D CA  1 
ATOM   6507  C C   . ASN D  1  63  ? 39.068  10.414  19.198  1.00 41.45  ?  63   ASN D C   1 
ATOM   6508  O O   . ASN D  1  63  ? 38.214  10.646  18.339  1.00 40.61  ?  63   ASN D O   1 
ATOM   6509  C CB  . ASN D  1  63  ? 37.981  8.175   19.512  1.00 40.95  ?  63   ASN D CB  1 
ATOM   6510  C CG  . ASN D  1  63  ? 38.172  6.710   19.853  1.00 41.57  ?  63   ASN D CG  1 
ATOM   6511  O OD1 . ASN D  1  63  ? 39.298  6.224   19.971  1.00 42.90  ?  63   ASN D OD1 1 
ATOM   6512  N ND2 . ASN D  1  63  ? 37.059  5.996   20.010  1.00 40.83  ?  63   ASN D ND2 1 
ATOM   6513  N N   . GLN D  1  64  ? 39.903  11.348  19.641  1.00 36.37  ?  64   GLN D N   1 
ATOM   6514  C CA  . GLN D  1  64  ? 39.798  12.732  19.203  1.00 35.94  ?  64   GLN D CA  1 
ATOM   6515  C C   . GLN D  1  64  ? 40.672  12.957  17.977  1.00 36.99  ?  64   GLN D C   1 
ATOM   6516  O O   . GLN D  1  64  ? 41.837  12.549  17.952  1.00 38.43  ?  64   GLN D O   1 
ATOM   6517  C CB  . GLN D  1  64  ? 40.195  13.686  20.330  1.00 36.04  ?  64   GLN D CB  1 
ATOM   6518  C CG  . GLN D  1  64  ? 39.212  14.827  20.534  1.00 34.86  ?  64   GLN D CG  1 
ATOM   6519  C CD  . GLN D  1  64  ? 37.768  14.358  20.539  1.00 33.40  ?  64   GLN D CD  1 
ATOM   6520  O OE1 . GLN D  1  64  ? 37.405  13.428  21.262  1.00 33.23  ?  64   GLN D OE1 1 
ATOM   6521  N NE2 . GLN D  1  64  ? 36.936  15.000  19.726  1.00 32.54  ?  64   GLN D NE2 1 
ATOM   6522  N N   . THR D  1  65  ? 40.105  13.604  16.965  1.00 35.04  ?  65   THR D N   1 
ATOM   6523  C CA  . THR D  1  65  ? 40.809  13.885  15.725  1.00 35.97  ?  65   THR D CA  1 
ATOM   6524  C C   . THR D  1  65  ? 41.373  15.300  15.745  1.00 36.31  ?  65   THR D C   1 
ATOM   6525  O O   . THR D  1  65  ? 40.852  16.190  16.423  1.00 35.40  ?  65   THR D O   1 
ATOM   6526  C CB  . THR D  1  65  ? 39.887  13.706  14.514  1.00 35.22  ?  65   THR D CB  1 
ATOM   6527  O OG1 . THR D  1  65  ? 40.641  13.873  13.306  1.00 36.30  ?  65   THR D OG1 1 
ATOM   6528  C CG2 . THR D  1  65  ? 38.746  14.716  14.546  1.00 33.75  ?  65   THR D CG2 1 
ATOM   6529  N N   . SER D  1  66  ? 42.455  15.497  14.989  1.00 35.95  ?  66   SER D N   1 
ATOM   6530  C CA  . SER D  1  66  ? 43.071  16.812  14.861  1.00 36.49  ?  66   SER D CA  1 
ATOM   6531  C C   . SER D  1  66  ? 42.161  17.820  14.175  1.00 35.34  ?  66   SER D C   1 
ATOM   6532  O O   . SER D  1  66  ? 42.438  19.023  14.239  1.00 35.49  ?  66   SER D O   1 
ATOM   6533  C CB  . SER D  1  66  ? 44.390  16.698  14.094  1.00 38.42  ?  66   SER D CB  1 
ATOM   6534  O OG  . SER D  1  66  ? 45.129  17.906  14.163  1.00 39.21  ?  66   SER D OG  1 
ATOM   6535  N N   . SER D  1  67  ? 41.094  17.362  13.525  1.00 35.69  ?  67   SER D N   1 
ATOM   6536  C CA  . SER D  1  67  ? 40.188  18.217  12.772  1.00 34.68  ?  67   SER D CA  1 
ATOM   6537  C C   . SER D  1  67  ? 39.051  18.783  13.612  1.00 33.11  ?  67   SER D C   1 
ATOM   6538  O O   . SER D  1  67  ? 38.233  19.542  13.082  1.00 32.46  ?  67   SER D O   1 
ATOM   6539  C CB  . SER D  1  67  ? 39.598  17.437  11.593  1.00 34.84  ?  67   SER D CB  1 
ATOM   6540  O OG  . SER D  1  67  ? 38.358  16.849  11.950  1.00 33.11  ?  67   SER D OG  1 
ATOM   6541  N N   . SER D  1  68  ? 38.976  18.443  14.896  1.00 30.36  ?  68   SER D N   1 
ATOM   6542  C CA  . SER D  1  68  ? 37.862  18.893  15.717  1.00 29.00  ?  68   SER D CA  1 
ATOM   6543  C C   . SER D  1  68  ? 37.934  20.398  15.948  1.00 28.80  ?  68   SER D C   1 
ATOM   6544  O O   . SER D  1  68  ? 39.008  21.006  15.925  1.00 29.83  ?  68   SER D O   1 
ATOM   6545  C CB  . SER D  1  68  ? 37.852  18.162  17.060  1.00 28.92  ?  68   SER D CB  1 
ATOM   6546  O OG  . SER D  1  68  ? 38.726  18.782  17.987  1.00 29.57  ?  68   SER D OG  1 
ATOM   6547  N N   . LYS D  1  69  ? 36.764  21.000  16.168  1.00 27.93  ?  69   LYS D N   1 
ATOM   6548  C CA  . LYS D  1  69  ? 36.673  22.433  16.413  1.00 27.63  ?  69   LYS D CA  1 
ATOM   6549  C C   . LYS D  1  69  ? 37.345  22.855  17.713  1.00 28.07  ?  69   LYS D C   1 
ATOM   6550  O O   . LYS D  1  69  ? 37.566  24.054  17.912  1.00 28.15  ?  69   LYS D O   1 
ATOM   6551  C CB  . LYS D  1  69  ? 35.206  22.867  16.418  1.00 26.32  ?  69   LYS D CB  1 
ATOM   6552  C CG  . LYS D  1  69  ? 34.606  23.030  15.029  1.00 25.97  ?  69   LYS D CG  1 
ATOM   6553  C CD  . LYS D  1  69  ? 33.197  22.464  14.968  1.00 24.99  ?  69   LYS D CD  1 
ATOM   6554  C CE  . LYS D  1  69  ? 32.516  22.807  13.654  1.00 24.63  ?  69   LYS D CE  1 
ATOM   6555  N NZ  . LYS D  1  69  ? 31.088  22.384  13.641  1.00 23.76  ?  69   LYS D NZ  1 
ATOM   6556  N N   . LEU D  1  70  ? 37.679  21.910  18.593  1.00 25.56  ?  70   LEU D N   1 
ATOM   6557  C CA  . LEU D  1  70  ? 38.381  22.234  19.828  1.00 26.12  ?  70   LEU D CA  1 
ATOM   6558  C C   . LEU D  1  70  ? 39.865  22.497  19.613  1.00 27.64  ?  70   LEU D C   1 
ATOM   6559  O O   . LEU D  1  70  ? 40.588  22.702  20.595  1.00 28.35  ?  70   LEU D O   1 
ATOM   6560  C CB  . LEU D  1  70  ? 38.201  21.112  20.854  1.00 26.02  ?  70   LEU D CB  1 
ATOM   6561  C CG  . LEU D  1  70  ? 36.774  20.797  21.310  1.00 24.75  ?  70   LEU D CG  1 
ATOM   6562  C CD1 . LEU D  1  70  ? 36.791  20.130  22.675  1.00 24.85  ?  70   LEU D CD1 1 
ATOM   6563  C CD2 . LEU D  1  70  ? 35.924  22.055  21.343  1.00 23.91  ?  70   LEU D CD2 1 
ATOM   6564  N N   . SER D  1  71  ? 40.333  22.497  18.361  1.00 28.11  ?  71   SER D N   1 
ATOM   6565  C CA  . SER D  1  71  ? 41.695  22.928  18.071  1.00 29.71  ?  71   SER D CA  1 
ATOM   6566  C C   . SER D  1  71  ? 41.926  24.378  18.468  1.00 30.05  ?  71   SER D C   1 
ATOM   6567  O O   . SER D  1  71  ? 43.072  24.771  18.706  1.00 31.71  ?  71   SER D O   1 
ATOM   6568  C CB  . SER D  1  71  ? 42.004  22.744  16.583  1.00 30.35  ?  71   SER D CB  1 
ATOM   6569  O OG  . SER D  1  71  ? 41.638  21.450  16.135  1.00 30.08  ?  71   SER D OG  1 
ATOM   6570  N N   . SER D  1  72  ? 40.859  25.175  18.554  1.00 31.12  ?  72   SER D N   1 
ATOM   6571  C CA  . SER D  1  72  ? 40.963  26.576  18.937  1.00 31.97  ?  72   SER D CA  1 
ATOM   6572  C C   . SER D  1  72  ? 41.306  26.766  20.408  1.00 32.50  ?  72   SER D C   1 
ATOM   6573  O O   . SER D  1  72  ? 41.596  27.896  20.817  1.00 33.49  ?  72   SER D O   1 
ATOM   6574  C CB  . SER D  1  72  ? 39.651  27.291  18.619  1.00 30.80  ?  72   SER D CB  1 
ATOM   6575  O OG  . SER D  1  72  ? 38.558  26.623  19.225  1.00 29.16  ?  72   SER D OG  1 
ATOM   6576  N N   . TRP D  1  73  ? 41.281  25.698  21.208  1.00 30.01  ?  73   TRP D N   1 
ATOM   6577  C CA  . TRP D  1  73  ? 41.624  25.779  22.627  1.00 30.58  ?  73   TRP D CA  1 
ATOM   6578  C C   . TRP D  1  73  ? 43.139  25.657  22.746  1.00 32.44  ?  73   TRP D C   1 
ATOM   6579  O O   . TRP D  1  73  ? 43.693  24.582  22.980  1.00 32.68  ?  73   TRP D O   1 
ATOM   6580  C CB  . TRP D  1  73  ? 40.920  24.680  23.415  1.00 29.29  ?  73   TRP D CB  1 
ATOM   6581  C CG  . TRP D  1  73  ? 39.426  24.789  23.466  1.00 27.59  ?  73   TRP D CG  1 
ATOM   6582  C CD1 . TRP D  1  73  ? 38.622  25.517  22.636  1.00 26.92  ?  73   TRP D CD1 1 
ATOM   6583  C CD2 . TRP D  1  73  ? 38.553  24.129  24.390  1.00 26.44  ?  73   TRP D CD2 1 
ATOM   6584  N NE1 . TRP D  1  73  ? 37.305  25.356  22.992  1.00 25.44  ?  73   TRP D NE1 1 
ATOM   6585  C CE2 . TRP D  1  73  ? 37.236  24.509  24.066  1.00 25.12  ?  73   TRP D CE2 1 
ATOM   6586  C CE3 . TRP D  1  73  ? 38.759  23.257  25.463  1.00 26.51  ?  73   TRP D CE3 1 
ATOM   6587  C CZ2 . TRP D  1  73  ? 36.130  24.046  24.776  1.00 24.00  ?  73   TRP D CZ2 1 
ATOM   6588  C CZ3 . TRP D  1  73  ? 37.663  22.799  26.166  1.00 25.47  ?  73   TRP D CZ3 1 
ATOM   6589  C CH2 . TRP D  1  73  ? 36.364  23.194  25.820  1.00 24.33  ?  73   TRP D CH2 1 
ATOM   6590  N N   . VAL D  1  74  ? 43.826  26.786  22.585  1.00 35.94  ?  74   VAL D N   1 
ATOM   6591  C CA  . VAL D  1  74  ? 45.287  26.808  22.534  1.00 37.90  ?  74   VAL D CA  1 
ATOM   6592  C C   . VAL D  1  74  ? 45.888  27.484  23.763  1.00 39.17  ?  74   VAL D C   1 
ATOM   6593  O O   . VAL D  1  74  ? 46.621  26.856  24.528  1.00 39.96  ?  74   VAL D O   1 
ATOM   6594  C CB  . VAL D  1  74  ? 45.787  27.473  21.233  1.00 38.86  ?  74   VAL D CB  1 
ATOM   6595  C CG1 . VAL D  1  74  ? 47.308  27.459  21.180  1.00 41.00  ?  74   VAL D CG1 1 
ATOM   6596  C CG2 . VAL D  1  74  ? 45.207  26.769  20.021  1.00 37.68  ?  74   VAL D CG2 1 
ATOM   6597  N N   . ASN D  1  75  ? 45.575  28.761  23.982  1.00 42.04  ?  75   ASN D N   1 
ATOM   6598  C CA  . ASN D  1  75  ? 46.228  29.443  25.089  1.00 43.44  ?  75   ASN D CA  1 
ATOM   6599  C C   . ASN D  1  75  ? 45.227  29.785  26.180  1.00 42.45  ?  75   ASN D C   1 
ATOM   6600  O O   . ASN D  1  75  ? 44.132  30.288  25.890  1.00 41.27  ?  75   ASN D O   1 
ATOM   6601  C CB  . ASN D  1  75  ? 46.966  30.712  24.617  1.00 45.13  ?  75   ASN D CB  1 
ATOM   6602  C CG  . ASN D  1  75  ? 46.041  31.879  24.370  1.00 44.55  ?  75   ASN D CG  1 
ATOM   6603  O OD1 . ASN D  1  75  ? 44.957  31.721  23.813  1.00 42.95  ?  75   ASN D OD1 1 
ATOM   6604  N ND2 . ASN D  1  75  ? 46.466  33.066  24.789  1.00 45.93  ?  75   ASN D ND2 1 
ATOM   6605  N N   . PRO D  1  76  ? 45.557  29.497  27.441  1.00 42.47  ?  76   PRO D N   1 
ATOM   6606  C CA  . PRO D  1  76  ? 44.599  29.744  28.528  1.00 41.60  ?  76   PRO D CA  1 
ATOM   6607  C C   . PRO D  1  76  ? 44.413  31.211  28.867  1.00 42.29  ?  76   PRO D C   1 
ATOM   6608  O O   . PRO D  1  76  ? 43.474  31.541  29.604  1.00 41.50  ?  76   PRO D O   1 
ATOM   6609  C CB  . PRO D  1  76  ? 45.209  28.982  29.713  1.00 42.29  ?  76   PRO D CB  1 
ATOM   6610  C CG  . PRO D  1  76  ? 46.201  28.032  29.093  1.00 42.95  ?  76   PRO D CG  1 
ATOM   6611  C CD  . PRO D  1  76  ? 46.740  28.763  27.912  1.00 43.77  ?  76   PRO D CD  1 
ATOM   6612  N N   . ASN D  1  77  ? 45.264  32.097  28.357  1.00 44.72  ?  77   ASN D N   1 
ATOM   6613  C CA  . ASN D  1  77  ? 45.112  33.516  28.638  1.00 45.49  ?  77   ASN D CA  1 
ATOM   6614  C C   . ASN D  1  77  ? 43.815  34.039  28.036  1.00 44.69  ?  77   ASN D C   1 
ATOM   6615  O O   . ASN D  1  77  ? 43.373  33.595  26.973  1.00 44.06  ?  77   ASN D O   1 
ATOM   6616  C CB  . ASN D  1  77  ? 46.298  34.306  28.085  1.00 47.45  ?  77   ASN D CB  1 
ATOM   6617  C CG  . ASN D  1  77  ? 47.464  34.353  29.049  1.00 49.26  ?  77   ASN D CG  1 
ATOM   6618  O OD1 . ASN D  1  77  ? 47.307  34.102  30.244  1.00 49.17  ?  77   ASN D OD1 1 
ATOM   6619  N ND2 . ASN D  1  77  ? 48.643  34.682  28.535  1.00 51.01  ?  77   ASN D ND2 1 
ATOM   6620  N N   . THR D  1  78  ? 43.200  34.992  28.731  1.00 49.87  ?  78   THR D N   1 
ATOM   6621  C CA  . THR D  1  78  ? 42.003  35.620  28.204  1.00 48.61  ?  78   THR D CA  1 
ATOM   6622  C C   . THR D  1  78  ? 42.362  36.423  26.952  1.00 48.93  ?  78   THR D C   1 
ATOM   6623  O O   . THR D  1  78  ? 43.530  36.524  26.562  1.00 50.51  ?  78   THR D O   1 
ATOM   6624  C CB  . THR D  1  78  ? 41.357  36.510  29.270  1.00 47.95  ?  78   THR D CB  1 
ATOM   6625  O OG1 . THR D  1  78  ? 41.463  35.871  30.547  1.00 48.50  ?  78   THR D OG1 1 
ATOM   6626  C CG2 . THR D  1  78  ? 39.876  36.729  28.981  1.00 46.46  ?  78   THR D CG2 1 
ATOM   6627  N N   . SER D  1  79  ? 41.330  36.958  26.298  1.00 47.44  ?  79   SER D N   1 
ATOM   6628  C CA  . SER D  1  79  ? 41.424  37.752  25.076  1.00 48.59  ?  79   SER D CA  1 
ATOM   6629  C C   . SER D  1  79  ? 41.729  36.865  23.877  1.00 48.15  ?  79   SER D C   1 
ATOM   6630  O O   . SER D  1  79  ? 41.749  37.334  22.735  1.00 48.85  ?  79   SER D O   1 
ATOM   6631  C CB  . SER D  1  79  ? 42.486  38.844  25.210  1.00 49.88  ?  79   SER D CB  1 
ATOM   6632  O OG  . SER D  1  79  ? 43.794  38.303  25.138  1.00 50.29  ?  79   SER D OG  1 
ATOM   6633  N N   . SER D  1  80  ? 41.967  35.581  24.128  1.00 42.03  ?  80   SER D N   1 
ATOM   6634  C CA  . SER D  1  80  ? 41.920  34.568  23.086  1.00 41.43  ?  80   SER D CA  1 
ATOM   6635  C C   . SER D  1  80  ? 41.019  33.444  23.576  1.00 40.11  ?  80   SER D C   1 
ATOM   6636  O O   . SER D  1  80  ? 40.374  32.753  22.781  1.00 39.50  ?  80   SER D O   1 
ATOM   6637  C CB  . SER D  1  80  ? 43.322  34.068  22.746  1.00 41.81  ?  80   SER D CB  1 
ATOM   6638  O OG  . SER D  1  80  ? 43.299  33.206  21.622  1.00 41.12  ?  80   SER D OG  1 
ATOM   6639  N N   . PHE D  1  81  ? 40.983  33.262  24.898  1.00 37.91  ?  81   PHE D N   1 
ATOM   6640  C CA  . PHE D  1  81  ? 40.022  32.349  25.507  1.00 37.16  ?  81   PHE D CA  1 
ATOM   6641  C C   . PHE D  1  81  ? 38.594  32.821  25.270  1.00 36.31  ?  81   PHE D C   1 
ATOM   6642  O O   . PHE D  1  81  ? 37.747  32.063  24.788  1.00 35.39  ?  81   PHE D O   1 
ATOM   6643  C CB  . PHE D  1  81  ? 40.307  32.220  27.004  1.00 37.51  ?  81   PHE D CB  1 
ATOM   6644  C CG  . PHE D  1  81  ? 39.276  31.424  27.755  1.00 36.51  ?  81   PHE D CG  1 
ATOM   6645  C CD1 . PHE D  1  81  ? 39.063  30.089  27.465  1.00 35.93  ?  81   PHE D CD1 1 
ATOM   6646  C CD2 . PHE D  1  81  ? 38.529  32.012  28.763  1.00 36.08  ?  81   PHE D CD2 1 
ATOM   6647  C CE1 . PHE D  1  81  ? 38.117  29.354  28.160  1.00 34.69  ?  81   PHE D CE1 1 
ATOM   6648  C CE2 . PHE D  1  81  ? 37.583  31.284  29.461  1.00 34.83  ?  81   PHE D CE2 1 
ATOM   6649  C CZ  . PHE D  1  81  ? 37.376  29.954  29.159  1.00 34.29  ?  81   PHE D CZ  1 
ATOM   6650  N N   . CYS D  1  82  ? 38.317  34.083  25.583  1.00 39.77  ?  82   CYS D N   1 
ATOM   6651  C CA  . CYS D  1  82  ? 36.973  34.631  25.483  1.00 37.92  ?  82   CYS D CA  1 
ATOM   6652  C C   . CYS D  1  82  ? 36.638  35.139  24.088  1.00 37.72  ?  82   CYS D C   1 
ATOM   6653  O O   . CYS D  1  82  ? 35.560  35.711  23.897  1.00 36.60  ?  82   CYS D O   1 
ATOM   6654  C CB  . CYS D  1  82  ? 36.796  35.758  26.503  1.00 37.58  ?  82   CYS D CB  1 
ATOM   6655  S SG  . CYS D  1  82  ? 36.760  35.179  28.213  1.00 37.78  ?  82   CYS D SG  1 
ATOM   6656  N N   . THR D  1  83  ? 37.527  34.957  23.119  1.00 37.00  ?  83   THR D N   1 
ATOM   6657  C CA  . THR D  1  83  ? 37.241  35.397  21.758  1.00 36.92  ?  83   THR D CA  1 
ATOM   6658  C C   . THR D  1  83  ? 37.399  34.298  20.717  1.00 36.93  ?  83   THR D C   1 
ATOM   6659  O O   . THR D  1  83  ? 36.628  34.261  19.755  1.00 36.18  ?  83   THR D O   1 
ATOM   6660  C CB  . THR D  1  83  ? 38.147  36.579  21.386  1.00 38.32  ?  83   THR D CB  1 
ATOM   6661  O OG1 . THR D  1  83  ? 39.501  36.272  21.734  1.00 39.48  ?  83   THR D OG1 1 
ATOM   6662  C CG2 . THR D  1  83  ? 37.717  37.823  22.133  1.00 38.50  ?  83   THR D CG2 1 
ATOM   6663  N N   . SER D  1  84  ? 38.367  33.396  20.889  1.00 34.40  ?  84   SER D N   1 
ATOM   6664  C CA  . SER D  1  84  ? 38.742  32.466  19.835  1.00 34.10  ?  84   SER D CA  1 
ATOM   6665  C C   . SER D  1  84  ? 38.508  31.001  20.168  1.00 33.04  ?  84   SER D C   1 
ATOM   6666  O O   . SER D  1  84  ? 38.552  30.170  19.254  1.00 32.39  ?  84   SER D O   1 
ATOM   6667  C CB  . SER D  1  84  ? 40.223  32.649  19.464  1.00 35.36  ?  84   SER D CB  1 
ATOM   6668  O OG  . SER D  1  84  ? 41.043  31.732  20.168  1.00 35.37  ?  84   SER D OG  1 
ATOM   6669  N N   . TRP D  1  85  ? 38.251  30.656  21.426  1.00 30.90  ?  85   TRP D N   1 
ATOM   6670  C CA  . TRP D  1  85  ? 38.021  29.264  21.792  1.00 29.85  ?  85   TRP D CA  1 
ATOM   6671  C C   . TRP D  1  85  ? 36.619  28.862  21.359  1.00 28.75  ?  85   TRP D C   1 
ATOM   6672  O O   . TRP D  1  85  ? 35.634  29.484  21.772  1.00 28.26  ?  85   TRP D O   1 
ATOM   6673  C CB  . TRP D  1  85  ? 38.190  29.058  23.294  1.00 30.00  ?  85   TRP D CB  1 
ATOM   6674  C CG  . TRP D  1  85  ? 39.601  29.007  23.772  1.00 31.59  ?  85   TRP D CG  1 
ATOM   6675  C CD1 . TRP D  1  85  ? 40.665  29.707  23.282  1.00 33.18  ?  85   TRP D CD1 1 
ATOM   6676  C CD2 . TRP D  1  85  ? 40.107  28.206  24.844  1.00 31.87  ?  85   TRP D CD2 1 
ATOM   6677  N NE1 . TRP D  1  85  ? 41.802  29.392  23.987  1.00 34.43  ?  85   TRP D NE1 1 
ATOM   6678  C CE2 . TRP D  1  85  ? 41.485  28.471  24.952  1.00 33.66  ?  85   TRP D CE2 1 
ATOM   6679  C CE3 . TRP D  1  85  ? 39.526  27.287  25.724  1.00 30.87  ?  85   TRP D CE3 1 
ATOM   6680  C CZ2 . TRP D  1  85  ? 42.291  27.852  25.903  1.00 34.47  ?  85   TRP D CZ2 1 
ATOM   6681  C CZ3 . TRP D  1  85  ? 40.326  26.676  26.669  1.00 31.68  ?  85   TRP D CZ3 1 
ATOM   6682  C CH2 . TRP D  1  85  ? 41.694  26.960  26.751  1.00 33.45  ?  85   TRP D CH2 1 
ATOM   6683  N N   . TYR D  1  86  ? 36.530  27.835  20.518  1.00 30.06  ?  86   TYR D N   1 
ATOM   6684  C CA  . TYR D  1  86  ? 35.238  27.398  20.007  1.00 27.93  ?  86   TYR D CA  1 
ATOM   6685  C C   . TYR D  1  86  ? 34.331  26.954  21.148  1.00 24.92  ?  86   TYR D C   1 
ATOM   6686  O O   . TYR D  1  86  ? 34.733  26.169  22.011  1.00 24.86  ?  86   TYR D O   1 
ATOM   6687  C CB  . TYR D  1  86  ? 35.425  26.257  19.005  1.00 25.62  ?  86   TYR D CB  1 
ATOM   6688  C CG  . TYR D  1  86  ? 34.133  25.712  18.440  1.00 24.00  ?  86   TYR D CG  1 
ATOM   6689  C CD1 . TYR D  1  86  ? 33.445  24.686  19.079  1.00 23.60  ?  86   TYR D CD1 1 
ATOM   6690  C CD2 . TYR D  1  86  ? 33.599  26.226  17.267  1.00 23.65  ?  86   TYR D CD2 1 
ATOM   6691  C CE1 . TYR D  1  86  ? 32.264  24.191  18.566  1.00 22.92  ?  86   TYR D CE1 1 
ATOM   6692  C CE2 . TYR D  1  86  ? 32.418  25.736  16.746  1.00 22.98  ?  86   TYR D CE2 1 
ATOM   6693  C CZ  . TYR D  1  86  ? 31.755  24.719  17.399  1.00 22.63  ?  86   TYR D CZ  1 
ATOM   6694  O OH  . TYR D  1  86  ? 30.578  24.229  16.882  1.00 22.05  ?  86   TYR D OH  1 
ATOM   6695  N N   . GLY D  1  87  ? 33.100  27.458  21.143  1.00 25.36  ?  87   GLY D N   1 
ATOM   6696  C CA  . GLY D  1  87  ? 32.079  26.995  22.056  1.00 24.53  ?  87   GLY D CA  1 
ATOM   6697  C C   . GLY D  1  87  ? 32.068  27.640  23.424  1.00 24.84  ?  87   GLY D C   1 
ATOM   6698  O O   . GLY D  1  87  ? 31.277  27.217  24.277  1.00 24.53  ?  87   GLY D O   1 
ATOM   6699  N N   . VAL D  1  88  ? 32.908  28.641  23.673  1.00 24.24  ?  88   VAL D N   1 
ATOM   6700  C CA  . VAL D  1  88  ? 32.927  29.331  24.955  1.00 24.91  ?  88   VAL D CA  1 
ATOM   6701  C C   . VAL D  1  88  ? 32.504  30.776  24.738  1.00 25.42  ?  88   VAL D C   1 
ATOM   6702  O O   . VAL D  1  88  ? 32.813  31.381  23.705  1.00 25.92  ?  88   VAL D O   1 
ATOM   6703  C CB  . VAL D  1  88  ? 34.309  29.264  25.642  1.00 26.27  ?  88   VAL D CB  1 
ATOM   6704  C CG1 . VAL D  1  88  ? 34.778  27.822  25.774  1.00 25.90  ?  88   VAL D CG1 1 
ATOM   6705  C CG2 . VAL D  1  88  ? 35.323  30.111  24.906  1.00 29.13  ?  88   VAL D CG2 1 
ATOM   6706  N N   . ALA D  1  89  ? 31.764  31.312  25.702  1.00 24.82  ?  89   ALA D N   1 
ATOM   6707  C CA  . ALA D  1  89  ? 31.370  32.711  25.718  1.00 25.47  ?  89   ALA D CA  1 
ATOM   6708  C C   . ALA D  1  89  ? 31.493  33.215  27.144  1.00 26.26  ?  89   ALA D C   1 
ATOM   6709  O O   . ALA D  1  89  ? 31.084  32.530  28.086  1.00 25.71  ?  89   ALA D O   1 
ATOM   6710  C CB  . ALA D  1  89  ? 29.940  32.906  25.202  1.00 24.38  ?  89   ALA D CB  1 
ATOM   6711  N N   . CYS D  1  90  ? 32.068  34.400  27.306  1.00 26.49  ?  90   CYS D N   1 
ATOM   6712  C CA  . CYS D  1  90  ? 32.354  34.936  28.626  1.00 27.48  ?  90   CYS D CA  1 
ATOM   6713  C C   . CYS D  1  90  ? 31.461  36.128  28.943  1.00 27.78  ?  90   CYS D C   1 
ATOM   6714  O O   . CYS D  1  90  ? 30.738  36.654  28.093  1.00 27.40  ?  90   CYS D O   1 
ATOM   6715  C CB  . CYS D  1  90  ? 33.821  35.360  28.746  1.00 29.07  ?  90   CYS D CB  1 
ATOM   6716  S SG  . CYS D  1  90  ? 35.039  34.109  28.330  1.00 29.12  ?  90   CYS D SG  1 
ATOM   6717  N N   . SER D  1  91  ? 31.533  36.539  30.206  1.00 26.90  ?  91   SER D N   1 
ATOM   6718  C CA  . SER D  1  91  ? 30.970  37.790  30.688  1.00 27.65  ?  91   SER D CA  1 
ATOM   6719  C C   . SER D  1  91  ? 31.904  38.310  31.766  1.00 29.17  ?  91   SER D C   1 
ATOM   6720  O O   . SER D  1  91  ? 32.227  37.578  32.707  1.00 29.18  ?  91   SER D O   1 
ATOM   6721  C CB  . SER D  1  91  ? 29.556  37.599  31.245  1.00 26.68  ?  91   SER D CB  1 
ATOM   6722  O OG  . SER D  1  91  ? 29.017  38.828  31.704  1.00 27.52  ?  91   SER D OG  1 
ATOM   6723  N N   . LEU D  1  92  ? 32.344  39.560  31.622  1.00 27.17  ?  92   LEU D N   1 
ATOM   6724  C CA  . LEU D  1  92  ? 33.312  40.161  32.541  1.00 28.79  ?  92   LEU D CA  1 
ATOM   6725  C C   . LEU D  1  92  ? 34.558  39.286  32.680  1.00 29.14  ?  92   LEU D C   1 
ATOM   6726  O O   . LEU D  1  92  ? 35.131  39.147  33.763  1.00 29.94  ?  92   LEU D O   1 
ATOM   6727  C CB  . LEU D  1  92  ? 32.677  40.440  33.905  1.00 29.08  ?  92   LEU D CB  1 
ATOM   6728  C CG  . LEU D  1  92  ? 31.402  41.288  33.874  1.00 28.86  ?  92   LEU D CG  1 
ATOM   6729  C CD1 . LEU D  1  92  ? 30.799  41.422  35.263  1.00 29.17  ?  92   LEU D CD1 1 
ATOM   6730  C CD2 . LEU D  1  92  ? 31.681  42.655  33.278  1.00 30.08  ?  92   LEU D CD2 1 
ATOM   6731  N N   . GLY D  1  93  ? 34.971  38.677  31.568  1.00 31.10  ?  93   GLY D N   1 
ATOM   6732  C CA  . GLY D  1  93  ? 36.184  37.887  31.514  1.00 31.54  ?  93   GLY D CA  1 
ATOM   6733  C C   . GLY D  1  93  ? 36.089  36.480  32.067  1.00 30.54  ?  93   GLY D C   1 
ATOM   6734  O O   . GLY D  1  93  ? 37.116  35.792  32.128  1.00 31.03  ?  93   GLY D O   1 
ATOM   6735  N N   . SER D  1  94  ? 34.904  36.025  32.467  1.00 32.07  ?  94   SER D N   1 
ATOM   6736  C CA  . SER D  1  94  ? 34.712  34.676  32.985  1.00 31.12  ?  94   SER D CA  1 
ATOM   6737  C C   . SER D  1  94  ? 33.692  33.937  32.131  1.00 29.37  ?  94   SER D C   1 
ATOM   6738  O O   . SER D  1  94  ? 32.676  34.510  31.729  1.00 28.77  ?  94   SER D O   1 
ATOM   6739  C CB  . SER D  1  94  ? 34.248  34.696  34.444  1.00 31.36  ?  94   SER D CB  1 
ATOM   6740  O OG  . SER D  1  94  ? 33.795  33.414  34.847  1.00 30.28  ?  94   SER D OG  1 
ATOM   6741  N N   . ILE D  1  95  ? 33.965  32.655  31.867  1.00 29.39  ?  95   ILE D N   1 
ATOM   6742  C CA  . ILE D  1  95  ? 33.089  31.872  31.004  1.00 27.79  ?  95   ILE D CA  1 
ATOM   6743  C C   . ILE D  1  95  ? 31.722  31.716  31.654  1.00 26.82  ?  95   ILE D C   1 
ATOM   6744  O O   . ILE D  1  95  ? 31.601  31.302  32.814  1.00 26.94  ?  95   ILE D O   1 
ATOM   6745  C CB  . ILE D  1  95  ? 33.720  30.507  30.684  1.00 27.35  ?  95   ILE D CB  1 
ATOM   6746  C CG1 . ILE D  1  95  ? 32.765  29.671  29.827  1.00 25.71  ?  95   ILE D CG1 1 
ATOM   6747  C CG2 . ILE D  1  95  ? 34.109  29.763  31.955  1.00 27.74  ?  95   ILE D CG2 1 
ATOM   6748  C CD1 . ILE D  1  95  ? 33.372  28.397  29.296  1.00 25.31  ?  95   ILE D CD1 1 
ATOM   6749  N N   . ILE D  1  96  ? 30.682  32.076  30.907  1.00 25.40  ?  96   ILE D N   1 
ATOM   6750  C CA  . ILE D  1  96  ? 29.304  31.872  31.340  1.00 24.42  ?  96   ILE D CA  1 
ATOM   6751  C C   . ILE D  1  96  ? 28.541  30.926  30.431  1.00 23.19  ?  96   ILE D C   1 
ATOM   6752  O O   . ILE D  1  96  ? 27.418  30.528  30.779  1.00 22.91  ?  96   ILE D O   1 
ATOM   6753  C CB  . ILE D  1  96  ? 28.545  33.211  31.452  1.00 24.87  ?  96   ILE D CB  1 
ATOM   6754  C CG1 . ILE D  1  96  ? 28.540  33.925  30.099  1.00 24.86  ?  96   ILE D CG1 1 
ATOM   6755  C CG2 . ILE D  1  96  ? 29.174  34.093  32.518  1.00 26.37  ?  96   ILE D CG2 1 
ATOM   6756  C CD1 . ILE D  1  96  ? 27.469  34.983  29.968  1.00 25.20  ?  96   ILE D CD1 1 
ATOM   6757  N N   . ARG D  1  97  ? 29.106  30.547  29.288  1.00 28.14  ?  97   ARG D N   1 
ATOM   6758  C CA  . ARG D  1  97  ? 28.390  29.795  28.265  1.00 27.42  ?  97   ARG D CA  1 
ATOM   6759  C C   . ARG D  1  97  ? 29.346  28.793  27.639  1.00 27.13  ?  97   ARG D C   1 
ATOM   6760  O O   . ARG D  1  97  ? 30.403  29.180  27.132  1.00 27.42  ?  97   ARG D O   1 
ATOM   6761  C CB  . ARG D  1  97  ? 27.819  30.738  27.202  1.00 27.44  ?  97   ARG D CB  1 
ATOM   6762  C CG  . ARG D  1  97  ? 27.105  30.057  26.050  1.00 26.78  ?  97   ARG D CG  1 
ATOM   6763  C CD  . ARG D  1  97  ? 26.418  31.091  25.170  1.00 26.93  ?  97   ARG D CD  1 
ATOM   6764  N NE  . ARG D  1  97  ? 25.561  31.985  25.942  1.00 27.43  ?  97   ARG D NE  1 
ATOM   6765  C CZ  . ARG D  1  97  ? 24.882  33.002  25.429  1.00 27.80  ?  97   ARG D CZ  1 
ATOM   6766  N NH1 . ARG D  1  97  ? 24.943  33.295  24.140  1.00 27.70  ?  97   ARG D NH1 1 
ATOM   6767  N NH2 . ARG D  1  97  ? 24.126  33.747  26.230  1.00 28.37  ?  97   ARG D NH2 1 
ATOM   6768  N N   . LEU D  1  98  ? 28.980  27.514  27.681  1.00 23.44  ?  98   LEU D N   1 
ATOM   6769  C CA  . LEU D  1  98  ? 29.771  26.438  27.091  1.00 23.30  ?  98   LEU D CA  1 
ATOM   6770  C C   . LEU D  1  98  ? 28.874  25.679  26.122  1.00 22.70  ?  98   LEU D C   1 
ATOM   6771  O O   . LEU D  1  98  ? 27.982  24.937  26.546  1.00 22.39  ?  98   LEU D O   1 
ATOM   6772  C CB  . LEU D  1  98  ? 30.336  25.512  28.169  1.00 23.54  ?  98   LEU D CB  1 
ATOM   6773  C CG  . LEU D  1  98  ? 31.157  24.313  27.690  1.00 23.63  ?  98   LEU D CG  1 
ATOM   6774  C CD1 . LEU D  1  98  ? 32.480  24.766  27.095  1.00 24.17  ?  98   LEU D CD1 1 
ATOM   6775  C CD2 . LEU D  1  98  ? 31.389  23.338  28.834  1.00 23.87  ?  98   LEU D CD2 1 
ATOM   6776  N N   . ASN D  1  99  ? 29.112  25.866  24.827  1.00 26.59  ?  99   ASN D N   1 
ATOM   6777  C CA  . ASN D  1  99  ? 28.263  25.329  23.765  1.00 26.09  ?  99   ASN D CA  1 
ATOM   6778  C C   . ASN D  1  99  ? 29.090  24.346  22.942  1.00 26.13  ?  99   ASN D C   1 
ATOM   6779  O O   . ASN D  1  99  ? 29.844  24.752  22.053  1.00 26.35  ?  99   ASN D O   1 
ATOM   6780  C CB  . ASN D  1  99  ? 27.714  26.460  22.900  1.00 26.02  ?  99   ASN D CB  1 
ATOM   6781  C CG  . ASN D  1  99  ? 26.580  26.018  21.995  1.00 25.55  ?  99   ASN D CG  1 
ATOM   6782  O OD1 . ASN D  1  99  ? 26.079  24.898  22.094  1.00 25.24  ?  99   ASN D OD1 1 
ATOM   6783  N ND2 . ASN D  1  99  ? 26.169  26.914  21.101  1.00 25.55  ?  99   ASN D ND2 1 
ATOM   6784  N N   . LEU D  1  100 ? 28.933  23.054  23.224  1.00 22.31  ?  100  LEU D N   1 
ATOM   6785  C CA  . LEU D  1  100 ? 29.693  22.010  22.549  1.00 22.52  ?  100  LEU D CA  1 
ATOM   6786  C C   . LEU D  1  100 ? 28.775  20.997  21.875  1.00 22.07  ?  100  LEU D C   1 
ATOM   6787  O O   . LEU D  1  100 ? 29.094  19.809  21.804  1.00 22.22  ?  100  LEU D O   1 
ATOM   6788  C CB  . LEU D  1  100 ? 30.638  21.315  23.528  1.00 23.03  ?  100  LEU D CB  1 
ATOM   6789  C CG  . LEU D  1  100 ? 31.777  22.198  24.038  1.00 23.64  ?  100  LEU D CG  1 
ATOM   6790  C CD1 . LEU D  1  100 ? 32.622  21.456  25.059  1.00 24.23  ?  100  LEU D CD1 1 
ATOM   6791  C CD2 . LEU D  1  100 ? 32.631  22.691  22.880  1.00 24.00  ?  100  LEU D CD2 1 
ATOM   6792  N N   . THR D  1  101 ? 27.626  21.457  21.383  1.00 22.39  ?  101  THR D N   1 
ATOM   6793  C CA  . THR D  1  101 ? 26.708  20.571  20.682  1.00 22.00  ?  101  THR D CA  1 
ATOM   6794  C C   . THR D  1  101 ? 27.353  20.017  19.419  1.00 22.18  ?  101  THR D C   1 
ATOM   6795  O O   . THR D  1  101 ? 27.951  20.761  18.636  1.00 22.39  ?  101  THR D O   1 
ATOM   6796  C CB  . THR D  1  101 ? 25.423  21.317  20.320  1.00 21.61  ?  101  THR D CB  1 
ATOM   6797  O OG1 . THR D  1  101 ? 24.950  22.047  21.458  1.00 21.80  ?  101  THR D OG1 1 
ATOM   6798  C CG2 . THR D  1  101 ? 24.350  20.341  19.859  1.00 21.24  ?  101  THR D CG2 1 
ATOM   6799  N N   . ASN D  1  102 ? 27.229  18.701  19.231  1.00 22.80  ?  102  ASN D N   1 
ATOM   6800  C CA  . ASN D  1  102 ? 27.602  18.038  17.981  1.00 22.98  ?  102  ASN D CA  1 
ATOM   6801  C C   . ASN D  1  102 ? 29.061  18.306  17.612  1.00 23.66  ?  102  ASN D C   1 
ATOM   6802  O O   . ASN D  1  102 ? 29.396  18.519  16.445  1.00 24.01  ?  102  ASN D O   1 
ATOM   6803  C CB  . ASN D  1  102 ? 26.664  18.453  16.846  1.00 22.59  ?  102  ASN D CB  1 
ATOM   6804  C CG  . ASN D  1  102 ? 26.533  17.385  15.781  1.00 22.62  ?  102  ASN D CG  1 
ATOM   6805  O OD1 . ASN D  1  102 ? 27.368  16.487  15.679  1.00 23.10  ?  102  ASN D OD1 1 
ATOM   6806  N ND2 . ASN D  1  102 ? 25.474  17.471  14.987  1.00 22.96  ?  102  ASN D ND2 1 
ATOM   6807  N N   . THR D  1  103 ? 29.933  18.309  18.616  1.00 22.40  ?  103  THR D N   1 
ATOM   6808  C CA  . THR D  1  103 ? 31.359  18.520  18.408  1.00 23.20  ?  103  THR D CA  1 
ATOM   6809  C C   . THR D  1  103 ? 32.116  17.207  18.236  1.00 23.85  ?  103  THR D C   1 
ATOM   6810  O O   . THR D  1  103 ? 33.337  17.222  18.049  1.00 24.71  ?  103  THR D O   1 
ATOM   6811  C CB  . THR D  1  103 ? 31.941  19.326  19.581  1.00 23.45  ?  103  THR D CB  1 
ATOM   6812  O OG1 . THR D  1  103 ? 31.027  20.369  19.934  1.00 22.83  ?  103  THR D OG1 1 
ATOM   6813  C CG2 . THR D  1  103 ? 33.267  19.978  19.201  1.00 24.25  ?  103  THR D CG2 1 
ATOM   6814  N N   . GLY D  1  104 ? 31.417  16.074  18.271  1.00 24.02  ?  104  GLY D N   1 
ATOM   6815  C CA  . GLY D  1  104 ? 32.075  14.789  18.146  1.00 24.67  ?  104  GLY D CA  1 
ATOM   6816  C C   . GLY D  1  104 ? 32.974  14.436  19.305  1.00 25.31  ?  104  GLY D C   1 
ATOM   6817  O O   . GLY D  1  104 ? 33.911  13.652  19.136  1.00 26.17  ?  104  GLY D O   1 
ATOM   6818  N N   . ILE D  1  105 ? 32.717  15.003  20.483  1.00 25.00  ?  105  ILE D N   1 
ATOM   6819  C CA  . ILE D  1  105 ? 33.528  14.709  21.655  1.00 25.61  ?  105  ILE D CA  1 
ATOM   6820  C C   . ILE D  1  105 ? 33.205  13.312  22.164  1.00 25.63  ?  105  ILE D C   1 
ATOM   6821  O O   . ILE D  1  105 ? 32.040  12.894  22.198  1.00 24.88  ?  105  ILE D O   1 
ATOM   6822  C CB  . ILE D  1  105 ? 33.291  15.764  22.747  1.00 25.28  ?  105  ILE D CB  1 
ATOM   6823  C CG1 . ILE D  1  105 ? 33.417  17.171  22.161  1.00 25.16  ?  105  ILE D CG1 1 
ATOM   6824  C CG2 . ILE D  1  105 ? 34.267  15.568  23.891  1.00 26.06  ?  105  ILE D CG2 1 
ATOM   6825  C CD1 . ILE D  1  105 ? 33.389  18.273  23.198  1.00 25.03  ?  105  ILE D CD1 1 
ATOM   6826  N N   . GLU D  1  106 ? 34.242  12.577  22.554  1.00 29.51  ?  106  GLU D N   1 
ATOM   6827  C CA  . GLU D  1  106 ? 34.092  11.283  23.205  1.00 29.67  ?  106  GLU D CA  1 
ATOM   6828  C C   . GLU D  1  106 ? 34.855  11.325  24.520  1.00 30.30  ?  106  GLU D C   1 
ATOM   6829  O O   . GLU D  1  106 ? 36.069  11.555  24.528  1.00 31.27  ?  106  GLU D O   1 
ATOM   6830  C CB  . GLU D  1  106 ? 34.598  10.152  22.311  1.00 30.33  ?  106  GLU D CB  1 
ATOM   6831  C CG  . GLU D  1  106 ? 34.333  8.764   22.864  1.00 30.47  ?  106  GLU D CG  1 
ATOM   6832  C CD  . GLU D  1  106 ? 34.981  7.673   22.037  1.00 31.31  ?  106  GLU D CD  1 
ATOM   6833  O OE1 . GLU D  1  106 ? 34.631  7.539   20.845  1.00 31.10  ?  106  GLU D OE1 1 
ATOM   6834  O OE2 . GLU D  1  106 ? 35.843  6.949   22.577  1.00 32.39  -1 106  GLU D OE2 1 
ATOM   6835  N N   . GLY D  1  107 ? 34.151  11.096  25.623  1.00 26.82  ?  107  GLY D N   1 
ATOM   6836  C CA  . GLY D  1  107 ? 34.796  11.190  26.923  1.00 27.40  ?  107  GLY D CA  1 
ATOM   6837  C C   . GLY D  1  107 ? 33.802  11.055  28.055  1.00 26.76  ?  107  GLY D C   1 
ATOM   6838  O O   . GLY D  1  107 ? 32.754  10.415  27.912  1.00 26.09  ?  107  GLY D O   1 
ATOM   6839  N N   . THR D  1  108 ? 34.154  11.658  29.188  1.00 26.20  ?  108  THR D N   1 
ATOM   6840  C CA  . THR D  1  108 ? 33.387  11.529  30.417  1.00 25.82  ?  108  THR D CA  1 
ATOM   6841  C C   . THR D  1  108 ? 33.417  12.862  31.155  1.00 25.74  ?  108  THR D C   1 
ATOM   6842  O O   . THR D  1  108 ? 34.316  13.682  30.955  1.00 26.24  ?  108  THR D O   1 
ATOM   6843  C CB  . THR D  1  108 ? 33.955  10.388  31.284  1.00 26.62  ?  108  THR D CB  1 
ATOM   6844  O OG1 . THR D  1  108 ? 33.891  9.161   30.550  1.00 26.72  ?  108  THR D OG1 1 
ATOM   6845  C CG2 . THR D  1  108 ? 33.175  10.210  32.579  1.00 26.30  ?  108  THR D CG2 1 
ATOM   6846  N N   . PHE D  1  109 ? 32.416  13.077  32.012  1.00 25.76  ?  109  PHE D N   1 
ATOM   6847  C CA  . PHE D  1  109 ? 32.377  14.225  32.907  1.00 25.77  ?  109  PHE D CA  1 
ATOM   6848  C C   . PHE D  1  109 ? 33.074  13.953  34.238  1.00 26.58  ?  109  PHE D C   1 
ATOM   6849  O O   . PHE D  1  109 ? 32.798  14.644  35.227  1.00 26.56  ?  109  PHE D O   1 
ATOM   6850  C CB  . PHE D  1  109 ? 30.930  14.654  33.159  1.00 24.88  ?  109  PHE D CB  1 
ATOM   6851  C CG  . PHE D  1  109 ? 30.137  14.890  31.906  1.00 24.15  ?  109  PHE D CG  1 
ATOM   6852  C CD1 . PHE D  1  109 ? 30.644  15.677  30.887  1.00 24.17  ?  109  PHE D CD1 1 
ATOM   6853  C CD2 . PHE D  1  109 ? 28.879  14.331  31.753  1.00 23.51  ?  109  PHE D CD2 1 
ATOM   6854  C CE1 . PHE D  1  109 ? 29.913  15.897  29.734  1.00 23.57  ?  109  PHE D CE1 1 
ATOM   6855  C CE2 . PHE D  1  109 ? 28.143  14.548  30.603  1.00 22.94  ?  109  PHE D CE2 1 
ATOM   6856  C CZ  . PHE D  1  109 ? 28.661  15.332  29.593  1.00 22.96  ?  109  PHE D CZ  1 
ATOM   6857  N N   . GLU D  1  110 ? 33.965  12.960  34.286  1.00 31.57  ?  110  GLU D N   1 
ATOM   6858  C CA  . GLU D  1  110 ? 34.677  12.661  35.525  1.00 32.49  ?  110  GLU D CA  1 
ATOM   6859  C C   . GLU D  1  110 ? 35.685  13.753  35.857  1.00 33.24  ?  110  GLU D C   1 
ATOM   6860  O O   . GLU D  1  110 ? 35.857  14.113  37.027  1.00 33.81  ?  110  GLU D O   1 
ATOM   6861  C CB  . GLU D  1  110 ? 35.368  11.301  35.421  1.00 33.52  ?  110  GLU D CB  1 
ATOM   6862  C CG  . GLU D  1  110 ? 36.121  10.887  36.677  1.00 34.86  ?  110  GLU D CG  1 
ATOM   6863  C CD  . GLU D  1  110 ? 35.319  9.948   37.558  1.00 35.30  ?  110  GLU D CD  1 
ATOM   6864  O OE1 . GLU D  1  110 ? 34.461  9.214   37.023  1.00 34.70  ?  110  GLU D OE1 1 
ATOM   6865  O OE2 . GLU D  1  110 ? 35.542  9.945   38.787  1.00 35.23  -1 110  GLU D OE2 1 
ATOM   6866  N N   . ASP D  1  111 ? 36.361  14.293  34.842  1.00 29.91  ?  111  ASP D N   1 
ATOM   6867  C CA  . ASP D  1  111 ? 37.321  15.373  35.024  1.00 30.64  ?  111  ASP D CA  1 
ATOM   6868  C C   . ASP D  1  111 ? 36.767  16.718  34.570  1.00 29.85  ?  111  ASP D C   1 
ATOM   6869  O O   . ASP D  1  111 ? 37.528  17.598  34.151  1.00 30.30  ?  111  ASP D O   1 
ATOM   6870  C CB  . ASP D  1  111 ? 38.623  15.056  34.289  1.00 31.71  ?  111  ASP D CB  1 
ATOM   6871  C CG  . ASP D  1  111 ? 39.430  13.978  34.980  1.00 32.89  ?  111  ASP D CG  1 
ATOM   6872  O OD1 . ASP D  1  111 ? 39.832  14.190  36.144  1.00 33.62  ?  111  ASP D OD1 1 
ATOM   6873  O OD2 . ASP D  1  111 ? 39.660  12.917  34.362  1.00 33.17  -1 111  ASP D OD2 1 
ATOM   6874  N N   . PHE D  1  112 ? 35.456  16.894  34.649  1.00 27.98  ?  112  PHE D N   1 
ATOM   6875  C CA  . PHE D  1  112 ? 34.861  18.184  34.340  1.00 27.33  ?  112  PHE D CA  1 
ATOM   6876  C C   . PHE D  1  112 ? 35.178  19.163  35.463  1.00 27.82  ?  112  PHE D C   1 
ATOM   6877  O O   . PHE D  1  112 ? 34.969  18.839  36.638  1.00 28.05  ?  112  PHE D O   1 
ATOM   6878  C CB  . PHE D  1  112 ? 33.352  18.055  34.158  1.00 26.23  ?  112  PHE D CB  1 
ATOM   6879  C CG  . PHE D  1  112 ? 32.716  19.257  33.524  1.00 25.62  ?  112  PHE D CG  1 
ATOM   6880  C CD1 . PHE D  1  112 ? 32.899  19.522  32.177  1.00 25.40  ?  112  PHE D CD1 1 
ATOM   6881  C CD2 . PHE D  1  112 ? 31.941  20.125  34.274  1.00 25.36  ?  112  PHE D CD2 1 
ATOM   6882  C CE1 . PHE D  1  112 ? 32.317  20.629  31.589  1.00 24.91  ?  112  PHE D CE1 1 
ATOM   6883  C CE2 . PHE D  1  112 ? 31.357  21.234  33.692  1.00 24.92  ?  112  PHE D CE2 1 
ATOM   6884  C CZ  . PHE D  1  112 ? 31.546  21.485  32.348  1.00 24.69  ?  112  PHE D CZ  1 
ATOM   6885  N N   . PRO D  1  113 ? 35.692  20.348  35.156  1.00 28.84  ?  113  PRO D N   1 
ATOM   6886  C CA  . PRO D  1  113 ? 36.102  21.288  36.220  1.00 30.14  ?  113  PRO D CA  1 
ATOM   6887  C C   . PRO D  1  113 ? 34.914  21.990  36.867  1.00 29.62  ?  113  PRO D C   1 
ATOM   6888  O O   . PRO D  1  113 ? 34.645  23.177  36.651  1.00 29.67  ?  113  PRO D O   1 
ATOM   6889  C CB  . PRO D  1  113 ? 37.019  22.252  35.463  1.00 30.95  ?  113  PRO D CB  1 
ATOM   6890  C CG  . PRO D  1  113 ? 36.452  22.285  34.081  1.00 29.68  ?  113  PRO D CG  1 
ATOM   6891  C CD  . PRO D  1  113 ? 35.919  20.899  33.808  1.00 28.54  ?  113  PRO D CD  1 
ATOM   6892  N N   . PHE D  1  114 ? 34.170  21.235  37.679  1.00 29.12  ?  114  PHE D N   1 
ATOM   6893  C CA  . PHE D  1  114 ? 33.046  21.819  38.406  1.00 28.80  ?  114  PHE D CA  1 
ATOM   6894  C C   . PHE D  1  114 ? 33.506  22.952  39.313  1.00 30.19  ?  114  PHE D C   1 
ATOM   6895  O O   . PHE D  1  114 ? 32.883  24.020  39.354  1.00 30.10  ?  114  PHE D O   1 
ATOM   6896  C CB  . PHE D  1  114 ? 32.332  20.748  39.230  1.00 28.40  ?  114  PHE D CB  1 
ATOM   6897  C CG  . PHE D  1  114 ? 31.785  19.615  38.417  1.00 27.19  ?  114  PHE D CG  1 
ATOM   6898  C CD1 . PHE D  1  114 ? 30.602  19.759  37.713  1.00 26.33  ?  114  PHE D CD1 1 
ATOM   6899  C CD2 . PHE D  1  114 ? 32.441  18.397  38.374  1.00 27.57  ?  114  PHE D CD2 1 
ATOM   6900  C CE1 . PHE D  1  114 ? 30.090  18.714  36.971  1.00 25.82  ?  114  PHE D CE1 1 
ATOM   6901  C CE2 . PHE D  1  114 ? 31.935  17.348  37.633  1.00 27.04  ?  114  PHE D CE2 1 
ATOM   6902  C CZ  . PHE D  1  114 ? 30.757  17.507  36.930  1.00 26.14  ?  114  PHE D CZ  1 
ATOM   6903  N N   . SER D  1  115 ? 34.601  22.737  40.044  1.00 28.41  ?  115  SER D N   1 
ATOM   6904  C CA  . SER D  1  115 ? 35.083  23.730  40.995  1.00 29.87  ?  115  SER D CA  1 
ATOM   6905  C C   . SER D  1  115 ? 35.587  24.995  40.316  1.00 30.35  ?  115  SER D C   1 
ATOM   6906  O O   . SER D  1  115 ? 35.684  26.038  40.972  1.00 31.32  ?  115  SER D O   1 
ATOM   6907  C CB  . SER D  1  115 ? 36.199  23.129  41.851  1.00 31.30  ?  115  SER D CB  1 
ATOM   6908  O OG  . SER D  1  115 ? 35.747  21.985  42.554  1.00 31.03  ?  115  SER D OG  1 
ATOM   6909  N N   . SER D  1  116 ? 35.907  24.931  39.025  1.00 29.15  ?  116  SER D N   1 
ATOM   6910  C CA  . SER D  1  116 ? 36.577  26.027  38.342  1.00 29.83  ?  116  SER D CA  1 
ATOM   6911  C C   . SER D  1  116 ? 35.645  26.915  37.527  1.00 28.86  ?  116  SER D C   1 
ATOM   6912  O O   . SER D  1  116 ? 36.096  27.952  37.029  1.00 29.50  ?  116  SER D O   1 
ATOM   6913  C CB  . SER D  1  116 ? 37.674  25.474  37.426  1.00 30.12  ?  116  SER D CB  1 
ATOM   6914  O OG  . SER D  1  116 ? 38.301  24.344  38.009  1.00 30.64  ?  116  SER D OG  1 
ATOM   6915  N N   . LEU D  1  117 ? 34.370  26.558  37.385  1.00 29.26  ?  117  LEU D N   1 
ATOM   6916  C CA  . LEU D  1  117 ? 33.441  27.286  36.515  1.00 28.31  ?  117  LEU D CA  1 
ATOM   6917  C C   . LEU D  1  117 ? 32.203  27.718  37.291  1.00 27.95  ?  117  LEU D C   1 
ATOM   6918  O O   . LEU D  1  117 ? 31.086  27.279  37.001  1.00 26.69  ?  117  LEU D O   1 
ATOM   6919  C CB  . LEU D  1  117 ? 33.052  26.423  35.317  1.00 26.89  ?  117  LEU D CB  1 
ATOM   6920  C CG  . LEU D  1  117 ? 34.202  25.722  34.599  1.00 27.19  ?  117  LEU D CG  1 
ATOM   6921  C CD1 . LEU D  1  117 ? 33.678  24.899  33.436  1.00 25.77  ?  117  LEU D CD1 1 
ATOM   6922  C CD2 . LEU D  1  117 ? 35.219  26.747  34.131  1.00 28.37  ?  117  LEU D CD2 1 
ATOM   6923  N N   . PRO D  1  118 ? 32.363  28.600  38.281  1.00 29.22  ?  118  PRO D N   1 
ATOM   6924  C CA  . PRO D  1  118 ? 31.197  29.026  39.071  1.00 29.05  ?  118  PRO D CA  1 
ATOM   6925  C C   . PRO D  1  118 ? 30.142  29.764  38.265  1.00 28.18  ?  118  PRO D C   1 
ATOM   6926  O O   . PRO D  1  118 ? 28.949  29.649  38.571  1.00 27.49  ?  118  PRO D O   1 
ATOM   6927  C CB  . PRO D  1  118 ? 31.820  29.924  40.146  1.00 30.72  ?  118  PRO D CB  1 
ATOM   6928  C CG  . PRO D  1  118 ? 33.037  30.477  39.494  1.00 31.56  ?  118  PRO D CG  1 
ATOM   6929  C CD  . PRO D  1  118 ? 33.572  29.368  38.630  1.00 30.83  ?  118  PRO D CD  1 
ATOM   6930  N N   . ASN D  1  119 ? 30.543  30.520  37.243  1.00 31.22  ?  119  ASN D N   1 
ATOM   6931  C CA  . ASN D  1  119 ? 29.651  31.446  36.559  1.00 30.76  ?  119  ASN D CA  1 
ATOM   6932  C C   . ASN D  1  119 ? 28.971  30.833  35.334  1.00 29.24  ?  119  ASN D C   1 
ATOM   6933  O O   . ASN D  1  119 ? 28.456  31.576  34.491  1.00 28.93  ?  119  ASN D O   1 
ATOM   6934  C CB  . ASN D  1  119 ? 30.417  32.710  36.158  1.00 31.90  ?  119  ASN D CB  1 
ATOM   6935  C CG  . ASN D  1  119 ? 30.819  33.555  37.357  1.00 33.42  ?  119  ASN D CG  1 
ATOM   6936  O OD1 . ASN D  1  119 ? 30.083  33.650  38.338  1.00 33.54  ?  119  ASN D OD1 1 
ATOM   6937  N ND2 . ASN D  1  119 ? 31.994  34.179  37.275  1.00 34.67  ?  119  ASN D ND2 1 
ATOM   6938  N N   . LEU D  1  120 ? 28.956  29.507  35.214  1.00 26.38  ?  120  LEU D N   1 
ATOM   6939  C CA  . LEU D  1  120 ? 28.298  28.873  34.077  1.00 25.28  ?  120  LEU D CA  1 
ATOM   6940  C C   . LEU D  1  120 ? 26.786  29.051  34.161  1.00 25.13  ?  120  LEU D C   1 
ATOM   6941  O O   . LEU D  1  120 ? 26.168  28.736  35.182  1.00 25.28  ?  120  LEU D O   1 
ATOM   6942  C CB  . LEU D  1  120 ? 28.642  27.386  34.013  1.00 24.80  ?  120  LEU D CB  1 
ATOM   6943  C CG  . LEU D  1  120 ? 29.959  26.992  33.345  1.00 24.82  ?  120  LEU D CG  1 
ATOM   6944  C CD1 . LEU D  1  120 ? 30.090  25.479  33.307  1.00 24.50  ?  120  LEU D CD1 1 
ATOM   6945  C CD2 . LEU D  1  120 ? 30.041  27.577  31.943  1.00 24.60  ?  120  LEU D CD2 1 
ATOM   6946  N N   . THR D  1  121 ? 26.193  29.563  33.082  1.00 24.21  ?  121  THR D N   1 
ATOM   6947  C CA  . THR D  1  121 ? 24.747  29.716  32.984  1.00 24.11  ?  121  THR D CA  1 
ATOM   6948  C C   . THR D  1  121 ? 24.121  28.931  31.840  1.00 23.34  ?  121  THR D C   1 
ATOM   6949  O O   . THR D  1  121 ? 22.950  28.558  31.940  1.00 23.16  ?  121  THR D O   1 
ATOM   6950  C CB  . THR D  1  121 ? 24.369  31.199  32.822  1.00 24.76  ?  121  THR D CB  1 
ATOM   6951  O OG1 . THR D  1  121 ? 24.677  31.632  31.492  1.00 24.56  ?  121  THR D OG1 1 
ATOM   6952  C CG2 . THR D  1  121 ? 25.132  32.060  33.817  1.00 25.64  ?  121  THR D CG2 1 
ATOM   6953  N N   . PHE D  1  122 ? 24.865  28.663  30.768  1.00 24.64  ?  122  PHE D N   1 
ATOM   6954  C CA  . PHE D  1  122 ? 24.364  27.921  29.616  1.00 23.99  ?  122  PHE D CA  1 
ATOM   6955  C C   . PHE D  1  122 ? 25.316  26.770  29.335  1.00 23.64  ?  122  PHE D C   1 
ATOM   6956  O O   . PHE D  1  122 ? 26.496  26.996  29.045  1.00 23.83  ?  122  PHE D O   1 
ATOM   6957  C CB  . PHE D  1  122 ? 24.239  28.831  28.386  1.00 24.01  ?  122  PHE D CB  1 
ATOM   6958  C CG  . PHE D  1  122 ? 23.785  28.120  27.134  1.00 23.40  ?  122  PHE D CG  1 
ATOM   6959  C CD1 . PHE D  1  122 ? 24.680  27.398  26.356  1.00 23.07  ?  122  PHE D CD1 1 
ATOM   6960  C CD2 . PHE D  1  122 ? 22.464  28.193  26.725  1.00 23.25  ?  122  PHE D CD2 1 
ATOM   6961  C CE1 . PHE D  1  122 ? 24.262  26.748  25.211  1.00 22.60  ?  122  PHE D CE1 1 
ATOM   6962  C CE2 . PHE D  1  122 ? 22.042  27.552  25.575  1.00 22.75  ?  122  PHE D CE2 1 
ATOM   6963  C CZ  . PHE D  1  122 ? 22.941  26.827  24.819  1.00 22.41  ?  122  PHE D CZ  1 
ATOM   6964  N N   . VAL D  1  123 ? 24.807  25.542  29.409  1.00 21.15  ?  123  VAL D N   1 
ATOM   6965  C CA  . VAL D  1  123 ? 25.591  24.344  29.134  1.00 20.93  ?  123  VAL D CA  1 
ATOM   6966  C C   . VAL D  1  123 ? 24.808  23.467  28.167  1.00 20.40  ?  123  VAL D C   1 
ATOM   6967  O O   . VAL D  1  123 ? 23.712  22.997  28.498  1.00 20.20  ?  123  VAL D O   1 
ATOM   6968  C CB  . VAL D  1  123 ? 25.926  23.564  30.416  1.00 21.13  ?  123  VAL D CB  1 
ATOM   6969  C CG1 . VAL D  1  123 ? 26.512  22.203  30.069  1.00 20.97  ?  123  VAL D CG1 1 
ATOM   6970  C CG2 . VAL D  1  123 ? 26.893  24.356  31.280  1.00 21.72  ?  123  VAL D CG2 1 
ATOM   6971  N N   . ASP D  1  124 ? 25.366  23.247  26.978  1.00 21.48  ?  124  ASP D N   1 
ATOM   6972  C CA  . ASP D  1  124 ? 24.806  22.317  25.998  1.00 21.06  ?  124  ASP D CA  1 
ATOM   6973  C C   . ASP D  1  124 ? 25.940  21.419  25.516  1.00 21.15  ?  124  ASP D C   1 
ATOM   6974  O O   . ASP D  1  124 ? 26.788  21.847  24.726  1.00 21.32  ?  124  ASP D O   1 
ATOM   6975  C CB  . ASP D  1  124 ? 24.147  23.056  24.836  1.00 20.85  ?  124  ASP D CB  1 
ATOM   6976  C CG  . ASP D  1  124 ? 23.287  22.145  23.974  1.00 20.44  ?  124  ASP D CG  1 
ATOM   6977  O OD1 . ASP D  1  124 ? 23.680  20.982  23.739  1.00 20.33  ?  124  ASP D OD1 1 
ATOM   6978  O OD2 . ASP D  1  124 ? 22.211  22.596  23.529  1.00 20.29  -1 124  ASP D OD2 1 
ATOM   6979  N N   . LEU D  1  125 ? 25.952  20.178  25.993  1.00 20.65  ?  125  LEU D N   1 
ATOM   6980  C CA  . LEU D  1  125 ? 26.928  19.172  25.597  1.00 20.86  ?  125  LEU D CA  1 
ATOM   6981  C C   . LEU D  1  125 ? 26.244  18.023  24.868  1.00 20.53  ?  125  LEU D C   1 
ATOM   6982  O O   . LEU D  1  125 ? 26.614  16.857  25.017  1.00 20.69  ?  125  LEU D O   1 
ATOM   6983  C CB  . LEU D  1  125 ? 27.700  18.661  26.811  1.00 21.30  ?  125  LEU D CB  1 
ATOM   6984  C CG  . LEU D  1  125 ? 28.375  19.741  27.657  1.00 21.70  ?  125  LEU D CG  1 
ATOM   6985  C CD1 . LEU D  1  125 ? 28.840  19.170  28.986  1.00 22.10  ?  125  LEU D CD1 1 
ATOM   6986  C CD2 . LEU D  1  125 ? 29.537  20.364  26.903  1.00 22.08  ?  125  LEU D CD2 1 
ATOM   6987  N N   . SER D  1  126 ? 25.234  18.346  24.069  1.00 22.57  ?  126  SER D N   1 
ATOM   6988  C CA  . SER D  1  126 ? 24.403  17.333  23.440  1.00 22.18  ?  126  SER D CA  1 
ATOM   6989  C C   . SER D  1  126 ? 25.005  16.864  22.120  1.00 22.26  ?  126  SER D C   1 
ATOM   6990  O O   . SER D  1  126 ? 25.867  17.522  21.530  1.00 22.73  ?  126  SER D O   1 
ATOM   6991  C CB  . SER D  1  126 ? 22.986  17.864  23.213  1.00 21.80  ?  126  SER D CB  1 
ATOM   6992  O OG  . SER D  1  126 ? 23.003  19.041  22.428  1.00 21.79  ?  126  SER D OG  1 
ATOM   6993  N N   . MET D  1  127 ? 24.546  15.693  21.674  1.00 24.04  ?  127  MET D N   1 
ATOM   6994  C CA  . MET D  1  127 ? 24.962  15.087  20.408  1.00 24.15  ?  127  MET D CA  1 
ATOM   6995  C C   . MET D  1  127 ? 26.467  14.815  20.394  1.00 24.77  ?  127  MET D C   1 
ATOM   6996  O O   . MET D  1  127 ? 27.204  15.254  19.509  1.00 25.11  ?  127  MET D O   1 
ATOM   6997  C CB  . MET D  1  127 ? 24.547  15.951  19.213  1.00 24.03  ?  127  MET D CB  1 
ATOM   6998  C CG  . MET D  1  127 ? 23.085  15.821  18.835  1.00 23.84  ?  127  MET D CG  1 
ATOM   6999  S SD  . MET D  1  127 ? 22.758  16.398  17.160  1.00 23.83  ?  127  MET D SD  1 
ATOM   7000  C CE  . MET D  1  127 ? 22.761  18.172  17.408  1.00 24.67  ?  127  MET D CE  1 
ATOM   7001  N N   . ASN D  1  128 ? 26.914  14.071  21.400  1.00 22.78  ?  128  ASN D N   1 
ATOM   7002  C CA  . ASN D  1  128 ? 28.312  13.683  21.515  1.00 23.49  ?  128  ASN D CA  1 
ATOM   7003  C C   . ASN D  1  128 ? 28.360  12.244  22.014  1.00 23.72  ?  128  ASN D C   1 
ATOM   7004  O O   . ASN D  1  128 ? 27.344  11.544  22.055  1.00 23.45  ?  128  ASN D O   1 
ATOM   7005  C CB  . ASN D  1  128 ? 29.077  14.650  22.429  1.00 23.80  ?  128  ASN D CB  1 
ATOM   7006  C CG  . ASN D  1  128 ? 29.241  16.028  21.816  1.00 23.72  ?  128  ASN D CG  1 
ATOM   7007  O OD1 . ASN D  1  128 ? 29.924  16.192  20.805  1.00 24.05  ?  128  ASN D OD1 1 
ATOM   7008  N ND2 . ASN D  1  128 ? 28.615  17.027  22.427  1.00 23.35  ?  128  ASN D ND2 1 
ATOM   7009  N N   . ARG D  1  129 ? 29.550  11.802  22.402  1.00 25.75  ?  129  ARG D N   1 
ATOM   7010  C CA  . ARG D  1  129 ? 29.768  10.451  22.900  1.00 26.12  ?  129  ARG D CA  1 
ATOM   7011  C C   . ARG D  1  129 ? 30.225  10.481  24.352  1.00 26.44  ?  129  ARG D C   1 
ATOM   7012  O O   . ARG D  1  129 ? 31.133  9.750   24.756  1.00 27.23  ?  129  ARG D O   1 
ATOM   7013  C CB  . ARG D  1  129 ? 30.769  9.696   22.030  1.00 26.90  ?  129  ARG D CB  1 
ATOM   7014  C CG  . ARG D  1  129 ? 30.588  9.920   20.539  1.00 26.92  ?  129  ARG D CG  1 
ATOM   7015  C CD  . ARG D  1  129 ? 31.179  8.768   19.748  1.00 27.52  ?  129  ARG D CD  1 
ATOM   7016  N NE  . ARG D  1  129 ? 30.428  7.535   19.954  1.00 28.02  ?  129  ARG D NE  1 
ATOM   7017  C CZ  . ARG D  1  129 ? 30.929  6.435   20.499  1.00 29.18  ?  129  ARG D CZ  1 
ATOM   7018  N NH1 . ARG D  1  129 ? 32.185  6.378   20.914  1.00 30.03  ?  129  ARG D NH1 1 
ATOM   7019  N NH2 . ARG D  1  129 ? 30.151  5.365   20.632  1.00 28.68  ?  129  ARG D NH2 1 
ATOM   7020  N N   . PHE D  1  130 ? 29.605  11.344  25.151  1.00 23.19  ?  130  PHE D N   1 
ATOM   7021  C CA  . PHE D  1  130 ? 29.903  11.377  26.574  1.00 23.47  ?  130  PHE D CA  1 
ATOM   7022  C C   . PHE D  1  130 ? 29.266  10.177  27.257  1.00 23.36  ?  130  PHE D C   1 
ATOM   7023  O O   . PHE D  1  130 ? 28.072  9.910   27.090  1.00 22.73  ?  130  PHE D O   1 
ATOM   7024  C CB  . PHE D  1  130 ? 29.394  12.674  27.200  1.00 23.05  ?  130  PHE D CB  1 
ATOM   7025  C CG  . PHE D  1  130 ? 30.214  13.878  26.846  1.00 23.32  ?  130  PHE D CG  1 
ATOM   7026  C CD1 . PHE D  1  130 ? 31.524  13.989  27.280  1.00 24.13  ?  130  PHE D CD1 1 
ATOM   7027  C CD2 . PHE D  1  130 ? 29.676  14.900  26.084  1.00 22.84  ?  130  PHE D CD2 1 
ATOM   7028  C CE1 . PHE D  1  130 ? 32.284  15.097  26.957  1.00 24.44  ?  130  PHE D CE1 1 
ATOM   7029  C CE2 . PHE D  1  130 ? 30.429  16.011  25.758  1.00 23.11  ?  130  PHE D CE2 1 
ATOM   7030  C CZ  . PHE D  1  130 ? 31.733  16.111  26.196  1.00 23.89  ?  130  PHE D CZ  1 
ATOM   7031  N N   . SER D  1  131 ? 30.071  9.451   28.024  1.00 23.41  ?  131  SER D N   1 
ATOM   7032  C CA  . SER D  1  131 ? 29.633  8.267   28.741  1.00 23.44  ?  131  SER D CA  1 
ATOM   7033  C C   . SER D  1  131 ? 29.919  8.439   30.226  1.00 23.78  ?  131  SER D C   1 
ATOM   7034  O O   . SER D  1  131 ? 30.776  9.229   30.629  1.00 24.23  ?  131  SER D O   1 
ATOM   7035  C CB  . SER D  1  131 ? 30.325  7.005   28.208  1.00 24.09  ?  131  SER D CB  1 
ATOM   7036  O OG  . SER D  1  131 ? 31.732  7.107   28.330  1.00 25.04  ?  131  SER D OG  1 
ATOM   7037  N N   . GLY D  1  132 ? 29.178  7.691   31.042  1.00 23.62  ?  132  GLY D N   1 
ATOM   7038  C CA  . GLY D  1  132 ? 29.324  7.747   32.480  1.00 23.94  ?  132  GLY D CA  1 
ATOM   7039  C C   . GLY D  1  132 ? 28.024  8.144   33.157  1.00 23.26  ?  132  GLY D C   1 
ATOM   7040  O O   . GLY D  1  132 ? 26.930  7.843   32.664  1.00 22.64  ?  132  GLY D O   1 
ATOM   7041  N N   . THR D  1  133 ? 28.157  8.825   34.288  1.00 23.32  ?  133  THR D N   1 
ATOM   7042  C CA  . THR D  1  133 ? 27.020  9.222   35.099  1.00 22.87  ?  133  THR D CA  1 
ATOM   7043  C C   . THR D  1  133 ? 26.958  10.740  35.206  1.00 22.70  ?  133  THR D C   1 
ATOM   7044  O O   . THR D  1  133 ? 27.891  11.456  34.832  1.00 22.98  ?  133  THR D O   1 
ATOM   7045  C CB  . THR D  1  133 ? 27.096  8.593   36.496  1.00 23.33  ?  133  THR D CB  1 
ATOM   7046  O OG1 . THR D  1  133 ? 28.402  8.806   37.045  1.00 24.14  ?  133  THR D OG1 1 
ATOM   7047  C CG2 . THR D  1  133 ? 26.831  7.098   36.419  1.00 23.40  ?  133  THR D CG2 1 
ATOM   7048  N N   . ILE D  1  134 ? 25.836  11.224  35.727  1.00 22.41  ?  134  ILE D N   1 
ATOM   7049  C CA  . ILE D  1  134 ? 25.631  12.649  35.950  1.00 22.31  ?  134  ILE D CA  1 
ATOM   7050  C C   . ILE D  1  134 ? 26.020  12.941  37.394  1.00 22.84  ?  134  ILE D C   1 
ATOM   7051  O O   . ILE D  1  134 ? 25.294  12.591  38.328  1.00 22.87  ?  134  ILE D O   1 
ATOM   7052  C CB  . ILE D  1  134 ? 24.184  13.063  35.660  1.00 21.76  ?  134  ILE D CB  1 
ATOM   7053  C CG1 . ILE D  1  134 ? 23.829  12.745  34.206  1.00 21.64  ?  134  ILE D CG1 1 
ATOM   7054  C CG2 . ILE D  1  134 ? 23.986  14.544  35.948  1.00 22.14  ?  134  ILE D CG2 1 
ATOM   7055  C CD1 . ILE D  1  134 ? 22.382  13.008  33.857  1.00 21.19  ?  134  ILE D CD1 1 
ATOM   7056  N N   . SER D  1  135 ? 27.181  13.565  37.572  1.00 24.79  ?  135  SER D N   1 
ATOM   7057  C CA  . SER D  1  135 ? 27.702  13.823  38.903  1.00 25.42  ?  135  SER D CA  1 
ATOM   7058  C C   . SER D  1  135 ? 26.774  14.762  39.674  1.00 25.27  ?  135  SER D C   1 
ATOM   7059  O O   . SER D  1  135 ? 26.133  15.639  39.086  1.00 24.87  ?  135  SER D O   1 
ATOM   7060  C CB  . SER D  1  135 ? 29.101  14.429  38.816  1.00 26.06  ?  135  SER D CB  1 
ATOM   7061  O OG  . SER D  1  135 ? 29.609  14.729  40.103  1.00 26.72  ?  135  SER D OG  1 
ATOM   7062  N N   . PRO D  1  136 ? 26.680  14.592  40.994  1.00 25.31  ?  136  PRO D N   1 
ATOM   7063  C CA  . PRO D  1  136 ? 25.938  15.567  41.807  1.00 25.39  ?  136  PRO D CA  1 
ATOM   7064  C C   . PRO D  1  136 ? 26.496  16.971  41.699  1.00 25.61  ?  136  PRO D C   1 
ATOM   7065  O O   . PRO D  1  136 ? 25.766  17.937  41.952  1.00 25.60  ?  136  PRO D O   1 
ATOM   7066  C CB  . PRO D  1  136 ? 26.082  15.016  43.232  1.00 25.97  ?  136  PRO D CB  1 
ATOM   7067  C CG  . PRO D  1  136 ? 26.345  13.558  43.047  1.00 25.96  ?  136  PRO D CG  1 
ATOM   7068  C CD  . PRO D  1  136 ? 27.164  13.456  41.796  1.00 25.80  ?  136  PRO D CD  1 
ATOM   7069  N N   . GLU D  1  137 ? 27.769  17.110  41.320  1.00 30.02  ?  137  GLU D N   1 
ATOM   7070  C CA  . GLU D  1  137 ? 28.407  18.417  41.226  1.00 30.31  ?  137  GLU D CA  1 
ATOM   7071  C C   . GLU D  1  137 ? 27.725  19.329  40.215  1.00 30.01  ?  137  GLU D C   1 
ATOM   7072  O O   . GLU D  1  137 ? 27.924  20.548  40.266  1.00 30.30  ?  137  GLU D O   1 
ATOM   7073  C CB  . GLU D  1  137 ? 29.879  18.246  40.858  1.00 30.81  ?  137  GLU D CB  1 
ATOM   7074  C CG  . GLU D  1  137 ? 30.648  17.314  41.776  1.00 31.81  ?  137  GLU D CG  1 
ATOM   7075  C CD  . GLU D  1  137 ? 31.172  18.015  43.010  1.00 33.94  ?  137  GLU D CD  1 
ATOM   7076  O OE1 . GLU D  1  137 ? 30.360  18.331  43.905  1.00 34.32  ?  137  GLU D OE1 1 
ATOM   7077  O OE2 . GLU D  1  137 ? 32.396  18.251  43.084  1.00 35.89  -1 137  GLU D OE2 1 
ATOM   7078  N N   . TRP D  1  138 ? 26.937  18.769  39.292  1.00 24.78  ?  138  TRP D N   1 
ATOM   7079  C CA  . TRP D  1  138 ? 26.213  19.599  38.336  1.00 24.34  ?  138  TRP D CA  1 
ATOM   7080  C C   . TRP D  1  138 ? 25.250  20.548  39.037  1.00 24.52  ?  138  TRP D C   1 
ATOM   7081  O O   . TRP D  1  138 ? 24.941  21.622  38.508  1.00 24.49  ?  138  TRP D O   1 
ATOM   7082  C CB  . TRP D  1  138 ? 25.458  18.717  37.343  1.00 23.71  ?  138  TRP D CB  1 
ATOM   7083  C CG  . TRP D  1  138 ? 26.335  18.083  36.302  1.00 23.57  ?  138  TRP D CG  1 
ATOM   7084  C CD1 . TRP D  1  138 ? 26.727  16.777  36.246  1.00 23.60  ?  138  TRP D CD1 1 
ATOM   7085  C CD2 . TRP D  1  138 ? 26.924  18.727  35.165  1.00 23.47  ?  138  TRP D CD2 1 
ATOM   7086  N NE1 . TRP D  1  138 ? 27.525  16.569  35.148  1.00 23.59  ?  138  TRP D NE1 1 
ATOM   7087  C CE2 . TRP D  1  138 ? 27.662  17.749  34.467  1.00 23.49  ?  138  TRP D CE2 1 
ATOM   7088  C CE3 . TRP D  1  138 ? 26.904  20.035  34.671  1.00 23.44  ?  138  TRP D CE3 1 
ATOM   7089  C CZ2 . TRP D  1  138 ? 28.370  18.038  33.302  1.00 23.48  ?  138  TRP D CZ2 1 
ATOM   7090  C CZ3 . TRP D  1  138 ? 27.605  20.318  33.511  1.00 23.37  ?  138  TRP D CZ3 1 
ATOM   7091  C CH2 . TRP D  1  138 ? 28.329  19.325  32.841  1.00 23.40  ?  138  TRP D CH2 1 
ATOM   7092  N N   . GLY D  1  139 ? 24.772  20.177  40.225  1.00 25.94  ?  139  GLY D N   1 
ATOM   7093  C CA  . GLY D  1  139 ? 23.903  21.050  40.993  1.00 26.35  ?  139  GLY D CA  1 
ATOM   7094  C C   . GLY D  1  139 ? 24.602  22.230  41.636  1.00 27.01  ?  139  GLY D C   1 
ATOM   7095  O O   . GLY D  1  139 ? 23.922  23.097  42.196  1.00 27.49  ?  139  GLY D O   1 
ATOM   7096  N N   . ARG D  1  140 ? 25.934  22.283  41.574  1.00 29.29  ?  140  ARG D N   1 
ATOM   7097  C CA  . ARG D  1  140 ? 26.687  23.385  42.159  1.00 30.17  ?  140  ARG D CA  1 
ATOM   7098  C C   . ARG D  1  140 ? 26.688  24.637  41.291  1.00 30.01  ?  140  ARG D C   1 
ATOM   7099  O O   . ARG D  1  140 ? 27.074  25.706  41.778  1.00 31.74  ?  140  ARG D O   1 
ATOM   7100  C CB  . ARG D  1  140 ? 28.128  22.946  42.431  1.00 31.25  ?  140  ARG D CB  1 
ATOM   7101  C CG  . ARG D  1  140 ? 28.242  21.838  43.467  1.00 32.63  ?  140  ARG D CG  1 
ATOM   7102  C CD  . ARG D  1  140 ? 29.536  21.941  44.253  1.00 34.82  ?  140  ARG D CD  1 
ATOM   7103  N NE  . ARG D  1  140 ? 30.691  21.594  43.435  1.00 34.64  ?  140  ARG D NE  1 
ATOM   7104  C CZ  . ARG D  1  140 ? 31.830  22.273  43.418  1.00 35.51  ?  140  ARG D CZ  1 
ATOM   7105  N NH1 . ARG D  1  140 ? 32.006  23.345  44.172  1.00 37.33  ?  140  ARG D NH1 1 
ATOM   7106  N NH2 . ARG D  1  140 ? 32.816  21.864  42.626  1.00 35.00  ?  140  ARG D NH2 1 
ATOM   7107  N N   . PHE D  1  141 ? 26.267  24.538  40.032  1.00 24.85  ?  141  PHE D N   1 
ATOM   7108  C CA  . PHE D  1  141 ? 26.256  25.682  39.122  1.00 24.83  ?  141  PHE D CA  1 
ATOM   7109  C C   . PHE D  1  141 ? 25.034  26.535  39.442  1.00 25.16  ?  141  PHE D C   1 
ATOM   7110  O O   . PHE D  1  141 ? 23.974  26.402  38.830  1.00 24.77  ?  141  PHE D O   1 
ATOM   7111  C CB  . PHE D  1  141 ? 26.260  25.215  37.672  1.00 24.09  ?  141  PHE D CB  1 
ATOM   7112  C CG  . PHE D  1  141 ? 27.515  24.488  37.275  1.00 23.98  ?  141  PHE D CG  1 
ATOM   7113  C CD1 . PHE D  1  141 ? 28.737  25.139  37.274  1.00 24.45  ?  141  PHE D CD1 1 
ATOM   7114  C CD2 . PHE D  1  141 ? 27.472  23.154  36.906  1.00 23.53  ?  141  PHE D CD2 1 
ATOM   7115  C CE1 . PHE D  1  141 ? 29.893  24.473  36.912  1.00 24.59  ?  141  PHE D CE1 1 
ATOM   7116  C CE2 . PHE D  1  141 ? 28.625  22.483  36.542  1.00 23.62  ?  141  PHE D CE2 1 
ATOM   7117  C CZ  . PHE D  1  141 ? 29.837  23.144  36.545  1.00 24.15  ?  141  PHE D CZ  1 
ATOM   7118  N N   . SER D  1  142 ? 25.193  27.430  40.421  1.00 25.55  ?  142  SER D N   1 
ATOM   7119  C CA  . SER D  1  142 ? 24.065  28.216  40.912  1.00 26.13  ?  142  SER D CA  1 
ATOM   7120  C C   . SER D  1  142 ? 23.489  29.113  39.823  1.00 26.01  ?  142  SER D C   1 
ATOM   7121  O O   . SER D  1  142 ? 22.271  29.317  39.755  1.00 26.11  ?  142  SER D O   1 
ATOM   7122  C CB  . SER D  1  142 ? 24.495  29.047  42.121  1.00 27.23  ?  142  SER D CB  1 
ATOM   7123  O OG  . SER D  1  142 ? 25.501  29.980  41.766  1.00 27.59  ?  142  SER D OG  1 
ATOM   7124  N N   . LYS D  1  143 ? 24.345  29.660  38.963  1.00 25.43  ?  143  LYS D N   1 
ATOM   7125  C CA  . LYS D  1  143 ? 23.894  30.571  37.921  1.00 25.41  ?  143  LYS D CA  1 
ATOM   7126  C C   . LYS D  1  143 ? 23.313  29.852  36.712  1.00 24.48  ?  143  LYS D C   1 
ATOM   7127  O O   . LYS D  1  143 ? 22.812  30.519  35.801  1.00 24.44  ?  143  LYS D O   1 
ATOM   7128  C CB  . LYS D  1  143 ? 25.054  31.462  37.472  1.00 25.74  ?  143  LYS D CB  1 
ATOM   7129  C CG  . LYS D  1  143 ? 25.557  32.411  38.543  1.00 26.86  ?  143  LYS D CG  1 
ATOM   7130  C CD  . LYS D  1  143 ? 26.617  33.344  37.990  1.00 27.27  ?  143  LYS D CD  1 
ATOM   7131  C CE  . LYS D  1  143 ? 27.009  34.401  39.006  1.00 28.80  ?  143  LYS D CE  1 
ATOM   7132  N NZ  . LYS D  1  143 ? 27.960  35.383  38.418  1.00 29.70  ?  143  LYS D NZ  1 
ATOM   7133  N N   . LEU D  1  144 ? 23.367  28.521  36.683  1.00 23.57  ?  144  LEU D N   1 
ATOM   7134  C CA  . LEU D  1  144 ? 22.958  27.771  35.503  1.00 22.75  ?  144  LEU D CA  1 
ATOM   7135  C C   . LEU D  1  144 ? 21.469  27.939  35.227  1.00 22.73  ?  144  LEU D C   1 
ATOM   7136  O O   . LEU D  1  144 ? 20.634  27.780  36.123  1.00 23.06  ?  144  LEU D O   1 
ATOM   7137  C CB  . LEU D  1  144 ? 23.293  26.291  35.673  1.00 22.24  ?  144  LEU D CB  1 
ATOM   7138  C CG  . LEU D  1  144 ? 23.260  25.486  34.373  1.00 21.49  ?  144  LEU D CG  1 
ATOM   7139  C CD1 . LEU D  1  144 ? 24.384  25.923  33.451  1.00 21.42  ?  144  LEU D CD1 1 
ATOM   7140  C CD2 . LEU D  1  144 ? 23.337  23.994  34.653  1.00 21.14  ?  144  LEU D CD2 1 
ATOM   7141  N N   . GLU D  1  145 ? 21.142  28.251  33.976  1.00 22.35  ?  145  GLU D N   1 
ATOM   7142  C CA  . GLU D  1  145 ? 19.770  28.419  33.520  1.00 22.34  ?  145  GLU D CA  1 
ATOM   7143  C C   . GLU D  1  145 ? 19.373  27.440  32.427  1.00 21.56  ?  145  GLU D C   1 
ATOM   7144  O O   . GLU D  1  145 ? 18.194  27.097  32.325  1.00 21.49  ?  145  GLU D O   1 
ATOM   7145  C CB  . GLU D  1  145 ? 19.553  29.852  33.008  1.00 22.86  ?  145  GLU D CB  1 
ATOM   7146  C CG  . GLU D  1  145 ? 20.264  30.909  33.834  1.00 23.67  ?  145  GLU D CG  1 
ATOM   7147  C CD  . GLU D  1  145 ? 19.974  32.317  33.360  1.00 24.31  ?  145  GLU D CD  1 
ATOM   7148  O OE1 . GLU D  1  145 ? 19.673  32.492  32.161  1.00 23.99  ?  145  GLU D OE1 1 
ATOM   7149  O OE2 . GLU D  1  145 ? 20.058  33.251  34.186  1.00 25.20  -1 145  GLU D OE2 1 
ATOM   7150  N N   . TYR D  1  146 ? 20.324  26.984  31.614  1.00 20.36  ?  146  TYR D N   1 
ATOM   7151  C CA  . TYR D  1  146 ? 20.066  26.055  30.521  1.00 19.69  ?  146  TYR D CA  1 
ATOM   7152  C C   . TYR D  1  146 ? 21.003  24.868  30.678  1.00 19.33  ?  146  TYR D C   1 
ATOM   7153  O O   . TYR D  1  146 ? 22.225  25.044  30.723  1.00 19.44  ?  146  TYR D O   1 
ATOM   7154  C CB  . TYR D  1  146 ? 20.277  26.737  29.166  1.00 19.55  ?  146  TYR D CB  1 
ATOM   7155  C CG  . TYR D  1  146 ? 19.822  25.929  27.974  1.00 18.97  ?  146  TYR D CG  1 
ATOM   7156  C CD1 . TYR D  1  146 ? 18.517  26.019  27.507  1.00 18.94  ?  146  TYR D CD1 1 
ATOM   7157  C CD2 . TYR D  1  146 ? 20.695  25.074  27.316  1.00 18.54  ?  146  TYR D CD2 1 
ATOM   7158  C CE1 . TYR D  1  146 ? 18.098  25.286  26.415  1.00 18.46  ?  146  TYR D CE1 1 
ATOM   7159  C CE2 . TYR D  1  146 ? 20.285  24.337  26.223  1.00 18.09  ?  146  TYR D CE2 1 
ATOM   7160  C CZ  . TYR D  1  146 ? 18.985  24.445  25.778  1.00 18.03  ?  146  TYR D CZ  1 
ATOM   7161  O OH  . TYR D  1  146 ? 18.570  23.712  24.691  1.00 17.62  ?  146  TYR D OH  1 
ATOM   7162  N N   . PHE D  1  147 ? 20.436  23.667  30.762  1.00 19.37  ?  147  PHE D N   1 
ATOM   7163  C CA  . PHE D  1  147 ? 21.201  22.447  31.005  1.00 19.14  ?  147  PHE D CA  1 
ATOM   7164  C C   . PHE D  1  147 ? 20.779  21.401  29.983  1.00 18.63  ?  147  PHE D C   1 
ATOM   7165  O O   . PHE D  1  147 ? 19.641  20.923  30.016  1.00 18.50  ?  147  PHE D O   1 
ATOM   7166  C CB  . PHE D  1  147 ? 20.981  21.946  32.432  1.00 19.41  ?  147  PHE D CB  1 
ATOM   7167  C CG  . PHE D  1  147 ? 21.963  20.902  32.869  1.00 19.37  ?  147  PHE D CG  1 
ATOM   7168  C CD1 . PHE D  1  147 ? 23.256  20.903  32.375  1.00 19.38  ?  147  PHE D CD1 1 
ATOM   7169  C CD2 . PHE D  1  147 ? 21.599  19.927  33.783  1.00 19.42  ?  147  PHE D CD2 1 
ATOM   7170  C CE1 . PHE D  1  147 ? 24.163  19.945  32.775  1.00 19.48  ?  147  PHE D CE1 1 
ATOM   7171  C CE2 . PHE D  1  147 ? 22.504  18.967  34.189  1.00 19.47  ?  147  PHE D CE2 1 
ATOM   7172  C CZ  . PHE D  1  147 ? 23.788  18.977  33.684  1.00 19.53  ?  147  PHE D CZ  1 
ATOM   7173  N N   . ASP D  1  148 ? 21.693  21.037  29.084  1.00 20.39  ?  148  ASP D N   1 
ATOM   7174  C CA  . ASP D  1  148 ? 21.392  20.126  27.979  1.00 19.98  ?  148  ASP D CA  1 
ATOM   7175  C C   . ASP D  1  148 ? 22.508  19.091  27.865  1.00 19.98  ?  148  ASP D C   1 
ATOM   7176  O O   . ASP D  1  148 ? 23.597  19.391  27.369  1.00 20.12  ?  148  ASP D O   1 
ATOM   7177  C CB  . ASP D  1  148 ? 21.218  20.893  26.672  1.00 19.83  ?  148  ASP D CB  1 
ATOM   7178  C CG  . ASP D  1  148 ? 20.475  20.094  25.616  1.00 19.45  ?  148  ASP D CG  1 
ATOM   7179  O OD1 . ASP D  1  148 ? 20.489  18.846  25.684  1.00 19.30  ?  148  ASP D OD1 1 
ATOM   7180  O OD2 . ASP D  1  148 ? 19.872  20.715  24.716  1.00 19.35  -1 148  ASP D OD2 1 
ATOM   7181  N N   . LEU D  1  149 ? 22.221  17.868  28.313  1.00 17.81  ?  149  LEU D N   1 
ATOM   7182  C CA  . LEU D  1  149 ? 23.120  16.730  28.170  1.00 17.89  ?  149  LEU D CA  1 
ATOM   7183  C C   . LEU D  1  149 ? 22.533  15.655  27.263  1.00 17.58  ?  149  LEU D C   1 
ATOM   7184  O O   . LEU D  1  149 ? 22.912  14.484  27.364  1.00 17.67  ?  149  LEU D O   1 
ATOM   7185  C CB  . LEU D  1  149 ? 23.458  16.139  29.538  1.00 18.18  ?  149  LEU D CB  1 
ATOM   7186  C CG  . LEU D  1  149 ? 24.381  16.947  30.452  1.00 18.62  ?  149  LEU D CG  1 
ATOM   7187  C CD1 . LEU D  1  149 ? 24.763  16.127  31.674  1.00 18.94  ?  149  LEU D CD1 1 
ATOM   7188  C CD2 . LEU D  1  149 ? 25.620  17.398  29.698  1.00 18.83  ?  149  LEU D CD2 1 
ATOM   7189  N N   . SER D  1  150 ? 21.609  16.033  26.383  1.00 20.84  ?  150  SER D N   1 
ATOM   7190  C CA  . SER D  1  150 ? 20.859  15.068  25.598  1.00 20.56  ?  150  SER D CA  1 
ATOM   7191  C C   . SER D  1  150 ? 21.748  14.370  24.573  1.00 20.61  ?  150  SER D C   1 
ATOM   7192  O O   . SER D  1  150 ? 22.851  14.818  24.256  1.00 20.84  ?  150  SER D O   1 
ATOM   7193  C CB  . SER D  1  150 ? 19.696  15.753  24.883  1.00 20.32  ?  150  SER D CB  1 
ATOM   7194  O OG  . SER D  1  150 ? 19.017  16.644  25.748  1.00 20.44  ?  150  SER D OG  1 
ATOM   7195  N N   . ILE D  1  151 ? 21.244  13.244  24.064  1.00 20.58  ?  151  ILE D N   1 
ATOM   7196  C CA  . ILE D  1  151 ? 21.859  12.503  22.966  1.00 20.65  ?  151  ILE D CA  1 
ATOM   7197  C C   . ILE D  1  151 ? 23.318  12.205  23.290  1.00 21.11  ?  151  ILE D C   1 
ATOM   7198  O O   . ILE D  1  151 ? 24.237  12.816  22.733  1.00 22.80  ?  151  ILE D O   1 
ATOM   7199  C CB  . ILE D  1  151 ? 21.710  13.267  21.638  1.00 20.48  ?  151  ILE D CB  1 
ATOM   7200  C CG1 . ILE D  1  151 ? 20.255  13.708  21.462  1.00 20.13  ?  151  ILE D CG1 1 
ATOM   7201  C CG2 . ILE D  1  151 ? 22.121  12.387  20.468  1.00 20.59  ?  151  ILE D CG2 1 
ATOM   7202  C CD1 . ILE D  1  151 ? 20.016  14.601  20.271  1.00 20.00  ?  151  ILE D CD1 1 
ATOM   7203  N N   . ASN D  1  152 ? 23.525  11.270  24.210  1.00 22.06  ?  152  ASN D N   1 
ATOM   7204  C CA  . ASN D  1  152 ? 24.841  10.841  24.661  1.00 22.62  ?  152  ASN D CA  1 
ATOM   7205  C C   . ASN D  1  152 ? 24.723  9.371   25.047  1.00 22.77  ?  152  ASN D C   1 
ATOM   7206  O O   . ASN D  1  152 ? 23.752  8.697   24.690  1.00 22.63  ?  152  ASN D O   1 
ATOM   7207  C CB  . ASN D  1  152 ? 25.340  11.722  25.815  1.00 22.82  ?  152  ASN D CB  1 
ATOM   7208  C CG  . ASN D  1  152 ? 26.053  12.974  25.333  1.00 23.17  ?  152  ASN D CG  1 
ATOM   7209  O OD1 . ASN D  1  152 ? 27.044  12.899  24.608  1.00 23.38  ?  152  ASN D OD1 1 
ATOM   7210  N ND2 . ASN D  1  152 ? 25.548  14.134  25.737  1.00 22.84  ?  152  ASN D ND2 1 
ATOM   7211  N N   . GLN D  1  153 ? 25.721  8.861   25.759  1.00 23.50  ?  153  GLN D N   1 
ATOM   7212  C CA  . GLN D  1  153 ? 25.678  7.508   26.298  1.00 23.73  ?  153  GLN D CA  1 
ATOM   7213  C C   . GLN D  1  153 ? 25.851  7.522   27.813  1.00 23.96  ?  153  GLN D C   1 
ATOM   7214  O O   . GLN D  1  153 ? 26.582  6.712   28.385  1.00 24.73  ?  153  GLN D O   1 
ATOM   7215  C CB  . GLN D  1  153 ? 26.723  6.618   25.629  1.00 24.35  ?  153  GLN D CB  1 
ATOM   7216  C CG  . GLN D  1  153 ? 26.626  6.603   24.109  1.00 24.22  ?  153  GLN D CG  1 
ATOM   7217  C CD  . GLN D  1  153 ? 27.844  7.201   23.438  1.00 25.18  ?  153  GLN D CD  1 
ATOM   7218  O OE1 . GLN D  1  153 ? 28.923  7.262   24.026  1.00 26.51  ?  153  GLN D OE1 1 
ATOM   7219  N NE2 . GLN D  1  153 ? 27.675  7.658   22.202  1.00 25.37  ?  153  GLN D NE2 1 
ATOM   7220  N N   . LEU D  1  154 ? 25.170  8.454   28.477  1.00 21.10  ?  154  LEU D N   1 
ATOM   7221  C CA  . LEU D  1  154 ? 25.181  8.516   29.931  1.00 21.30  ?  154  LEU D CA  1 
ATOM   7222  C C   . LEU D  1  154 ? 24.281  7.441   30.528  1.00 21.17  ?  154  LEU D C   1 
ATOM   7223  O O   . LEU D  1  154 ? 23.249  7.072   29.959  1.00 20.75  ?  154  LEU D O   1 
ATOM   7224  C CB  . LEU D  1  154 ? 24.730  9.894   30.421  1.00 21.04  ?  154  LEU D CB  1 
ATOM   7225  C CG  . LEU D  1  154 ? 25.428  11.117  29.828  1.00 21.10  ?  154  LEU D CG  1 
ATOM   7226  C CD1 . LEU D  1  154 ? 24.933  12.384  30.505  1.00 20.94  ?  154  LEU D CD1 1 
ATOM   7227  C CD2 . LEU D  1  154 ? 26.934  10.985  29.970  1.00 21.77  ?  154  LEU D CD2 1 
ATOM   7228  N N   . VAL D  1  155 ? 24.688  6.941   31.692  1.00 22.75  ?  155  VAL D N   1 
ATOM   7229  C CA  . VAL D  1  155 ? 23.981  5.898   32.415  1.00 22.74  ?  155  VAL D CA  1 
ATOM   7230  C C   . VAL D  1  155 ? 23.868  6.317   33.878  1.00 22.93  ?  155  VAL D C   1 
ATOM   7231  O O   . VAL D  1  155 ? 24.397  7.348   34.291  1.00 23.08  ?  155  VAL D O   1 
ATOM   7232  C CB  . VAL D  1  155 ? 24.674  4.526   32.285  1.00 20.40  ?  155  VAL D CB  1 
ATOM   7233  C CG1 . VAL D  1  155 ? 24.404  3.925   30.915  1.00 20.17  ?  155  VAL D CG1 1 
ATOM   7234  C CG2 . VAL D  1  155 ? 26.168  4.663   32.528  1.00 21.12  ?  155  VAL D CG2 1 
ATOM   7235  N N   . GLY D  1  156 ? 23.159  5.510   34.656  1.00 23.20  ?  156  GLY D N   1 
ATOM   7236  C CA  . GLY D  1  156 ? 22.981  5.806   36.061  1.00 23.42  ?  156  GLY D CA  1 
ATOM   7237  C C   . GLY D  1  156 ? 21.691  6.549   36.333  1.00 23.02  ?  156  GLY D C   1 
ATOM   7238  O O   . GLY D  1  156 ? 20.789  6.645   35.497  1.00 24.06  ?  156  GLY D O   1 
ATOM   7239  N N   . GLU D  1  157 ? 21.609  7.086   37.543  1.00 28.42  ?  157  GLU D N   1 
ATOM   7240  C CA  . GLU D  1  157 ? 20.431  7.815   37.983  1.00 28.26  ?  157  GLU D CA  1 
ATOM   7241  C C   . GLU D  1  157 ? 20.645  9.317   37.840  1.00 28.22  ?  157  GLU D C   1 
ATOM   7242  O O   . GLU D  1  157 ? 21.737  9.795   37.523  1.00 28.38  ?  157  GLU D O   1 
ATOM   7243  C CB  . GLU D  1  157 ? 20.088  7.463   39.434  1.00 28.89  ?  157  GLU D CB  1 
ATOM   7244  C CG  . GLU D  1  157 ? 19.949  5.974   39.698  1.00 29.00  ?  157  GLU D CG  1 
ATOM   7245  C CD  . GLU D  1  157 ? 19.146  5.678   40.949  1.00 30.24  ?  157  GLU D CD  1 
ATOM   7246  O OE1 . GLU D  1  157 ? 18.510  6.612   41.484  1.00 30.66  ?  157  GLU D OE1 1 
ATOM   7247  O OE2 . GLU D  1  157 ? 19.151  4.513   41.398  1.00 30.42  -1 157  GLU D OE2 1 
ATOM   7248  N N   . ILE D  1  158 ? 19.571  10.061  38.074  1.00 22.43  ?  158  ILE D N   1 
ATOM   7249  C CA  . ILE D  1  158 ? 19.610  11.519  38.078  1.00 22.48  ?  158  ILE D CA  1 
ATOM   7250  C C   . ILE D  1  158 ? 19.857  11.969  39.515  1.00 23.01  ?  158  ILE D C   1 
ATOM   7251  O O   . ILE D  1  158 ? 19.060  11.625  40.401  1.00 23.28  ?  158  ILE D O   1 
ATOM   7252  C CB  . ILE D  1  158 ? 18.310  12.118  37.530  1.00 22.27  ?  158  ILE D CB  1 
ATOM   7253  C CG1 . ILE D  1  158 ? 18.197  11.863  36.026  1.00 21.77  ?  158  ILE D CG1 1 
ATOM   7254  C CG2 . ILE D  1  158 ? 18.242  13.608  37.825  1.00 22.51  ?  158  ILE D CG2 1 
ATOM   7255  C CD1 . ILE D  1  158 ? 16.791  12.015  35.486  1.00 21.61  ?  158  ILE D CD1 1 
ATOM   7256  N N   . PRO D  1  159 ? 20.943  12.681  39.795  1.00 23.79  ?  159  PRO D N   1 
ATOM   7257  C CA  . PRO D  1  159 ? 21.218  13.106  41.171  1.00 24.36  ?  159  PRO D CA  1 
ATOM   7258  C C   . PRO D  1  159 ? 20.135  14.038  41.680  1.00 24.60  ?  159  PRO D C   1 
ATOM   7259  O O   . PRO D  1  159 ? 19.603  14.860  40.918  1.00 24.38  ?  159  PRO D O   1 
ATOM   7260  C CB  . PRO D  1  159 ? 22.567  13.832  41.055  1.00 24.55  ?  159  PRO D CB  1 
ATOM   7261  C CG  . PRO D  1  159 ? 22.654  14.251  39.625  1.00 24.08  ?  159  PRO D CG  1 
ATOM   7262  C CD  . PRO D  1  159 ? 21.935  13.198  38.837  1.00 23.63  ?  159  PRO D CD  1 
ATOM   7263  N N   . PRO D  1  160 ? 19.770  13.936  42.960  1.00 26.27  ?  160  PRO D N   1 
ATOM   7264  C CA  . PRO D  1  160 ? 18.861  14.938  43.540  1.00 26.75  ?  160  PRO D CA  1 
ATOM   7265  C C   . PRO D  1  160 ? 19.457  16.330  43.555  1.00 26.99  ?  160  PRO D C   1 
ATOM   7266  O O   . PRO D  1  160 ? 18.708  17.313  43.624  1.00 27.31  ?  160  PRO D O   1 
ATOM   7267  C CB  . PRO D  1  160 ? 18.611  14.417  44.964  1.00 27.42  ?  160  PRO D CB  1 
ATOM   7268  C CG  . PRO D  1  160 ? 19.180  13.025  45.000  1.00 27.15  ?  160  PRO D CG  1 
ATOM   7269  C CD  . PRO D  1  160 ? 20.250  12.976  43.965  1.00 26.62  ?  160  PRO D CD  1 
ATOM   7270  N N   . GLU D  1  161 ? 20.787  16.438  43.484  1.00 29.83  ?  161  GLU D N   1 
ATOM   7271  C CA  . GLU D  1  161 ? 21.461  17.731  43.483  1.00 30.06  ?  161  GLU D CA  1 
ATOM   7272  C C   . GLU D  1  161 ? 21.034  18.614  42.320  1.00 29.70  ?  161  GLU D C   1 
ATOM   7273  O O   . GLU D  1  161 ? 21.215  19.834  42.386  1.00 30.27  ?  161  GLU D O   1 
ATOM   7274  C CB  . GLU D  1  161 ? 22.975  17.522  43.457  1.00 30.08  ?  161  GLU D CB  1 
ATOM   7275  C CG  . GLU D  1  161 ? 23.581  17.281  44.826  1.00 31.15  ?  161  GLU D CG  1 
ATOM   7276  C CD  . GLU D  1  161 ? 23.493  15.832  45.265  1.00 30.99  ?  161  GLU D CD  1 
ATOM   7277  O OE1 . GLU D  1  161 ? 22.862  15.026  44.549  1.00 30.49  ?  161  GLU D OE1 1 
ATOM   7278  O OE2 . GLU D  1  161 ? 24.060  15.497  46.327  1.00 31.64  -1 161  GLU D OE2 1 
ATOM   7279  N N   . LEU D  1  162 ? 20.485  18.028  41.252  1.00 24.12  ?  162  LEU D N   1 
ATOM   7280  C CA  . LEU D  1  162 ? 19.954  18.839  40.162  1.00 23.84  ?  162  LEU D CA  1 
ATOM   7281  C C   . LEU D  1  162 ? 18.861  19.779  40.653  1.00 24.36  ?  162  LEU D C   1 
ATOM   7282  O O   . LEU D  1  162 ? 18.646  20.843  40.064  1.00 24.41  ?  162  LEU D O   1 
ATOM   7283  C CB  . LEU D  1  162 ? 19.428  17.939  39.044  1.00 23.19  ?  162  LEU D CB  1 
ATOM   7284  C CG  . LEU D  1  162 ? 20.501  17.216  38.227  1.00 22.75  ?  162  LEU D CG  1 
ATOM   7285  C CD1 . LEU D  1  162 ? 19.933  16.707  36.910  1.00 22.18  ?  162  LEU D CD1 1 
ATOM   7286  C CD2 . LEU D  1  162 ? 21.695  18.126  37.983  1.00 22.88  ?  162  LEU D CD2 1 
ATOM   7287  N N   . GLY D  1  163 ? 18.171  19.408  41.734  1.00 26.54  ?  163  GLY D N   1 
ATOM   7288  C CA  . GLY D  1  163 ? 17.202  20.297  42.351  1.00 27.27  ?  163  GLY D CA  1 
ATOM   7289  C C   . GLY D  1  163 ? 17.803  21.572  42.905  1.00 27.91  ?  163  GLY D C   1 
ATOM   7290  O O   . GLY D  1  163 ? 17.066  22.529  43.170  1.00 28.56  ?  163  GLY D O   1 
ATOM   7291  N N   . LYS D  1  164 ? 19.122  21.611  43.089  1.00 28.54  ?  164  LYS D N   1 
ATOM   7292  C CA  . LYS D  1  164 ? 19.796  22.798  43.600  1.00 29.19  ?  164  LYS D CA  1 
ATOM   7293  C C   . LYS D  1  164 ? 20.036  23.849  42.526  1.00 28.96  ?  164  LYS D C   1 
ATOM   7294  O O   . LYS D  1  164 ? 20.667  24.872  42.813  1.00 29.48  ?  164  LYS D O   1 
ATOM   7295  C CB  . LYS D  1  164 ? 21.133  22.404  44.238  1.00 29.28  ?  164  LYS D CB  1 
ATOM   7296  C CG  . LYS D  1  164 ? 21.007  21.740  45.597  1.00 29.88  ?  164  LYS D CG  1 
ATOM   7297  C CD  . LYS D  1  164 ? 22.294  21.868  46.396  1.00 30.36  ?  164  LYS D CD  1 
ATOM   7298  C CE  . LYS D  1  164 ? 23.403  21.024  45.787  1.00 29.66  ?  164  LYS D CE  1 
ATOM   7299  N NZ  . LYS D  1  164 ? 24.701  21.225  46.489  1.00 31.57  ?  164  LYS D NZ  1 
ATOM   7300  N N   . LEU D  1  165 ? 19.546  23.627  41.307  1.00 25.83  ?  165  LEU D N   1 
ATOM   7301  C CA  . LEU D  1  165 ? 19.692  24.589  40.214  1.00 25.63  ?  165  LEU D CA  1 
ATOM   7302  C C   . LEU D  1  165 ? 18.486  25.529  40.213  1.00 26.18  ?  165  LEU D C   1 
ATOM   7303  O O   . LEU D  1  165 ? 17.623  25.497  39.333  1.00 25.86  ?  165  LEU D O   1 
ATOM   7304  C CB  . LEU D  1  165 ? 19.848  23.863  38.885  1.00 24.71  ?  165  LEU D CB  1 
ATOM   7305  C CG  . LEU D  1  165 ? 21.037  22.905  38.791  1.00 24.28  ?  165  LEU D CG  1 
ATOM   7306  C CD1 . LEU D  1  165 ? 20.983  22.101  37.502  1.00 23.51  ?  165  LEU D CD1 1 
ATOM   7307  C CD2 . LEU D  1  165 ? 22.349  23.664  38.902  1.00 24.57  ?  165  LEU D CD2 1 
ATOM   7308  N N   . SER D  1  166 ? 18.440  26.369  41.252  1.00 24.94  ?  166  SER D N   1 
ATOM   7309  C CA  . SER D  1  166 ? 17.294  27.248  41.475  1.00 25.71  ?  166  SER D CA  1 
ATOM   7310  C C   . SER D  1  166 ? 16.968  28.093  40.250  1.00 25.52  ?  166  SER D C   1 
ATOM   7311  O O   . SER D  1  166 ? 15.793  28.305  39.926  1.00 25.72  ?  166  SER D O   1 
ATOM   7312  C CB  . SER D  1  166 ? 17.559  28.150  42.682  1.00 26.85  ?  166  SER D CB  1 
ATOM   7313  O OG  . SER D  1  166 ? 18.639  29.033  42.431  1.00 26.97  ?  166  SER D OG  1 
ATOM   7314  N N   . ASN D  1  167 ? 17.990  28.575  39.551  1.00 24.09  ?  167  ASN D N   1 
ATOM   7315  C CA  . ASN D  1  167 ? 17.801  29.491  38.434  1.00 24.03  ?  167  ASN D CA  1 
ATOM   7316  C C   . ASN D  1  167 ? 17.605  28.776  37.104  1.00 23.04  ?  167  ASN D C   1 
ATOM   7317  O O   . ASN D  1  167 ? 17.501  29.443  36.069  1.00 22.93  ?  167  ASN D O   1 
ATOM   7318  C CB  . ASN D  1  167 ? 18.993  30.448  38.335  1.00 24.32  ?  167  ASN D CB  1 
ATOM   7319  C CG  . ASN D  1  167 ? 18.880  31.618  39.290  1.00 25.52  ?  167  ASN D CG  1 
ATOM   7320  O OD1 . ASN D  1  167 ? 17.925  32.392  39.230  1.00 26.14  ?  167  ASN D OD1 1 
ATOM   7321  N ND2 . ASN D  1  167 ? 19.855  31.750  40.182  1.00 25.95  ?  167  ASN D ND2 1 
ATOM   7322  N N   . LEU D  1  168 ? 17.553  27.446  37.103  1.00 23.86  ?  168  LEU D N   1 
ATOM   7323  C CA  . LEU D  1  168 ? 17.443  26.700  35.857  1.00 22.99  ?  168  LEU D CA  1 
ATOM   7324  C C   . LEU D  1  168 ? 16.080  26.921  35.213  1.00 23.06  ?  168  LEU D C   1 
ATOM   7325  O O   . LEU D  1  168 ? 15.042  26.836  35.877  1.00 23.53  ?  168  LEU D O   1 
ATOM   7326  C CB  . LEU D  1  168 ? 17.670  25.211  36.111  1.00 22.44  ?  168  LEU D CB  1 
ATOM   7327  C CG  . LEU D  1  168 ? 18.053  24.368  34.895  1.00 21.59  ?  168  LEU D CG  1 
ATOM   7328  C CD1 . LEU D  1  168 ? 19.534  24.514  34.589  1.00 21.40  ?  168  LEU D CD1 1 
ATOM   7329  C CD2 . LEU D  1  168 ? 17.693  22.911  35.131  1.00 21.23  ?  168  LEU D CD2 1 
ATOM   7330  N N   . ASP D  1  169 ? 16.092  27.206  33.913  1.00 23.80  ?  169  ASP D N   1 
ATOM   7331  C CA  . ASP D  1  169 ? 14.884  27.388  33.119  1.00 23.82  ?  169  ASP D CA  1 
ATOM   7332  C C   . ASP D  1  169 ? 14.567  26.182  32.248  1.00 23.03  ?  169  ASP D C   1 
ATOM   7333  O O   . ASP D  1  169 ? 13.395  25.825  32.091  1.00 23.10  ?  169  ASP D O   1 
ATOM   7334  C CB  . ASP D  1  169 ? 15.017  28.639  32.240  1.00 24.05  ?  169  ASP D CB  1 
ATOM   7335  C CG  . ASP D  1  169 ? 14.049  28.639  31.068  1.00 23.85  ?  169  ASP D CG  1 
ATOM   7336  O OD1 . ASP D  1  169 ? 12.832  28.470  31.295  1.00 24.17  ?  169  ASP D OD1 1 
ATOM   7337  O OD2 . ASP D  1  169 ? 14.507  28.801  29.915  1.00 23.42  -1 169  ASP D OD2 1 
ATOM   7338  N N   . THR D  1  170 ? 15.588  25.548  31.673  1.00 20.26  ?  170  THR D N   1 
ATOM   7339  C CA  . THR D  1  170 ? 15.414  24.427  30.762  1.00 19.57  ?  170  THR D CA  1 
ATOM   7340  C C   . THR D  1  170 ? 16.328  23.278  31.169  1.00 19.18  ?  170  THR D C   1 
ATOM   7341  O O   . THR D  1  170 ? 17.501  23.490  31.492  1.00 19.22  ?  170  THR D O   1 
ATOM   7342  C CB  . THR D  1  170 ? 15.709  24.854  29.317  1.00 19.24  ?  170  THR D CB  1 
ATOM   7343  O OG1 . THR D  1  170 ? 14.809  25.903  28.936  1.00 19.67  ?  170  THR D OG1 1 
ATOM   7344  C CG2 . THR D  1  170 ? 15.547  23.687  28.363  1.00 18.60  ?  170  THR D CG2 1 
ATOM   7345  N N   . LEU D  1  171 ? 15.786  22.060  31.141  1.00 18.05  ?  171  LEU D N   1 
ATOM   7346  C CA  . LEU D  1  171 ? 16.519  20.852  31.505  1.00 17.75  ?  171  LEU D CA  1 
ATOM   7347  C C   . LEU D  1  171 ? 16.314  19.812  30.415  1.00 17.21  ?  171  LEU D C   1 
ATOM   7348  O O   . LEU D  1  171 ? 15.181  19.382  30.173  1.00 17.16  ?  171  LEU D O   1 
ATOM   7349  C CB  . LEU D  1  171 ? 16.056  20.310  32.860  1.00 18.08  ?  171  LEU D CB  1 
ATOM   7350  C CG  . LEU D  1  171 ? 16.622  18.950  33.277  1.00 17.84  ?  171  LEU D CG  1 
ATOM   7351  C CD1 . LEU D  1  171 ? 18.141  18.996  33.319  1.00 17.77  ?  171  LEU D CD1 1 
ATOM   7352  C CD2 . LEU D  1  171 ? 16.056  18.522  34.621  1.00 18.25  ?  171  LEU D CD2 1 
ATOM   7353  N N   . HIS D  1  172 ? 17.403  19.411  29.760  1.00 19.88  ?  172  HIS D N   1 
ATOM   7354  C CA  . HIS D  1  172 ? 17.359  18.444  28.666  1.00 19.44  ?  172  HIS D CA  1 
ATOM   7355  C C   . HIS D  1  172 ? 18.337  17.317  28.971  1.00 19.35  ?  172  HIS D C   1 
ATOM   7356  O O   . HIS D  1  172 ? 19.555  17.523  28.949  1.00 19.43  ?  172  HIS D O   1 
ATOM   7357  C CB  . HIS D  1  172 ? 17.697  19.109  27.330  1.00 19.26  ?  172  HIS D CB  1 
ATOM   7358  C CG  . HIS D  1  172 ? 16.637  20.038  26.824  1.00 19.35  ?  172  HIS D CG  1 
ATOM   7359  N ND1 . HIS D  1  172 ? 16.827  20.855  25.729  1.00 19.29  ?  172  HIS D ND1 1 
ATOM   7360  C CD2 . HIS D  1  172 ? 15.376  20.275  27.255  1.00 19.59  ?  172  HIS D CD2 1 
ATOM   7361  C CE1 . HIS D  1  172 ? 15.730  21.558  25.512  1.00 19.47  ?  172  HIS D CE1 1 
ATOM   7362  N NE2 . HIS D  1  172 ? 14.833  21.223  26.422  1.00 19.68  ?  172  HIS D NE2 1 
ATOM   7363  N N   . LEU D  1  173 ? 17.804  16.129  29.249  1.00 20.49  ?  173  LEU D N   1 
ATOM   7364  C CA  . LEU D  1  173 ? 18.578  14.924  29.545  1.00 20.47  ?  173  LEU D CA  1 
ATOM   7365  C C   . LEU D  1  173 ? 18.130  13.790  28.635  1.00 20.19  ?  173  LEU D C   1 
ATOM   7366  O O   . LEU D  1  173 ? 17.910  12.654  29.061  1.00 20.20  ?  173  LEU D O   1 
ATOM   7367  C CB  . LEU D  1  173 ? 18.442  14.531  31.011  1.00 20.76  ?  173  LEU D CB  1 
ATOM   7368  C CG  . LEU D  1  173 ? 19.141  15.459  32.005  1.00 13.42  ?  173  LEU D CG  1 
ATOM   7369  C CD1 . LEU D  1  173 ? 18.804  15.063  33.433  1.00 13.74  ?  173  LEU D CD1 1 
ATOM   7370  C CD2 . LEU D  1  173 ? 20.644  15.463  31.779  1.00 13.50  ?  173  LEU D CD2 1 
ATOM   7371  N N   . VAL D  1  174 ? 18.000  14.099  27.362  1.00 20.41  ?  174  VAL D N   1 
ATOM   7372  C CA  . VAL D  1  174 ? 17.194  13.324  26.429  1.00 20.16  ?  174  VAL D CA  1 
ATOM   7373  C C   . VAL D  1  174 ? 18.033  12.297  25.684  1.00 20.08  ?  174  VAL D C   1 
ATOM   7374  O O   . VAL D  1  174 ? 19.215  12.506  25.396  1.00 20.32  ?  174  VAL D O   1 
ATOM   7375  C CB  . VAL D  1  174 ? 16.485  14.266  25.441  1.00 20.02  ?  174  VAL D CB  1 
ATOM   7376  C CG1 . VAL D  1  174 ? 15.456  13.506  24.702  1.00 19.83  ?  174  VAL D CG1 1 
ATOM   7377  C CG2 . VAL D  1  174 ? 15.859  15.437  26.178  1.00 20.48  ?  174  VAL D CG2 1 
ATOM   7378  N N   . GLU D  1  175 ? 17.397  11.168  25.364  1.00 21.37  ?  175  GLU D N   1 
ATOM   7379  C CA  . GLU D  1  175 ? 17.987  10.134  24.516  1.00 21.36  ?  175  GLU D CA  1 
ATOM   7380  C C   . GLU D  1  175 ? 19.283  9.610   25.130  1.00 21.86  ?  175  GLU D C   1 
ATOM   7381  O O   . GLU D  1  175 ? 20.338  9.564   24.493  1.00 22.05  ?  175  GLU D O   1 
ATOM   7382  C CB  . GLU D  1  175 ? 18.194  10.647  23.088  1.00 21.40  ?  175  GLU D CB  1 
ATOM   7383  C CG  . GLU D  1  175 ? 16.888  10.753  22.305  1.00 21.32  ?  175  GLU D CG  1 
ATOM   7384  C CD  . GLU D  1  175 ? 17.099  11.009  20.826  1.00 21.54  ?  175  GLU D CD  1 
ATOM   7385  O OE1 . GLU D  1  175 ? 18.201  10.712  20.318  1.00 21.71  ?  175  GLU D OE1 1 
ATOM   7386  O OE2 . GLU D  1  175 ? 16.158  11.504  20.170  1.00 21.40  -1 175  GLU D OE2 1 
ATOM   7387  N N   . ASN D  1  176 ? 19.185  9.236   26.403  1.00 19.65  ?  176  ASN D N   1 
ATOM   7388  C CA  . ASN D  1  176 ? 20.262  8.598   27.143  1.00 20.00  ?  176  ASN D CA  1 
ATOM   7389  C C   . ASN D  1  176 ? 19.715  7.311   27.740  1.00 20.06  ?  176  ASN D C   1 
ATOM   7390  O O   . ASN D  1  176 ? 18.583  6.919   27.439  1.00 19.82  ?  176  ASN D O   1 
ATOM   7391  C CB  . ASN D  1  176 ? 20.804  9.526   28.232  1.00 20.21  ?  176  ASN D CB  1 
ATOM   7392  C CG  . ASN D  1  176 ? 21.776  10.558  27.691  1.00 20.31  ?  176  ASN D CG  1 
ATOM   7393  O OD1 . ASN D  1  176 ? 22.923  10.241  27.379  1.00 20.62  ?  176  ASN D OD1 1 
ATOM   7394  N ND2 . ASN D  1  176 ? 21.318  11.801  27.572  1.00 20.13  ?  176  ASN D ND2 1 
ATOM   7395  N N   . LYS D  1  177 ? 20.493  6.649   28.584  1.00 20.70  ?  177  LYS D N   1 
ATOM   7396  C CA  . LYS D  1  177 ? 20.072  5.407   29.215  1.00 20.82  ?  177  LYS D CA  1 
ATOM   7397  C C   . LYS D  1  177 ? 20.025  5.563   30.729  1.00 21.03  ?  177  LYS D C   1 
ATOM   7398  O O   . LYS D  1  177 ? 20.424  4.672   31.483  1.00 21.36  ?  177  LYS D O   1 
ATOM   7399  C CB  . LYS D  1  177 ? 20.981  4.252   28.804  1.00 21.16  ?  177  LYS D CB  1 
ATOM   7400  C CG  . LYS D  1  177 ? 20.742  3.740   27.385  1.00 20.99  ?  177  LYS D CG  1 
ATOM   7401  C CD  . LYS D  1  177 ? 19.266  3.794   26.998  1.00 20.53  ?  177  LYS D CD  1 
ATOM   7402  C CE  . LYS D  1  177 ? 19.078  3.857   25.486  1.00 20.93  ?  177  LYS D CE  1 
ATOM   7403  N NZ  . LYS D  1  177 ? 18.795  5.238   25.002  1.00 20.03  ?  177  LYS D NZ  1 
ATOM   7404  N N   . LEU D  1  178 ? 19.521  6.710   31.184  1.00 20.52  ?  178  LEU D N   1 
ATOM   7405  C CA  . LEU D  1  178 ? 19.417  6.975   32.612  1.00 20.76  ?  178  LEU D CA  1 
ATOM   7406  C C   . LEU D  1  178 ? 18.299  6.132   33.211  1.00 20.77  ?  178  LEU D C   1 
ATOM   7407  O O   . LEU D  1  178 ? 17.168  6.144   32.717  1.00 20.52  ?  178  LEU D O   1 
ATOM   7408  C CB  . LEU D  1  178 ? 19.142  8.460   32.861  1.00 20.70  ?  178  LEU D CB  1 
ATOM   7409  C CG  . LEU D  1  178 ? 20.038  9.478   32.154  1.00 20.66  ?  178  LEU D CG  1 
ATOM   7410  C CD1 . LEU D  1  178 ? 19.601  10.893  32.496  1.00 20.65  ?  178  LEU D CD1 1 
ATOM   7411  C CD2 . LEU D  1  178 ? 21.499  9.260   32.506  1.00 21.04  ?  178  LEU D CD2 1 
ATOM   7412  N N   . ASN D  1  179 ? 18.616  5.385   34.265  1.00 26.07  ?  179  ASN D N   1 
ATOM   7413  C CA  . ASN D  1  179 ? 17.623  4.575   34.950  1.00 26.09  ?  179  ASN D CA  1 
ATOM   7414  C C   . ASN D  1  179 ? 17.460  5.054   36.387  1.00 26.41  ?  179  ASN D C   1 
ATOM   7415  O O   . ASN D  1  179 ? 18.288  5.795   36.922  1.00 26.62  ?  179  ASN D O   1 
ATOM   7416  C CB  . ASN D  1  179 ? 17.991  3.082   34.927  1.00 26.27  ?  179  ASN D CB  1 
ATOM   7417  C CG  . ASN D  1  179 ? 19.299  2.792   35.622  1.00 26.85  ?  179  ASN D CG  1 
ATOM   7418  O OD1 . ASN D  1  179 ? 20.097  3.695   35.872  1.00 26.83  ?  179  ASN D OD1 1 
ATOM   7419  N ND2 . ASN D  1  179 ? 19.527  1.521   35.935  1.00 26.99  ?  179  ASN D ND2 1 
ATOM   7420  N N   . GLY D  1  180 ? 16.375  4.617   37.004  1.00 24.69  ?  180  GLY D N   1 
ATOM   7421  C CA  . GLY D  1  180 ? 16.043  4.985   38.364  1.00 25.10  ?  180  GLY D CA  1 
ATOM   7422  C C   . GLY D  1  180 ? 14.773  5.813   38.402  1.00 25.18  ?  180  GLY D C   1 
ATOM   7423  O O   . GLY D  1  180 ? 14.102  6.027   37.391  1.00 25.11  ?  180  GLY D O   1 
ATOM   7424  N N   . SER D  1  181 ? 14.448  6.276   39.604  1.00 25.81  ?  181  SER D N   1 
ATOM   7425  C CA  . SER D  1  181 ? 13.287  7.135   39.788  1.00 26.16  ?  181  SER D CA  1 
ATOM   7426  C C   . SER D  1  181 ? 13.689  8.597   39.659  1.00 26.16  ?  181  SER D C   1 
ATOM   7427  O O   . SER D  1  181 ? 14.834  8.971   39.928  1.00 26.58  ?  181  SER D O   1 
ATOM   7428  C CB  . SER D  1  181 ? 12.644  6.889   41.154  1.00 26.77  ?  181  SER D CB  1 
ATOM   7429  O OG  . SER D  1  181 ? 11.868  5.706   41.146  1.00 27.33  ?  181  SER D OG  1 
ATOM   7430  N N   . ILE D  1  182 ? 12.738  9.421   39.243  1.00 24.25  ?  182  ILE D N   1 
ATOM   7431  C CA  . ILE D  1  182 ? 13.001  10.860  39.171  1.00 24.33  ?  182  ILE D CA  1 
ATOM   7432  C C   . ILE D  1  182 ? 13.034  11.422  40.587  1.00 25.03  ?  182  ILE D C   1 
ATOM   7433  O O   . ILE D  1  182 ? 12.076  11.217  41.354  1.00 25.61  ?  182  ILE D O   1 
ATOM   7434  C CB  . ILE D  1  182 ? 11.939  11.560  38.318  1.00 24.29  ?  182  ILE D CB  1 
ATOM   7435  C CG1 . ILE D  1  182 ? 11.804  10.870  36.962  1.00 23.68  ?  182  ILE D CG1 1 
ATOM   7436  C CG2 . ILE D  1  182 ? 12.291  13.026  38.139  1.00 24.36  ?  182  ILE D CG2 1 
ATOM   7437  C CD1 . ILE D  1  182 ? 10.766  11.484  36.061  1.00 23.64  ?  182  ILE D CD1 1 
ATOM   7438  N N   . PRO D  1  183 ? 14.110  12.098  40.986  1.00 24.99  ?  183  PRO D N   1 
ATOM   7439  C CA  . PRO D  1  183 ? 14.196  12.598  42.362  1.00 25.72  ?  183  PRO D CA  1 
ATOM   7440  C C   . PRO D  1  183 ? 13.079  13.579  42.683  1.00 26.35  ?  183  PRO D C   1 
ATOM   7441  O O   . PRO D  1  183 ? 12.681  14.392  41.848  1.00 26.18  ?  183  PRO D O   1 
ATOM   7442  C CB  . PRO D  1  183 ? 15.568  13.280  42.411  1.00 25.60  ?  183  PRO D CB  1 
ATOM   7443  C CG  . PRO D  1  183 ? 16.327  12.724  41.263  1.00 24.86  ?  183  PRO D CG  1 
ATOM   7444  C CD  . PRO D  1  183 ? 15.318  12.404  40.206  1.00 24.48  ?  183  PRO D CD  1 
ATOM   7445  N N   . SER D  1  184 ? 12.566  13.482  43.914  1.00 28.58  ?  184  SER D N   1 
ATOM   7446  C CA  . SER D  1  184 ? 11.573  14.441  44.385  1.00 29.41  ?  184  SER D CA  1 
ATOM   7447  C C   . SER D  1  184 ? 12.113  15.865  44.360  1.00 29.59  ?  184  SER D C   1 
ATOM   7448  O O   . SER D  1  184 ? 11.340  16.822  44.232  1.00 30.05  ?  184  SER D O   1 
ATOM   7449  C CB  . SER D  1  184 ? 11.121  14.071  45.798  1.00 30.42  ?  184  SER D CB  1 
ATOM   7450  O OG  . SER D  1  184 ? 10.725  12.712  45.867  1.00 31.39  ?  184  SER D OG  1 
ATOM   7451  N N   . GLU D  1  185 ? 13.434  16.024  44.476  1.00 31.48  ?  185  GLU D N   1 
ATOM   7452  C CA  . GLU D  1  185 ? 14.052  17.342  44.538  1.00 31.70  ?  185  GLU D CA  1 
ATOM   7453  C C   . GLU D  1  185 ? 13.972  18.104  43.222  1.00 31.16  ?  185  GLU D C   1 
ATOM   7454  O O   . GLU D  1  185 ? 14.271  19.302  43.209  1.00 31.44  ?  185  GLU D O   1 
ATOM   7455  C CB  . GLU D  1  185 ? 15.513  17.209  44.969  1.00 31.54  ?  185  GLU D CB  1 
ATOM   7456  C CG  . GLU D  1  185 ? 15.698  16.811  46.425  1.00 32.40  ?  185  GLU D CG  1 
ATOM   7457  C CD  . GLU D  1  185 ? 15.458  15.331  46.668  1.00 32.26  ?  185  GLU D CD  1 
ATOM   7458  O OE1 . GLU D  1  185 ? 15.463  14.555  45.689  1.00 31.68  ?  185  GLU D OE1 1 
ATOM   7459  O OE2 . GLU D  1  185 ? 15.265  14.945  47.839  1.00 33.09  -1 185  GLU D OE2 1 
ATOM   7460  N N   . ILE D  1  186 ? 13.586  17.449  42.122  1.00 27.49  ?  186  ILE D N   1 
ATOM   7461  C CA  . ILE D  1  186 ? 13.359  18.172  40.873  1.00 27.09  ?  186  ILE D CA  1 
ATOM   7462  C C   . ILE D  1  186 ? 12.245  19.193  41.050  1.00 27.83  ?  186  ILE D C   1 
ATOM   7463  O O   . ILE D  1  186 ? 12.236  20.240  40.390  1.00 27.82  ?  186  ILE D O   1 
ATOM   7464  C CB  . ILE D  1  186 ? 13.056  17.184  39.728  1.00 26.32  ?  186  ILE D CB  1 
ATOM   7465  C CG1 . ILE D  1  186 ? 14.170  16.141  39.615  1.00 25.75  ?  186  ILE D CG1 1 
ATOM   7466  C CG2 . ILE D  1  186 ? 12.901  17.919  38.403  1.00 25.93  ?  186  ILE D CG2 1 
ATOM   7467  C CD1 . ILE D  1  186 ? 15.533  16.730  39.321  1.00 25.49  ?  186  ILE D CD1 1 
ATOM   7468  N N   . GLY D  1  187 ? 11.301  18.920  41.953  1.00 27.92  ?  187  GLY D N   1 
ATOM   7469  C CA  . GLY D  1  187 ? 10.245  19.862  42.282  1.00 28.85  ?  187  GLY D CA  1 
ATOM   7470  C C   . GLY D  1  187 ? 10.732  21.177  42.862  1.00 29.50  ?  187  GLY D C   1 
ATOM   7471  O O   . GLY D  1  187 ? 9.930   22.107  43.000  1.00 30.30  ?  187  GLY D O   1 
ATOM   7472  N N   . ARG D  1  188 ? 12.013  21.271  43.224  1.00 31.78  ?  188  ARG D N   1 
ATOM   7473  C CA  . ARG D  1  188 ? 12.580  22.520  43.713  1.00 32.39  ?  188  ARG D CA  1 
ATOM   7474  C C   . ARG D  1  188 ? 12.916  23.497  42.595  1.00 31.98  ?  188  ARG D C   1 
ATOM   7475  O O   . ARG D  1  188 ? 13.274  24.644  42.885  1.00 32.80  ?  188  ARG D O   1 
ATOM   7476  C CB  . ARG D  1  188 ? 13.840  22.235  44.532  1.00 32.39  ?  188  ARG D CB  1 
ATOM   7477  C CG  . ARG D  1  188 ? 13.584  21.424  45.785  1.00 33.00  ?  188  ARG D CG  1 
ATOM   7478  C CD  . ARG D  1  188 ? 14.752  21.510  46.750  1.00 33.36  ?  188  ARG D CD  1 
ATOM   7479  N NE  . ARG D  1  188 ? 14.571  20.624  47.892  1.00 34.21  ?  188  ARG D NE  1 
ATOM   7480  C CZ  . ARG D  1  188 ? 15.128  20.810  49.081  1.00 34.89  ?  188  ARG D CZ  1 
ATOM   7481  N NH1 . ARG D  1  188 ? 15.916  21.846  49.320  1.00 35.69  ?  188  ARG D NH1 1 
ATOM   7482  N NH2 . ARG D  1  188 ? 14.890  19.935  50.053  1.00 35.39  ?  188  ARG D NH2 1 
ATOM   7483  N N   . LEU D  1  189 ? 12.805  23.079  41.332  1.00 28.77  ?  189  LEU D N   1 
ATOM   7484  C CA  . LEU D  1  189 ? 13.157  23.928  40.194  1.00 28.29  ?  189  LEU D CA  1 
ATOM   7485  C C   . LEU D  1  189 ? 11.996  24.883  39.909  1.00 29.05  ?  189  LEU D C   1 
ATOM   7486  O O   . LEU D  1  189 ? 11.263  24.761  38.925  1.00 28.99  ?  189  LEU D O   1 
ATOM   7487  C CB  . LEU D  1  189 ? 13.496  23.076  38.979  1.00 27.20  ?  189  LEU D CB  1 
ATOM   7488  C CG  . LEU D  1  189 ? 14.635  22.064  39.128  1.00 26.59  ?  189  LEU D CG  1 
ATOM   7489  C CD1 . LEU D  1  189 ? 14.919  21.381  37.798  1.00 25.66  ?  189  LEU D CD1 1 
ATOM   7490  C CD2 . LEU D  1  189 ? 15.889  22.727  39.676  1.00 26.82  ?  189  LEU D CD2 1 
ATOM   7491  N N   . THR D  1  190 ? 11.852  25.864  40.804  1.00 27.27  ?  190  THR D N   1 
ATOM   7492  C CA  . THR D  1  190 ? 10.710  26.773  40.755  1.00 28.13  ?  190  THR D CA  1 
ATOM   7493  C C   . THR D  1  190 ? 10.640  27.534  39.435  1.00 27.78  ?  190  THR D C   1 
ATOM   7494  O O   . THR D  1  190 ? 9.542   27.804  38.932  1.00 28.10  ?  190  THR D O   1 
ATOM   7495  C CB  . THR D  1  190 ? 10.780  27.743  41.939  1.00 29.36  ?  190  THR D CB  1 
ATOM   7496  O OG1 . THR D  1  190 ? 10.514  27.031  43.153  1.00 29.89  ?  190  THR D OG1 1 
ATOM   7497  C CG2 . THR D  1  190 ? 9.761   28.866  41.795  1.00 30.53  ?  190  THR D CG2 1 
ATOM   7498  N N   . LYS D  1  191 ? 11.786  27.855  38.841  1.00 25.61  ?  191  LYS D N   1 
ATOM   7499  C CA  . LYS D  1  191 ? 11.828  28.677  37.640  1.00 25.39  ?  191  LYS D CA  1 
ATOM   7500  C C   . LYS D  1  191 ? 11.835  27.866  36.349  1.00 24.30  ?  191  LYS D C   1 
ATOM   7501  O O   . LYS D  1  191 ? 11.874  28.461  35.267  1.00 24.08  ?  191  LYS D O   1 
ATOM   7502  C CB  . LYS D  1  191 ? 13.059  29.588  37.678  1.00 25.49  ?  191  LYS D CB  1 
ATOM   7503  C CG  . LYS D  1  191 ? 12.952  30.727  38.680  1.00 26.72  ?  191  LYS D CG  1 
ATOM   7504  C CD  . LYS D  1  191 ? 14.120  31.691  38.558  1.00 26.87  ?  191  LYS D CD  1 
ATOM   7505  C CE  . LYS D  1  191 ? 14.111  32.709  39.688  1.00 28.17  ?  191  LYS D CE  1 
ATOM   7506  N NZ  . LYS D  1  191 ? 15.311  33.591  39.648  1.00 28.37  ?  191  LYS D NZ  1 
ATOM   7507  N N   . VAL D  1  192 ? 11.791  26.535  36.427  1.00 24.64  ?  192  VAL D N   1 
ATOM   7508  C CA  . VAL D  1  192 ? 11.888  25.722  35.221  1.00 23.68  ?  192  VAL D CA  1 
ATOM   7509  C C   . VAL D  1  192 ? 10.590  25.813  34.427  1.00 23.80  ?  192  VAL D C   1 
ATOM   7510  O O   . VAL D  1  192 ? 9.488   25.869  34.992  1.00 24.50  ?  192  VAL D O   1 
ATOM   7511  C CB  . VAL D  1  192 ? 12.250  24.266  35.571  1.00 23.10  ?  192  VAL D CB  1 
ATOM   7512  C CG1 . VAL D  1  192 ? 11.027  23.471  36.011  1.00 23.37  ?  192  VAL D CG1 1 
ATOM   7513  C CG2 . VAL D  1  192 ? 12.929  23.590  34.388  1.00 22.14  ?  192  VAL D CG2 1 
ATOM   7514  N N   . THR D  1  193 ? 10.722  25.873  33.104  1.00 21.01  ?  193  THR D N   1 
ATOM   7515  C CA  . THR D  1  193 ? 9.584   25.920  32.198  1.00 21.06  ?  193  THR D CA  1 
ATOM   7516  C C   . THR D  1  193 ? 9.475   24.702  31.294  1.00 24.75  ?  193  THR D C   1 
ATOM   7517  O O   . THR D  1  193 ? 8.364   24.351  30.891  1.00 24.86  ?  193  THR D O   1 
ATOM   7518  C CB  . THR D  1  193 ? 9.643   27.182  31.323  1.00 21.29  ?  193  THR D CB  1 
ATOM   7519  O OG1 . THR D  1  193 ? 10.881  27.210  30.603  1.00 20.60  ?  193  THR D OG1 1 
ATOM   7520  C CG2 . THR D  1  193 ? 9.537   28.432  32.183  1.00 22.30  ?  193  THR D CG2 1 
ATOM   7521  N N   . GLU D  1  194 ? 10.591  24.059  30.957  1.00 23.40  ?  194  GLU D N   1 
ATOM   7522  C CA  . GLU D  1  194 ? 10.589  22.849  30.145  1.00 22.67  ?  194  GLU D CA  1 
ATOM   7523  C C   . GLU D  1  194 ? 11.494  21.806  30.784  1.00 22.28  ?  194  GLU D C   1 
ATOM   7524  O O   . GLU D  1  194 ? 12.620  22.118  31.186  1.00 22.24  ?  194  GLU D O   1 
ATOM   7525  C CB  . GLU D  1  194 ? 11.045  23.137  28.711  1.00 22.19  ?  194  GLU D CB  1 
ATOM   7526  C CG  . GLU D  1  194 ? 11.198  21.887  27.860  1.00 21.48  ?  194  GLU D CG  1 
ATOM   7527  C CD  . GLU D  1  194 ? 11.234  22.188  26.376  1.00 21.17  ?  194  GLU D CD  1 
ATOM   7528  O OE1 . GLU D  1  194 ? 10.198  22.623  25.830  1.00 21.42  ?  194  GLU D OE1 1 
ATOM   7529  O OE2 . GLU D  1  194 ? 12.298  21.984  25.755  1.00 20.74  -1 194  GLU D OE2 1 
ATOM   7530  N N   . ILE D  1  195 ? 10.997  20.575  30.882  1.00 19.96  ?  195  ILE D N   1 
ATOM   7531  C CA  . ILE D  1  195 ? 11.762  19.440  31.389  1.00 19.61  ?  195  ILE D CA  1 
ATOM   7532  C C   . ILE D  1  195 ? 11.591  18.302  30.393  1.00 19.05  ?  195  ILE D C   1 
ATOM   7533  O O   . ILE D  1  195 ? 10.492  17.747  30.264  1.00 19.14  ?  195  ILE D O   1 
ATOM   7534  C CB  . ILE D  1  195 ? 11.308  19.007  32.790  1.00 20.09  ?  195  ILE D CB  1 
ATOM   7535  C CG1 . ILE D  1  195 ? 11.555  20.118  33.811  1.00 20.72  ?  195  ILE D CG1 1 
ATOM   7536  C CG2 . ILE D  1  195 ? 12.028  17.737  33.209  1.00 19.74  ?  195  ILE D CG2 1 
ATOM   7537  C CD1 . ILE D  1  195 ? 10.964  19.828  35.174  1.00 21.35  ?  195  ILE D CD1 1 
ATOM   7538  N N   . ALA D  1  196 ? 12.665  17.952  29.687  1.00 19.88  ?  196  ALA D N   1 
ATOM   7539  C CA  . ALA D  1  196 ? 12.643  16.868  28.708  1.00 19.41  ?  196  ALA D CA  1 
ATOM   7540  C C   . ALA D  1  196 ? 13.636  15.796  29.141  1.00 19.20  ?  196  ALA D C   1 
ATOM   7541  O O   . ALA D  1  196 ? 14.850  16.031  29.140  1.00 19.12  ?  196  ALA D O   1 
ATOM   7542  C CB  . ALA D  1  196 ? 12.968  17.388  27.309  1.00 19.11  ?  196  ALA D CB  1 
ATOM   7543  N N   . ILE D  1  197 ? 13.120  14.625  29.519  1.00 20.15  ?  197  ILE D N   1 
ATOM   7544  C CA  . ILE D  1  197 ? 13.947  13.492  29.925  1.00 20.03  ?  197  ILE D CA  1 
ATOM   7545  C C   . ILE D  1  197 ? 13.534  12.262  29.123  1.00 19.75  ?  197  ILE D C   1 
ATOM   7546  O O   . ILE D  1  197 ? 13.727  11.124  29.566  1.00 19.76  ?  197  ILE D O   1 
ATOM   7547  C CB  . ILE D  1  197 ? 13.844  13.218  31.438  1.00 20.40  ?  197  ILE D CB  1 
ATOM   7548  C CG1 . ILE D  1  197 ? 13.720  14.520  32.226  1.00 20.80  ?  197  ILE D CG1 1 
ATOM   7549  C CG2 . ILE D  1  197 ? 15.078  12.473  31.934  1.00 20.36  ?  197  ILE D CG2 1 
ATOM   7550  C CD1 . ILE D  1  197 ? 13.274  14.317  33.658  1.00 21.28  ?  197  ILE D CD1 1 
ATOM   7551  N N   . TYR D  1  198 ? 12.946  12.473  27.950  1.00 20.10  ?  198  TYR D N   1 
ATOM   7552  C CA  . TYR D  1  198 ? 12.323  11.364  27.245  1.00 19.92  ?  198  TYR D CA  1 
ATOM   7553  C C   . TYR D  1  198 ? 13.372  10.471  26.580  1.00 19.66  ?  198  TYR D C   1 
ATOM   7554  O O   . TYR D  1  198 ? 14.545  10.829  26.444  1.00 20.02  ?  198  TYR D O   1 
ATOM   7555  C CB  . TYR D  1  198 ? 11.311  11.876  26.218  1.00 19.93  ?  198  TYR D CB  1 
ATOM   7556  C CG  . TYR D  1  198 ? 11.870  12.713  25.086  1.00 19.65  ?  198  TYR D CG  1 
ATOM   7557  C CD1 . TYR D  1  198 ? 12.300  12.123  23.901  1.00 19.35  ?  198  TYR D CD1 1 
ATOM   7558  C CD2 . TYR D  1  198 ? 11.947  14.095  25.195  1.00 19.80  ?  198  TYR D CD2 1 
ATOM   7559  C CE1 . TYR D  1  198 ? 12.786  12.888  22.854  1.00 19.22  ?  198  TYR D CE1 1 
ATOM   7560  C CE2 . TYR D  1  198 ? 12.444  14.868  24.163  1.00 19.65  ?  198  TYR D CE2 1 
ATOM   7561  C CZ  . TYR D  1  198 ? 12.860  14.260  22.992  1.00 19.35  ?  198  TYR D CZ  1 
ATOM   7562  O OH  . TYR D  1  198 ? 13.358  15.028  21.964  1.00 19.24  ?  198  TYR D OH  1 
ATOM   7563  N N   . ASP D  1  199 ? 12.921  9.280   26.176  1.00 19.69  ?  199  ASP D N   1 
ATOM   7564  C CA  . ASP D  1  199 ? 13.757  8.251   25.555  1.00 19.56  ?  199  ASP D CA  1 
ATOM   7565  C C   . ASP D  1  199 ? 14.919  7.856   26.472  1.00 19.74  ?  199  ASP D C   1 
ATOM   7566  O O   . ASP D  1  199 ? 16.097  8.011   26.145  1.00 19.77  ?  199  ASP D O   1 
ATOM   7567  C CB  . ASP D  1  199 ? 14.255  8.705   24.178  1.00 19.54  ?  199  ASP D CB  1 
ATOM   7568  C CG  . ASP D  1  199 ? 14.714  7.548   23.314  1.00 19.32  ?  199  ASP D CG  1 
ATOM   7569  O OD1 . ASP D  1  199 ? 14.744  6.404   23.815  1.00 19.43  ?  199  ASP D OD1 1 
ATOM   7570  O OD2 . ASP D  1  199 ? 15.030  7.778   22.128  1.00 19.30  -1 199  ASP D OD2 1 
ATOM   7571  N N   . ASN D  1  200 ? 14.549  7.327   27.637  1.00 18.95  ?  200  ASN D N   1 
ATOM   7572  C CA  . ASN D  1  200 ? 15.483  6.928   28.685  1.00 19.19  ?  200  ASN D CA  1 
ATOM   7573  C C   . ASN D  1  200 ? 14.978  5.623   29.292  1.00 19.32  ?  200  ASN D C   1 
ATOM   7574  O O   . ASN D  1  200 ? 14.098  4.956   28.738  1.00 19.22  ?  200  ASN D O   1 
ATOM   7575  C CB  . ASN D  1  200 ? 15.638  8.032   29.740  1.00 19.37  ?  200  ASN D CB  1 
ATOM   7576  C CG  . ASN D  1  200 ? 16.795  8.965   29.443  1.00 19.36  ?  200  ASN D CG  1 
ATOM   7577  O OD1 . ASN D  1  200 ? 17.943  8.664   29.767  1.00 19.54  ?  200  ASN D OD1 1 
ATOM   7578  N ND2 . ASN D  1  200 ? 16.500  10.103  28.824  1.00 19.23  ?  200  ASN D ND2 1 
ATOM   7579  N N   . LEU D  1  201 ? 15.552  5.246   30.430  1.00 18.59  ?  201  LEU D N   1 
ATOM   7580  C CA  . LEU D  1  201 ? 15.174  4.035   31.148  1.00 18.79  ?  201  LEU D CA  1 
ATOM   7581  C C   . LEU D  1  201 ? 14.644  4.367   32.539  1.00 19.06  ?  201  LEU D C   1 
ATOM   7582  O O   . LEU D  1  201 ? 14.884  3.640   33.505  1.00 19.33  ?  201  LEU D O   1 
ATOM   7583  C CB  . LEU D  1  201 ? 16.352  3.070   31.238  1.00 18.98  ?  201  LEU D CB  1 
ATOM   7584  C CG  . LEU D  1  201 ? 16.896  2.579   29.897  1.00 18.87  ?  201  LEU D CG  1 
ATOM   7585  C CD1 . LEU D  1  201 ? 18.332  2.112   30.047  1.00 19.21  ?  201  LEU D CD1 1 
ATOM   7586  C CD2 . LEU D  1  201 ? 16.020  1.470   29.344  1.00 18.78  ?  201  LEU D CD2 1 
ATOM   7587  N N   . LEU D  1  202 ? 13.906  5.468   32.654  1.00 20.52  ?  202  LEU D N   1 
ATOM   7588  C CA  . LEU D  1  202 ? 13.415  5.911   33.951  1.00 20.88  ?  202  LEU D CA  1 
ATOM   7589  C C   . LEU D  1  202 ? 12.362  4.952   34.495  1.00 21.13  ?  202  LEU D C   1 
ATOM   7590  O O   . LEU D  1  202 ? 11.589  4.346   33.747  1.00 20.99  ?  202  LEU D O   1 
ATOM   7591  C CB  . LEU D  1  202 ? 12.830  7.321   33.854  1.00 20.92  ?  202  LEU D CB  1 
ATOM   7592  C CG  . LEU D  1  202 ? 13.731  8.500   34.227  1.00 20.99  ?  202  LEU D CG  1 
ATOM   7593  C CD1 . LEU D  1  202 ? 15.135  8.327   33.679  1.00 20.76  ?  202  LEU D CD1 1 
ATOM   7594  C CD2 . LEU D  1  202 ? 13.128  9.799   33.725  1.00 20.98  ?  202  LEU D CD2 1 
ATOM   7595  N N   . THR D  1  203 ? 12.343  4.819   35.819  1.00 23.20  ?  203  THR D N   1 
ATOM   7596  C CA  . THR D  1  203 ? 11.418  3.947   36.529  1.00 23.56  ?  203  THR D CA  1 
ATOM   7597  C C   . THR D  1  203 ? 10.734  4.743   37.634  1.00 24.21  ?  203  THR D C   1 
ATOM   7598  O O   . THR D  1  203 ? 10.969  5.943   37.805  1.00 24.33  ?  203  THR D O   1 
ATOM   7599  C CB  . THR D  1  203 ? 12.137  2.725   37.117  1.00 23.67  ?  203  THR D CB  1 
ATOM   7600  O OG1 . THR D  1  203 ? 13.052  3.150   38.134  1.00 23.91  ?  203  THR D OG1 1 
ATOM   7601  C CG2 . THR D  1  203 ? 12.903  1.975   36.037  1.00 23.28  ?  203  THR D CG2 1 
ATOM   7602  N N   . GLY D  1  204 ? 9.874   4.063   38.387  1.00 25.37  ?  204  GLY D N   1 
ATOM   7603  C CA  . GLY D  1  204 ? 9.198   4.668   39.509  1.00 25.98  ?  204  GLY D CA  1 
ATOM   7604  C C   . GLY D  1  204 ? 8.083   5.601   39.088  1.00 26.19  ?  204  GLY D C   1 
ATOM   7605  O O   . GLY D  1  204 ? 7.754   5.723   37.905  1.00 25.78  ?  204  GLY D O   1 
ATOM   7606  N N   . PRO D  1  205 ? 7.476   6.278   40.055  1.00 26.38  ?  205  PRO D N   1 
ATOM   7607  C CA  . PRO D  1  205 ? 6.378   7.197   39.748  1.00 26.75  ?  205  PRO D CA  1 
ATOM   7608  C C   . PRO D  1  205 ? 6.895   8.560   39.307  1.00 26.61  ?  205  PRO D C   1 
ATOM   7609  O O   . PRO D  1  205 ? 8.081   8.878   39.411  1.00 26.15  ?  205  PRO D O   1 
ATOM   7610  C CB  . PRO D  1  205 ? 5.636   7.297   41.081  1.00 27.80  ?  205  PRO D CB  1 
ATOM   7611  C CG  . PRO D  1  205 ? 6.724   7.153   42.095  1.00 27.88  ?  205  PRO D CG  1 
ATOM   7612  C CD  . PRO D  1  205 ? 7.716   6.172   41.505  1.00 27.03  ?  205  PRO D CD  1 
ATOM   7613  N N   . ILE D  1  206 ? 5.971   9.366   38.804  1.00 23.91  ?  206  ILE D N   1 
ATOM   7614  C CA  . ILE D  1  206 ? 6.255   10.785  38.586  1.00 23.91  ?  206  ILE D CA  1 
ATOM   7615  C C   . ILE D  1  206 ? 6.209   11.495  39.936  1.00 24.77  ?  206  ILE D C   1 
ATOM   7616  O O   . ILE D  1  206 ? 5.236   11.315  40.685  1.00 25.61  ?  206  ILE D O   1 
ATOM   7617  C CB  . ILE D  1  206 ? 5.251   11.392  37.610  1.00 23.97  ?  206  ILE D CB  1 
ATOM   7618  C CG1 . ILE D  1  206 ? 5.520   10.895  36.188  1.00 23.09  ?  206  ILE D CG1 1 
ATOM   7619  C CG2 . ILE D  1  206 ? 5.306   12.914  37.657  1.00 24.28  ?  206  ILE D CG2 1 
ATOM   7620  C CD1 . ILE D  1  206 ? 4.337   11.041  35.258  1.00 23.21  ?  206  ILE D CD1 1 
ATOM   7621  N N   . PRO D  1  207 ? 7.232   12.267  40.297  1.00 26.13  ?  207  PRO D N   1 
ATOM   7622  C CA  . PRO D  1  207 ? 7.247   12.905  41.623  1.00 27.00  ?  207  PRO D CA  1 
ATOM   7623  C C   . PRO D  1  207 ? 6.065   13.846  41.795  1.00 27.89  ?  207  PRO D C   1 
ATOM   7624  O O   . PRO D  1  207 ? 5.847   14.753  40.988  1.00 27.75  ?  207  PRO D O   1 
ATOM   7625  C CB  . PRO D  1  207 ? 8.583   13.658  41.636  1.00 26.62  ?  207  PRO D CB  1 
ATOM   7626  C CG  . PRO D  1  207 ? 9.420   12.972  40.607  1.00 25.58  ?  207  PRO D CG  1 
ATOM   7627  C CD  . PRO D  1  207 ? 8.464   12.537  39.539  1.00 25.29  ?  207  PRO D CD  1 
ATOM   7628  N N   . SER D  1  208 ? 5.296   13.622  42.864  1.00 29.49  ?  208  SER D N   1 
ATOM   7629  C CA  . SER D  1  208 ? 4.154   14.481  43.149  1.00 30.54  ?  208  SER D CA  1 
ATOM   7630  C C   . SER D  1  208 ? 4.580   15.905  43.470  1.00 30.94  ?  208  SER D C   1 
ATOM   7631  O O   . SER D  1  208 ? 3.749   16.818  43.416  1.00 31.67  ?  208  SER D O   1 
ATOM   7632  C CB  . SER D  1  208 ? 3.338   13.907  44.309  1.00 31.93  ?  208  SER D CB  1 
ATOM   7633  O OG  . SER D  1  208 ? 4.171   13.574  45.405  1.00 33.10  ?  208  SER D OG  1 
ATOM   7634  N N   . SER D  1  209 ? 5.855   16.116  43.797  1.00 29.47  ?  209  SER D N   1 
ATOM   7635  C CA  . SER D  1  209 ? 6.393   17.457  43.982  1.00 29.74  ?  209  SER D CA  1 
ATOM   7636  C C   . SER D  1  209 ? 6.439   18.258  42.689  1.00 29.12  ?  209  SER D C   1 
ATOM   7637  O O   . SER D  1  209 ? 6.819   19.433  42.727  1.00 29.37  ?  209  SER D O   1 
ATOM   7638  C CB  . SER D  1  209 ? 7.794   17.380  44.589  1.00 29.43  ?  209  SER D CB  1 
ATOM   7639  O OG  . SER D  1  209 ? 8.691   16.719  43.713  1.00 28.21  ?  209  SER D OG  1 
ATOM   7640  N N   . PHE D  1  210 ? 6.064   17.661  41.554  1.00 28.75  ?  210  PHE D N   1 
ATOM   7641  C CA  . PHE D  1  210 ? 6.070   18.385  40.290  1.00 28.23  ?  210  PHE D CA  1 
ATOM   7642  C C   . PHE D  1  210 ? 5.004   19.469  40.246  1.00 29.14  ?  210  PHE D C   1 
ATOM   7643  O O   . PHE D  1  210 ? 5.096   20.376  39.412  1.00 28.92  ?  210  PHE D O   1 
ATOM   7644  C CB  . PHE D  1  210 ? 5.884   17.414  39.123  1.00 27.33  ?  210  PHE D CB  1 
ATOM   7645  C CG  . PHE D  1  210 ? 7.175   16.889  38.563  1.00 26.28  ?  210  PHE D CG  1 
ATOM   7646  C CD1 . PHE D  1  210 ? 8.329   16.893  39.330  1.00 26.21  ?  210  PHE D CD1 1 
ATOM   7647  C CD2 . PHE D  1  210 ? 7.236   16.389  37.273  1.00 25.53  ?  210  PHE D CD2 1 
ATOM   7648  C CE1 . PHE D  1  210 ? 9.521   16.412  38.820  1.00 25.34  ?  210  PHE D CE1 1 
ATOM   7649  C CE2 . PHE D  1  210 ? 8.426   15.905  36.757  1.00 24.62  ?  210  PHE D CE2 1 
ATOM   7650  C CZ  . PHE D  1  210 ? 9.569   15.917  37.532  1.00 24.58  ?  210  PHE D CZ  1 
ATOM   7651  N N   . GLY D  1  211 ? 3.994   19.393  41.116  1.00 28.43  ?  211  GLY D N   1 
ATOM   7652  C CA  . GLY D  1  211 ? 3.061   20.497  41.247  1.00 29.49  ?  211  GLY D CA  1 
ATOM   7653  C C   . GLY D  1  211 ? 3.740   21.791  41.649  1.00 29.89  ?  211  GLY D C   1 
ATOM   7654  O O   . GLY D  1  211 ? 3.253   22.878  41.329  1.00 30.46  ?  211  GLY D O   1 
ATOM   7655  N N   . ASN D  1  212 ? 4.874   21.694  42.347  1.00 29.97  ?  212  ASN D N   1 
ATOM   7656  C CA  . ASN D  1  212 ? 5.633   22.873  42.746  1.00 30.34  ?  212  ASN D CA  1 
ATOM   7657  C C   . ASN D  1  212 ? 6.297   23.577  41.569  1.00 29.51  ?  212  ASN D C   1 
ATOM   7658  O O   . ASN D  1  212 ? 6.847   24.668  41.755  1.00 29.85  ?  212  ASN D O   1 
ATOM   7659  C CB  . ASN D  1  212 ? 6.694   22.484  43.778  1.00 30.30  ?  212  ASN D CB  1 
ATOM   7660  C CG  . ASN D  1  212 ? 6.089   22.026  45.093  1.00 31.39  ?  212  ASN D CG  1 
ATOM   7661  O OD1 . ASN D  1  212 ? 4.883   22.143  45.310  1.00 32.31  ?  212  ASN D OD1 1 
ATOM   7662  N ND2 . ASN D  1  212 ? 6.927   21.497  45.976  1.00 31.57  ?  212  ASN D ND2 1 
ATOM   7663  N N   . LEU D  1  213 ? 6.260   22.987  40.373  1.00 28.25  ?  213  LEU D N   1 
ATOM   7664  C CA  . LEU D  1  213 ? 6.872   23.583  39.183  1.00 27.49  ?  213  LEU D CA  1 
ATOM   7665  C C   . LEU D  1  213 ? 5.838   24.448  38.460  1.00 27.99  ?  213  LEU D C   1 
ATOM   7666  O O   . LEU D  1  213 ? 5.392   24.156  37.349  1.00 27.47  ?  213  LEU D O   1 
ATOM   7667  C CB  . LEU D  1  213 ? 7.431   22.496  38.274  1.00 26.25  ?  213  LEU D CB  1 
ATOM   7668  C CG  . LEU D  1  213 ? 8.344   21.456  38.926  1.00 25.78  ?  213  LEU D CG  1 
ATOM   7669  C CD1 . LEU D  1  213 ? 8.566   20.276  37.993  1.00 24.76  ?  213  LEU D CD1 1 
ATOM   7670  C CD2 . LEU D  1  213 ? 9.667   22.076  39.334  1.00 25.69  ?  213  LEU D CD2 1 
ATOM   7671  N N   . THR D  1  214 ? 5.459   25.539  39.131  1.00 28.84  ?  214  THR D N   1 
ATOM   7672  C CA  . THR D  1  214 ? 4.368   26.381  38.643  1.00 29.59  ?  214  THR D CA  1 
ATOM   7673  C C   . THR D  1  214 ? 4.666   26.981  37.273  1.00 28.94  ?  214  THR D C   1 
ATOM   7674  O O   . THR D  1  214 ? 3.746   27.176  36.471  1.00 29.12  ?  214  THR D O   1 
ATOM   7675  C CB  . THR D  1  214 ? 4.073   27.492  39.652  1.00 30.99  ?  214  THR D CB  1 
ATOM   7676  O OG1 . THR D  1  214 ? 5.274   28.225  39.925  1.00 30.87  ?  214  THR D OG1 1 
ATOM   7677  C CG2 . THR D  1  214 ? 3.542   26.902  40.951  1.00 31.83  ?  214  THR D CG2 1 
ATOM   7678  N N   . LYS D  1  215 ? 5.931   27.285  36.987  1.00 28.32  ?  215  LYS D N   1 
ATOM   7679  C CA  . LYS D  1  215 ? 6.304   27.903  35.719  1.00 27.79  ?  215  LYS D CA  1 
ATOM   7680  C C   . LYS D  1  215 ? 6.436   26.901  34.576  1.00 26.62  ?  215  LYS D C   1 
ATOM   7681  O O   . LYS D  1  215 ? 6.694   27.317  33.441  1.00 26.18  ?  215  LYS D O   1 
ATOM   7682  C CB  . LYS D  1  215 ? 7.618   28.674  35.879  1.00 27.65  ?  215  LYS D CB  1 
ATOM   7683  C CG  . LYS D  1  215 ? 7.590   29.754  36.954  1.00 28.85  ?  215  LYS D CG  1 
ATOM   7684  C CD  . LYS D  1  215 ? 7.017   31.067  36.437  1.00 29.65  ?  215  LYS D CD  1 
ATOM   7685  C CE  . LYS D  1  215 ? 6.487   31.920  37.583  1.00 31.11  ?  215  LYS D CE  1 
ATOM   7686  N NZ  . LYS D  1  215 ? 5.668   33.070  37.104  1.00 32.05  ?  215  LYS D NZ  1 
ATOM   7687  N N   . LEU D  1  216 ? 6.273   25.606  34.843  1.00 25.64  ?  216  LEU D N   1 
ATOM   7688  C CA  . LEU D  1  216 ? 6.443   24.587  33.813  1.00 24.61  ?  216  LEU D CA  1 
ATOM   7689  C C   . LEU D  1  216 ? 5.385   24.724  32.725  1.00 24.68  ?  216  LEU D C   1 
ATOM   7690  O O   . LEU D  1  216 ? 4.194   24.870  33.017  1.00 25.48  ?  216  LEU D O   1 
ATOM   7691  C CB  . LEU D  1  216 ? 6.362   23.196  34.443  1.00 24.33  ?  216  LEU D CB  1 
ATOM   7692  C CG  . LEU D  1  216 ? 6.750   21.988  33.590  1.00 23.29  ?  216  LEU D CG  1 
ATOM   7693  C CD1 . LEU D  1  216 ? 8.237   22.002  33.266  1.00 22.55  ?  216  LEU D CD1 1 
ATOM   7694  C CD2 . LEU D  1  216 ? 6.357   20.694  34.291  1.00 23.30  ?  216  LEU D CD2 1 
ATOM   7695  N N   . VAL D  1  217 ? 5.820   24.680  31.463  1.00 23.88  ?  217  VAL D N   1 
ATOM   7696  C CA  . VAL D  1  217 ? 4.881   24.718  30.346  1.00 23.89  ?  217  VAL D CA  1 
ATOM   7697  C C   . VAL D  1  217 ? 5.000   23.462  29.487  1.00 22.96  ?  217  VAL D C   1 
ATOM   7698  O O   . VAL D  1  217 ? 4.030   23.052  28.839  1.00 23.01  ?  217  VAL D O   1 
ATOM   7699  C CB  . VAL D  1  217 ? 5.087   25.986  29.492  1.00 24.04  ?  217  VAL D CB  1 
ATOM   7700  C CG1 . VAL D  1  217 ? 5.103   27.228  30.371  1.00 24.99  ?  217  VAL D CG1 1 
ATOM   7701  C CG2 . VAL D  1  217 ? 6.368   25.893  28.676  1.00 23.12  ?  217  VAL D CG2 1 
ATOM   7702  N N   . ASN D  1  218 ? 6.177   22.833  29.486  1.00 22.07  ?  218  ASN D N   1 
ATOM   7703  C CA  . ASN D  1  218 ? 6.460   21.683  28.629  1.00 21.23  ?  218  ASN D CA  1 
ATOM   7704  C C   . ASN D  1  218 ? 7.049   20.558  29.470  1.00 20.91  ?  218  ASN D C   1 
ATOM   7705  O O   . ASN D  1  218 ? 8.163   20.685  29.988  1.00 20.73  ?  218  ASN D O   1 
ATOM   7706  C CB  . ASN D  1  218 ? 7.414   22.059  27.492  1.00 20.64  ?  218  ASN D CB  1 
ATOM   7707  C CG  . ASN D  1  218 ? 6.775   22.979  26.466  1.00 20.89  ?  218  ASN D CG  1 
ATOM   7708  O OD1 . ASN D  1  218 ? 5.572   23.234  26.501  1.00 21.48  ?  218  ASN D OD1 1 
ATOM   7709  N ND2 . ASN D  1  218 ? 7.585   23.480  25.540  1.00 20.52  ?  218  ASN D ND2 1 
ATOM   7710  N N   . LEU D  1  219 ? 6.312   19.457  29.601  1.00 18.45  ?  219  LEU D N   1 
ATOM   7711  C CA  . LEU D  1  219 ? 6.783   18.275  30.319  1.00 18.18  ?  219  LEU D CA  1 
ATOM   7712  C C   . LEU D  1  219 ? 6.825   17.103  29.346  1.00 17.52  ?  219  LEU D C   1 
ATOM   7713  O O   . LEU D  1  219 ? 5.779   16.642  28.877  1.00 17.63  ?  219  LEU D O   1 
ATOM   7714  C CB  . LEU D  1  219 ? 5.886   17.967  31.518  1.00 18.88  ?  219  LEU D CB  1 
ATOM   7715  C CG  . LEU D  1  219 ? 6.389   16.887  32.479  1.00 18.75  ?  219  LEU D CG  1 
ATOM   7716  C CD1 . LEU D  1  219 ? 7.862   17.095  32.802  1.00 18.38  ?  219  LEU D CD1 1 
ATOM   7717  C CD2 . LEU D  1  219 ? 5.556   16.870  33.750  1.00 19.61  ?  219  LEU D CD2 1 
ATOM   7718  N N   . TYR D  1  220 ? 8.031   16.618  29.050  1.00 19.85  ?  220  TYR D N   1 
ATOM   7719  C CA  . TYR D  1  220 ? 8.245   15.534  28.094  1.00 19.28  ?  220  TYR D CA  1 
ATOM   7720  C C   . TYR D  1  220 ? 8.936   14.382  28.815  1.00 19.08  ?  220  TYR D C   1 
ATOM   7721  O O   . TYR D  1  220 ? 10.117  14.482  29.163  1.00 18.92  ?  220  TYR D O   1 
ATOM   7722  C CB  . TYR D  1  220 ? 9.076   16.011  26.903  1.00 18.83  ?  220  TYR D CB  1 
ATOM   7723  C CG  . TYR D  1  220 ? 8.491   17.207  26.184  1.00 19.05  ?  220  TYR D CG  1 
ATOM   7724  C CD1 . TYR D  1  220 ? 7.121   17.317  25.982  1.00 19.42  ?  220  TYR D CD1 1 
ATOM   7725  C CD2 . TYR D  1  220 ? 9.307   18.225  25.707  1.00 18.95  ?  220  TYR D CD2 1 
ATOM   7726  C CE1 . TYR D  1  220 ? 6.581   18.406  25.326  1.00 19.69  ?  220  TYR D CE1 1 
ATOM   7727  C CE2 . TYR D  1  220 ? 8.775   19.319  25.049  1.00 19.19  ?  220  TYR D CE2 1 
ATOM   7728  C CZ  . TYR D  1  220 ? 7.412   19.404  24.862  1.00 19.57  ?  220  TYR D CZ  1 
ATOM   7729  O OH  . TYR D  1  220 ? 6.876   20.490  24.208  1.00 19.89  ?  220  TYR D OH  1 
ATOM   7730  N N   . LEU D  1  221 ? 8.199   13.289  29.037  1.00 18.10  ?  221  LEU D N   1 
ATOM   7731  C CA  . LEU D  1  221 ? 8.708   12.142  29.782  1.00 18.02  ?  221  LEU D CA  1 
ATOM   7732  C C   . LEU D  1  221 ? 8.404   10.822  29.080  1.00 17.73  ?  221  LEU D C   1 
ATOM   7733  O O   . LEU D  1  221 ? 8.266   9.788   29.739  1.00 17.84  ?  221  LEU D O   1 
ATOM   7734  C CB  . LEU D  1  221 ? 8.130   12.118  31.196  1.00 18.60  ?  221  LEU D CB  1 
ATOM   7735  C CG  . LEU D  1  221 ? 8.427   13.296  32.120  1.00 19.01  ?  221  LEU D CG  1 
ATOM   7736  C CD1 . LEU D  1  221 ? 7.690   13.127  33.437  1.00 19.69  ?  221  LEU D CD1 1 
ATOM   7737  C CD2 . LEU D  1  221 ? 9.922   13.414  32.349  1.00 18.71  ?  221  LEU D CD2 1 
ATOM   7738  N N   . PHE D  1  222 ? 8.296   10.825  27.756  1.00 18.10  ?  222  PHE D N   1 
ATOM   7739  C CA  . PHE D  1  222 ? 7.848   9.622   27.071  1.00 17.92  ?  222  PHE D CA  1 
ATOM   7740  C C   . PHE D  1  222 ? 9.024   8.697   26.762  1.00 17.55  ?  222  PHE D C   1 
ATOM   7741  O O   . PHE D  1  222 ? 10.191  9.049   26.936  1.00 17.43  ?  222  PHE D O   1 
ATOM   7742  C CB  . PHE D  1  222 ? 7.090   9.963   25.791  1.00 17.82  ?  222  PHE D CB  1 
ATOM   7743  C CG  . PHE D  1  222 ? 7.810   10.898  24.886  1.00 17.55  ?  222  PHE D CG  1 
ATOM   7744  C CD1 . PHE D  1  222 ? 7.783   12.262  25.103  1.00 17.75  ?  222  PHE D CD1 1 
ATOM   7745  C CD2 . PHE D  1  222 ? 8.506   10.407  23.799  1.00 17.15  ?  222  PHE D CD2 1 
ATOM   7746  C CE1 . PHE D  1  222 ? 8.448   13.103  24.259  1.00 17.53  ?  222  PHE D CE1 1 
ATOM   7747  C CE2 . PHE D  1  222 ? 9.168   11.244  22.955  1.00 16.96  ?  222  PHE D CE2 1 
ATOM   7748  C CZ  . PHE D  1  222 ? 9.138   12.587  23.181  1.00 17.13  ?  222  PHE D CZ  1 
ATOM   7749  N N   . ILE D  1  223 ? 8.690   7.493   26.294  1.00 18.32  ?  223  ILE D N   1 
ATOM   7750  C CA  . ILE D  1  223 ? 9.657   6.428   26.038  1.00 18.10  ?  223  ILE D CA  1 
ATOM   7751  C C   . ILE D  1  223 ? 10.454  6.181   27.313  1.00 18.27  ?  223  ILE D C   1 
ATOM   7752  O O   . ILE D  1  223 ? 11.647  6.497   27.396  1.00 18.18  ?  223  ILE D O   1 
ATOM   7753  C CB  . ILE D  1  223 ? 10.574  6.761   24.846  1.00 17.80  ?  223  ILE D CB  1 
ATOM   7754  C CG1 . ILE D  1  223 ? 9.737   7.206   23.646  1.00 17.68  ?  223  ILE D CG1 1 
ATOM   7755  C CG2 . ILE D  1  223 ? 11.406  5.548   24.453  1.00 17.71  ?  223  ILE D CG2 1 
ATOM   7756  C CD1 . ILE D  1  223 ? 10.555  7.705   22.475  1.00 17.45  ?  223  ILE D CD1 1 
ATOM   7757  N N   . ASN D  1  224 ? 9.790   5.609   28.309  1.00 20.71  ?  224  ASN D N   1 
ATOM   7758  C CA  . ASN D  1  224 ? 10.369  5.329   29.614  1.00 20.93  ?  224  ASN D CA  1 
ATOM   7759  C C   . ASN D  1  224 ? 9.521   4.239   30.257  1.00 21.20  ?  224  ASN D C   1 
ATOM   7760  O O   . ASN D  1  224 ? 8.629   3.670   29.619  1.00 21.82  ?  224  ASN D O   1 
ATOM   7761  C CB  . ASN D  1  224 ? 10.436  6.596   30.475  1.00 21.15  ?  224  ASN D CB  1 
ATOM   7762  C CG  . ASN D  1  224 ? 11.734  7.352   30.304  1.00 20.97  ?  224  ASN D CG  1 
ATOM   7763  O OD1 . ASN D  1  224 ? 12.784  6.910   30.762  1.00 20.99  ?  224  ASN D OD1 1 
ATOM   7764  N ND2 . ASN D  1  224 ? 11.670  8.501   29.642  1.00 20.86  ?  224  ASN D ND2 1 
ATOM   7765  N N   . SER D  1  225 ? 9.794   3.945   31.522  1.00 24.69  ?  225  SER D N   1 
ATOM   7766  C CA  . SER D  1  225 ? 9.031   2.948   32.261  1.00 24.98  ?  225  SER D CA  1 
ATOM   7767  C C   . SER D  1  225 ? 8.551   3.518   33.587  1.00 25.57  ?  225  SER D C   1 
ATOM   7768  O O   . SER D  1  225 ? 8.563   2.839   34.619  1.00 25.90  ?  225  SER D O   1 
ATOM   7769  C CB  . SER D  1  225 ? 9.848   1.676   32.471  1.00 24.94  ?  225  SER D CB  1 
ATOM   7770  O OG  . SER D  1  225 ? 9.824   0.864   31.308  1.00 24.86  ?  225  SER D OG  1 
ATOM   7771  N N   . LEU D  1  226 ? 8.135   4.784   33.578  1.00 23.25  ?  226  LEU D N   1 
ATOM   7772  C CA  . LEU D  1  226 ? 7.519   5.376   34.757  1.00 23.85  ?  226  LEU D CA  1 
ATOM   7773  C C   . LEU D  1  226 ? 6.247   4.616   35.113  1.00 24.33  ?  226  LEU D C   1 
ATOM   7774  O O   . LEU D  1  226 ? 5.495   4.188   34.234  1.00 24.22  ?  226  LEU D O   1 
ATOM   7775  C CB  . LEU D  1  226 ? 7.207   6.852   34.509  1.00 23.95  ?  226  LEU D CB  1 
ATOM   7776  C CG  . LEU D  1  226 ? 8.402   7.717   34.101  1.00 23.53  ?  226  LEU D CG  1 
ATOM   7777  C CD1 . LEU D  1  226 ? 7.943   9.098   33.661  1.00 23.63  ?  226  LEU D CD1 1 
ATOM   7778  C CD2 . LEU D  1  226 ? 9.404   7.819   35.240  1.00 23.69  ?  226  LEU D CD2 1 
ATOM   7779  N N   . SER D  1  227 ? 6.003   4.458   36.411  1.00 26.84  ?  227  SER D N   1 
ATOM   7780  C CA  . SER D  1  227 ? 4.980   3.549   36.910  1.00 27.38  ?  227  SER D CA  1 
ATOM   7781  C C   . SER D  1  227 ? 4.039   4.284   37.859  1.00 28.26  ?  227  SER D C   1 
ATOM   7782  O O   . SER D  1  227 ? 4.209   5.471   38.152  1.00 28.43  ?  227  SER D O   1 
ATOM   7783  C CB  . SER D  1  227 ? 5.619   2.338   37.603  1.00 27.39  ?  227  SER D CB  1 
ATOM   7784  O OG  . SER D  1  227 ? 6.532   2.748   38.607  1.00 27.54  ?  227  SER D OG  1 
ATOM   7785  N N   . GLY D  1  228 ? 3.029   3.559   38.332  1.00 30.14  ?  228  GLY D N   1 
ATOM   7786  C CA  . GLY D  1  228 ? 2.063   4.102   39.268  1.00 31.48  ?  228  GLY D CA  1 
ATOM   7787  C C   . GLY D  1  228 ? 1.097   5.073   38.613  1.00 31.41  ?  228  GLY D C   1 
ATOM   7788  O O   . GLY D  1  228 ? 1.094   5.290   37.402  1.00 31.06  ?  228  GLY D O   1 
ATOM   7789  N N   . SER D  1  229 ? 0.253   5.667   39.453  1.00 30.84  ?  229  SER D N   1 
ATOM   7790  C CA  . SER D  1  229 ? -0.724  6.632   38.977  1.00 31.62  ?  229  SER D CA  1 
ATOM   7791  C C   . SER D  1  229 ? -0.066  7.981   38.706  1.00 30.94  ?  229  SER D C   1 
ATOM   7792  O O   . SER D  1  229 ? 1.007   8.299   39.225  1.00 30.67  ?  229  SER D O   1 
ATOM   7793  C CB  . SER D  1  229 ? -1.856  6.797   39.992  1.00 32.99  ?  229  SER D CB  1 
ATOM   7794  O OG  . SER D  1  229 ? -2.442  5.548   40.314  1.00 33.68  ?  229  SER D OG  1 
ATOM   7795  N N   . ILE D  1  230 ? -0.729  8.775   37.877  1.00 28.53  ?  230  ILE D N   1 
ATOM   7796  C CA  . ILE D  1  230 ? -0.259  10.136  37.603  1.00 28.36  ?  230  ILE D CA  1 
ATOM   7797  C C   . ILE D  1  230 ? -0.575  11.021  38.804  1.00 29.44  ?  230  ILE D C   1 
ATOM   7798  O O   . ILE D  1  230 ? -1.717  11.003  39.297  1.00 30.48  ?  230  ILE D O   1 
ATOM   7799  C CB  . ILE D  1  230 ? -0.912  10.677  36.331  1.00 28.17  ?  230  ILE D CB  1 
ATOM   7800  C CG1 . ILE D  1  230 ? -0.863  9.626   35.223  1.00 27.35  ?  230  ILE D CG1 1 
ATOM   7801  C CG2 . ILE D  1  230 ? -0.244  11.970  35.886  1.00 27.82  ?  230  ILE D CG2 1 
ATOM   7802  C CD1 . ILE D  1  230 ? -1.519  10.065  33.939  1.00 27.19  ?  230  ILE D CD1 1 
ATOM   7803  N N   . PRO D  1  231 ? 0.386   11.788  39.316  1.00 29.14  ?  231  PRO D N   1 
ATOM   7804  C CA  . PRO D  1  231 ? 0.088   12.705  40.423  1.00 30.24  ?  231  PRO D CA  1 
ATOM   7805  C C   . PRO D  1  231 ? -0.983  13.710  40.026  1.00 30.97  ?  231  PRO D C   1 
ATOM   7806  O O   . PRO D  1  231 ? -0.875  14.381  38.997  1.00 30.44  ?  231  PRO D O   1 
ATOM   7807  C CB  . PRO D  1  231 ? 1.432   13.391  40.698  1.00 29.76  ?  231  PRO D CB  1 
ATOM   7808  C CG  . PRO D  1  231 ? 2.459   12.551  40.025  1.00 28.53  ?  231  PRO D CG  1 
ATOM   7809  C CD  . PRO D  1  231 ? 1.786   11.884  38.873  1.00 28.08  ?  231  PRO D CD  1 
ATOM   7810  N N   . SER D  1  232 ? -2.030  13.803  40.850  1.00 32.51  ?  232  SER D N   1 
ATOM   7811  C CA  . SER D  1  232 ? -3.089  14.771  40.586  1.00 33.40  ?  232  SER D CA  1 
ATOM   7812  C C   . SER D  1  232 ? -2.550  16.195  40.549  1.00 33.45  ?  232  SER D C   1 
ATOM   7813  O O   . SER D  1  232 ? -3.131  17.061  39.886  1.00 33.73  ?  232  SER D O   1 
ATOM   7814  C CB  . SER D  1  232 ? -4.195  14.647  41.635  1.00 34.95  ?  232  SER D CB  1 
ATOM   7815  O OG  . SER D  1  232 ? -3.669  14.308  42.906  1.00 35.37  ?  232  SER D OG  1 
ATOM   7816  N N   . GLU D  1  233 ? -1.441  16.452  41.250  1.00 33.33  ?  233  GLU D N   1 
ATOM   7817  C CA  . GLU D  1  233 ? -0.862  17.791  41.290  1.00 33.42  ?  233  GLU D CA  1 
ATOM   7818  C C   . GLU D  1  233 ? -0.486  18.299  39.903  1.00 32.42  ?  233  GLU D C   1 
ATOM   7819  O O   . GLU D  1  233 ? -0.415  19.517  39.693  1.00 32.70  ?  233  GLU D O   1 
ATOM   7820  C CB  . GLU D  1  233 ? 0.369   17.806  42.198  1.00 33.21  ?  233  GLU D CB  1 
ATOM   7821  C CG  . GLU D  1  233 ? 0.068   17.617  43.675  1.00 34.42  ?  233  GLU D CG  1 
ATOM   7822  C CD  . GLU D  1  233 ? -0.268  16.181  44.027  1.00 34.41  ?  233  GLU D CD  1 
ATOM   7823  O OE1 . GLU D  1  233 ? 0.481   15.272  43.612  1.00 33.28  ?  233  GLU D OE1 1 
ATOM   7824  O OE2 . GLU D  1  233 ? -1.284  15.963  44.722  1.00 36.18  -1 233  GLU D OE2 1 
ATOM   7825  N N   . ILE D  1  234 ? -0.227  17.396  38.953  1.00 30.59  ?  234  ILE D N   1 
ATOM   7826  C CA  . ILE D  1  234 ? 0.123   17.820  37.598  1.00 29.70  ?  234  ILE D CA  1 
ATOM   7827  C C   . ILE D  1  234 ? -0.999  18.658  36.996  1.00 30.39  ?  234  ILE D C   1 
ATOM   7828  O O   . ILE D  1  234 ? -0.750  19.625  36.264  1.00 30.18  ?  234  ILE D O   1 
ATOM   7829  C CB  . ILE D  1  234 ? 0.449   16.597  36.718  1.00 29.90  ?  234  ILE D CB  1 
ATOM   7830  C CG1 . ILE D  1  234 ? 1.573   15.768  37.346  1.00 29.32  ?  234  ILE D CG1 1 
ATOM   7831  C CG2 . ILE D  1  234 ? 0.820   17.036  35.305  1.00 29.07  ?  234  ILE D CG2 1 
ATOM   7832  C CD1 . ILE D  1  234 ? 2.967   16.242  36.992  1.00 27.18  ?  234  ILE D CD1 1 
ATOM   7833  N N   . GLY D  1  235 ? -2.248  18.319  37.314  1.00 32.90  ?  235  GLY D N   1 
ATOM   7834  C CA  . GLY D  1  235 ? -3.386  19.082  36.834  1.00 33.85  ?  235  GLY D CA  1 
ATOM   7835  C C   . GLY D  1  235 ? -3.470  20.499  37.365  1.00 34.93  ?  235  GLY D C   1 
ATOM   7836  O O   . GLY D  1  235 ? -4.251  21.294  36.829  1.00 35.45  ?  235  GLY D O   1 
ATOM   7837  N N   . ASN D  1  236 ? -2.695  20.834  38.394  1.00 35.26  ?  236  ASN D N   1 
ATOM   7838  C CA  . ASN D  1  236 ? -2.714  22.165  38.985  1.00 36.43  ?  236  ASN D CA  1 
ATOM   7839  C C   . ASN D  1  236 ? -1.571  23.043  38.493  1.00 35.63  ?  236  ASN D C   1 
ATOM   7840  O O   . ASN D  1  236 ? -1.322  24.104  39.076  1.00 36.90  ?  236  ASN D O   1 
ATOM   7841  C CB  . ASN D  1  236 ? -2.683  22.061  40.510  1.00 37.74  ?  236  ASN D CB  1 
ATOM   7842  C CG  . ASN D  1  236 ? -3.956  21.466  41.076  1.00 38.89  ?  236  ASN D CG  1 
ATOM   7843  O OD1 . ASN D  1  236 ? -5.059  21.813  40.651  1.00 39.42  ?  236  ASN D OD1 1 
ATOM   7844  N ND2 . ASN D  1  236 ? -3.811  20.553  42.028  1.00 38.53  ?  236  ASN D ND2 1 
ATOM   7845  N N   . LEU D  1  237 ? -0.873  22.628  37.440  1.00 32.93  ?  237  LEU D N   1 
ATOM   7846  C CA  . LEU D  1  237 ? 0.168   23.451  36.842  1.00 32.25  ?  237  LEU D CA  1 
ATOM   7847  C C   . LEU D  1  237 ? -0.494  24.498  35.954  1.00 32.69  ?  237  LEU D C   1 
ATOM   7848  O O   . LEU D  1  237 ? -1.087  24.155  34.923  1.00 32.35  ?  237  LEU D O   1 
ATOM   7849  C CB  . LEU D  1  237 ? 1.144   22.583  36.049  1.00 30.77  ?  237  LEU D CB  1 
ATOM   7850  C CG  . LEU D  1  237 ? 1.860   21.529  36.899  1.00 30.35  ?  237  LEU D CG  1 
ATOM   7851  C CD1 . LEU D  1  237 ? 2.534   20.480  36.026  1.00 29.06  ?  237  LEU D CD1 1 
ATOM   7852  C CD2 . LEU D  1  237 ? 2.865   22.185  37.833  1.00 30.56  ?  237  LEU D CD2 1 
ATOM   7853  N N   . PRO D  1  238 ? -0.411  25.782  36.315  1.00 35.79  ?  238  PRO D N   1 
ATOM   7854  C CA  . PRO D  1  238 ? -1.214  26.785  35.595  1.00 36.48  ?  238  PRO D CA  1 
ATOM   7855  C C   . PRO D  1  238 ? -0.726  27.064  34.185  1.00 35.51  ?  238  PRO D C   1 
ATOM   7856  O O   . PRO D  1  238 ? -1.548  27.234  33.276  1.00 35.70  ?  238  PRO D O   1 
ATOM   7857  C CB  . PRO D  1  238 ? -1.102  28.022  36.497  1.00 37.63  ?  238  PRO D CB  1 
ATOM   7858  C CG  . PRO D  1  238 ? 0.219   27.864  37.174  1.00 37.01  ?  238  PRO D CG  1 
ATOM   7859  C CD  . PRO D  1  238 ? 0.423   26.383  37.370  1.00 36.16  ?  238  PRO D CD  1 
ATOM   7860  N N   . ASN D  1  239 ? 0.586   27.115  33.972  1.00 35.42  ?  239  ASN D N   1 
ATOM   7861  C CA  . ASN D  1  239 ? 1.147   27.492  32.682  1.00 34.38  ?  239  ASN D CA  1 
ATOM   7862  C C   . ASN D  1  239 ? 1.437   26.302  31.779  1.00 33.14  ?  239  ASN D C   1 
ATOM   7863  O O   . ASN D  1  239 ? 1.950   26.499  30.672  1.00 32.45  ?  239  ASN D O   1 
ATOM   7864  C CB  . ASN D  1  239 ? 2.430   28.304  32.882  1.00 34.15  ?  239  ASN D CB  1 
ATOM   7865  C CG  . ASN D  1  239 ? 2.245   29.457  33.848  1.00 35.41  ?  239  ASN D CG  1 
ATOM   7866  O OD1 . ASN D  1  239 ? 1.121   29.806  34.209  1.00 36.91  ?  239  ASN D OD1 1 
ATOM   7867  N ND2 . ASN D  1  239 ? 3.351   30.056  34.272  1.00 35.45  ?  239  ASN D ND2 1 
ATOM   7868  N N   . LEU D  1  240 ? 1.141   25.081  32.223  1.00 28.79  ?  240  LEU D N   1 
ATOM   7869  C CA  . LEU D  1  240 ? 1.410   23.900  31.413  1.00 27.70  ?  240  LEU D CA  1 
ATOM   7870  C C   . LEU D  1  240 ? 0.699   23.999  30.068  1.00 27.58  ?  240  LEU D C   1 
ATOM   7871  O O   . LEU D  1  240 ? -0.481  24.353  29.999  1.00 28.44  ?  240  LEU D O   1 
ATOM   7872  C CB  . LEU D  1  240 ? 0.972   22.639  32.157  1.00 27.74  ?  240  LEU D CB  1 
ATOM   7873  C CG  . LEU D  1  240 ? 1.404   21.309  31.535  1.00 26.66  ?  240  LEU D CG  1 
ATOM   7874  C CD1 . LEU D  1  240 ? 2.911   21.137  31.642  1.00 25.82  ?  240  LEU D CD1 1 
ATOM   7875  C CD2 . LEU D  1  240 ? 0.683   20.145  32.193  1.00 26.92  ?  240  LEU D CD2 1 
ATOM   7876  N N   . ARG D  1  241 ? 1.429   23.699  28.999  1.00 29.97  ?  241  ARG D N   1 
ATOM   7877  C CA  . ARG D  1  241 ? 0.893   23.744  27.644  1.00 29.76  ?  241  ARG D CA  1 
ATOM   7878  C C   . ARG D  1  241 ? 0.929   22.399  26.940  1.00 28.97  ?  241  ARG D C   1 
ATOM   7879  O O   . ARG D  1  241 ? -0.024  22.052  26.239  1.00 29.63  ?  241  ARG D O   1 
ATOM   7880  C CB  . ARG D  1  241 ? 1.656   24.776  26.798  1.00 29.50  ?  241  ARG D CB  1 
ATOM   7881  C CG  . ARG D  1  241 ? 1.852   26.122  27.471  1.00 30.69  ?  241  ARG D CG  1 
ATOM   7882  C CD  . ARG D  1  241 ? 1.073   27.210  26.748  1.00 32.40  ?  241  ARG D CD  1 
ATOM   7883  N NE  . ARG D  1  241 ? 0.996   26.969  25.312  1.00 31.28  ?  241  ARG D NE  1 
ATOM   7884  C CZ  . ARG D  1  241 ? -0.041  27.298  24.552  1.00 32.49  ?  241  ARG D CZ  1 
ATOM   7885  N NH1 . ARG D  1  241 ? -1.117  27.874  25.062  1.00 33.01  ?  241  ARG D NH1 1 
ATOM   7886  N NH2 . ARG D  1  241 ? 0.003   27.040  23.249  1.00 31.98  ?  241  ARG D NH2 1 
ATOM   7887  N N   . GLU D  1  242 ? 2.005   21.632  27.097  1.00 23.44  ?  242  GLU D N   1 
ATOM   7888  C CA  . GLU D  1  242 ? 2.129   20.327  26.463  1.00 22.68  ?  242  GLU D CA  1 
ATOM   7889  C C   . GLU D  1  242 ? 2.558   19.302  27.501  1.00 22.47  ?  242  GLU D C   1 
ATOM   7890  O O   . GLU D  1  242 ? 3.576   19.484  28.176  1.00 22.29  ?  242  GLU D O   1 
ATOM   7891  C CB  . GLU D  1  242 ? 3.129   20.359  25.302  1.00 21.85  ?  242  GLU D CB  1 
ATOM   7892  C CG  . GLU D  1  242 ? 3.051   21.611  24.445  1.00 22.08  ?  242  GLU D CG  1 
ATOM   7893  C CD  . GLU D  1  242 ? 3.564   21.387  23.039  1.00 21.38  ?  242  GLU D CD  1 
ATOM   7894  O OE1 . GLU D  1  242 ? 4.659   20.805  22.889  1.00 20.70  ?  242  GLU D OE1 1 
ATOM   7895  O OE2 . GLU D  1  242 ? 2.870   21.790  22.082  1.00 21.58  -1 242  GLU D OE2 1 
ATOM   7896  N N   . LEU D  1  243 ? 1.778   18.230  27.623  1.00 19.36  ?  243  LEU D N   1 
ATOM   7897  C CA  . LEU D  1  243 ? 2.046   17.143  28.559  1.00 19.24  ?  243  LEU D CA  1 
ATOM   7898  C C   . LEU D  1  243 ? 2.136   15.847  27.763  1.00 18.56  ?  243  LEU D C   1 
ATOM   7899  O O   . LEU D  1  243 ? 1.140   15.398  27.186  1.00 18.72  ?  243  LEU D O   1 
ATOM   7900  C CB  . LEU D  1  243 ? 0.959   17.059  29.628  1.00 20.16  ?  243  LEU D CB  1 
ATOM   7901  C CG  . LEU D  1  243 ? 1.155   15.975  30.689  1.00 20.17  ?  243  LEU D CG  1 
ATOM   7902  C CD1 . LEU D  1  243 ? 2.521   16.113  31.344  1.00 19.78  ?  243  LEU D CD1 1 
ATOM   7903  C CD2 . LEU D  1  243 ? 0.049   16.035  31.729  1.00 21.23  ?  243  LEU D CD2 1 
ATOM   7904  N N   . CYS D  1  244 ? 3.327   15.255  27.722  1.00 18.92  ?  244  CYS D N   1 
ATOM   7905  C CA  . CYS D  1  244 ? 3.595   14.052  26.936  1.00 18.30  ?  244  CYS D CA  1 
ATOM   7906  C C   . CYS D  1  244 ? 4.129   12.959  27.860  1.00 18.16  ?  244  CYS D C   1 
ATOM   7907  O O   . CYS D  1  244 ? 5.339   12.833  28.058  1.00 17.76  ?  244  CYS D O   1 
ATOM   7908  C CB  . CYS D  1  244 ? 4.572   14.356  25.804  1.00 17.66  ?  244  CYS D CB  1 
ATOM   7909  S SG  . CYS D  1  244 ? 3.953   15.548  24.596  1.00 17.82  ?  244  CYS D SG  1 
ATOM   7910  N N   . LEU D  1  245 ? 3.216   12.166  28.426  1.00 18.18  ?  245  LEU D N   1 
ATOM   7911  C CA  . LEU D  1  245 ? 3.566   11.038  29.282  1.00 18.13  ?  245  LEU D CA  1 
ATOM   7912  C C   . LEU D  1  245 ? 3.380   9.699   28.575  1.00 17.78  ?  245  LEU D C   1 
ATOM   7913  O O   . LEU D  1  245 ? 3.252   8.663   29.236  1.00 17.91  ?  245  LEU D O   1 
ATOM   7914  C CB  . LEU D  1  245 ? 2.742   11.077  30.569  1.00 18.93  ?  245  LEU D CB  1 
ATOM   7915  C CG  . LEU D  1  245 ? 2.820   12.382  31.360  1.00 19.44  ?  245  LEU D CG  1 
ATOM   7916  C CD1 . LEU D  1  245 ? 2.065   12.261  32.671  1.00 20.30  ?  245  LEU D CD1 1 
ATOM   7917  C CD2 . LEU D  1  245 ? 4.272   12.764  31.612  1.00 18.98  ?  245  LEU D CD2 1 
ATOM   7918  N N   . ASP D  1  246 ? 3.368   9.702   27.246  1.00 19.32  ?  246  ASP D N   1 
ATOM   7919  C CA  . ASP D  1  246 ? 3.087   8.499   26.479  1.00 19.06  ?  246  ASP D CA  1 
ATOM   7920  C C   . ASP D  1  246 ? 4.220   7.483   26.610  1.00 18.62  ?  246  ASP D C   1 
ATOM   7921  O O   . ASP D  1  246 ? 5.329   7.799   27.043  1.00 18.43  ?  246  ASP D O   1 
ATOM   7922  C CB  . ASP D  1  246 ? 2.871   8.845   25.008  1.00 18.78  ?  246  ASP D CB  1 
ATOM   7923  C CG  . ASP D  1  246 ? 3.973   9.722   24.450  1.00 18.37  ?  246  ASP D CG  1 
ATOM   7924  O OD1 . ASP D  1  246 ? 4.089   10.885  24.889  1.00 18.59  ?  246  ASP D OD1 1 
ATOM   7925  O OD2 . ASP D  1  246 ? 4.734   9.244   23.584  1.00 17.90  -1 246  ASP D OD2 1 
ATOM   7926  N N   . ARG D  1  247 ? 3.914   6.237   26.242  1.00 19.73  ?  247  ARG D N   1 
ATOM   7927  C CA  . ARG D  1  247 ? 4.905   5.162   26.159  1.00 19.38  ?  247  ARG D CA  1 
ATOM   7928  C C   . ARG D  1  247 ? 5.622   4.962   27.496  1.00 19.51  ?  247  ARG D C   1 
ATOM   7929  O O   . ARG D  1  247 ? 6.839   5.122   27.618  1.00 19.26  ?  247  ARG D O   1 
ATOM   7930  C CB  . ARG D  1  247 ? 5.904   5.428   25.030  1.00 18.89  ?  247  ARG D CB  1 
ATOM   7931  C CG  . ARG D  1  247 ? 5.341   5.197   23.642  1.00 18.73  ?  247  ARG D CG  1 
ATOM   7932  C CD  . ARG D  1  247 ? 6.293   5.720   22.585  1.00 18.35  ?  247  ARG D CD  1 
ATOM   7933  N NE  . ARG D  1  247 ? 6.137   7.154   22.376  1.00 18.39  ?  247  ARG D NE  1 
ATOM   7934  C CZ  . ARG D  1  247 ? 6.752   7.841   21.424  1.00 18.14  ?  247  ARG D CZ  1 
ATOM   7935  N NH1 . ARG D  1  247 ? 7.601   7.262   20.592  1.00 17.86  ?  247  ARG D NH1 1 
ATOM   7936  N NH2 . ARG D  1  247 ? 6.513   9.144   21.306  1.00 18.24  ?  247  ARG D NH2 1 
ATOM   7937  N N   . ASN D  1  248 ? 4.834   4.608   28.507  1.00 23.72  ?  248  ASN D N   1 
ATOM   7938  C CA  . ASN D  1  248 ? 5.341   4.375   29.851  1.00 23.68  ?  248  ASN D CA  1 
ATOM   7939  C C   . ASN D  1  248 ? 4.528   3.238   30.460  1.00 24.28  ?  248  ASN D C   1 
ATOM   7940  O O   . ASN D  1  248 ? 3.767   2.556   29.767  1.00 24.47  ?  248  ASN D O   1 
ATOM   7941  C CB  . ASN D  1  248 ? 5.278   5.669   30.673  1.00 24.07  ?  248  ASN D CB  1 
ATOM   7942  C CG  . ASN D  1  248 ? 6.572   6.454   30.618  1.00 23.66  ?  248  ASN D CG  1 
ATOM   7943  O OD1 . ASN D  1  248 ? 7.517   6.155   31.343  1.00 23.61  ?  248  ASN D OD1 1 
ATOM   7944  N ND2 . ASN D  1  248 ? 6.629   7.449   29.740  1.00 23.45  ?  248  ASN D ND2 1 
ATOM   7945  N N   . ASN D  1  249 ? 4.691   3.020   31.761  1.00 35.63  ?  249  ASN D N   1 
ATOM   7946  C CA  . ASN D  1  249 ? 3.951   1.983   32.469  1.00 35.95  ?  249  ASN D CA  1 
ATOM   7947  C C   . ASN D  1  249 ? 3.057   2.590   33.543  1.00 36.67  ?  249  ASN D C   1 
ATOM   7948  O O   . ASN D  1  249 ? 2.927   2.061   34.648  1.00 37.53  ?  249  ASN D O   1 
ATOM   7949  C CB  . ASN D  1  249 ? 4.899   0.944   33.063  1.00 36.17  ?  249  ASN D CB  1 
ATOM   7950  C CG  . ASN D  1  249 ? 5.021   -0.279  32.184  1.00 36.14  ?  249  ASN D CG  1 
ATOM   7951  O OD1 . ASN D  1  249 ? 4.209   -1.202  32.266  1.00 36.67  ?  249  ASN D OD1 1 
ATOM   7952  N ND2 . ASN D  1  249 ? 6.039   -0.288  31.330  1.00 35.53  ?  249  ASN D ND2 1 
ATOM   7953  N N   . LEU D  1  250 ? 2.418   3.710   33.215  1.00 28.55  ?  250  LEU D N   1 
ATOM   7954  C CA  . LEU D  1  250 ? 1.552   4.398   34.161  1.00 29.45  ?  250  LEU D CA  1 
ATOM   7955  C C   . LEU D  1  250 ? 0.219   3.670   34.277  1.00 30.17  ?  250  LEU D C   1 
ATOM   7956  O O   . LEU D  1  250 ? -0.438  3.393   33.269  1.00 30.04  ?  250  LEU D O   1 
ATOM   7957  C CB  . LEU D  1  250 ? 1.328   5.846   33.727  1.00 29.40  ?  250  LEU D CB  1 
ATOM   7958  C CG  . LEU D  1  250 ? 2.574   6.732   33.670  1.00 28.91  ?  250  LEU D CG  1 
ATOM   7959  C CD1 . LEU D  1  250 ? 2.255   8.063   33.007  1.00 28.94  ?  250  LEU D CD1 1 
ATOM   7960  C CD2 . LEU D  1  250 ? 3.145   6.943   35.064  1.00 29.27  ?  250  LEU D CD2 1 
ATOM   7961  N N   . THR D  1  251 ? -0.170  3.357   35.507  1.00 30.95  ?  251  THR D N   1 
ATOM   7962  C CA  . THR D  1  251 ? -1.413  2.664   35.803  1.00 31.72  ?  251  THR D CA  1 
ATOM   7963  C C   . THR D  1  251 ? -2.396  3.627   36.463  1.00 32.73  ?  251  THR D C   1 
ATOM   7964  O O   . THR D  1  251 ? -2.099  4.803   36.689  1.00 32.73  ?  251  THR D O   1 
ATOM   7965  C CB  . THR D  1  251 ? -1.149  1.453   36.699  1.00 32.29  ?  251  THR D CB  1 
ATOM   7966  O OG1 . THR D  1  251 ? -0.801  1.900   38.015  1.00 33.16  ?  251  THR D OG1 1 
ATOM   7967  C CG2 . THR D  1  251 ? -0.003  0.620   36.141  1.00 30.91  ?  251  THR D CG2 1 
ATOM   7968  N N   . GLY D  1  252 ? -3.583  3.117   36.764  1.00 29.68  ?  252  GLY D N   1 
ATOM   7969  C CA  . GLY D  1  252 ? -4.562  3.888   37.500  1.00 30.85  ?  252  GLY D CA  1 
ATOM   7970  C C   . GLY D  1  252 ? -5.429  4.762   36.619  1.00 31.05  ?  252  GLY D C   1 
ATOM   7971  O O   . GLY D  1  252 ? -5.394  4.717   35.385  1.00 30.32  ?  252  GLY D O   1 
ATOM   7972  N N   . LYS D  1  253 ? -6.232  5.582   37.290  1.00 31.39  ?  253  LYS D N   1 
ATOM   7973  C CA  . LYS D  1  253 ? -7.152  6.484   36.620  1.00 31.83  ?  253  LYS D CA  1 
ATOM   7974  C C   . LYS D  1  253 ? -6.432  7.743   36.145  1.00 31.23  ?  253  LYS D C   1 
ATOM   7975  O O   . LYS D  1  253 ? -5.337  8.080   36.603  1.00 30.76  ?  253  LYS D O   1 
ATOM   7976  C CB  . LYS D  1  253 ? -8.304  6.865   37.552  1.00 33.40  ?  253  LYS D CB  1 
ATOM   7977  C CG  . LYS D  1  253 ? -9.398  5.815   37.646  1.00 34.17  ?  253  LYS D CG  1 
ATOM   7978  C CD  . LYS D  1  253 ? -10.526 6.272   38.556  1.00 35.85  ?  253  LYS D CD  1 
ATOM   7979  C CE  . LYS D  1  253 ? -11.756 6.659   37.750  1.00 36.48  ?  253  LYS D CE  1 
ATOM   7980  N NZ  . LYS D  1  253 ? -12.816 5.614   37.796  1.00 37.28  ?  253  LYS D NZ  1 
ATOM   7981  N N   . ILE D  1  254 ? -7.065  8.437   35.209  1.00 28.80  ?  254  ILE D N   1 
ATOM   7982  C CA  . ILE D  1  254 ? -6.569  9.744   34.777  1.00 28.47  ?  254  ILE D CA  1 
ATOM   7983  C C   . ILE D  1  254 ? -7.056  10.796  35.769  1.00 29.67  ?  254  ILE D C   1 
ATOM   7984  O O   . ILE D  1  254 ? -8.265  10.861  36.045  1.00 30.83  ?  254  ILE D O   1 
ATOM   7985  C CB  . ILE D  1  254 ? -7.045  10.060  33.362  1.00 28.12  ?  254  ILE D CB  1 
ATOM   7986  C CG1 . ILE D  1  254 ? -6.394  9.113   32.352  1.00 26.91  ?  254  ILE D CG1 1 
ATOM   7987  C CG2 . ILE D  1  254 ? -6.740  11.509  33.005  1.00 28.06  ?  254  ILE D CG2 1 
ATOM   7988  C CD1 . ILE D  1  254 ? -6.909  9.283   30.939  1.00 26.61  ?  254  ILE D CD1 1 
ATOM   7989  N N   . PRO D  1  255 ? -6.164  11.608  36.334  1.00 30.47  ?  255  PRO D N   1 
ATOM   7990  C CA  . PRO D  1  255 ? -6.576  12.553  37.380  1.00 31.70  ?  255  PRO D CA  1 
ATOM   7991  C C   . PRO D  1  255 ? -7.671  13.497  36.904  1.00 32.57  ?  255  PRO D C   1 
ATOM   7992  O O   . PRO D  1  255 ? -7.542  14.160  35.871  1.00 32.03  ?  255  PRO D O   1 
ATOM   7993  C CB  . PRO D  1  255 ? -5.282  13.307  37.706  1.00 31.11  ?  255  PRO D CB  1 
ATOM   7994  C CG  . PRO D  1  255 ? -4.186  12.389  37.270  1.00 29.76  ?  255  PRO D CG  1 
ATOM   7995  C CD  . PRO D  1  255 ? -4.717  11.671  36.069  1.00 29.25  ?  255  PRO D CD  1 
ATOM   7996  N N   . SER D  1  256 ? -8.760  13.552  37.675  1.00 34.95  ?  256  SER D N   1 
ATOM   7997  C CA  . SER D  1  256 ? -9.803  14.544  37.438  1.00 36.04  ?  256  SER D CA  1 
ATOM   7998  C C   . SER D  1  256 ? -9.275  15.963  37.586  1.00 36.17  ?  256  SER D C   1 
ATOM   7999  O O   . SER D  1  256 ? -9.908  16.907  37.098  1.00 36.78  ?  256  SER D O   1 
ATOM   8000  C CB  . SER D  1  256 ? -10.972 14.318  38.396  1.00 37.71  ?  256  SER D CB  1 
ATOM   8001  O OG  . SER D  1  256 ? -10.525 14.242  39.738  1.00 38.23  ?  256  SER D OG  1 
ATOM   8002  N N   . SER D  1  257 ? -8.130  16.129  38.254  1.00 37.05  ?  257  SER D N   1 
ATOM   8003  C CA  . SER D  1  257 ? -7.489  17.432  38.373  1.00 37.07  ?  257  SER D CA  1 
ATOM   8004  C C   . SER D  1  257 ? -7.102  18.009  37.019  1.00 36.07  ?  257  SER D C   1 
ATOM   8005  O O   . SER D  1  257 ? -6.870  19.218  36.917  1.00 36.31  ?  257  SER D O   1 
ATOM   8006  C CB  . SER D  1  257 ? -6.250  17.321  39.263  1.00 36.58  ?  257  SER D CB  1 
ATOM   8007  O OG  . SER D  1  257 ? -6.552  16.670  40.484  1.00 38.57  ?  257  SER D OG  1 
ATOM   8008  N N   . PHE D  1  258 ? -7.025  17.171  35.980  1.00 33.91  ?  258  PHE D N   1 
ATOM   8009  C CA  . PHE D  1  258 ? -6.647  17.644  34.654  1.00 32.99  ?  258  PHE D CA  1 
ATOM   8010  C C   . PHE D  1  258 ? -7.638  18.653  34.092  1.00 33.88  ?  258  PHE D C   1 
ATOM   8011  O O   . PHE D  1  258 ? -7.291  19.389  33.162  1.00 33.37  ?  258  PHE D O   1 
ATOM   8012  C CB  . PHE D  1  258 ? -6.512  16.463  33.691  1.00 31.91  ?  258  PHE D CB  1 
ATOM   8013  C CG  . PHE D  1  258 ? -5.155  15.822  33.706  1.00 30.66  ?  258  PHE D CG  1 
ATOM   8014  C CD1 . PHE D  1  258 ? -4.391  15.809  34.861  1.00 30.73  ?  258  PHE D CD1 1 
ATOM   8015  C CD2 . PHE D  1  258 ? -4.639  15.238  32.561  1.00 29.51  ?  258  PHE D CD2 1 
ATOM   8016  C CE1 . PHE D  1  258 ? -3.141  15.221  34.875  1.00 29.67  ?  258  PHE D CE1 1 
ATOM   8017  C CE2 . PHE D  1  258 ? -3.390  14.650  32.569  1.00 28.47  ?  258  PHE D CE2 1 
ATOM   8018  C CZ  . PHE D  1  258 ? -2.640  14.641  33.727  1.00 28.55  ?  258  PHE D CZ  1 
ATOM   8019  N N   . GLY D  1  259 ? -8.859  18.705  34.627  1.00 36.02  ?  259  GLY D N   1 
ATOM   8020  C CA  . GLY D  1  259 ? -9.807  19.721  34.210  1.00 37.05  ?  259  GLY D CA  1 
ATOM   8021  C C   . GLY D  1  259 ? -9.318  21.137  34.431  1.00 37.39  ?  259  GLY D C   1 
ATOM   8022  O O   . GLY D  1  259 ? -9.763  22.055  33.733  1.00 37.82  ?  259  GLY D O   1 
ATOM   8023  N N   . ASN D  1  260 ? -8.405  21.335  35.382  1.00 35.69  ?  260  ASN D N   1 
ATOM   8024  C CA  . ASN D  1  260 ? -7.840  22.651  35.646  1.00 36.00  ?  260  ASN D CA  1 
ATOM   8025  C C   . ASN D  1  260 ? -6.795  23.067  34.620  1.00 34.68  ?  260  ASN D C   1 
ATOM   8026  O O   . ASN D  1  260 ? -6.423  24.245  34.583  1.00 34.95  ?  260  ASN D O   1 
ATOM   8027  C CB  . ASN D  1  260 ? -7.219  22.683  37.045  1.00 36.36  ?  260  ASN D CB  1 
ATOM   8028  C CG  . ASN D  1  260 ? -8.181  22.220  38.122  1.00 37.71  ?  260  ASN D CG  1 
ATOM   8029  O OD1 . ASN D  1  260 ? -9.373  22.527  38.082  1.00 38.94  ?  260  ASN D OD1 1 
ATOM   8030  N ND2 . ASN D  1  260 ? -7.665  21.477  39.094  1.00 37.56  ?  260  ASN D ND2 1 
ATOM   8031  N N   . LEU D  1  261 ? -6.319  22.140  33.787  1.00 34.22  ?  261  LEU D N   1 
ATOM   8032  C CA  . LEU D  1  261 ? -5.292  22.437  32.788  1.00 33.00  ?  261  LEU D CA  1 
ATOM   8033  C C   . LEU D  1  261 ? -5.932  23.177  31.613  1.00 33.24  ?  261  LEU D C   1 
ATOM   8034  O O   . LEU D  1  261 ? -6.143  22.640  30.523  1.00 32.59  ?  261  LEU D O   1 
ATOM   8035  C CB  . LEU D  1  261 ? -4.603  21.157  32.339  1.00 31.65  ?  261  LEU D CB  1 
ATOM   8036  C CG  . LEU D  1  261 ? -3.779  20.431  33.401  1.00 31.29  ?  261  LEU D CG  1 
ATOM   8037  C CD1 . LEU D  1  261 ? -3.488  19.002  32.973  1.00 30.29  ?  261  LEU D CD1 1 
ATOM   8038  C CD2 . LEU D  1  261 ? -2.490  21.187  33.676  1.00 30.84  ?  261  LEU D CD2 1 
ATOM   8039  N N   . LYS D  1  262 ? -6.235  24.452  31.856  1.00 33.09  ?  262  LYS D N   1 
ATOM   8040  C CA  . LYS D  1  262 ? -6.942  25.270  30.880  1.00 33.59  ?  262  LYS D CA  1 
ATOM   8041  C C   . LYS D  1  262 ? -6.022  25.867  29.823  1.00 32.65  ?  262  LYS D C   1 
ATOM   8042  O O   . LYS D  1  262 ? -6.519  26.451  28.854  1.00 32.92  ?  262  LYS D O   1 
ATOM   8043  C CB  . LYS D  1  262 ? -7.705  26.389  31.594  1.00 35.24  ?  262  LYS D CB  1 
ATOM   8044  C CG  . LYS D  1  262 ? -8.596  25.902  32.730  1.00 36.37  ?  262  LYS D CG  1 
ATOM   8045  C CD  . LYS D  1  262 ? -9.882  25.269  32.221  1.00 36.89  ?  262  LYS D CD  1 
ATOM   8046  C CE  . LYS D  1  262 ? -10.662 26.214  31.324  1.00 37.66  ?  262  LYS D CE  1 
ATOM   8047  N NZ  . LYS D  1  262 ? -12.133 26.017  31.464  1.00 39.04  ?  262  LYS D NZ  1 
ATOM   8048  N N   . ASN D  1  263 ? -4.704  25.749  29.987  1.00 39.68  ?  263  ASN D N   1 
ATOM   8049  C CA  . ASN D  1  263 ? -3.750  26.235  29.001  1.00 38.78  ?  263  ASN D CA  1 
ATOM   8050  C C   . ASN D  1  263 ? -3.110  25.123  28.181  1.00 37.66  ?  263  ASN D C   1 
ATOM   8051  O O   . ASN D  1  263 ? -2.354  25.422  27.250  1.00 36.73  ?  263  ASN D O   1 
ATOM   8052  C CB  . ASN D  1  263 ? -2.643  27.054  29.687  1.00 38.75  ?  263  ASN D CB  1 
ATOM   8053  C CG  . ASN D  1  263 ? -3.006  28.520  29.840  1.00 40.22  ?  263  ASN D CG  1 
ATOM   8054  O OD1 . ASN D  1  263 ? -3.755  29.075  29.034  1.00 41.34  ?  263  ASN D OD1 1 
ATOM   8055  N ND2 . ASN D  1  263 ? -2.474  29.156  30.880  1.00 41.10  ?  263  ASN D ND2 1 
ATOM   8056  N N   . VAL D  1  264 ? -3.393  23.861  28.492  1.00 29.95  ?  264  VAL D N   1 
ATOM   8057  C CA  . VAL D  1  264 ? -2.742  22.737  27.827  1.00 28.70  ?  264  VAL D CA  1 
ATOM   8058  C C   . VAL D  1  264 ? -3.350  22.545  26.445  1.00 28.47  ?  264  VAL D C   1 
ATOM   8059  O O   . VAL D  1  264 ? -4.575  22.460  26.296  1.00 29.21  ?  264  VAL D O   1 
ATOM   8060  C CB  . VAL D  1  264 ? -2.872  21.457  28.670  1.00 28.58  ?  264  VAL D CB  1 
ATOM   8061  C CG1 . VAL D  1  264 ? -2.568  20.229  27.826  1.00 27.54  ?  264  VAL D CG1 1 
ATOM   8062  C CG2 . VAL D  1  264 ? -1.950  21.518  29.876  1.00 28.52  ?  264  VAL D CG2 1 
ATOM   8063  N N   . THR D  1  265 ? -2.491  22.472  25.425  1.00 25.71  ?  265  THR D N   1 
ATOM   8064  C CA  . THR D  1  265 ? -2.935  22.266  24.055  1.00 25.43  ?  265  THR D CA  1 
ATOM   8065  C C   . THR D  1  265 ? -2.603  20.888  23.500  1.00 24.47  ?  265  THR D C   1 
ATOM   8066  O O   . THR D  1  265 ? -3.197  20.490  22.493  1.00 24.36  ?  265  THR D O   1 
ATOM   8067  C CB  . THR D  1  265 ? -2.329  23.333  23.130  1.00 25.22  ?  265  THR D CB  1 
ATOM   8068  O OG1 . THR D  1  265 ? -0.899  23.275  23.201  1.00 24.37  ?  265  THR D OG1 1 
ATOM   8069  C CG2 . THR D  1  265 ? -2.794  24.721  23.544  1.00 26.30  ?  265  THR D CG2 1 
ATOM   8070  N N   . LEU D  1  266 ? -1.681  20.155  24.121  1.00 22.08  ?  266  LEU D N   1 
ATOM   8071  C CA  . LEU D  1  266 ? -1.307  18.818  23.679  1.00 21.26  ?  266  LEU D CA  1 
ATOM   8072  C C   . LEU D  1  266 ? -1.226  17.892  24.882  1.00 21.29  ?  266  LEU D C   1 
ATOM   8073  O O   . LEU D  1  266 ? -0.504  18.180  25.842  1.00 21.30  ?  266  LEU D O   1 
ATOM   8074  C CB  . LEU D  1  266 ? 0.032   18.830  22.936  1.00 20.33  ?  266  LEU D CB  1 
ATOM   8075  C CG  . LEU D  1  266 ? 0.688   17.458  22.767  1.00 19.55  ?  266  LEU D CG  1 
ATOM   8076  C CD1 . LEU D  1  266 ? -0.121  16.597  21.810  1.00 19.43  ?  266  LEU D CD1 1 
ATOM   8077  C CD2 . LEU D  1  266 ? 2.125   17.596  22.290  1.00 18.81  ?  266  LEU D CD2 1 
ATOM   8078  N N   . LEU D  1  267 ? -1.958  16.780  24.827  1.00 20.09  ?  267  LEU D N   1 
ATOM   8079  C CA  . LEU D  1  267 ? -1.949  15.774  25.888  1.00 20.14  ?  267  LEU D CA  1 
ATOM   8080  C C   . LEU D  1  267 ? -1.744  14.403  25.251  1.00 19.44  ?  267  LEU D C   1 
ATOM   8081  O O   . LEU D  1  267 ? -2.700  13.779  24.779  1.00 19.65  ?  267  LEU D O   1 
ATOM   8082  C CB  . LEU D  1  267 ? -3.237  15.817  26.704  1.00 21.20  ?  267  LEU D CB  1 
ATOM   8083  C CG  . LEU D  1  267 ? -3.297  14.845  27.886  1.00 21.41  ?  267  LEU D CG  1 
ATOM   8084  C CD1 . LEU D  1  267 ? -2.056  14.975  28.757  1.00 21.04  ?  267  LEU D CD1 1 
ATOM   8085  C CD2 . LEU D  1  267 ? -4.554  15.066  28.704  1.00 22.61  ?  267  LEU D CD2 1 
ATOM   8086  N N   . ASN D  1  268 ? -0.496  13.939  25.240  1.00 20.20  ?  268  ASN D N   1 
ATOM   8087  C CA  . ASN D  1  268 ? -0.139  12.609  24.759  1.00 19.59  ?  268  ASN D CA  1 
ATOM   8088  C C   . ASN D  1  268 ? 0.164   11.726  25.963  1.00 19.64  ?  268  ASN D C   1 
ATOM   8089  O O   . ASN D  1  268 ? 1.144   11.958  26.679  1.00 19.46  ?  268  ASN D O   1 
ATOM   8090  C CB  . ASN D  1  268 ? 1.054   12.666  23.808  1.00 18.80  ?  268  ASN D CB  1 
ATOM   8091  C CG  . ASN D  1  268 ? 0.686   13.203  22.440  1.00 18.70  ?  268  ASN D CG  1 
ATOM   8092  O OD1 . ASN D  1  268 ? -0.484  13.215  22.058  1.00 19.13  ?  268  ASN D OD1 1 
ATOM   8093  N ND2 . ASN D  1  268 ? 1.688   13.648  21.690  1.00 18.20  ?  268  ASN D ND2 1 
ATOM   8094  N N   . MET D  1  269 ? -0.684  10.723  26.190  1.00 20.41  ?  269  MET D N   1 
ATOM   8095  C CA  . MET D  1  269 ? -0.470  9.724   27.231  1.00 20.48  ?  269  MET D CA  1 
ATOM   8096  C C   . MET D  1  269 ? -0.744  8.325   26.697  1.00 20.22  ?  269  MET D C   1 
ATOM   8097  O O   . MET D  1  269 ? -1.116  7.423   27.454  1.00 20.53  ?  269  MET D O   1 
ATOM   8098  C CB  . MET D  1  269 ? -1.333  10.007  28.461  1.00 21.39  ?  269  MET D CB  1 
ATOM   8099  C CG  . MET D  1  269 ? -1.178  11.407  29.022  1.00 21.79  ?  269  MET D CG  1 
ATOM   8100  S SD  . MET D  1  269 ? -1.709  11.526  30.738  1.00 22.80  ?  269  MET D SD  1 
ATOM   8101  C CE  . MET D  1  269 ? -3.443  11.110  30.592  1.00 23.68  ?  269  MET D CE  1 
ATOM   8102  N N   . PHE D  1  270 ? -0.567  8.134   25.393  1.00 20.67  ?  270  PHE D N   1 
ATOM   8103  C CA  . PHE D  1  270 ? -0.867  6.861   24.764  1.00 20.47  ?  270  PHE D CA  1 
ATOM   8104  C C   . PHE D  1  270 ? 0.178   5.813   25.142  1.00 20.03  ?  270  PHE D C   1 
ATOM   8105  O O   . PHE D  1  270 ? 1.256   6.122   25.656  1.00 19.77  ?  270  PHE D O   1 
ATOM   8106  C CB  . PHE D  1  270 ? -0.938  7.019   23.246  1.00 20.10  ?  270  PHE D CB  1 
ATOM   8107  C CG  . PHE D  1  270 ? 0.270   7.679   22.640  1.00 19.53  ?  270  PHE D CG  1 
ATOM   8108  C CD1 . PHE D  1  270 ? 1.370   6.927   22.258  1.00 18.96  ?  270  PHE D CD1 1 
ATOM   8109  C CD2 . PHE D  1  270 ? 0.301   9.048   22.438  1.00 19.63  ?  270  PHE D CD2 1 
ATOM   8110  C CE1 . PHE D  1  270 ? 2.480   7.528   21.695  1.00 18.52  ?  270  PHE D CE1 1 
ATOM   8111  C CE2 . PHE D  1  270 ? 1.406   9.654   21.875  1.00 19.15  ?  270  PHE D CE2 1 
ATOM   8112  C CZ  . PHE D  1  270 ? 2.496   8.894   21.502  1.00 18.60  ?  270  PHE D CZ  1 
ATOM   8113  N N   . GLU D  1  271 ? -0.161  4.550   24.880  1.00 22.91  ?  271  GLU D N   1 
ATOM   8114  C CA  . GLU D  1  271 ? 0.714   3.411   25.159  1.00 22.58  ?  271  GLU D CA  1 
ATOM   8115  C C   . GLU D  1  271 ? 1.104   3.366   26.639  1.00 22.84  ?  271  GLU D C   1 
ATOM   8116  O O   . GLU D  1  271 ? 2.276   3.453   27.012  1.00 22.52  ?  271  GLU D O   1 
ATOM   8117  C CB  . GLU D  1  271 ? 1.952   3.441   24.256  1.00 21.93  ?  271  GLU D CB  1 
ATOM   8118  C CG  . GLU D  1  271 ? 1.631   3.512   22.773  1.00 21.87  ?  271  GLU D CG  1 
ATOM   8119  C CD  . GLU D  1  271 ? 2.650   2.784   21.922  1.00 21.56  ?  271  GLU D CD  1 
ATOM   8120  O OE1 . GLU D  1  271 ? 3.438   1.994   22.482  1.00 22.13  ?  271  GLU D OE1 1 
ATOM   8121  O OE2 . GLU D  1  271 ? 2.665   3.005   20.693  1.00 21.24  -1 271  GLU D OE2 1 
ATOM   8122  N N   . ASN D  1  272 ? 0.083   3.228   27.481  1.00 23.90  ?  272  ASN D N   1 
ATOM   8123  C CA  . ASN D  1  272 ? 0.257   3.128   28.925  1.00 24.28  ?  272  ASN D CA  1 
ATOM   8124  C C   . ASN D  1  272 ? -0.700  2.058   29.439  1.00 24.82  ?  272  ASN D C   1 
ATOM   8125  O O   . ASN D  1  272 ? -1.379  1.378   28.661  1.00 25.19  ?  272  ASN D O   1 
ATOM   8126  C CB  . ASN D  1  272 ? 0.027   4.487   29.599  1.00 24.71  ?  272  ASN D CB  1 
ATOM   8127  C CG  . ASN D  1  272 ? 1.300   5.300   29.723  1.00 24.35  ?  272  ASN D CG  1 
ATOM   8128  O OD1 . ASN D  1  272 ? 2.087   5.098   30.647  1.00 24.24  ?  272  ASN D OD1 1 
ATOM   8129  N ND2 . ASN D  1  272 ? 1.506   6.229   28.796  1.00 23.94  ?  272  ASN D ND2 1 
ATOM   8130  N N   . GLN D  1  273 ? -0.750  1.899   30.762  1.00 29.30  ?  273  GLN D N   1 
ATOM   8131  C CA  . GLN D  1  273 ? -1.673  0.976   31.411  1.00 30.05  ?  273  GLN D CA  1 
ATOM   8132  C C   . GLN D  1  273 ? -2.750  1.712   32.204  1.00 30.96  ?  273  GLN D C   1 
ATOM   8133  O O   . GLN D  1  273 ? -3.273  1.181   33.187  1.00 31.93  ?  273  GLN D O   1 
ATOM   8134  C CB  . GLN D  1  273 ? -0.923  0.004   32.320  1.00 30.51  ?  273  GLN D CB  1 
ATOM   8135  C CG  . GLN D  1  273 ? 0.086   -0.874  31.605  1.00 29.15  ?  273  GLN D CG  1 
ATOM   8136  C CD  . GLN D  1  273 ? 0.374   -2.158  32.362  1.00 30.40  ?  273  GLN D CD  1 
ATOM   8137  O OE1 . GLN D  1  273 ? -0.505  -3.005  32.528  1.00 31.05  ?  273  GLN D OE1 1 
ATOM   8138  N NE2 . GLN D  1  273 ? 1.608   -2.307  32.826  1.00 29.86  ?  273  GLN D NE2 1 
ATOM   8139  N N   . LEU D  1  274 ? -3.075  2.939   31.799  1.00 25.69  ?  274  LEU D N   1 
ATOM   8140  C CA  . LEU D  1  274 ? -4.123  3.697   32.468  1.00 26.68  ?  274  LEU D CA  1 
ATOM   8141  C C   . LEU D  1  274 ? -5.449  2.949   32.398  1.00 27.40  ?  274  LEU D C   1 
ATOM   8142  O O   . LEU D  1  274 ? -5.756  2.273   31.413  1.00 27.07  ?  274  LEU D O   1 
ATOM   8143  C CB  . LEU D  1  274 ? -4.262  5.086   31.844  1.00 26.64  ?  274  LEU D CB  1 
ATOM   8144  C CG  . LEU D  1  274 ? -3.008  5.962   31.848  1.00 26.00  ?  274  LEU D CG  1 
ATOM   8145  C CD1 . LEU D  1  274 ? -3.119  7.071   30.811  1.00 25.77  ?  274  LEU D CD1 1 
ATOM   8146  C CD2 . LEU D  1  274 ? -2.768  6.540   33.234  1.00 26.58  ?  274  LEU D CD2 1 
ATOM   8147  N N   . SER D  1  275 ? -6.242  3.078   33.459  1.00 28.21  ?  275  SER D N   1 
ATOM   8148  C CA  . SER D  1  275 ? -7.454  2.287   33.620  1.00 29.06  ?  275  SER D CA  1 
ATOM   8149  C C   . SER D  1  275 ? -8.572  3.200   34.110  1.00 30.26  ?  275  SER D C   1 
ATOM   8150  O O   . SER D  1  275 ? -8.431  4.427   34.149  1.00 30.35  ?  275  SER D O   1 
ATOM   8151  C CB  . SER D  1  275 ? -7.213  1.115   34.580  1.00 29.29  ?  275  SER D CB  1 
ATOM   8152  O OG  . SER D  1  275 ? -6.956  1.585   35.893  1.00 29.89  ?  275  SER D OG  1 
ATOM   8153  N N   . GLY D  1  276 ? -9.692  2.590   34.488  1.00 32.10  ?  276  GLY D N   1 
ATOM   8154  C CA  . GLY D  1  276 ? -10.857 3.344   34.893  1.00 33.39  ?  276  GLY D CA  1 
ATOM   8155  C C   . GLY D  1  276 ? -11.540 3.994   33.700  1.00 33.35  ?  276  GLY D C   1 
ATOM   8156  O O   . GLY D  1  276 ? -11.369 3.595   32.545  1.00 32.49  ?  276  GLY D O   1 
ATOM   8157  N N   . GLU D  1  277 ? -12.325 5.022   33.999  1.00 34.40  ?  277  GLU D N   1 
ATOM   8158  C CA  . GLU D  1  277 ? -13.075 5.754   32.992  1.00 34.60  ?  277  GLU D CA  1 
ATOM   8159  C C   . GLU D  1  277 ? -12.448 7.122   32.759  1.00 34.19  ?  277  GLU D C   1 
ATOM   8160  O O   . GLU D  1  277 ? -11.794 7.683   33.643  1.00 34.26  ?  277  GLU D O   1 
ATOM   8161  C CB  . GLU D  1  277 ? -14.540 5.912   33.409  1.00 36.23  ?  277  GLU D CB  1 
ATOM   8162  C CG  . GLU D  1  277 ? -15.124 4.673   34.072  1.00 36.95  ?  277  GLU D CG  1 
ATOM   8163  C CD  . GLU D  1  277 ? -16.637 4.628   33.997  1.00 38.38  ?  277  GLU D CD  1 
ATOM   8164  O OE1 . GLU D  1  277 ? -17.269 5.704   34.043  1.00 39.28  ?  277  GLU D OE1 1 
ATOM   8165  O OE2 . GLU D  1  277 ? -17.194 3.515   33.889  1.00 38.66  -1 277  GLU D OE2 1 
ATOM   8166  N N   . ILE D  1  278 ? -12.642 7.648   31.553  1.00 30.54  ?  278  ILE D N   1 
ATOM   8167  C CA  . ILE D  1  278 ? -12.158 8.983   31.215  1.00 30.25  ?  278  ILE D CA  1 
ATOM   8168  C C   . ILE D  1  278 ? -12.946 9.998   32.035  1.00 31.67  ?  278  ILE D C   1 
ATOM   8169  O O   . ILE D  1  278 ? -14.180 10.053  31.934  1.00 32.77  ?  278  ILE D O   1 
ATOM   8170  C CB  . ILE D  1  278 ? -12.280 9.262   29.709  1.00 29.63  ?  278  ILE D CB  1 
ATOM   8171  C CG1 . ILE D  1  278 ? -11.401 8.295   28.918  1.00 28.27  ?  278  ILE D CG1 1 
ATOM   8172  C CG2 . ILE D  1  278 ? -11.891 10.693  29.398  1.00 29.51  ?  278  ILE D CG2 1 
ATOM   8173  C CD1 . ILE D  1  278 ? -11.635 8.331   27.425  1.00 27.76  ?  278  ILE D CD1 1 
ATOM   8174  N N   . PRO D  1  279 ? -12.282 10.806  32.856  1.00 33.34  ?  279  PRO D N   1 
ATOM   8175  C CA  . PRO D  1  279 ? -12.995 11.763  33.709  1.00 34.79  ?  279  PRO D CA  1 
ATOM   8176  C C   . PRO D  1  279 ? -13.743 12.788  32.877  1.00 35.31  ?  279  PRO D C   1 
ATOM   8177  O O   . PRO D  1  279 ? -13.174 13.375  31.943  1.00 34.42  ?  279  PRO D O   1 
ATOM   8178  C CB  . PRO D  1  279 ? -11.871 12.419  34.526  1.00 34.45  ?  279  PRO D CB  1 
ATOM   8179  C CG  . PRO D  1  279 ? -10.620 12.151  33.756  1.00 32.78  ?  279  PRO D CG  1 
ATOM   8180  C CD  . PRO D  1  279 ? -10.826 10.841  33.070  1.00 32.19  ?  279  PRO D CD  1 
ATOM   8181  N N   . PRO D  1  280 ? -15.021 13.031  33.182  1.00 38.63  ?  280  PRO D N   1 
ATOM   8182  C CA  . PRO D  1  280 ? -15.761 14.075  32.455  1.00 39.30  ?  280  PRO D CA  1 
ATOM   8183  C C   . PRO D  1  280 ? -15.131 15.447  32.576  1.00 39.25  ?  280  PRO D C   1 
ATOM   8184  O O   . PRO D  1  280 ? -15.343 16.290  31.695  1.00 39.27  ?  280  PRO D O   1 
ATOM   8185  C CB  . PRO D  1  280 ? -17.153 14.039  33.102  1.00 41.14  ?  280  PRO D CB  1 
ATOM   8186  C CG  . PRO D  1  280 ? -17.257 12.680  33.711  1.00 41.16  ?  280  PRO D CG  1 
ATOM   8187  C CD  . PRO D  1  280 ? -15.870 12.322  34.153  1.00 39.87  ?  280  PRO D CD  1 
ATOM   8188  N N   . GLU D  1  281 ? -14.366 15.701  33.641  1.00 41.49  ?  281  GLU D N   1 
ATOM   8189  C CA  . GLU D  1  281 ? -13.659 16.967  33.795  1.00 41.39  ?  281  GLU D CA  1 
ATOM   8190  C C   . GLU D  1  281 ? -12.676 17.245  32.663  1.00 39.86  ?  281  GLU D C   1 
ATOM   8191  O O   . GLU D  1  281 ? -12.204 18.381  32.550  1.00 39.82  ?  281  GLU D O   1 
ATOM   8192  C CB  . GLU D  1  281 ? -12.917 17.003  35.137  1.00 41.54  ?  281  GLU D CB  1 
ATOM   8193  C CG  . GLU D  1  281 ? -13.773 16.708  36.369  1.00 43.10  ?  281  GLU D CG  1 
ATOM   8194  C CD  . GLU D  1  281 ? -13.964 15.223  36.638  1.00 42.89  ?  281  GLU D CD  1 
ATOM   8195  O OE1 . GLU D  1  281 ? -14.022 14.431  35.674  1.00 41.99  ?  281  GLU D OE1 1 
ATOM   8196  O OE2 . GLU D  1  281 ? -14.067 14.848  37.826  1.00 43.70  -1 281  GLU D OE2 1 
ATOM   8197  N N   . ILE D  1  282 ? -12.350 16.249  31.833  1.00 36.87  ?  282  ILE D N   1 
ATOM   8198  C CA  . ILE D  1  282 ? -11.454 16.491  30.704  1.00 35.53  ?  282  ILE D CA  1 
ATOM   8199  C C   . ILE D  1  282 ? -12.077 17.481  29.728  1.00 35.96  ?  282  ILE D C   1 
ATOM   8200  O O   . ILE D  1  282 ? -11.367 18.282  29.106  1.00 35.33  ?  282  ILE D O   1 
ATOM   8201  C CB  . ILE D  1  282 ? -11.073 15.158  30.025  1.00 34.34  ?  282  ILE D CB  1 
ATOM   8202  C CG1 . ILE D  1  282 ? -9.915  14.505  30.787  1.00 33.53  ?  282  ILE D CG1 1 
ATOM   8203  C CG2 . ILE D  1  282 ? -10.697 15.360  28.561  1.00 33.36  ?  282  ILE D CG2 1 
ATOM   8204  C CD1 . ILE D  1  282 ? -9.527  13.136  30.285  1.00 32.51  ?  282  ILE D CD1 1 
ATOM   8205  N N   . GLY D  1  283 ? -13.405 17.462  29.592  1.00 35.73  ?  283  GLY D N   1 
ATOM   8206  C CA  . GLY D  1  283 ? -14.073 18.439  28.747  1.00 36.34  ?  283  GLY D CA  1 
ATOM   8207  C C   . GLY D  1  283 ? -13.756 19.876  29.117  1.00 36.89  ?  283  GLY D C   1 
ATOM   8208  O O   . GLY D  1  283 ? -13.773 20.760  28.255  1.00 36.88  ?  283  GLY D O   1 
ATOM   8209  N N   . ASN D  1  284 ? -13.463 20.132  30.394  1.00 41.74  ?  284  ASN D N   1 
ATOM   8210  C CA  . ASN D  1  284 ? -13.090 21.471  30.833  1.00 42.27  ?  284  ASN D CA  1 
ATOM   8211  C C   . ASN D  1  284 ? -11.743 21.924  30.276  1.00 40.91  ?  284  ASN D C   1 
ATOM   8212  O O   . ASN D  1  284 ? -11.409 23.106  30.408  1.00 41.27  ?  284  ASN D O   1 
ATOM   8213  C CB  . ASN D  1  284 ? -13.087 21.544  32.364  1.00 43.19  ?  284  ASN D CB  1 
ATOM   8214  C CG  . ASN D  1  284 ? -14.355 22.186  32.924  1.00 45.15  ?  284  ASN D CG  1 
ATOM   8215  O OD1 . ASN D  1  284 ? -14.844 23.182  32.389  1.00 45.87  ?  284  ASN D OD1 1 
ATOM   8216  N ND2 . ASN D  1  284 ? -14.889 21.617  34.005  1.00 46.10  ?  284  ASN D ND2 1 
ATOM   8217  N N   . MET D  1  285 ? -10.968 21.026  29.661  1.00 34.97  ?  285  MET D N   1 
ATOM   8218  C CA  . MET D  1  285 ? -9.699  21.385  29.020  1.00 33.70  ?  285  MET D CA  1 
ATOM   8219  C C   . MET D  1  285 ? -9.988  22.074  27.685  1.00 33.64  ?  285  MET D C   1 
ATOM   8220  O O   . MET D  1  285 ? -9.738  21.548  26.598  1.00 32.68  ?  285  MET D O   1 
ATOM   8221  C CB  . MET D  1  285 ? -8.825  20.155  28.826  1.00 32.31  ?  285  MET D CB  1 
ATOM   8222  C CG  . MET D  1  285 ? -8.336  19.509  30.107  1.00 32.25  ?  285  MET D CG  1 
ATOM   8223  S SD  . MET D  1  285 ? -6.810  18.587  29.839  1.00 30.54  ?  285  MET D SD  1 
ATOM   8224  C CE  . MET D  1  285 ? -7.451  16.920  29.749  1.00 30.36  ?  285  MET D CE  1 
ATOM   8225  N N   . THR D  1  286 ? -10.527 23.290  27.788  1.00 33.13  ?  286  THR D N   1 
ATOM   8226  C CA  . THR D  1  286 ? -11.024 24.035  26.637  1.00 33.43  ?  286  THR D CA  1 
ATOM   8227  C C   . THR D  1  286 ? -9.924  24.502  25.690  1.00 32.30  ?  286  THR D C   1 
ATOM   8228  O O   . THR D  1  286 ? -10.243 25.117  24.666  1.00 32.48  ?  286  THR D O   1 
ATOM   8229  C CB  . THR D  1  286 ? -11.829 25.244  27.110  1.00 35.06  ?  286  THR D CB  1 
ATOM   8230  O OG1 . THR D  1  286 ? -10.982 26.114  27.873  1.00 35.15  ?  286  THR D OG1 1 
ATOM   8231  C CG2 . THR D  1  286 ? -12.994 24.794  27.980  1.00 36.34  ?  286  THR D CG2 1 
ATOM   8232  N N   . ALA D  1  287 ? -8.655  24.231  25.986  1.00 30.16  ?  287  ALA D N   1 
ATOM   8233  C CA  . ALA D  1  287 ? -7.556  24.615  25.113  1.00 29.12  ?  287  ALA D CA  1 
ATOM   8234  C C   . ALA D  1  287 ? -6.947  23.434  24.371  1.00 27.76  ?  287  ALA D C   1 
ATOM   8235  O O   . ALA D  1  287 ? -5.949  23.613  23.666  1.00 26.85  ?  287  ALA D O   1 
ATOM   8236  C CB  . ALA D  1  287 ? -6.464  25.335  25.911  1.00 28.97  ?  287  ALA D CB  1 
ATOM   8237  N N   . LEU D  1  288 ? -7.523  22.241  24.499  1.00 29.24  ?  288  LEU D N   1 
ATOM   8238  C CA  . LEU D  1  288 ? -6.919  21.054  23.911  1.00 28.03  ?  288  LEU D CA  1 
ATOM   8239  C C   . LEU D  1  288 ? -6.984  21.106  22.391  1.00 27.56  ?  288  LEU D C   1 
ATOM   8240  O O   . LEU D  1  288 ? -8.036  21.385  21.808  1.00 28.27  ?  288  LEU D O   1 
ATOM   8241  C CB  . LEU D  1  288 ? -7.615  19.791  24.415  1.00 28.19  ?  288  LEU D CB  1 
ATOM   8242  C CG  . LEU D  1  288 ? -7.001  19.100  25.631  1.00 27.93  ?  288  LEU D CG  1 
ATOM   8243  C CD1 . LEU D  1  288 ? -7.818  17.876  26.006  1.00 28.21  ?  288  LEU D CD1 1 
ATOM   8244  C CD2 . LEU D  1  288 ? -5.557  18.718  25.347  1.00 26.64  ?  288  LEU D CD2 1 
ATOM   8245  N N   . ASP D  1  289 ? -5.844  20.844  21.756  1.00 24.84  ?  289  ASP D N   1 
ATOM   8246  C CA  . ASP D  1  289 ? -5.738  20.709  20.310  1.00 24.28  ?  289  ASP D CA  1 
ATOM   8247  C C   . ASP D  1  289 ? -5.584  19.260  19.873  1.00 23.48  ?  289  ASP D C   1 
ATOM   8248  O O   . ASP D  1  289 ? -6.138  18.865  18.842  1.00 23.41  ?  289  ASP D O   1 
ATOM   8249  C CB  . ASP D  1  289 ? -4.553  21.532  19.793  1.00 23.70  ?  289  ASP D CB  1 
ATOM   8250  C CG  . ASP D  1  289 ? -4.032  21.034  18.463  1.00 22.83  ?  289  ASP D CG  1 
ATOM   8251  O OD1 . ASP D  1  289 ? -4.641  21.362  17.423  1.00 23.09  ?  289  ASP D OD1 1 
ATOM   8252  O OD2 . ASP D  1  289 ? -3.013  20.312  18.457  1.00 21.95  -1 289  ASP D OD2 1 
ATOM   8253  N N   . THR D  1  290 ? -4.856  18.456  20.647  1.00 22.17  ?  290  THR D N   1 
ATOM   8254  C CA  . THR D  1  290 ? -4.611  17.055  20.320  1.00 21.45  ?  290  THR D CA  1 
ATOM   8255  C C   . THR D  1  290 ? -4.686  16.242  21.601  1.00 21.60  ?  290  THR D C   1 
ATOM   8256  O O   . THR D  1  290 ? -3.919  16.487  22.538  1.00 21.50  ?  290  THR D O   1 
ATOM   8257  C CB  . THR D  1  290 ? -3.243  16.874  19.653  1.00 20.43  ?  290  THR D CB  1 
ATOM   8258  O OG1 . THR D  1  290 ? -3.270  17.431  18.333  1.00 20.30  ?  290  THR D OG1 1 
ATOM   8259  C CG2 . THR D  1  290 ? -2.877  15.399  19.572  1.00 19.79  ?  290  THR D CG2 1 
ATOM   8260  N N   . LEU D  1  291 ? -5.602  15.277  21.642  1.00 22.00  ?  291  LEU D N   1 
ATOM   8261  C CA  . LEU D  1  291 ? -5.758  14.381  22.782  1.00 22.19  ?  291  LEU D CA  1 
ATOM   8262  C C   . LEU D  1  291 ? -5.563  12.952  22.299  1.00 21.54  ?  291  LEU D C   1 
ATOM   8263  O O   . LEU D  1  291 ? -6.291  12.487  21.415  1.00 21.60  ?  291  LEU D O   1 
ATOM   8264  C CB  . LEU D  1  291 ? -7.131  14.553  23.436  1.00 23.36  ?  291  LEU D CB  1 
ATOM   8265  C CG  . LEU D  1  291 ? -7.519  13.548  24.522  1.00 23.72  ?  291  LEU D CG  1 
ATOM   8266  C CD1 . LEU D  1  291 ? -6.566  13.630  25.704  1.00 23.54  ?  291  LEU D CD1 1 
ATOM   8267  C CD2 . LEU D  1  291 ? -8.952  13.782  24.974  1.00 24.99  ?  291  LEU D CD2 1 
ATOM   8268  N N   . SER D  1  292 ? -4.580  12.260  22.873  1.00 22.03  ?  292  SER D N   1 
ATOM   8269  C CA  . SER D  1  292 ? -4.231  10.903  22.465  1.00 21.41  ?  292  SER D CA  1 
ATOM   8270  C C   . SER D  1  292 ? -4.071  10.027  23.699  1.00 21.52  ?  292  SER D C   1 
ATOM   8271  O O   . SER D  1  292 ? -3.069  10.133  24.414  1.00 21.22  ?  292  SER D O   1 
ATOM   8272  C CB  . SER D  1  292 ? -2.951  10.890  21.637  1.00 20.50  ?  292  SER D CB  1 
ATOM   8273  O OG  . SER D  1  292 ? -2.596  9.562   21.293  1.00 20.00  ?  292  SER D OG  1 
ATOM   8274  N N   . LEU D  1  293 ? -5.055  9.167   23.949  1.00 21.92  ?  293  LEU D N   1 
ATOM   8275  C CA  . LEU D  1  293 ? -4.988  8.190   25.028  1.00 22.07  ?  293  LEU D CA  1 
ATOM   8276  C C   . LEU D  1  293 ? -5.028  6.763   24.490  1.00 21.69  ?  293  LEU D C   1 
ATOM   8277  O O   . LEU D  1  293 ? -5.442  5.839   25.195  1.00 22.04  ?  293  LEU D O   1 
ATOM   8278  C CB  . LEU D  1  293 ? -6.114  8.421   26.035  1.00 23.15  ?  293  LEU D CB  1 
ATOM   8279  C CG  . LEU D  1  293 ? -6.324  9.877   26.459  1.00 23.73  ?  293  LEU D CG  1 
ATOM   8280  C CD1 . LEU D  1  293 ? -7.748  10.102  26.948  1.00 24.93  ?  293  LEU D CD1 1 
ATOM   8281  C CD2 . LEU D  1  293 ? -5.312  10.287  27.521  1.00 23.58  ?  293  LEU D CD2 1 
ATOM   8282  N N   . HIS D  1  294 ? -4.605  6.567   23.242  1.00 22.47  ?  294  HIS D N   1 
ATOM   8283  C CA  . HIS D  1  294 ? -4.754  5.265   22.609  1.00 22.21  ?  294  HIS D CA  1 
ATOM   8284  C C   . HIS D  1  294 ? -3.796  4.244   23.222  1.00 21.79  ?  294  HIS D C   1 
ATOM   8285  O O   . HIS D  1  294 ? -2.831  4.588   23.908  1.00 21.55  ?  294  HIS D O   1 
ATOM   8286  C CB  . HIS D  1  294 ? -4.544  5.371   21.093  1.00 21.70  ?  294  HIS D CB  1 
ATOM   8287  C CG  . HIS D  1  294 ? -3.111  5.467   20.669  1.00 20.92  ?  294  HIS D CG  1 
ATOM   8288  N ND1 . HIS D  1  294 ? -2.278  4.370   20.602  1.00 20.45  ?  294  HIS D ND1 1 
ATOM   8289  C CD2 . HIS D  1  294 ? -2.373  6.523   20.254  1.00 20.60  ?  294  HIS D CD2 1 
ATOM   8290  C CE1 . HIS D  1  294 ? -1.084  4.750   20.186  1.00 19.90  ?  294  HIS D CE1 1 
ATOM   8291  N NE2 . HIS D  1  294 ? -1.114  6.052   19.968  1.00 19.97  ?  294  HIS D NE2 1 
ATOM   8292  N N   . THR D  1  295 ? -4.093  2.969   22.975  1.00 23.72  ?  295  THR D N   1 
ATOM   8293  C CA  . THR D  1  295 ? -3.326  1.841   23.507  1.00 23.43  ?  295  THR D CA  1 
ATOM   8294  C C   . THR D  1  295 ? -3.222  1.923   25.031  1.00 24.00  ?  295  THR D C   1 
ATOM   8295  O O   . THR D  1  295 ? -2.141  2.034   25.614  1.00 23.50  ?  295  THR D O   1 
ATOM   8296  C CB  . THR D  1  295 ? -1.940  1.757   22.857  1.00 22.65  ?  295  THR D CB  1 
ATOM   8297  O OG1 . THR D  1  295 ? -2.055  1.995   21.449  1.00 22.42  ?  295  THR D OG1 1 
ATOM   8298  C CG2 . THR D  1  295 ? -1.332  0.376   23.074  1.00 22.66  ?  295  THR D CG2 1 
ATOM   8299  N N   . ASN D  1  296 ? -4.385  1.879   25.674  1.00 24.55  ?  296  ASN D N   1 
ATOM   8300  C CA  . ASN D  1  296 ? -4.474  1.897   27.127  1.00 24.53  ?  296  ASN D CA  1 
ATOM   8301  C C   . ASN D  1  296 ? -5.512  0.861   27.544  1.00 25.29  ?  296  ASN D C   1 
ATOM   8302  O O   . ASN D  1  296 ? -5.988  0.066   26.728  1.00 25.70  ?  296  ASN D O   1 
ATOM   8303  C CB  . ASN D  1  296 ? -4.808  3.307   27.633  1.00 25.00  ?  296  ASN D CB  1 
ATOM   8304  C CG  . ASN D  1  296 ? -3.568  4.124   27.934  1.00 24.51  ?  296  ASN D CG  1 
ATOM   8305  O OD1 . ASN D  1  296 ? -3.067  4.117   29.056  1.00 24.66  ?  296  ASN D OD1 1 
ATOM   8306  N ND2 . ASN D  1  296 ? -3.065  4.833   26.929  1.00 23.95  ?  296  ASN D ND2 1 
ATOM   8307  N N   . LYS D  1  297 ? -5.863  0.864   28.828  1.00 26.74  ?  297  LYS D N   1 
ATOM   8308  C CA  . LYS D  1  297 ? -6.853  -0.060  29.369  1.00 27.47  ?  297  LYS D CA  1 
ATOM   8309  C C   . LYS D  1  297 ? -8.067  0.690   29.907  1.00 28.55  ?  297  LYS D C   1 
ATOM   8310  O O   . LYS D  1  297 ? -8.714  0.247   30.858  1.00 29.40  ?  297  LYS D O   1 
ATOM   8311  C CB  . LYS D  1  297 ? -6.226  -0.945  30.445  1.00 27.50  ?  297  LYS D CB  1 
ATOM   8312  C CG  . LYS D  1  297 ? -5.288  -2.001  29.875  1.00 26.66  ?  297  LYS D CG  1 
ATOM   8313  C CD  . LYS D  1  297 ? -4.646  -2.848  30.960  1.00 27.03  ?  297  LYS D CD  1 
ATOM   8314  C CE  . LYS D  1  297 ? -3.662  -3.840  30.359  1.00 25.98  ?  297  LYS D CE  1 
ATOM   8315  N NZ  . LYS D  1  297 ? -2.711  -4.371  31.373  1.00 26.79  ?  297  LYS D NZ  1 
ATOM   8316  N N   . LEU D  1  298 ? -8.376  1.832   29.299  1.00 27.12  ?  298  LEU D N   1 
ATOM   8317  C CA  . LEU D  1  298 ? -9.513  2.644   29.709  1.00 28.20  ?  298  LEU D CA  1 
ATOM   8318  C C   . LEU D  1  298 ? -10.824 1.905   29.459  1.00 28.97  ?  298  LEU D C   1 
ATOM   8319  O O   . LEU D  1  298 ? -10.961 1.139   28.501  1.00 28.54  ?  298  LEU D O   1 
ATOM   8320  C CB  . LEU D  1  298 ? -9.504  3.974   28.953  1.00 28.02  ?  298  LEU D CB  1 
ATOM   8321  C CG  . LEU D  1  298 ? -8.743  5.157   29.558  1.00 27.92  ?  298  LEU D CG  1 
ATOM   8322  C CD1 . LEU D  1  298 ? -7.376  4.746   30.060  1.00 27.13  ?  298  LEU D CD1 1 
ATOM   8323  C CD2 . LEU D  1  298 ? -8.587  6.239   28.509  1.00 27.51  ?  298  LEU D CD2 1 
ATOM   8324  N N   . THR D  1  299 ? -11.796 2.147   30.334  1.00 31.41  ?  299  THR D N   1 
ATOM   8325  C CA  . THR D  1  299 ? -13.102 1.504   30.275  1.00 32.36  ?  299  THR D CA  1 
ATOM   8326  C C   . THR D  1  299 ? -14.189 2.560   30.443  1.00 33.53  ?  299  THR D C   1 
ATOM   8327  O O   . THR D  1  299 ? -13.910 3.741   30.672  1.00 33.60  ?  299  THR D O   1 
ATOM   8328  C CB  . THR D  1  299 ? -13.238 0.410   31.344  1.00 32.92  ?  299  THR D CB  1 
ATOM   8329  O OG1 . THR D  1  299 ? -12.864 0.937   32.622  1.00 33.39  ?  299  THR D OG1 1 
ATOM   8330  C CG2 . THR D  1  299 ? -12.348 -0.780  31.008  1.00 31.89  ?  299  THR D CG2 1 
ATOM   8331  N N   . GLY D  1  300 ? -15.440 2.129   30.318  1.00 32.55  ?  300  GLY D N   1 
ATOM   8332  C CA  . GLY D  1  300 ? -16.567 3.021   30.443  1.00 33.81  ?  300  GLY D CA  1 
ATOM   8333  C C   . GLY D  1  300 ? -16.827 3.791   29.165  1.00 33.48  ?  300  GLY D C   1 
ATOM   8334  O O   . GLY D  1  300 ? -16.152 3.598   28.150  1.00 32.27  ?  300  GLY D O   1 
ATOM   8335  N N   . PRO D  1  301 ? -17.809 4.686   29.192  1.00 32.46  ?  301  PRO D N   1 
ATOM   8336  C CA  . PRO D  1  301 ? -18.190 5.403   27.973  1.00 32.32  ?  301  PRO D CA  1 
ATOM   8337  C C   . PRO D  1  301 ? -17.294 6.602   27.698  1.00 31.58  ?  301  PRO D C   1 
ATOM   8338  O O   . PRO D  1  301 ? -16.601 7.120   28.576  1.00 31.50  ?  301  PRO D O   1 
ATOM   8339  C CB  . PRO D  1  301 ? -19.623 5.852   28.273  1.00 34.03  ?  301  PRO D CB  1 
ATOM   8340  C CG  . PRO D  1  301 ? -19.620 6.068   29.750  1.00 34.94  ?  301  PRO D CG  1 
ATOM   8341  C CD  . PRO D  1  301 ? -18.685 5.025   30.327  1.00 34.07  ?  301  PRO D CD  1 
ATOM   8342  N N   . ILE D  1  302 ? -17.326 7.035   26.445  1.00 29.82  ?  302  ILE D N   1 
ATOM   8343  C CA  . ILE D  1  302 ? -16.666 8.285   26.053  1.00 29.32  ?  302  ILE D CA  1 
ATOM   8344  C C   . ILE D  1  302 ? -17.388 9.451   26.718  1.00 30.66  ?  302  ILE D C   1 
ATOM   8345  O O   . ILE D  1  302 ? -18.629 9.515   26.667  1.00 31.88  ?  302  ILE D O   1 
ATOM   8346  C CB  . ILE D  1  302 ? -16.668 8.432   24.528  1.00 28.64  ?  302  ILE D CB  1 
ATOM   8347  C CG1 . ILE D  1  302 ? -15.941 7.255   23.873  1.00 27.40  ?  302  ILE D CG1 1 
ATOM   8348  C CG2 . ILE D  1  302 ? -16.030 9.749   24.108  1.00 28.23  ?  302  ILE D CG2 1 
ATOM   8349  C CD1 . ILE D  1  302 ? -16.060 7.228   22.363  1.00 26.87  ?  302  ILE D CD1 1 
ATOM   8350  N N   . PRO D  1  303 ? -16.680 10.379  27.361  1.00 31.68  ?  303  PRO D N   1 
ATOM   8351  C CA  . PRO D  1  303 ? -17.371 11.474  28.057  1.00 33.06  ?  303  PRO D CA  1 
ATOM   8352  C C   . PRO D  1  303 ? -18.039 12.418  27.067  1.00 33.53  ?  303  PRO D C   1 
ATOM   8353  O O   . PRO D  1  303 ? -17.396 12.946  26.158  1.00 32.61  ?  303  PRO D O   1 
ATOM   8354  C CB  . PRO D  1  303 ? -16.247 12.170  28.832  1.00 32.60  ?  303  PRO D CB  1 
ATOM   8355  C CG  . PRO D  1  303 ? -15.008 11.831  28.084  1.00 30.90  ?  303  PRO D CG  1 
ATOM   8356  C CD  . PRO D  1  303 ? -15.218 10.458  27.515  1.00 30.39  ?  303  PRO D CD  1 
ATOM   8357  N N   . SER D  1  304 ? -19.347 12.622  27.254  1.00 34.92  ?  304  SER D N   1 
ATOM   8358  C CA  . SER D  1  304 ? -20.089 13.563  26.422  1.00 35.62  ?  304  SER D CA  1 
ATOM   8359  C C   . SER D  1  304 ? -19.562 14.984  26.558  1.00 35.69  ?  304  SER D C   1 
ATOM   8360  O O   . SER D  1  304 ? -19.859 15.830  25.708  1.00 35.92  ?  304  SER D O   1 
ATOM   8361  C CB  . SER D  1  304 ? -21.576 13.521  26.779  1.00 37.44  ?  304  SER D CB  1 
ATOM   8362  O OG  . SER D  1  304 ? -21.779 13.815  28.150  1.00 38.57  ?  304  SER D OG  1 
ATOM   8363  N N   . THR D  1  305 ? -18.791 15.262  27.610  1.00 36.36  ?  305  THR D N   1 
ATOM   8364  C CA  . THR D  1  305 ? -18.226 16.585  27.833  1.00 36.44  ?  305  THR D CA  1 
ATOM   8365  C C   . THR D  1  305 ? -17.126 16.934  26.840  1.00 34.92  ?  305  THR D C   1 
ATOM   8366  O O   . THR D  1  305 ? -16.680 18.086  26.821  1.00 34.96  ?  305  THR D O   1 
ATOM   8367  C CB  . THR D  1  305 ? -17.686 16.680  29.259  1.00 36.70  ?  305  THR D CB  1 
ATOM   8368  O OG1 . THR D  1  305 ? -16.593 15.768  29.417  1.00 35.27  ?  305  THR D OG1 1 
ATOM   8369  C CG2 . THR D  1  305 ? -18.774 16.314  30.252  1.00 38.30  ?  305  THR D CG2 1 
ATOM   8370  N N   . LEU D  1  306 ? -16.677 15.974  26.024  1.00 33.91  ?  306  LEU D N   1 
ATOM   8371  C CA  . LEU D  1  306 ? -15.644 16.261  25.033  1.00 32.55  ?  306  LEU D CA  1 
ATOM   8372  C C   . LEU D  1  306 ? -16.110 17.285  24.008  1.00 32.96  ?  306  LEU D C   1 
ATOM   8373  O O   . LEU D  1  306 ? -15.284 18.004  23.432  1.00 32.23  ?  306  LEU D O   1 
ATOM   8374  C CB  . LEU D  1  306 ? -15.216 14.975  24.325  1.00 31.32  ?  306  LEU D CB  1 
ATOM   8375  C CG  . LEU D  1  306 ? -14.356 13.985  25.109  1.00 30.52  ?  306  LEU D CG  1 
ATOM   8376  C CD1 . LEU D  1  306 ? -13.593 13.089  24.150  1.00 29.13  ?  306  LEU D CD1 1 
ATOM   8377  C CD2 . LEU D  1  306 ? -13.398 14.726  26.025  1.00 30.34  ?  306  LEU D CD2 1 
ATOM   8378  N N   . GLY D  1  307 ? -17.419 17.370  23.765  1.00 32.25  ?  307  GLY D N   1 
ATOM   8379  C CA  . GLY D  1  307 ? -17.937 18.358  22.836  1.00 32.81  ?  307  GLY D CA  1 
ATOM   8380  C C   . GLY D  1  307 ? -17.646 19.786  23.244  1.00 33.38  ?  307  GLY D C   1 
ATOM   8381  O O   . GLY D  1  307 ? -17.634 20.677  22.389  1.00 33.44  ?  307  GLY D O   1 
ATOM   8382  N N   . ASN D  1  308 ? -17.406 20.022  24.537  1.00 37.37  ?  308  ASN D N   1 
ATOM   8383  C CA  . ASN D  1  308 ? -17.081 21.365  25.005  1.00 37.94  ?  308  ASN D CA  1 
ATOM   8384  C C   . ASN D  1  308 ? -15.779 21.875  24.402  1.00 36.61  ?  308  ASN D C   1 
ATOM   8385  O O   . ASN D  1  308 ? -15.625 23.085  24.194  1.00 37.01  ?  308  ASN D O   1 
ATOM   8386  C CB  . ASN D  1  308 ? -16.997 21.383  26.532  1.00 38.61  ?  308  ASN D CB  1 
ATOM   8387  C CG  . ASN D  1  308 ? -18.343 21.163  27.193  1.00 40.28  ?  308  ASN D CG  1 
ATOM   8388  O OD1 . ASN D  1  308 ? -19.365 21.032  26.519  1.00 40.99  ?  308  ASN D OD1 1 
ATOM   8389  N ND2 . ASN D  1  308 ? -18.350 21.123  28.521  1.00 41.00  ?  308  ASN D ND2 1 
ATOM   8390  N N   . ILE D  1  309 ? -14.838 20.980  24.108  1.00 31.81  ?  309  ILE D N   1 
ATOM   8391  C CA  . ILE D  1  309 ? -13.528 21.376  23.595  1.00 30.55  ?  309  ILE D CA  1 
ATOM   8392  C C   . ILE D  1  309 ? -13.703 21.693  22.113  1.00 30.28  ?  309  ILE D C   1 
ATOM   8393  O O   . ILE D  1  309 ? -13.707 20.794  21.270  1.00 29.51  ?  309  ILE D O   1 
ATOM   8394  C CB  . ILE D  1  309 ? -12.475 20.289  23.817  1.00 29.17  ?  309  ILE D CB  1 
ATOM   8395  C CG1 . ILE D  1  309 ? -12.574 19.729  25.237  1.00 29.60  ?  309  ILE D CG1 1 
ATOM   8396  C CG2 . ILE D  1  309 ? -11.082 20.843  23.554  1.00 28.11  ?  309  ILE D CG2 1 
ATOM   8397  C CD1 . ILE D  1  309 ? -11.838 18.420  25.430  1.00 28.46  ?  309  ILE D CD1 1 
ATOM   8398  N N   . LYS D  1  310 ? -13.842 22.978  21.788  1.00 31.33  ?  310  LYS D N   1 
ATOM   8399  C CA  . LYS D  1  310 ? -14.039 23.386  20.405  1.00 31.22  ?  310  LYS D CA  1 
ATOM   8400  C C   . LYS D  1  310 ? -12.735 23.510  19.628  1.00 29.83  ?  310  LYS D C   1 
ATOM   8401  O O   . LYS D  1  310 ? -12.778 23.638  18.400  1.00 29.54  ?  310  LYS D O   1 
ATOM   8402  C CB  . LYS D  1  310 ? -14.791 24.718  20.354  1.00 32.66  ?  310  LYS D CB  1 
ATOM   8403  C CG  . LYS D  1  310 ? -16.098 24.720  21.129  1.00 34.24  ?  310  LYS D CG  1 
ATOM   8404  C CD  . LYS D  1  310 ? -16.985 23.555  20.725  1.00 34.30  ?  310  LYS D CD  1 
ATOM   8405  C CE  . LYS D  1  310 ? -18.440 23.834  21.055  1.00 36.11  ?  310  LYS D CE  1 
ATOM   8406  N NZ  . LYS D  1  310 ? -19.327 22.705  20.667  1.00 36.24  ?  310  LYS D NZ  1 
ATOM   8407  N N   . THR D  1  311 ? -11.588 23.481  20.304  1.00 29.64  ?  311  THR D N   1 
ATOM   8408  C CA  . THR D  1  311 ? -10.296 23.558  19.637  1.00 28.38  ?  311  THR D CA  1 
ATOM   8409  C C   . THR D  1  311 ? -9.720  22.192  19.293  1.00 27.13  ?  311  THR D C   1 
ATOM   8410  O O   . THR D  1  311 ? -8.719  22.125  18.572  1.00 26.12  ?  311  THR D O   1 
ATOM   8411  C CB  . THR D  1  311 ? -9.290  24.316  20.513  1.00 28.25  ?  311  THR D CB  1 
ATOM   8412  O OG1 . THR D  1  311 ? -9.270  23.748  21.828  1.00 28.38  ?  311  THR D OG1 1 
ATOM   8413  C CG2 . THR D  1  311 ? -9.671  25.785  20.613  1.00 29.40  ?  311  THR D CG2 1 
ATOM   8414  N N   . LEU D  1  312 ? -10.323 21.112  19.783  1.00 27.05  ?  312  LEU D N   1 
ATOM   8415  C CA  . LEU D  1  312 ? -9.748  19.783  19.620  1.00 25.96  ?  312  LEU D CA  1 
ATOM   8416  C C   . LEU D  1  312 ? -9.865  19.331  18.169  1.00 25.43  ?  312  LEU D C   1 
ATOM   8417  O O   . LEU D  1  312 ? -10.974 19.179  17.646  1.00 26.07  ?  312  LEU D O   1 
ATOM   8418  C CB  . LEU D  1  312 ? -10.439 18.792  20.552  1.00 26.38  ?  312  LEU D CB  1 
ATOM   8419  C CG  . LEU D  1  312 ? -9.857  17.379  20.570  1.00 25.38  ?  312  LEU D CG  1 
ATOM   8420  C CD1 . LEU D  1  312 ? -8.507  17.379  21.266  1.00 24.61  ?  312  LEU D CD1 1 
ATOM   8421  C CD2 . LEU D  1  312 ? -10.813 16.414  21.251  1.00 25.99  ?  312  LEU D CD2 1 
ATOM   8422  N N   . ALA D  1  313 ? -8.718  19.118  17.519  1.00 23.87  ?  313  ALA D N   1 
ATOM   8423  C CA  . ALA D  1  313 ? -8.688  18.672  16.134  1.00 23.33  ?  313  ALA D CA  1 
ATOM   8424  C C   . ALA D  1  313 ? -8.228  17.233  15.960  1.00 22.44  ?  313  ALA D C   1 
ATOM   8425  O O   . ALA D  1  313 ? -8.500  16.641  14.911  1.00 22.18  ?  313  ALA D O   1 
ATOM   8426  C CB  . ALA D  1  313 ? -7.776  19.584  15.299  1.00 22.87  ?  313  ALA D CB  1 
ATOM   8427  N N   . VAL D  1  314 ? -7.545  16.658  16.947  1.00 21.12  ?  314  VAL D N   1 
ATOM   8428  C CA  . VAL D  1  314 ? -7.082  15.275  16.889  1.00 20.37  ?  314  VAL D CA  1 
ATOM   8429  C C   . VAL D  1  314 ? -7.520  14.571  18.165  1.00 20.75  ?  314  VAL D C   1 
ATOM   8430  O O   . VAL D  1  314 ? -7.122  14.969  19.266  1.00 20.91  ?  314  VAL D O   1 
ATOM   8431  C CB  . VAL D  1  314 ? -5.557  15.179  16.717  1.00 19.38  ?  314  VAL D CB  1 
ATOM   8432  C CG1 . VAL D  1  314 ? -5.122  13.723  16.659  1.00 18.73  ?  314  VAL D CG1 1 
ATOM   8433  C CG2 . VAL D  1  314 ? -5.113  15.917  15.462  1.00 19.08  ?  314  VAL D CG2 1 
ATOM   8434  N N   . LEU D  1  315 ? -8.336  13.528  18.017  1.00 20.35  ?  315  LEU D N   1 
ATOM   8435  C CA  . LEU D  1  315 ? -8.775  12.699  19.135  1.00 20.72  ?  315  LEU D CA  1 
ATOM   8436  C C   . LEU D  1  315 ? -8.429  11.252  18.811  1.00 20.03  ?  315  LEU D C   1 
ATOM   8437  O O   . LEU D  1  315 ? -8.974  10.679  17.862  1.00 20.00  ?  315  LEU D O   1 
ATOM   8438  C CB  . LEU D  1  315 ? -10.276 12.861  19.385  1.00 21.88  ?  315  LEU D CB  1 
ATOM   8439  C CG  . LEU D  1  315 ? -10.891 12.068  20.540  1.00 22.47  ?  315  LEU D CG  1 
ATOM   8440  C CD1 . LEU D  1  315 ? -10.143 12.340  21.834  1.00 22.42  ?  315  LEU D CD1 1 
ATOM   8441  C CD2 . LEU D  1  315 ? -12.368 12.398  20.687  1.00 23.74  ?  315  LEU D CD2 1 
ATOM   8442  N N   . HIS D  1  316 ? -7.525  10.663  19.591  1.00 21.12  ?  316  HIS D N   1 
ATOM   8443  C CA  . HIS D  1  316 ? -7.101  9.276   19.402  1.00 20.52  ?  316  HIS D CA  1 
ATOM   8444  C C   . HIS D  1  316 ? -7.443  8.493   20.666  1.00 20.93  ?  316  HIS D C   1 
ATOM   8445  O O   . HIS D  1  316 ? -6.686  8.510   21.642  1.00 20.76  ?  316  HIS D O   1 
ATOM   8446  C CB  . HIS D  1  316 ? -5.611  9.196   19.077  1.00 19.58  ?  316  HIS D CB  1 
ATOM   8447  C CG  . HIS D  1  316 ? -5.269  9.679   17.702  1.00 19.16  ?  316  HIS D CG  1 
ATOM   8448  N ND1 . HIS D  1  316 ? -3.972  9.757   17.240  1.00 18.41  ?  316  HIS D ND1 1 
ATOM   8449  C CD2 . HIS D  1  316 ? -6.056  10.111  16.689  1.00 19.44  ?  316  HIS D CD2 1 
ATOM   8450  C CE1 . HIS D  1  316 ? -3.976  10.215  16.000  1.00 18.26  ?  316  HIS D CE1 1 
ATOM   8451  N NE2 . HIS D  1  316 ? -5.228  10.437  15.642  1.00 18.85  ?  316  HIS D NE2 1 
ATOM   8452  N N   . LEU D  1  317 ? -8.588  7.811   20.644  1.00 21.86  ?  317  LEU D N   1 
ATOM   8453  C CA  . LEU D  1  317 ? -9.034  6.976   21.751  1.00 22.35  ?  317  LEU D CA  1 
ATOM   8454  C C   . LEU D  1  317 ? -9.017  5.492   21.410  1.00 21.99  ?  317  LEU D C   1 
ATOM   8455  O O   . LEU D  1  317 ? -9.597  4.690   22.150  1.00 22.49  ?  317  LEU D O   1 
ATOM   8456  C CB  . LEU D  1  317 ? -10.439 7.390   22.194  1.00 23.52  ?  317  LEU D CB  1 
ATOM   8457  C CG  . LEU D  1  317 ? -10.601 8.832   22.669  1.00 24.10  ?  317  LEU D CG  1 
ATOM   8458  C CD1 . LEU D  1  317 ? -11.984 9.048   23.260  1.00 25.41  ?  317  LEU D CD1 1 
ATOM   8459  C CD2 . LEU D  1  317 ? -9.521  9.180   23.680  1.00 23.77  ?  317  LEU D CD2 1 
ATOM   8460  N N   . TYR D  1  318 ? -8.372  5.105   20.313  1.00 24.07  ?  318  TYR D N   1 
ATOM   8461  C CA  . TYR D  1  318 ? -8.463  3.729   19.857  1.00 23.83  ?  318  TYR D CA  1 
ATOM   8462  C C   . TYR D  1  318 ? -7.620  2.805   20.737  1.00 23.49  ?  318  TYR D C   1 
ATOM   8463  O O   . TYR D  1  318 ? -6.828  3.244   21.574  1.00 23.32  ?  318  TYR D O   1 
ATOM   8464  C CB  . TYR D  1  318 ? -8.050  3.621   18.388  1.00 23.20  ?  318  TYR D CB  1 
ATOM   8465  C CG  . TYR D  1  318 ? -6.611  3.976   18.092  1.00 22.38  ?  318  TYR D CG  1 
ATOM   8466  C CD1 . TYR D  1  318 ? -5.598  3.035   18.231  1.00 21.83  ?  318  TYR D CD1 1 
ATOM   8467  C CD2 . TYR D  1  318 ? -6.267  5.248   17.655  1.00 22.24  ?  318  TYR D CD2 1 
ATOM   8468  C CE1 . TYR D  1  318 ? -4.284  3.354   17.955  1.00 21.18  ?  318  TYR D CE1 1 
ATOM   8469  C CE2 . TYR D  1  318 ? -4.956  5.576   17.376  1.00 21.56  ?  318  TYR D CE2 1 
ATOM   8470  C CZ  . TYR D  1  318 ? -3.969  4.626   17.527  1.00 21.05  ?  318  TYR D CZ  1 
ATOM   8471  O OH  . TYR D  1  318 ? -2.661  4.948   17.251  1.00 20.47  ?  318  TYR D OH  1 
ATOM   8472  N N   . LEU D  1  319 ? -7.821  1.500   20.546  1.00 24.11  ?  319  LEU D N   1 
ATOM   8473  C CA  . LEU D  1  319 ? -7.130  0.457   21.306  1.00 23.82  ?  319  LEU D CA  1 
ATOM   8474  C C   . LEU D  1  319 ? -7.359  0.630   22.809  1.00 24.44  ?  319  LEU D C   1 
ATOM   8475  O O   . LEU D  1  319 ? -6.431  0.818   23.598  1.00 24.00  ?  319  LEU D O   1 
ATOM   8476  C CB  . LEU D  1  319 ? -5.635  0.428   20.972  1.00 22.83  ?  319  LEU D CB  1 
ATOM   8477  C CG  . LEU D  1  319 ? -5.249  -0.450  19.782  1.00 22.33  ?  319  LEU D CG  1 
ATOM   8478  C CD1 . LEU D  1  319 ? -3.799  -0.217  19.389  1.00 21.72  ?  319  LEU D CD1 1 
ATOM   8479  C CD2 . LEU D  1  319 ? -5.494  -1.915  20.106  1.00 22.50  ?  319  LEU D CD2 1 
ATOM   8480  N N   . ASN D  1  320 ? -8.630  0.562   23.190  1.00 26.39  ?  320  ASN D N   1 
ATOM   8481  C CA  . ASN D  1  320 ? -9.040  0.670   24.582  1.00 26.98  ?  320  ASN D CA  1 
ATOM   8482  C C   . ASN D  1  320 ? -10.214 -0.279  24.795  1.00 27.69  ?  320  ASN D C   1 
ATOM   8483  O O   . ASN D  1  320 ? -10.515 -1.124  23.945  1.00 27.77  ?  320  ASN D O   1 
ATOM   8484  C CB  . ASN D  1  320 ? -9.364  2.127   24.935  1.00 27.64  ?  320  ASN D CB  1 
ATOM   8485  C CG  . ASN D  1  320 ? -8.165  2.866   25.495  1.00 26.84  ?  320  ASN D CG  1 
ATOM   8486  O OD1 . ASN D  1  320 ? -7.776  2.658   26.642  1.00 26.97  ?  320  ASN D OD1 1 
ATOM   8487  N ND2 . ASN D  1  320 ? -7.565  3.727   24.681  1.00 26.22  ?  320  ASN D ND2 1 
ATOM   8488  N N   . GLN D  1  321 ? -10.886 -0.148  25.938  1.00 30.68  ?  321  GLN D N   1 
ATOM   8489  C CA  . GLN D  1  321 ? -12.036 -0.984  26.261  1.00 31.58  ?  321  GLN D CA  1 
ATOM   8490  C C   . GLN D  1  321 ? -13.278 -0.139  26.525  1.00 32.71  ?  321  GLN D C   1 
ATOM   8491  O O   . GLN D  1  321 ? -14.110 -0.489  27.365  1.00 33.73  ?  321  GLN D O   1 
ATOM   8492  C CB  . GLN D  1  321 ? -11.738 -1.878  27.464  1.00 32.00  ?  321  GLN D CB  1 
ATOM   8493  C CG  . GLN D  1  321 ? -10.332 -2.450  27.487  1.00 31.08  ?  321  GLN D CG  1 
ATOM   8494  C CD  . GLN D  1  321 ? -10.223 -3.692  28.350  1.00 32.09  ?  321  GLN D CD  1 
ATOM   8495  O OE1 . GLN D  1  321 ? -11.090 -4.566  28.313  1.00 33.14  ?  321  GLN D OE1 1 
ATOM   8496  N NE2 . GLN D  1  321 ? -9.155  -3.775  29.134  1.00 30.74  ?  321  GLN D NE2 1 
ATOM   8497  N N   . LEU D  1  322 ? -13.416 0.973   25.808  1.00 29.16  ?  322  LEU D N   1 
ATOM   8498  C CA  . LEU D  1  322 ? -14.573 1.838   25.985  1.00 30.28  ?  322  LEU D CA  1 
ATOM   8499  C C   . LEU D  1  322 ? -15.820 1.168   25.421  1.00 30.98  ?  322  LEU D C   1 
ATOM   8500  O O   . LEU D  1  322 ? -15.804 0.649   24.300  1.00 30.41  ?  322  LEU D O   1 
ATOM   8501  C CB  . LEU D  1  322 ? -14.336 3.183   25.299  1.00 29.97  ?  322  LEU D CB  1 
ATOM   8502  C CG  . LEU D  1  322 ? -13.016 3.885   25.628  1.00 29.16  ?  322  LEU D CG  1 
ATOM   8503  C CD1 . LEU D  1  322 ? -12.831 5.123   24.761  1.00 28.85  ?  322  LEU D CD1 1 
ATOM   8504  C CD2 . LEU D  1  322 ? -12.944 4.241   27.105  1.00 29.82  ?  322  LEU D CD2 1 
ATOM   8505  N N   . ASN D  1  323 ? -16.900 1.183   26.193  1.00 36.42  ?  323  ASN D N   1 
ATOM   8506  C CA  . ASN D  1  323 ? -18.165 0.592   25.778  1.00 37.29  ?  323  ASN D CA  1 
ATOM   8507  C C   . ASN D  1  323 ? -19.261 1.659   25.783  1.00 38.49  ?  323  ASN D C   1 
ATOM   8508  O O   . ASN D  1  323 ? -19.002 2.848   25.996  1.00 38.55  ?  323  ASN D O   1 
ATOM   8509  C CB  . ASN D  1  323 ? -18.521 -0.612  26.659  1.00 37.91  ?  323  ASN D CB  1 
ATOM   8510  C CG  . ASN D  1  323 ? -18.718 -0.246  28.122  1.00 38.91  ?  323  ASN D CG  1 
ATOM   8511  O OD1 . ASN D  1  323 ? -18.406 0.865   28.555  1.00 39.01  ?  323  ASN D OD1 1 
ATOM   8512  N ND2 . ASN D  1  323 ? -19.240 -1.199  28.892  1.00 39.73  ?  323  ASN D ND2 1 
ATOM   8513  N N   . GLY D  1  324 ? -20.491 1.226   25.533  1.00 35.17  ?  324  GLY D N   1 
ATOM   8514  C CA  . GLY D  1  324 ? -21.602 2.146   25.427  1.00 36.40  ?  324  GLY D CA  1 
ATOM   8515  C C   . GLY D  1  324 ? -21.738 2.726   24.035  1.00 35.94  ?  324  GLY D C   1 
ATOM   8516  O O   . GLY D  1  324 ? -21.140 2.262   23.060  1.00 34.78  ?  324  GLY D O   1 
ATOM   8517  N N   . SER D  1  325 ? -22.552 3.772   23.950  1.00 34.12  ?  325  SER D N   1 
ATOM   8518  C CA  . SER D  1  325 ? -22.847 4.429   22.687  1.00 33.96  ?  325  SER D CA  1 
ATOM   8519  C C   . SER D  1  325 ? -21.985 5.675   22.518  1.00 33.28  ?  325  SER D C   1 
ATOM   8520  O O   . SER D  1  325 ? -21.457 6.232   23.483  1.00 33.33  ?  325  SER D O   1 
ATOM   8521  C CB  . SER D  1  325 ? -24.329 4.804   22.607  1.00 35.62  ?  325  SER D CB  1 
ATOM   8522  O OG  . SER D  1  325 ? -25.153 3.653   22.664  1.00 36.28  ?  325  SER D OG  1 
ATOM   8523  N N   . ILE D  1  326 ? -21.839 6.099   21.267  1.00 32.44  ?  326  ILE D N   1 
ATOM   8524  C CA  . ILE D  1  326 ? -21.100 7.319   20.951  1.00 31.88  ?  326  ILE D CA  1 
ATOM   8525  C C   . ILE D  1  326 ? -21.948 8.514   21.370  1.00 33.28  ?  326  ILE D C   1 
ATOM   8526  O O   . ILE D  1  326 ? -23.092 8.652   20.911  1.00 34.33  ?  326  ILE D O   1 
ATOM   8527  C CB  . ILE D  1  326 ? -20.735 7.390   19.460  1.00 30.91  ?  326  ILE D CB  1 
ATOM   8528  C CG1 . ILE D  1  326 ? -19.837 6.213   19.073  1.00 29.59  ?  326  ILE D CG1 1 
ATOM   8529  C CG2 . ILE D  1  326 ? -20.054 8.713   19.142  1.00 30.49  ?  326  ILE D CG2 1 
ATOM   8530  C CD1 . ILE D  1  326 ? -19.594 6.096   17.583  1.00 28.79  ?  326  ILE D CD1 1 
ATOM   8531  N N   . PRO D  1  327 ? -21.440 9.388   22.231  1.00 32.06  ?  327  PRO D N   1 
ATOM   8532  C CA  . PRO D  1  327 ? -22.216 10.555  22.658  1.00 33.48  ?  327  PRO D CA  1 
ATOM   8533  C C   . PRO D  1  327 ? -22.516 11.467  21.484  1.00 33.58  ?  327  PRO D C   1 
ATOM   8534  O O   . PRO D  1  327 ? -21.602 11.856  20.741  1.00 32.41  ?  327  PRO D O   1 
ATOM   8535  C CB  . PRO D  1  327 ? -21.295 11.244  23.677  1.00 33.21  ?  327  PRO D CB  1 
ATOM   8536  C CG  . PRO D  1  327 ? -20.339 10.185  24.110  1.00 32.06  ?  327  PRO D CG  1 
ATOM   8537  C CD  . PRO D  1  327 ? -20.141 9.303   22.919  1.00 31.01  ?  327  PRO D CD  1 
ATOM   8538  N N   . PRO D  1  328 ? -23.786 11.824  21.276  1.00 33.93  ?  328  PRO D N   1 
ATOM   8539  C CA  . PRO D  1  328 ? -24.117 12.744  20.176  1.00 34.16  ?  328  PRO D CA  1 
ATOM   8540  C C   . PRO D  1  328 ? -23.447 14.097  20.307  1.00 34.02  ?  328  PRO D C   1 
ATOM   8541  O O   . PRO D  1  328 ? -23.311 14.807  19.303  1.00 33.74  ?  328  PRO D O   1 
ATOM   8542  C CB  . PRO D  1  328 ? -25.645 12.865  20.263  1.00 36.02  ?  328  PRO D CB  1 
ATOM   8543  C CG  . PRO D  1  328 ? -26.085 11.636  20.992  1.00 36.39  ?  328  PRO D CG  1 
ATOM   8544  C CD  . PRO D  1  328 ? -24.988 11.328  21.967  1.00 35.45  ?  328  PRO D CD  1 
ATOM   8545  N N   . GLU D  1  329 ? -23.018 14.475  21.511  1.00 35.08  ?  329  GLU D N   1 
ATOM   8546  C CA  . GLU D  1  329 ? -22.327 15.739  21.717  1.00 34.95  ?  329  GLU D CA  1 
ATOM   8547  C C   . GLU D  1  329 ? -20.944 15.767  21.078  1.00 33.16  ?  329  GLU D C   1 
ATOM   8548  O O   . GLU D  1  329 ? -20.353 16.848  20.979  1.00 32.97  ?  329  GLU D O   1 
ATOM   8549  C CB  . GLU D  1  329 ? -22.223 16.032  23.215  1.00 35.67  ?  329  GLU D CB  1 
ATOM   8550  C CG  . GLU D  1  329 ? -23.573 16.115  23.919  1.00 37.62  ?  329  GLU D CG  1 
ATOM   8551  C CD  . GLU D  1  329 ? -24.077 14.763  24.399  1.00 37.86  ?  329  GLU D CD  1 
ATOM   8552  O OE1 . GLU D  1  329 ? -23.639 13.729  23.851  1.00 36.62  ?  329  GLU D OE1 1 
ATOM   8553  O OE2 . GLU D  1  329 ? -24.921 14.737  25.319  1.00 39.37  -1 329  GLU D OE2 1 
ATOM   8554  N N   . LEU D  1  330 ? -20.415 14.616  20.650  1.00 33.97  ?  330  LEU D N   1 
ATOM   8555  C CA  . LEU D  1  330 ? -19.130 14.605  19.957  1.00 32.36  ?  330  LEU D CA  1 
ATOM   8556  C C   . LEU D  1  330 ? -19.193 15.381  18.650  1.00 32.24  ?  330  LEU D C   1 
ATOM   8557  O O   . LEU D  1  330 ? -18.183 15.944  18.213  1.00 31.33  ?  330  LEU D O   1 
ATOM   8558  C CB  . LEU D  1  330 ? -18.681 13.168  19.689  1.00 31.27  ?  330  LEU D CB  1 
ATOM   8559  C CG  . LEU D  1  330 ? -18.161 12.345  20.869  1.00 30.94  ?  330  LEU D CG  1 
ATOM   8560  C CD1 . LEU D  1  330 ? -17.305 11.191  20.370  1.00 29.56  ?  330  LEU D CD1 1 
ATOM   8561  C CD2 . LEU D  1  330 ? -17.376 13.218  21.836  1.00 30.89  ?  330  LEU D CD2 1 
ATOM   8562  N N   . GLY D  1  331 ? -20.366 15.433  18.017  1.00 33.04  ?  331  GLY D N   1 
ATOM   8563  C CA  . GLY D  1  331 ? -20.533 16.213  16.803  1.00 33.11  ?  331  GLY D CA  1 
ATOM   8564  C C   . GLY D  1  331 ? -20.325 17.700  16.991  1.00 33.64  ?  331  GLY D C   1 
ATOM   8565  O O   . GLY D  1  331 ? -20.166 18.419  15.998  1.00 33.49  ?  331  GLY D O   1 
ATOM   8566  N N   . GLU D  1  332 ? -20.320 18.175  18.234  1.00 34.97  ?  332  GLU D N   1 
ATOM   8567  C CA  . GLU D  1  332 ? -20.102 19.582  18.533  1.00 35.55  ?  332  GLU D CA  1 
ATOM   8568  C C   . GLU D  1  332 ? -18.625 19.946  18.613  1.00 34.23  ?  332  GLU D C   1 
ATOM   8569  O O   . GLU D  1  332 ? -18.304 21.107  18.886  1.00 34.61  ?  332  GLU D O   1 
ATOM   8570  C CB  . GLU D  1  332 ? -20.811 19.947  19.840  1.00 37.01  ?  332  GLU D CB  1 
ATOM   8571  C CG  . GLU D  1  332 ? -22.192 19.320  19.974  1.00 38.27  ?  332  GLU D CG  1 
ATOM   8572  C CD  . GLU D  1  332 ? -23.247 20.035  19.148  1.00 39.52  ?  332  GLU D CD  1 
ATOM   8573  O OE1 . GLU D  1  332 ? -22.953 21.126  18.614  1.00 39.58  ?  332  GLU D OE1 1 
ATOM   8574  O OE2 . GLU D  1  332 ? -24.369 19.500  19.022  1.00 40.50  -1 332  GLU D OE2 1 
ATOM   8575  N N   . MET D  1  333 ? -17.725 18.990  18.385  1.00 32.48  ?  333  MET D N   1 
ATOM   8576  C CA  . MET D  1  333 ? -16.291 19.267  18.301  1.00 31.20  ?  333  MET D CA  1 
ATOM   8577  C C   . MET D  1  333 ? -16.035 19.900  16.939  1.00 30.82  ?  333  MET D C   1 
ATOM   8578  O O   . MET D  1  333 ? -15.717 19.221  15.962  1.00 29.91  ?  333  MET D O   1 
ATOM   8579  C CB  . MET D  1  333 ? -15.475 17.993  18.491  1.00 29.93  ?  333  MET D CB  1 
ATOM   8580  C CG  . MET D  1  333 ? -15.554 17.393  19.888  1.00 30.23  ?  333  MET D CG  1 
ATOM   8581  S SD  . MET D  1  333 ? -14.778 15.765  20.015  1.00 28.92  ?  333  MET D SD  1 
ATOM   8582  C CE  . MET D  1  333 ? -15.034 15.117  18.364  1.00 28.33  ?  333  MET D CE  1 
ATOM   8583  N N   . GLU D  1  334 ? -16.178 21.228  16.885  1.00 31.91  ?  334  GLU D N   1 
ATOM   8584  C CA  . GLU D  1  334 ? -16.147 21.940  15.610  1.00 31.87  ?  334  GLU D CA  1 
ATOM   8585  C C   . GLU D  1  334 ? -14.832 21.724  14.873  1.00 30.34  ?  334  GLU D C   1 
ATOM   8586  O O   . GLU D  1  334 ? -14.823 21.506  13.655  1.00 29.91  ?  334  GLU D O   1 
ATOM   8587  C CB  . GLU D  1  334 ? -16.377 23.433  15.841  1.00 32.98  ?  334  GLU D CB  1 
ATOM   8588  C CG  . GLU D  1  334 ? -17.067 23.763  17.151  1.00 34.25  ?  334  GLU D CG  1 
ATOM   8589  C CD  . GLU D  1  334 ? -17.403 25.236  17.272  1.00 35.51  ?  334  GLU D CD  1 
ATOM   8590  O OE1 . GLU D  1  334 ? -16.533 26.068  16.940  1.00 35.05  ?  334  GLU D OE1 1 
ATOM   8591  O OE2 . GLU D  1  334 ? -18.532 25.562  17.698  1.00 37.03  -1 334  GLU D OE2 1 
ATOM   8592  N N   . SER D  1  335 ? -13.713 21.780  15.590  1.00 28.98  ?  335  SER D N   1 
ATOM   8593  C CA  . SER D  1  335 ? -12.399 21.733  14.963  1.00 27.68  ?  335  SER D CA  1 
ATOM   8594  C C   . SER D  1  335 ? -11.924 20.320  14.661  1.00 26.55  ?  335  SER D C   1 
ATOM   8595  O O   . SER D  1  335 ? -10.801 20.163  14.169  1.00 25.49  ?  335  SER D O   1 
ATOM   8596  C CB  . SER D  1  335 ? -11.367 22.427  15.856  1.00 27.41  ?  335  SER D CB  1 
ATOM   8597  O OG  . SER D  1  335 ? -11.749 23.760  16.142  1.00 28.49  ?  335  SER D OG  1 
ATOM   8598  N N   . MET D  1  336 ? -12.737 19.301  14.935  1.00 26.37  ?  336  MET D N   1 
ATOM   8599  C CA  . MET D  1  336 ? -12.272 17.924  14.823  1.00 25.39  ?  336  MET D CA  1 
ATOM   8600  C C   . MET D  1  336 ? -11.849 17.600  13.396  1.00 24.61  ?  336  MET D C   1 
ATOM   8601  O O   . MET D  1  336 ? -12.599 17.824  12.442  1.00 25.06  ?  336  MET D O   1 
ATOM   8602  C CB  . MET D  1  336 ? -13.366 16.962  15.287  1.00 26.00  ?  336  MET D CB  1 
ATOM   8603  C CG  . MET D  1  336 ? -12.976 15.489  15.235  1.00 25.12  ?  336  MET D CG  1 
ATOM   8604  S SD  . MET D  1  336 ? -11.386 15.093  16.002  1.00 23.96  ?  336  MET D SD  1 
ATOM   8605  C CE  . MET D  1  336 ? -11.569 15.827  17.627  1.00 24.80  ?  336  MET D CE  1 
ATOM   8606  N N   . ILE D  1  337 ? -10.635 17.063  13.263  1.00 24.48  ?  337  ILE D N   1 
ATOM   8607  C CA  . ILE D  1  337 ? -10.052 16.718  11.976  1.00 23.70  ?  337  ILE D CA  1 
ATOM   8608  C C   . ILE D  1  337 ? -9.736  15.232  11.882  1.00 22.97  ?  337  ILE D C   1 
ATOM   8609  O O   . ILE D  1  337 ? -10.036 14.589  10.868  1.00 22.79  ?  337  ILE D O   1 
ATOM   8610  C CB  . ILE D  1  337 ? -8.787  17.562  11.703  1.00 23.11  ?  337  ILE D CB  1 
ATOM   8611  C CG1 . ILE D  1  337 ? -9.181  18.974  11.269  1.00 23.83  ?  337  ILE D CG1 1 
ATOM   8612  C CG2 . ILE D  1  337 ? -7.907  16.908  10.646  1.00 22.15  ?  337  ILE D CG2 1 
ATOM   8613  C CD1 . ILE D  1  337 ? -8.038  19.961  11.291  1.00 23.48  ?  337  ILE D CD1 1 
ATOM   8614  N N   . ASP D  1  338 ? -9.141  14.665  12.929  1.00 23.51  ?  338  ASP D N   1 
ATOM   8615  C CA  . ASP D  1  338 ? -8.733  13.264  12.966  1.00 22.85  ?  338  ASP D CA  1 
ATOM   8616  C C   . ASP D  1  338 ? -9.418  12.612  14.165  1.00 23.35  ?  338  ASP D C   1 
ATOM   8617  O O   . ASP D  1  338 ? -8.949  12.737  15.301  1.00 23.32  ?  338  ASP D O   1 
ATOM   8618  C CB  . ASP D  1  338 ? -7.213  13.152  13.052  1.00 21.93  ?  338  ASP D CB  1 
ATOM   8619  C CG  . ASP D  1  338 ? -6.736  11.720  13.135  1.00 21.34  ?  338  ASP D CG  1 
ATOM   8620  O OD1 . ASP D  1  338 ? -7.493  10.818  12.723  1.00 21.49  ?  338  ASP D OD1 1 
ATOM   8621  O OD2 . ASP D  1  338 ? -5.603  11.496  13.608  1.00 20.76  -1 338  ASP D OD2 1 
ATOM   8622  N N   . LEU D  1  339 ? -10.522 11.912  13.911  1.00 22.89  ?  339  LEU D N   1 
ATOM   8623  C CA  . LEU D  1  339 ? -11.338 11.294  14.953  1.00 23.51  ?  339  LEU D CA  1 
ATOM   8624  C C   . LEU D  1  339 ? -11.208 9.778   14.851  1.00 23.03  ?  339  LEU D C   1 
ATOM   8625  O O   . LEU D  1  339 ? -11.659 9.176   13.871  1.00 22.98  ?  339  LEU D O   1 
ATOM   8626  C CB  . LEU D  1  339 ? -12.796 11.729  14.824  1.00 24.65  ?  339  LEU D CB  1 
ATOM   8627  C CG  . LEU D  1  339 ? -13.770 11.078  15.806  1.00 25.46  ?  339  LEU D CG  1 
ATOM   8628  C CD1 . LEU D  1  339 ? -13.328 11.326  17.240  1.00 25.59  ?  339  LEU D CD1 1 
ATOM   8629  C CD2 . LEU D  1  339 ? -15.184 11.589  15.578  1.00 26.67  ?  339  LEU D CD2 1 
ATOM   8630  N N   . GLU D  1  340 ? -10.598 9.162   15.865  1.00 23.40  ?  340  GLU D N   1 
ATOM   8631  C CA  . GLU D  1  340 ? -10.339 7.723   15.872  1.00 22.94  ?  340  GLU D CA  1 
ATOM   8632  C C   . GLU D  1  340 ? -10.721 7.146   17.227  1.00 23.42  ?  340  GLU D C   1 
ATOM   8633  O O   . GLU D  1  340 ? -10.073 7.440   18.237  1.00 23.32  ?  340  GLU D O   1 
ATOM   8634  C CB  . GLU D  1  340 ? -8.872  7.424   15.565  1.00 21.92  ?  340  GLU D CB  1 
ATOM   8635  C CG  . GLU D  1  340 ? -8.229  8.375   14.586  1.00 21.50  ?  340  GLU D CG  1 
ATOM   8636  C CD  . GLU D  1  340 ? -7.009  7.779   13.930  1.00 20.61  ?  340  GLU D CD  1 
ATOM   8637  O OE1 . GLU D  1  340 ? -6.429  6.833   14.502  1.00 20.28  ?  340  GLU D OE1 1 
ATOM   8638  O OE2 . GLU D  1  340 ? -6.638  8.246   12.835  1.00 20.31  -1 340  GLU D OE2 1 
ATOM   8639  N N   . ILE D  1  341 ? -11.765 6.320   17.246  1.00 21.51  ?  341  ILE D N   1 
ATOM   8640  C CA  . ILE D  1  341 ? -12.173 5.610   18.452  1.00 22.01  ?  341  ILE D CA  1 
ATOM   8641  C C   . ILE D  1  341 ? -12.257 4.115   18.157  1.00 21.75  ?  341  ILE D C   1 
ATOM   8642  O O   . ILE D  1  341 ? -13.035 3.390   18.786  1.00 22.38  ?  341  ILE D O   1 
ATOM   8643  C CB  . ILE D  1  341 ? -13.498 6.167   19.004  1.00 23.24  ?  341  ILE D CB  1 
ATOM   8644  C CG1 . ILE D  1  341 ? -14.483 6.457   17.872  1.00 23.70  ?  341  ILE D CG1 1 
ATOM   8645  C CG2 . ILE D  1  341 ? -13.245 7.435   19.802  1.00 23.56  ?  341  ILE D CG2 1 
ATOM   8646  C CD1 . ILE D  1  341 ? -15.911 6.640   18.343  1.00 25.03  ?  341  ILE D CD1 1 
ATOM   8647  N N   . SER D  1  342 ? -11.462 3.651   17.192  1.00 25.35  ?  342  SER D N   1 
ATOM   8648  C CA  . SER D  1  342 ? -11.504 2.264   16.749  1.00 25.10  ?  342  SER D CA  1 
ATOM   8649  C C   . SER D  1  342 ? -11.026 1.316   17.846  1.00 24.99  ?  342  SER D C   1 
ATOM   8650  O O   . SER D  1  342 ? -10.542 1.729   18.901  1.00 25.01  ?  342  SER D O   1 
ATOM   8651  C CB  . SER D  1  342 ? -10.640 2.069   15.504  1.00 24.26  ?  342  SER D CB  1 
ATOM   8652  O OG  . SER D  1  342 ? -10.974 2.996   14.495  1.00 24.40  ?  342  SER D OG  1 
ATOM   8653  N N   . GLU D  1  343 ? -11.171 0.019   17.574  1.00 25.98  ?  343  GLU D N   1 
ATOM   8654  C CA  . GLU D  1  343 ? -10.659 -1.047  18.434  1.00 25.83  ?  343  GLU D CA  1 
ATOM   8655  C C   . GLU D  1  343 ? -11.098 -0.843  19.885  1.00 26.69  ?  343  GLU D C   1 
ATOM   8656  O O   . GLU D  1  343 ? -10.293 -0.665  20.802  1.00 26.49  ?  343  GLU D O   1 
ATOM   8657  C CB  . GLU D  1  343 ? -9.138  -1.159  18.303  1.00 24.91  ?  343  GLU D CB  1 
ATOM   8658  C CG  . GLU D  1  343 ? -8.705  -1.789  16.983  1.00 24.68  ?  343  GLU D CG  1 
ATOM   8659  C CD  . GLU D  1  343 ? -7.321  -1.363  16.539  1.00 23.78  ?  343  GLU D CD  1 
ATOM   8660  O OE1 . GLU D  1  343 ? -6.331  -1.993  16.967  1.00 23.33  ?  343  GLU D OE1 1 
ATOM   8661  O OE2 . GLU D  1  343 ? -7.226  -0.402  15.748  1.00 23.89  -1 343  GLU D OE2 1 
ATOM   8662  N N   . ASN D  1  344 ? -12.414 -0.862  20.068  1.00 26.59  ?  344  ASN D N   1 
ATOM   8663  C CA  . ASN D  1  344 ? -13.042 -0.648  21.362  1.00 27.47  ?  344  ASN D CA  1 
ATOM   8664  C C   . ASN D  1  344 ? -14.245 -1.580  21.446  1.00 28.30  ?  344  ASN D C   1 
ATOM   8665  O O   . ASN D  1  344 ? -14.414 -2.482  20.619  1.00 28.07  ?  344  ASN D O   1 
ATOM   8666  C CB  . ASN D  1  344 ? -13.424 0.828   21.537  1.00 27.94  ?  344  ASN D CB  1 
ATOM   8667  C CG  . ASN D  1  344 ? -12.354 1.626   22.253  1.00 27.50  ?  344  ASN D CG  1 
ATOM   8668  O OD1 . ASN D  1  344 ? -12.211 1.537   23.471  1.00 27.83  ?  344  ASN D OD1 1 
ATOM   8669  N ND2 . ASN D  1  344 ? -11.598 2.416   21.499  1.00 26.80  ?  344  ASN D ND2 1 
ATOM   8670  N N   . LYS D  1  345 ? -15.088 -1.371  22.451  1.00 29.07  ?  345  LYS D N   1 
ATOM   8671  C CA  . LYS D  1  345 ? -16.292 -2.169  22.642  1.00 30.04  ?  345  LYS D CA  1 
ATOM   8672  C C   . LYS D  1  345 ? -17.536 -1.289  22.608  1.00 31.14  ?  345  LYS D C   1 
ATOM   8673  O O   . LYS D  1  345 ? -18.503 -1.512  23.340  1.00 32.28  ?  345  LYS D O   1 
ATOM   8674  C CB  . LYS D  1  345 ? -16.218 -2.963  23.944  1.00 30.46  ?  345  LYS D CB  1 
ATOM   8675  C CG  . LYS D  1  345 ? -15.141 -4.037  23.943  1.00 29.53  ?  345  LYS D CG  1 
ATOM   8676  C CD  . LYS D  1  345 ? -15.019 -4.707  25.301  1.00 29.98  ?  345  LYS D CD  1 
ATOM   8677  C CE  . LYS D  1  345 ? -13.823 -5.643  25.349  1.00 29.06  ?  345  LYS D CE  1 
ATOM   8678  N NZ  . LYS D  1  345 ? -13.526 -6.083  26.740  1.00 29.43  ?  345  LYS D NZ  1 
ATOM   8679  N N   . LEU D  1  346 ? -17.520 -0.279  21.742  1.00 29.37  ?  346  LEU D N   1 
ATOM   8680  C CA  . LEU D  1  346 ? -18.654 0.621   21.602  1.00 30.42  ?  346  LEU D CA  1 
ATOM   8681  C C   . LEU D  1  346 ? -19.825 -0.085  20.929  1.00 31.10  ?  346  LEU D C   1 
ATOM   8682  O O   . LEU D  1  346 ? -19.651 -1.025  20.151  1.00 30.51  ?  346  LEU D O   1 
ATOM   8683  C CB  . LEU D  1  346 ? -18.259 1.854   20.791  1.00 29.92  ?  346  LEU D CB  1 
ATOM   8684  C CG  . LEU D  1  346 ? -17.090 2.671   21.337  1.00 29.25  ?  346  LEU D CG  1 
ATOM   8685  C CD1 . LEU D  1  346 ? -16.828 3.867   20.446  1.00 28.89  ?  346  LEU D CD1 1 
ATOM   8686  C CD2 . LEU D  1  346 ? -17.369 3.113   22.764  1.00 30.15  ?  346  LEU D CD2 1 
ATOM   8687  N N   . THR D  1  347 ? -21.031 0.390   21.231  1.00 32.08  ?  347  THR D N   1 
ATOM   8688  C CA  . THR D  1  347 ? -22.260 -0.189  20.709  1.00 32.96  ?  347  THR D CA  1 
ATOM   8689  C C   . THR D  1  347 ? -23.192 0.934   20.277  1.00 33.89  ?  347  THR D C   1 
ATOM   8690  O O   . THR D  1  347 ? -22.918 2.117   20.494  1.00 33.93  ?  347  THR D O   1 
ATOM   8691  C CB  . THR D  1  347 ? -22.962 -1.078  21.746  1.00 33.99  ?  347  THR D CB  1 
ATOM   8692  O OG1 . THR D  1  347 ? -23.307 -0.292  22.894  1.00 35.02  ?  347  THR D OG1 1 
ATOM   8693  C CG2 . THR D  1  347 ? -22.066 -2.233  22.175  1.00 33.15  ?  347  THR D CG2 1 
ATOM   8694  N N   . GLY D  1  348 ? -24.300 0.551   19.649  1.00 36.76  ?  348  GLY D N   1 
ATOM   8695  C CA  . GLY D  1  348 ? -25.322 1.496   19.271  1.00 37.85  ?  348  GLY D CA  1 
ATOM   8696  C C   . GLY D  1  348 ? -25.013 2.236   17.985  1.00 37.13  ?  348  GLY D C   1 
ATOM   8697  O O   . GLY D  1  348 ? -23.983 2.017   17.340  1.00 35.75  ?  348  GLY D O   1 
ATOM   8698  N N   . PRO D  1  349 ? -25.908 3.137   17.594  1.00 35.81  ?  349  PRO D N   1 
ATOM   8699  C CA  . PRO D  1  349 ? -25.769 3.819   16.305  1.00 35.31  ?  349  PRO D CA  1 
ATOM   8700  C C   . PRO D  1  349 ? -24.821 5.008   16.373  1.00 34.62  ?  349  PRO D C   1 
ATOM   8701  O O   . PRO D  1  349 ? -24.506 5.539   17.440  1.00 34.85  ?  349  PRO D O   1 
ATOM   8702  C CB  . PRO D  1  349 ? -27.198 4.280   16.008  1.00 36.88  ?  349  PRO D CB  1 
ATOM   8703  C CG  . PRO D  1  349 ? -27.764 4.556   17.367  1.00 38.16  ?  349  PRO D CG  1 
ATOM   8704  C CD  . PRO D  1  349 ? -27.132 3.547   18.305  1.00 37.58  ?  349  PRO D CD  1 
ATOM   8705  N N   . VAL D  1  350 ? -24.361 5.410   15.196  1.00 35.05  ?  350  VAL D N   1 
ATOM   8706  C CA  . VAL D  1  350 ? -23.582 6.642   15.061  1.00 34.54  ?  350  VAL D CA  1 
ATOM   8707  C C   . VAL D  1  350 ? -24.536 7.832   15.120  1.00 35.90  ?  350  VAL D C   1 
ATOM   8708  O O   . VAL D  1  350 ? -25.585 7.807   14.457  1.00 36.79  ?  350  VAL D O   1 
ATOM   8709  C CB  . VAL D  1  350 ? -22.789 6.638   13.758  1.00 33.31  ?  350  VAL D CB  1 
ATOM   8710  C CG1 . VAL D  1  350 ? -22.110 7.983   13.547  1.00 32.96  ?  350  VAL D CG1 1 
ATOM   8711  C CG2 . VAL D  1  350 ? -21.767 5.512   13.761  1.00 32.04  ?  350  VAL D CG2 1 
ATOM   8712  N N   . PRO D  1  351 ? -24.231 8.865   15.901  1.00 33.90  ?  351  PRO D N   1 
ATOM   8713  C CA  . PRO D  1  351 ? -25.135 10.017  15.986  1.00 35.31  ?  351  PRO D CA  1 
ATOM   8714  C C   . PRO D  1  351 ? -25.216 10.784  14.675  1.00 35.20  ?  351  PRO D C   1 
ATOM   8715  O O   . PRO D  1  351 ? -24.250 10.870  13.913  1.00 33.92  ?  351  PRO D O   1 
ATOM   8716  C CB  . PRO D  1  351 ? -24.508 10.878  17.089  1.00 35.35  ?  351  PRO D CB  1 
ATOM   8717  C CG  . PRO D  1  351 ? -23.625 9.941   17.857  1.00 34.36  ?  351  PRO D CG  1 
ATOM   8718  C CD  . PRO D  1  351 ? -23.107 8.975   16.844  1.00 33.10  ?  351  PRO D CD  1 
ATOM   8719  N N   . ASP D  1  352 ? -26.401 11.350  14.421  1.00 40.96  ?  352  ASP D N   1 
ATOM   8720  C CA  . ASP D  1  352 ? -26.580 12.246  13.283  1.00 41.14  ?  352  ASP D CA  1 
ATOM   8721  C C   . ASP D  1  352 ? -25.683 13.470  13.375  1.00 40.67  ?  352  ASP D C   1 
ATOM   8722  O O   . ASP D  1  352 ? -25.392 14.093  12.348  1.00 40.28  ?  352  ASP D O   1 
ATOM   8723  C CB  . ASP D  1  352 ? -28.038 12.702  13.180  1.00 43.00  ?  352  ASP D CB  1 
ATOM   8724  C CG  . ASP D  1  352 ? -29.019 11.550  13.217  1.00 43.70  ?  352  ASP D CG  1 
ATOM   8725  O OD1 . ASP D  1  352 ? -28.963 10.748  14.173  1.00 43.65  ?  352  ASP D OD1 1 
ATOM   8726  O OD2 . ASP D  1  352 ? -29.857 11.454  12.295  1.00 44.35  -1 352  ASP D OD2 1 
ATOM   8727  N N   . SER D  1  353 ? -25.240 13.826  14.583  1.00 36.46  ?  353  SER D N   1 
ATOM   8728  C CA  . SER D  1  353 ? -24.452 15.033  14.796  1.00 36.18  ?  353  SER D CA  1 
ATOM   8729  C C   . SER D  1  353 ? -23.097 14.986  14.105  1.00 34.45  ?  353  SER D C   1 
ATOM   8730  O O   . SER D  1  353 ? -22.453 16.033  13.979  1.00 34.19  ?  353  SER D O   1 
ATOM   8731  C CB  . SER D  1  353 ? -24.255 15.268  16.293  1.00 36.61  ?  353  SER D CB  1 
ATOM   8732  O OG  . SER D  1  353 ? -23.876 14.070  16.948  1.00 35.90  ?  353  SER D OG  1 
ATOM   8733  N N   . PHE D  1  354 ? -22.648 13.810  13.660  1.00 34.92  ?  354  PHE D N   1 
ATOM   8734  C CA  . PHE D  1  354 ? -21.386 13.721  12.936  1.00 33.38  ?  354  PHE D CA  1 
ATOM   8735  C C   . PHE D  1  354 ? -21.405 14.534  11.648  1.00 33.38  ?  354  PHE D C   1 
ATOM   8736  O O   . PHE D  1  354 ? -20.337 14.850  11.113  1.00 32.32  ?  354  PHE D O   1 
ATOM   8737  C CB  . PHE D  1  354 ? -21.056 12.258  12.633  1.00 32.41  ?  354  PHE D CB  1 
ATOM   8738  C CG  . PHE D  1  354 ? -20.330 11.556  13.747  1.00 31.78  ?  354  PHE D CG  1 
ATOM   8739  C CD1 . PHE D  1  354 ? -20.634 11.826  15.072  1.00 32.57  ?  354  PHE D CD1 1 
ATOM   8740  C CD2 . PHE D  1  354 ? -19.344 10.624  13.469  1.00 30.47  ?  354  PHE D CD2 1 
ATOM   8741  C CE1 . PHE D  1  354 ? -19.967 11.183  16.097  1.00 32.04  ?  354  PHE D CE1 1 
ATOM   8742  C CE2 . PHE D  1  354 ? -18.674 9.976   14.491  1.00 29.95  ?  354  PHE D CE2 1 
ATOM   8743  C CZ  . PHE D  1  354 ? -18.986 10.256  15.807  1.00 30.72  ?  354  PHE D CZ  1 
ATOM   8744  N N   . GLY D  1  355 ? -22.591 14.876  11.138  1.00 33.70  ?  355  GLY D N   1 
ATOM   8745  C CA  . GLY D  1  355 ? -22.669 15.802  10.023  1.00 33.91  ?  355  GLY D CA  1 
ATOM   8746  C C   . GLY D  1  355 ? -22.146 17.183  10.360  1.00 34.10  ?  355  GLY D C   1 
ATOM   8747  O O   . GLY D  1  355 ? -21.701 17.914  9.471   1.00 33.79  ?  355  GLY D O   1 
ATOM   8748  N N   . LYS D  1  356 ? -22.176 17.556  11.642  1.00 32.79  ?  356  LYS D N   1 
ATOM   8749  C CA  . LYS D  1  356 ? -21.693 18.863  12.069  1.00 33.06  ?  356  LYS D CA  1 
ATOM   8750  C C   . LYS D  1  356 ? -20.175 18.961  12.072  1.00 31.55  ?  356  LYS D C   1 
ATOM   8751  O O   . LYS D  1  356 ? -19.645 20.073  12.178  1.00 31.62  ?  356  LYS D O   1 
ATOM   8752  C CB  . LYS D  1  356 ? -22.221 19.193  13.469  1.00 34.19  ?  356  LYS D CB  1 
ATOM   8753  C CG  . LYS D  1  356 ? -23.722 19.397  13.548  1.00 35.98  ?  356  LYS D CG  1 
ATOM   8754  C CD  . LYS D  1  356 ? -24.141 19.784  14.957  1.00 37.13  ?  356  LYS D CD  1 
ATOM   8755  C CE  . LYS D  1  356 ? -25.492 20.475  14.968  1.00 39.12  ?  356  LYS D CE  1 
ATOM   8756  N NZ  . LYS D  1  356 ? -25.789 21.092  16.289  1.00 40.32  ?  356  LYS D NZ  1 
ATOM   8757  N N   . LEU D  1  357 ? -19.466 17.837  11.965  1.00 32.65  ?  357  LEU D N   1 
ATOM   8758  C CA  . LEU D  1  357 ? -18.008 17.838  11.849  1.00 31.24  ?  357  LEU D CA  1 
ATOM   8759  C C   . LEU D  1  357 ? -17.652 18.219  10.414  1.00 30.76  ?  357  LEU D C   1 
ATOM   8760  O O   . LEU D  1  357 ? -17.428 17.373  9.545   1.00 30.00  ?  357  LEU D O   1 
ATOM   8761  C CB  . LEU D  1  357 ? -17.436 16.480  12.235  1.00 30.21  ?  357  LEU D CB  1 
ATOM   8762  C CG  . LEU D  1  357 ? -17.944 15.870  13.543  1.00 30.75  ?  357  LEU D CG  1 
ATOM   8763  C CD1 . LEU D  1  357 ? -17.482 14.428  13.675  1.00 29.80  ?  357  LEU D CD1 1 
ATOM   8764  C CD2 . LEU D  1  357 ? -17.483 16.693  14.736  1.00 31.01  ?  357  LEU D CD2 1 
ATOM   8765  N N   . THR D  1  358 ? -17.597 19.528  10.167  1.00 31.04  ?  358  THR D N   1 
ATOM   8766  C CA  . THR D  1  358 ? -17.413 20.035  8.812   1.00 30.86  ?  358  THR D CA  1 
ATOM   8767  C C   . THR D  1  358 ? -15.969 19.965  8.331   1.00 29.46  ?  358  THR D C   1 
ATOM   8768  O O   . THR D  1  358 ? -15.729 20.128  7.129   1.00 29.15  ?  358  THR D O   1 
ATOM   8769  C CB  . THR D  1  358 ? -17.908 21.481  8.716   1.00 32.06  ?  358  THR D CB  1 
ATOM   8770  O OG1 . THR D  1  358 ? -17.351 22.251  9.788   1.00 32.17  ?  358  THR D OG1 1 
ATOM   8771  C CG2 . THR D  1  358 ? -19.426 21.530  8.800   1.00 33.56  ?  358  THR D CG2 1 
ATOM   8772  N N   . ALA D  1  359 ? -15.010 19.722  9.223   1.00 28.69  ?  359  ALA D N   1 
ATOM   8773  C CA  . ALA D  1  359 ? -13.599 19.659  8.861   1.00 27.45  ?  359  ALA D CA  1 
ATOM   8774  C C   . ALA D  1  359 ? -13.016 18.265  9.057   1.00 26.41  ?  359  ALA D C   1 
ATOM   8775  O O   . ALA D  1  359 ? -11.791 18.109  9.105   1.00 25.44  ?  359  ALA D O   1 
ATOM   8776  C CB  . ALA D  1  359 ? -12.799 20.686  9.662   1.00 27.43  ?  359  ALA D CB  1 
ATOM   8777  N N   . LEU D  1  360 ? -13.870 17.252  9.171   1.00 26.49  ?  360  LEU D N   1 
ATOM   8778  C CA  . LEU D  1  360 ? -13.408 15.894  9.419   1.00 25.65  ?  360  LEU D CA  1 
ATOM   8779  C C   . LEU D  1  360 ? -12.672 15.340  8.204   1.00 24.72  ?  360  LEU D C   1 
ATOM   8780  O O   . LEU D  1  360 ? -13.105 15.511  7.061   1.00 24.94  ?  360  LEU D O   1 
ATOM   8781  C CB  . LEU D  1  360 ? -14.593 14.997  9.773   1.00 26.29  ?  360  LEU D CB  1 
ATOM   8782  C CG  . LEU D  1  360 ? -14.286 13.640  10.405  1.00 25.70  ?  360  LEU D CG  1 
ATOM   8783  C CD1 . LEU D  1  360 ? -13.585 13.820  11.741  1.00 25.49  ?  360  LEU D CD1 1 
ATOM   8784  C CD2 . LEU D  1  360 ? -15.566 12.837  10.573  1.00 26.47  ?  360  LEU D CD2 1 
ATOM   8785  N N   . GLU D  1  361 ? -11.553 14.672  8.460   1.00 26.50  ?  361  GLU D N   1 
ATOM   8786  C CA  . GLU D  1  361 ? -10.740 14.059  7.415   1.00 25.63  ?  361  GLU D CA  1 
ATOM   8787  C C   . GLU D  1  361 ? -10.496 12.577  7.650   1.00 25.08  ?  361  GLU D C   1 
ATOM   8788  O O   . GLU D  1  361 ? -10.446 11.808  6.687   1.00 24.75  ?  361  GLU D O   1 
ATOM   8789  C CB  . GLU D  1  361 ? -9.394  14.795  7.302   1.00 25.00  ?  361  GLU D CB  1 
ATOM   8790  C CG  . GLU D  1  361 ? -9.517  16.262  6.931   1.00 25.51  ?  361  GLU D CG  1 
ATOM   8791  C CD  . GLU D  1  361 ? -8.174  16.908  6.653   1.00 24.90  ?  361  GLU D CD  1 
ATOM   8792  O OE1 . GLU D  1  361 ? -7.221  16.177  6.310   1.00 24.07  ?  361  GLU D OE1 1 
ATOM   8793  O OE2 . GLU D  1  361 ? -8.071  18.146  6.781   1.00 25.27  -1 361  GLU D OE2 1 
ATOM   8794  N N   . TRP D  1  362 ? -10.342 12.158  8.904   1.00 25.44  ?  362  TRP D N   1 
ATOM   8795  C CA  . TRP D  1  362 ? -10.212 10.753  9.267   1.00 25.06  ?  362  TRP D CA  1 
ATOM   8796  C C   . TRP D  1  362 ? -11.301 10.412  10.271  1.00 25.82  ?  362  TRP D C   1 
ATOM   8797  O O   . TRP D  1  362 ? -11.373 11.024  11.343  1.00 26.19  ?  362  TRP D O   1 
ATOM   8798  C CB  . TRP D  1  362 ? -8.836  10.449  9.865   1.00 24.27  ?  362  TRP D CB  1 
ATOM   8799  C CG  . TRP D  1  362 ? -7.693  10.588  8.912   1.00 23.55  ?  362  TRP D CG  1 
ATOM   8800  C CD1 . TRP D  1  362 ? -7.192  9.626   8.086   1.00 23.28  ?  362  TRP D CD1 1 
ATOM   8801  C CD2 . TRP D  1  362 ? -6.888  11.753  8.705   1.00 23.50  ?  362  TRP D CD2 1 
ATOM   8802  N NE1 . TRP D  1  362 ? -6.134  10.124  7.365   1.00 22.88  ?  362  TRP D NE1 1 
ATOM   8803  C CE2 . TRP D  1  362 ? -5.926  11.428  7.729   1.00 22.71  ?  362  TRP D CE2 1 
ATOM   8804  C CE3 . TRP D  1  362 ? -6.892  13.042  9.246   1.00 23.87  ?  362  TRP D CE3 1 
ATOM   8805  C CZ2 . TRP D  1  362 ? -4.978  12.345  7.282   1.00 22.42  ?  362  TRP D CZ2 1 
ATOM   8806  C CZ3 . TRP D  1  362 ? -5.951  13.950  8.802   1.00 23.38  ?  362  TRP D CZ3 1 
ATOM   8807  C CH2 . TRP D  1  362 ? -5.006  13.598  7.830   1.00 22.74  ?  362  TRP D CH2 1 
ATOM   8808  N N   . LEU D  1  363 ? -12.144 9.443   9.931   1.00 23.69  ?  363  LEU D N   1 
ATOM   8809  C CA  . LEU D  1  363 ? -13.135 8.906   10.861  1.00 24.39  ?  363  LEU D CA  1 
ATOM   8810  C C   . LEU D  1  363 ? -12.852 7.416   11.008  1.00 23.92  ?  363  LEU D C   1 
ATOM   8811  O O   . LEU D  1  363 ? -13.162 6.624   10.112  1.00 23.82  ?  363  LEU D O   1 
ATOM   8812  C CB  . LEU D  1  363 ? -14.559 9.163   10.379  1.00 25.38  ?  363  LEU D CB  1 
ATOM   8813  C CG  . LEU D  1  363 ? -15.648 8.576   11.282  1.00 26.23  ?  363  LEU D CG  1 
ATOM   8814  C CD1 . LEU D  1  363 ? -15.589 9.202   12.668  1.00 26.65  ?  363  LEU D CD1 1 
ATOM   8815  C CD2 . LEU D  1  363 ? -17.026 8.759   10.669  1.00 27.22  ?  363  LEU D CD2 1 
ATOM   8816  N N   . PHE D  1  364 ? -12.262 7.041   12.140  1.00 23.50  ?  364  PHE D N   1 
ATOM   8817  C CA  . PHE D  1  364 ? -11.902 5.655   12.429  1.00 23.09  ?  364  PHE D CA  1 
ATOM   8818  C C   . PHE D  1  364 ? -12.928 5.094   13.410  1.00 23.87  ?  364  PHE D C   1 
ATOM   8819  O O   . PHE D  1  364 ? -12.881 5.382   14.609  1.00 24.15  ?  364  PHE D O   1 
ATOM   8820  C CB  . PHE D  1  364 ? -10.487 5.577   12.991  1.00 22.31  ?  364  PHE D CB  1 
ATOM   8821  C CG  . PHE D  1  364 ? -9.426  5.342   11.952  1.00 21.48  ?  364  PHE D CG  1 
ATOM   8822  C CD1 . PHE D  1  364 ? -8.976  6.379   11.153  1.00 21.25  ?  364  PHE D CD1 1 
ATOM   8823  C CD2 . PHE D  1  364 ? -8.868  4.085   11.788  1.00 21.01  ?  364  PHE D CD2 1 
ATOM   8824  C CE1 . PHE D  1  364 ? -7.996  6.163   10.200  1.00 20.58  ?  364  PHE D CE1 1 
ATOM   8825  C CE2 . PHE D  1  364 ? -7.888  3.863   10.839  1.00 20.36  ?  364  PHE D CE2 1 
ATOM   8826  C CZ  . PHE D  1  364 ? -7.452  4.903   10.044  1.00 20.15  ?  364  PHE D CZ  1 
ATOM   8827  N N   . LEU D  1  365 ? -13.857 4.288   12.896  1.00 24.68  ?  365  LEU D N   1 
ATOM   8828  C CA  . LEU D  1  365 ? -14.862 3.627   13.720  1.00 25.47  ?  365  LEU D CA  1 
ATOM   8829  C C   . LEU D  1  365 ? -14.739 2.111   13.674  1.00 25.16  ?  365  LEU D C   1 
ATOM   8830  O O   . LEU D  1  365 ? -15.578 1.411   14.256  1.00 25.82  ?  365  LEU D O   1 
ATOM   8831  C CB  . LEU D  1  365 ? -16.272 4.040   13.288  1.00 26.48  ?  365  LEU D CB  1 
ATOM   8832  C CG  . LEU D  1  365 ? -16.660 5.508   13.442  1.00 27.08  ?  365  LEU D CG  1 
ATOM   8833  C CD1 . LEU D  1  365 ? -18.099 5.720   13.003  1.00 28.18  ?  365  LEU D CD1 1 
ATOM   8834  C CD2 . LEU D  1  365 ? -16.470 5.961   14.873  1.00 27.40  ?  365  LEU D CD2 1 
ATOM   8835  N N   . ARG D  1  366 ? -13.715 1.589   13.006  1.00 24.57  ?  366  ARG D N   1 
ATOM   8836  C CA  . ARG D  1  366 ? -13.606 0.160   12.763  1.00 24.31  ?  366  ARG D CA  1 
ATOM   8837  C C   . ARG D  1  366 ? -13.380 -0.608  14.062  1.00 24.38  ?  366  ARG D C   1 
ATOM   8838  O O   . ARG D  1  366 ? -13.008 -0.046  15.095  1.00 24.42  ?  366  ARG D O   1 
ATOM   8839  C CB  . ARG D  1  366 ? -12.471 -0.122  11.781  1.00 23.40  ?  366  ARG D CB  1 
ATOM   8840  C CG  . ARG D  1  366 ? -11.175 0.607   12.100  1.00 22.75  ?  366  ARG D CG  1 
ATOM   8841  C CD  . ARG D  1  366 ? -10.020 0.079   11.261  1.00 21.97  ?  366  ARG D CD  1 
ATOM   8842  N NE  . ARG D  1  366 ? -10.122 -1.355  11.016  1.00 21.94  ?  366  ARG D NE  1 
ATOM   8843  C CZ  . ARG D  1  366 ? -9.778  -2.291  11.891  1.00 21.87  ?  366  ARG D CZ  1 
ATOM   8844  N NH1 . ARG D  1  366 ? -9.276  -1.981  13.075  1.00 21.80  ?  366  ARG D NH1 1 
ATOM   8845  N NH2 . ARG D  1  366 ? -9.937  -3.571  11.567  1.00 21.90  ?  366  ARG D NH2 1 
ATOM   8846  N N   . ASP D  1  367 ? -13.619 -1.920  13.992  1.00 25.93  ?  367  ASP D N   1 
ATOM   8847  C CA  . ASP D  1  367 ? -13.360 -2.845  15.095  1.00 25.97  ?  367  ASP D CA  1 
ATOM   8848  C C   . ASP D  1  367 ? -14.123 -2.442  16.360  1.00 26.94  ?  367  ASP D C   1 
ATOM   8849  O O   . ASP D  1  367 ? -13.543 -2.125  17.400  1.00 26.71  ?  367  ASP D O   1 
ATOM   8850  C CB  . ASP D  1  367 ? -11.859 -2.967  15.369  1.00 25.11  ?  367  ASP D CB  1 
ATOM   8851  C CG  . ASP D  1  367 ? -11.493 -4.295  15.997  1.00 25.03  ?  367  ASP D CG  1 
ATOM   8852  O OD1 . ASP D  1  367 ? -12.374 -4.918  16.630  1.00 25.69  ?  367  ASP D OD1 1 
ATOM   8853  O OD2 . ASP D  1  367 ? -10.326 -4.717  15.861  1.00 25.01  -1 367  ASP D OD2 1 
ATOM   8854  N N   . ASN D  1  368 ? -15.446 -2.464  16.249  1.00 27.88  ?  368  ASN D N   1 
ATOM   8855  C CA  . ASN D  1  368 ? -16.320 -2.121  17.361  1.00 28.86  ?  368  ASN D CA  1 
ATOM   8856  C C   . ASN D  1  368 ? -17.584 -2.965  17.238  1.00 29.74  ?  368  ASN D C   1 
ATOM   8857  O O   . ASN D  1  368 ? -17.629 -3.936  16.477  1.00 29.68  ?  368  ASN D O   1 
ATOM   8858  C CB  . ASN D  1  368 ? -16.622 -0.617  17.367  1.00 29.23  ?  368  ASN D CB  1 
ATOM   8859  C CG  . ASN D  1  368 ? -15.678 0.163   18.258  1.00 28.87  ?  368  ASN D CG  1 
ATOM   8860  O OD1 . ASN D  1  368 ? -15.799 0.140   19.481  1.00 29.36  ?  368  ASN D OD1 1 
ATOM   8861  N ND2 . ASN D  1  368 ? -14.731 0.864   17.645  1.00 28.05  ?  368  ASN D ND2 1 
ATOM   8862  N N   . GLN D  1  369 ? -18.612 -2.603  18.001  1.00 32.43  ?  369  GLN D N   1 
ATOM   8863  C CA  . GLN D  1  369 ? -19.880 -3.322  17.992  1.00 33.43  ?  369  GLN D CA  1 
ATOM   8864  C C   . GLN D  1  369 ? -21.041 -2.383  17.684  1.00 34.43  ?  369  GLN D C   1 
ATOM   8865  O O   . GLN D  1  369 ? -22.171 -2.610  18.123  1.00 35.94  ?  369  GLN D O   1 
ATOM   8866  C CB  . GLN D  1  369 ? -20.101 -4.043  19.321  1.00 34.05  ?  369  GLN D CB  1 
ATOM   8867  C CG  . GLN D  1  369 ? -19.203 -5.253  19.518  1.00 33.28  ?  369  GLN D CG  1 
ATOM   8868  C CD  . GLN D  1  369 ? -19.261 -5.800  20.930  1.00 34.17  ?  369  GLN D CD  1 
ATOM   8869  O OE1 . GLN D  1  369 ? -19.895 -5.215  21.809  1.00 35.64  ?  369  GLN D OE1 1 
ATOM   8870  N NE2 . GLN D  1  369 ? -18.594 -6.925  21.156  1.00 34.45  ?  369  GLN D NE2 1 
ATOM   8871  N N   . LEU D  1  370 ? -20.768 -1.325  16.925  1.00 32.06  ?  370  LEU D N   1 
ATOM   8872  C CA  . LEU D  1  370 ? -21.807 -0.390  16.532  1.00 32.99  ?  370  LEU D CA  1 
ATOM   8873  C C   . LEU D  1  370 ? -22.770 -1.056  15.553  1.00 33.45  ?  370  LEU D C   1 
ATOM   8874  O O   . LEU D  1  370 ? -22.454 -2.065  14.916  1.00 32.81  ?  370  LEU D O   1 
ATOM   8875  C CB  . LEU D  1  370 ? -21.190 0.860   15.906  1.00 32.40  ?  370  LEU D CB  1 
ATOM   8876  C CG  . LEU D  1  370 ? -20.085 1.531   16.725  1.00 31.79  ?  370  LEU D CG  1 
ATOM   8877  C CD1 . LEU D  1  370 ? -19.272 2.478   15.857  1.00 30.95  ?  370  LEU D CD1 1 
ATOM   8878  C CD2 . LEU D  1  370 ? -20.672 2.261   17.922  1.00 32.87  ?  370  LEU D CD2 1 
ATOM   8879  N N   . SER D  1  371 ? -23.959 -0.472  15.432  1.00 34.03  ?  371  SER D N   1 
ATOM   8880  C CA  . SER D  1  371 ? -25.042 -1.105  14.695  1.00 34.73  ?  371  SER D CA  1 
ATOM   8881  C C   . SER D  1  371 ? -25.976 -0.033  14.150  1.00 35.67  ?  371  SER D C   1 
ATOM   8882  O O   . SER D  1  371 ? -25.758 1.167   14.335  1.00 35.74  ?  371  SER D O   1 
ATOM   8883  C CB  . SER D  1  371 ? -25.795 -2.099  15.585  1.00 35.67  ?  371  SER D CB  1 
ATOM   8884  O OG  . SER D  1  371 ? -26.343 -1.451  16.721  1.00 36.78  ?  371  SER D OG  1 
ATOM   8885  N N   . GLY D  1  372 ? -27.028 -0.484  13.469  1.00 36.36  ?  372  GLY D N   1 
ATOM   8886  C CA  . GLY D  1  372 ? -28.012 0.404   12.901  1.00 37.38  ?  372  GLY D CA  1 
ATOM   8887  C C   . GLY D  1  372 ? -27.598 0.916   11.539  1.00 36.59  ?  372  GLY D C   1 
ATOM   8888  O O   . GLY D  1  372 ? -26.575 0.508   10.978  1.00 35.26  ?  372  GLY D O   1 
ATOM   8889  N N   . PRO D  1  373 ? -28.391 1.822   10.975  1.00 35.96  ?  373  PRO D N   1 
ATOM   8890  C CA  . PRO D  1  373 ? -28.028 2.419   9.689   1.00 35.31  ?  373  PRO D CA  1 
ATOM   8891  C C   . PRO D  1  373 ? -26.909 3.435   9.852   1.00 34.43  ?  373  PRO D C   1 
ATOM   8892  O O   . PRO D  1  373 ? -26.633 3.935   10.945  1.00 34.59  ?  373  PRO D O   1 
ATOM   8893  C CB  . PRO D  1  373 ? -29.326 3.090   9.235   1.00 36.77  ?  373  PRO D CB  1 
ATOM   8894  C CG  . PRO D  1  373 ? -29.993 3.470   10.516  1.00 38.03  ?  373  PRO D CG  1 
ATOM   8895  C CD  . PRO D  1  373 ? -29.646 2.382   11.509  1.00 37.67  ?  373  PRO D CD  1 
ATOM   8896  N N   . ILE D  1  374 ? -26.253 3.731   8.737   1.00 34.59  ?  374  ILE D N   1 
ATOM   8897  C CA  . ILE D  1  374 ? -25.208 4.747   8.692   1.00 33.79  ?  374  ILE D CA  1 
ATOM   8898  C C   . ILE D  1  374 ? -25.875 6.084   8.384   1.00 34.75  ?  374  ILE D C   1 
ATOM   8899  O O   . ILE D  1  374 ? -26.471 6.228   7.304   1.00 35.14  ?  374  ILE D O   1 
ATOM   8900  C CB  . ILE D  1  374 ? -24.138 4.410   7.647   1.00 32.41  ?  374  ILE D CB  1 
ATOM   8901  C CG1 . ILE D  1  374 ? -23.242 3.280   8.153   1.00 31.43  ?  374  ILE D CG1 1 
ATOM   8902  C CG2 . ILE D  1  374 ? -23.294 5.634   7.337   1.00 31.86  ?  374  ILE D CG2 1 
ATOM   8903  C CD1 . ILE D  1  374 ? -22.597 3.567   9.488   1.00 31.21  ?  374  ILE D CD1 1 
ATOM   8904  N N   . PRO D  1  375 ? -25.818 7.060   9.284   1.00 35.11  ?  375  PRO D N   1 
ATOM   8905  C CA  . PRO D  1  375 ? -26.439 8.361   9.016   1.00 36.12  ?  375  PRO D CA  1 
ATOM   8906  C C   . PRO D  1  375 ? -25.753 9.057   7.857   1.00 35.34  ?  375  PRO D C   1 
ATOM   8907  O O   . PRO D  1  375 ? -24.527 8.953   7.698   1.00 34.01  ?  375  PRO D O   1 
ATOM   8908  C CB  . PRO D  1  375 ? -26.242 9.136   10.331  1.00 36.54  ?  375  PRO D CB  1 
ATOM   8909  C CG  . PRO D  1  375 ? -25.806 8.121   11.340  1.00 36.02  ?  375  PRO D CG  1 
ATOM   8910  C CD  . PRO D  1  375 ? -25.144 7.018   10.590  1.00 34.76  ?  375  PRO D CD  1 
ATOM   8911  N N   . PRO D  1  376 ? -26.508 9.776   7.022   1.00 38.51  ?  376  PRO D N   1 
ATOM   8912  C CA  . PRO D  1  376 ? -25.885 10.457  5.876   1.00 37.85  ?  376  PRO D CA  1 
ATOM   8913  C C   . PRO D  1  376 ? -24.846 11.483  6.280   1.00 37.25  ?  376  PRO D C   1 
ATOM   8914  O O   . PRO D  1  376 ? -23.998 11.845  5.455   1.00 36.38  ?  376  PRO D O   1 
ATOM   8915  C CB  . PRO D  1  376 ? -27.075 11.115  5.163   1.00 39.23  ?  376  PRO D CB  1 
ATOM   8916  C CG  . PRO D  1  376 ? -28.285 10.384  5.661   1.00 40.38  ?  376  PRO D CG  1 
ATOM   8917  C CD  . PRO D  1  376 ? -27.964 9.986   7.068   1.00 40.19  ?  376  PRO D CD  1 
ATOM   8918  N N   . GLY D  1  377 ? -24.871 11.948  7.528   1.00 38.14  ?  377  GLY D N   1 
ATOM   8919  C CA  . GLY D  1  377 ? -23.925 12.941  7.995   1.00 37.67  ?  377  GLY D CA  1 
ATOM   8920  C C   . GLY D  1  377 ? -22.525 12.434  8.254   1.00 36.12  ?  377  GLY D C   1 
ATOM   8921  O O   . GLY D  1  377 ? -21.622 13.251  8.459   1.00 35.60  ?  377  GLY D O   1 
ATOM   8922  N N   . ILE D  1  378 ? -22.319 11.115  8.251   1.00 35.13  ?  378  ILE D N   1 
ATOM   8923  C CA  . ILE D  1  378 ? -20.982 10.573  8.492   1.00 33.73  ?  378  ILE D CA  1 
ATOM   8924  C C   . ILE D  1  378 ? -20.022 11.028  7.400   1.00 32.80  ?  378  ILE D C   1 
ATOM   8925  O O   . ILE D  1  378 ? -18.908 11.488  7.677   1.00 32.03  ?  378  ILE D O   1 
ATOM   8926  C CB  . ILE D  1  378 ? -21.033 9.037   8.593   1.00 33.31  ?  378  ILE D CB  1 
ATOM   8927  C CG1 . ILE D  1  378 ? -21.402 8.601   10.010  1.00 33.84  ?  378  ILE D CG1 1 
ATOM   8928  C CG2 . ILE D  1  378 ? -19.701 8.423   8.191   1.00 31.88  ?  378  ILE D CG2 1 
ATOM   8929  C CD1 . ILE D  1  378 ? -21.516 7.100   10.165  1.00 33.56  ?  378  ILE D CD1 1 
ATOM   8930  N N   . ALA D  1  379 ? -20.446 10.919  6.142   1.00 36.10  ?  379  ALA D N   1 
ATOM   8931  C CA  . ALA D  1  379 ? -19.642 11.340  5.005   1.00 35.37  ?  379  ALA D CA  1 
ATOM   8932  C C   . ALA D  1  379 ? -20.008 12.740  4.524   1.00 36.17  ?  379  ALA D C   1 
ATOM   8933  O O   . ALA D  1  379 ? -19.652 13.118  3.403   1.00 36.66  ?  379  ALA D O   1 
ATOM   8934  C CB  . ALA D  1  379 ? -19.775 10.331  3.866   1.00 35.00  ?  379  ALA D CB  1 
ATOM   8935  N N   . ASN D  1  380 ? -20.708 13.515  5.356   1.00 38.47  ?  380  ASN D N   1 
ATOM   8936  C CA  . ASN D  1  380 ? -21.133 14.857  4.976   1.00 39.36  ?  380  ASN D CA  1 
ATOM   8937  C C   . ASN D  1  380 ? -19.957 15.798  4.755   1.00 38.64  ?  380  ASN D C   1 
ATOM   8938  O O   . ASN D  1  380 ? -20.093 16.778  4.013   1.00 39.15  ?  380  ASN D O   1 
ATOM   8939  C CB  . ASN D  1  380 ? -22.063 15.423  6.053   1.00 40.67  ?  380  ASN D CB  1 
ATOM   8940  C CG  . ASN D  1  380 ? -22.849 16.635  5.583   1.00 41.94  ?  380  ASN D CG  1 
ATOM   8941  O OD1 . ASN D  1  380 ? -23.179 16.759  4.403   1.00 42.49  ?  380  ASN D OD1 1 
ATOM   8942  N ND2 . ASN D  1  380 ? -23.159 17.534  6.516   1.00 42.87  ?  380  ASN D ND2 1 
ATOM   8943  N N   . SER D  1  381 ? -18.810 15.527  5.375   1.00 34.29  ?  381  SER D N   1 
ATOM   8944  C CA  . SER D  1  381 ? -17.669 16.428  5.271   1.00 33.67  ?  381  SER D CA  1 
ATOM   8945  C C   . SER D  1  381 ? -17.095 16.412  3.859   1.00 33.01  ?  381  SER D C   1 
ATOM   8946  O O   . SER D  1  381 ? -16.834 15.346  3.293   1.00 32.31  ?  381  SER D O   1 
ATOM   8947  C CB  . SER D  1  381 ? -16.593 16.036  6.282   1.00 32.73  ?  381  SER D CB  1 
ATOM   8948  O OG  . SER D  1  381 ? -15.370 16.697  6.006   1.00 31.97  ?  381  SER D OG  1 
ATOM   8949  N N   . THR D  1  382 ? -16.890 17.605  3.295   1.00 33.69  ?  382  THR D N   1 
ATOM   8950  C CA  . THR D  1  382 ? -16.281 17.715  1.976   1.00 33.14  ?  382  THR D CA  1 
ATOM   8951  C C   . THR D  1  382 ? -14.787 17.419  2.001   1.00 31.85  ?  382  THR D C   1 
ATOM   8952  O O   . THR D  1  382 ? -14.204 17.150  0.945   1.00 31.29  ?  382  THR D O   1 
ATOM   8953  C CB  . THR D  1  382 ? -16.522 19.109  1.394   1.00 33.96  ?  382  THR D CB  1 
ATOM   8954  O OG1 . THR D  1  382 ? -16.143 20.103  2.354   1.00 34.19  ?  382  THR D OG1 1 
ATOM   8955  C CG2 . THR D  1  382 ? -17.991 19.291  1.038   1.00 35.33  ?  382  THR D CG2 1 
ATOM   8956  N N   . GLU D  1  383 ? -14.160 17.454  3.175   1.00 32.78  ?  383  GLU D N   1 
ATOM   8957  C CA  . GLU D  1  383 ? -12.736 17.184  3.316   1.00 31.73  ?  383  GLU D CA  1 
ATOM   8958  C C   . GLU D  1  383 ? -12.455 15.773  3.815   1.00 31.16  ?  383  GLU D C   1 
ATOM   8959  O O   . GLU D  1  383 ? -11.300 15.450  4.111   1.00 30.08  ?  383  GLU D O   1 
ATOM   8960  C CB  . GLU D  1  383 ? -12.094 18.207  4.255   1.00 31.66  ?  383  GLU D CB  1 
ATOM   8961  C CG  . GLU D  1  383 ? -12.468 19.648  3.953   1.00 32.95  ?  383  GLU D CG  1 
ATOM   8962  C CD  . GLU D  1  383 ? -12.047 20.077  2.560   1.00 33.04  ?  383  GLU D CD  1 
ATOM   8963  O OE1 . GLU D  1  383 ? -10.829 20.235  2.329   1.00 32.28  ?  383  GLU D OE1 1 
ATOM   8964  O OE2 . GLU D  1  383 ? -12.931 20.252  1.696   1.00 33.99  -1 383  GLU D OE2 1 
ATOM   8965  N N   . LEU D  1  384 ? -13.482 14.933  3.923   1.00 26.53  ?  384  LEU D N   1 
ATOM   8966  C CA  . LEU D  1  384 ? -13.285 13.553  4.347   1.00 25.97  ?  384  LEU D CA  1 
ATOM   8967  C C   . LEU D  1  384 ? -12.418 12.807  3.341   1.00 25.09  ?  384  LEU D C   1 
ATOM   8968  O O   . LEU D  1  384 ? -12.631 12.899  2.128   1.00 25.19  ?  384  LEU D O   1 
ATOM   8969  C CB  . LEU D  1  384 ? -14.631 12.849  4.509   1.00 26.71  ?  384  LEU D CB  1 
ATOM   8970  C CG  . LEU D  1  384 ? -14.587 11.525  5.275   1.00 26.36  ?  384  LEU D CG  1 
ATOM   8971  C CD1 . LEU D  1  384 ? -14.459 11.778  6.771   1.00 26.52  ?  384  LEU D CD1 1 
ATOM   8972  C CD2 . LEU D  1  384 ? -15.811 10.677  4.970   1.00 26.97  ?  384  LEU D CD2 1 
ATOM   8973  N N   . THR D  1  385 ? -11.433 12.071  3.851   1.00 26.20  ?  385  THR D N   1 
ATOM   8974  C CA  . THR D  1  385 ? -10.541 11.288  3.007   1.00 25.43  ?  385  THR D CA  1 
ATOM   8975  C C   . THR D  1  385 ? -10.412 9.832   3.424   1.00 25.05  ?  385  THR D C   1 
ATOM   8976  O O   . THR D  1  385 ? -10.049 9.005   2.580   1.00 24.65  ?  385  THR D O   1 
ATOM   8977  C CB  . THR D  1  385 ? -9.136  11.913  2.974   1.00 24.78  ?  385  THR D CB  1 
ATOM   8978  O OG1 . THR D  1  385 ? -8.661  12.098  4.313   1.00 24.63  ?  385  THR D OG1 1 
ATOM   8979  C CG2 . THR D  1  385 ? -9.158  13.257  2.257   1.00 25.36  ?  385  THR D CG2 1 
ATOM   8980  N N   . VAL D  1  386 ? -10.685 9.485   4.681   1.00 24.04  ?  386  VAL D N   1 
ATOM   8981  C CA  . VAL D  1  386 ? -10.605 8.110   5.159   1.00 23.77  ?  386  VAL D CA  1 
ATOM   8982  C C   . VAL D  1  386 ? -11.841 7.810   5.995   1.00 24.50  ?  386  VAL D C   1 
ATOM   8983  O O   . VAL D  1  386 ? -12.153 8.548   6.936   1.00 24.93  ?  386  VAL D O   1 
ATOM   8984  C CB  . VAL D  1  386 ? -9.326  7.861   5.980   1.00 23.09  ?  386  VAL D CB  1 
ATOM   8985  C CG1 . VAL D  1  386 ? -9.296  6.433   6.493   1.00 22.90  ?  386  VAL D CG1 1 
ATOM   8986  C CG2 . VAL D  1  386 ? -8.099  8.137   5.135   1.00 22.46  ?  386  VAL D CG2 1 
ATOM   8987  N N   . LEU D  1  387 ? -12.539 6.727   5.652   1.00 24.21  ?  387  LEU D N   1 
ATOM   8988  C CA  . LEU D  1  387 ? -13.738 6.285   6.366   1.00 24.96  ?  387  LEU D CA  1 
ATOM   8989  C C   . LEU D  1  387 ? -13.598 4.793   6.661   1.00 24.66  ?  387  LEU D C   1 
ATOM   8990  O O   . LEU D  1  387 ? -13.962 3.949   5.836   1.00 24.68  ?  387  LEU D O   1 
ATOM   8991  C CB  . LEU D  1  387 ? -14.996 6.591   5.558   1.00 25.75  ?  387  LEU D CB  1 
ATOM   8992  C CG  . LEU D  1  387 ? -16.321 6.225   6.227   1.00 26.69  ?  387  LEU D CG  1 
ATOM   8993  C CD1 . LEU D  1  387 ? -16.430 6.899   7.581   1.00 27.10  ?  387  LEU D CD1 1 
ATOM   8994  C CD2 . LEU D  1  387 ? -17.491 6.615   5.342   1.00 27.51  ?  387  LEU D CD2 1 
ATOM   8995  N N   . GLN D  1  388 ? -13.072 4.471   7.841   1.00 24.97  ?  388  GLN D N   1 
ATOM   8996  C CA  . GLN D  1  388 ? -12.880 3.090   8.274   1.00 24.88  ?  388  GLN D CA  1 
ATOM   8997  C C   . GLN D  1  388 ? -14.076 2.666   9.120   1.00 25.57  ?  388  GLN D C   1 
ATOM   8998  O O   . GLN D  1  388 ? -14.280 3.183   10.223  1.00 25.93  ?  388  GLN D O   1 
ATOM   8999  C CB  . GLN D  1  388 ? -11.574 2.940   9.051   1.00 24.06  ?  388  GLN D CB  1 
ATOM   9000  C CG  . GLN D  1  388 ? -10.376 3.543   8.348   1.00 23.36  ?  388  GLN D CG  1 
ATOM   9001  C CD  . GLN D  1  388 ? -9.703  2.561   7.411   1.00 22.84  ?  388  GLN D CD  1 
ATOM   9002  O OE1 . GLN D  1  388 ? -9.720  1.353   7.645   1.00 22.82  ?  388  GLN D OE1 1 
ATOM   9003  N NE2 . GLN D  1  388 ? -9.110  3.076   6.340   1.00 22.51  ?  388  GLN D NE2 1 
ATOM   9004  N N   . LEU D  1  389 ? -14.859 1.718   8.603   1.00 26.18  ?  389  LEU D N   1 
ATOM   9005  C CA  . LEU D  1  389 ? -16.066 1.259   9.272   1.00 27.19  ?  389  LEU D CA  1 
ATOM   9006  C C   . LEU D  1  389 ? -16.144 -0.255  9.418   1.00 27.08  ?  389  LEU D C   1 
ATOM   9007  O O   . LEU D  1  389 ? -17.169 -0.758  9.892   1.00 27.82  ?  389  LEU D O   1 
ATOM   9008  C CB  . LEU D  1  389 ? -17.314 1.751   8.520   1.00 27.86  ?  389  LEU D CB  1 
ATOM   9009  C CG  . LEU D  1  389 ? -17.520 3.264   8.441   1.00 28.22  ?  389  LEU D CG  1 
ATOM   9010  C CD1 . LEU D  1  389 ? -18.699 3.590   7.540   1.00 29.01  ?  389  LEU D CD1 1 
ATOM   9011  C CD2 . LEU D  1  389 ? -17.713 3.854   9.825   1.00 28.73  ?  389  LEU D CD2 1 
ATOM   9012  N N   . ASP D  1  390 ? -15.101 -0.989  9.039   1.00 27.32  ?  390  ASP D N   1 
ATOM   9013  C CA  . ASP D  1  390 ? -15.151 -2.443  9.034   1.00 27.27  ?  390  ASP D CA  1 
ATOM   9014  C C   . ASP D  1  390 ? -15.259 -2.990  10.456  1.00 27.54  ?  390  ASP D C   1 
ATOM   9015  O O   . ASP D  1  390 ? -15.063 -2.280  11.446  1.00 27.84  ?  390  ASP D O   1 
ATOM   9016  C CB  . ASP D  1  390 ? -13.914 -3.022  8.350   1.00 26.40  ?  390  ASP D CB  1 
ATOM   9017  C CG  . ASP D  1  390 ? -12.634 -2.742  9.115   1.00 25.87  ?  390  ASP D CG  1 
ATOM   9018  O OD1 . ASP D  1  390 ? -12.145 -1.597  9.059   1.00 26.02  ?  390  ASP D OD1 1 
ATOM   9019  O OD2 . ASP D  1  390 ? -12.116 -3.671  9.772   1.00 25.71  -1 390  ASP D OD2 1 
ATOM   9020  N N   . THR D  1  391 ? -15.577 -4.283  10.544  1.00 26.90  ?  391  THR D N   1 
ATOM   9021  C CA  . THR D  1  391 ? -15.658 -5.004  11.813  1.00 27.18  ?  391  THR D CA  1 
ATOM   9022  C C   . THR D  1  391 ? -16.661 -4.337  12.760  1.00 28.08  ?  391  THR D C   1 
ATOM   9023  O O   . THR D  1  391 ? -16.321 -3.847  13.839  1.00 28.11  ?  391  THR D O   1 
ATOM   9024  C CB  . THR D  1  391 ? -14.275 -5.131  12.461  1.00 26.43  ?  391  THR D CB  1 
ATOM   9025  O OG1 . THR D  1  391 ? -13.301 -5.419  11.450  1.00 25.67  ?  391  THR D OG1 1 
ATOM   9026  C CG2 . THR D  1  391 ? -14.266 -6.254  13.487  1.00 26.64  ?  391  THR D CG2 1 
ATOM   9027  N N   . ASN D  1  392 ? -17.914 -4.311  12.315  1.00 30.46  ?  392  ASN D N   1 
ATOM   9028  C CA  . ASN D  1  392 ? -19.009 -3.724  13.074  1.00 31.50  ?  392  ASN D CA  1 
ATOM   9029  C C   . ASN D  1  392 ? -20.278 -4.501  12.742  1.00 32.41  ?  392  ASN D C   1 
ATOM   9030  O O   . ASN D  1  392 ? -20.235 -5.532  12.064  1.00 32.73  ?  392  ASN D O   1 
ATOM   9031  C CB  . ASN D  1  392 ? -19.137 -2.227  12.763  1.00 31.72  ?  392  ASN D CB  1 
ATOM   9032  C CG  . ASN D  1  392 ? -18.286 -1.367  13.677  1.00 31.29  ?  392  ASN D CG  1 
ATOM   9033  O OD1 . ASN D  1  392 ? -18.575 -1.231  14.866  1.00 31.93  ?  392  ASN D OD1 1 
ATOM   9034  N ND2 . ASN D  1  392 ? -17.225 -0.787  13.128  1.00 30.39  ?  392  ASN D ND2 1 
ATOM   9035  N N   . ASN D  1  393 ? -21.414 -4.015  13.232  1.00 36.37  ?  393  ASN D N   1 
ATOM   9036  C CA  . ASN D  1  393 ? -22.710 -4.630  12.974  1.00 37.36  ?  393  ASN D CA  1 
ATOM   9037  C C   . ASN D  1  393 ? -23.656 -3.648  12.292  1.00 38.10  ?  393  ASN D C   1 
ATOM   9038  O O   . ASN D  1  393 ? -24.839 -3.563  12.626  1.00 39.73  ?  393  ASN D O   1 
ATOM   9039  C CB  . ASN D  1  393 ? -23.330 -5.162  14.264  1.00 38.41  ?  393  ASN D CB  1 
ATOM   9040  C CG  . ASN D  1  393 ? -22.406 -6.104  15.012  1.00 38.37  ?  393  ASN D CG  1 
ATOM   9041  O OD1 . ASN D  1  393 ? -22.493 -7.323  14.867  1.00 38.83  ?  393  ASN D OD1 1 
ATOM   9042  N ND2 . ASN D  1  393 ? -21.518 -5.541  15.824  1.00 37.76  ?  393  ASN D ND2 1 
ATOM   9043  N N   . PHE D  1  394 ? -23.145 -2.901  11.317  1.00 34.68  ?  394  PHE D N   1 
ATOM   9044  C CA  . PHE D  1  394 ? -23.960 -1.914  10.629  1.00 35.36  ?  394  PHE D CA  1 
ATOM   9045  C C   . PHE D  1  394 ? -24.930 -2.591  9.666   1.00 35.91  ?  394  PHE D C   1 
ATOM   9046  O O   . PHE D  1  394 ? -24.731 -3.729  9.235   1.00 35.47  ?  394  PHE D O   1 
ATOM   9047  C CB  . PHE D  1  394 ? -23.082 -0.919  9.873   1.00 34.50  ?  394  PHE D CB  1 
ATOM   9048  C CG  . PHE D  1  394 ? -22.327 0.017   10.766  1.00 34.20  ?  394  PHE D CG  1 
ATOM   9049  C CD1 . PHE D  1  394 ? -22.982 0.716   11.764  1.00 35.17  ?  394  PHE D CD1 1 
ATOM   9050  C CD2 . PHE D  1  394 ? -20.964 0.201   10.606  1.00 33.01  ?  394  PHE D CD2 1 
ATOM   9051  C CE1 . PHE D  1  394 ? -22.293 1.580   12.589  1.00 34.92  ?  394  PHE D CE1 1 
ATOM   9052  C CE2 . PHE D  1  394 ? -20.269 1.065   11.429  1.00 32.75  ?  394  PHE D CE2 1 
ATOM   9053  C CZ  . PHE D  1  394 ? -20.935 1.755   12.422  1.00 33.69  ?  394  PHE D CZ  1 
ATOM   9054  N N   . THR D  1  395 ? -25.991 -1.862  9.325   1.00 36.46  ?  395  THR D N   1 
ATOM   9055  C CA  . THR D  1  395 ? -27.076 -2.382  8.507   1.00 37.22  ?  395  THR D CA  1 
ATOM   9056  C C   . THR D  1  395 ? -27.536 -1.302  7.538   1.00 37.61  ?  395  THR D C   1 
ATOM   9057  O O   . THR D  1  395 ? -27.297 -0.110  7.744   1.00 37.64  ?  395  THR D O   1 
ATOM   9058  C CB  . THR D  1  395 ? -28.270 -2.847  9.360   1.00 38.59  ?  395  THR D CB  1 
ATOM   9059  O OG1 . THR D  1  395 ? -28.780 -1.742  10.118  1.00 39.53  ?  395  THR D OG1 1 
ATOM   9060  C CG2 . THR D  1  395 ? -27.868 -3.970  10.310  1.00 38.30  ?  395  THR D CG2 1 
ATOM   9061  N N   . GLY D  1  396 ? -28.195 -1.736  6.471   1.00 38.28  ?  396  GLY D N   1 
ATOM   9062  C CA  . GLY D  1  396 ? -28.819 -0.812  5.546   1.00 38.93  ?  396  GLY D CA  1 
ATOM   9063  C C   . GLY D  1  396 ? -27.920 -0.395  4.397   1.00 36.97  ?  396  GLY D C   1 
ATOM   9064  O O   . GLY D  1  396 ? -26.917 -1.035  4.066   1.00 35.12  ?  396  GLY D O   1 
ATOM   9065  N N   . PHE D  1  397 ? -28.302 0.719   3.783   1.00 40.41  ?  397  PHE D N   1 
ATOM   9066  C CA  . PHE D  1  397 ? -27.669 1.223   2.576   1.00 39.12  ?  397  PHE D CA  1 
ATOM   9067  C C   . PHE D  1  397 ? -26.563 2.217   2.921   1.00 37.82  ?  397  PHE D C   1 
ATOM   9068  O O   . PHE D  1  397 ? -26.484 2.739   4.036   1.00 38.24  ?  397  PHE D O   1 
ATOM   9069  C CB  . PHE D  1  397 ? -28.698 1.903   1.666   1.00 40.83  ?  397  PHE D CB  1 
ATOM   9070  C CG  . PHE D  1  397 ? -29.767 0.980   1.136   1.00 42.20  ?  397  PHE D CG  1 
ATOM   9071  C CD1 . PHE D  1  397 ? -30.677 0.372   1.988   1.00 43.86  ?  397  PHE D CD1 1 
ATOM   9072  C CD2 . PHE D  1  397 ? -29.878 0.744   -0.224  1.00 42.04  ?  397  PHE D CD2 1 
ATOM   9073  C CE1 . PHE D  1  397 ? -31.660 -0.466  1.497   1.00 45.30  ?  397  PHE D CE1 1 
ATOM   9074  C CE2 . PHE D  1  397 ? -30.861 -0.090  -0.722  1.00 43.43  ?  397  PHE D CE2 1 
ATOM   9075  C CZ  . PHE D  1  397 ? -31.752 -0.697  0.139   1.00 45.06  ?  397  PHE D CZ  1 
ATOM   9076  N N   . LEU D  1  398 ? -25.697 2.469   1.941   1.00 38.10  ?  398  LEU D N   1 
ATOM   9077  C CA  . LEU D  1  398 ? -24.708 3.526   2.088   1.00 37.15  ?  398  LEU D CA  1 
ATOM   9078  C C   . LEU D  1  398 ? -25.330 4.875   1.734   1.00 38.65  ?  398  LEU D C   1 
ATOM   9079  O O   . LEU D  1  398 ? -26.127 4.964   0.796   1.00 39.76  ?  398  LEU D O   1 
ATOM   9080  C CB  . LEU D  1  398 ? -23.499 3.266   1.193   1.00 35.23  ?  398  LEU D CB  1 
ATOM   9081  C CG  . LEU D  1  398 ? -22.572 2.114   1.579   1.00 33.65  ?  398  LEU D CG  1 
ATOM   9082  C CD1 . LEU D  1  398 ? -21.303 2.164   0.747   1.00 32.02  ?  398  LEU D CD1 1 
ATOM   9083  C CD2 . LEU D  1  398 ? -22.244 2.165   3.062   1.00 33.63  ?  398  LEU D CD2 1 
ATOM   9084  N N   . PRO D  1  399 ? -24.994 5.931   2.468   1.00 39.32  ?  399  PRO D N   1 
ATOM   9085  C CA  . PRO D  1  399 ? -25.524 7.256   2.132   1.00 41.12  ?  399  PRO D CA  1 
ATOM   9086  C C   . PRO D  1  399 ? -24.980 7.751   0.802   1.00 40.39  ?  399  PRO D C   1 
ATOM   9087  O O   . PRO D  1  399 ? -23.855 7.438   0.405   1.00 38.47  ?  399  PRO D O   1 
ATOM   9088  C CB  . PRO D  1  399 ? -25.040 8.137   3.290   1.00 40.95  ?  399  PRO D CB  1 
ATOM   9089  C CG  . PRO D  1  399 ? -24.705 7.180   4.393   1.00 40.07  ?  399  PRO D CG  1 
ATOM   9090  C CD  . PRO D  1  399 ? -24.193 5.956   3.701   1.00 38.46  ?  399  PRO D CD  1 
ATOM   9091  N N   . ASP D  1  400 ? -25.804 8.539   0.109   1.00 44.32  ?  400  ASP D N   1 
ATOM   9092  C CA  . ASP D  1  400 ? -25.398 9.121   -1.163  1.00 44.36  ?  400  ASP D CA  1 
ATOM   9093  C C   . ASP D  1  400 ? -24.389 10.248  -0.998  1.00 43.74  ?  400  ASP D C   1 
ATOM   9094  O O   . ASP D  1  400 ? -23.845 10.723  -2.001  1.00 43.86  ?  400  ASP D O   1 
ATOM   9095  C CB  . ASP D  1  400 ? -26.626 9.620   -1.924  1.00 47.14  ?  400  ASP D CB  1 
ATOM   9096  C CG  . ASP D  1  400 ? -27.603 8.505   -2.242  1.00 48.65  ?  400  ASP D CG  1 
ATOM   9097  O OD1 . ASP D  1  400 ? -28.446 8.184   -1.378  1.00 49.98  ?  400  ASP D OD1 1 
ATOM   9098  O OD2 . ASP D  1  400 ? -27.519 7.940   -3.353  1.00 47.17  -1 400  ASP D OD2 1 
ATOM   9099  N N   . THR D  1  401 ? -24.138 10.692  0.233   1.00 39.94  ?  401  THR D N   1 
ATOM   9100  C CA  . THR D  1  401 ? -23.130 11.696  0.544   1.00 39.46  ?  401  THR D CA  1 
ATOM   9101  C C   . THR D  1  401 ? -21.725 11.109  0.680   1.00 37.10  ?  401  THR D C   1 
ATOM   9102  O O   . THR D  1  401 ? -20.848 11.785  1.229   1.00 36.63  ?  401  THR D O   1 
ATOM   9103  C CB  . THR D  1  401 ? -23.502 12.438  1.831   1.00 40.64  ?  401  THR D CB  1 
ATOM   9104  O OG1 . THR D  1  401 ? -23.618 11.501  2.910   1.00 39.97  ?  401  THR D OG1 1 
ATOM   9105  C CG2 . THR D  1  401 ? -24.824 13.175  1.662   1.00 43.28  ?  401  THR D CG2 1 
ATOM   9106  N N   . ILE D  1  402 ? -21.498 9.882   0.198   1.00 39.84  ?  402  ILE D N   1 
ATOM   9107  C CA  . ILE D  1  402 ? -20.299 9.133   0.579   1.00 37.87  ?  402  ILE D CA  1 
ATOM   9108  C C   . ILE D  1  402 ? -19.032 9.853   0.119   1.00 37.95  ?  402  ILE D C   1 
ATOM   9109  O O   . ILE D  1  402 ? -18.071 9.994   0.885   1.00 37.95  ?  402  ILE D O   1 
ATOM   9110  C CB  . ILE D  1  402 ? -20.373 7.688   0.044   1.00 36.87  ?  402  ILE D CB  1 
ATOM   9111  C CG1 . ILE D  1  402 ? -19.147 6.883   0.485   1.00 35.24  ?  402  ILE D CG1 1 
ATOM   9112  C CG2 . ILE D  1  402 ? -20.556 7.653   -1.468  1.00 37.53  ?  402  ILE D CG2 1 
ATOM   9113  C CD1 . ILE D  1  402 ? -18.965 6.823   1.983   1.00 35.09  ?  402  ILE D CD1 1 
ATOM   9114  N N   . CYS D  1  403 ? -19.014 10.336  -1.120  1.00 37.05  ?  403  CYS D N   1 
ATOM   9115  C CA  . CYS D  1  403 ? -17.871 11.062  -1.661  1.00 36.48  ?  403  CYS D CA  1 
ATOM   9116  C C   . CYS D  1  403 ? -18.286 12.463  -2.091  1.00 38.31  ?  403  CYS D C   1 
ATOM   9117  O O   . CYS D  1  403 ? -17.931 12.932  -3.174  1.00 38.75  ?  403  CYS D O   1 
ATOM   9118  C CB  . CYS D  1  403 ? -17.223 10.304  -2.819  1.00 35.88  ?  403  CYS D CB  1 
ATOM   9119  S SG  . CYS D  1  403 ? -15.536 10.867  -3.178  1.00 35.75  ?  403  CYS D SG  1 
ATOM   9120  N N   . ARG D  1  404 ? -19.072 13.127  -1.238  1.00 34.79  ?  404  ARG D N   1 
ATOM   9121  C CA  . ARG D  1  404 ? -19.618 14.445  -1.553  1.00 36.87  ?  404  ARG D CA  1 
ATOM   9122  C C   . ARG D  1  404 ? -18.521 15.435  -1.929  1.00 36.95  ?  404  ARG D C   1 
ATOM   9123  O O   . ARG D  1  404 ? -18.636 16.160  -2.923  1.00 38.27  ?  404  ARG D O   1 
ATOM   9124  C CB  . ARG D  1  404 ? -20.416 14.963  -0.355  1.00 38.10  ?  404  ARG D CB  1 
ATOM   9125  C CG  . ARG D  1  404 ? -21.178 16.245  -0.609  1.00 40.57  ?  404  ARG D CG  1 
ATOM   9126  C CD  . ARG D  1  404 ? -22.277 16.430  0.427   1.00 41.99  ?  404  ARG D CD  1 
ATOM   9127  N NE  . ARG D  1  404 ? -21.795 17.091  1.635   1.00 41.99  ?  404  ARG D NE  1 
ATOM   9128  C CZ  . ARG D  1  404 ? -21.391 18.354  1.696   1.00 43.06  ?  404  ARG D CZ  1 
ATOM   9129  N NH1 . ARG D  1  404 ? -21.419 19.142  0.633   1.00 44.34  ?  404  ARG D NH1 1 
ATOM   9130  N NH2 . ARG D  1  404 ? -20.954 18.840  2.854   1.00 43.00  ?  404  ARG D NH2 1 
ATOM   9131  N N   . GLY D  1  405 ? -17.449 15.483  -1.140  1.00 32.71  ?  405  GLY D N   1 
ATOM   9132  C CA  . GLY D  1  405 ? -16.369 16.412  -1.418  1.00 32.91  ?  405  GLY D CA  1 
ATOM   9133  C C   . GLY D  1  405 ? -15.414 15.986  -2.509  1.00 31.96  ?  405  GLY D C   1 
ATOM   9134  O O   . GLY D  1  405 ? -14.571 16.788  -2.923  1.00 32.45  ?  405  GLY D O   1 
ATOM   9135  N N   . GLY D  1  406 ? -15.519 14.747  -2.983  1.00 31.06  ?  406  GLY D N   1 
ATOM   9136  C CA  . GLY D  1  406 ? -14.632 14.284  -4.030  1.00 30.26  ?  406  GLY D CA  1 
ATOM   9137  C C   . GLY D  1  406 ? -13.202 14.077  -3.593  1.00 28.93  ?  406  GLY D C   1 
ATOM   9138  O O   . GLY D  1  406 ? -12.301 14.071  -4.435  1.00 28.74  ?  406  GLY D O   1 
ATOM   9139  N N   . LYS D  1  407 ? -12.964 13.912  -2.292  1.00 28.60  ?  407  LYS D N   1 
ATOM   9140  C CA  . LYS D  1  407 ? -11.622 13.736  -1.757  1.00 27.55  ?  407  LYS D CA  1 
ATOM   9141  C C   . LYS D  1  407 ? -11.434 12.405  -1.047  1.00 25.99  ?  407  LYS D C   1 
ATOM   9142  O O   . LYS D  1  407 ? -10.319 12.117  -0.594  1.00 25.18  ?  407  LYS D O   1 
ATOM   9143  C CB  . LYS D  1  407 ? -11.278 14.876  -0.788  1.00 28.33  ?  407  LYS D CB  1 
ATOM   9144  C CG  . LYS D  1  407 ? -11.273 16.256  -1.416  1.00 30.04  ?  407  LYS D CG  1 
ATOM   9145  C CD  . LYS D  1  407 ? -10.696 17.280  -0.453  1.00 30.70  ?  407  LYS D CD  1 
ATOM   9146  C CE  . LYS D  1  407 ? -10.766 18.684  -1.027  1.00 32.65  ?  407  LYS D CE  1 
ATOM   9147  N NZ  . LYS D  1  407 ? -10.086 19.673  -0.148  1.00 33.35  ?  407  LYS D NZ  1 
ATOM   9148  N N   . LEU D  1  408 ? -12.482 11.592  -0.935  1.00 27.10  ?  408  LEU D N   1 
ATOM   9149  C CA  . LEU D  1  408 ? -12.390 10.339  -0.198  1.00 25.89  ?  408  LEU D CA  1 
ATOM   9150  C C   . LEU D  1  408 ? -11.347 9.422   -0.820  1.00 24.75  ?  408  LEU D C   1 
ATOM   9151  O O   . LEU D  1  408 ? -11.371 9.151   -2.024  1.00 24.74  ?  408  LEU D O   1 
ATOM   9152  C CB  . LEU D  1  408 ? -13.746 9.640   -0.165  1.00 26.11  ?  408  LEU D CB  1 
ATOM   9153  C CG  . LEU D  1  408 ? -13.838 8.431   0.768   1.00 25.25  ?  408  LEU D CG  1 
ATOM   9154  C CD1 . LEU D  1  408 ? -13.851 8.868   2.226   1.00 25.59  ?  408  LEU D CD1 1 
ATOM   9155  C CD2 . LEU D  1  408 ? -15.065 7.593   0.445   1.00 25.51  ?  408  LEU D CD2 1 
ATOM   9156  N N   . GLU D  1  409 ? -10.425 8.944   0.012   1.00 26.05  ?  409  GLU D N   1 
ATOM   9157  C CA  . GLU D  1  409 ? -9.342  8.083   -0.437  1.00 25.63  ?  409  GLU D CA  1 
ATOM   9158  C C   . GLU D  1  409 ? -9.571  6.629   -0.054  1.00 25.58  ?  409  GLU D C   1 
ATOM   9159  O O   . GLU D  1  409 ? -9.512  5.743   -0.913  1.00 25.62  ?  409  GLU D O   1 
ATOM   9160  C CB  . GLU D  1  409 ? -8.001  8.569   0.134   1.00 25.54  ?  409  GLU D CB  1 
ATOM   9161  C CG  . GLU D  1  409 ? -7.390  9.761   -0.601  1.00 25.76  ?  409  GLU D CG  1 
ATOM   9162  C CD  . GLU D  1  409 ? -6.061  10.209  -0.004  1.00 25.92  ?  409  GLU D CD  1 
ATOM   9163  O OE1 . GLU D  1  409 ? -5.588  9.564   0.955   1.00 25.50  ?  409  GLU D OE1 1 
ATOM   9164  O OE2 . GLU D  1  409 ? -5.491  11.210  -0.494  1.00 27.26  -1 409  GLU D OE2 1 
ATOM   9165  N N   . ASN D  1  410 ? -9.838  6.364   1.222   1.00 23.93  ?  410  ASN D N   1 
ATOM   9166  C CA  . ASN D  1  410 ? -9.862  5.004   1.744   1.00 23.34  ?  410  ASN D CA  1 
ATOM   9167  C C   . ASN D  1  410 ? -11.164 4.744   2.478   1.00 23.77  ?  410  ASN D C   1 
ATOM   9168  O O   . ASN D  1  410 ? -11.487 5.438   3.445   1.00 24.36  ?  410  ASN D O   1 
ATOM   9169  C CB  . ASN D  1  410 ? -8.662  4.790   2.649   1.00 23.07  ?  410  ASN D CB  1 
ATOM   9170  C CG  . ASN D  1  410 ? -7.401  5.075   1.921   1.00 22.89  ?  410  ASN D CG  1 
ATOM   9171  O OD1 . ASN D  1  410 ? -7.292  4.773   0.734   1.00 22.67  ?  410  ASN D OD1 1 
ATOM   9172  N ND2 . ASN D  1  410 ? -6.461  5.711   2.578   1.00 23.16  ?  410  ASN D ND2 1 
ATOM   9173  N N   . LEU D  1  411 ? -11.899 3.740   2.017   1.00 22.56  ?  411  LEU D N   1 
ATOM   9174  C CA  . LEU D  1  411 ? -13.188 3.383   2.582   1.00 23.16  ?  411  LEU D CA  1 
ATOM   9175  C C   . LEU D  1  411 ? -13.157 1.905   2.927   1.00 22.78  ?  411  LEU D C   1 
ATOM   9176  O O   . LEU D  1  411 ? -12.791 1.078   2.086   1.00 22.21  ?  411  LEU D O   1 
ATOM   9177  C CB  . LEU D  1  411 ? -14.315 3.700   1.595   1.00 23.76  ?  411  LEU D CB  1 
ATOM   9178  C CG  . LEU D  1  411 ? -15.731 3.260   1.954   1.00 24.60  ?  411  LEU D CG  1 
ATOM   9179  C CD1 . LEU D  1  411 ? -16.178 3.922   3.240   1.00 25.45  ?  411  LEU D CD1 1 
ATOM   9180  C CD2 . LEU D  1  411 ? -16.684 3.610   0.819   1.00 25.30  ?  411  LEU D CD2 1 
ATOM   9181  N N   . THR D  1  412 ? -13.535 1.575   4.159   1.00 25.27  ?  412  THR D N   1 
ATOM   9182  C CA  . THR D  1  412 ? -13.424 0.212   4.661   1.00 25.49  ?  412  THR D CA  1 
ATOM   9183  C C   . THR D  1  412 ? -14.757 -0.183  5.275   1.00 26.27  ?  412  THR D C   1 
ATOM   9184  O O   . THR D  1  412 ? -15.205 0.440   6.244   1.00 26.27  ?  412  THR D O   1 
ATOM   9185  C CB  . THR D  1  412 ? -12.300 0.095   5.693   1.00 25.71  ?  412  THR D CB  1 
ATOM   9186  O OG1 . THR D  1  412 ? -11.128 0.751   5.199   1.00 25.16  ?  412  THR D OG1 1 
ATOM   9187  C CG2 . THR D  1  412 ? -11.963 -1.358  5.923   1.00 26.82  ?  412  THR D CG2 1 
ATOM   9188  N N   . LEU D  1  413 ? -15.385 -1.219  4.713   1.00 26.37  ?  413  LEU D N   1 
ATOM   9189  C CA  . LEU D  1  413 ? -16.718 -1.645  5.126   1.00 26.94  ?  413  LEU D CA  1 
ATOM   9190  C C   . LEU D  1  413 ? -16.780 -3.141  5.416   1.00 28.14  ?  413  LEU D C   1 
ATOM   9191  O O   . LEU D  1  413 ? -17.864 -3.730  5.358   1.00 28.69  ?  413  LEU D O   1 
ATOM   9192  C CB  . LEU D  1  413 ? -17.752 -1.279  4.058   1.00 27.17  ?  413  LEU D CB  1 
ATOM   9193  C CG  . LEU D  1  413 ? -17.794 0.181   3.605   1.00 27.21  ?  413  LEU D CG  1 
ATOM   9194  C CD1 . LEU D  1  413 ? -18.619 0.314   2.339   1.00 27.59  ?  413  LEU D CD1 1 
ATOM   9195  C CD2 . LEU D  1  413 ? -18.345 1.076   4.703   1.00 28.27  ?  413  LEU D CD2 1 
ATOM   9196  N N   . ASP D  1  414 ? -15.646 -3.763  5.731   1.00 28.03  ?  414  ASP D N   1 
ATOM   9197  C CA  . ASP D  1  414 ? -15.584 -5.216  5.825   1.00 29.73  ?  414  ASP D CA  1 
ATOM   9198  C C   . ASP D  1  414 ? -16.489 -5.741  6.931   1.00 31.39  ?  414  ASP D C   1 
ATOM   9199  O O   . ASP D  1  414 ? -16.723 -5.077  7.943   1.00 31.74  ?  414  ASP D O   1 
ATOM   9200  C CB  . ASP D  1  414 ? -14.151 -5.681  6.085   1.00 30.77  ?  414  ASP D CB  1 
ATOM   9201  C CG  . ASP D  1  414 ? -13.264 -5.518  4.879   1.00 29.35  ?  414  ASP D CG  1 
ATOM   9202  O OD1 . ASP D  1  414 ? -13.501 -4.565  4.116   1.00 27.50  ?  414  ASP D OD1 1 
ATOM   9203  O OD2 . ASP D  1  414 ? -12.342 -6.338  4.690   1.00 30.05  -1 414  ASP D OD2 1 
ATOM   9204  N N   . ASP D  1  415 ? -17.003 -6.951  6.715   1.00 31.46  ?  415  ASP D N   1 
ATOM   9205  C CA  . ASP D  1  415 ? -17.675 -7.738  7.746   1.00 33.52  ?  415  ASP D CA  1 
ATOM   9206  C C   . ASP D  1  415 ? -18.800 -6.945  8.412   1.00 32.84  ?  415  ASP D C   1 
ATOM   9207  O O   . ASP D  1  415 ? -18.790 -6.664  9.612   1.00 33.46  ?  415  ASP D O   1 
ATOM   9208  C CB  . ASP D  1  415 ? -16.656 -8.241  8.770   1.00 35.91  ?  415  ASP D CB  1 
ATOM   9209  C CG  . ASP D  1  415 ? -15.587 -9.113  8.135   1.00 37.39  ?  415  ASP D CG  1 
ATOM   9210  O OD1 . ASP D  1  415 ? -15.923 -9.891  7.217   1.00 36.68  ?  415  ASP D OD1 1 
ATOM   9211  O OD2 . ASP D  1  415 ? -14.410 -9.008  8.541   1.00 38.02  -1 415  ASP D OD2 1 
ATOM   9212  N N   . ASN D  1  416 ? -19.781 -6.582  7.591   1.00 35.71  ?  416  ASN D N   1 
ATOM   9213  C CA  . ASN D  1  416 ? -20.915 -5.776  8.016   1.00 34.86  ?  416  ASN D CA  1 
ATOM   9214  C C   . ASN D  1  416 ? -22.172 -6.397  7.417   1.00 35.85  ?  416  ASN D C   1 
ATOM   9215  O O   . ASN D  1  416 ? -22.140 -7.503  6.866   1.00 36.66  ?  416  ASN D O   1 
ATOM   9216  C CB  . ASN D  1  416 ? -20.723 -4.312  7.598   1.00 33.81  ?  416  ASN D CB  1 
ATOM   9217  C CG  . ASN D  1  416 ? -20.093 -3.471  8.690   1.00 33.82  ?  416  ASN D CG  1 
ATOM   9218  O OD1 . ASN D  1  416 ? -20.310 -3.711  9.876   1.00 35.11  ?  416  ASN D OD1 1 
ATOM   9219  N ND2 . ASN D  1  416 ? -19.304 -2.479  8.294   1.00 32.77  ?  416  ASN D ND2 1 
ATOM   9220  N N   . HIS D  1  417 ? -23.291 -5.691  7.531   1.00 38.76  ?  417  HIS D N   1 
ATOM   9221  C CA  . HIS D  1  417 ? -24.576 -6.153  7.014   1.00 40.19  ?  417  HIS D CA  1 
ATOM   9222  C C   . HIS D  1  417 ? -25.186 -5.093  6.106   1.00 39.98  ?  417  HIS D C   1 
ATOM   9223  O O   . HIS D  1  417 ? -26.370 -4.760  6.193   1.00 41.74  ?  417  HIS D O   1 
ATOM   9224  C CB  . HIS D  1  417 ? -25.525 -6.521  8.151   1.00 42.58  ?  417  HIS D CB  1 
ATOM   9225  C CG  . HIS D  1  417 ? -25.058 -7.680  8.975   1.00 43.03  ?  417  HIS D CG  1 
ATOM   9226  N ND1 . HIS D  1  417 ? -24.941 -7.620  10.347  1.00 43.72  ?  417  HIS D ND1 1 
ATOM   9227  C CD2 . HIS D  1  417 ? -24.678 -8.930  8.620   1.00 42.92  ?  417  HIS D CD2 1 
ATOM   9228  C CE1 . HIS D  1  417 ? -24.509 -8.783  10.801  1.00 44.75  ?  417  HIS D CE1 1 
ATOM   9229  N NE2 . HIS D  1  417 ? -24.341 -9.595  9.773   1.00 44.44  ?  417  HIS D NE2 1 
ATOM   9230  N N   . PHE D  1  418 ? -24.363 -4.540  5.220   1.00 36.30  ?  418  PHE D N   1 
ATOM   9231  C CA  . PHE D  1  418 ? -24.823 -3.534  4.279   1.00 36.39  ?  418  PHE D CA  1 
ATOM   9232  C C   . PHE D  1  418 ? -25.571 -4.185  3.119   1.00 36.91  ?  418  PHE D C   1 
ATOM   9233  O O   . PHE D  1  418 ? -25.363 -5.355  2.784   1.00 36.52  ?  418  PHE D O   1 
ATOM   9234  C CB  . PHE D  1  418 ? -23.649 -2.715  3.743   1.00 34.60  ?  418  PHE D CB  1 
ATOM   9235  C CG  . PHE D  1  418 ? -23.049 -1.777  4.751   1.00 34.35  ?  418  PHE D CG  1 
ATOM   9236  C CD1 . PHE D  1  418 ? -23.831 -0.820  5.377   1.00 35.74  ?  418  PHE D CD1 1 
ATOM   9237  C CD2 . PHE D  1  418 ? -21.702 -1.846  5.065   1.00 32.87  ?  418  PHE D CD2 1 
ATOM   9238  C CE1 . PHE D  1  418 ? -23.281 0.047   6.303   1.00 35.59  ?  418  PHE D CE1 1 
ATOM   9239  C CE2 . PHE D  1  418 ? -21.147 -0.981  5.990   1.00 32.75  ?  418  PHE D CE2 1 
ATOM   9240  C CZ  . PHE D  1  418 ? -21.937 -0.034  6.608   1.00 34.07  ?  418  PHE D CZ  1 
ATOM   9241  N N   . GLU D  1  419 ? -26.456 -3.402  2.504   1.00 38.37  ?  419  GLU D N   1 
ATOM   9242  C CA  . GLU D  1  419 ? -27.273 -3.858  1.389   1.00 39.12  ?  419  GLU D CA  1 
ATOM   9243  C C   . GLU D  1  419 ? -27.267 -2.794  0.300   1.00 38.89  ?  419  GLU D C   1 
ATOM   9244  O O   . GLU D  1  419 ? -26.617 -1.750  0.419   1.00 38.37  ?  419  GLU D O   1 
ATOM   9245  C CB  . GLU D  1  419 ? -28.713 -4.149  1.826   1.00 41.56  ?  419  GLU D CB  1 
ATOM   9246  C CG  . GLU D  1  419 ? -28.859 -5.150  2.952   1.00 42.28  ?  419  GLU D CG  1 
ATOM   9247  C CD  . GLU D  1  419 ? -30.264 -5.164  3.517   1.00 45.23  ?  419  GLU D CD  1 
ATOM   9248  O OE1 . GLU D  1  419 ? -31.126 -5.872  2.955   1.00 46.70  ?  419  GLU D OE1 1 
ATOM   9249  O OE2 . GLU D  1  419 ? -30.507 -4.460  4.520   1.00 46.19  -1 419  GLU D OE2 1 
ATOM   9250  N N   . GLY D  1  420 ? -28.000 -3.073  -0.774  1.00 39.64  ?  420  GLY D N   1 
ATOM   9251  C CA  . GLY D  1  420 ? -28.283 -2.089  -1.789  1.00 40.07  ?  420  GLY D CA  1 
ATOM   9252  C C   . GLY D  1  420 ? -27.130 -1.820  -2.730  1.00 38.18  ?  420  GLY D C   1 
ATOM   9253  O O   . GLY D  1  420 ? -26.088 -2.482  -2.693  1.00 36.48  ?  420  GLY D O   1 
ATOM   9254  N N   . PRO D  1  421 ? -27.302 -0.822  -3.597  1.00 36.59  ?  421  PRO D N   1 
ATOM   9255  C CA  . PRO D  1  421 ? -26.285 -0.538  -4.616  1.00 35.18  ?  421  PRO D CA  1 
ATOM   9256  C C   . PRO D  1  421 ? -25.190 0.401   -4.139  1.00 33.95  ?  421  PRO D C   1 
ATOM   9257  O O   . PRO D  1  421 ? -25.201 0.871   -2.997  1.00 34.13  ?  421  PRO D O   1 
ATOM   9258  C CB  . PRO D  1  421 ? -27.107 0.097   -5.741  1.00 36.78  ?  421  PRO D CB  1 
ATOM   9259  C CG  . PRO D  1  421 ? -28.186 0.834   -5.008  1.00 38.74  ?  421  PRO D CG  1 
ATOM   9260  C CD  . PRO D  1  421 ? -28.500 0.020   -3.766  1.00 38.83  ?  421  PRO D CD  1 
ATOM   9261  N N   . VAL D  1  422 ? -24.238 0.671   -5.021  1.00 34.57  ?  422  VAL D N   1 
ATOM   9262  C CA  . VAL D  1  422 ? -23.198 1.665   -4.751  1.00 33.66  ?  422  VAL D CA  1 
ATOM   9263  C C   . VAL D  1  422 ? -23.732 3.045   -5.126  1.00 35.12  ?  422  VAL D C   1 
ATOM   9264  O O   . VAL D  1  422 ? -24.221 3.223   -6.253  1.00 36.10  ?  422  VAL D O   1 
ATOM   9265  C CB  . VAL D  1  422 ? -21.930 1.335   -5.532  1.00 33.69  ?  422  VAL D CB  1 
ATOM   9266  C CG1 . VAL D  1  422 ? -20.773 2.186   -5.049  1.00 32.74  ?  422  VAL D CG1 1 
ATOM   9267  C CG2 . VAL D  1  422 ? -21.597 -0.145  -5.394  1.00 32.66  ?  422  VAL D CG2 1 
ATOM   9268  N N   . PRO D  1  423 ? -23.676 4.025   -4.223  1.00 38.56  ?  423  PRO D N   1 
ATOM   9269  C CA  . PRO D  1  423 ? -24.203 5.357   -4.547  1.00 40.39  ?  423  PRO D CA  1 
ATOM   9270  C C   . PRO D  1  423 ? -23.499 5.964   -5.752  1.00 40.27  ?  423  PRO D C   1 
ATOM   9271  O O   . PRO D  1  423 ? -22.312 5.730   -5.988  1.00 38.63  ?  423  PRO D O   1 
ATOM   9272  C CB  . PRO D  1  423 ? -23.927 6.166   -3.273  1.00 40.18  ?  423  PRO D CB  1 
ATOM   9273  C CG  . PRO D  1  423 ? -23.831 5.139   -2.189  1.00 39.25  ?  423  PRO D CG  1 
ATOM   9274  C CD  . PRO D  1  423 ? -23.196 3.942   -2.834  1.00 37.74  ?  423  PRO D CD  1 
ATOM   9275  N N   . LYS D  1  424 ? -24.261 6.744   -6.528  1.00 43.04  ?  424  LYS D N   1 
ATOM   9276  C CA  . LYS D  1  424 ? -23.718 7.353   -7.740  1.00 43.12  ?  424  LYS D CA  1 
ATOM   9277  C C   . LYS D  1  424 ? -22.499 8.217   -7.448  1.00 42.23  ?  424  LYS D C   1 
ATOM   9278  O O   . LYS D  1  424 ? -21.587 8.301   -8.278  1.00 41.86  ?  424  LYS D O   1 
ATOM   9279  C CB  . LYS D  1  424 ? -24.790 8.187   -8.445  1.00 46.06  ?  424  LYS D CB  1 
ATOM   9280  C CG  . LYS D  1  424 ? -25.865 7.376   -9.152  1.00 47.36  ?  424  LYS D CG  1 
ATOM   9281  C CD  . LYS D  1  424 ? -26.631 8.239   -10.147 1.00 50.79  ?  424  LYS D CD  1 
ATOM   9282  C CE  . LYS D  1  424 ? -27.881 8.838   -9.520  1.00 53.59  ?  424  LYS D CE  1 
ATOM   9283  N NZ  . LYS D  1  424 ? -28.603 9.731   -10.471 1.00 55.16  ?  424  LYS D NZ  1 
ATOM   9284  N N   . SER D  1  425 ? -22.463 8.868   -6.282  1.00 41.78  ?  425  SER D N   1 
ATOM   9285  C CA  . SER D  1  425 ? -21.306 9.688   -5.942  1.00 41.32  ?  425  SER D CA  1 
ATOM   9286  C C   . SER D  1  425 ? -20.070 8.836   -5.689  1.00 38.94  ?  425  SER D C   1 
ATOM   9287  O O   . SER D  1  425 ? -18.946 9.294   -5.923  1.00 38.22  ?  425  SER D O   1 
ATOM   9288  C CB  . SER D  1  425 ? -21.617 10.560  -4.725  1.00 41.98  ?  425  SER D CB  1 
ATOM   9289  O OG  . SER D  1  425 ? -21.397 9.853   -3.520  1.00 40.65  ?  425  SER D OG  1 
ATOM   9290  N N   . LEU D  1  426 ? -20.252 7.599   -5.217  1.00 39.61  ?  426  LEU D N   1 
ATOM   9291  C CA  . LEU D  1  426 ? -19.118 6.692   -5.080  1.00 37.60  ?  426  LEU D CA  1 
ATOM   9292  C C   . LEU D  1  426 ? -18.672 6.154   -6.432  1.00 37.20  ?  426  LEU D C   1 
ATOM   9293  O O   . LEU D  1  426 ? -17.479 5.901   -6.636  1.00 36.07  ?  426  LEU D O   1 
ATOM   9294  C CB  . LEU D  1  426 ? -19.472 5.541   -4.138  1.00 36.80  ?  426  LEU D CB  1 
ATOM   9295  C CG  . LEU D  1  426 ? -18.306 4.664   -3.678  1.00 35.75  ?  426  LEU D CG  1 
ATOM   9296  C CD1 . LEU D  1  426 ? -17.121 5.525   -3.276  1.00 36.30  ?  426  LEU D CD1 1 
ATOM   9297  C CD2 . LEU D  1  426 ? -18.733 3.774   -2.523  1.00 35.19  ?  426  LEU D CD2 1 
ATOM   9298  N N   . ARG D  1  427 ? -19.613 5.965   -7.359  1.00 37.22  ?  427  ARG D N   1 
ATOM   9299  C CA  . ARG D  1  427 ? -19.253 5.576   -8.718  1.00 36.81  ?  427  ARG D CA  1 
ATOM   9300  C C   . ARG D  1  427 ? -18.383 6.637   -9.382  1.00 37.14  ?  427  ARG D C   1 
ATOM   9301  O O   . ARG D  1  427 ? -17.411 6.311   -10.074 1.00 36.45  ?  427  ARG D O   1 
ATOM   9302  C CB  . ARG D  1  427 ? -20.520 5.320   -9.535  1.00 38.27  ?  427  ARG D CB  1 
ATOM   9303  C CG  . ARG D  1  427 ? -20.305 5.225   -11.035 1.00 39.08  ?  427  ARG D CG  1 
ATOM   9304  C CD  . ARG D  1  427 ? -21.637 5.142   -11.767 1.00 40.83  ?  427  ARG D CD  1 
ATOM   9305  N NE  . ARG D  1  427 ? -22.132 6.460   -12.145 1.00 42.87  ?  427  ARG D NE  1 
ATOM   9306  C CZ  . ARG D  1  427 ? -23.415 6.770   -12.273 1.00 45.03  ?  427  ARG D CZ  1 
ATOM   9307  N NH1 . ARG D  1  427 ? -24.366 5.872   -12.073 1.00 45.77  ?  427  ARG D NH1 1 
ATOM   9308  N NH2 . ARG D  1  427 ? -23.753 8.012   -12.608 1.00 47.10  ?  427  ARG D NH2 1 
ATOM   9309  N N   . ASP D  1  428 ? -18.715 7.910   -9.180  1.00 36.23  ?  428  ASP D N   1 
ATOM   9310  C CA  . ASP D  1  428 ? -17.982 9.021   -9.773  1.00 36.92  ?  428  ASP D CA  1 
ATOM   9311  C C   . ASP D  1  428 ? -16.826 9.511   -8.907  1.00 35.92  ?  428  ASP D C   1 
ATOM   9312  O O   . ASP D  1  428 ? -16.101 10.419  -9.328  1.00 36.94  ?  428  ASP D O   1 
ATOM   9313  C CB  . ASP D  1  428 ? -18.936 10.186  -10.060 1.00 39.17  ?  428  ASP D CB  1 
ATOM   9314  C CG  . ASP D  1  428 ? -20.245 9.729   -10.679 1.00 40.56  ?  428  ASP D CG  1 
ATOM   9315  O OD1 . ASP D  1  428 ? -20.302 8.587   -11.182 1.00 39.62  ?  428  ASP D OD1 1 
ATOM   9316  O OD2 . ASP D  1  428 ? -21.219 10.513  -10.665 1.00 42.96  -1 428  ASP D OD2 1 
ATOM   9317  N N   . CYS D  1  429 ? -16.639 8.946   -7.717  1.00 33.96  ?  429  CYS D N   1 
ATOM   9318  C CA  . CYS D  1  429 ? -15.589 9.386   -6.799  1.00 33.14  ?  429  CYS D CA  1 
ATOM   9319  C C   . CYS D  1  429 ? -14.238 8.920   -7.328  1.00 32.38  ?  429  CYS D C   1 
ATOM   9320  O O   . CYS D  1  429 ? -13.871 7.753   -7.184  1.00 31.42  ?  429  CYS D O   1 
ATOM   9321  C CB  . CYS D  1  429 ? -15.855 8.841   -5.401  1.00 32.60  ?  429  CYS D CB  1 
ATOM   9322  S SG  . CYS D  1  429 ? -14.646 9.322   -4.155  1.00 32.80  ?  429  CYS D SG  1 
ATOM   9323  N N   . LYS D  1  430 ? -13.480 9.836   -7.929  1.00 30.53  ?  430  LYS D N   1 
ATOM   9324  C CA  . LYS D  1  430 ? -12.241 9.485   -8.611  1.00 29.91  ?  430  LYS D CA  1 
ATOM   9325  C C   . LYS D  1  430 ? -11.027 9.418   -7.692  1.00 28.86  ?  430  LYS D C   1 
ATOM   9326  O O   . LYS D  1  430 ? -9.954  9.004   -8.144  1.00 28.95  ?  430  LYS D O   1 
ATOM   9327  C CB  . LYS D  1  430 ? -11.964 10.482  -9.743  1.00 31.41  ?  430  LYS D CB  1 
ATOM   9328  C CG  . LYS D  1  430 ? -12.959 10.409  -10.890 1.00 32.57  ?  430  LYS D CG  1 
ATOM   9329  C CD  . LYS D  1  430 ? -12.780 11.568  -11.857 1.00 34.43  ?  430  LYS D CD  1 
ATOM   9330  C CE  . LYS D  1  430 ? -13.685 11.419  -13.070 1.00 35.71  ?  430  LYS D CE  1 
ATOM   9331  N NZ  . LYS D  1  430 ? -13.988 9.993   -13.370 1.00 34.54  ?  430  LYS D NZ  1 
ATOM   9332  N N   . SER D  1  431 ? -11.157 9.809   -6.426  1.00 28.07  ?  431  SER D N   1 
ATOM   9333  C CA  . SER D  1  431 ? -10.017 9.884   -5.522  1.00 27.35  ?  431  SER D CA  1 
ATOM   9334  C C   . SER D  1  431 ? -9.812  8.616   -4.699  1.00 25.95  ?  431  SER D C   1 
ATOM   9335  O O   . SER D  1  431 ? -9.033  8.638   -3.741  1.00 25.48  ?  431  SER D O   1 
ATOM   9336  C CB  . SER D  1  431 ? -10.171 11.084  -4.585  1.00 28.13  ?  431  SER D CB  1 
ATOM   9337  O OG  . SER D  1  431 ? -11.378 11.001  -3.847  1.00 28.27  ?  431  SER D OG  1 
ATOM   9338  N N   . LEU D  1  432 ? -10.479 7.519   -5.048  1.00 26.65  ?  432  LEU D N   1 
ATOM   9339  C CA  . LEU D  1  432 ? -10.387 6.303   -4.249  1.00 25.57  ?  432  LEU D CA  1 
ATOM   9340  C C   . LEU D  1  432 ? -8.995  5.689   -4.352  1.00 24.84  ?  432  LEU D C   1 
ATOM   9341  O O   . LEU D  1  432 ? -8.382  5.673   -5.424  1.00 25.00  ?  432  LEU D O   1 
ATOM   9342  C CB  . LEU D  1  432 ? -11.446 5.297   -4.702  1.00 25.43  ?  432  LEU D CB  1 
ATOM   9343  C CG  . LEU D  1  432 ? -12.904 5.728   -4.518  1.00 26.31  ?  432  LEU D CG  1 
ATOM   9344  C CD1 . LEU D  1  432 ? -13.853 4.572   -4.784  1.00 26.18  ?  432  LEU D CD1 1 
ATOM   9345  C CD2 . LEU D  1  432 ? -13.120 6.278   -3.117  1.00 26.48  ?  432  LEU D CD2 1 
ATOM   9346  N N   . ILE D  1  433 ? -8.496  5.180   -3.224  1.00 23.82  ?  433  ILE D N   1 
ATOM   9347  C CA  . ILE D  1  433 ? -7.181  4.546   -3.177  1.00 23.33  ?  433  ILE D CA  1 
ATOM   9348  C C   . ILE D  1  433 ? -7.318  3.123   -2.654  1.00 22.65  ?  433  ILE D C   1 
ATOM   9349  O O   . ILE D  1  433 ? -6.892  2.165   -3.309  1.00 22.34  ?  433  ILE D O   1 
ATOM   9350  C CB  . ILE D  1  433 ? -6.200  5.350   -2.306  1.00 23.57  ?  433  ILE D CB  1 
ATOM   9351  C CG1 . ILE D  1  433 ? -6.055  6.780   -2.830  1.00 24.45  ?  433  ILE D CG1 1 
ATOM   9352  C CG2 . ILE D  1  433 ? -4.848  4.653   -2.252  1.00 23.29  ?  433  ILE D CG2 1 
ATOM   9353  C CD1 . ILE D  1  433 ? -4.945  7.563   -2.162  1.00 24.84  ?  433  ILE D CD1 1 
ATOM   9354  N N   . ARG D  1  434 ? -7.905  2.973   -1.468  1.00 23.61  ?  434  ARG D N   1 
ATOM   9355  C CA  . ARG D  1  434 ? -8.214  1.666   -0.899  1.00 22.77  ?  434  ARG D CA  1 
ATOM   9356  C C   . ARG D  1  434 ? -9.715  1.564   -0.686  1.00 22.99  ?  434  ARG D C   1 
ATOM   9357  O O   . ARG D  1  434 ? -10.299 2.372   0.043   1.00 23.44  ?  434  ARG D O   1 
ATOM   9358  C CB  . ARG D  1  434 ? -7.467  1.428   0.416   1.00 22.68  ?  434  ARG D CB  1 
ATOM   9359  C CG  . ARG D  1  434 ? -6.287  0.478   0.276   1.00 22.44  ?  434  ARG D CG  1 
ATOM   9360  C CD  . ARG D  1  434 ? -5.609  0.202   1.607   1.00 22.63  ?  434  ARG D CD  1 
ATOM   9361  N NE  . ARG D  1  434 ? -6.050  -1.061  2.189   1.00 22.63  ?  434  ARG D NE  1 
ATOM   9362  C CZ  . ARG D  1  434 ? -5.495  -2.238  1.935   1.00 22.61  ?  434  ARG D CZ  1 
ATOM   9363  N NH1 . ARG D  1  434 ? -4.501  -2.362  1.070   1.00 22.54  ?  434  ARG D NH1 1 
ATOM   9364  N NH2 . ARG D  1  434 ? -5.952  -3.319  2.560   1.00 22.82  ?  434  ARG D NH2 1 
ATOM   9365  N N   . VAL D  1  435 ? -10.334 0.572   -1.318  1.00 22.19  ?  435  VAL D N   1 
ATOM   9366  C CA  . VAL D  1  435 ? -11.762 0.318   -1.190  1.00 22.62  ?  435  VAL D CA  1 
ATOM   9367  C C   . VAL D  1  435 ? -11.936 -1.108  -0.697  1.00 22.46  ?  435  VAL D C   1 
ATOM   9368  O O   . VAL D  1  435 ? -11.335 -2.037  -1.247  1.00 22.07  ?  435  VAL D O   1 
ATOM   9369  C CB  . VAL D  1  435 ? -12.497 0.535   -2.524  1.00 22.95  ?  435  VAL D CB  1 
ATOM   9370  C CG1 . VAL D  1  435 ? -13.991 0.334   -2.344  1.00 23.64  ?  435  VAL D CG1 1 
ATOM   9371  C CG2 . VAL D  1  435 ? -12.202 1.920   -3.064  1.00 23.30  ?  435  VAL D CG2 1 
ATOM   9372  N N   . ARG D  1  436 ? -12.751 -1.282  0.340   1.00 24.62  ?  436  ARG D N   1 
ATOM   9373  C CA  . ARG D  1  436 ? -12.946 -2.598  0.947   1.00 24.88  ?  436  ARG D CA  1 
ATOM   9374  C C   . ARG D  1  436 ? -14.433 -2.788  1.232   1.00 25.32  ?  436  ARG D C   1 
ATOM   9375  O O   . ARG D  1  436 ? -14.954 -2.275  2.227   1.00 25.45  ?  436  ARG D O   1 
ATOM   9376  C CB  . ARG D  1  436 ? -12.111 -2.741  2.212   1.00 25.23  ?  436  ARG D CB  1 
ATOM   9377  C CG  . ARG D  1  436 ? -10.611 -2.748  1.984   1.00 25.12  ?  436  ARG D CG  1 
ATOM   9378  C CD  . ARG D  1  436 ? -9.933  -3.715  2.937   1.00 25.73  ?  436  ARG D CD  1 
ATOM   9379  N NE  . ARG D  1  436 ? -10.366 -5.089  2.717   1.00 26.66  ?  436  ARG D NE  1 
ATOM   9380  C CZ  . ARG D  1  436 ? -9.609  -6.155  2.934   1.00 27.68  ?  436  ARG D CZ  1 
ATOM   9381  N NH1 . ARG D  1  436 ? -8.375  -6.042  3.396   1.00 28.38  ?  436  ARG D NH1 1 
ATOM   9382  N NH2 . ARG D  1  436 ? -10.103 -7.364  2.684   1.00 28.75  ?  436  ARG D NH2 1 
ATOM   9383  N N   . PHE D  1  437 ? -15.105 -3.532  0.355   1.00 24.98  ?  437  PHE D N   1 
ATOM   9384  C CA  . PHE D  1  437 ? -16.511 -3.876  0.505   1.00 25.96  ?  437  PHE D CA  1 
ATOM   9385  C C   . PHE D  1  437 ? -16.712 -5.294  1.027   1.00 26.34  ?  437  PHE D C   1 
ATOM   9386  O O   . PHE D  1  437 ? -17.854 -5.757  1.097   1.00 27.29  ?  437  PHE D O   1 
ATOM   9387  C CB  . PHE D  1  437 ? -17.239 -3.721  -0.833  1.00 26.21  ?  437  PHE D CB  1 
ATOM   9388  C CG  . PHE D  1  437 ? -17.675 -2.313  -1.142  1.00 26.62  ?  437  PHE D CG  1 
ATOM   9389  C CD1 . PHE D  1  437 ? -16.872 -1.229  -0.831  1.00 26.20  ?  437  PHE D CD1 1 
ATOM   9390  C CD2 . PHE D  1  437 ? -18.889 -2.079  -1.769  1.00 27.63  ?  437  PHE D CD2 1 
ATOM   9391  C CE1 . PHE D  1  437 ? -17.278 0.060   -1.124  1.00 26.77  ?  437  PHE D CE1 1 
ATOM   9392  C CE2 . PHE D  1  437 ? -19.300 -0.794  -2.065  1.00 28.25  ?  437  PHE D CE2 1 
ATOM   9393  C CZ  . PHE D  1  437 ? -18.493 0.277   -1.742  1.00 27.82  ?  437  PHE D CZ  1 
ATOM   9394  N N   . LYS D  1  438 ? -15.630 -5.988  1.381   1.00 26.87  ?  438  LYS D N   1 
ATOM   9395  C CA  . LYS D  1  438 ? -15.683 -7.423  1.640   1.00 27.29  ?  438  LYS D CA  1 
ATOM   9396  C C   . LYS D  1  438 ? -16.687 -7.771  2.734   1.00 28.53  ?  438  LYS D C   1 
ATOM   9397  O O   . LYS D  1  438 ? -16.881 -7.019  3.692   1.00 28.93  ?  438  LYS D O   1 
ATOM   9398  C CB  . LYS D  1  438 ? -14.293 -7.936  2.024   1.00 26.77  ?  438  LYS D CB  1 
ATOM   9399  C CG  . LYS D  1  438 ? -14.111 -9.434  1.832   1.00 27.10  ?  438  LYS D CG  1 
ATOM   9400  C CD  . LYS D  1  438 ? -13.081 -9.998  2.795   1.00 27.31  ?  438  LYS D CD  1 
ATOM   9401  C CE  . LYS D  1  438 ? -12.478 -11.293 2.265   1.00 27.43  ?  438  LYS D CE  1 
ATOM   9402  N NZ  . LYS D  1  438 ? -11.607 -11.061 1.079   1.00 26.47  ?  438  LYS D NZ  1 
ATOM   9403  N N   . GLY D  1  439 ? -17.336 -8.923  2.573   1.00 31.29  ?  439  GLY D N   1 
ATOM   9404  C CA  . GLY D  1  439 ? -18.276 -9.433  3.552   1.00 32.93  ?  439  GLY D CA  1 
ATOM   9405  C C   . GLY D  1  439 ? -19.495 -8.560  3.767   1.00 31.99  ?  439  GLY D C   1 
ATOM   9406  O O   . GLY D  1  439 ? -19.694 -8.018  4.858   1.00 32.07  ?  439  GLY D O   1 
ATOM   9407  N N   . ASN D  1  440 ? -20.319 -8.420  2.733   1.00 34.15  ?  440  ASN D N   1 
ATOM   9408  C CA  . ASN D  1  440 ? -21.555 -7.654  2.821   1.00 33.34  ?  440  ASN D CA  1 
ATOM   9409  C C   . ASN D  1  440 ? -22.568 -8.265  1.859   1.00 33.35  ?  440  ASN D C   1 
ATOM   9410  O O   . ASN D  1  440 ? -22.383 -9.378  1.358   1.00 34.16  ?  440  ASN D O   1 
ATOM   9411  C CB  . ASN D  1  440 ? -21.296 -6.169  2.539   1.00 31.80  ?  440  ASN D CB  1 
ATOM   9412  C CG  . ASN D  1  440 ? -20.813 -5.422  3.764   1.00 31.85  ?  440  ASN D CG  1 
ATOM   9413  O OD1 . ASN D  1  440 ? -21.602 -5.080  4.644   1.00 32.91  ?  440  ASN D OD1 1 
ATOM   9414  N ND2 . ASN D  1  440 ? -19.510 -5.174  3.835   1.00 31.58  ?  440  ASN D ND2 1 
ATOM   9415  N N   . SER D  1  441 ? -23.648 -7.532  1.604   1.00 34.60  ?  441  SER D N   1 
ATOM   9416  C CA  . SER D  1  441 ? -24.689 -7.952  0.674   1.00 35.51  ?  441  SER D CA  1 
ATOM   9417  C C   . SER D  1  441 ? -24.972 -6.848  -0.333  1.00 35.22  ?  441  SER D C   1 
ATOM   9418  O O   . SER D  1  441 ? -26.123 -6.596  -0.704  1.00 36.66  ?  441  SER D O   1 
ATOM   9419  C CB  . SER D  1  441 ? -25.961 -8.352  1.417   1.00 37.56  ?  441  SER D CB  1 
ATOM   9420  O OG  . SER D  1  441 ? -25.764 -9.539  2.167   1.00 38.09  ?  441  SER D OG  1 
ATOM   9421  N N   . PHE D  1  442 ? -23.919 -6.167  -0.780  1.00 35.99  ?  442  PHE D N   1 
ATOM   9422  C CA  . PHE D  1  442 ? -24.066 -5.160  -1.820  1.00 35.79  ?  442  PHE D CA  1 
ATOM   9423  C C   . PHE D  1  442 ? -24.553 -5.809  -3.109  1.00 36.29  ?  442  PHE D C   1 
ATOM   9424  O O   . PHE D  1  442 ? -24.217 -6.954  -3.421  1.00 35.74  ?  442  PHE D O   1 
ATOM   9425  C CB  . PHE D  1  442 ? -22.739 -4.440  -2.060  1.00 34.19  ?  442  PHE D CB  1 
ATOM   9426  C CG  . PHE D  1  442 ? -22.353 -3.496  -0.959  1.00 34.08  ?  442  PHE D CG  1 
ATOM   9427  C CD1 . PHE D  1  442 ? -23.036 -2.304  -0.779  1.00 34.96  ?  442  PHE D CD1 1 
ATOM   9428  C CD2 . PHE D  1  442 ? -21.307 -3.799  -0.104  1.00 33.15  ?  442  PHE D CD2 1 
ATOM   9429  C CE1 . PHE D  1  442 ? -22.683 -1.433  0.235   1.00 35.05  ?  442  PHE D CE1 1 
ATOM   9430  C CE2 . PHE D  1  442 ? -20.948 -2.932  0.911   1.00 33.09  ?  442  PHE D CE2 1 
ATOM   9431  C CZ  . PHE D  1  442 ? -21.635 -1.748  1.080   1.00 33.91  ?  442  PHE D CZ  1 
ATOM   9432  N N   . SER D  1  443 ? -25.353 -5.061  -3.866  1.00 36.01  ?  443  SER D N   1 
ATOM   9433  C CA  . SER D  1  443 ? -26.037 -5.599  -5.031  1.00 36.85  ?  443  SER D CA  1 
ATOM   9434  C C   . SER D  1  443 ? -25.988 -4.585  -6.163  1.00 36.93  ?  443  SER D C   1 
ATOM   9435  O O   . SER D  1  443 ? -25.597 -3.429  -5.979  1.00 36.60  ?  443  SER D O   1 
ATOM   9436  C CB  . SER D  1  443 ? -27.490 -5.964  -4.707  1.00 38.97  ?  443  SER D CB  1 
ATOM   9437  O OG  . SER D  1  443 ? -28.140 -4.902  -4.030  1.00 40.13  ?  443  SER D OG  1 
ATOM   9438  N N   . GLY D  1  444 ? -26.380 -5.036  -7.346  1.00 42.57  ?  444  GLY D N   1 
ATOM   9439  C CA  . GLY D  1  444 ? -26.456 -4.194  -8.520  1.00 43.16  ?  444  GLY D CA  1 
ATOM   9440  C C   . GLY D  1  444 ? -25.572 -4.707  -9.639  1.00 41.70  ?  444  GLY D C   1 
ATOM   9441  O O   . GLY D  1  444 ? -24.848 -5.692  -9.500  1.00 40.50  ?  444  GLY D O   1 
ATOM   9442  N N   . ASP D  1  445 ? -25.647 -4.008  -10.767 1.00 42.36  ?  445  ASP D N   1 
ATOM   9443  C CA  . ASP D  1  445 ? -24.832 -4.350  -11.924 1.00 41.55  ?  445  ASP D CA  1 
ATOM   9444  C C   . ASP D  1  445 ? -23.412 -3.861  -11.672 1.00 39.83  ?  445  ASP D C   1 
ATOM   9445  O O   . ASP D  1  445 ? -23.193 -2.665  -11.450 1.00 39.90  ?  445  ASP D O   1 
ATOM   9446  C CB  . ASP D  1  445 ? -25.415 -3.728  -13.192 1.00 43.05  ?  445  ASP D CB  1 
ATOM   9447  C CG  . ASP D  1  445 ? -24.834 -4.325  -14.464 1.00 42.68  ?  445  ASP D CG  1 
ATOM   9448  O OD1 . ASP D  1  445 ? -23.633 -4.667  -14.482 1.00 41.23  ?  445  ASP D OD1 1 
ATOM   9449  O OD2 . ASP D  1  445 ? -25.587 -4.453  -15.452 1.00 44.15  -1 445  ASP D OD2 1 
ATOM   9450  N N   . ILE D  1  446 ? -22.453 -4.789  -11.693 1.00 39.98  ?  446  ILE D N   1 
ATOM   9451  C CA  . ILE D  1  446 ? -21.075 -4.449  -11.351 1.00 38.47  ?  446  ILE D CA  1 
ATOM   9452  C C   . ILE D  1  446 ? -20.520 -3.409  -12.318 1.00 38.63  ?  446  ILE D C   1 
ATOM   9453  O O   . ILE D  1  446 ? -19.741 -2.530  -11.928 1.00 38.21  ?  446  ILE D O   1 
ATOM   9454  C CB  . ILE D  1  446 ? -20.206 -5.722  -11.306 1.00 37.32  ?  446  ILE D CB  1 
ATOM   9455  C CG1 . ILE D  1  446 ? -18.762 -5.376  -10.931 1.00 36.01  ?  446  ILE D CG1 1 
ATOM   9456  C CG2 . ILE D  1  446 ? -20.279 -6.481  -12.626 1.00 37.72  ?  446  ILE D CG2 1 
ATOM   9457  C CD1 . ILE D  1  446 ? -18.546 -5.213  -9.439  1.00 35.54  ?  446  ILE D CD1 1 
ATOM   9458  N N   . SER D  1  447 ? -20.918 -3.481  -13.591 1.00 39.14  ?  447  SER D N   1 
ATOM   9459  C CA  . SER D  1  447 ? -20.487 -2.486  -14.565 1.00 39.63  ?  447  SER D CA  1 
ATOM   9460  C C   . SER D  1  447 ? -21.236 -1.169  -14.419 1.00 40.93  ?  447  SER D C   1 
ATOM   9461  O O   . SER D  1  447 ? -20.739 -0.135  -14.878 1.00 41.45  ?  447  SER D O   1 
ATOM   9462  C CB  . SER D  1  447 ? -20.663 -3.022  -15.987 1.00 40.42  ?  447  SER D CB  1 
ATOM   9463  O OG  . SER D  1  447 ? -22.035 -3.141  -16.324 1.00 42.59  ?  447  SER D OG  1 
ATOM   9464  N N   . GLU D  1  448 ? -22.413 -1.182  -13.793 1.00 40.90  ?  448  GLU D N   1 
ATOM   9465  C CA  . GLU D  1  448 ? -23.146 0.044   -13.510 1.00 42.27  ?  448  GLU D CA  1 
ATOM   9466  C C   . GLU D  1  448 ? -22.803 0.637   -12.153 1.00 41.49  ?  448  GLU D C   1 
ATOM   9467  O O   . GLU D  1  448 ? -23.115 1.807   -11.906 1.00 42.65  ?  448  GLU D O   1 
ATOM   9468  C CB  . GLU D  1  448 ? -24.657 -0.213  -13.561 1.00 44.16  ?  448  GLU D CB  1 
ATOM   9469  C CG  . GLU D  1  448 ? -25.305 0.005   -14.917 1.00 46.54  ?  448  GLU D CG  1 
ATOM   9470  C CD  . GLU D  1  448 ? -26.744 -0.481  -14.951 1.00 48.38  ?  448  GLU D CD  1 
ATOM   9471  O OE1 . GLU D  1  448 ? -27.342 -0.646  -13.866 1.00 48.16  ?  448  GLU D OE1 1 
ATOM   9472  O OE2 . GLU D  1  448 ? -27.276 -0.700  -16.059 1.00 49.40  -1 448  GLU D OE2 1 
ATOM   9473  N N   . ALA D  1  449 ? -22.163 -0.137  -11.275 1.00 38.03  ?  449  ALA D N   1 
ATOM   9474  C CA  . ALA D  1  449 ? -21.932 0.312   -9.907  1.00 37.44  ?  449  ALA D CA  1 
ATOM   9475  C C   . ALA D  1  449 ? -20.698 1.197   -9.793  1.00 36.52  ?  449  ALA D C   1 
ATOM   9476  O O   . ALA D  1  449 ? -20.715 2.196   -9.065  1.00 36.90  ?  449  ALA D O   1 
ATOM   9477  C CB  . ALA D  1  449 ? -21.806 -0.893  -8.975  1.00 36.44  ?  449  ALA D CB  1 
ATOM   9478  N N   . PHE D  1  450 ? -19.620 0.847   -10.488 1.00 33.37  ?  450  PHE D N   1 
ATOM   9479  C CA  . PHE D  1  450 ? -18.337 1.519   -10.339 1.00 32.50  ?  450  PHE D CA  1 
ATOM   9480  C C   . PHE D  1  450 ? -17.948 2.228   -11.629 1.00 33.20  ?  450  PHE D C   1 
ATOM   9481  O O   . PHE D  1  450 ? -18.173 1.711   -12.728 1.00 33.67  ?  450  PHE D O   1 
ATOM   9482  C CB  . PHE D  1  450 ? -17.248 0.521   -9.938  1.00 31.04  ?  450  PHE D CB  1 
ATOM   9483  C CG  . PHE D  1  450 ? -17.503 -0.151  -8.619  1.00 30.69  ?  450  PHE D CG  1 
ATOM   9484  C CD1 . PHE D  1  450 ? -17.269 0.519   -7.429  1.00 30.87  ?  450  PHE D CD1 1 
ATOM   9485  C CD2 . PHE D  1  450 ? -17.997 -1.443  -8.569  1.00 30.49  ?  450  PHE D CD2 1 
ATOM   9486  C CE1 . PHE D  1  450 ? -17.508 -0.094  -6.213  1.00 30.83  ?  450  PHE D CE1 1 
ATOM   9487  C CE2 . PHE D  1  450 ? -18.240 -2.061  -7.357  1.00 30.28  ?  450  PHE D CE2 1 
ATOM   9488  C CZ  . PHE D  1  450 ? -17.995 -1.385  -6.177  1.00 30.43  ?  450  PHE D CZ  1 
ATOM   9489  N N   . GLY D  1  451 ? -17.367 3.417   -11.484 1.00 31.12  ?  451  GLY D N   1 
ATOM   9490  C CA  . GLY D  1  451 ? -16.834 4.161   -12.610 1.00 31.89  ?  451  GLY D CA  1 
ATOM   9491  C C   . GLY D  1  451 ? -15.360 3.892   -12.837 1.00 30.79  ?  451  GLY D C   1 
ATOM   9492  O O   . GLY D  1  451 ? -14.898 2.759   -12.671 1.00 29.62  ?  451  GLY D O   1 
ATOM   9493  N N   . VAL D  1  452 ? -14.611 4.924   -13.223 1.00 30.07  ?  452  VAL D N   1 
ATOM   9494  C CA  . VAL D  1  452 ? -13.166 4.826   -13.408 1.00 29.33  ?  452  VAL D CA  1 
ATOM   9495  C C   . VAL D  1  452 ? -12.477 5.465   -12.211 1.00 28.71  ?  452  VAL D C   1 
ATOM   9496  O O   . VAL D  1  452 ? -12.964 6.458   -11.654 1.00 29.38  ?  452  VAL D O   1 
ATOM   9497  C CB  . VAL D  1  452 ? -12.721 5.491   -14.726 1.00 30.63  ?  452  VAL D CB  1 
ATOM   9498  C CG1 . VAL D  1  452 ? -13.134 4.637   -15.917 1.00 31.06  ?  452  VAL D CG1 1 
ATOM   9499  C CG2 . VAL D  1  452 ? -13.300 6.895   -14.840 1.00 32.24  ?  452  VAL D CG2 1 
ATOM   9500  N N   . TYR D  1  453 ? -11.340 4.896   -11.812 1.00 29.01  ?  453  TYR D N   1 
ATOM   9501  C CA  . TYR D  1  453 ? -10.593 5.368   -10.647 1.00 29.47  ?  453  TYR D CA  1 
ATOM   9502  C C   . TYR D  1  453 ? -9.108  5.397   -10.980 1.00 29.88  ?  453  TYR D C   1 
ATOM   9503  O O   . TYR D  1  453 ? -8.401  4.392   -10.828 1.00 29.87  ?  453  TYR D O   1 
ATOM   9504  C CB  . TYR D  1  453 ? -10.860 4.494   -9.421  1.00 29.12  ?  453  TYR D CB  1 
ATOM   9505  C CG  . TYR D  1  453 ? -12.323 4.213   -9.162  1.00 28.46  ?  453  TYR D CG  1 
ATOM   9506  C CD1 . TYR D  1  453 ? -13.138 5.174   -8.583  1.00 28.72  ?  453  TYR D CD1 1 
ATOM   9507  C CD2 . TYR D  1  453 ? -12.887 2.985   -9.483  1.00 27.99  ?  453  TYR D CD2 1 
ATOM   9508  C CE1 . TYR D  1  453 ? -14.474 4.928   -8.339  1.00 28.70  ?  453  TYR D CE1 1 
ATOM   9509  C CE2 . TYR D  1  453 ? -14.226 2.728   -9.241  1.00 27.89  ?  453  TYR D CE2 1 
ATOM   9510  C CZ  . TYR D  1  453 ? -15.013 3.705   -8.668  1.00 28.34  ?  453  TYR D CZ  1 
ATOM   9511  O OH  . TYR D  1  453 ? -16.345 3.461   -8.423  1.00 28.72  ?  453  TYR D OH  1 
ATOM   9512  N N   . PRO D  1  454 ? -8.597  6.543   -11.439 1.00 27.78  ?  454  PRO D N   1 
ATOM   9513  C CA  . PRO D  1  454 ? -7.184  6.605   -11.849 1.00 27.94  ?  454  PRO D CA  1 
ATOM   9514  C C   . PRO D  1  454 ? -6.198  6.386   -10.712 1.00 28.29  ?  454  PRO D C   1 
ATOM   9515  O O   . PRO D  1  454 ? -5.056  5.992   -10.980 1.00 28.62  ?  454  PRO D O   1 
ATOM   9516  C CB  . PRO D  1  454 ? -7.044  8.018   -12.439 1.00 29.54  ?  454  PRO D CB  1 
ATOM   9517  C CG  . PRO D  1  454 ? -8.447  8.552   -12.571 1.00 30.28  ?  454  PRO D CG  1 
ATOM   9518  C CD  . PRO D  1  454 ? -9.264  7.849   -11.542 1.00 29.07  ?  454  PRO D CD  1 
ATOM   9519  N N   . THR D  1  455 ? -6.590  6.632   -9.462  1.00 26.90  ?  455  THR D N   1 
ATOM   9520  C CA  . THR D  1  455 ? -5.704  6.456   -8.319  1.00 27.20  ?  455  THR D CA  1 
ATOM   9521  C C   . THR D  1  455 ? -6.033  5.212   -7.502  1.00 26.31  ?  455  THR D C   1 
ATOM   9522  O O   . THR D  1  455 ? -5.527  5.067   -6.384  1.00 25.78  ?  455  THR D O   1 
ATOM   9523  C CB  . THR D  1  455 ? -5.742  7.695   -7.421  1.00 27.37  ?  455  THR D CB  1 
ATOM   9524  O OG1 . THR D  1  455 ? -7.083  7.925   -6.972  1.00 27.34  ?  455  THR D OG1 1 
ATOM   9525  C CG2 . THR D  1  455 ? -5.254  8.920   -8.183  1.00 28.12  ?  455  THR D CG2 1 
ATOM   9526  N N   . LEU D  1  456 ? -6.866  4.316   -8.026  1.00 28.06  ?  456  LEU D N   1 
ATOM   9527  C CA  . LEU D  1  456 ? -7.242  3.122   -7.281  1.00 26.96  ?  456  LEU D CA  1 
ATOM   9528  C C   . LEU D  1  456 ? -6.050  2.180   -7.156  1.00 27.07  ?  456  LEU D C   1 
ATOM   9529  O O   . LEU D  1  456 ? -5.377  1.874   -8.146  1.00 27.36  ?  456  LEU D O   1 
ATOM   9530  C CB  . LEU D  1  456 ? -8.412  2.416   -7.962  1.00 26.67  ?  456  LEU D CB  1 
ATOM   9531  C CG  . LEU D  1  456 ? -9.145  1.350   -7.146  1.00 26.10  ?  456  LEU D CG  1 
ATOM   9532  C CD1 . LEU D  1  456 ? -9.727  1.953   -5.878  1.00 26.28  ?  456  LEU D CD1 1 
ATOM   9533  C CD2 . LEU D  1  456 ? -10.237 0.704   -7.983  1.00 25.49  ?  456  LEU D CD2 1 
ATOM   9534  N N   . ASN D  1  457 ? -5.795  1.718   -5.934  1.00 26.39  ?  457  ASN D N   1 
ATOM   9535  C CA  . ASN D  1  457 ? -4.685  0.823   -5.636  1.00 26.55  ?  457  ASN D CA  1 
ATOM   9536  C C   . ASN D  1  457 ? -5.146  -0.562  -5.209  1.00 26.29  ?  457  ASN D C   1 
ATOM   9537  O O   . ASN D  1  457 ? -4.654  -1.568  -5.730  1.00 26.12  ?  457  ASN D O   1 
ATOM   9538  C CB  . ASN D  1  457 ? -3.800  1.437   -4.542  1.00 26.49  ?  457  ASN D CB  1 
ATOM   9539  C CG  . ASN D  1  457 ? -2.698  0.499   -4.086  1.00 26.73  ?  457  ASN D CG  1 
ATOM   9540  O OD1 . ASN D  1  457 ? -2.863  -0.244  -3.119  1.00 26.54  ?  457  ASN D OD1 1 
ATOM   9541  N ND2 . ASN D  1  457 ? -1.565  0.535   -4.777  1.00 26.77  ?  457  ASN D ND2 1 
ATOM   9542  N N   . PHE D  1  458 ? -6.087  -0.640  -4.271  1.00 23.90  ?  458  PHE D N   1 
ATOM   9543  C CA  . PHE D  1  458 ? -6.548  -1.905  -3.718  1.00 23.28  ?  458  PHE D CA  1 
ATOM   9544  C C   . PHE D  1  458 ? -8.064  -1.858  -3.621  1.00 23.32  ?  458  PHE D C   1 
ATOM   9545  O O   . PHE D  1  458 ? -8.624  -0.874  -3.130  1.00 23.52  ?  458  PHE D O   1 
ATOM   9546  C CB  . PHE D  1  458 ? -5.924  -2.151  -2.334  1.00 23.27  ?  458  PHE D CB  1 
ATOM   9547  C CG  . PHE D  1  458 ? -6.155  -3.536  -1.787  1.00 23.25  ?  458  PHE D CG  1 
ATOM   9548  C CD1 . PHE D  1  458 ? -7.397  -3.918  -1.305  1.00 23.29  ?  458  PHE D CD1 1 
ATOM   9549  C CD2 . PHE D  1  458 ? -5.113  -4.446  -1.723  1.00 23.42  ?  458  PHE D CD2 1 
ATOM   9550  C CE1 . PHE D  1  458 ? -7.602  -5.188  -0.798  1.00 23.49  ?  458  PHE D CE1 1 
ATOM   9551  C CE2 . PHE D  1  458 ? -5.310  -5.717  -1.217  1.00 23.62  ?  458  PHE D CE2 1 
ATOM   9552  C CZ  . PHE D  1  458 ? -6.556  -6.088  -0.753  1.00 23.65  ?  458  PHE D CZ  1 
ATOM   9553  N N   . ILE D  1  459 ? -8.725  -2.917  -4.086  1.00 24.69  ?  459  ILE D N   1 
ATOM   9554  C CA  . ILE D  1  459 ? -10.179 -3.025  -4.022  1.00 24.25  ?  459  ILE D CA  1 
ATOM   9555  C C   . ILE D  1  459 ? -10.543 -4.476  -3.735  1.00 23.75  ?  459  ILE D C   1 
ATOM   9556  O O   . ILE D  1  459 ? -9.995  -5.394  -4.354  1.00 23.70  ?  459  ILE D O   1 
ATOM   9557  C CB  . ILE D  1  459 ? -10.855 -2.526  -5.316  1.00 24.58  ?  459  ILE D CB  1 
ATOM   9558  C CG1 . ILE D  1  459 ? -12.373 -2.707  -5.235  1.00 24.20  ?  459  ILE D CG1 1 
ATOM   9559  C CG2 . ILE D  1  459 ? -10.273 -3.219  -6.543  1.00 24.43  ?  459  ILE D CG2 1 
ATOM   9560  C CD1 . ILE D  1  459 ? -13.150 -1.743  -6.107  1.00 24.48  ?  459  ILE D CD1 1 
ATOM   9561  N N   . ASP D  1  460 ? -11.452 -4.685  -2.783  1.00 25.88  ?  460  ASP D N   1 
ATOM   9562  C CA  . ASP D  1  460 ? -11.850 -6.032  -2.371  1.00 26.27  ?  460  ASP D CA  1 
ATOM   9563  C C   . ASP D  1  460 ? -13.368 -6.047  -2.212  1.00 26.66  ?  460  ASP D C   1 
ATOM   9564  O O   . ASP D  1  460 ? -13.898 -5.590  -1.195  1.00 27.25  ?  460  ASP D O   1 
ATOM   9565  C CB  . ASP D  1  460 ? -11.143 -6.439  -1.084  1.00 26.82  ?  460  ASP D CB  1 
ATOM   9566  C CG  . ASP D  1  460 ? -11.265 -7.922  -0.793  1.00 27.92  ?  460  ASP D CG  1 
ATOM   9567  O OD1 . ASP D  1  460 ? -11.871 -8.644  -1.611  1.00 28.19  ?  460  ASP D OD1 1 
ATOM   9568  O OD2 . ASP D  1  460 ? -10.742 -8.368  0.251   1.00 28.89  -1 460  ASP D OD2 1 
ATOM   9569  N N   . LEU D  1  461 ? -14.060 -6.584  -3.219  1.00 24.95  ?  461  LEU D N   1 
ATOM   9570  C CA  . LEU D  1  461 ? -15.514 -6.667  -3.237  1.00 25.23  ?  461  LEU D CA  1 
ATOM   9571  C C   . LEU D  1  461 ? -16.015 -8.069  -2.910  1.00 26.28  ?  461  LEU D C   1 
ATOM   9572  O O   . LEU D  1  461 ? -17.175 -8.389  -3.192  1.00 26.58  ?  461  LEU D O   1 
ATOM   9573  C CB  . LEU D  1  461 ? -16.051 -6.227  -4.600  1.00 24.73  ?  461  LEU D CB  1 
ATOM   9574  C CG  . LEU D  1  461 ? -15.510 -4.915  -5.167  1.00 24.33  ?  461  LEU D CG  1 
ATOM   9575  C CD1 . LEU D  1  461 ? -15.979 -4.725  -6.601  1.00 24.25  ?  461  LEU D CD1 1 
ATOM   9576  C CD2 . LEU D  1  461 ? -15.937 -3.743  -4.301  1.00 24.41  ?  461  LEU D CD2 1 
ATOM   9577  N N   . SER D  1  462 ? -15.162 -8.906  -2.324  1.00 27.22  ?  462  SER D N   1 
ATOM   9578  C CA  . SER D  1  462 ? -15.469 -10.315 -2.147  1.00 28.44  ?  462  SER D CA  1 
ATOM   9579  C C   . SER D  1  462 ? -16.652 -10.511 -1.202  1.00 29.58  ?  462  SER D C   1 
ATOM   9580  O O   . SER D  1  462 ? -16.953 -9.670  -0.349  1.00 29.54  ?  462  SER D O   1 
ATOM   9581  C CB  . SER D  1  462 ? -14.249 -11.062 -1.611  1.00 29.25  ?  462  SER D CB  1 
ATOM   9582  O OG  . SER D  1  462 ? -13.067 -10.615 -2.250  1.00 28.04  ?  462  SER D OG  1 
ATOM   9583  N N   . ASN D  1  463 ? -17.326 -11.650 -1.373  1.00 31.68  ?  463  ASN D N   1 
ATOM   9584  C CA  . ASN D  1  463 ? -18.466 -12.044 -0.547  1.00 33.12  ?  463  ASN D CA  1 
ATOM   9585  C C   . ASN D  1  463 ? -19.569 -10.984 -0.592  1.00 32.13  ?  463  ASN D C   1 
ATOM   9586  O O   . ASN D  1  463 ? -19.937 -10.378 0.417   1.00 32.35  ?  463  ASN D O   1 
ATOM   9587  C CB  . ASN D  1  463 ? -18.020 -12.329 0.891   1.00 35.03  ?  463  ASN D CB  1 
ATOM   9588  C CG  . ASN D  1  463 ? -16.880 -13.327 0.958   1.00 36.05  ?  463  ASN D CG  1 
ATOM   9589  O OD1 . ASN D  1  463 ? -16.769 -14.218 0.116   1.00 35.97  ?  463  ASN D OD1 1 
ATOM   9590  N ND2 . ASN D  1  463 ? -16.024 -13.178 1.961   1.00 37.47  ?  463  ASN D ND2 1 
ATOM   9591  N N   . ASN D  1  464 ? -20.089 -10.767 -1.797  1.00 35.56  ?  464  ASN D N   1 
ATOM   9592  C CA  . ASN D  1  464 ? -21.142 -9.788  -2.032  1.00 34.63  ?  464  ASN D CA  1 
ATOM   9593  C C   . ASN D  1  464 ? -22.095 -10.362 -3.076  1.00 34.61  ?  464  ASN D C   1 
ATOM   9594  O O   . ASN D  1  464 ? -21.980 -11.523 -3.479  1.00 35.32  ?  464  ASN D O   1 
ATOM   9595  C CB  . ASN D  1  464 ? -20.547 -8.439  -2.455  1.00 33.18  ?  464  ASN D CB  1 
ATOM   9596  C CG  . ASN D  1  464 ? -20.154 -7.580  -1.269  1.00 33.16  ?  464  ASN D CG  1 
ATOM   9597  O OD1 . ASN D  1  464 ? -21.008 -7.009  -0.592  1.00 33.23  ?  464  ASN D OD1 1 
ATOM   9598  N ND2 . ASN D  1  464 ? -18.855 -7.490  -1.008  1.00 33.01  ?  464  ASN D ND2 1 
ATOM   9599  N N   . ASN D  1  465 ? -23.042 -9.541  -3.523  1.00 38.49  ?  465  ASN D N   1 
ATOM   9600  C CA  . ASN D  1  465 ? -24.095 -9.969  -4.435  1.00 39.56  ?  465  ASN D CA  1 
ATOM   9601  C C   . ASN D  1  465 ? -24.091 -9.135  -5.710  1.00 39.16  ?  465  ASN D C   1 
ATOM   9602  O O   . ASN D  1  465 ? -25.142 -8.751  -6.229  1.00 40.77  ?  465  ASN D O   1 
ATOM   9603  C CB  . ASN D  1  465 ? -25.463 -9.899  -3.759  1.00 41.34  ?  465  ASN D CB  1 
ATOM   9604  C CG  . ASN D  1  465 ? -25.934 -11.246 -3.253  1.00 42.98  ?  465  ASN D CG  1 
ATOM   9605  O OD1 . ASN D  1  465 ? -26.436 -12.069 -4.020  1.00 43.96  ?  465  ASN D OD1 1 
ATOM   9606  N ND2 . ASN D  1  465 ? -25.780 -11.477 -1.955  1.00 43.45  ?  465  ASN D ND2 1 
ATOM   9607  N N   . PHE D  1  466 ? -22.903 -8.843  -6.231  1.00 36.66  ?  466  PHE D N   1 
ATOM   9608  C CA  . PHE D  1  466 ? -22.790 -8.132  -7.496  1.00 36.46  ?  466  PHE D CA  1 
ATOM   9609  C C   . PHE D  1  466 ? -23.024 -9.094  -8.653  1.00 36.85  ?  466  PHE D C   1 
ATOM   9610  O O   . PHE D  1  466 ? -22.390 -10.151 -8.732  1.00 36.27  ?  466  PHE D O   1 
ATOM   9611  C CB  . PHE D  1  466 ? -21.417 -7.474  -7.627  1.00 34.99  ?  466  PHE D CB  1 
ATOM   9612  C CG  . PHE D  1  466 ? -21.195 -6.336  -6.674  1.00 34.71  ?  466  PHE D CG  1 
ATOM   9613  C CD1 . PHE D  1  466 ? -21.937 -5.171  -6.782  1.00 35.58  ?  466  PHE D CD1 1 
ATOM   9614  C CD2 . PHE D  1  466 ? -20.240 -6.426  -5.676  1.00 33.82  ?  466  PHE D CD2 1 
ATOM   9615  C CE1 . PHE D  1  466 ? -21.734 -4.119  -5.909  1.00 35.44  ?  466  PHE D CE1 1 
ATOM   9616  C CE2 . PHE D  1  466 ? -20.032 -5.376  -4.800  1.00 33.66  ?  466  PHE D CE2 1 
ATOM   9617  C CZ  . PHE D  1  466 ? -20.780 -4.221  -4.918  1.00 34.41  ?  466  PHE D CZ  1 
ATOM   9618  N N   . HIS D  1  467 ? -23.944 -8.733  -9.539  1.00 39.00  ?  467  HIS D N   1 
ATOM   9619  C CA  . HIS D  1  467 ? -24.199 -9.477  -10.762 1.00 39.54  ?  467  HIS D CA  1 
ATOM   9620  C C   . HIS D  1  467 ? -23.746 -8.657  -11.963 1.00 39.29  ?  467  HIS D C   1 
ATOM   9621  O O   . HIS D  1  467 ? -23.333 -7.501  -11.838 1.00 38.85  ?  467  HIS D O   1 
ATOM   9622  C CB  . HIS D  1  467 ? -25.684 -9.844  -10.877 1.00 41.47  ?  467  HIS D CB  1 
ATOM   9623  C CG  . HIS D  1  467 ? -26.569 -8.687  -11.221 1.00 43.24  ?  467  HIS D CG  1 
ATOM   9624  N ND1 . HIS D  1  467 ? -27.082 -7.833  -10.268 1.00 43.35  ?  467  HIS D ND1 1 
ATOM   9625  C CD2 . HIS D  1  467 ? -27.043 -8.249  -12.411 1.00 44.41  ?  467  HIS D CD2 1 
ATOM   9626  C CE1 . HIS D  1  467 ? -27.827 -6.916  -10.857 1.00 44.70  ?  467  HIS D CE1 1 
ATOM   9627  N NE2 . HIS D  1  467 ? -27.821 -7.145  -12.157 1.00 45.01  ?  467  HIS D NE2 1 
ATOM   9628  N N   . GLY D  1  468 ? -23.823 -9.270  -13.135 1.00 39.63  ?  468  GLY D N   1 
ATOM   9629  C CA  . GLY D  1  468 ? -23.417 -8.611  -14.359 1.00 39.65  ?  468  GLY D CA  1 
ATOM   9630  C C   . GLY D  1  468 ? -22.019 -9.005  -14.789 1.00 38.26  ?  468  GLY D C   1 
ATOM   9631  O O   . GLY D  1  468 ? -21.373 -9.891  -14.221 1.00 37.34  ?  468  GLY D O   1 
ATOM   9632  N N   . GLN D  1  469 ? -21.546 -8.316  -15.822 1.00 40.61  ?  469  GLN D N   1 
ATOM   9633  C CA  . GLN D  1  469 ? -20.239 -8.571  -16.405 1.00 39.63  ?  469  GLN D CA  1 
ATOM   9634  C C   . GLN D  1  469 ? -19.268 -7.458  -16.033 1.00 38.73  ?  469  GLN D C   1 
ATOM   9635  O O   . GLN D  1  469 ? -19.670 -6.324  -15.760 1.00 39.15  ?  469  GLN D O   1 
ATOM   9636  C CB  . GLN D  1  469 ? -20.331 -8.689  -17.929 1.00 40.57  ?  469  GLN D CB  1 
ATOM   9637  C CG  . GLN D  1  469 ? -21.591 -9.383  -18.417 1.00 41.98  ?  469  GLN D CG  1 
ATOM   9638  C CD  . GLN D  1  469 ? -21.508 -9.782  -19.876 1.00 42.95  ?  469  GLN D CD  1 
ATOM   9639  O OE1 . GLN D  1  469 ? -20.503 -9.535  -20.543 1.00 42.42  ?  469  GLN D OE1 1 
ATOM   9640  N NE2 . GLN D  1  469 ? -22.568 -10.404 -20.380 1.00 44.72  ?  469  GLN D NE2 1 
ATOM   9641  N N   . LEU D  1  470 ? -17.982 -7.797  -16.033 1.00 35.15  ?  470  LEU D N   1 
ATOM   9642  C CA  . LEU D  1  470 ? -16.953 -6.830  -15.677 1.00 34.37  ?  470  LEU D CA  1 
ATOM   9643  C C   . LEU D  1  470 ? -16.842 -5.759  -16.753 1.00 35.16  ?  470  LEU D C   1 
ATOM   9644  O O   . LEU D  1  470 ? -16.701 -6.065  -17.940 1.00 35.76  ?  470  LEU D O   1 
ATOM   9645  C CB  . LEU D  1  470 ? -15.608 -7.530  -15.485 1.00 33.57  ?  470  LEU D CB  1 
ATOM   9646  C CG  . LEU D  1  470 ? -15.460 -8.413  -14.244 1.00 33.01  ?  470  LEU D CG  1 
ATOM   9647  C CD1 . LEU D  1  470 ? -13.996 -8.550  -13.859 1.00 32.43  ?  470  LEU D CD1 1 
ATOM   9648  C CD2 . LEU D  1  470 ? -16.270 -7.857  -13.082 1.00 32.99  ?  470  LEU D CD2 1 
ATOM   9649  N N   . SER D  1  471 ? -16.923 -4.501  -16.335 1.00 35.64  ?  471  SER D N   1 
ATOM   9650  C CA  . SER D  1  471 ? -16.724 -3.397  -17.257 1.00 36.53  ?  471  SER D CA  1 
ATOM   9651  C C   . SER D  1  471 ? -15.250 -3.270  -17.622 1.00 35.92  ?  471  SER D C   1 
ATOM   9652  O O   . SER D  1  471 ? -14.360 -3.553  -16.816 1.00 34.90  ?  471  SER D O   1 
ATOM   9653  C CB  . SER D  1  471 ? -17.224 -2.090  -16.644 1.00 37.03  ?  471  SER D CB  1 
ATOM   9654  O OG  . SER D  1  471 ? -16.845 -0.978  -17.435 1.00 38.08  ?  471  SER D OG  1 
ATOM   9655  N N   . ALA D  1  472 ? -14.995 -2.836  -18.855 1.00 33.41  ?  472  ALA D N   1 
ATOM   9656  C CA  . ALA D  1  472 ? -13.629 -2.520  -19.252 1.00 33.21  ?  472  ALA D CA  1 
ATOM   9657  C C   . ALA D  1  472 ? -13.125 -1.232  -18.617 1.00 33.11  ?  472  ALA D C   1 
ATOM   9658  O O   . ALA D  1  472 ? -12.000 -0.812  -18.912 1.00 33.17  ?  472  ALA D O   1 
ATOM   9659  C CB  . ALA D  1  472 ? -13.534 -2.424  -20.776 1.00 34.56  ?  472  ALA D CB  1 
ATOM   9660  N N   . ASN D  1  473 ? -13.932 -0.603  -17.758 1.00 35.84  ?  473  ASN D N   1 
ATOM   9661  C CA  . ASN D  1  473 ? -13.517 0.622   -17.083 1.00 35.83  ?  473  ASN D CA  1 
ATOM   9662  C C   . ASN D  1  473 ? -12.318 0.391   -16.173 1.00 34.73  ?  473  ASN D C   1 
ATOM   9663  O O   . ASN D  1  473 ? -11.532 1.317   -15.940 1.00 35.60  ?  473  ASN D O   1 
ATOM   9664  C CB  . ASN D  1  473 ? -14.684 1.194   -16.277 1.00 36.67  ?  473  ASN D CB  1 
ATOM   9665  C CG  . ASN D  1  473 ? -15.730 1.858   -17.153 1.00 38.46  ?  473  ASN D CG  1 
ATOM   9666  O OD1 . ASN D  1  473 ? -15.525 2.047   -18.352 1.00 39.36  ?  473  ASN D OD1 1 
ATOM   9667  N ND2 . ASN D  1  473 ? -16.863 2.208   -16.555 1.00 38.50  ?  473  ASN D ND2 1 
ATOM   9668  N N   . TRP D  1  474 ? -12.167 -0.826  -15.642 1.00 33.26  ?  474  TRP D N   1 
ATOM   9669  C CA  . TRP D  1  474 ? -11.084 -1.100  -14.701 1.00 32.80  ?  474  TRP D CA  1 
ATOM   9670  C C   . TRP D  1  474 ? -9.712  -0.882  -15.326 1.00 33.32  ?  474  TRP D C   1 
ATOM   9671  O O   . TRP D  1  474 ? -8.739  -0.623  -14.606 1.00 33.63  ?  474  TRP D O   1 
ATOM   9672  C CB  . TRP D  1  474 ? -11.194 -2.528  -14.162 1.00 32.01  ?  474  TRP D CB  1 
ATOM   9673  C CG  . TRP D  1  474 ? -12.477 -2.809  -13.443 1.00 31.67  ?  474  TRP D CG  1 
ATOM   9674  C CD1 . TRP D  1  474 ? -13.520 -3.566  -13.888 1.00 31.80  ?  474  TRP D CD1 1 
ATOM   9675  C CD2 . TRP D  1  474 ? -12.852 -2.332  -12.144 1.00 31.68  ?  474  TRP D CD2 1 
ATOM   9676  N NE1 . TRP D  1  474 ? -14.522 -3.592  -12.947 1.00 32.10  ?  474  TRP D NE1 1 
ATOM   9677  C CE2 . TRP D  1  474 ? -14.136 -2.841  -11.868 1.00 31.58  ?  474  TRP D CE2 1 
ATOM   9678  C CE3 . TRP D  1  474 ? -12.227 -1.524  -11.190 1.00 32.01  ?  474  TRP D CE3 1 
ATOM   9679  C CZ2 . TRP D  1  474 ? -14.806 -2.569  -10.677 1.00 31.81  ?  474  TRP D CZ2 1 
ATOM   9680  C CZ3 . TRP D  1  474 ? -12.893 -1.255  -10.009 1.00 32.20  ?  474  TRP D CZ3 1 
ATOM   9681  C CH2 . TRP D  1  474 ? -14.169 -1.776  -9.762  1.00 32.10  ?  474  TRP D CH2 1 
ATOM   9682  N N   . GLU D  1  475 ? -9.607  -0.988  -16.655 1.00 34.87  ?  475  GLU D N   1 
ATOM   9683  C CA  . GLU D  1  475 ? -8.321  -0.773  -17.311 1.00 35.73  ?  475  GLU D CA  1 
ATOM   9684  C C   . GLU D  1  475 ? -7.799  0.638   -17.069 1.00 36.41  ?  475  GLU D C   1 
ATOM   9685  O O   . GLU D  1  475 ? -6.582  0.845   -16.984 1.00 37.15  ?  475  GLU D O   1 
ATOM   9686  C CB  . GLU D  1  475 ? -8.446  -1.041  -18.811 1.00 36.37  ?  475  GLU D CB  1 
ATOM   9687  C CG  . GLU D  1  475 ? -7.163  -0.829  -19.595 1.00 37.43  ?  475  GLU D CG  1 
ATOM   9688  C CD  . GLU D  1  475 ? -7.419  -0.582  -21.066 1.00 39.22  ?  475  GLU D CD  1 
ATOM   9689  O OE1 . GLU D  1  475 ? -8.521  -0.101  -21.400 1.00 39.64  ?  475  GLU D OE1 1 
ATOM   9690  O OE2 . GLU D  1  475 ? -6.521  -0.866  -21.887 1.00 40.38  -1 475  GLU D OE2 1 
ATOM   9691  N N   . GLN D  1  476 ? -8.698  1.615   -16.932 1.00 35.19  ?  476  GLN D N   1 
ATOM   9692  C CA  . GLN D  1  476 ? -8.289  2.985   -16.651 1.00 35.77  ?  476  GLN D CA  1 
ATOM   9693  C C   . GLN D  1  476 ? -7.713  3.148   -15.252 1.00 35.55  ?  476  GLN D C   1 
ATOM   9694  O O   . GLN D  1  476 ? -7.087  4.177   -14.975 1.00 36.48  ?  476  GLN D O   1 
ATOM   9695  C CB  . GLN D  1  476 ? -9.471  3.936   -16.844 1.00 36.35  ?  476  GLN D CB  1 
ATOM   9696  C CG  . GLN D  1  476 ? -10.150 3.806   -18.197 1.00 37.23  ?  476  GLN D CG  1 
ATOM   9697  C CD  . GLN D  1  476 ? -10.625 5.138   -18.737 1.00 39.38  ?  476  GLN D CD  1 
ATOM   9698  O OE1 . GLN D  1  476 ? -10.724 6.118   -18.001 1.00 39.63  ?  476  GLN D OE1 1 
ATOM   9699  N NE2 . GLN D  1  476 ? -10.920 5.181   -20.032 1.00 41.36  ?  476  GLN D NE2 1 
ATOM   9700  N N   . SER D  1  477 ? -7.919  2.173   -14.367 1.00 34.06  ?  477  SER D N   1 
ATOM   9701  C CA  . SER D  1  477 ? -7.248  2.133   -13.068 1.00 34.48  ?  477  SER D CA  1 
ATOM   9702  C C   . SER D  1  477 ? -5.864  1.509   -13.253 1.00 35.03  ?  477  SER D C   1 
ATOM   9703  O O   . SER D  1  477 ? -5.552  0.426   -12.755 1.00 35.32  ?  477  SER D O   1 
ATOM   9704  C CB  . SER D  1  477 ? -8.083  1.361   -12.055 1.00 33.47  ?  477  SER D CB  1 
ATOM   9705  O OG  . SER D  1  477 ? -9.337  1.983   -11.842 1.00 33.24  ?  477  SER D OG  1 
ATOM   9706  N N   . GLN D  1  478 ? -5.022  2.225   -14.001 1.00 34.13  ?  478  GLN D N   1 
ATOM   9707  C CA  . GLN D  1  478 ? -3.734  1.683   -14.416 1.00 34.96  ?  478  GLN D CA  1 
ATOM   9708  C C   . GLN D  1  478 ? -2.774  1.464   -13.254 1.00 35.50  ?  478  GLN D C   1 
ATOM   9709  O O   . GLN D  1  478 ? -1.774  0.760   -13.426 1.00 36.17  ?  478  GLN D O   1 
ATOM   9710  C CB  . GLN D  1  478 ? -3.089  2.602   -15.456 1.00 35.77  ?  478  GLN D CB  1 
ATOM   9711  C CG  . GLN D  1  478 ? -3.600  2.373   -16.871 1.00 35.86  ?  478  GLN D CG  1 
ATOM   9712  C CD  . GLN D  1  478 ? -3.182  1.027   -17.433 1.00 36.43  ?  478  GLN D CD  1 
ATOM   9713  O OE1 . GLN D  1  478 ? -2.106  0.516   -17.122 1.00 36.76  ?  478  GLN D OE1 1 
ATOM   9714  N NE2 . GLN D  1  478 ? -4.038  0.442   -18.264 1.00 35.91  ?  478  GLN D NE2 1 
ATOM   9715  N N   . LYS D  1  479 ? -3.051  2.035   -12.083 1.00 33.87  ?  479  LYS D N   1 
ATOM   9716  C CA  . LYS D  1  479 ? -2.219  1.846   -10.904 1.00 33.61  ?  479  LYS D CA  1 
ATOM   9717  C C   . LYS D  1  479 ? -2.775  0.785   -9.964  1.00 32.49  ?  479  LYS D C   1 
ATOM   9718  O O   . LYS D  1  479 ? -2.277  0.637   -8.844  1.00 31.95  ?  479  LYS D O   1 
ATOM   9719  C CB  . LYS D  1  479 ? -2.043  3.171   -10.159 1.00 33.36  ?  479  LYS D CB  1 
ATOM   9720  C CG  . LYS D  1  479 ? -1.411  4.262   -11.004 1.00 34.18  ?  479  LYS D CG  1 
ATOM   9721  C CD  . LYS D  1  479 ? -0.868  5.389   -10.144 1.00 33.73  ?  479  LYS D CD  1 
ATOM   9722  C CE  . LYS D  1  479 ? -0.148  6.422   -10.994 1.00 34.44  ?  479  LYS D CE  1 
ATOM   9723  N NZ  . LYS D  1  479 ? 0.496   7.473   -10.161 1.00 35.18  ?  479  LYS D NZ  1 
ATOM   9724  N N   . LEU D  1  480 ? -3.792  0.046   -10.399 1.00 31.85  ?  480  LEU D N   1 
ATOM   9725  C CA  . LEU D  1  480 ? -4.376  -1.003  -9.575  1.00 30.59  ?  480  LEU D CA  1 
ATOM   9726  C C   . LEU D  1  480 ? -3.431  -2.193  -9.483  1.00 30.59  ?  480  LEU D C   1 
ATOM   9727  O O   . LEU D  1  480 ? -2.913  -2.670  -10.498 1.00 31.14  ?  480  LEU D O   1 
ATOM   9728  C CB  . LEU D  1  480 ? -5.721  -1.439  -10.156 1.00 29.99  ?  480  LEU D CB  1 
ATOM   9729  C CG  . LEU D  1  480 ? -6.615  -2.304  -9.268  1.00 29.14  ?  480  LEU D CG  1 
ATOM   9730  C CD1 . LEU D  1  480 ? -7.117  -1.510  -8.075  1.00 29.22  ?  480  LEU D CD1 1 
ATOM   9731  C CD2 . LEU D  1  480 ? -7.780  -2.866  -10.070 1.00 29.14  ?  480  LEU D CD2 1 
ATOM   9732  N N   . VAL D  1  481 ? -3.208  -2.670  -8.262  1.00 28.03  ?  481  VAL D N   1 
ATOM   9733  C CA  . VAL D  1  481 ? -2.345  -3.820  -8.033  1.00 28.15  ?  481  VAL D CA  1 
ATOM   9734  C C   . VAL D  1  481 ? -3.089  -5.010  -7.445  1.00 27.76  ?  481  VAL D C   1 
ATOM   9735  O O   . VAL D  1  481 ? -2.593  -6.144  -7.552  1.00 27.74  ?  481  VAL D O   1 
ATOM   9736  C CB  . VAL D  1  481 ? -1.145  -3.448  -7.134  1.00 28.51  ?  481  VAL D CB  1 
ATOM   9737  C CG1 . VAL D  1  481 ? -0.229  -2.468  -7.848  1.00 28.86  ?  481  VAL D CG1 1 
ATOM   9738  C CG2 . VAL D  1  481 ? -1.626  -2.875  -5.809  1.00 28.44  ?  481  VAL D CG2 1 
ATOM   9739  N N   . ALA D  1  482 ? -4.250  -4.809  -6.823  1.00 26.90  ?  482  ALA D N   1 
ATOM   9740  C CA  . ALA D  1  482 ? -5.055  -5.900  -6.283  1.00 26.09  ?  482  ALA D CA  1 
ATOM   9741  C C   . ALA D  1  482 ? -6.506  -5.702  -6.704  1.00 25.83  ?  482  ALA D C   1 
ATOM   9742  O O   . ALA D  1  482 ? -7.167  -4.761  -6.250  1.00 25.73  ?  482  ALA D O   1 
ATOM   9743  C CB  . ALA D  1  482 ? -4.935  -5.974  -4.762  1.00 25.57  ?  482  ALA D CB  1 
ATOM   9744  N N   . PHE D  1  483 ? -6.992  -6.577  -7.580  1.00 27.99  ?  483  PHE D N   1 
ATOM   9745  C CA  . PHE D  1  483 ? -8.396  -6.625  -7.978  1.00 27.39  ?  483  PHE D CA  1 
ATOM   9746  C C   . PHE D  1  483 ? -8.977  -7.935  -7.459  1.00 26.99  ?  483  PHE D C   1 
ATOM   9747  O O   . PHE D  1  483 ? -8.664  -9.006  -7.988  1.00 27.02  ?  483  PHE D O   1 
ATOM   9748  C CB  . PHE D  1  483 ? -8.536  -6.519  -9.495  1.00 27.25  ?  483  PHE D CB  1 
ATOM   9749  C CG  . PHE D  1  483 ? -9.943  -6.273  -9.961  1.00 27.09  ?  483  PHE D CG  1 
ATOM   9750  C CD1 . PHE D  1  483 ? -10.854 -5.619  -9.149  1.00 27.64  ?  483  PHE D CD1 1 
ATOM   9751  C CD2 . PHE D  1  483 ? -10.356 -6.706  -11.211 1.00 26.82  ?  483  PHE D CD2 1 
ATOM   9752  C CE1 . PHE D  1  483 ? -12.147 -5.392  -9.576  1.00 27.56  ?  483  PHE D CE1 1 
ATOM   9753  C CE2 . PHE D  1  483 ? -11.651 -6.484  -11.643 1.00 26.90  ?  483  PHE D CE2 1 
ATOM   9754  C CZ  . PHE D  1  483 ? -12.547 -5.826  -10.823 1.00 26.79  ?  483  PHE D CZ  1 
ATOM   9755  N N   . ILE D  1  484 ? -9.812  -7.857  -6.424  1.00 23.48  ?  484  ILE D N   1 
ATOM   9756  C CA  . ILE D  1  484 ? -10.341 -9.041  -5.747  1.00 23.82  ?  484  ILE D CA  1 
ATOM   9757  C C   . ILE D  1  484 ? -11.859 -8.932  -5.707  1.00 24.18  ?  484  ILE D C   1 
ATOM   9758  O O   . ILE D  1  484 ? -12.407 -8.050  -5.033  1.00 24.20  ?  484  ILE D O   1 
ATOM   9759  C CB  . ILE D  1  484 ? -9.766  -9.204  -4.333  1.00 24.22  ?  484  ILE D CB  1 
ATOM   9760  C CG1 . ILE D  1  484 ? -8.238  -9.148  -4.366  1.00 23.84  ?  484  ILE D CG1 1 
ATOM   9761  C CG2 . ILE D  1  484 ? -10.230 -10.509 -3.722  1.00 25.31  ?  484  ILE D CG2 1 
ATOM   9762  C CD1 . ILE D  1  484 ? -7.584  -9.225  -3.001  1.00 24.17  ?  484  ILE D CD1 1 
ATOM   9763  N N   . LEU D  1  485 ? -12.539 -9.818  -6.430  1.00 26.81  ?  485  LEU D N   1 
ATOM   9764  C CA  . LEU D  1  485 ? -13.986 -9.734  -6.584  1.00 27.04  ?  485  LEU D CA  1 
ATOM   9765  C C   . LEU D  1  485 ? -14.598 -11.128 -6.437  1.00 28.16  ?  485  LEU D C   1 
ATOM   9766  O O   . LEU D  1  485 ? -15.380 -11.574 -7.280  1.00 28.54  ?  485  LEU D O   1 
ATOM   9767  C CB  . LEU D  1  485 ? -14.345 -9.092  -7.928  1.00 26.38  ?  485  LEU D CB  1 
ATOM   9768  C CG  . LEU D  1  485 ? -15.701 -8.407  -8.189  1.00 26.47  ?  485  LEU D CG  1 
ATOM   9769  C CD1 . LEU D  1  485 ? -15.621 -7.522  -9.440  1.00 26.17  ?  485  LEU D CD1 1 
ATOM   9770  C CD2 . LEU D  1  485 ? -16.920 -9.305  -8.227  1.00 27.32  ?  485  LEU D CD2 1 
ATOM   9771  N N   . SER D  1  486 ? -14.175 -11.882 -5.427  1.00 28.80  ?  486  SER D N   1 
ATOM   9772  C CA  . SER D  1  486 ? -14.552 -13.288 -5.366  1.00 30.22  ?  486  SER D CA  1 
ATOM   9773  C C   . SER D  1  486 ? -15.905 -13.487 -4.679  1.00 30.91  ?  486  SER D C   1 
ATOM   9774  O O   . SER D  1  486 ? -16.421 -12.608 -3.985  1.00 30.69  ?  486  SER D O   1 
ATOM   9775  C CB  . SER D  1  486 ? -13.475 -14.104 -4.650  1.00 31.11  ?  486  SER D CB  1 
ATOM   9776  O OG  . SER D  1  486 ? -13.275 -13.635 -3.329  1.00 32.31  ?  486  SER D OG  1 
ATOM   9777  N N   . ASN D  1  487 ? -16.474 -14.673 -4.895  1.00 36.33  ?  487  ASN D N   1 
ATOM   9778  C CA  . ASN D  1  487 ? -17.779 -15.084 -4.370  1.00 37.28  ?  487  ASN D CA  1 
ATOM   9779  C C   . ASN D  1  487 ? -18.862 -14.034 -4.633  1.00 36.34  ?  487  ASN D C   1 
ATOM   9780  O O   . ASN D  1  487 ? -19.487 -13.491 -3.719  1.00 36.55  ?  487  ASN D O   1 
ATOM   9781  C CB  . ASN D  1  487 ? -17.701 -15.419 -2.880  1.00 38.97  ?  487  ASN D CB  1 
ATOM   9782  C CG  . ASN D  1  487 ? -18.923 -16.190 -2.400  1.00 40.64  ?  487  ASN D CG  1 
ATOM   9783  O OD1 . ASN D  1  487 ? -19.594 -16.854 -3.190  1.00 41.17  ?  487  ASN D OD1 1 
ATOM   9784  N ND2 . ASN D  1  487 ? -19.224 -16.098 -1.109  1.00 41.59  ?  487  ASN D ND2 1 
ATOM   9785  N N   . ASN D  1  488 ? -19.069 -13.751 -5.916  1.00 36.43  ?  488  ASN D N   1 
ATOM   9786  C CA  . ASN D  1  488 ? -20.163 -12.893 -6.347  1.00 35.58  ?  488  ASN D CA  1 
ATOM   9787  C C   . ASN D  1  488 ? -20.985 -13.602 -7.415  1.00 35.80  ?  488  ASN D C   1 
ATOM   9788  O O   . ASN D  1  488 ? -20.777 -14.791 -7.679  1.00 37.13  ?  488  ASN D O   1 
ATOM   9789  C CB  . ASN D  1  488 ? -19.631 -11.558 -6.870  1.00 34.26  ?  488  ASN D CB  1 
ATOM   9790  C CG  . ASN D  1  488 ? -19.429 -10.539 -5.766  1.00 34.31  ?  488  ASN D CG  1 
ATOM   9791  O OD1 . ASN D  1  488 ? -20.289 -9.692  -5.524  1.00 33.96  ?  488  ASN D OD1 1 
ATOM   9792  N ND2 . ASN D  1  488 ? -18.288 -10.614 -5.091  1.00 34.27  ?  488  ASN D ND2 1 
ATOM   9793  N N   . SER D  1  489 ? -21.926 -12.886 -8.027  1.00 38.10  ?  489  SER D N   1 
ATOM   9794  C CA  . SER D  1  489 ? -22.728 -13.407 -9.133  1.00 38.95  ?  489  SER D CA  1 
ATOM   9795  C C   . SER D  1  489 ? -22.273 -12.839 -10.470 1.00 38.28  ?  489  SER D C   1 
ATOM   9796  O O   . SER D  1  489 ? -23.091 -12.580 -11.359 1.00 39.73  ?  489  SER D O   1 
ATOM   9797  C CB  . SER D  1  489 ? -24.209 -13.121 -8.900  1.00 40.62  ?  489  SER D CB  1 
ATOM   9798  O OG  . SER D  1  489 ? -24.652 -13.684 -7.678  1.00 41.66  ?  489  SER D OG  1 
ATOM   9799  N N   . ILE D  1  490 ? -20.965 -12.633 -10.629 1.00 37.08  ?  490  ILE D N   1 
ATOM   9800  C CA  . ILE D  1  490 ? -20.438 -12.027 -11.844 1.00 36.69  ?  490  ILE D CA  1 
ATOM   9801  C C   . ILE D  1  490 ? -20.569 -13.008 -12.999 1.00 37.50  ?  490  ILE D C   1 
ATOM   9802  O O   . ILE D  1  490 ? -20.092 -14.148 -12.928 1.00 37.29  ?  490  ILE D O   1 
ATOM   9803  C CB  . ILE D  1  490 ? -18.978 -11.602 -11.646 1.00 35.92  ?  490  ILE D CB  1 
ATOM   9804  C CG1 . ILE D  1  490 ? -18.883 -10.635 -10.476 1.00 35.31  ?  490  ILE D CG1 1 
ATOM   9805  C CG2 . ILE D  1  490 ? -18.438 -10.956 -12.917 1.00 35.47  ?  490  ILE D CG2 1 
ATOM   9806  C CD1 . ILE D  1  490 ? -19.816 -9.457  -10.582 1.00 35.53  ?  490  ILE D CD1 1 
ATOM   9807  N N   . THR D  1  491 ? -21.215 -12.566 -14.066 1.00 35.40  ?  491  THR D N   1 
ATOM   9808  C CA  . THR D  1  491 ? -21.444 -13.352 -15.265 1.00 36.16  ?  491  THR D CA  1 
ATOM   9809  C C   . THR D  1  491 ? -20.613 -12.787 -16.414 1.00 35.76  ?  491  THR D C   1 
ATOM   9810  O O   . THR D  1  491 ? -19.822 -11.854 -16.244 1.00 34.90  ?  491  THR D O   1 
ATOM   9811  C CB  . THR D  1  491 ? -22.934 -13.369 -15.606 1.00 37.82  ?  491  THR D CB  1 
ATOM   9812  O OG1 . THR D  1  491 ? -23.353 -12.045 -15.960 1.00 38.27  ?  491  THR D OG1 1 
ATOM   9813  C CG2 . THR D  1  491 ? -23.742 -13.845 -14.406 1.00 38.39  ?  491  THR D CG2 1 
ATOM   9814  N N   . GLY D  1  492 ? -20.792 -13.375 -17.593 1.00 36.86  ?  492  GLY D N   1 
ATOM   9815  C CA  . GLY D  1  492 ? -20.107 -12.901 -18.777 1.00 37.06  ?  492  GLY D CA  1 
ATOM   9816  C C   . GLY D  1  492 ? -18.653 -13.336 -18.820 1.00 36.02  ?  492  GLY D C   1 
ATOM   9817  O O   . GLY D  1  492 ? -18.212 -14.229 -18.090 1.00 35.70  ?  492  GLY D O   1 
ATOM   9818  N N   . ALA D  1  493 ? -17.899 -12.688 -19.702 1.00 32.78  ?  493  ALA D N   1 
ATOM   9819  C CA  . ALA D  1  493 ? -16.496 -13.008 -19.916 1.00 32.06  ?  493  ALA D CA  1 
ATOM   9820  C C   . ALA D  1  493 ? -15.600 -11.926 -19.326 1.00 31.12  ?  493  ALA D C   1 
ATOM   9821  O O   . ALA D  1  493 ? -16.051 -10.839 -18.952 1.00 31.10  ?  493  ALA D O   1 
ATOM   9822  C CB  . ALA D  1  493 ? -16.204 -13.186 -21.410 1.00 32.92  ?  493  ALA D CB  1 
ATOM   9823  N N   . ILE D  1  494 ? -14.310 -12.240 -19.257 1.00 29.88  ?  494  ILE D N   1 
ATOM   9824  C CA  . ILE D  1  494 ? -13.296 -11.309 -18.768 1.00 29.12  ?  494  ILE D CA  1 
ATOM   9825  C C   . ILE D  1  494 ? -12.894 -10.391 -19.915 1.00 29.75  ?  494  ILE D C   1 
ATOM   9826  O O   . ILE D  1  494 ? -12.408 -10.875 -20.947 1.00 30.34  ?  494  ILE D O   1 
ATOM   9827  C CB  . ILE D  1  494 ? -12.076 -12.053 -18.201 1.00 28.47  ?  494  ILE D CB  1 
ATOM   9828  C CG1 . ILE D  1  494 ? -12.492 -12.963 -17.045 1.00 28.09  ?  494  ILE D CG1 1 
ATOM   9829  C CG2 . ILE D  1  494 ? -11.009 -11.063 -17.752 1.00 27.88  ?  494  ILE D CG2 1 
ATOM   9830  C CD1 . ILE D  1  494 ? -11.333 -13.645 -16.352 1.00 27.63  ?  494  ILE D CD1 1 
ATOM   9831  N N   . PRO D  1  495 ? -13.085 -9.081  -19.788 1.00 31.38  ?  495  PRO D N   1 
ATOM   9832  C CA  . PRO D  1  495 ? -12.712 -8.159  -20.869 1.00 32.18  ?  495  PRO D CA  1 
ATOM   9833  C C   . PRO D  1  495 ? -11.241 -8.297  -21.213 1.00 32.11  ?  495  PRO D C   1 
ATOM   9834  O O   . PRO D  1  495 ? -10.394 -8.417  -20.314 1.00 31.64  ?  495  PRO D O   1 
ATOM   9835  C CB  . PRO D  1  495 ? -13.017 -6.773  -20.280 1.00 32.12  ?  495  PRO D CB  1 
ATOM   9836  C CG  . PRO D  1  495 ? -13.950 -7.024  -19.146 1.00 31.59  ?  495  PRO D CG  1 
ATOM   9837  C CD  . PRO D  1  495 ? -13.608 -8.375  -18.607 1.00 30.88  ?  495  PRO D CD  1 
ATOM   9838  N N   . PRO D  1  496 ? -10.895 -8.298  -22.502 1.00 33.13  ?  496  PRO D N   1 
ATOM   9839  C CA  . PRO D  1  496 ? -9.475  -8.403  -22.875 1.00 33.27  ?  496  PRO D CA  1 
ATOM   9840  C C   . PRO D  1  496 ? -8.632  -7.256  -22.354 1.00 32.99  ?  496  PRO D C   1 
ATOM   9841  O O   . PRO D  1  496 ? -7.411  -7.410  -22.228 1.00 32.87  ?  496  PRO D O   1 
ATOM   9842  C CB  . PRO D  1  496 ? -9.515  -8.415  -24.411 1.00 34.75  ?  496  PRO D CB  1 
ATOM   9843  C CG  . PRO D  1  496 ? -10.913 -8.827  -24.757 1.00 35.17  ?  496  PRO D CG  1 
ATOM   9844  C CD  . PRO D  1  496 ? -11.773 -8.240  -23.681 1.00 34.42  ?  496  PRO D CD  1 
ATOM   9845  N N   . GLU D  1  497 ? -9.247  -6.114  -22.037 1.00 36.37  ?  497  GLU D N   1 
ATOM   9846  C CA  . GLU D  1  497 ? -8.504  -4.970  -21.524 1.00 36.63  ?  497  GLU D CA  1 
ATOM   9847  C C   . GLU D  1  497 ? -7.921  -5.223  -20.140 1.00 35.42  ?  497  GLU D C   1 
ATOM   9848  O O   . GLU D  1  497 ? -6.972  -4.534  -19.750 1.00 35.82  ?  497  GLU D O   1 
ATOM   9849  C CB  . GLU D  1  497 ? -9.411  -3.739  -21.490 1.00 36.87  ?  497  GLU D CB  1 
ATOM   9850  C CG  . GLU D  1  497 ? -9.711  -3.150  -22.859 1.00 38.48  ?  497  GLU D CG  1 
ATOM   9851  C CD  . GLU D  1  497 ? -10.918 -3.793  -23.518 1.00 38.91  ?  497  GLU D CD  1 
ATOM   9852  O OE1 . GLU D  1  497 ? -11.749 -4.384  -22.796 1.00 37.92  ?  497  GLU D OE1 1 
ATOM   9853  O OE2 . GLU D  1  497 ? -11.037 -3.707  -24.758 1.00 40.11  -1 497  GLU D OE2 1 
ATOM   9854  N N   . ILE D  1  498 ? -8.467  -6.186  -19.391 1.00 33.01  ?  498  ILE D N   1 
ATOM   9855  C CA  . ILE D  1  498 ? -7.964  -6.467  -18.047 1.00 31.94  ?  498  ILE D CA  1 
ATOM   9856  C C   . ILE D  1  498 ? -6.508  -6.907  -18.105 1.00 32.01  ?  498  ILE D C   1 
ATOM   9857  O O   . ILE D  1  498 ? -5.704  -6.569  -17.229 1.00 31.58  ?  498  ILE D O   1 
ATOM   9858  C CB  . ILE D  1  498 ? -8.847  -7.520  -17.352 1.00 31.33  ?  498  ILE D CB  1 
ATOM   9859  C CG1 . ILE D  1  498 ? -10.286 -7.016  -17.231 1.00 31.47  ?  498  ILE D CG1 1 
ATOM   9860  C CG2 . ILE D  1  498 ? -8.290  -7.865  -15.975 1.00 30.45  ?  498  ILE D CG2 1 
ATOM   9861  C CD1 . ILE D  1  498 ? -10.498 -6.026  -16.107 1.00 30.97  ?  498  ILE D CD1 1 
ATOM   9862  N N   . TRP D  1  499 ? -6.145  -7.674  -19.133 1.00 32.61  ?  499  TRP D N   1 
ATOM   9863  C CA  . TRP D  1  499 ? -4.764  -8.117  -19.268 1.00 33.35  ?  499  TRP D CA  1 
ATOM   9864  C C   . TRP D  1  499 ? -3.818  -6.973  -19.603 1.00 34.57  ?  499  TRP D C   1 
ATOM   9865  O O   . TRP D  1  499 ? -2.618  -7.080  -19.331 1.00 35.60  ?  499  TRP D O   1 
ATOM   9866  C CB  . TRP D  1  499 ? -4.683  -9.222  -20.319 1.00 33.80  ?  499  TRP D CB  1 
ATOM   9867  C CG  . TRP D  1  499 ? -5.829  -10.181 -20.212 1.00 32.83  ?  499  TRP D CG  1 
ATOM   9868  C CD1 . TRP D  1  499 ? -6.789  -10.421 -21.151 1.00 32.91  ?  499  TRP D CD1 1 
ATOM   9869  C CD2 . TRP D  1  499 ? -6.148  -11.013 -19.089 1.00 31.84  ?  499  TRP D CD2 1 
ATOM   9870  N NE1 . TRP D  1  499 ? -7.680  -11.358 -20.686 1.00 32.85  ?  499  TRP D NE1 1 
ATOM   9871  C CE2 . TRP D  1  499 ? -7.308  -11.737 -19.422 1.00 31.80  ?  499  TRP D CE2 1 
ATOM   9872  C CE3 . TRP D  1  499 ? -5.561  -11.219 -17.835 1.00 31.45  ?  499  TRP D CE3 1 
ATOM   9873  C CZ2 . TRP D  1  499 ? -7.894  -12.653 -18.550 1.00 30.97  ?  499  TRP D CZ2 1 
ATOM   9874  C CZ3 . TRP D  1  499 ? -6.144  -12.128 -16.970 1.00 30.70  ?  499  TRP D CZ3 1 
ATOM   9875  C CH2 . TRP D  1  499 ? -7.298  -12.833 -17.331 1.00 30.52  ?  499  TRP D CH2 1 
ATOM   9876  N N   . ASN D  1  500 ? -4.323  -5.883  -20.177 1.00 41.04  ?  500  ASN D N   1 
ATOM   9877  C CA  . ASN D  1  500 ? -3.511  -4.689  -20.374 1.00 42.22  ?  500  ASN D CA  1 
ATOM   9878  C C   . ASN D  1  500 ? -3.337  -3.876  -19.090 1.00 42.36  ?  500  ASN D C   1 
ATOM   9879  O O   . ASN D  1  500 ? -2.748  -2.791  -19.135 1.00 43.80  ?  500  ASN D O   1 
ATOM   9880  C CB  . ASN D  1  500 ? -4.106  -3.823  -21.491 1.00 42.48  ?  500  ASN D CB  1 
ATOM   9881  C CG  . ASN D  1  500 ? -3.472  -4.108  -22.847 1.00 43.73  ?  500  ASN D CG  1 
ATOM   9882  O OD1 . ASN D  1  500 ? -2.476  -4.826  -22.932 1.00 44.06  ?  500  ASN D OD1 1 
ATOM   9883  N ND2 . ASN D  1  500 ? -4.044  -3.548  -23.909 1.00 44.60  ?  500  ASN D ND2 1 
ATOM   9884  N N   . MET D  1  501 ? -3.836  -4.374  -17.956 1.00 35.34  ?  501  MET D N   1 
ATOM   9885  C CA  . MET D  1  501 ? -3.565  -3.778  -16.645 1.00 35.50  ?  501  MET D CA  1 
ATOM   9886  C C   . MET D  1  501 ? -2.266  -4.367  -16.092 1.00 36.33  ?  501  MET D C   1 
ATOM   9887  O O   . MET D  1  501 ? -2.249  -5.183  -15.168 1.00 35.38  ?  501  MET D O   1 
ATOM   9888  C CB  . MET D  1  501 ? -4.736  -4.007  -15.694 1.00 34.09  ?  501  MET D CB  1 
ATOM   9889  C CG  . MET D  1  501 ? -6.096  -3.613  -16.252 1.00 33.98  ?  501  MET D CG  1 
ATOM   9890  S SD  . MET D  1  501 ? -7.420  -3.612  -15.022 1.00 32.68  ?  501  MET D SD  1 
ATOM   9891  C CE  . MET D  1  501 ? -6.590  -4.298  -13.593 1.00 32.21  ?  501  MET D CE  1 
ATOM   9892  N N   . THR D  1  502 ? -1.156  -3.924  -16.691 1.00 34.61  ?  502  THR D N   1 
ATOM   9893  C CA  . THR D  1  502 ? 0.145   -4.545  -16.451 1.00 35.26  ?  502  THR D CA  1 
ATOM   9894  C C   . THR D  1  502 ? 0.587   -4.469  -14.994 1.00 34.62  ?  502  THR D C   1 
ATOM   9895  O O   . THR D  1  502 ? 1.381   -5.309  -14.557 1.00 34.07  ?  502  THR D O   1 
ATOM   9896  C CB  . THR D  1  502 ? 1.209   -3.895  -17.337 1.00 36.06  ?  502  THR D CB  1 
ATOM   9897  O OG1 . THR D  1  502 ? 1.409   -2.536  -16.929 1.00 35.77  ?  502  THR D OG1 1 
ATOM   9898  C CG2 . THR D  1  502 ? 0.776   -3.920  -18.795 1.00 36.25  ?  502  THR D CG2 1 
ATOM   9899  N N   . GLN D  1  503 ? 0.099   -3.492  -14.232 1.00 33.79  ?  503  GLN D N   1 
ATOM   9900  C CA  . GLN D  1  503 ? 0.548   -3.311  -12.857 1.00 33.14  ?  503  GLN D CA  1 
ATOM   9901  C C   . GLN D  1  503 ? -0.139  -4.247  -11.871 1.00 32.26  ?  503  GLN D C   1 
ATOM   9902  O O   . GLN D  1  503 ? 0.132   -4.157  -10.668 1.00 31.96  ?  503  GLN D O   1 
ATOM   9903  C CB  . GLN D  1  503 ? 0.336   -1.859  -12.421 1.00 33.33  ?  503  GLN D CB  1 
ATOM   9904  C CG  . GLN D  1  503 ? 1.435   -0.923  -12.884 1.00 33.86  ?  503  GLN D CG  1 
ATOM   9905  C CD  . GLN D  1  503 ? 2.728   -1.136  -12.123 1.00 34.08  ?  503  GLN D CD  1 
ATOM   9906  O OE1 . GLN D  1  503 ? 3.693   -1.687  -12.655 1.00 34.28  ?  503  GLN D OE1 1 
ATOM   9907  N NE2 . GLN D  1  503 ? 2.754   -0.702  -10.869 1.00 33.45  ?  503  GLN D NE2 1 
ATOM   9908  N N   . LEU D  1  504 ? -1.004  -5.140  -12.343 1.00 31.43  ?  504  LEU D N   1 
ATOM   9909  C CA  . LEU D  1  504 ? -1.683  -6.073  -11.455 1.00 30.34  ?  504  LEU D CA  1 
ATOM   9910  C C   . LEU D  1  504 ? -0.688  -7.056  -10.854 1.00 30.45  ?  504  LEU D C   1 
ATOM   9911  O O   . LEU D  1  504 ? 0.126   -7.648  -11.569 1.00 31.24  ?  504  LEU D O   1 
ATOM   9912  C CB  . LEU D  1  504 ? -2.768  -6.831  -12.218 1.00 29.72  ?  504  LEU D CB  1 
ATOM   9913  C CG  . LEU D  1  504 ? -4.224  -6.477  -11.921 1.00 28.94  ?  504  LEU D CG  1 
ATOM   9914  C CD1 . LEU D  1  504 ? -5.151  -7.489  -12.576 1.00 28.23  ?  504  LEU D CD1 1 
ATOM   9915  C CD2 . LEU D  1  504 ? -4.474  -6.404  -10.424 1.00 28.85  ?  504  LEU D CD2 1 
ATOM   9916  N N   . SER D  1  505 ? -0.751  -7.227  -9.534  1.00 29.33  ?  505  SER D N   1 
ATOM   9917  C CA  . SER D  1  505 ? 0.045   -8.244  -8.865  1.00 29.77  ?  505  SER D CA  1 
ATOM   9918  C C   . SER D  1  505 ? -0.789  -9.336  -8.216  1.00 29.43  ?  505  SER D C   1 
ATOM   9919  O O   . SER D  1  505 ? -0.275  -10.440 -8.011  1.00 30.02  ?  505  SER D O   1 
ATOM   9920  C CB  . SER D  1  505 ? 0.946   -7.605  -7.799  1.00 30.02  ?  505  SER D CB  1 
ATOM   9921  O OG  . SER D  1  505 ? 1.928   -8.521  -7.350  1.00 30.84  ?  505  SER D OG  1 
ATOM   9922  N N   . GLN D  1  506 ? -2.050  -9.061  -7.889  1.00 28.47  ?  506  GLN D N   1 
ATOM   9923  C CA  . GLN D  1  506 ? -2.966  -10.081 -7.391  1.00 27.58  ?  506  GLN D CA  1 
ATOM   9924  C C   . GLN D  1  506 ? -4.320  -9.887  -8.052  1.00 27.15  ?  506  GLN D C   1 
ATOM   9925  O O   . GLN D  1  506 ? -4.916  -8.811  -7.942  1.00 27.26  ?  506  GLN D O   1 
ATOM   9926  C CB  . GLN D  1  506 ? -3.098  -10.018 -5.868  1.00 27.12  ?  506  GLN D CB  1 
ATOM   9927  C CG  . GLN D  1  506 ? -4.279  -10.804 -5.323  1.00 26.59  ?  506  GLN D CG  1 
ATOM   9928  C CD  . GLN D  1  506 ? -4.123  -11.144 -3.855  1.00 26.87  ?  506  GLN D CD  1 
ATOM   9929  O OE1 . GLN D  1  506 ? -3.336  -10.523 -3.143  1.00 27.13  ?  506  GLN D OE1 1 
ATOM   9930  N NE2 . GLN D  1  506 ? -4.874  -12.138 -3.395  1.00 27.16  ?  506  GLN D NE2 1 
ATOM   9931  N N   . LEU D  1  507 ? -4.809  -10.923 -8.727  1.00 25.00  ?  507  LEU D N   1 
ATOM   9932  C CA  . LEU D  1  507 ? -6.130  -10.910 -9.339  1.00 24.81  ?  507  LEU D CA  1 
ATOM   9933  C C   . LEU D  1  507 ? -6.920  -12.103 -8.823  1.00 25.02  ?  507  LEU D C   1 
ATOM   9934  O O   . LEU D  1  507 ? -6.437  -13.239 -8.874  1.00 25.53  ?  507  LEU D O   1 
ATOM   9935  C CB  . LEU D  1  507 ? -6.030  -10.944 -10.866 1.00 25.13  ?  507  LEU D CB  1 
ATOM   9936  C CG  . LEU D  1  507 ? -7.350  -11.028 -11.633 1.00 25.19  ?  507  LEU D CG  1 
ATOM   9937  C CD1 . LEU D  1  507 ? -8.208  -9.812  -11.336 1.00 24.84  ?  507  LEU D CD1 1 
ATOM   9938  C CD2 . LEU D  1  507 ? -7.094  -11.153 -13.126 1.00 25.70  ?  507  LEU D CD2 1 
ATOM   9939  N N   . ASP D  1  508 ? -8.130  -11.845 -8.331  1.00 25.26  ?  508  ASP D N   1 
ATOM   9940  C CA  . ASP D  1  508 ? -8.959  -12.885 -7.722  1.00 25.64  ?  508  ASP D CA  1 
ATOM   9941  C C   . ASP D  1  508 ? -10.399 -12.670 -8.177  1.00 25.72  ?  508  ASP D C   1 
ATOM   9942  O O   . ASP D  1  508 ? -11.115 -11.835 -7.616  1.00 25.54  ?  508  ASP D O   1 
ATOM   9943  C CB  . ASP D  1  508 ? -8.844  -12.856 -6.202  1.00 25.67  ?  508  ASP D CB  1 
ATOM   9944  C CG  . ASP D  1  508 ? -9.609  -13.984 -5.532  1.00 26.33  ?  508  ASP D CG  1 
ATOM   9945  O OD1 . ASP D  1  508 ? -10.114 -14.875 -6.245  1.00 26.78  ?  508  ASP D OD1 1 
ATOM   9946  O OD2 . ASP D  1  508 ? -9.707  -13.975 -4.287  1.00 26.54  -1 508  ASP D OD2 1 
ATOM   9947  N N   . LEU D  1  509 ? -10.818 -13.430 -9.188  1.00 26.58  ?  509  LEU D N   1 
ATOM   9948  C CA  . LEU D  1  509 ? -12.199 -13.455 -9.650  1.00 27.13  ?  509  LEU D CA  1 
ATOM   9949  C C   . LEU D  1  509 ? -12.847 -14.807 -9.372  1.00 28.84  ?  509  LEU D C   1 
ATOM   9950  O O   . LEU D  1  509 ? -13.747 -15.238 -10.096 1.00 29.38  ?  509  LEU D O   1 
ATOM   9951  C CB  . LEU D  1  509 ? -12.275 -13.120 -11.139 1.00 26.28  ?  509  LEU D CB  1 
ATOM   9952  C CG  . LEU D  1  509 ? -11.579 -11.832 -11.585 1.00 25.40  ?  509  LEU D CG  1 
ATOM   9953  C CD1 . LEU D  1  509 ? -11.810 -11.584 -13.068 1.00 25.38  ?  509  LEU D CD1 1 
ATOM   9954  C CD2 . LEU D  1  509 ? -12.056 -10.648 -10.757 1.00 25.69  ?  509  LEU D CD2 1 
ATOM   9955  N N   . SER D  1  510 ? -12.390 -15.481 -8.320  1.00 28.60  ?  510  SER D N   1 
ATOM   9956  C CA  . SER D  1  510 ? -12.813 -16.841 -8.031  1.00 29.50  ?  510  SER D CA  1 
ATOM   9957  C C   . SER D  1  510 ? -14.261 -16.881 -7.549  1.00 30.10  ?  510  SER D C   1 
ATOM   9958  O O   . SER D  1  510 ? -14.836 -15.876 -7.124  1.00 29.82  ?  510  SER D O   1 
ATOM   9959  C CB  . SER D  1  510 ? -11.898 -17.476 -6.984  1.00 29.76  ?  510  SER D CB  1 
ATOM   9960  O OG  . SER D  1  510 ? -12.014 -16.820 -5.733  1.00 29.68  ?  510  SER D OG  1 
ATOM   9961  N N   . SER D  1  511 ? -14.850 -18.076 -7.635  1.00 31.83  ?  511  SER D N   1 
ATOM   9962  C CA  . SER D  1  511 ? -16.199 -18.347 -7.135  1.00 32.62  ?  511  SER D CA  1 
ATOM   9963  C C   . SER D  1  511 ? -17.236 -17.448 -7.807  1.00 31.66  ?  511  SER D C   1 
ATOM   9964  O O   . SER D  1  511 ? -18.054 -16.800 -7.151  1.00 32.12  ?  511  SER D O   1 
ATOM   9965  C CB  . SER D  1  511 ? -16.254 -18.210 -5.611  1.00 33.86  ?  511  SER D CB  1 
ATOM   9966  O OG  . SER D  1  511 ? -15.302 -19.059 -4.994  1.00 34.87  ?  511  SER D OG  1 
ATOM   9967  N N   . ASN D  1  512 ? -17.194 -17.416 -9.138  1.00 35.88  ?  512  ASN D N   1 
ATOM   9968  C CA  . ASN D  1  512 ? -18.174 -16.678 -9.925  1.00 35.04  ?  512  ASN D CA  1 
ATOM   9969  C C   . ASN D  1  512 ? -18.718 -17.553 -11.046 1.00 35.58  ?  512  ASN D C   1 
ATOM   9970  O O   . ASN D  1  512 ? -18.435 -18.754 -11.101 1.00 35.99  ?  512  ASN D O   1 
ATOM   9971  C CB  . ASN D  1  512 ? -17.561 -15.397 -10.496 1.00 33.93  ?  512  ASN D CB  1 
ATOM   9972  C CG  . ASN D  1  512 ? -17.424 -14.303 -9.457  1.00 33.57  ?  512  ASN D CG  1 
ATOM   9973  O OD1 . ASN D  1  512 ? -18.395 -13.624 -9.126  1.00 33.35  ?  512  ASN D OD1 1 
ATOM   9974  N ND2 . ASN D  1  512 ? -16.215 -14.126 -8.937  1.00 33.75  ?  512  ASN D ND2 1 
ATOM   9975  N N   . ARG D  1  513 ? -19.503 -16.962 -11.940 1.00 42.38  ?  513  ARG D N   1 
ATOM   9976  C CA  . ARG D  1  513 ? -20.013 -17.639 -13.125 1.00 42.43  ?  513  ARG D CA  1 
ATOM   9977  C C   . ARG D  1  513 ? -19.474 -16.979 -14.389 1.00 41.77  ?  513  ARG D C   1 
ATOM   9978  O O   . ARG D  1  513 ? -20.191 -16.795 -15.375 1.00 42.89  ?  513  ARG D O   1 
ATOM   9979  C CB  . ARG D  1  513 ? -21.539 -17.664 -13.128 1.00 43.67  ?  513  ARG D CB  1 
ATOM   9980  C CG  . ARG D  1  513 ? -22.141 -18.708 -12.196 1.00 44.71  ?  513  ARG D CG  1 
ATOM   9981  C CD  . ARG D  1  513 ? -22.510 -18.116 -10.844 1.00 45.60  ?  513  ARG D CD  1 
ATOM   9982  N NE  . ARG D  1  513 ? -23.814 -17.464 -10.867 1.00 47.56  ?  513  ARG D NE  1 
ATOM   9983  C CZ  . ARG D  1  513 ? -24.602 -17.329 -9.810  1.00 47.81  ?  513  ARG D CZ  1 
ATOM   9984  N NH1 . ARG D  1  513 ? -24.252 -17.794 -8.621  1.00 47.48  ?  513  ARG D NH1 1 
ATOM   9985  N NH2 . ARG D  1  513 ? -25.773 -16.712 -9.947  1.00 47.58  ?  513  ARG D NH2 1 
ATOM   9986  N N   . ILE D  1  514 ? -18.193 -16.617 -14.367 1.00 35.08  ?  514  ILE D N   1 
ATOM   9987  C CA  . ILE D  1  514 ? -17.551 -15.989 -15.516 1.00 34.72  ?  514  ILE D CA  1 
ATOM   9988  C C   . ILE D  1  514 ? -17.249 -17.055 -16.561 1.00 35.29  ?  514  ILE D C   1 
ATOM   9989  O O   . ILE D  1  514 ? -16.678 -18.107 -16.249 1.00 35.30  ?  514  ILE D O   1 
ATOM   9990  C CB  . ILE D  1  514 ? -16.273 -15.248 -15.092 1.00 33.89  ?  514  ILE D CB  1 
ATOM   9991  C CG1 . ILE D  1  514 ? -16.611 -14.072 -14.173 1.00 33.64  ?  514  ILE D CG1 1 
ATOM   9992  C CG2 . ILE D  1  514 ? -15.505 -14.766 -16.311 1.00 33.49  ?  514  ILE D CG2 1 
ATOM   9993  C CD1 . ILE D  1  514 ? -15.515 -13.739 -13.181 1.00 33.13  ?  514  ILE D CD1 1 
ATOM   9994  N N   . THR D  1  515 ? -17.625 -16.781 -17.805 1.00 34.01  ?  515  THR D N   1 
ATOM   9995  C CA  . THR D  1  515 ? -17.466 -17.702 -18.919 1.00 34.75  ?  515  THR D CA  1 
ATOM   9996  C C   . THR D  1  515 ? -16.405 -17.176 -19.881 1.00 34.45  ?  515  THR D C   1 
ATOM   9997  O O   . THR D  1  515 ? -15.765 -16.148 -19.642 1.00 33.66  ?  515  THR D O   1 
ATOM   9998  C CB  . THR D  1  515 ? -18.801 -17.915 -19.636 1.00 36.08  ?  515  THR D CB  1 
ATOM   9999  O OG1 . THR D  1  515 ? -19.288 -16.657 -20.122 1.00 36.29  ?  515  THR D OG1 1 
ATOM   10000 C CG2 . THR D  1  515 ? -19.825 -18.515 -18.683 1.00 36.63  ?  515  THR D CG2 1 
ATOM   10001 N N   . GLY D  1  516 ? -16.219 -17.898 -20.979 1.00 34.67  ?  516  GLY D N   1 
ATOM   10002 C CA  . GLY D  1  516 ? -15.199 -17.565 -21.953 1.00 34.85  ?  516  GLY D CA  1 
ATOM   10003 C C   . GLY D  1  516 ? -13.918 -18.338 -21.717 1.00 34.30  ?  516  GLY D C   1 
ATOM   10004 O O   . GLY D  1  516 ? -13.834 -19.237 -20.876 1.00 34.15  ?  516  GLY D O   1 
ATOM   10005 N N   . GLU D  1  517 ? -12.895 -17.971 -22.485 1.00 35.50  ?  517  GLU D N   1 
ATOM   10006 C CA  . GLU D  1  517 ? -11.599 -18.626 -22.399 1.00 35.67  ?  517  GLU D CA  1 
ATOM   10007 C C   . GLU D  1  517 ? -10.496 -17.591 -22.235 1.00 34.92  ?  517  GLU D C   1 
ATOM   10008 O O   . GLU D  1  517 ? -10.615 -16.449 -22.688 1.00 34.77  ?  517  GLU D O   1 
ATOM   10009 C CB  . GLU D  1  517 ? -11.325 -19.509 -23.629 1.00 37.00  ?  517  GLU D CB  1 
ATOM   10010 C CG  . GLU D  1  517 ? -11.822 -18.968 -24.954 1.00 37.46  ?  517  GLU D CG  1 
ATOM   10011 C CD  . GLU D  1  517 ? -11.499 -19.904 -26.106 1.00 39.12  ?  517  GLU D CD  1 
ATOM   10012 O OE1 . GLU D  1  517 ? -10.362 -19.852 -26.620 1.00 40.86  ?  517  GLU D OE1 1 
ATOM   10013 O OE2 . GLU D  1  517 ? -12.380 -20.703 -26.488 1.00 40.12  -1 517  GLU D OE2 1 
ATOM   10014 N N   . LEU D  1  518 ? -9.423  -18.006 -21.570 1.00 32.35  ?  518  LEU D N   1 
ATOM   10015 C CA  . LEU D  1  518 ? -8.306  -17.109 -21.300 1.00 31.88  ?  518  LEU D CA  1 
ATOM   10016 C C   . LEU D  1  518 ? -7.469  -16.929 -22.560 1.00 32.78  ?  518  LEU D C   1 
ATOM   10017 O O   . LEU D  1  518 ? -7.107  -17.919 -23.204 1.00 33.67  ?  518  LEU D O   1 
ATOM   10018 C CB  . LEU D  1  518 ? -7.441  -17.654 -20.169 1.00 31.50  ?  518  LEU D CB  1 
ATOM   10019 C CG  . LEU D  1  518 ? -8.147  -17.817 -18.823 1.00 30.75  ?  518  LEU D CG  1 
ATOM   10020 C CD1 . LEU D  1  518 ? -7.190  -18.354 -17.771 1.00 30.64  ?  518  LEU D CD1 1 
ATOM   10021 C CD2 . LEU D  1  518 ? -8.750  -16.492 -18.383 1.00 29.93  ?  518  LEU D CD2 1 
ATOM   10022 N N   . PRO D  1  519 ? -7.153  -15.699 -22.943 1.00 31.21  ?  519  PRO D N   1 
ATOM   10023 C CA  . PRO D  1  519 ? -6.366  -15.478 -24.157 1.00 32.30  ?  519  PRO D CA  1 
ATOM   10024 C C   . PRO D  1  519 ? -4.879  -15.678 -23.915 1.00 32.56  ?  519  PRO D C   1 
ATOM   10025 O O   . PRO D  1  519 ? -4.394  -15.681 -22.782 1.00 31.82  ?  519  PRO D O   1 
ATOM   10026 C CB  . PRO D  1  519 ? -6.670  -14.018 -24.503 1.00 32.28  ?  519  PRO D CB  1 
ATOM   10027 C CG  . PRO D  1  519 ? -6.893  -13.384 -23.171 1.00 31.01  ?  519  PRO D CG  1 
ATOM   10028 C CD  . PRO D  1  519 ? -7.567  -14.432 -22.315 1.00 30.39  ?  519  PRO D CD  1 
ATOM   10029 N N   . GLU D  1  520 ? -4.151  -15.845 -25.020 1.00 36.21  ?  520  GLU D N   1 
ATOM   10030 C CA  . GLU D  1  520 ? -2.696  -15.819 -24.965 1.00 36.81  ?  520  GLU D CA  1 
ATOM   10031 C C   . GLU D  1  520 ? -2.161  -14.439 -24.610 1.00 36.47  ?  520  GLU D C   1 
ATOM   10032 O O   . GLU D  1  520 ? -0.971  -14.313 -24.303 1.00 36.95  ?  520  GLU D O   1 
ATOM   10033 C CB  . GLU D  1  520 ? -2.109  -16.288 -26.298 1.00 38.48  ?  520  GLU D CB  1 
ATOM   10034 C CG  . GLU D  1  520 ? -2.550  -17.686 -26.705 1.00 39.40  ?  520  GLU D CG  1 
ATOM   10035 C CD  . GLU D  1  520 ? -1.856  -18.777 -25.912 1.00 39.53  ?  520  GLU D CD  1 
ATOM   10036 O OE1 . GLU D  1  520 ? -0.877  -18.467 -25.201 1.00 39.02  ?  520  GLU D OE1 1 
ATOM   10037 O OE2 . GLU D  1  520 ? -2.293  -19.944 -25.996 1.00 39.90  -1 520  GLU D OE2 1 
ATOM   10038 N N   . SER D  1  521 ? -3.011  -13.410 -24.656 1.00 34.63  ?  521  SER D N   1 
ATOM   10039 C CA  . SER D  1  521 ? -2.659  -12.076 -24.188 1.00 34.31  ?  521  SER D CA  1 
ATOM   10040 C C   . SER D  1  521 ? -2.543  -11.996 -22.672 1.00 33.27  ?  521  SER D C   1 
ATOM   10041 O O   . SER D  1  521 ? -2.106  -10.961 -22.158 1.00 33.40  ?  521  SER D O   1 
ATOM   10042 C CB  . SER D  1  521 ? -3.692  -11.060 -24.680 1.00 34.27  ?  521  SER D CB  1 
ATOM   10043 O OG  . SER D  1  521 ? -3.363  -9.750  -24.251 1.00 34.74  ?  521  SER D OG  1 
ATOM   10044 N N   . ILE D  1  522 ? -2.935  -13.051 -21.950 1.00 33.67  ?  522  ILE D N   1 
ATOM   10045 C CA  . ILE D  1  522 ? -2.782  -13.091 -20.499 1.00 32.80  ?  522  ILE D CA  1 
ATOM   10046 C C   . ILE D  1  522 ? -1.330  -12.897 -20.080 1.00 33.52  ?  522  ILE D C   1 
ATOM   10047 O O   . ILE D  1  522 ? -1.056  -12.601 -18.913 1.00 33.25  ?  522  ILE D O   1 
ATOM   10048 C CB  . ILE D  1  522 ? -3.348  -14.417 -19.944 1.00 32.23  ?  522  ILE D CB  1 
ATOM   10049 C CG1 . ILE D  1  522 ? -3.623  -14.303 -18.443 1.00 31.29  ?  522  ILE D CG1 1 
ATOM   10050 C CG2 . ILE D  1  522 ? -2.392  -15.566 -20.224 1.00 33.08  ?  522  ILE D CG2 1 
ATOM   10051 C CD1 . ILE D  1  522 ? -4.242  -15.545 -17.840 1.00 31.01  ?  522  ILE D CD1 1 
ATOM   10052 N N   . SER D  1  523 ? -0.385  -13.060 -21.010 1.00 34.24  ?  523  SER D N   1 
ATOM   10053 C CA  . SER D  1  523 ? 1.026   -12.841 -20.713 1.00 35.01  ?  523  SER D CA  1 
ATOM   10054 C C   . SER D  1  523 ? 1.322   -11.410 -20.278 1.00 35.40  ?  523  SER D C   1 
ATOM   10055 O O   . SER D  1  523 ? 2.352   -11.170 -19.637 1.00 36.19  ?  523  SER D O   1 
ATOM   10056 C CB  . SER D  1  523 ? 1.868   -13.193 -21.941 1.00 36.43  ?  523  SER D CB  1 
ATOM   10057 O OG  . SER D  1  523 ? 3.249   -13.207 -21.632 1.00 38.14  ?  523  SER D OG  1 
ATOM   10058 N N   . ASN D  1  524 ? 0.447   -10.458 -20.606 1.00 36.00  ?  524  ASN D N   1 
ATOM   10059 C CA  . ASN D  1  524 ? 0.696   -9.032  -20.420 1.00 36.86  ?  524  ASN D CA  1 
ATOM   10060 C C   . ASN D  1  524 ? 0.679   -8.582  -18.958 1.00 36.07  ?  524  ASN D C   1 
ATOM   10061 O O   . ASN D  1  524 ? 0.851   -7.384  -18.707 1.00 36.54  ?  524  ASN D O   1 
ATOM   10062 C CB  . ASN D  1  524 ? -0.333  -8.225  -21.215 1.00 36.12  ?  524  ASN D CB  1 
ATOM   10063 C CG  . ASN D  1  524 ? 0.079   -8.021  -22.660 1.00 36.98  ?  524  ASN D CG  1 
ATOM   10064 O OD1 . ASN D  1  524 ? 1.191   -8.370  -23.055 1.00 37.93  ?  524  ASN D OD1 1 
ATOM   10065 N ND2 . ASN D  1  524 ? -0.819  -7.450  -23.457 1.00 36.98  ?  524  ASN D ND2 1 
ATOM   10066 N N   . ILE D  1  525 ? 0.478   -9.482  -17.998 1.00 34.38  ?  525  ILE D N   1 
ATOM   10067 C CA  . ILE D  1  525 ? 0.352   -9.105  -16.592 1.00 33.38  ?  525  ILE D CA  1 
ATOM   10068 C C   . ILE D  1  525 ? 1.496   -9.714  -15.791 1.00 33.78  ?  525  ILE D C   1 
ATOM   10069 O O   . ILE D  1  525 ? 1.321   -10.071 -14.620 1.00 33.10  ?  525  ILE D O   1 
ATOM   10070 C CB  . ILE D  1  525 ? -1.011  -9.501  -15.994 1.00 32.23  ?  525  ILE D CB  1 
ATOM   10071 C CG1 . ILE D  1  525 ? -1.367  -10.946 -16.337 1.00 32.42  ?  525  ILE D CG1 1 
ATOM   10072 C CG2 . ILE D  1  525 ? -2.094  -8.546  -16.469 1.00 31.90  ?  525  ILE D CG2 1 
ATOM   10073 C CD1 . ILE D  1  525 ? -2.577  -11.470 -15.586 1.00 31.53  ?  525  ILE D CD1 1 
ATOM   10074 N N   . ASN D  1  526 ? 2.670   -9.841  -16.420 1.00 36.60  ?  526  ASN D N   1 
ATOM   10075 C CA  . ASN D  1  526 ? 3.779   -10.623 -15.875 1.00 36.73  ?  526  ASN D CA  1 
ATOM   10076 C C   . ASN D  1  526 ? 4.117   -10.280 -14.427 1.00 36.18  ?  526  ASN D C   1 
ATOM   10077 O O   . ASN D  1  526 ? 4.760   -11.088 -13.745 1.00 35.80  ?  526  ASN D O   1 
ATOM   10078 C CB  . ASN D  1  526 ? 5.024   -10.423 -16.746 1.00 37.71  ?  526  ASN D CB  1 
ATOM   10079 C CG  . ASN D  1  526 ? 5.405   -8.959  -16.895 1.00 37.80  ?  526  ASN D CG  1 
ATOM   10080 O OD1 . ASN D  1  526 ? 4.746   -8.074  -16.348 1.00 37.33  ?  526  ASN D OD1 1 
ATOM   10081 N ND2 . ASN D  1  526 ? 6.478   -8.700  -17.634 1.00 39.53  ?  526  ASN D ND2 1 
ATOM   10082 N N   . ARG D  1  527 ? 3.709   -9.109  -13.939 1.00 39.09  ?  527  ARG D N   1 
ATOM   10083 C CA  . ARG D  1  527 ? 3.874   -8.772  -12.528 1.00 38.30  ?  527  ARG D CA  1 
ATOM   10084 C C   . ARG D  1  527 ? 2.919   -9.538  -11.615 1.00 37.62  ?  527  ARG D C   1 
ATOM   10085 O O   . ARG D  1  527 ? 2.976   -9.343  -10.396 1.00 37.31  ?  527  ARG D O   1 
ATOM   10086 C CB  . ARG D  1  527 ? 3.678   -7.268  -12.326 1.00 38.35  ?  527  ARG D CB  1 
ATOM   10087 C CG  . ARG D  1  527 ? 4.823   -6.409  -12.840 1.00 39.00  ?  527  ARG D CG  1 
ATOM   10088 C CD  . ARG D  1  527 ? 4.761   -5.004  -12.256 1.00 38.97  ?  527  ARG D CD  1 
ATOM   10089 N NE  . ARG D  1  527 ? 6.022   -4.286  -12.405 1.00 39.82  ?  527  ARG D NE  1 
ATOM   10090 C CZ  . ARG D  1  527 ? 6.935   -4.165  -11.450 1.00 40.21  ?  527  ARG D CZ  1 
ATOM   10091 N NH1 . ARG D  1  527 ? 6.755   -4.695  -10.251 1.00 39.03  ?  527  ARG D NH1 1 
ATOM   10092 N NH2 . ARG D  1  527 ? 8.055   -3.495  -11.704 1.00 40.23  ?  527  ARG D NH2 1 
ATOM   10093 N N   . ILE D  1  528 ? 2.047   -10.387 -12.167 1.00 35.03  ?  528  ILE D N   1 
ATOM   10094 C CA  . ILE D  1  528 ? 1.094   -11.132 -11.351 1.00 34.19  ?  528  ILE D CA  1 
ATOM   10095 C C   . ILE D  1  528 ? 1.831   -12.106 -10.436 1.00 34.01  ?  528  ILE D C   1 
ATOM   10096 O O   . ILE D  1  528 ? 2.860   -12.687 -10.809 1.00 34.18  ?  528  ILE D O   1 
ATOM   10097 C CB  . ILE D  1  528 ? 0.088   -11.859 -12.262 1.00 33.75  ?  528  ILE D CB  1 
ATOM   10098 C CG1 . ILE D  1  528 ? -1.068  -12.455 -11.456 1.00 32.61  ?  528  ILE D CG1 1 
ATOM   10099 C CG2 . ILE D  1  528 ? 0.781   -12.925 -13.102 1.00 34.19  ?  528  ILE D CG2 1 
ATOM   10100 C CD1 . ILE D  1  528 ? -1.836  -11.443 -10.651 1.00 32.38  ?  528  ILE D CD1 1 
ATOM   10101 N N   . SER D  1  529 ? 1.320   -12.269 -9.213  1.00 33.37  ?  529  SER D N   1 
ATOM   10102 C CA  . SER D  1  529 ? 1.920   -13.208 -8.271  1.00 33.05  ?  529  SER D CA  1 
ATOM   10103 C C   . SER D  1  529 ? 0.884   -14.150 -7.666  1.00 32.24  ?  529  SER D C   1 
ATOM   10104 O O   . SER D  1  529 ? 1.221   -15.265 -7.254  1.00 32.55  ?  529  SER D O   1 
ATOM   10105 C CB  . SER D  1  529 ? 2.655   -12.452 -7.163  1.00 33.17  ?  529  SER D CB  1 
ATOM   10106 O OG  . SER D  1  529 ? 1.790   -11.537 -6.514  1.00 32.80  ?  529  SER D OG  1 
ATOM   10107 N N   . LYS D  1  530 ? -0.375  -13.717 -7.607  1.00 31.74  ?  530  LYS D N   1 
ATOM   10108 C CA  . LYS D  1  530 ? -1.487  -14.577 -7.212  1.00 31.08  ?  530  LYS D CA  1 
ATOM   10109 C C   . LYS D  1  530 ? -2.581  -14.457 -8.258  1.00 30.84  ?  530  LYS D C   1 
ATOM   10110 O O   . LYS D  1  530 ? -3.151  -13.377 -8.442  1.00 30.95  ?  530  LYS D O   1 
ATOM   10111 C CB  . LYS D  1  530 ? -2.029  -14.215 -5.825  1.00 30.83  ?  530  LYS D CB  1 
ATOM   10112 C CG  . LYS D  1  530 ? -1.161  -14.673 -4.667  1.00 31.51  ?  530  LYS D CG  1 
ATOM   10113 C CD  . LYS D  1  530 ? -1.968  -14.716 -3.376  1.00 31.94  ?  530  LYS D CD  1 
ATOM   10114 C CE  . LYS D  1  530 ? -1.078  -14.936 -2.165  1.00 32.02  ?  530  LYS D CE  1 
ATOM   10115 N NZ  . LYS D  1  530 ? -1.673  -14.357 -0.929  1.00 32.61  ?  530  LYS D NZ  1 
ATOM   10116 N N   . LEU D  1  531 ? -2.878  -15.564 -8.931  1.00 27.24  ?  531  LEU D N   1 
ATOM   10117 C CA  . LEU D  1  531 ? -3.865  -15.600 -10.004 1.00 26.94  ?  531  LEU D CA  1 
ATOM   10118 C C   . LEU D  1  531 ? -4.934  -16.613 -9.615  1.00 27.16  ?  531  LEU D C   1 
ATOM   10119 O O   . LEU D  1  531 ? -4.699  -17.824 -9.679  1.00 28.02  ?  531  LEU D O   1 
ATOM   10120 C CB  . LEU D  1  531 ? -3.196  -15.955 -11.333 1.00 27.57  ?  531  LEU D CB  1 
ATOM   10121 C CG  . LEU D  1  531 ? -3.866  -15.560 -12.650 1.00 27.36  ?  531  LEU D CG  1 
ATOM   10122 C CD1 . LEU D  1  531 ? -2.851  -15.587 -13.778 1.00 28.10  ?  531  LEU D CD1 1 
ATOM   10123 C CD2 . LEU D  1  531 ? -5.014  -16.488 -12.969 1.00 27.53  ?  531  LEU D CD2 1 
ATOM   10124 N N   . GLN D  1  532 ? -6.100  -16.120 -9.202  1.00 27.01  ?  532  GLN D N   1 
ATOM   10125 C CA  . GLN D  1  532 ? -7.196  -16.969 -8.739  1.00 27.36  ?  532  GLN D CA  1 
ATOM   10126 C C   . GLN D  1  532 ? -8.413  -16.755 -9.635  1.00 27.24  ?  532  GLN D C   1 
ATOM   10127 O O   . GLN D  1  532 ? -9.186  -15.813 -9.434  1.00 27.54  ?  532  GLN D O   1 
ATOM   10128 C CB  . GLN D  1  532 ? -7.518  -16.679 -7.276  1.00 27.88  ?  532  GLN D CB  1 
ATOM   10129 C CG  . GLN D  1  532 ? -6.327  -16.852 -6.341  1.00 28.08  ?  532  GLN D CG  1 
ATOM   10130 C CD  . GLN D  1  532 ? -6.539  -16.200 -4.989  1.00 28.94  ?  532  GLN D CD  1 
ATOM   10131 O OE1 . GLN D  1  532 ? -5.911  -15.192 -4.665  1.00 28.35  ?  532  GLN D OE1 1 
ATOM   10132 N NE2 . GLN D  1  532 ? -7.428  -16.777 -4.189  1.00 30.61  ?  532  GLN D NE2 1 
ATOM   10133 N N   . LEU D  1  533 ? -8.581  -17.637 -10.622 1.00 26.57  ?  533  LEU D N   1 
ATOM   10134 C CA  . LEU D  1  533 ? -9.765  -17.671 -11.471 1.00 26.68  ?  533  LEU D CA  1 
ATOM   10135 C C   . LEU D  1  533 ? -10.585 -18.936 -11.249 1.00 27.54  ?  533  LEU D C   1 
ATOM   10136 O O   . LEU D  1  533 ? -11.428 -19.284 -12.082 1.00 27.96  ?  533  LEU D O   1 
ATOM   10137 C CB  . LEU D  1  533 ? -9.370  -17.550 -12.943 1.00 26.82  ?  533  LEU D CB  1 
ATOM   10138 C CG  . LEU D  1  533 ? -8.502  -16.346 -13.305 1.00 26.26  ?  533  LEU D CG  1 
ATOM   10139 C CD1 . LEU D  1  533 ? -8.286  -16.277 -14.805 1.00 26.66  ?  533  LEU D CD1 1 
ATOM   10140 C CD2 . LEU D  1  533 ? -9.119  -15.056 -12.787 1.00 25.54  ?  533  LEU D CD2 1 
ATOM   10141 N N   . ASN D  1  534 ? -10.351 -19.627 -10.138 1.00 29.71  ?  534  ASN D N   1 
ATOM   10142 C CA  . ASN D  1  534 ? -10.989 -20.905 -9.874  1.00 30.78  ?  534  ASN D CA  1 
ATOM   10143 C C   . ASN D  1  534 ? -12.475 -20.730 -9.573  1.00 32.31  ?  534  ASN D C   1 
ATOM   10144 O O   . ASN D  1  534 ? -12.948 -19.644 -9.234  1.00 32.56  ?  534  ASN D O   1 
ATOM   10145 C CB  . ASN D  1  534 ? -10.299 -21.603 -8.704  1.00 31.41  ?  534  ASN D CB  1 
ATOM   10146 C CG  . ASN D  1  534 ? -10.281 -20.751 -7.452  1.00 31.69  ?  534  ASN D CG  1 
ATOM   10147 O OD1 . ASN D  1  534 ? -9.632  -19.706 -7.412  1.00 31.02  ?  534  ASN D OD1 1 
ATOM   10148 N ND2 . ASN D  1  534 ? -11.000 -21.186 -6.424  1.00 33.88  ?  534  ASN D ND2 1 
ATOM   10149 N N   . GLY D  1  535 ? -13.216 -21.827 -9.708  1.00 34.31  ?  535  GLY D N   1 
ATOM   10150 C CA  . GLY D  1  535 ? -14.638 -21.807 -9.430  1.00 35.70  ?  535  GLY D CA  1 
ATOM   10151 C C   . GLY D  1  535 ? -15.413 -20.952 -10.410 1.00 35.16  ?  535  GLY D C   1 
ATOM   10152 O O   . GLY D  1  535 ? -16.132 -20.033 -10.006 1.00 35.46  ?  535  GLY D O   1 
ATOM   10153 N N   . ASN D  1  536 ? -15.265 -21.233 -11.702 1.00 35.08  ?  536  ASN D N   1 
ATOM   10154 C CA  . ASN D  1  536 ? -15.913 -20.447 -12.743 1.00 34.28  ?  536  ASN D CA  1 
ATOM   10155 C C   . ASN D  1  536 ? -16.302 -21.383 -13.883 1.00 34.77  ?  536  ASN D C   1 
ATOM   10156 O O   . ASN D  1  536 ? -16.205 -22.609 -13.771 1.00 35.35  ?  536  ASN D O   1 
ATOM   10157 C CB  . ASN D  1  536 ? -14.990 -19.312 -13.204 1.00 33.13  ?  536  ASN D CB  1 
ATOM   10158 C CG  . ASN D  1  536 ? -15.222 -18.028 -12.436 1.00 33.45  ?  536  ASN D CG  1 
ATOM   10159 O OD1 . ASN D  1  536 ? -16.215 -17.336 -12.651 1.00 33.77  ?  536  ASN D OD1 1 
ATOM   10160 N ND2 . ASN D  1  536 ? -14.312 -17.711 -11.524 1.00 33.25  ?  536  ASN D ND2 1 
ATOM   10161 N N   . ARG D  1  537 ? -16.745 -20.794 -14.994 1.00 37.27  ?  537  ARG D N   1 
ATOM   10162 C CA  . ARG D  1  537 ? -17.093 -21.536 -16.199 1.00 38.02  ?  537  ARG D CA  1 
ATOM   10163 C C   . ARG D  1  537 ? -16.134 -21.230 -17.347 1.00 37.65  ?  537  ARG D C   1 
ATOM   10164 O O   . ARG D  1  537 ? -16.535 -21.226 -18.514 1.00 38.76  ?  537  ARG D O   1 
ATOM   10165 C CB  . ARG D  1  537 ? -18.533 -21.243 -16.618 1.00 39.08  ?  537  ARG D CB  1 
ATOM   10166 C CG  . ARG D  1  537 ? -19.522 -21.168 -15.468 1.00 39.94  ?  537  ARG D CG  1 
ATOM   10167 C CD  . ARG D  1  537 ? -20.811 -21.897 -15.813 1.00 41.47  ?  537  ARG D CD  1 
ATOM   10168 N NE  . ARG D  1  537 ? -21.581 -21.188 -16.829 1.00 42.24  ?  537  ARG D NE  1 
ATOM   10169 C CZ  . ARG D  1  537 ? -22.281 -21.779 -17.788 1.00 44.16  ?  537  ARG D CZ  1 
ATOM   10170 N NH1 . ARG D  1  537 ? -22.350 -23.097 -17.881 1.00 44.99  ?  537  ARG D NH1 1 
ATOM   10171 N NH2 . ARG D  1  537 ? -22.928 -21.029 -18.675 1.00 43.92  ?  537  ARG D NH2 1 
ATOM   10172 N N   . LEU D  1  538 ? -14.868 -20.965 -17.030 1.00 33.75  ?  538  LEU D N   1 
ATOM   10173 C CA  . LEU D  1  538 ? -13.878 -20.707 -18.066 1.00 33.59  ?  538  LEU D CA  1 
ATOM   10174 C C   . LEU D  1  538 ? -13.594 -21.978 -18.854 1.00 34.61  ?  538  LEU D C   1 
ATOM   10175 O O   . LEU D  1  538 ? -13.407 -23.054 -18.280 1.00 35.09  ?  538  LEU D O   1 
ATOM   10176 C CB  . LEU D  1  538 ? -12.588 -20.159 -17.456 1.00 32.67  ?  538  LEU D CB  1 
ATOM   10177 C CG  . LEU D  1  538 ? -12.744 -18.942 -16.544 1.00 31.70  ?  538  LEU D CG  1 
ATOM   10178 C CD1 . LEU D  1  538 ? -11.699 -18.958 -15.445 1.00 31.14  ?  538  LEU D CD1 1 
ATOM   10179 C CD2 . LEU D  1  538 ? -12.650 -17.660 -17.358 1.00 31.35  ?  538  LEU D CD2 1 
ATOM   10180 N N   . SER D  1  539 ? -13.545 -21.843 -20.177 1.00 33.83  ?  539  SER D N   1 
ATOM   10181 C CA  . SER D  1  539 ? -13.456 -22.982 -21.080 1.00 34.98  ?  539  SER D CA  1 
ATOM   10182 C C   . SER D  1  539 ? -12.268 -22.817 -22.020 1.00 35.10  ?  539  SER D C   1 
ATOM   10183 O O   . SER D  1  539 ? -11.430 -21.931 -21.826 1.00 34.32  ?  539  SER D O   1 
ATOM   10184 C CB  . SER D  1  539 ? -14.759 -23.147 -21.870 1.00 35.90  ?  539  SER D CB  1 
ATOM   10185 O OG  . SER D  1  539 ? -15.075 -21.968 -22.589 1.00 35.70  ?  539  SER D OG  1 
ATOM   10186 N N   . GLY D  1  540 ? -12.165 -23.692 -23.010 1.00 35.27  ?  540  GLY D N   1 
ATOM   10187 C CA  . GLY D  1  540 ? -11.052 -23.647 -23.937 1.00 35.69  ?  540  GLY D CA  1 
ATOM   10188 C C   . GLY D  1  540 ? -9.768  -24.143 -23.295 1.00 35.61  ?  540  GLY D C   1 
ATOM   10189 O O   . GLY D  1  540 ? -9.738  -24.616 -22.162 1.00 35.32  ?  540  GLY D O   1 
ATOM   10190 N N   . LYS D  1  541 ? -8.682  -24.033 -24.055 1.00 36.42  ?  541  LYS D N   1 
ATOM   10191 C CA  . LYS D  1  541 ? -7.389  -24.472 -23.556 1.00 36.64  ?  541  LYS D CA  1 
ATOM   10192 C C   . LYS D  1  541 ? -6.765  -23.408 -22.655 1.00 35.47  ?  541  LYS D C   1 
ATOM   10193 O O   . LYS D  1  541 ? -7.068  -22.214 -22.751 1.00 34.65  ?  541  LYS D O   1 
ATOM   10194 C CB  . LYS D  1  541 ? -6.444  -24.805 -24.713 1.00 37.88  ?  541  LYS D CB  1 
ATOM   10195 C CG  . LYS D  1  541 ? -5.883  -23.595 -25.443 1.00 37.71  ?  541  LYS D CG  1 
ATOM   10196 C CD  . LYS D  1  541 ? -4.866  -24.020 -26.491 1.00 39.18  ?  541  LYS D CD  1 
ATOM   10197 C CE  . LYS D  1  541 ? -4.638  -22.926 -27.519 1.00 39.44  ?  541  LYS D CE  1 
ATOM   10198 N NZ  . LYS D  1  541 ? -5.768  -22.814 -28.478 1.00 39.80  ?  541  LYS D NZ  1 
ATOM   10199 N N   . ILE D  1  542 ? -5.891  -23.861 -21.762 1.00 33.87  ?  542  ILE D N   1 
ATOM   10200 C CA  . ILE D  1  542 ? -5.109  -22.967 -20.912 1.00 33.01  ?  542  ILE D CA  1 
ATOM   10201 C C   . ILE D  1  542 ? -4.049  -22.306 -21.783 1.00 33.45  ?  542  ILE D C   1 
ATOM   10202 O O   . ILE D  1  542 ? -3.255  -23.007 -22.427 1.00 34.71  ?  542  ILE D O   1 
ATOM   10203 C CB  . ILE D  1  542 ? -4.479  -23.722 -19.731 1.00 33.29  ?  542  ILE D CB  1 
ATOM   10204 C CG1 . ILE D  1  542 ? -5.563  -24.201 -18.762 1.00 32.89  ?  542  ILE D CG1 1 
ATOM   10205 C CG2 . ILE D  1  542 ? -3.459  -22.845 -19.019 1.00 32.74  ?  542  ILE D CG2 1 
ATOM   10206 C CD1 . ILE D  1  542 ? -5.032  -24.627 -17.407 1.00 33.00  ?  542  ILE D CD1 1 
ATOM   10207 N N   . PRO D  1  543 ? -3.999  -20.976 -21.840 1.00 35.26  ?  543  PRO D N   1 
ATOM   10208 C CA  . PRO D  1  543 ? -3.074  -20.314 -22.768 1.00 36.04  ?  543  PRO D CA  1 
ATOM   10209 C C   . PRO D  1  543 ? -1.623  -20.598 -22.409 1.00 36.66  ?  543  PRO D C   1 
ATOM   10210 O O   . PRO D  1  543 ? -1.235  -20.572 -21.239 1.00 36.15  ?  543  PRO D O   1 
ATOM   10211 C CB  . PRO D  1  543 ? -3.413  -18.829 -22.606 1.00 34.87  ?  543  PRO D CB  1 
ATOM   10212 C CG  . PRO D  1  543 ? -4.000  -18.725 -21.239 1.00 33.65  ?  543  PRO D CG  1 
ATOM   10213 C CD  . PRO D  1  543 ? -4.743  -20.010 -21.013 1.00 33.90  ?  543  PRO D CD  1 
ATOM   10214 N N   . SER D  1  544 ? -0.819  -20.870 -23.438 1.00 38.27  ?  544  SER D N   1 
ATOM   10215 C CA  . SER D  1  544 ? 0.606   -21.094 -23.231 1.00 39.31  ?  544  SER D CA  1 
ATOM   10216 C C   . SER D  1  544 ? 1.331   -19.837 -22.771 1.00 38.84  ?  544  SER D C   1 
ATOM   10217 O O   . SER D  1  544 ? 2.479   -19.935 -22.329 1.00 39.79  ?  544  SER D O   1 
ATOM   10218 C CB  . SER D  1  544 ? 1.250   -21.628 -24.513 1.00 41.12  ?  544  SER D CB  1 
ATOM   10219 O OG  . SER D  1  544 ? 1.358   -20.616 -25.499 1.00 41.50  ?  544  SER D OG  1 
ATOM   10220 N N   . GLY D  1  545 ? 0.693   -18.670 -22.861 1.00 39.20  ?  545  GLY D N   1 
ATOM   10221 C CA  . GLY D  1  545 ? 1.285   -17.435 -22.380 1.00 38.74  ?  545  GLY D CA  1 
ATOM   10222 C C   . GLY D  1  545 ? 1.421   -17.345 -20.874 1.00 38.10  ?  545  GLY D C   1 
ATOM   10223 O O   . GLY D  1  545 ? 2.084   -16.422 -20.387 1.00 37.92  ?  545  GLY D O   1 
ATOM   10224 N N   . ILE D  1  546 ? 0.803   -18.265 -20.129 1.00 37.21  ?  546  ILE D N   1 
ATOM   10225 C CA  . ILE D  1  546 ? 0.993   -18.309 -18.684 1.00 36.58  ?  546  ILE D CA  1 
ATOM   10226 C C   . ILE D  1  546 ? 2.435   -18.653 -18.325 1.00 37.81  ?  546  ILE D C   1 
ATOM   10227 O O   . ILE D  1  546 ? 2.898   -18.314 -17.230 1.00 37.51  ?  546  ILE D O   1 
ATOM   10228 C CB  . ILE D  1  546 ? -0.007  -19.302 -18.057 1.00 36.11  ?  546  ILE D CB  1 
ATOM   10229 C CG1 . ILE D  1  546 ? -1.437  -18.908 -18.432 1.00 35.11  ?  546  ILE D CG1 1 
ATOM   10230 C CG2 . ILE D  1  546 ? 0.139   -19.353 -16.541 1.00 35.62  ?  546  ILE D CG2 1 
ATOM   10231 C CD1 . ILE D  1  546 ? -2.505  -19.574 -17.592 1.00 34.53  ?  546  ILE D CD1 1 
ATOM   10232 N N   . ARG D  1  547 ? 3.164   -19.304 -19.237 1.00 39.16  ?  547  ARG D N   1 
ATOM   10233 C CA  . ARG D  1  547 ? 4.575   -19.602 -19.005 1.00 40.66  ?  547  ARG D CA  1 
ATOM   10234 C C   . ARG D  1  547 ? 5.375   -18.344 -18.687 1.00 40.58  ?  547  ARG D C   1 
ATOM   10235 O O   . ARG D  1  547 ? 6.363   -18.409 -17.946 1.00 41.38  ?  547  ARG D O   1 
ATOM   10236 C CB  . ARG D  1  547 ? 5.169   -20.307 -20.227 1.00 42.45  ?  547  ARG D CB  1 
ATOM   10237 C CG  . ARG D  1  547 ? 5.388   -19.380 -21.412 1.00 42.84  ?  547  ARG D CG  1 
ATOM   10238 C CD  . ARG D  1  547 ? 5.993   -20.076 -22.612 1.00 44.78  ?  547  ARG D CD  1 
ATOM   10239 N NE  . ARG D  1  547 ? 6.735   -19.132 -23.438 1.00 46.89  ?  547  ARG D NE  1 
ATOM   10240 C CZ  . ARG D  1  547 ? 6.193   -18.393 -24.398 1.00 46.54  ?  547  ARG D CZ  1 
ATOM   10241 N NH1 . ARG D  1  547 ? 4.898   -18.444 -24.661 1.00 44.24  ?  547  ARG D NH1 1 
ATOM   10242 N NH2 . ARG D  1  547 ? 6.969   -17.576 -25.104 1.00 46.77  ?  547  ARG D NH2 1 
ATOM   10243 N N   . LEU D  1  548 ? 4.971   -17.198 -19.232 1.00 36.66  ?  548  LEU D N   1 
ATOM   10244 C CA  . LEU D  1  548 ? 5.709   -15.952 -19.077 1.00 36.77  ?  548  LEU D CA  1 
ATOM   10245 C C   . LEU D  1  548 ? 5.327   -15.180 -17.821 1.00 35.27  ?  548  LEU D C   1 
ATOM   10246 O O   . LEU D  1  548 ? 5.846   -14.080 -17.609 1.00 35.27  ?  548  LEU D O   1 
ATOM   10247 C CB  . LEU D  1  548 ? 5.507   -15.066 -20.310 1.00 36.98  ?  548  LEU D CB  1 
ATOM   10248 C CG  . LEU D  1  548 ? 5.976   -15.658 -21.642 1.00 38.70  ?  548  LEU D CG  1 
ATOM   10249 C CD1 . LEU D  1  548 ? 5.901   -14.625 -22.756 1.00 39.14  ?  548  LEU D CD1 1 
ATOM   10250 C CD2 . LEU D  1  548 ? 7.386   -16.209 -21.514 1.00 40.53  ?  548  LEU D CD2 1 
ATOM   10251 N N   . LEU D  1  549 ? 4.437   -15.720 -16.990 1.00 38.13  ?  549  LEU D N   1 
ATOM   10252 C CA  . LEU D  1  549 ? 4.110   -15.101 -15.706 1.00 37.04  ?  549  LEU D CA  1 
ATOM   10253 C C   . LEU D  1  549 ? 5.042   -15.672 -14.636 1.00 37.70  ?  549  LEU D C   1 
ATOM   10254 O O   . LEU D  1  549 ? 4.648   -16.434 -13.752 1.00 37.65  ?  549  LEU D O   1 
ATOM   10255 C CB  . LEU D  1  549 ? 2.643   -15.331 -15.360 1.00 36.14  ?  549  LEU D CB  1 
ATOM   10256 C CG  . LEU D  1  549 ? 1.623   -15.210 -16.495 1.00 35.79  ?  549  LEU D CG  1 
ATOM   10257 C CD1 . LEU D  1  549 ? 0.221   -15.519 -15.991 1.00 34.50  ?  549  LEU D CD1 1 
ATOM   10258 C CD2 . LEU D  1  549 ? 1.672   -13.830 -17.132 1.00 36.04  ?  549  LEU D CD2 1 
ATOM   10259 N N   . THR D  1  550 ? 6.313   -15.275 -14.734 1.00 37.17  ?  550  THR D N   1 
ATOM   10260 C CA  . THR D  1  550 ? 7.347   -15.899 -13.913 1.00 38.45  ?  550  THR D CA  1 
ATOM   10261 C C   . THR D  1  550 ? 7.226   -15.513 -12.444 1.00 37.63  ?  550  THR D C   1 
ATOM   10262 O O   . THR D  1  550 ? 7.644   -16.281 -11.570 1.00 38.42  ?  550  THR D O   1 
ATOM   10263 C CB  . THR D  1  550 ? 8.734   -15.535 -14.442 1.00 40.21  ?  550  THR D CB  1 
ATOM   10264 O OG1 . THR D  1  550 ? 8.989   -14.145 -14.203 1.00 39.74  ?  550  THR D OG1 1 
ATOM   10265 C CG2 . THR D  1  550 ? 8.823   -15.815 -15.935 1.00 41.11  ?  550  THR D CG2 1 
ATOM   10266 N N   . ASN D  1  551 ? 6.664   -14.343 -12.150 1.00 39.69  ?  551  ASN D N   1 
ATOM   10267 C CA  . ASN D  1  551 ? 6.480   -13.915 -10.769 1.00 39.19  ?  551  ASN D CA  1 
ATOM   10268 C C   . ASN D  1  551 ? 5.331   -14.632 -10.073 1.00 38.47  ?  551  ASN D C   1 
ATOM   10269 O O   . ASN D  1  551 ? 5.051   -14.331 -8.908  1.00 37.29  ?  551  ASN D O   1 
ATOM   10270 C CB  . ASN D  1  551 ? 6.255   -12.401 -10.714 1.00 38.00  ?  551  ASN D CB  1 
ATOM   10271 C CG  . ASN D  1  551 ? 7.554   -11.626 -10.611 1.00 39.43  ?  551  ASN D CG  1 
ATOM   10272 O OD1 . ASN D  1  551 ? 8.089   -11.153 -11.614 1.00 40.36  ?  551  ASN D OD1 1 
ATOM   10273 N ND2 . ASN D  1  551 ? 8.069   -11.493 -9.394  1.00 40.10  ?  551  ASN D ND2 1 
ATOM   10274 N N   . LEU D  1  552 ? 4.656   -15.552 -10.760 1.00 36.87  ?  552  LEU D N   1 
ATOM   10275 C CA  . LEU D  1  552 ? 3.540   -16.279 -10.169 1.00 35.85  ?  552  LEU D CA  1 
ATOM   10276 C C   . LEU D  1  552 ? 3.997   -17.090 -8.962  1.00 36.88  ?  552  LEU D C   1 
ATOM   10277 O O   . LEU D  1  552 ? 4.950   -17.872 -9.047  1.00 38.33  ?  552  LEU D O   1 
ATOM   10278 C CB  . LEU D  1  552 ? 2.913   -17.200 -11.216 1.00 36.00  ?  552  LEU D CB  1 
ATOM   10279 C CG  . LEU D  1  552 ? 1.528   -16.829 -11.748 1.00 34.79  ?  552  LEU D CG  1 
ATOM   10280 C CD1 . LEU D  1  552 ? 1.037   -17.884 -12.727 1.00 35.17  ?  552  LEU D CD1 1 
ATOM   10281 C CD2 . LEU D  1  552 ? 0.538   -16.649 -10.609 1.00 34.11  ?  552  LEU D CD2 1 
ATOM   10282 N N   . GLU D  1  553 ? 3.316   -16.896 -7.834  1.00 36.82  ?  553  GLU D N   1 
ATOM   10283 C CA  . GLU D  1  553 ? 3.521   -17.712 -6.643  1.00 37.39  ?  553  GLU D CA  1 
ATOM   10284 C C   . GLU D  1  553 ? 2.379   -18.674 -6.364  1.00 37.48  ?  553  GLU D C   1 
ATOM   10285 O O   . GLU D  1  553 ? 2.620   -19.769 -5.853  1.00 38.51  ?  553  GLU D O   1 
ATOM   10286 C CB  . GLU D  1  553 ? 3.715   -16.824 -5.407  1.00 37.02  ?  553  GLU D CB  1 
ATOM   10287 C CG  . GLU D  1  553 ? 4.889   -15.865 -5.482  1.00 37.42  ?  553  GLU D CG  1 
ATOM   10288 C CD  . GLU D  1  553 ? 4.855   -14.830 -4.373  1.00 36.79  ?  553  GLU D CD  1 
ATOM   10289 O OE1 . GLU D  1  553 ? 4.014   -14.964 -3.460  1.00 36.24  ?  553  GLU D OE1 1 
ATOM   10290 O OE2 . GLU D  1  553 ? 5.672   -13.887 -4.411  1.00 36.98  -1 553  GLU D OE2 1 
ATOM   10291 N N   . TYR D  1  554 ? 1.148   -18.290 -6.692  1.00 33.96  ?  554  TYR D N   1 
ATOM   10292 C CA  . TYR D  1  554 ? -0.044  -19.055 -6.337  1.00 33.61  ?  554  TYR D CA  1 
ATOM   10293 C C   . TYR D  1  554 ? -0.979  -19.032 -7.537  1.00 32.97  ?  554  TYR D C   1 
ATOM   10294 O O   . TYR D  1  554 ? -1.488  -17.970 -7.907  1.00 32.16  ?  554  TYR D O   1 
ATOM   10295 C CB  . TYR D  1  554 ? -0.711  -18.459 -5.094  1.00 32.93  ?  554  TYR D CB  1 
ATOM   10296 C CG  . TYR D  1  554 ? -1.928  -19.195 -4.579  1.00 33.09  ?  554  TYR D CG  1 
ATOM   10297 C CD1 . TYR D  1  554 ? -3.185  -18.970 -5.126  1.00 32.36  ?  554  TYR D CD1 1 
ATOM   10298 C CD2 . TYR D  1  554 ? -1.825  -20.093 -3.525  1.00 34.20  ?  554  TYR D CD2 1 
ATOM   10299 C CE1 . TYR D  1  554 ? -4.301  -19.631 -4.650  1.00 32.42  ?  554  TYR D CE1 1 
ATOM   10300 C CE2 . TYR D  1  554 ? -2.936  -20.759 -3.042  1.00 34.50  ?  554  TYR D CE2 1 
ATOM   10301 C CZ  . TYR D  1  554 ? -4.170  -20.524 -3.608  1.00 33.55  ?  554  TYR D CZ  1 
ATOM   10302 O OH  . TYR D  1  554 ? -5.279  -21.185 -3.131  1.00 34.79  ?  554  TYR D OH  1 
ATOM   10303 N N   . LEU D  1  555 ? -1.210  -20.197 -8.138  1.00 30.36  ?  555  LEU D N   1 
ATOM   10304 C CA  . LEU D  1  555 ? -2.044  -20.318 -9.328  1.00 29.91  ?  555  LEU D CA  1 
ATOM   10305 C C   . LEU D  1  555 ? -3.198  -21.263 -9.030  1.00 30.20  ?  555  LEU D C   1 
ATOM   10306 O O   . LEU D  1  555 ? -2.977  -22.409 -8.623  1.00 31.43  ?  555  LEU D O   1 
ATOM   10307 C CB  . LEU D  1  555 ? -1.231  -20.823 -10.521 1.00 30.81  ?  555  LEU D CB  1 
ATOM   10308 C CG  . LEU D  1  555 ? -1.969  -20.827 -11.860 1.00 30.45  ?  555  LEU D CG  1 
ATOM   10309 C CD1 . LEU D  1  555 ? -2.555  -19.456 -12.148 1.00 29.08  ?  555  LEU D CD1 1 
ATOM   10310 C CD2 . LEU D  1  555 ? -1.043  -21.265 -12.983 1.00 31.50  ?  555  LEU D CD2 1 
ATOM   10311 N N   . ASP D  1  556 ? -4.422  -20.790 -9.247  1.00 31.45  ?  556  ASP D N   1 
ATOM   10312 C CA  . ASP D  1  556 ? -5.626  -21.577 -8.991  1.00 31.79  ?  556  ASP D CA  1 
ATOM   10313 C C   . ASP D  1  556 ? -6.565  -21.403 -10.182 1.00 31.33  ?  556  ASP D C   1 
ATOM   10314 O O   . ASP D  1  556 ? -7.260  -20.388 -10.292 1.00 30.35  ?  556  ASP D O   1 
ATOM   10315 C CB  . ASP D  1  556 ? -6.289  -21.151 -7.684  1.00 31.40  ?  556  ASP D CB  1 
ATOM   10316 C CG  . ASP D  1  556 ? -7.221  -22.211 -7.130  1.00 32.34  ?  556  ASP D CG  1 
ATOM   10317 O OD1 . ASP D  1  556 ? -7.584  -23.141 -7.879  1.00 33.06  ?  556  ASP D OD1 1 
ATOM   10318 O OD2 . ASP D  1  556 ? -7.587  -22.116 -5.938  1.00 32.50  -1 556  ASP D OD2 1 
ATOM   10319 N N   . LEU D  1  557 ? -6.580  -22.400 -11.069 1.00 29.77  ?  557  LEU D N   1 
ATOM   10320 C CA  . LEU D  1  557 ? -7.462  -22.420 -12.231 1.00 29.65  ?  557  LEU D CA  1 
ATOM   10321 C C   . LEU D  1  557 ? -8.470  -23.560 -12.151 1.00 30.56  ?  557  LEU D C   1 
ATOM   10322 O O   . LEU D  1  557 ? -9.079  -23.922 -13.162 1.00 30.90  ?  557  LEU D O   1 
ATOM   10323 C CB  . LEU D  1  557 ? -6.646  -22.528 -13.521 1.00 30.01  ?  557  LEU D CB  1 
ATOM   10324 C CG  . LEU D  1  557 ? -5.612  -21.432 -13.779 1.00 29.40  ?  557  LEU D CG  1 
ATOM   10325 C CD1 . LEU D  1  557 ? -4.851  -21.708 -15.066 1.00 30.12  ?  557  LEU D CD1 1 
ATOM   10326 C CD2 . LEU D  1  557 ? -6.276  -20.066 -13.828 1.00 28.20  ?  557  LEU D CD2 1 
ATOM   10327 N N   . SER D  1  558 ? -8.661  -24.125 -10.964 1.00 34.28  ?  558  SER D N   1 
ATOM   10328 C CA  . SER D  1  558 ? -9.441  -25.339 -10.800 1.00 35.51  ?  558  SER D CA  1 
ATOM   10329 C C   . SER D  1  558 ? -10.934 -25.019 -10.744 1.00 35.23  ?  558  SER D C   1 
ATOM   10330 O O   . SER D  1  558 ? -11.349 -23.858 -10.745 1.00 34.12  ?  558  SER D O   1 
ATOM   10331 C CB  . SER D  1  558 ? -8.980  -26.083 -9.550  1.00 36.52  ?  558  SER D CB  1 
ATOM   10332 O OG  . SER D  1  558 ? -9.191  -25.304 -8.390  1.00 35.86  ?  558  SER D OG  1 
ATOM   10333 N N   . SER D  1  559 ? -11.751 -26.070 -10.690 1.00 37.68  ?  559  SER D N   1 
ATOM   10334 C CA  . SER D  1  559 ? -13.210 -25.953 -10.722 1.00 37.73  ?  559  SER D CA  1 
ATOM   10335 C C   . SER D  1  559 ? -13.661 -25.061 -11.879 1.00 36.81  ?  559  SER D C   1 
ATOM   10336 O O   . SER D  1  559 ? -14.263 -24.002 -11.698 1.00 36.08  ?  559  SER D O   1 
ATOM   10337 C CB  . SER D  1  559 ? -13.747 -25.443 -9.383  1.00 37.66  ?  559  SER D CB  1 
ATOM   10338 O OG  . SER D  1  559 ? -13.776 -26.482 -8.419  1.00 39.05  ?  559  SER D OG  1 
ATOM   10339 N N   . ASN D  1  560 ? -13.338 -25.513 -13.086 1.00 36.39  ?  560  ASN D N   1 
ATOM   10340 C CA  . ASN D  1  560 ? -13.555 -24.744 -14.302 1.00 35.67  ?  560  ASN D CA  1 
ATOM   10341 C C   . ASN D  1  560 ? -13.843 -25.727 -15.431 1.00 36.88  ?  560  ASN D C   1 
ATOM   10342 O O   . ASN D  1  560 ? -14.123 -26.905 -15.191 1.00 37.94  ?  560  ASN D O   1 
ATOM   10343 C CB  . ASN D  1  560 ? -12.344 -23.846 -14.590 1.00 34.54  ?  560  ASN D CB  1 
ATOM   10344 C CG  . ASN D  1  560 ? -12.585 -22.400 -14.212 1.00 33.50  ?  560  ASN D CG  1 
ATOM   10345 O OD1 . ASN D  1  560 ? -13.438 -21.732 -14.791 1.00 33.58  ?  560  ASN D OD1 1 
ATOM   10346 N ND2 . ASN D  1  560 ? -11.832 -21.909 -13.235 1.00 33.01  ?  560  ASN D ND2 1 
ATOM   10347 N N   . ARG D  1  561 ? -13.785 -25.240 -16.670 1.00 35.66  ?  561  ARG D N   1 
ATOM   10348 C CA  . ARG D  1  561 ? -14.118 -26.054 -17.834 1.00 36.76  ?  561  ARG D CA  1 
ATOM   10349 C C   . ARG D  1  561 ? -12.977 -26.081 -18.846 1.00 36.77  ?  561  ARG D C   1 
ATOM   10350 O O   . ARG D  1  561 ? -13.209 -26.286 -20.041 1.00 37.41  ?  561  ARG D O   1 
ATOM   10351 C CB  . ARG D  1  561 ? -15.403 -25.556 -18.495 1.00 36.95  ?  561  ARG D CB  1 
ATOM   10352 C CG  . ARG D  1  561 ? -16.597 -25.471 -17.558 1.00 37.16  ?  561  ARG D CG  1 
ATOM   10353 C CD  . ARG D  1  561 ? -17.894 -25.398 -18.344 1.00 38.01  ?  561  ARG D CD  1 
ATOM   10354 N NE  . ARG D  1  561 ? -17.959 -24.186 -19.152 1.00 37.88  ?  561  ARG D NE  1 
ATOM   10355 C CZ  . ARG D  1  561 ? -19.067 -23.712 -19.706 1.00 38.10  ?  561  ARG D CZ  1 
ATOM   10356 N NH1 . ARG D  1  561 ? -20.227 -24.333 -19.573 1.00 39.58  ?  561  ARG D NH1 1 
ATOM   10357 N NH2 . ARG D  1  561 ? -19.008 -22.589 -20.415 1.00 37.43  ?  561  ARG D NH2 1 
ATOM   10358 N N   . PHE D  1  562 ? -11.742 -25.862 -18.391 1.00 36.05  ?  562  PHE D N   1 
ATOM   10359 C CA  . PHE D  1  562 ? -10.590 -26.008 -19.273 1.00 36.37  ?  562  PHE D CA  1 
ATOM   10360 C C   . PHE D  1  562 ? -10.546 -27.430 -19.820 1.00 37.90  ?  562  PHE D C   1 
ATOM   10361 O O   . PHE D  1  562 ? -10.713 -28.399 -19.076 1.00 38.65  ?  562  PHE D O   1 
ATOM   10362 C CB  . PHE D  1  562 ? -9.298  -25.686 -18.521 1.00 35.85  ?  562  PHE D CB  1 
ATOM   10363 C CG  . PHE D  1  562 ? -9.204  -24.260 -18.055 1.00 34.46  ?  562  PHE D CG  1 
ATOM   10364 C CD1 . PHE D  1  562 ? -9.079  -23.221 -18.965 1.00 33.95  ?  562  PHE D CD1 1 
ATOM   10365 C CD2 . PHE D  1  562 ? -9.241  -23.958 -16.703 1.00 33.82  ?  562  PHE D CD2 1 
ATOM   10366 C CE1 . PHE D  1  562 ? -8.995  -21.907 -18.532 1.00 32.83  ?  562  PHE D CE1 1 
ATOM   10367 C CE2 . PHE D  1  562 ? -9.157  -22.650 -16.265 1.00 32.63  ?  562  PHE D CE2 1 
ATOM   10368 C CZ  . PHE D  1  562 ? -9.033  -21.623 -17.179 1.00 32.13  ?  562  PHE D CZ  1 
ATOM   10369 N N   . SER D  1  563 ? -10.306 -27.559 -21.127 1.00 38.92  ?  563  SER D N   1 
ATOM   10370 C CA  . SER D  1  563 ? -10.658 -28.790 -21.831 1.00 40.42  ?  563  SER D CA  1 
ATOM   10371 C C   . SER D  1  563 ? -9.534  -29.451 -22.620 1.00 41.62  ?  563  SER D C   1 
ATOM   10372 O O   . SER D  1  563 ? -9.628  -30.659 -22.872 1.00 43.22  ?  563  SER D O   1 
ATOM   10373 C CB  . SER D  1  563 ? -11.830 -28.532 -22.791 1.00 40.65  ?  563  SER D CB  1 
ATOM   10374 O OG  . SER D  1  563 ? -11.419 -27.761 -23.909 1.00 40.86  ?  563  SER D OG  1 
ATOM   10375 N N   . PHE D  1  564 ? -8.497  -28.731 -23.029 1.00 40.25  ?  564  PHE D N   1 
ATOM   10376 C CA  . PHE D  1  564 ? -7.460  -29.332 -23.853 1.00 41.49  ?  564  PHE D CA  1 
ATOM   10377 C C   . PHE D  1  564 ? -6.213  -29.622 -23.017 1.00 41.74  ?  564  PHE D C   1 
ATOM   10378 O O   . PHE D  1  564 ? -6.189  -29.434 -21.799 1.00 41.29  ?  564  PHE D O   1 
ATOM   10379 C CB  . PHE D  1  564 ? -7.163  -28.444 -25.062 1.00 41.38  ?  564  PHE D CB  1 
ATOM   10380 C CG  . PHE D  1  564 ? -8.170  -28.593 -26.168 1.00 41.98  ?  564  PHE D CG  1 
ATOM   10381 C CD1 . PHE D  1  564 ? -8.118  -29.676 -27.034 1.00 43.60  ?  564  PHE D CD1 1 
ATOM   10382 C CD2 . PHE D  1  564 ? -9.183  -27.664 -26.327 1.00 41.10  ?  564  PHE D CD2 1 
ATOM   10383 C CE1 . PHE D  1  564 ? -9.054  -29.818 -28.046 1.00 44.29  ?  564  PHE D CE1 1 
ATOM   10384 C CE2 . PHE D  1  564 ? -10.119 -27.800 -27.334 1.00 41.86  ?  564  PHE D CE2 1 
ATOM   10385 C CZ  . PHE D  1  564 ? -10.055 -28.878 -28.195 1.00 43.43  ?  564  PHE D CZ  1 
ATOM   10386 N N   . GLU D  1  565 ? -5.168  -30.103 -23.687 1.00 44.43  ?  565  GLU D N   1 
ATOM   10387 C CA  . GLU D  1  565 ? -3.993  -30.614 -22.996 1.00 45.22  ?  565  GLU D CA  1 
ATOM   10388 C C   . GLU D  1  565 ? -3.224  -29.497 -22.295 1.00 44.07  ?  565  GLU D C   1 
ATOM   10389 O O   . GLU D  1  565 ? -3.211  -28.344 -22.736 1.00 43.06  ?  565  GLU D O   1 
ATOM   10390 C CB  . GLU D  1  565 ? -3.075  -31.342 -23.981 1.00 47.06  ?  565  GLU D CB  1 
ATOM   10391 C CG  . GLU D  1  565 ? -3.095  -30.771 -25.393 1.00 47.17  ?  565  GLU D CG  1 
ATOM   10392 C CD  . GLU D  1  565 ? -4.059  -31.504 -26.309 1.00 47.99  ?  565  GLU D CD  1 
ATOM   10393 O OE1 . GLU D  1  565 ? -5.117  -31.956 -25.822 1.00 47.69  ?  565  GLU D OE1 1 
ATOM   10394 O OE2 . GLU D  1  565 ? -3.760  -31.627 -27.516 1.00 49.26  -1 565  GLU D OE2 1 
ATOM   10395 N N   . ILE D  1  566 ? -2.587  -29.860 -21.183 1.00 42.32  ?  566  ILE D N   1 
ATOM   10396 C CA  . ILE D  1  566 ? -1.805  -28.907 -20.385 1.00 41.43  ?  566  ILE D CA  1 
ATOM   10397 C C   . ILE D  1  566 ? -0.670  -28.352 -21.235 1.00 41.96  ?  566  ILE D C   1 
ATOM   10398 O O   . ILE D  1  566 ? 0.006   -29.127 -21.945 1.00 43.65  ?  566  ILE D O   1 
ATOM   10399 C CB  . ILE D  1  566 ? -1.260  -29.588 -19.116 1.00 42.18  ?  566  ILE D CB  1 
ATOM   10400 C CG1 . ILE D  1  566 ? -2.409  -30.058 -18.220 1.00 41.76  ?  566  ILE D CG1 1 
ATOM   10401 C CG2 . ILE D  1  566 ? -0.330  -28.652 -18.353 1.00 41.55  ?  566  ILE D CG2 1 
ATOM   10402 C CD1 . ILE D  1  566 ? -2.058  -30.150 -16.744 1.00 41.82  ?  566  ILE D CD1 1 
ATOM   10403 N N   . PRO D  1  567 ? -0.415  -27.046 -21.219 1.00 42.64  ?  567  PRO D N   1 
ATOM   10404 C CA  . PRO D  1  567 ? 0.672   -26.482 -22.032 1.00 43.37  ?  567  PRO D CA  1 
ATOM   10405 C C   . PRO D  1  567 ? 2.009   -27.099 -21.667 1.00 44.98  ?  567  PRO D C   1 
ATOM   10406 O O   . PRO D  1  567 ? 2.453   -27.008 -20.512 1.00 44.92  ?  567  PRO D O   1 
ATOM   10407 C CB  . PRO D  1  567 ? 0.637   -24.987 -21.681 1.00 41.75  ?  567  PRO D CB  1 
ATOM   10408 C CG  . PRO D  1  567 ? -0.757  -24.743 -21.222 1.00 40.22  ?  567  PRO D CG  1 
ATOM   10409 C CD  . PRO D  1  567 ? -1.180  -25.999 -20.519 1.00 40.74  ?  567  PRO D CD  1 
ATOM   10410 N N   . PRO D  1  568 ? 2.689   -27.729 -22.630 1.00 46.71  ?  568  PRO D N   1 
ATOM   10411 C CA  . PRO D  1  568 ? 3.988   -28.350 -22.331 1.00 48.78  ?  568  PRO D CA  1 
ATOM   10412 C C   . PRO D  1  568 ? 5.105   -27.348 -22.095 1.00 48.68  ?  568  PRO D C   1 
ATOM   10413 O O   . PRO D  1  568 ? 6.209   -27.760 -21.715 1.00 50.51  ?  568  PRO D O   1 
ATOM   10414 C CB  . PRO D  1  568 ? 4.268   -29.212 -23.573 1.00 50.96  ?  568  PRO D CB  1 
ATOM   10415 C CG  . PRO D  1  568 ? 3.220   -28.835 -24.602 1.00 49.61  ?  568  PRO D CG  1 
ATOM   10416 C CD  . PRO D  1  568 ? 2.404   -27.700 -24.072 1.00 47.22  ?  568  PRO D CD  1 
ATOM   10417 N N   . THR D  1  569 ? 4.860   -26.058 -22.312 1.00 48.53  ?  569  THR D N   1 
ATOM   10418 C CA  . THR D  1  569 ? 5.865   -25.022 -22.121 1.00 48.64  ?  569  THR D CA  1 
ATOM   10419 C C   . THR D  1  569 ? 5.818   -24.396 -20.730 1.00 47.25  ?  569  THR D C   1 
ATOM   10420 O O   . THR D  1  569 ? 6.539   -23.425 -20.478 1.00 47.21  ?  569  THR D O   1 
ATOM   10421 C CB  . THR D  1  569 ? 5.701   -23.932 -23.184 1.00 48.32  ?  569  THR D CB  1 
ATOM   10422 O OG1 . THR D  1  569 ? 4.470   -23.230 -22.965 1.00 46.19  ?  569  THR D OG1 1 
ATOM   10423 C CG2 . THR D  1  569 ? 5.684   -24.546 -24.577 1.00 49.60  ?  569  THR D CG2 1 
ATOM   10424 N N   . LEU D  1  570 ? 4.994   -24.929 -19.825 1.00 47.59  ?  570  LEU D N   1 
ATOM   10425 C CA  . LEU D  1  570 ? 4.868   -24.393 -18.469 1.00 46.72  ?  570  LEU D CA  1 
ATOM   10426 C C   . LEU D  1  570 ? 5.967   -25.003 -17.601 1.00 48.06  ?  570  LEU D C   1 
ATOM   10427 O O   . LEU D  1  570 ? 5.744   -25.913 -16.797 1.00 48.38  ?  570  LEU D O   1 
ATOM   10428 C CB  . LEU D  1  570 ? 3.482   -24.679 -17.904 1.00 45.19  ?  570  LEU D CB  1 
ATOM   10429 C CG  . LEU D  1  570 ? 2.447   -23.551 -17.938 1.00 42.89  ?  570  LEU D CG  1 
ATOM   10430 C CD1 . LEU D  1  570 ? 2.680   -22.572 -16.799 1.00 41.84  ?  570  LEU D CD1 1 
ATOM   10431 C CD2 . LEU D  1  570 ? 2.457   -22.837 -19.281 1.00 43.65  ?  570  LEU D CD2 1 
ATOM   10432 N N   . ASN D  1  571 ? 7.188   -24.485 -17.781 1.00 46.19  ?  571  ASN D N   1 
ATOM   10433 C CA  . ASN D  1  571 ? 8.337   -24.992 -17.038 1.00 48.01  ?  571  ASN D CA  1 
ATOM   10434 C C   . ASN D  1  571 ? 9.266   -23.889 -16.532 1.00 48.04  ?  571  ASN D C   1 
ATOM   10435 O O   . ASN D  1  571 ? 10.446  -24.161 -16.273 1.00 50.00  ?  571  ASN D O   1 
ATOM   10436 C CB  . ASN D  1  571 ? 9.125   -25.980 -17.910 1.00 50.47  ?  571  ASN D CB  1 
ATOM   10437 C CG  . ASN D  1  571 ? 9.544   -25.386 -19.246 1.00 50.97  ?  571  ASN D CG  1 
ATOM   10438 O OD1 . ASN D  1  571 ? 10.018  -24.252 -19.321 1.00 50.58  ?  571  ASN D OD1 1 
ATOM   10439 N ND2 . ASN D  1  571 ? 9.367   -26.157 -20.311 1.00 51.98  ?  571  ASN D ND2 1 
ATOM   10440 N N   . ASN D  1  572 ? 8.783   -22.657 -16.384 1.00 48.70  ?  572  ASN D N   1 
ATOM   10441 C CA  . ASN D  1  572 ? 9.649   -21.525 -16.055 1.00 48.62  ?  572  ASN D CA  1 
ATOM   10442 C C   . ASN D  1  572 ? 9.021   -20.643 -14.977 1.00 46.62  ?  572  ASN D C   1 
ATOM   10443 O O   . ASN D  1  572 ? 8.987   -19.416 -15.089 1.00 45.62  ?  572  ASN D O   1 
ATOM   10444 C CB  . ASN D  1  572 ? 9.986   -20.707 -17.300 1.00 49.23  ?  572  ASN D CB  1 
ATOM   10445 C CG  . ASN D  1  572 ? 11.182  -19.795 -17.087 1.00 49.92  ?  572  ASN D CG  1 
ATOM   10446 O OD1 . ASN D  1  572 ? 12.142  -20.162 -16.407 1.00 51.46  ?  572  ASN D OD1 1 
ATOM   10447 N ND2 . ASN D  1  572 ? 11.128  -18.601 -17.665 1.00 49.45  ?  572  ASN D ND2 1 
ATOM   10448 N N   . LEU D  1  573 ? 8.484   -21.260 -13.928 1.00 44.25  ?  573  LEU D N   1 
ATOM   10449 C CA  . LEU D  1  573 ? 7.901   -20.483 -12.839 1.00 42.57  ?  573  LEU D CA  1 
ATOM   10450 C C   . LEU D  1  573 ? 8.736   -20.638 -11.572 1.00 43.63  ?  573  LEU D C   1 
ATOM   10451 O O   . LEU D  1  573 ? 8.385   -21.429 -10.686 1.00 43.84  ?  573  LEU D O   1 
ATOM   10452 C CB  . LEU D  1  573 ? 6.454   -20.910 -12.590 1.00 41.09  ?  573  LEU D CB  1 
ATOM   10453 C CG  . LEU D  1  573 ? 5.570   -21.016 -13.835 1.00 40.38  ?  573  LEU D CG  1 
ATOM   10454 C CD1 . LEU D  1  573 ? 4.181   -21.513 -13.471 1.00 39.24  ?  573  LEU D CD1 1 
ATOM   10455 C CD2 . LEU D  1  573 ? 5.494   -19.678 -14.551 1.00 39.38  ?  573  LEU D CD2 1 
ATOM   10456 N N   . PRO D  1  574 ? 9.838   -19.890 -11.442 1.00 46.06  ?  574  PRO D N   1 
ATOM   10457 C CA  . PRO D  1  574 ? 10.790  -20.133 -10.345 1.00 47.59  ?  574  PRO D CA  1 
ATOM   10458 C C   . PRO D  1  574 ? 10.272  -19.781 -8.960  1.00 46.44  ?  574  PRO D C   1 
ATOM   10459 O O   . PRO D  1  574 ? 11.002  -19.986 -7.984  1.00 47.75  ?  574  PRO D O   1 
ATOM   10460 C CB  . PRO D  1  574 ? 11.985  -19.236 -10.715 1.00 48.66  ?  574  PRO D CB  1 
ATOM   10461 C CG  . PRO D  1  574 ? 11.783  -18.879 -12.161 1.00 48.30  ?  574  PRO D CG  1 
ATOM   10462 C CD  . PRO D  1  574 ? 10.301  -18.811 -12.327 1.00 46.12  ?  574  PRO D CD  1 
ATOM   10463 N N   . ARG D  1  575 ? 9.063   -19.238 -8.829  1.00 47.11  ?  575  ARG D N   1 
ATOM   10464 C CA  . ARG D  1  575 ? 8.504   -18.912 -7.525  1.00 46.10  ?  575  ARG D CA  1 
ATOM   10465 C C   . ARG D  1  575 ? 7.190   -19.623 -7.242  1.00 45.20  ?  575  ARG D C   1 
ATOM   10466 O O   . ARG D  1  575 ? 6.624   -19.435 -6.159  1.00 44.39  ?  575  ARG D O   1 
ATOM   10467 C CB  . ARG D  1  575 ? 8.300   -17.397 -7.392  1.00 44.54  ?  575  ARG D CB  1 
ATOM   10468 C CG  . ARG D  1  575 ? 9.581   -16.590 -7.495  1.00 45.61  ?  575  ARG D CG  1 
ATOM   10469 C CD  . ARG D  1  575 ? 9.286   -15.102 -7.590  1.00 44.85  ?  575  ARG D CD  1 
ATOM   10470 N NE  . ARG D  1  575 ? 10.467  -14.328 -7.956  1.00 46.26  ?  575  ARG D NE  1 
ATOM   10471 C CZ  . ARG D  1  575 ? 10.988  -14.282 -9.175  1.00 46.69  ?  575  ARG D CZ  1 
ATOM   10472 N NH1 . ARG D  1  575 ? 10.447  -14.943 -10.185 1.00 46.04  ?  575  ARG D NH1 1 
ATOM   10473 N NH2 . ARG D  1  575 ? 12.078  -13.550 -9.387  1.00 47.93  ?  575  ARG D NH2 1 
ATOM   10474 N N   . LEU D  1  576 ? 6.691   -20.427 -8.175  1.00 41.95  ?  576  LEU D N   1 
ATOM   10475 C CA  . LEU D  1  576 ? 5.394   -21.069 -8.007  1.00 41.09  ?  576  LEU D CA  1 
ATOM   10476 C C   . LEU D  1  576 ? 5.480   -22.190 -6.979  1.00 42.49  ?  576  LEU D C   1 
ATOM   10477 O O   . LEU D  1  576 ? 6.249   -23.141 -7.148  1.00 44.40  ?  576  LEU D O   1 
ATOM   10478 C CB  . LEU D  1  576 ? 4.903   -21.616 -9.342  1.00 41.01  ?  576  LEU D CB  1 
ATOM   10479 C CG  . LEU D  1  576 ? 3.460   -22.112 -9.315  1.00 40.03  ?  576  LEU D CG  1 
ATOM   10480 C CD1 . LEU D  1  576 ? 2.495   -20.953 -9.517  1.00 38.00  ?  576  LEU D CD1 1 
ATOM   10481 C CD2 . LEU D  1  576 ? 3.254   -23.187 -10.359 1.00 40.89  ?  576  LEU D CD2 1 
ATOM   10482 N N   . TYR D  1  577 ? 4.682   -22.081 -5.917  1.00 41.52  ?  577  TYR D N   1 
ATOM   10483 C CA  . TYR D  1  577 ? 4.578   -23.131 -4.917  1.00 42.88  ?  577  TYR D CA  1 
ATOM   10484 C C   . TYR D  1  577 ? 3.182   -23.732 -4.824  1.00 42.23  ?  577  TYR D C   1 
ATOM   10485 O O   . TYR D  1  577 ? 2.966   -24.629 -4.001  1.00 43.51  ?  577  TYR D O   1 
ATOM   10486 C CB  . TYR D  1  577 ? 5.013   -22.605 -3.540  1.00 43.19  ?  577  TYR D CB  1 
ATOM   10487 C CG  . TYR D  1  577 ? 4.100   -21.559 -2.931  1.00 41.28  ?  577  TYR D CG  1 
ATOM   10488 C CD1 . TYR D  1  577 ? 3.051   -21.921 -2.095  1.00 41.04  ?  577  TYR D CD1 1 
ATOM   10489 C CD2 . TYR D  1  577 ? 4.307   -20.206 -3.171  1.00 39.93  ?  577  TYR D CD2 1 
ATOM   10490 C CE1 . TYR D  1  577 ? 2.222   -20.968 -1.531  1.00 39.49  ?  577  TYR D CE1 1 
ATOM   10491 C CE2 . TYR D  1  577 ? 3.484   -19.246 -2.611  1.00 38.36  ?  577  TYR D CE2 1 
ATOM   10492 C CZ  . TYR D  1  577 ? 2.444   -19.633 -1.792  1.00 38.15  ?  577  TYR D CZ  1 
ATOM   10493 O OH  . TYR D  1  577 ? 1.622   -18.682 -1.231  1.00 36.76  ?  577  TYR D OH  1 
ATOM   10494 N N   . TYR D  1  578 ? 2.235   -23.276 -5.642  1.00 38.73  ?  578  TYR D N   1 
ATOM   10495 C CA  . TYR D  1  578 ? 0.872   -23.784 -5.612  1.00 38.21  ?  578  TYR D CA  1 
ATOM   10496 C C   . TYR D  1  578 ? 0.334   -23.895 -7.031  1.00 37.55  ?  578  TYR D C   1 
ATOM   10497 O O   . TYR D  1  578 ? 0.579   -23.019 -7.865  1.00 36.74  ?  578  TYR D O   1 
ATOM   10498 C CB  . TYR D  1  578 ? -0.034  -22.872 -4.772  1.00 36.76  ?  578  TYR D CB  1 
ATOM   10499 C CG  . TYR D  1  578 ? -1.452  -23.370 -4.610  1.00 36.47  ?  578  TYR D CG  1 
ATOM   10500 C CD1 . TYR D  1  578 ? -2.422  -23.093 -5.566  1.00 35.30  ?  578  TYR D CD1 1 
ATOM   10501 C CD2 . TYR D  1  578 ? -1.824  -24.110 -3.496  1.00 37.57  ?  578  TYR D CD2 1 
ATOM   10502 C CE1 . TYR D  1  578 ? -3.717  -23.543 -5.420  1.00 35.25  ?  578  TYR D CE1 1 
ATOM   10503 C CE2 . TYR D  1  578 ? -3.120  -24.565 -3.341  1.00 37.52  ?  578  TYR D CE2 1 
ATOM   10504 C CZ  . TYR D  1  578 ? -4.062  -24.278 -4.307  1.00 36.37  ?  578  TYR D CZ  1 
ATOM   10505 O OH  . TYR D  1  578 ? -5.354  -24.728 -4.158  1.00 37.09  ?  578  TYR D OH  1 
ATOM   10506 N N   . MET D  1  579 ? -0.409  -24.971 -7.294  1.00 37.60  ?  579  MET D N   1 
ATOM   10507 C CA  . MET D  1  579 ? -1.059  -25.152 -8.591  1.00 37.10  ?  579  MET D CA  1 
ATOM   10508 C C   . MET D  1  579 ? -2.258  -26.074 -8.402  1.00 37.51  ?  579  MET D C   1 
ATOM   10509 O O   . MET D  1  579 ? -2.085  -27.271 -8.153  1.00 39.17  ?  579  MET D O   1 
ATOM   10510 C CB  . MET D  1  579 ? -0.077  -25.714 -9.617  1.00 38.28  ?  579  MET D CB  1 
ATOM   10511 C CG  . MET D  1  579 ? -0.733  -26.337 -10.843 1.00 38.68  ?  579  MET D CG  1 
ATOM   10512 S SD  . MET D  1  579 ? 0.296   -26.301 -12.327 1.00 39.07  ?  579  MET D SD  1 
ATOM   10513 C CE  . MET D  1  579 ? 0.739   -24.570 -12.405 1.00 37.49  ?  579  MET D CE  1 
ATOM   10514 N N   . ASN D  1  580 ? -3.463  -25.514 -8.505  1.00 36.25  ?  580  ASN D N   1 
ATOM   10515 C CA  . ASN D  1  580 ? -4.713  -26.270 -8.449  1.00 36.63  ?  580  ASN D CA  1 
ATOM   10516 C C   . ASN D  1  580 ? -5.331  -26.223 -9.841  1.00 36.09  ?  580  ASN D C   1 
ATOM   10517 O O   . ASN D  1  580 ? -5.747  -25.155 -10.303 1.00 34.69  ?  580  ASN D O   1 
ATOM   10518 C CB  . ASN D  1  580 ? -5.663  -25.684 -7.401  1.00 35.87  ?  580  ASN D CB  1 
ATOM   10519 C CG  . ASN D  1  580 ? -6.574  -26.731 -6.758  1.00 37.10  ?  580  ASN D CG  1 
ATOM   10520 O OD1 . ASN D  1  580 ? -6.703  -27.852 -7.245  1.00 38.34  ?  580  ASN D OD1 1 
ATOM   10521 N ND2 . ASN D  1  580 ? -7.214  -26.347 -5.650  1.00 36.88  ?  580  ASN D ND2 1 
ATOM   10522 N N   . LEU D  1  581 ? -5.384  -27.376 -10.511 1.00 35.45  ?  581  LEU D N   1 
ATOM   10523 C CA  . LEU D  1  581 ? -5.993  -27.493 -11.833 1.00 35.25  ?  581  LEU D CA  1 
ATOM   10524 C C   . LEU D  1  581 ? -7.141  -28.496 -11.840 1.00 36.17  ?  581  LEU D C   1 
ATOM   10525 O O   . LEU D  1  581 ? -7.544  -28.966 -12.909 1.00 36.58  ?  581  LEU D O   1 
ATOM   10526 C CB  . LEU D  1  581 ? -4.953  -27.891 -12.884 1.00 36.04  ?  581  LEU D CB  1 
ATOM   10527 C CG  . LEU D  1  581 ? -3.680  -27.069 -13.096 1.00 35.62  ?  581  LEU D CG  1 
ATOM   10528 C CD1 . LEU D  1  581 ? -3.098  -27.378 -14.465 1.00 36.33  ?  581  LEU D CD1 1 
ATOM   10529 C CD2 . LEU D  1  581 ? -3.949  -25.581 -12.963 1.00 33.83  ?  581  LEU D CD2 1 
ATOM   10530 N N   . SER D  1  582 ? -7.686  -28.821 -10.672 1.00 39.02  ?  582  SER D N   1 
ATOM   10531 C CA  . SER D  1  582 ? -8.642  -29.908 -10.552 1.00 40.33  ?  582  SER D CA  1 
ATOM   10532 C C   . SER D  1  582 ? -10.032 -29.479 -11.023 1.00 39.58  ?  582  SER D C   1 
ATOM   10533 O O   . SER D  1  582 ? -10.312 -28.298 -11.237 1.00 38.06  ?  582  SER D O   1 
ATOM   10534 C CB  . SER D  1  582 ? -8.696  -30.410 -9.109  1.00 41.37  ?  582  SER D CB  1 
ATOM   10535 O OG  . SER D  1  582 ? -9.075  -29.377 -8.216  1.00 40.18  ?  582  SER D OG  1 
ATOM   10536 N N   . ARG D  1  583 ? -10.906 -30.472 -11.202 1.00 42.76  ?  583  ARG D N   1 
ATOM   10537 C CA  . ARG D  1  583 ? -12.307 -30.243 -11.556 1.00 42.54  ?  583  ARG D CA  1 
ATOM   10538 C C   . ARG D  1  583 ? -12.420 -29.479 -12.877 1.00 41.41  ?  583  ARG D C   1 
ATOM   10539 O O   . ARG D  1  583 ? -12.967 -28.376 -12.958 1.00 40.19  ?  583  ARG D O   1 
ATOM   10540 C CB  . ARG D  1  583 ? -13.043 -29.536 -10.414 1.00 41.98  ?  583  ARG D CB  1 
ATOM   10541 C CG  . ARG D  1  583 ? -12.937 -30.304 -9.109  1.00 43.32  ?  583  ARG D CG  1 
ATOM   10542 C CD  . ARG D  1  583 ? -13.237 -29.452 -7.894  1.00 42.64  ?  583  ARG D CD  1 
ATOM   10543 N NE  . ARG D  1  583 ? -12.313 -29.765 -6.811  1.00 43.29  ?  583  ARG D NE  1 
ATOM   10544 C CZ  . ARG D  1  583 ? -12.310 -30.905 -6.133  1.00 45.22  ?  583  ARG D CZ  1 
ATOM   10545 N NH1 . ARG D  1  583 ? -13.199 -31.855 -6.372  1.00 46.69  ?  583  ARG D NH1 1 
ATOM   10546 N NH2 . ARG D  1  583 ? -11.392 -31.095 -5.190  1.00 45.86  ?  583  ARG D NH2 1 
ATOM   10547 N N   . ASN D  1  584 ? -11.878 -30.101 -13.918 1.00 41.09  ?  584  ASN D N   1 
ATOM   10548 C CA  . ASN D  1  584 ? -11.782 -29.513 -15.245 1.00 40.36  ?  584  ASN D CA  1 
ATOM   10549 C C   . ASN D  1  584 ? -11.886 -30.646 -16.261 1.00 41.80  ?  584  ASN D C   1 
ATOM   10550 O O   . ASN D  1  584 ? -12.274 -31.768 -15.923 1.00 43.25  ?  584  ASN D O   1 
ATOM   10551 C CB  . ASN D  1  584 ? -10.477 -28.721 -15.384 1.00 39.36  ?  584  ASN D CB  1 
ATOM   10552 C CG  . ASN D  1  584 ? -10.615 -27.280 -14.943 1.00 37.73  ?  584  ASN D CG  1 
ATOM   10553 O OD1 . ASN D  1  584 ? -10.938 -26.406 -15.744 1.00 36.92  ?  584  ASN D OD1 1 
ATOM   10554 N ND2 . ASN D  1  584 ? -10.362 -27.024 -13.665 1.00 37.38  ?  584  ASN D ND2 1 
ATOM   10555 N N   . ASP D  1  585 ? -11.541 -30.357 -17.516 1.00 43.86  ?  585  ASP D N   1 
ATOM   10556 C CA  . ASP D  1  585 ? -11.664 -31.345 -18.582 1.00 45.23  ?  585  ASP D CA  1 
ATOM   10557 C C   . ASP D  1  585 ? -10.360 -31.524 -19.353 1.00 45.59  ?  585  ASP D C   1 
ATOM   10558 O O   . ASP D  1  585 ? -10.384 -31.907 -20.526 1.00 46.44  ?  585  ASP D O   1 
ATOM   10559 C CB  . ASP D  1  585 ? -12.793 -30.970 -19.543 1.00 45.12  ?  585  ASP D CB  1 
ATOM   10560 C CG  . ASP D  1  585 ? -14.130 -31.550 -19.127 1.00 47.26  ?  585  ASP D CG  1 
ATOM   10561 O OD1 . ASP D  1  585 ? -14.257 -32.791 -19.096 1.00 48.90  ?  585  ASP D OD1 1 
ATOM   10562 O OD2 . ASP D  1  585 ? -15.057 -30.763 -18.833 1.00 46.51  -1 585  ASP D OD2 1 
ATOM   10563 N N   . LEU D  1  586 ? -9.215  -31.267 -18.721 1.00 40.58  ?  586  LEU D N   1 
ATOM   10564 C CA  . LEU D  1  586 ? -7.952  -31.414 -19.434 1.00 41.13  ?  586  LEU D CA  1 
ATOM   10565 C C   . LEU D  1  586 ? -7.662  -32.887 -19.688 1.00 43.14  ?  586  LEU D C   1 
ATOM   10566 O O   . LEU D  1  586 ? -7.876  -33.742 -18.822 1.00 44.08  ?  586  LEU D O   1 
ATOM   10567 C CB  . LEU D  1  586 ? -6.791  -30.783 -18.662 1.00 40.47  ?  586  LEU D CB  1 
ATOM   10568 C CG  . LEU D  1  586 ? -6.936  -29.400 -18.023 1.00 38.64  ?  586  LEU D CG  1 
ATOM   10569 C CD1 . LEU D  1  586 ? -7.388  -29.528 -16.589 1.00 38.43  ?  586  LEU D CD1 1 
ATOM   10570 C CD2 . LEU D  1  586 ? -5.641  -28.617 -18.103 1.00 38.17  ?  586  LEU D CD2 1 
ATOM   10571 N N   . ASP D  1  587 ? -7.164  -33.177 -20.882 1.00 47.09  ?  587  ASP D N   1 
ATOM   10572 C CA  . ASP D  1  587 ? -6.953  -34.537 -21.353 1.00 49.13  ?  587  ASP D CA  1 
ATOM   10573 C C   . ASP D  1  587 ? -5.480  -34.756 -21.692 1.00 50.08  ?  587  ASP D C   1 
ATOM   10574 O O   . ASP D  1  587 ? -4.628  -33.888 -21.476 1.00 49.21  ?  587  ASP D O   1 
ATOM   10575 C CB  . ASP D  1  587 ? -7.857  -34.833 -22.557 1.00 49.80  ?  587  ASP D CB  1 
ATOM   10576 C CG  . ASP D  1  587 ? -7.553  -33.947 -23.752 1.00 49.41  ?  587  ASP D CG  1 
ATOM   10577 O OD1 . ASP D  1  587 ? -6.822  -32.945 -23.593 1.00 48.21  ?  587  ASP D OD1 1 
ATOM   10578 O OD2 . ASP D  1  587 ? -8.047  -34.253 -24.858 1.00 50.91  -1 587  ASP D OD2 1 
ATOM   10579 N N   . GLN D  1  588 ? -5.194  -35.954 -22.204 1.00 49.62  ?  588  GLN D N   1 
ATOM   10580 C CA  . GLN D  1  588 ? -3.858  -36.374 -22.613 1.00 51.07  ?  588  GLN D CA  1 
ATOM   10581 C C   . GLN D  1  588 ? -2.898  -36.440 -21.428 1.00 51.41  ?  588  GLN D C   1 
ATOM   10582 O O   . GLN D  1  588 ? -3.326  -36.415 -20.270 1.00 50.85  ?  588  GLN D O   1 
ATOM   10583 C CB  . GLN D  1  588 ? -3.317  -35.452 -23.708 1.00 50.44  ?  588  GLN D CB  1 
ATOM   10584 C CG  . GLN D  1  588 ? -4.262  -35.316 -24.892 1.00 50.21  ?  588  GLN D CG  1 
ATOM   10585 C CD  . GLN D  1  588 ? -3.544  -34.997 -26.186 1.00 50.84  ?  588  GLN D CD  1 
ATOM   10586 O OE1 . GLN D  1  588 ? -2.318  -34.885 -26.219 1.00 51.50  ?  588  GLN D OE1 1 
ATOM   10587 N NE2 . GLN D  1  588 ? -4.305  -34.858 -27.265 1.00 50.83  ?  588  GLN D NE2 1 
ATOM   10588 N N   . THR D  1  589 ? -1.602  -36.528 -21.709 1.00 47.03  ?  589  THR D N   1 
ATOM   10589 C CA  . THR D  1  589 ? -0.609  -36.860 -20.699 1.00 48.08  ?  589  THR D CA  1 
ATOM   10590 C C   . THR D  1  589 ? -0.092  -35.614 -19.991 1.00 46.42  ?  589  THR D C   1 
ATOM   10591 O O   . THR D  1  589 ? -0.033  -34.523 -20.566 1.00 44.97  ?  589  THR D O   1 
ATOM   10592 C CB  . THR D  1  589 ? 0.565   -37.614 -21.325 1.00 50.45  ?  589  THR D CB  1 
ATOM   10593 O OG1 . THR D  1  589 ? 1.658   -37.653 -20.400 1.00 51.36  ?  589  THR D OG1 1 
ATOM   10594 C CG2 . THR D  1  589 ? 1.017   -36.925 -22.602 1.00 50.13  ?  589  THR D CG2 1 
ATOM   10595 N N   . ILE D  1  590 ? 0.274   -35.791 -18.726 1.00 46.62  ?  590  ILE D N   1 
ATOM   10596 C CA  . ILE D  1  590 ? 0.897   -34.706 -17.959 1.00 45.39  ?  590  ILE D CA  1 
ATOM   10597 C C   . ILE D  1  590 ? 2.228   -34.338 -18.605 1.00 46.20  ?  590  ILE D C   1 
ATOM   10598 O O   . ILE D  1  590 ? 3.074   -35.226 -18.831 1.00 48.48  ?  590  ILE D O   1 
ATOM   10599 C CB  . ILE D  1  590 ? 1.093   -35.126 -16.492 1.00 46.11  ?  590  ILE D CB  1 
ATOM   10600 C CG1 . ILE D  1  590 ? -0.262  -35.343 -15.818 1.00 45.28  ?  590  ILE D CG1 1 
ATOM   10601 C CG2 . ILE D  1  590 ? 1.915   -34.088 -15.740 1.00 45.24  ?  590  ILE D CG2 1 
ATOM   10602 C CD1 . ILE D  1  590 ? -0.650  -36.790 -15.681 1.00 47.36  ?  590  ILE D CD1 1 
ATOM   10603 N N   . PRO D  1  591 ? 2.467   -33.068 -18.924 1.00 49.40  ?  591  PRO D N   1 
ATOM   10604 C CA  . PRO D  1  591 ? 3.702   -32.705 -19.625 1.00 50.37  ?  591  PRO D CA  1 
ATOM   10605 C C   . PRO D  1  591 ? 4.934   -32.868 -18.748 1.00 51.81  ?  591  PRO D C   1 
ATOM   10606 O O   . PRO D  1  591 ? 4.898   -32.668 -17.531 1.00 51.25  ?  591  PRO D O   1 
ATOM   10607 C CB  . PRO D  1  591 ? 3.476   -31.237 -19.998 1.00 48.24  ?  591  PRO D CB  1 
ATOM   10608 C CG  . PRO D  1  591 ? 2.536   -30.737 -18.959 1.00 46.31  ?  591  PRO D CG  1 
ATOM   10609 C CD  . PRO D  1  591 ? 1.628   -31.893 -18.633 1.00 46.88  ?  591  PRO D CD  1 
ATOM   10610 N N   . GLU D  1  592 ? 6.041   -33.232 -19.399 1.00 62.40  ?  592  GLU D N   1 
ATOM   10611 C CA  . GLU D  1  592 ? 7.313   -33.397 -18.706 1.00 63.95  ?  592  GLU D CA  1 
ATOM   10612 C C   . GLU D  1  592 ? 7.832   -32.081 -18.138 1.00 62.07  ?  592  GLU D C   1 
ATOM   10613 O O   . GLU D  1  592 ? 8.607   -32.093 -17.175 1.00 63.02  ?  592  GLU D O   1 
ATOM   10614 C CB  . GLU D  1  592 ? 8.335   -34.015 -19.667 1.00 66.09  ?  592  GLU D CB  1 
ATOM   10615 C CG  . GLU D  1  592 ? 9.761   -34.099 -19.149 1.00 68.17  ?  592  GLU D CG  1 
ATOM   10616 C CD  . GLU D  1  592 ? 10.088  -35.459 -18.568 1.00 71.01  ?  592  GLU D CD  1 
ATOM   10617 O OE1 . GLU D  1  592 ? 9.149   -36.248 -18.329 1.00 70.73  ?  592  GLU D OE1 1 
ATOM   10618 O OE2 . GLU D  1  592 ? 11.286  -35.743 -18.359 1.00 73.56  -1 592  GLU D OE2 1 
ATOM   10619 N N   . GLY D  1  593 ? 7.401   -30.945 -18.693 1.00 55.80  ?  593  GLY D N   1 
ATOM   10620 C CA  . GLY D  1  593 ? 7.896   -29.658 -18.238 1.00 54.67  ?  593  GLY D CA  1 
ATOM   10621 C C   . GLY D  1  593 ? 7.443   -29.274 -16.846 1.00 53.22  ?  593  GLY D C   1 
ATOM   10622 O O   . GLY D  1  593 ? 8.067   -28.409 -16.221 1.00 52.85  ?  593  GLY D O   1 
ATOM   10623 N N   . LEU D  1  594 ? 6.376   -29.898 -16.341 1.00 53.53  ?  594  LEU D N   1 
ATOM   10624 C CA  . LEU D  1  594 ? 5.945   -29.621 -14.976 1.00 52.44  ?  594  LEU D CA  1 
ATOM   10625 C C   . LEU D  1  594 ? 6.984   -30.071 -13.957 1.00 54.53  ?  594  LEU D C   1 
ATOM   10626 O O   . LEU D  1  594 ? 7.085   -29.482 -12.875 1.00 53.63  ?  594  LEU D O   1 
ATOM   10627 C CB  . LEU D  1  594 ? 4.600   -30.292 -14.699 1.00 51.74  ?  594  LEU D CB  1 
ATOM   10628 C CG  . LEU D  1  594 ? 3.410   -29.342 -14.543 1.00 49.15  ?  594  LEU D CG  1 
ATOM   10629 C CD1 . LEU D  1  594 ? 3.285   -28.428 -15.753 1.00 48.08  ?  594  LEU D CD1 1 
ATOM   10630 C CD2 . LEU D  1  594 ? 2.123   -30.119 -14.316 1.00 48.90  ?  594  LEU D CD2 1 
ATOM   10631 N N   . THR D  1  595 ? 7.768   -31.101 -14.286 1.00 57.48  ?  595  THR D N   1 
ATOM   10632 C CA  . THR D  1  595 ? 8.815   -31.579 -13.392 1.00 59.47  ?  595  THR D CA  1 
ATOM   10633 C C   . THR D  1  595 ? 9.945   -30.573 -13.217 1.00 59.67  ?  595  THR D C   1 
ATOM   10634 O O   . THR D  1  595 ? 10.804  -30.778 -12.353 1.00 61.55  ?  595  THR D O   1 
ATOM   10635 C CB  . THR D  1  595 ? 9.384   -32.905 -13.900 1.00 62.52  ?  595  THR D CB  1 
ATOM   10636 O OG1 . THR D  1  595 ? 10.309  -32.654 -14.966 1.00 63.95  ?  595  THR D OG1 1 
ATOM   10637 C CG2 . THR D  1  595 ? 8.267   -33.805 -14.405 1.00 62.34  ?  595  THR D CG2 1 
ATOM   10638 N N   . LYS D  1  596 ? 9.985   -29.519 -14.026 1.00 55.99  ?  596  LYS D N   1 
ATOM   10639 C CA  . LYS D  1  596 ? 10.978  -28.464 -13.887 1.00 56.10  ?  596  LYS D CA  1 
ATOM   10640 C C   . LYS D  1  596 ? 10.531  -27.342 -12.955 1.00 53.86  ?  596  LYS D C   1 
ATOM   10641 O O   . LYS D  1  596 ? 11.295  -26.396 -12.738 1.00 53.95  ?  596  LYS D O   1 
ATOM   10642 C CB  . LYS D  1  596 ? 11.330  -27.902 -15.268 1.00 56.10  ?  596  LYS D CB  1 
ATOM   10643 C CG  . LYS D  1  596 ? 11.840  -28.969 -16.229 1.00 58.50  ?  596  LYS D CG  1 
ATOM   10644 C CD  . LYS D  1  596 ? 11.717  -28.551 -17.684 1.00 58.10  ?  596  LYS D CD  1 
ATOM   10645 C CE  . LYS D  1  596 ? 11.870  -29.753 -18.608 1.00 60.18  ?  596  LYS D CE  1 
ATOM   10646 N NZ  . LYS D  1  596 ? 11.458  -29.448 -20.006 1.00 59.57  ?  596  LYS D NZ  1 
ATOM   10647 N N   . LEU D  1  597 ? 9.321   -27.422 -12.400 1.00 55.65  ?  597  LEU D N   1 
ATOM   10648 C CA  . LEU D  1  597 ? 8.838   -26.450 -11.416 1.00 53.68  ?  597  LEU D CA  1 
ATOM   10649 C C   . LEU D  1  597 ? 9.414   -26.828 -10.056 1.00 55.24  ?  597  LEU D C   1 
ATOM   10650 O O   . LEU D  1  597 ? 8.806   -27.565 -9.279  1.00 55.54  ?  597  LEU D O   1 
ATOM   10651 C CB  . LEU D  1  597 ? 7.314   -26.415 -11.390 1.00 51.58  ?  597  LEU D CB  1 
ATOM   10652 C CG  . LEU D  1  597 ? 6.571   -26.122 -12.696 1.00 50.61  ?  597  LEU D CG  1 
ATOM   10653 C CD1 . LEU D  1  597 ? 5.165   -25.628 -12.404 1.00 48.00  ?  597  LEU D CD1 1 
ATOM   10654 C CD2 . LEU D  1  597 ? 7.324   -25.099 -13.530 1.00 50.14  ?  597  LEU D CD2 1 
ATOM   10655 N N   . SER D  1  598 ? 10.604  -26.298 -9.762  1.00 55.38  ?  598  SER D N   1 
ATOM   10656 C CA  . SER D  1  598 ? 11.360  -26.750 -8.596  1.00 57.61  ?  598  SER D CA  1 
ATOM   10657 C C   . SER D  1  598 ? 10.669  -26.384 -7.288  1.00 55.95  ?  598  SER D C   1 
ATOM   10658 O O   . SER D  1  598 ? 10.668  -27.176 -6.339  1.00 57.47  ?  598  SER D O   1 
ATOM   10659 C CB  . SER D  1  598 ? 12.771  -26.164 -8.631  1.00 58.81  ?  598  SER D CB  1 
ATOM   10660 O OG  . SER D  1  598 ? 12.731  -24.748 -8.680  1.00 56.90  ?  598  SER D OG  1 
ATOM   10661 N N   . GLN D  1  599 ? 10.078  -25.195 -7.215  1.00 56.97  ?  599  GLN D N   1 
ATOM   10662 C CA  . GLN D  1  599 ? 9.572   -24.655 -5.961  1.00 55.97  ?  599  GLN D CA  1 
ATOM   10663 C C   . GLN D  1  599 ? 8.149   -25.096 -5.651  1.00 54.60  ?  599  GLN D C   1 
ATOM   10664 O O   . GLN D  1  599 ? 7.554   -24.593 -4.692  1.00 53.58  ?  599  GLN D O   1 
ATOM   10665 C CB  . GLN D  1  599 ? 9.653   -23.128 -5.980  1.00 54.27  ?  599  GLN D CB  1 
ATOM   10666 C CG  . GLN D  1  599 ? 11.033  -22.589 -6.325  1.00 55.95  ?  599  GLN D CG  1 
ATOM   10667 C CD  . GLN D  1  599 ? 12.139  -23.173 -5.464  1.00 58.94  ?  599  GLN D CD  1 
ATOM   10668 O OE1 . GLN D  1  599 ? 11.944  -23.452 -4.281  1.00 59.47  ?  599  GLN D OE1 1 
ATOM   10669 N NE2 . GLN D  1  599 ? 13.310  -23.364 -6.062  1.00 60.84  ?  599  GLN D NE2 1 
ATOM   10670 N N   . LEU D  1  600 ? 7.591   -26.013 -6.438  1.00 52.74  ?  600  LEU D N   1 
ATOM   10671 C CA  . LEU D  1  600 ? 6.221   -26.458 -6.221  1.00 51.89  ?  600  LEU D CA  1 
ATOM   10672 C C   . LEU D  1  600 ? 6.081   -27.129 -4.860  1.00 53.14  ?  600  LEU D C   1 
ATOM   10673 O O   . LEU D  1  600 ? 6.892   -27.981 -4.485  1.00 55.39  ?  600  LEU D O   1 
ATOM   10674 C CB  . LEU D  1  600 ? 5.812   -27.425 -7.332  1.00 52.28  ?  600  LEU D CB  1 
ATOM   10675 C CG  . LEU D  1  600 ? 4.353   -27.457 -7.786  1.00 50.37  ?  600  LEU D CG  1 
ATOM   10676 C CD1 . LEU D  1  600 ? 3.865   -26.061 -8.119  1.00 47.94  ?  600  LEU D CD1 1 
ATOM   10677 C CD2 . LEU D  1  600 ? 4.202   -28.377 -8.988  1.00 51.20  ?  600  LEU D CD2 1 
ATOM   10678 N N   . GLN D  1  601 ? 5.049   -26.735 -4.119  1.00 51.92  ?  601  GLN D N   1 
ATOM   10679 C CA  . GLN D  1  601 ? 4.706   -27.344 -2.838  1.00 53.03  ?  601  GLN D CA  1 
ATOM   10680 C C   . GLN D  1  601 ? 3.404   -28.125 -2.879  1.00 52.94  ?  601  GLN D C   1 
ATOM   10681 O O   . GLN D  1  601 ? 3.319   -29.209 -2.296  1.00 54.95  ?  601  GLN D O   1 
ATOM   10682 C CB  . GLN D  1  601 ? 4.617   -26.273 -1.745  1.00 51.97  ?  601  GLN D CB  1 
ATOM   10683 C CG  . GLN D  1  601 ? 4.250   -26.823 -0.374  1.00 53.61  ?  601  GLN D CG  1 
ATOM   10684 C CD  . GLN D  1  601 ? 4.050   -25.736 0.662   1.00 52.84  ?  601  GLN D CD  1 
ATOM   10685 O OE1 . GLN D  1  601 ? 4.733   -24.711 0.644   1.00 51.64  ?  601  GLN D OE1 1 
ATOM   10686 N NE2 . GLN D  1  601 ? 3.108   -25.953 1.572   1.00 52.36  ?  601  GLN D NE2 1 
ATOM   10687 N N   . MET D  1  602 ? 2.386   -27.599 -3.555  1.00 50.38  ?  602  MET D N   1 
ATOM   10688 C CA  . MET D  1  602 ? 1.107   -28.275 -3.702  1.00 50.20  ?  602  MET D CA  1 
ATOM   10689 C C   . MET D  1  602 ? 0.730   -28.307 -5.175  1.00 49.20  ?  602  MET D C   1 
ATOM   10690 O O   . MET D  1  602 ? 0.873   -27.307 -5.885  1.00 47.62  ?  602  MET D O   1 
ATOM   10691 C CB  . MET D  1  602 ? 0.013   -27.576 -2.885  1.00 48.69  ?  602  MET D CB  1 
ATOM   10692 C CG  . MET D  1  602 ? 0.064   -27.886 -1.397  1.00 50.05  ?  602  MET D CG  1 
ATOM   10693 S SD  . MET D  1  602 ? -0.614  -26.557 -0.384  1.00 48.76  ?  602  MET D SD  1 
ATOM   10694 C CE  . MET D  1  602 ? -2.276  -27.162 -0.094  1.00 48.63  ?  602  MET D CE  1 
ATOM   10695 N N   . LEU D  1  603 ? 0.245   -29.461 -5.626  1.00 43.04  ?  603  LEU D N   1 
ATOM   10696 C CA  . LEU D  1  603 ? -0.042  -29.673 -7.042  1.00 42.58  ?  603  LEU D CA  1 
ATOM   10697 C C   . LEU D  1  603 ? -1.239  -30.607 -7.140  1.00 43.08  ?  603  LEU D C   1 
ATOM   10698 O O   . LEU D  1  603 ? -1.108  -31.811 -6.900  1.00 45.13  ?  603  LEU D O   1 
ATOM   10699 C CB  . LEU D  1  603 ? 1.173   -30.252 -7.763  1.00 44.17  ?  603  LEU D CB  1 
ATOM   10700 C CG  . LEU D  1  603 ? 0.975   -30.787 -9.183  1.00 44.38  ?  603  LEU D CG  1 
ATOM   10701 C CD1 . LEU D  1  603 ? 0.527   -29.678 -10.119 1.00 42.18  ?  603  LEU D CD1 1 
ATOM   10702 C CD2 . LEU D  1  603 ? 2.250   -31.444 -9.692  1.00 46.39  ?  603  LEU D CD2 1 
ATOM   10703 N N   . ASP D  1  604 ? -2.399  -30.055 -7.478  1.00 41.92  ?  604  ASP D N   1 
ATOM   10704 C CA  . ASP D  1  604 ? -3.627  -30.826 -7.614  1.00 42.36  ?  604  ASP D CA  1 
ATOM   10705 C C   . ASP D  1  604 ? -4.032  -30.868 -9.082  1.00 41.74  ?  604  ASP D C   1 
ATOM   10706 O O   . ASP D  1  604 ? -4.309  -29.825 -9.684  1.00 39.97  ?  604  ASP D O   1 
ATOM   10707 C CB  . ASP D  1  604 ? -4.746  -30.231 -6.761  1.00 41.30  ?  604  ASP D CB  1 
ATOM   10708 C CG  . ASP D  1  604 ? -5.953  -31.143 -6.664  1.00 42.27  ?  604  ASP D CG  1 
ATOM   10709 O OD1 . ASP D  1  604 ? -5.922  -32.242 -7.256  1.00 43.72  ?  604  ASP D OD1 1 
ATOM   10710 O OD2 . ASP D  1  604 ? -6.938  -30.760 -6.001  1.00 41.71  -1 604  ASP D OD2 1 
ATOM   10711 N N   . LEU D  1  605 ? -4.055  -32.074 -9.652  1.00 39.72  ?  605  LEU D N   1 
ATOM   10712 C CA  . LEU D  1  605 ? -4.525  -32.300 -11.014 1.00 39.50  ?  605  LEU D CA  1 
ATOM   10713 C C   . LEU D  1  605 ? -5.725  -33.241 -11.047 1.00 40.44  ?  605  LEU D C   1 
ATOM   10714 O O   . LEU D  1  605 ? -5.978  -33.883 -12.071 1.00 41.12  ?  605  LEU D O   1 
ATOM   10715 C CB  . LEU D  1  605 ? -3.395  -32.856 -11.882 1.00 40.73  ?  605  LEU D CB  1 
ATOM   10716 C CG  . LEU D  1  605 ? -2.106  -32.038 -11.966 1.00 40.25  ?  605  LEU D CG  1 
ATOM   10717 C CD1 . LEU D  1  605 ? -1.113  -32.704 -12.906 1.00 41.79  ?  605  LEU D CD1 1 
ATOM   10718 C CD2 . LEU D  1  605 ? -2.399  -30.616 -12.414 1.00 37.97  ?  605  LEU D CD2 1 
ATOM   10719 N N   . SER D  1  606 ? -6.475  -33.325 -9.952  1.00 43.48  ?  606  SER D N   1 
ATOM   10720 C CA  . SER D  1  606 ? -7.522  -34.324 -9.811  1.00 44.84  ?  606  SER D CA  1 
ATOM   10721 C C   . SER D  1  606 ? -8.743  -33.958 -10.651 1.00 43.76  ?  606  SER D C   1 
ATOM   10722 O O   . SER D  1  606 ? -8.864  -32.850 -11.175 1.00 41.90  ?  606  SER D O   1 
ATOM   10723 C CB  . SER D  1  606 ? -7.918  -34.482 -8.343  1.00 45.57  ?  606  SER D CB  1 
ATOM   10724 O OG  . SER D  1  606 ? -8.367  -33.256 -7.793  1.00 43.73  ?  606  SER D OG  1 
ATOM   10725 N N   . TYR D  1  607 ? -9.644  -34.930 -10.801 1.00 49.09  ?  607  TYR D N   1 
ATOM   10726 C CA  . TYR D  1  607 ? -10.939 -34.723 -11.448 1.00 48.40  ?  607  TYR D CA  1 
ATOM   10727 C C   . TYR D  1  607 ? -10.757 -34.174 -12.864 1.00 47.17  ?  607  TYR D C   1 
ATOM   10728 O O   . TYR D  1  607 ? -11.199 -33.073 -13.202 1.00 45.22  ?  607  TYR D O   1 
ATOM   10729 C CB  . TYR D  1  607 ? -11.828 -33.807 -10.600 1.00 46.94  ?  607  TYR D CB  1 
ATOM   10730 C CG  . TYR D  1  607 ? -12.314 -34.453 -9.323  1.00 48.44  ?  607  TYR D CG  1 
ATOM   10731 C CD1 . TYR D  1  607 ? -11.491 -34.535 -8.206  1.00 49.02  ?  607  TYR D CD1 1 
ATOM   10732 C CD2 . TYR D  1  607 ? -13.594 -34.983 -9.233  1.00 50.26  ?  607  TYR D CD2 1 
ATOM   10733 C CE1 . TYR D  1  607 ? -11.930 -35.127 -7.037  1.00 50.54  ?  607  TYR D CE1 1 
ATOM   10734 C CE2 . TYR D  1  607 ? -14.042 -35.576 -8.068  1.00 51.41  ?  607  TYR D CE2 1 
ATOM   10735 C CZ  . TYR D  1  607 ? -13.206 -35.645 -6.973  1.00 51.65  ?  607  TYR D CZ  1 
ATOM   10736 O OH  . TYR D  1  607 ? -13.650 -36.235 -5.812  1.00 53.67  ?  607  TYR D OH  1 
ATOM   10737 N N   . ASN D  1  608 ? -10.083 -34.968 -13.690 1.00 47.11  ?  608  ASN D N   1 
ATOM   10738 C CA  . ASN D  1  608 ? -9.738  -34.552 -15.039 1.00 46.35  ?  608  ASN D CA  1 
ATOM   10739 C C   . ASN D  1  608 ? -9.810  -35.769 -15.953 1.00 48.15  ?  608  ASN D C   1 
ATOM   10740 O O   . ASN D  1  608 ? -10.311 -36.829 -15.566 1.00 49.82  ?  608  ASN D O   1 
ATOM   10741 C CB  . ASN D  1  608 ? -8.355  -33.890 -15.051 1.00 45.55  ?  608  ASN D CB  1 
ATOM   10742 C CG  . ASN D  1  608 ? -8.433  -32.392 -14.881 1.00 43.40  ?  608  ASN D CG  1 
ATOM   10743 O OD1 . ASN D  1  608 ? -9.286  -31.738 -15.474 1.00 42.39  ?  608  ASN D OD1 1 
ATOM   10744 N ND2 . ASN D  1  608 ? -7.546  -31.840 -14.063 1.00 42.84  ?  608  ASN D ND2 1 
ATOM   10745 N N   . GLN D  1  609 ? -9.306  -35.614 -17.177 1.00 48.95  ?  609  GLN D N   1 
ATOM   10746 C CA  . GLN D  1  609 ? -9.300  -36.685 -18.166 1.00 50.63  ?  609  GLN D CA  1 
ATOM   10747 C C   . GLN D  1  609 ? -7.882  -37.014 -18.619 1.00 51.47  ?  609  GLN D C   1 
ATOM   10748 O O   . GLN D  1  609 ? -7.663  -37.394 -19.771 1.00 52.74  ?  609  GLN D O   1 
ATOM   10749 C CB  . GLN D  1  609 ? -10.170 -36.315 -19.367 1.00 50.07  ?  609  GLN D CB  1 
ATOM   10750 C CG  . GLN D  1  609 ? -11.583 -36.870 -19.310 1.00 50.86  ?  609  GLN D CG  1 
ATOM   10751 C CD  . GLN D  1  609 ? -12.461 -36.327 -20.419 1.00 50.71  ?  609  GLN D CD  1 
ATOM   10752 O OE1 . GLN D  1  609 ? -12.169 -36.508 -21.602 1.00 51.37  ?  609  GLN D OE1 1 
ATOM   10753 N NE2 . GLN D  1  609 ? -13.537 -35.645 -20.043 1.00 49.86  ?  609  GLN D NE2 1 
ATOM   10754 N N   . LEU D  1  610 ? -6.912  -36.873 -17.720 1.00 49.81  ?  610  LEU D N   1 
ATOM   10755 C CA  . LEU D  1  610 ? -5.524  -37.154 -18.054 1.00 50.81  ?  610  LEU D CA  1 
ATOM   10756 C C   . LEU D  1  610 ? -5.296  -38.658 -18.123 1.00 53.42  ?  610  LEU D C   1 
ATOM   10757 O O   . LEU D  1  610 ? -5.715  -39.400 -17.229 1.00 54.53  ?  610  LEU D O   1 
ATOM   10758 C CB  . LEU D  1  610 ? -4.590  -36.521 -17.022 1.00 50.19  ?  610  LEU D CB  1 
ATOM   10759 C CG  . LEU D  1  610 ? -4.730  -35.011 -16.807 1.00 47.74  ?  610  LEU D CG  1 
ATOM   10760 C CD1 . LEU D  1  610 ? -4.670  -34.662 -15.326 1.00 47.24  ?  610  LEU D CD1 1 
ATOM   10761 C CD2 . LEU D  1  610 ? -3.663  -34.252 -17.583 1.00 47.20  ?  610  LEU D CD2 1 
ATOM   10762 N N   . ASP D  1  611 ? -4.634  -39.104 -19.183 1.00 57.83  ?  611  ASP D N   1 
ATOM   10763 C CA  . ASP D  1  611 ? -4.260  -40.500 -19.354 1.00 60.51  ?  611  ASP D CA  1 
ATOM   10764 C C   . ASP D  1  611 ? -2.742  -40.604 -19.489 1.00 61.78  ?  611  ASP D C   1 
ATOM   10765 O O   . ASP D  1  611 ? -2.016  -39.612 -19.383 1.00 60.37  ?  611  ASP D O   1 
ATOM   10766 C CB  . ASP D  1  611 ? -4.987  -41.122 -20.553 1.00 61.34  ?  611  ASP D CB  1 
ATOM   10767 C CG  . ASP D  1  611 ? -4.608  -40.480 -21.875 1.00 60.56  ?  611  ASP D CG  1 
ATOM   10768 O OD1 . ASP D  1  611 ? -3.961  -39.414 -21.867 1.00 59.11  ?  611  ASP D OD1 1 
ATOM   10769 O OD2 . ASP D  1  611 ? -4.967  -41.044 -22.930 1.00 61.85  -1 611  ASP D OD2 1 
ATOM   10770 N N   . GLY D  1  612 ? -2.264  -41.818 -19.721 1.00 63.95  ?  612  GLY D N   1 
ATOM   10771 C CA  . GLY D  1  612 ? -0.838  -42.057 -19.768 1.00 65.52  ?  612  GLY D CA  1 
ATOM   10772 C C   . GLY D  1  612 ? -0.271  -42.394 -18.405 1.00 66.64  ?  612  GLY D C   1 
ATOM   10773 O O   . GLY D  1  612 ? -0.981  -42.533 -17.406 1.00 66.37  ?  612  GLY D O   1 
ATOM   10774 N N   . GLU D  1  613 ? 1.050   -42.517 -18.370 1.00 69.05  ?  613  GLU D N   1 
ATOM   10775 C CA  . GLU D  1  613 ? 1.758   -42.977 -17.186 1.00 70.34  ?  613  GLU D CA  1 
ATOM   10776 C C   . GLU D  1  613 ? 2.318   -41.799 -16.399 1.00 68.62  ?  613  GLU D C   1 
ATOM   10777 O O   . GLU D  1  613 ? 2.725   -40.783 -16.968 1.00 67.02  ?  613  GLU D O   1 
ATOM   10778 C CB  . GLU D  1  613 ? 2.891   -43.929 -17.573 1.00 73.47  ?  613  GLU D CB  1 
ATOM   10779 C CG  . GLU D  1  613 ? 2.421   -45.165 -18.321 1.00 75.50  ?  613  GLU D CG  1 
ATOM   10780 C CD  . GLU D  1  613 ? 3.517   -46.193 -18.498 1.00 78.98  ?  613  GLU D CD  1 
ATOM   10781 O OE1 . GLU D  1  613 ? 4.495   -45.901 -19.218 1.00 79.60  ?  613  GLU D OE1 1 
ATOM   10782 O OE2 . GLU D  1  613 ? 3.401   -47.294 -17.921 1.00 81.68  -1 613  GLU D OE2 1 
ATOM   10783 N N   . ILE D  1  614 ? 2.325   -41.945 -15.075 1.00 68.87  ?  614  ILE D N   1 
ATOM   10784 C CA  . ILE D  1  614 ? 2.894   -40.920 -14.207 1.00 67.60  ?  614  ILE D CA  1 
ATOM   10785 C C   . ILE D  1  614 ? 4.401   -40.892 -14.415 1.00 69.22  ?  614  ILE D C   1 
ATOM   10786 O O   . ILE D  1  614 ? 5.097   -41.879 -14.149 1.00 72.17  ?  614  ILE D O   1 
ATOM   10787 C CB  . ILE D  1  614 ? 2.542   -41.180 -12.737 1.00 68.11  ?  614  ILE D CB  1 
ATOM   10788 C CG1 . ILE D  1  614 ? 1.031   -41.338 -12.564 1.00 66.96  ?  614  ILE D CG1 1 
ATOM   10789 C CG2 . ILE D  1  614 ? 3.072   -40.060 -11.854 1.00 66.69  ?  614  ILE D CG2 1 
ATOM   10790 C CD1 . ILE D  1  614 ? 0.639   -41.975 -11.252 1.00 68.71  ?  614  ILE D CD1 1 
ATOM   10791 N N   . SER D  1  615 ? 4.908   -39.762 -14.903 1.00 69.12  ?  615  SER D N   1 
ATOM   10792 C CA  . SER D  1  615 ? 6.327   -39.643 -15.205 1.00 70.68  ?  615  SER D CA  1 
ATOM   10793 C C   . SER D  1  615 ? 7.164   -39.839 -13.949 1.00 72.41  ?  615  SER D C   1 
ATOM   10794 O O   . SER D  1  615 ? 6.878   -39.258 -12.898 1.00 71.09  ?  615  SER D O   1 
ATOM   10795 C CB  . SER D  1  615 ? 6.619   -38.277 -15.827 1.00 68.46  ?  615  SER D CB  1 
ATOM   10796 O OG  . SER D  1  615 ? 8.008   -38.106 -16.049 1.00 70.10  ?  615  SER D OG  1 
ATOM   10797 N N   . SER D  1  616 ? 8.207   -40.663 -14.063 1.00 73.78  ?  616  SER D N   1 
ATOM   10798 C CA  . SER D  1  616 ? 9.154   -40.830 -12.969 1.00 75.81  ?  616  SER D CA  1 
ATOM   10799 C C   . SER D  1  616 ? 10.017  -39.594 -12.765 1.00 74.72  ?  616  SER D C   1 
ATOM   10800 O O   . SER D  1  616 ? 10.695  -39.494 -11.737 1.00 75.89  ?  616  SER D O   1 
ATOM   10801 C CB  . SER D  1  616 ? 10.043  -42.048 -13.221 1.00 79.72  ?  616  SER D CB  1 
ATOM   10802 O OG  . SER D  1  616 ? 10.821  -41.879 -14.393 1.00 80.39  ?  616  SER D OG  1 
ATOM   10803 N N   . GLN D  1  617 ? 10.005  -38.658 -13.717 1.00 75.76  ?  617  GLN D N   1 
ATOM   10804 C CA  . GLN D  1  617 ? 10.736  -37.406 -13.584 1.00 74.60  ?  617  GLN D CA  1 
ATOM   10805 C C   . GLN D  1  617 ? 10.170  -36.507 -12.493 1.00 72.24  ?  617  GLN D C   1 
ATOM   10806 O O   . GLN D  1  617 ? 10.778  -35.475 -12.191 1.00 70.98  ?  617  GLN D O   1 
ATOM   10807 C CB  . GLN D  1  617 ? 10.741  -36.663 -14.921 1.00 72.75  ?  617  GLN D CB  1 
ATOM   10808 C CG  . GLN D  1  617 ? 12.002  -35.856 -15.178 1.00 73.55  ?  617  GLN D CG  1 
ATOM   10809 C CD  . GLN D  1  617 ? 13.244  -36.725 -15.235 1.00 77.84  ?  617  GLN D CD  1 
ATOM   10810 O OE1 . GLN D  1  617 ? 13.331  -37.650 -16.044 1.00 79.56  ?  617  GLN D OE1 1 
ATOM   10811 N NE2 . GLN D  1  617 ? 14.214  -36.429 -14.378 1.00 78.88  ?  617  GLN D NE2 1 
ATOM   10812 N N   . PHE D  1  618 ? 9.025   -36.866 -11.901 1.00 73.67  ?  618  PHE D N   1 
ATOM   10813 C CA  . PHE D  1  618 ? 8.488   -36.126 -10.763 1.00 71.57  ?  618  PHE D CA  1 
ATOM   10814 C C   . PHE D  1  618 ? 9.448   -36.093 -9.581  1.00 73.46  ?  618  PHE D C   1 
ATOM   10815 O O   . PHE D  1  618 ? 9.236   -35.303 -8.655  1.00 71.59  ?  618  PHE D O   1 
ATOM   10816 C CB  . PHE D  1  618 ? 7.153   -36.731 -10.321 1.00 71.38  ?  618  PHE D CB  1 
ATOM   10817 C CG  . PHE D  1  618 ? 5.956   -36.130 -11.004 1.00 68.90  ?  618  PHE D CG  1 
ATOM   10818 C CD1 . PHE D  1  618 ? 6.079   -35.522 -12.241 1.00 67.25  ?  618  PHE D CD1 1 
ATOM   10819 C CD2 . PHE D  1  618 ? 4.707   -36.171 -10.404 1.00 67.52  ?  618  PHE D CD2 1 
ATOM   10820 C CE1 . PHE D  1  618 ? 4.980   -34.967 -12.870 1.00 64.28  ?  618  PHE D CE1 1 
ATOM   10821 C CE2 . PHE D  1  618 ? 3.604   -35.618 -11.028 1.00 64.34  ?  618  PHE D CE2 1 
ATOM   10822 C CZ  . PHE D  1  618 ? 3.741   -35.015 -12.263 1.00 62.91  ?  618  PHE D CZ  1 
ATOM   10823 N N   . ARG D  1  619 ? 10.496  -36.923 -9.599  1.00 76.16  ?  619  ARG D N   1 
ATOM   10824 C CA  . ARG D  1  619 ? 11.508  -36.922 -8.549  1.00 77.80  ?  619  ARG D CA  1 
ATOM   10825 C C   . ARG D  1  619 ? 12.197  -35.570 -8.409  1.00 76.21  ?  619  ARG D C   1 
ATOM   10826 O O   . ARG D  1  619 ? 12.769  -35.283 -7.352  1.00 77.09  ?  619  ARG D O   1 
ATOM   10827 C CB  . ARG D  1  619 ? 12.539  -38.014 -8.844  1.00 81.58  ?  619  ARG D CB  1 
ATOM   10828 C CG  . ARG D  1  619 ? 13.419  -38.421 -7.674  1.00 84.76  ?  619  ARG D CG  1 
ATOM   10829 C CD  . ARG D  1  619 ? 14.698  -39.071 -8.185  1.00 88.11  ?  619  ARG D CD  1 
ATOM   10830 N NE  . ARG D  1  619 ? 15.397  -39.825 -7.151  1.00 91.99  ?  619  ARG D NE  1 
ATOM   10831 C CZ  . ARG D  1  619 ? 16.715  -39.851 -7.008  1.00 94.81  ?  619  ARG D CZ  1 
ATOM   10832 N NH1 . ARG D  1  619 ? 17.512  -39.173 -7.817  1.00 94.46  ?  619  ARG D NH1 1 
ATOM   10833 N NH2 . ARG D  1  619 ? 17.246  -40.581 -6.031  1.00 97.88  ?  619  ARG D NH2 1 
ATOM   10834 N N   . SER D  1  620 ? 12.148  -34.732 -9.447  1.00 71.54  ?  620  SER D N   1 
ATOM   10835 C CA  . SER D  1  620 ? 12.838  -33.449 -9.420  1.00 70.33  ?  620  SER D CA  1 
ATOM   10836 C C   . SER D  1  620 ? 12.193  -32.452 -8.464  1.00 67.56  ?  620  SER D C   1 
ATOM   10837 O O   . SER D  1  620 ? 12.879  -31.542 -7.987  1.00 67.32  ?  620  SER D O   1 
ATOM   10838 C CB  . SER D  1  620 ? 12.883  -32.852 -10.827 1.00 68.82  ?  620  SER D CB  1 
ATOM   10839 O OG  . SER D  1  620 ? 13.275  -33.822 -11.782 1.00 71.01  ?  620  SER D OG  1 
ATOM   10840 N N   . LEU D  1  621 ? 10.902  -32.601 -8.171  1.00 63.67  ?  621  LEU D N   1 
ATOM   10841 C CA  . LEU D  1  621 ? 10.173  -31.646 -7.334  1.00 61.19  ?  621  LEU D CA  1 
ATOM   10842 C C   . LEU D  1  621 ? 10.554  -31.886 -5.878  1.00 62.76  ?  621  LEU D C   1 
ATOM   10843 O O   . LEU D  1  621 ? 9.895   -32.626 -5.144  1.00 63.36  ?  621  LEU D O   1 
ATOM   10844 C CB  . LEU D  1  621 ? 8.670   -31.773 -7.559  1.00 59.08  ?  621  LEU D CB  1 
ATOM   10845 C CG  . LEU D  1  621 ? 8.057   -30.893 -8.658  1.00 56.46  ?  621  LEU D CG  1 
ATOM   10846 C CD1 . LEU D  1  621 ? 8.930   -30.859 -9.887  1.00 57.36  ?  621  LEU D CD1 1 
ATOM   10847 C CD2 . LEU D  1  621 ? 6.670   -31.376 -9.041  1.00 55.27  ?  621  LEU D CD2 1 
ATOM   10848 N N   . GLN D  1  622 ? 11.637  -31.230 -5.454  1.00 61.82  ?  622  GLN D N   1 
ATOM   10849 C CA  . GLN D  1  622 ? 12.218  -31.477 -4.141  1.00 63.84  ?  622  GLN D CA  1 
ATOM   10850 C C   . GLN D  1  622 ? 11.382  -30.907 -3.003  1.00 62.08  ?  622  GLN D C   1 
ATOM   10851 O O   . GLN D  1  622 ? 11.552  -31.333 -1.856  1.00 63.78  ?  622  GLN D O   1 
ATOM   10852 C CB  . GLN D  1  622 ? 13.629  -30.889 -4.078  1.00 65.31  ?  622  GLN D CB  1 
ATOM   10853 C CG  . GLN D  1  622 ? 14.634  -31.574 -4.988  1.00 67.90  ?  622  GLN D CG  1 
ATOM   10854 C CD  . GLN D  1  622 ? 15.249  -32.805 -4.355  1.00 71.58  ?  622  GLN D CD  1 
ATOM   10855 O OE1 . GLN D  1  622 ? 14.584  -33.825 -4.176  1.00 72.31  ?  622  GLN D OE1 1 
ATOM   10856 N NE2 . GLN D  1  622 ? 16.528  -32.714 -4.009  1.00 74.13  ?  622  GLN D NE2 1 
ATOM   10857 N N   . ASN D  1  623 ? 10.492  -29.957 -3.284  1.00 63.06  ?  623  ASN D N   1 
ATOM   10858 C CA  . ASN D  1  623 ? 9.713   -29.291 -2.249  1.00 61.36  ?  623  ASN D CA  1 
ATOM   10859 C C   . ASN D  1  623 ? 8.264   -29.750 -2.191  1.00 60.09  ?  623  ASN D C   1 
ATOM   10860 O O   . ASN D  1  623 ? 7.509   -29.256 -1.347  1.00 58.79  ?  623  ASN D O   1 
ATOM   10861 C CB  . ASN D  1  623 ? 9.763   -27.772 -2.447  1.00 59.08  ?  623  ASN D CB  1 
ATOM   10862 C CG  . ASN D  1  623 ? 11.096  -27.176 -2.041  1.00 60.24  ?  623  ASN D CG  1 
ATOM   10863 O OD1 . ASN D  1  623 ? 11.434  -27.131 -0.858  1.00 61.38  ?  623  ASN D OD1 1 
ATOM   10864 N ND2 . ASN D  1  623 ? 11.862  -26.716 -3.023  1.00 60.28  ?  623  ASN D ND2 1 
ATOM   10865 N N   . LEU D  1  624 ? 7.854   -30.671 -3.062  1.00 58.86  ?  624  LEU D N   1 
ATOM   10866 C CA  . LEU D  1  624 ? 6.460   -31.094 -3.108  1.00 57.74  ?  624  LEU D CA  1 
ATOM   10867 C C   . LEU D  1  624 ? 6.043   -31.753 -1.799  1.00 59.17  ?  624  LEU D C   1 
ATOM   10868 O O   . LEU D  1  624 ? 6.685   -32.696 -1.327  1.00 61.98  ?  624  LEU D O   1 
ATOM   10869 C CB  . LEU D  1  624 ? 6.245   -32.057 -4.278  1.00 58.46  ?  624  LEU D CB  1 
ATOM   10870 C CG  . LEU D  1  624 ? 4.849   -32.116 -4.902  1.00 56.57  ?  624  LEU D CG  1 
ATOM   10871 C CD1 . LEU D  1  624 ? 4.916   -32.665 -6.307  1.00 56.90  ?  624  LEU D CD1 1 
ATOM   10872 C CD2 . LEU D  1  624 ? 3.936   -32.985 -4.064  1.00 57.52  ?  624  LEU D CD2 1 
ATOM   10873 N N   . GLU D  1  625 ? 4.953   -31.251 -1.218  1.00 58.89  ?  625  GLU D N   1 
ATOM   10874 C CA  . GLU D  1  625 ? 4.379   -31.809 -0.003  1.00 60.12  ?  625  GLU D CA  1 
ATOM   10875 C C   . GLU D  1  625 ? 3.027   -32.472 -0.213  1.00 59.74  ?  625  GLU D C   1 
ATOM   10876 O O   . GLU D  1  625 ? 2.723   -33.451 0.472   1.00 61.81  ?  625  GLU D O   1 
ATOM   10877 C CB  . GLU D  1  625 ? 4.232   -30.718 1.065   1.00 58.87  ?  625  GLU D CB  1 
ATOM   10878 C CG  . GLU D  1  625 ? 5.537   -30.031 1.431   1.00 59.42  ?  625  GLU D CG  1 
ATOM   10879 C CD  . GLU D  1  625 ? 5.395   -29.106 2.624   1.00 58.66  ?  625  GLU D CD  1 
ATOM   10880 O OE1 . GLU D  1  625 ? 4.678   -29.470 3.580   1.00 59.33  ?  625  GLU D OE1 1 
ATOM   10881 O OE2 . GLU D  1  625 ? 6.002   -28.015 2.605   1.00 57.53  -1 625  GLU D OE2 1 
ATOM   10882 N N   . ARG D  1  626 ? 2.210   -31.968 -1.136  1.00 60.05  ?  626  ARG D N   1 
ATOM   10883 C CA  . ARG D  1  626 ? 0.879   -32.507 -1.381  1.00 59.57  ?  626  ARG D CA  1 
ATOM   10884 C C   . ARG D  1  626 ? 0.708   -32.782 -2.866  1.00 58.73  ?  626  ARG D C   1 
ATOM   10885 O O   . ARG D  1  626 ? 1.011   -31.921 -3.699  1.00 56.99  ?  626  ARG D O   1 
ATOM   10886 C CB  . ARG D  1  626 ? -0.207  -31.543 -0.897  1.00 57.23  ?  626  ARG D CB  1 
ATOM   10887 C CG  . ARG D  1  626 ? -0.553  -31.691 0.571   1.00 58.59  ?  626  ARG D CG  1 
ATOM   10888 C CD  . ARG D  1  626 ? -1.136  -30.406 1.135   1.00 56.22  ?  626  ARG D CD  1 
ATOM   10889 N NE  . ARG D  1  626 ? -1.824  -30.631 2.401   1.00 57.69  ?  626  ARG D NE  1 
ATOM   10890 C CZ  . ARG D  1  626 ? -2.975  -31.278 2.529   1.00 58.78  ?  626  ARG D CZ  1 
ATOM   10891 N NH1 . ARG D  1  626 ? -3.618  -31.763 1.479   1.00 58.45  ?  626  ARG D NH1 1 
ATOM   10892 N NH2 . ARG D  1  626 ? -3.493  -31.445 3.742   1.00 59.48  ?  626  ARG D NH2 1 
ATOM   10893 N N   . LEU D  1  627 ? 0.203   -33.970 -3.190  1.00 50.92  ?  627  LEU D N   1 
ATOM   10894 C CA  . LEU D  1  627 ? 0.020   -34.391 -4.571  1.00 50.67  ?  627  LEU D CA  1 
ATOM   10895 C C   . LEU D  1  627 ? -1.311  -35.115 -4.690  1.00 50.92  ?  627  LEU D C   1 
ATOM   10896 O O   . LEU D  1  627 ? -1.591  -36.032 -3.913  1.00 52.94  ?  627  LEU D O   1 
ATOM   10897 C CB  . LEU D  1  627 ? 1.166   -35.305 -5.021  1.00 53.03  ?  627  LEU D CB  1 
ATOM   10898 C CG  . LEU D  1  627 ? 1.354   -35.525 -6.522  1.00 52.78  ?  627  LEU D CG  1 
ATOM   10899 C CD1 . LEU D  1  627 ? 1.105   -34.236 -7.289  1.00 49.89  ?  627  LEU D CD1 1 
ATOM   10900 C CD2 . LEU D  1  627 ? 2.746   -36.068 -6.811  1.00 54.98  ?  627  LEU D CD2 1 
ATOM   10901 N N   . ASP D  1  628 ? -2.129  -34.701 -5.656  1.00 49.54  ?  628  ASP D N   1 
ATOM   10902 C CA  . ASP D  1  628 ? -3.423  -35.328 -5.910  1.00 49.76  ?  628  ASP D CA  1 
ATOM   10903 C C   . ASP D  1  628 ? -3.555  -35.570 -7.408  1.00 49.35  ?  628  ASP D C   1 
ATOM   10904 O O   . ASP D  1  628 ? -3.685  -34.618 -8.186  1.00 47.27  ?  628  ASP D O   1 
ATOM   10905 C CB  . ASP D  1  628 ? -4.568  -34.458 -5.387  1.00 47.95  ?  628  ASP D CB  1 
ATOM   10906 C CG  . ASP D  1  628 ? -5.879  -35.216 -5.285  1.00 48.83  ?  628  ASP D CG  1 
ATOM   10907 O OD1 . ASP D  1  628 ? -5.943  -36.368 -5.761  1.00 50.61  ?  628  ASP D OD1 1 
ATOM   10908 O OD2 . ASP D  1  628 ? -6.848  -34.659 -4.725  1.00 47.88  -1 628  ASP D OD2 1 
ATOM   10909 N N   . LEU D  1  629 ? -3.517  -36.843 -7.809  1.00 47.40  ?  629  LEU D N   1 
ATOM   10910 C CA  . LEU D  1  629 ? -3.695  -37.250 -9.200  1.00 47.42  ?  629  LEU D CA  1 
ATOM   10911 C C   . LEU D  1  629 ? -4.953  -38.090 -9.390  1.00 48.27  ?  629  LEU D C   1 
ATOM   10912 O O   . LEU D  1  629 ? -5.046  -38.852 -10.357 1.00 49.25  ?  629  LEU D O   1 
ATOM   10913 C CB  . LEU D  1  629 ? -2.472  -38.022 -9.703  1.00 49.38  ?  629  LEU D CB  1 
ATOM   10914 C CG  . LEU D  1  629 ? -1.293  -37.274 -10.334 1.00 48.56  ?  629  LEU D CG  1 
ATOM   10915 C CD1 . LEU D  1  629 ? -1.027  -35.935 -9.664  1.00 46.59  ?  629  LEU D CD1 1 
ATOM   10916 C CD2 . LEU D  1  629 ? -0.043  -38.145 -10.314 1.00 51.17  ?  629  LEU D CD2 1 
ATOM   10917 N N   . SER D  1  630 ? -5.923  -37.962 -8.490  1.00 52.05  ?  630  SER D N   1 
ATOM   10918 C CA  . SER D  1  630 ? -7.079  -38.843 -8.482  1.00 53.33  ?  630  SER D CA  1 
ATOM   10919 C C   . SER D  1  630 ? -8.043  -38.501 -9.616  1.00 51.89  ?  630  SER D C   1 
ATOM   10920 O O   . SER D  1  630 ? -7.986  -37.425 -10.216 1.00 49.69  ?  630  SER D O   1 
ATOM   10921 C CB  . SER D  1  630 ? -7.804  -38.764 -7.136  1.00 53.71  ?  630  SER D CB  1 
ATOM   10922 O OG  . SER D  1  630 ? -8.343  -37.472 -6.912  1.00 51.27  ?  630  SER D OG  1 
ATOM   10923 N N   . HIS D  1  631 ? -8.938  -39.449 -9.901  1.00 56.67  ?  631  HIS D N   1 
ATOM   10924 C CA  . HIS D  1  631 ? -10.018 -39.274 -10.874 1.00 55.90  ?  631  HIS D CA  1 
ATOM   10925 C C   . HIS D  1  631 ? -9.478  -38.927 -12.265 1.00 54.53  ?  631  HIS D C   1 
ATOM   10926 O O   . HIS D  1  631 ? -9.729  -37.852 -12.814 1.00 52.42  ?  631  HIS D O   1 
ATOM   10927 C CB  . HIS D  1  631 ? -11.018 -38.223 -10.380 1.00 53.83  ?  631  HIS D CB  1 
ATOM   10928 C CG  . HIS D  1  631 ? -11.704 -38.604 -9.105  1.00 55.11  ?  631  HIS D CG  1 
ATOM   10929 N ND1 . HIS D  1  631 ? -11.213 -38.257 -7.865  1.00 55.08  ?  631  HIS D ND1 1 
ATOM   10930 C CD2 . HIS D  1  631 ? -12.837 -39.310 -8.877  1.00 56.88  ?  631  HIS D CD2 1 
ATOM   10931 C CE1 . HIS D  1  631 ? -12.015 -38.729 -6.928  1.00 56.55  ?  631  HIS D CE1 1 
ATOM   10932 N NE2 . HIS D  1  631 ? -13.009 -39.371 -7.515  1.00 57.54  ?  631  HIS D NE2 1 
ATOM   10933 N N   . ASN D  1  632 ? -8.717  -39.867 -12.824 1.00 57.05  ?  632  ASN D N   1 
ATOM   10934 C CA  . ASN D  1  632 ? -8.139  -39.718 -14.152 1.00 56.56  ?  632  ASN D CA  1 
ATOM   10935 C C   . ASN D  1  632 ? -8.049  -41.099 -14.797 1.00 59.02  ?  632  ASN D C   1 
ATOM   10936 O O   . ASN D  1  632 ? -8.515  -42.096 -14.238 1.00 60.97  ?  632  ASN D O   1 
ATOM   10937 C CB  . ASN D  1  632 ? -6.771  -39.035 -14.069 1.00 55.73  ?  632  ASN D CB  1 
ATOM   10938 C CG  . ASN D  1  632 ? -6.881  -37.533 -13.896 1.00 53.08  ?  632  ASN D CG  1 
ATOM   10939 O OD1 . ASN D  1  632 ? -7.044  -36.795 -14.866 1.00 51.63  ?  632  ASN D OD1 1 
ATOM   10940 N ND2 . ASN D  1  632 ? -6.803  -37.075 -12.652 1.00 52.58  ?  632  ASN D ND2 1 
ATOM   10941 N N   . ASN D  1  633 ? -7.444  -41.156 -15.988 1.00 64.58  ?  633  ASN D N   1 
ATOM   10942 C CA  . ASN D  1  633 ? -7.263  -42.401 -16.731 1.00 66.90  ?  633  ASN D CA  1 
ATOM   10943 C C   . ASN D  1  633 ? -5.790  -42.788 -16.815 1.00 68.24  ?  633  ASN D C   1 
ATOM   10944 O O   . ASN D  1  633 ? -5.343  -43.348 -17.818 1.00 69.47  ?  633  ASN D O   1 
ATOM   10945 C CB  . ASN D  1  633 ? -7.856  -42.284 -18.138 1.00 66.34  ?  633  ASN D CB  1 
ATOM   10946 C CG  . ASN D  1  633 ? -8.484  -43.591 -18.646 1.00 68.65  ?  633  ASN D CG  1 
ATOM   10947 O OD1 . ASN D  1  633 ? -8.826  -44.480 -17.867 1.00 70.41  ?  633  ASN D OD1 1 
ATOM   10948 N ND2 . ASN D  1  633 ? -8.637  -43.693 -19.975 1.00 68.76  ?  633  ASN D ND2 1 
ATOM   10949 N N   . LEU D  1  634 ? -5.026  -42.493 -15.765 1.00 65.57  ?  634  LEU D N   1 
ATOM   10950 C CA  . LEU D  1  634 ? -3.609  -42.827 -15.750 1.00 67.49  ?  634  LEU D CA  1 
ATOM   10951 C C   . LEU D  1  634 ? -3.414  -44.335 -15.671 1.00 70.42  ?  634  LEU D C   1 
ATOM   10952 O O   . LEU D  1  634 ? -4.075  -45.016 -14.882 1.00 71.58  ?  634  LEU D O   1 
ATOM   10953 C CB  . LEU D  1  634 ? -2.908  -42.145 -14.577 1.00 66.78  ?  634  LEU D CB  1 
ATOM   10954 C CG  . LEU D  1  634 ? -2.881  -40.616 -14.574 1.00 63.36  ?  634  LEU D CG  1 
ATOM   10955 C CD1 . LEU D  1  634 ? -3.319  -40.051 -13.230 1.00 62.31  ?  634  LEU D CD1 1 
ATOM   10956 C CD2 . LEU D  1  634 ? -1.491  -40.137 -14.929 1.00 63.35  ?  634  LEU D CD2 1 
ATOM   10957 N N   . SER D  1  635 ? -2.500  -44.853 -16.484 1.00 71.01  ?  635  SER D N   1 
ATOM   10958 C CA  . SER D  1  635 ? -2.167  -46.270 -16.507 1.00 74.33  ?  635  SER D CA  1 
ATOM   10959 C C   . SER D  1  635 ? -0.697  -46.453 -16.142 1.00 76.02  ?  635  SER D C   1 
ATOM   10960 O O   . SER D  1  635 ? 0.017   -45.495 -15.837 1.00 74.60  ?  635  SER D O   1 
ATOM   10961 C CB  . SER D  1  635 ? -2.469  -46.881 -17.878 1.00 75.19  ?  635  SER D CB  1 
ATOM   10962 O OG  . SER D  1  635 ? -1.475  -46.524 -18.823 1.00 75.06  ?  635  SER D OG  1 
ATOM   10963 N N   . GLY D  1  636 ? -0.246  -47.704 -16.180 1.00 77.09  ?  636  GLY D N   1 
ATOM   10964 C CA  . GLY D  1  636 ? 1.107   -48.021 -15.778 1.00 79.24  ?  636  GLY D CA  1 
ATOM   10965 C C   . GLY D  1  636 ? 1.240   -48.127 -14.272 1.00 80.13  ?  636  GLY D C   1 
ATOM   10966 O O   . GLY D  1  636 ? 0.283   -47.979 -13.510 1.00 79.13  ?  636  GLY D O   1 
ATOM   10967 N N   . GLN D  1  637 ? 2.467   -48.390 -13.837 1.00 81.68  ?  637  GLN D N   1 
ATOM   10968 C CA  . GLN D  1  637 ? 2.760   -48.522 -12.419 1.00 82.95  ?  637  GLN D CA  1 
ATOM   10969 C C   . GLN D  1  637 ? 3.251   -47.197 -11.853 1.00 80.55  ?  637  GLN D C   1 
ATOM   10970 O O   . GLN D  1  637 ? 3.892   -46.404 -12.547 1.00 79.11  ?  637  GLN D O   1 
ATOM   10971 C CB  . GLN D  1  637 ? 3.805   -49.614 -12.176 1.00 87.04  ?  637  GLN D CB  1 
ATOM   10972 C CG  . GLN D  1  637 ? 3.494   -50.937 -12.857 1.00 89.73  ?  637  GLN D CG  1 
ATOM   10973 C CD  . GLN D  1  637 ? 4.071   -52.127 -12.115 1.00 93.99  ?  637  GLN D CD  1 
ATOM   10974 O OE1 . GLN D  1  637 ? 4.747   -51.972 -11.098 1.00 95.04  ?  637  GLN D OE1 1 
ATOM   10975 N NE2 . GLN D  1  637 ? 3.807   -53.326 -12.624 1.00 96.64  ?  637  GLN D NE2 1 
ATOM   10976 N N   . ILE D  1  638 ? 2.924   -46.956 -10.586 1.00 81.08  ?  638  ILE D N   1 
ATOM   10977 C CA  . ILE D  1  638 ? 3.403   -45.765 -9.891  1.00 79.15  ?  638  ILE D CA  1 
ATOM   10978 C C   . ILE D  1  638 ? 4.924   -45.845 -9.880  1.00 81.19  ?  638  ILE D C   1 
ATOM   10979 O O   . ILE D  1  638 ? 5.482   -46.858 -9.432  1.00 84.62  ?  638  ILE D O   1 
ATOM   10980 C CB  . ILE D  1  638 ? 2.832   -45.664 -8.467  1.00 79.10  ?  638  ILE D CB  1 
ATOM   10981 C CG1 . ILE D  1  638 ? 1.343   -46.008 -8.460  1.00 78.36  ?  638  ILE D CG1 1 
ATOM   10982 C CG2 . ILE D  1  638 ? 3.043   -44.266 -7.908  1.00 76.38  ?  638  ILE D CG2 1 
ATOM   10983 C CD1 . ILE D  1  638 ? 0.779   -46.251 -7.076  1.00 79.34  ?  638  ILE D CD1 1 
ATOM   10984 N N   . PRO D  1  639 ? 5.625   -44.827 -10.373 1.00 81.35  ?  639  PRO D N   1 
ATOM   10985 C CA  . PRO D  1  639 ? 7.083   -44.923 -10.530 1.00 83.49  ?  639  PRO D CA  1 
ATOM   10986 C C   . PRO D  1  639 ? 7.765   -45.237 -9.212  1.00 85.91  ?  639  PRO D C   1 
ATOM   10987 O O   . PRO D  1  639 ? 7.601   -44.503 -8.226  1.00 84.49  ?  639  PRO D O   1 
ATOM   10988 C CB  . PRO D  1  639 ? 7.478   -43.530 -11.048 1.00 80.64  ?  639  PRO D CB  1 
ATOM   10989 C CG  . PRO D  1  639 ? 6.314   -42.646 -10.726 1.00 77.18  ?  639  PRO D CG  1 
ATOM   10990 C CD  . PRO D  1  639 ? 5.106   -43.521 -10.809 1.00 77.50  ?  639  PRO D CD  1 
ATOM   10991 N N   . PRO D  1  640 ? 8.534   -46.329 -9.155  1.00 84.24  ?  640  PRO D N   1 
ATOM   10992 C CA  . PRO D  1  640 ? 9.242   -46.672 -7.911  1.00 86.97  ?  640  PRO D CA  1 
ATOM   10993 C C   . PRO D  1  640 ? 10.241  -45.619 -7.459  1.00 86.27  ?  640  PRO D C   1 
ATOM   10994 O O   . PRO D  1  640 ? 10.761  -45.729 -6.342  1.00 88.17  ?  640  PRO D O   1 
ATOM   10995 C CB  . PRO D  1  640 ? 9.945   -47.990 -8.261  1.00 91.24  ?  640  PRO D CB  1 
ATOM   10996 C CG  . PRO D  1  640 ? 9.106   -48.579 -9.350  1.00 90.70  ?  640  PRO D CG  1 
ATOM   10997 C CD  . PRO D  1  640 ? 8.640   -47.400 -10.162 1.00 86.49  ?  640  PRO D CD  1 
ATOM   10998 N N   . SER D  1  641 ? 10.530  -44.611 -8.281  1.00 90.97  ?  641  SER D N   1 
ATOM   10999 C CA  . SER D  1  641 ? 11.417  -43.526 -7.881  1.00 90.34  ?  641  SER D CA  1 
ATOM   11000 C C   . SER D  1  641 ? 10.812  -42.622 -6.813  1.00 87.97  ?  641  SER D C   1 
ATOM   11001 O O   . SER D  1  641 ? 11.467  -41.654 -6.411  1.00 86.76  ?  641  SER D O   1 
ATOM   11002 C CB  . SER D  1  641 ? 11.803  -42.691 -9.104  1.00 88.36  ?  641  SER D CB  1 
ATOM   11003 O OG  . SER D  1  641 ? 12.780  -41.721 -8.771  1.00 87.88  ?  641  SER D OG  1 
ATOM   11004 N N   . PHE D  1  642 ? 9.596   -42.902 -6.349  1.00 89.68  ?  642  PHE D N   1 
ATOM   11005 C CA  . PHE D  1  642 ? 8.925   -42.059 -5.368  1.00 87.21  ?  642  PHE D CA  1 
ATOM   11006 C C   . PHE D  1  642 ? 9.306   -42.387 -3.929  1.00 89.79  ?  642  PHE D C   1 
ATOM   11007 O O   . PHE D  1  642 ? 8.835   -41.704 -3.013  1.00 87.76  ?  642  PHE D O   1 
ATOM   11008 C CB  . PHE D  1  642 ? 7.404   -42.156 -5.534  1.00 85.45  ?  642  PHE D CB  1 
ATOM   11009 C CG  . PHE D  1  642 ? 6.860   -41.324 -6.665  1.00 82.37  ?  642  PHE D CG  1 
ATOM   11010 C CD1 . PHE D  1  642 ? 7.713   -40.722 -7.578  1.00 81.67  ?  642  PHE D CD1 1 
ATOM   11011 C CD2 . PHE D  1  642 ? 5.496   -41.128 -6.804  1.00 79.37  ?  642  PHE D CD2 1 
ATOM   11012 C CE1 . PHE D  1  642 ? 7.214   -39.952 -8.614  1.00 78.20  ?  642  PHE D CE1 1 
ATOM   11013 C CE2 . PHE D  1  642 ? 4.992   -40.359 -7.837  1.00 76.29  ?  642  PHE D CE2 1 
ATOM   11014 C CZ  . PHE D  1  642 ? 5.852   -39.769 -8.742  1.00 75.69  ?  642  PHE D CZ  1 
ATOM   11015 N N   . LYS D  1  643 ? 10.137  -43.410 -3.700  1.00 87.49  ?  643  LYS D N   1 
ATOM   11016 C CA  . LYS D  1  643 ? 10.633  -43.659 -2.349  1.00 90.05  ?  643  LYS D CA  1 
ATOM   11017 C C   . LYS D  1  643 ? 11.438  -42.478 -1.823  1.00 88.98  ?  643  LYS D C   1 
ATOM   11018 O O   . LYS D  1  643 ? 11.536  -42.287 -0.605  1.00 89.79  ?  643  LYS D O   1 
ATOM   11019 C CB  . LYS D  1  643 ? 11.503  -44.918 -2.307  1.00 94.72  ?  643  LYS D CB  1 
ATOM   11020 C CG  . LYS D  1  643 ? 10.766  -46.246 -2.180  1.00 97.02  ?  643  LYS D CG  1 
ATOM   11021 C CD  . LYS D  1  643 ? 10.678  -46.979 -3.507  1.00 97.58  ?  643  LYS D CD  1 
ATOM   11022 C CE  . LYS D  1  643 ? 9.459   -47.882 -3.562  1.00 97.92  ?  643  LYS D CE  1 
ATOM   11023 N NZ  . LYS D  1  643 ? 8.904   -47.997 -4.937  1.00 96.14  ?  643  LYS D NZ  1 
ATOM   11024 N N   . ASP D  1  644 ? 12.015  -41.679 -2.717  1.00 90.27  ?  644  ASP D N   1 
ATOM   11025 C CA  . ASP D  1  644 ? 12.938  -40.613 -2.357  1.00 89.90  ?  644  ASP D CA  1 
ATOM   11026 C C   . ASP D  1  644 ? 12.244  -39.282 -2.085  1.00 86.33  ?  644  ASP D C   1 
ATOM   11027 O O   . ASP D  1  644 ? 12.924  -38.257 -1.974  1.00 85.26  ?  644  ASP D O   1 
ATOM   11028 C CB  . ASP D  1  644 ? 13.981  -40.437 -3.462  1.00 90.30  ?  644  ASP D CB  1 
ATOM   11029 C CG  . ASP D  1  644 ? 14.584  -41.756 -3.906  1.00 94.20  ?  644  ASP D CG  1 
ATOM   11030 O OD1 . ASP D  1  644 ? 14.609  -42.703 -3.092  1.00 97.14  ?  644  ASP D OD1 1 
ATOM   11031 O OD2 . ASP D  1  644 ? 15.031  -41.847 -5.069  1.00 94.50  -1 644  ASP D OD2 1 
ATOM   11032 N N   . MET D  1  645 ? 10.916  -39.269 -1.978  1.00 87.34  ?  645  MET D N   1 
ATOM   11033 C CA  . MET D  1  645 ? 10.176  -38.033 -1.727  1.00 83.36  ?  645  MET D CA  1 
ATOM   11034 C C   . MET D  1  645 ? 10.032  -37.859 -0.221  1.00 83.97  ?  645  MET D C   1 
ATOM   11035 O O   . MET D  1  645 ? 9.073   -38.326 0.395   1.00 84.21  ?  645  MET D O   1 
ATOM   11036 C CB  . MET D  1  645 ? 8.822   -38.062 -2.425  1.00 80.75  ?  645  MET D CB  1 
ATOM   11037 C CG  . MET D  1  645 ? 8.898   -38.425 -3.895  1.00 80.91  ?  645  MET D CG  1 
ATOM   11038 S SD  . MET D  1  645 ? 7.743   -37.475 -4.897  1.00 76.56  ?  645  MET D SD  1 
ATOM   11039 C CE  . MET D  1  645 ? 8.585   -37.502 -6.473  1.00 76.42  ?  645  MET D CE  1 
ATOM   11040 N N   . LEU D  1  646 ? 11.002  -37.167 0.378   1.00 79.52  ?  646  LEU D N   1 
ATOM   11041 C CA  . LEU D  1  646 ? 10.995  -36.952 1.820   1.00 80.37  ?  646  LEU D CA  1 
ATOM   11042 C C   . LEU D  1  646 ? 10.000  -35.876 2.235   1.00 76.89  ?  646  LEU D C   1 
ATOM   11043 O O   . LEU D  1  646 ? 9.423   -35.959 3.325   1.00 77.27  ?  646  LEU D O   1 
ATOM   11044 C CB  . LEU D  1  646 ? 12.399  -36.581 2.301   1.00 82.37  ?  646  LEU D CB  1 
ATOM   11045 C CG  . LEU D  1  646 ? 13.516  -37.569 1.960   1.00 86.19  ?  646  LEU D CG  1 
ATOM   11046 C CD1 . LEU D  1  646 ? 14.467  -36.978 0.929   1.00 85.69  ?  646  LEU D CD1 1 
ATOM   11047 C CD2 . LEU D  1  646 ? 14.270  -37.979 3.216   1.00 89.77  ?  646  LEU D CD2 1 
ATOM   11048 N N   . ALA D  1  647 ? 9.791   -34.865 1.391   1.00 74.52  ?  647  ALA D N   1 
ATOM   11049 C CA  . ALA D  1  647 ? 8.872   -33.782 1.722   1.00 71.30  ?  647  ALA D CA  1 
ATOM   11050 C C   . ALA D  1  647 ? 7.412   -34.197 1.606   1.00 70.00  ?  647  ALA D C   1 
ATOM   11051 O O   . ALA D  1  647 ? 6.555   -33.590 2.257   1.00 68.29  ?  647  ALA D O   1 
ATOM   11052 C CB  . ALA D  1  647 ? 9.140   -32.576 0.820   1.00 68.59  ?  647  ALA D CB  1 
ATOM   11053 N N   . LEU D  1  648 ? 7.114   -35.209 0.798   1.00 70.33  ?  648  LEU D N   1 
ATOM   11054 C CA  . LEU D  1  648 ? 5.736   -35.529 0.460   1.00 69.08  ?  648  LEU D CA  1 
ATOM   11055 C C   . LEU D  1  648 ? 5.002   -36.070 1.684   1.00 70.29  ?  648  LEU D C   1 
ATOM   11056 O O   . LEU D  1  648 ? 5.526   -36.906 2.423   1.00 73.39  ?  648  LEU D O   1 
ATOM   11057 C CB  . LEU D  1  648 ? 5.713   -36.551 -0.679  1.00 70.27  ?  648  LEU D CB  1 
ATOM   11058 C CG  . LEU D  1  648 ? 4.518   -36.635 -1.634  1.00 68.02  ?  648  LEU D CG  1 
ATOM   11059 C CD1 . LEU D  1  648 ? 4.786   -37.667 -2.725  1.00 69.61  ?  648  LEU D CD1 1 
ATOM   11060 C CD2 . LEU D  1  648 ? 3.216   -36.935 -0.928  1.00 68.03  ?  648  LEU D CD2 1 
ATOM   11061 N N   . THR D  1  649 ? 3.778   -35.581 1.898   1.00 67.31  ?  649  THR D N   1 
ATOM   11062 C CA  . THR D  1  649 ? 2.968   -35.976 3.043   1.00 68.42  ?  649  THR D CA  1 
ATOM   11063 C C   . THR D  1  649 ? 1.591   -36.515 2.684   1.00 67.88  ?  649  THR D C   1 
ATOM   11064 O O   . THR D  1  649 ? 1.076   -37.368 3.411   1.00 70.00  ?  649  THR D O   1 
ATOM   11065 C CB  . THR D  1  649 ? 2.785   -34.793 4.007   1.00 66.82  ?  649  THR D CB  1 
ATOM   11066 O OG1 . THR D  1  649 ? 2.091   -33.733 3.337   1.00 63.36  ?  649  THR D OG1 1 
ATOM   11067 C CG2 . THR D  1  649 ? 4.128   -34.289 4.493   1.00 67.68  ?  649  THR D CG2 1 
ATOM   11068 N N   . HIS D  1  650 ? 0.978   -36.050 1.597   1.00 66.21  ?  650  HIS D N   1 
ATOM   11069 C CA  . HIS D  1  650 ? -0.361  -36.482 1.216   1.00 65.65  ?  650  HIS D CA  1 
ATOM   11070 C C   . HIS D  1  650 ? -0.351  -36.974 -0.223  1.00 65.35  ?  650  HIS D C   1 
ATOM   11071 O O   . HIS D  1  650 ? 0.140   -36.278 -1.116  1.00 63.56  ?  650  HIS D O   1 
ATOM   11072 C CB  . HIS D  1  650 ? -1.381  -35.346 1.367   1.00 62.79  ?  650  HIS D CB  1 
ATOM   11073 C CG  . HIS D  1  650 ? -1.580  -34.889 2.778   1.00 63.20  ?  650  HIS D CG  1 
ATOM   11074 N ND1 . HIS D  1  650 ? -0.565  -34.352 3.539   1.00 63.53  ?  650  HIS D ND1 1 
ATOM   11075 C CD2 . HIS D  1  650 ? -2.681  -34.889 3.567   1.00 63.80  ?  650  HIS D CD2 1 
ATOM   11076 C CE1 . HIS D  1  650 ? -1.030  -34.043 4.736   1.00 63.86  ?  650  HIS D CE1 1 
ATOM   11077 N NE2 . HIS D  1  650 ? -2.312  -34.358 4.779   1.00 64.03  ?  650  HIS D NE2 1 
ATOM   11078 N N   . VAL D  1  651 ? -0.915  -38.159 -0.445  1.00 65.55  ?  651  VAL D N   1 
ATOM   11079 C CA  . VAL D  1  651 ? -1.064  -38.728 -1.778  1.00 65.47  ?  651  VAL D CA  1 
ATOM   11080 C C   . VAL D  1  651 ? -2.521  -39.112 -1.973  1.00 65.30  ?  651  VAL D C   1 
ATOM   11081 O O   . VAL D  1  651 ? -3.169  -39.609 -1.046  1.00 66.99  ?  651  VAL D O   1 
ATOM   11082 C CB  . VAL D  1  651 ? -0.164  -39.966 -1.992  1.00 68.63  ?  651  VAL D CB  1 
ATOM   11083 C CG1 . VAL D  1  651 ? -0.236  -40.424 -3.435  1.00 68.77  ?  651  VAL D CG1 1 
ATOM   11084 C CG2 . VAL D  1  651 ? 1.265   -39.683 -1.595  1.00 69.59  ?  651  VAL D CG2 1 
ATOM   11085 N N   . ASP D  1  652 ? -3.040  -38.878 -3.175  1.00 61.41  ?  652  ASP D N   1 
ATOM   11086 C CA  . ASP D  1  652 ? -4.334  -39.423 -3.575  1.00 61.53  ?  652  ASP D CA  1 
ATOM   11087 C C   . ASP D  1  652 ? -4.246  -39.795 -5.047  1.00 61.26  ?  652  ASP D C   1 
ATOM   11088 O O   . ASP D  1  652 ? -4.149  -38.913 -5.906  1.00 58.94  ?  652  ASP D O   1 
ATOM   11089 C CB  . ASP D  1  652 ? -5.468  -38.430 -3.322  1.00 59.18  ?  652  ASP D CB  1 
ATOM   11090 C CG  . ASP D  1  652 ? -6.803  -39.116 -3.110  1.00 60.28  ?  652  ASP D CG  1 
ATOM   11091 O OD1 . ASP D  1  652 ? -7.006  -40.210 -3.679  1.00 62.04  ?  652  ASP D OD1 1 
ATOM   11092 O OD2 . ASP D  1  652 ? -7.648  -38.564 -2.376  1.00 59.52  -1 652  ASP D OD2 1 
ATOM   11093 N N   . VAL D  1  653 ? -4.266  -41.094 -5.335  1.00 58.12  ?  653  VAL D N   1 
ATOM   11094 C CA  . VAL D  1  653 ? -4.247  -41.604 -6.698  1.00 58.29  ?  653  VAL D CA  1 
ATOM   11095 C C   . VAL D  1  653 ? -5.463  -42.499 -6.953  1.00 59.46  ?  653  VAL D C   1 
ATOM   11096 O O   . VAL D  1  653 ? -5.475  -43.305 -7.876  1.00 60.62  ?  653  VAL D O   1 
ATOM   11097 C CB  . VAL D  1  653 ? -2.918  -42.333 -6.992  1.00 60.45  ?  653  VAL D CB  1 
ATOM   11098 C CG1 . VAL D  1  653 ? -2.732  -42.566 -8.480  1.00 60.16  ?  653  VAL D CG1 1 
ATOM   11099 C CG2 . VAL D  1  653 ? -1.738  -41.554 -6.437  1.00 59.92  ?  653  VAL D CG2 1 
ATOM   11100 N N   . SER D  1  654 ? -6.491  -42.358 -6.121  1.00 63.47  ?  654  SER D N   1 
ATOM   11101 C CA  . SER D  1  654 ? -7.678  -43.192 -6.225  1.00 64.84  ?  654  SER D CA  1 
ATOM   11102 C C   . SER D  1  654 ? -8.412  -42.941 -7.540  1.00 63.20  ?  654  SER D C   1 
ATOM   11103 O O   . SER D  1  654 ? -8.246  -41.905 -8.191  1.00 60.63  ?  654  SER D O   1 
ATOM   11104 C CB  . SER D  1  654 ? -8.617  -42.928 -5.049  1.00 64.92  ?  654  SER D CB  1 
ATOM   11105 O OG  . SER D  1  654 ? -9.009  -41.566 -5.000  1.00 61.92  ?  654  SER D OG  1 
ATOM   11106 N N   . HIS D  1  655 ? -9.235  -43.919 -7.924  1.00 67.79  ?  655  HIS D N   1 
ATOM   11107 C CA  . HIS D  1  655 ? -10.091 -43.830 -9.107  1.00 66.88  ?  655  HIS D CA  1 
ATOM   11108 C C   . HIS D  1  655 ? -9.268  -43.578 -10.373 1.00 65.83  ?  655  HIS D C   1 
ATOM   11109 O O   . HIS D  1  655 ? -9.394  -42.551 -11.043 1.00 63.18  ?  655  HIS D O   1 
ATOM   11110 C CB  . HIS D  1  655 ? -11.168 -42.758 -8.911  1.00 64.49  ?  655  HIS D CB  1 
ATOM   11111 C CG  . HIS D  1  655 ? -12.088 -43.039 -7.765  1.00 65.81  ?  655  HIS D CG  1 
ATOM   11112 N ND1 . HIS D  1  655 ? -13.256 -43.757 -7.906  1.00 67.81  ?  655  HIS D ND1 1 
ATOM   11113 C CD2 . HIS D  1  655 ? -12.004 -42.712 -6.453  1.00 66.00  ?  655  HIS D CD2 1 
ATOM   11114 C CE1 . HIS D  1  655 ? -13.856 -43.854 -6.733  1.00 68.70  ?  655  HIS D CE1 1 
ATOM   11115 N NE2 . HIS D  1  655 ? -13.117 -43.228 -5.835  1.00 67.68  ?  655  HIS D NE2 1 
ATOM   11116 N N   . ASN D  1  656 ? -8.405  -44.542 -10.679 1.00 68.46  ?  656  ASN D N   1 
ATOM   11117 C CA  . ASN D  1  656 ? -7.495  -44.453 -11.813 1.00 67.91  ?  656  ASN D CA  1 
ATOM   11118 C C   . ASN D  1  656 ? -7.378  -45.839 -12.442 1.00 70.71  ?  656  ASN D C   1 
ATOM   11119 O O   . ASN D  1  656 ? -8.169  -46.742 -12.155 1.00 73.42  ?  656  ASN D O   1 
ATOM   11120 C CB  . ASN D  1  656 ? -6.140  -43.887 -11.373 1.00 67.48  ?  656  ASN D CB  1 
ATOM   11121 C CG  . ASN D  1  656 ? -5.973  -42.433 -11.751 1.00 64.51  ?  656  ASN D CG  1 
ATOM   11122 O OD1 . ASN D  1  656 ? -5.666  -42.111 -12.897 1.00 63.36  ?  656  ASN D OD1 1 
ATOM   11123 N ND2 . ASN D  1  656 ? -6.173  -41.544 -10.786 1.00 62.73  ?  656  ASN D ND2 1 
ATOM   11124 N N   . ASN D  1  657 ? -6.402  -46.006 -13.331 1.00 75.25  ?  657  ASN D N   1 
ATOM   11125 C CA  . ASN D  1  657 ? -6.202  -47.255 -14.060 1.00 78.37  ?  657  ASN D CA  1 
ATOM   11126 C C   . ASN D  1  657 ? -4.769  -47.746 -13.896 1.00 80.23  ?  657  ASN D C   1 
ATOM   11127 O O   . ASN D  1  657 ? -4.139  -48.219 -14.847 1.00 81.14  ?  657  ASN D O   1 
ATOM   11128 C CB  . ASN D  1  657 ? -6.554  -47.083 -15.537 1.00 76.81  ?  657  ASN D CB  1 
ATOM   11129 C CG  . ASN D  1  657 ? -6.755  -48.407 -16.251 1.00 79.56  ?  657  ASN D CG  1 
ATOM   11130 O OD1 . ASN D  1  657 ? -7.355  -49.333 -15.707 1.00 82.15  ?  657  ASN D OD1 1 
ATOM   11131 N ND2 . ASN D  1  657 ? -6.253  -48.500 -17.478 1.00 80.00  ?  657  ASN D ND2 1 
ATOM   11132 N N   . LEU D  1  658 ? -4.232  -47.642 -12.683 1.00 79.06  ?  658  LEU D N   1 
ATOM   11133 C CA  . LEU D  1  658 ? -2.842  -47.982 -12.431 1.00 80.72  ?  658  LEU D CA  1 
ATOM   11134 C C   . LEU D  1  658 ? -2.702  -49.437 -11.992 1.00 85.01  ?  658  LEU D C   1 
ATOM   11135 O O   . LEU D  1  658 ? -3.682  -50.168 -11.825 1.00 86.45  ?  658  LEU D O   1 
ATOM   11136 C CB  . LEU D  1  658 ? -2.243  -47.059 -11.372 1.00 79.35  ?  658  LEU D CB  1 
ATOM   11137 C CG  . LEU D  1  658 ? -2.135  -45.567 -11.668 1.00 76.08  ?  658  LEU D CG  1 
ATOM   11138 C CD1 . LEU D  1  658 ? -1.329  -44.916 -10.577 1.00 75.55  ?  658  LEU D CD1 1 
ATOM   11139 C CD2 . LEU D  1  658 ? -1.480  -45.329 -13.006 1.00 75.68  ?  658  LEU D CD2 1 
ATOM   11140 N N   . GLN D  1  659 ? -1.455  -49.859 -11.798 1.00 81.64  ?  659  GLN D N   1 
ATOM   11141 C CA  . GLN D  1  659 ? -1.148  -51.215 -11.373 1.00 85.63  ?  659  GLN D CA  1 
ATOM   11142 C C   . GLN D  1  659 ? 0.179   -51.211 -10.626 1.00 87.28  ?  659  GLN D C   1 
ATOM   11143 O O   . GLN D  1  659 ? 0.916   -50.224 -10.635 1.00 85.42  ?  659  GLN D O   1 
ATOM   11144 C CB  . GLN D  1  659 ? -1.108  -52.178 -12.564 1.00 87.51  ?  659  GLN D CB  1 
ATOM   11145 C CG  . GLN D  1  659 ? -0.015  -51.871 -13.572 1.00 87.17  ?  659  GLN D CG  1 
ATOM   11146 C CD  . GLN D  1  659 ? -0.247  -52.555 -14.904 1.00 88.12  ?  659  GLN D CD  1 
ATOM   11147 O OE1 . GLN D  1  659 ? -1.354  -52.532 -15.442 1.00 86.83  ?  659  GLN D OE1 1 
ATOM   11148 N NE2 . GLN D  1  659 ? 0.799   -53.170 -15.444 1.00 90.55  ?  659  GLN D NE2 1 
ATOM   11149 N N   . GLY D  1  660 ? 0.465   -52.321 -9.949  1.00 91.19  ?  660  GLY D N   1 
ATOM   11150 C CA  . GLY D  1  660 ? 1.764   -52.523 -9.351  1.00 93.51  ?  660  GLY D CA  1 
ATOM   11151 C C   . GLY D  1  660 ? 1.833   -52.161 -7.881  1.00 93.71  ?  660  GLY D C   1 
ATOM   11152 O O   . GLY D  1  660 ? 0.916   -51.555 -7.317  1.00 91.54  ?  660  GLY D O   1 
ATOM   11153 N N   . PRO D  1  661 ? 2.935   -52.536 -7.230  1.00 94.33  ?  661  PRO D N   1 
ATOM   11154 C CA  . PRO D  1  661 ? 3.099   -52.214 -5.808  1.00 94.85  ?  661  PRO D CA  1 
ATOM   11155 C C   . PRO D  1  661 ? 3.334   -50.728 -5.592  1.00 91.17  ?  661  PRO D C   1 
ATOM   11156 O O   . PRO D  1  661 ? 4.036   -50.070 -6.364  1.00 89.55  ?  661  PRO D O   1 
ATOM   11157 C CB  . PRO D  1  661 ? 4.324   -53.040 -5.398  1.00 99.09  ?  661  PRO D CB  1 
ATOM   11158 C CG  . PRO D  1  661 ? 5.099   -53.203 -6.665  1.00 99.41  ?  661  PRO D CG  1 
ATOM   11159 C CD  . PRO D  1  661 ? 4.075   -53.304 -7.762  1.00 97.45  ?  661  PRO D CD  1 
ATOM   11160 N N   . ILE D  1  662 ? 2.738   -50.203 -4.526  1.00 91.72  ?  662  ILE D N   1 
ATOM   11161 C CA  . ILE D  1  662 ? 2.832   -48.783 -4.193  1.00 88.30  ?  662  ILE D CA  1 
ATOM   11162 C C   . ILE D  1  662 ? 4.254   -48.443 -3.756  1.00 89.46  ?  662  ILE D C   1 
ATOM   11163 O O   . ILE D  1  662 ? 4.948   -49.294 -3.180  1.00 93.17  ?  662  ILE D O   1 
ATOM   11164 C CB  . ILE D  1  662 ? 1.792   -48.393 -3.126  1.00 87.16  ?  662  ILE D CB  1 
ATOM   11165 C CG1 . ILE D  1  662 ? 1.832   -49.332 -1.910  1.00 90.97  ?  662  ILE D CG1 1 
ATOM   11166 C CG2 . ILE D  1  662 ? 0.395   -48.372 -3.732  1.00 85.16  ?  662  ILE D CG2 1 
ATOM   11167 C CD1 . ILE D  1  662 ? 2.870   -48.990 -0.852  1.00 92.28  ?  662  ILE D CD1 1 
ATOM   11168 N N   . PRO D  1  663 ? 4.735   -47.234 -4.034  1.00 87.97  ?  663  PRO D N   1 
ATOM   11169 C CA  . PRO D  1  663 ? 6.048   -46.825 -3.526  1.00 89.06  ?  663  PRO D CA  1 
ATOM   11170 C C   . PRO D  1  663 ? 6.041   -46.698 -2.010  1.00 90.14  ?  663  PRO D C   1 
ATOM   11171 O O   . PRO D  1  663 ? 5.005   -46.487 -1.377  1.00 88.88  ?  663  PRO D O   1 
ATOM   11172 C CB  . PRO D  1  663 ? 6.290   -45.467 -4.194  1.00 85.34  ?  663  PRO D CB  1 
ATOM   11173 C CG  . PRO D  1  663 ? 5.384   -45.448 -5.376  1.00 83.15  ?  663  PRO D CG  1 
ATOM   11174 C CD  . PRO D  1  663 ? 4.186   -46.267 -4.998  1.00 84.00  ?  663  PRO D CD  1 
ATOM   11175 N N   . ASP D  1  664 ? 7.229   -46.840 -1.428  1.00 89.55  ?  664  ASP D N   1 
ATOM   11176 C CA  . ASP D  1  664 ? 7.402   -46.852 0.023   1.00 91.35  ?  664  ASP D CA  1 
ATOM   11177 C C   . ASP D  1  664 ? 7.939   -45.495 0.467   1.00 89.01  ?  664  ASP D C   1 
ATOM   11178 O O   . ASP D  1  664 ? 9.127   -45.202 0.311   1.00 89.86  ?  664  ASP D O   1 
ATOM   11179 C CB  . ASP D  1  664 ? 8.337   -47.982 0.443   1.00 96.26  ?  664  ASP D CB  1 
ATOM   11180 C CG  . ASP D  1  664 ? 8.533   -48.053 1.947   1.00 98.52  ?  664  ASP D CG  1 
ATOM   11181 O OD1 . ASP D  1  664 ? 7.717   -47.466 2.688   1.00 96.58  ?  664  ASP D OD1 1 
ATOM   11182 O OD2 . ASP D  1  664 ? 9.511   -48.693 2.389   1.00 102.40 -1 664  ASP D OD2 1 
ATOM   11183 N N   . ASN D  1  665 ? 7.057   -44.669 1.023   1.00 94.15  ?  665  ASN D N   1 
ATOM   11184 C CA  . ASN D  1  665 ? 7.457   -43.440 1.693   1.00 92.26  ?  665  ASN D CA  1 
ATOM   11185 C C   . ASN D  1  665 ? 6.481   -43.187 2.836   1.00 91.40  ?  665  ASN D C   1 
ATOM   11186 O O   . ASN D  1  665 ? 5.515   -43.931 3.029   1.00 92.26  ?  665  ASN D O   1 
ATOM   11187 C CB  . ASN D  1  665 ? 7.527   -42.260 0.714   1.00 88.19  ?  665  ASN D CB  1 
ATOM   11188 C CG  . ASN D  1  665 ? 6.241   -42.058 -0.065  1.00 85.38  ?  665  ASN D CG  1 
ATOM   11189 O OD1 . ASN D  1  665 ? 5.143   -42.265 0.451   1.00 85.18  ?  665  ASN D OD1 1 
ATOM   11190 N ND2 . ASN D  1  665 ? 6.373   -41.647 -1.321  1.00 83.72  ?  665  ASN D ND2 1 
ATOM   11191 N N   . ALA D  1  666 ? 6.743   -42.123 3.599   1.00 90.34  ?  666  ALA D N   1 
ATOM   11192 C CA  . ALA D  1  666 ? 5.904   -41.817 4.754   1.00 90.06  ?  666  ALA D CA  1 
ATOM   11193 C C   . ALA D  1  666 ? 4.462   -41.545 4.341   1.00 87.39  ?  666  ALA D C   1 
ATOM   11194 O O   . ALA D  1  666 ? 3.524   -41.901 5.064   1.00 87.85  ?  666  ALA D O   1 
ATOM   11195 C CB  . ALA D  1  666 ? 6.477   -40.623 5.516   1.00 88.64  ?  666  ALA D CB  1 
ATOM   11196 N N   . ALA D  1  667 ? 4.264   -40.918 3.180   1.00 83.99  ?  667  ALA D N   1 
ATOM   11197 C CA  . ALA D  1  667 ? 2.914   -40.561 2.755   1.00 81.04  ?  667  ALA D CA  1 
ATOM   11198 C C   . ALA D  1  667 ? 2.126   -41.790 2.317   1.00 82.72  ?  667  ALA D C   1 
ATOM   11199 O O   . ALA D  1  667 ? 0.958   -41.954 2.688   1.00 82.38  ?  667  ALA D O   1 
ATOM   11200 C CB  . ALA D  1  667 ? 2.977   -39.529 1.630   1.00 77.53  ?  667  ALA D CB  1 
ATOM   11201 N N   . PHE D  1  668 ? 2.746   -42.664 1.520   1.00 80.97  ?  668  PHE D N   1 
ATOM   11202 C CA  . PHE D  1  668 ? 2.058   -43.872 1.074   1.00 82.75  ?  668  PHE D CA  1 
ATOM   11203 C C   . PHE D  1  668 ? 1.793   -44.829 2.228   1.00 86.22  ?  668  PHE D C   1 
ATOM   11204 O O   . PHE D  1  668 ? 0.774   -45.529 2.230   1.00 87.07  ?  668  PHE D O   1 
ATOM   11205 C CB  . PHE D  1  668 ? 2.873   -44.571 -0.014  1.00 84.17  ?  668  PHE D CB  1 
ATOM   11206 C CG  . PHE D  1  668 ? 2.694   -43.980 -1.384  1.00 81.14  ?  668  PHE D CG  1 
ATOM   11207 C CD1 . PHE D  1  668 ? 1.468   -44.036 -2.021  1.00 79.43  ?  668  PHE D CD1 1 
ATOM   11208 C CD2 . PHE D  1  668 ? 3.754   -43.371 -2.035  1.00 80.21  ?  668  PHE D CD2 1 
ATOM   11209 C CE1 . PHE D  1  668 ? 1.302   -43.498 -3.282  1.00 76.85  ?  668  PHE D CE1 1 
ATOM   11210 C CE2 . PHE D  1  668 ? 3.594   -42.827 -3.294  1.00 77.63  ?  668  PHE D CE2 1 
ATOM   11211 C CZ  . PHE D  1  668 ? 2.366   -42.890 -3.919  1.00 75.94  ?  668  PHE D CZ  1 
ATOM   11212 N N   . ARG D  1  669 ? 2.697   -44.878 3.209   1.00 85.04  ?  669  ARG D N   1 
ATOM   11213 C CA  . ARG D  1  669 ? 2.491   -45.734 4.374   1.00 88.57  ?  669  ARG D CA  1 
ATOM   11214 C C   . ARG D  1  669 ? 1.265   -45.295 5.167   1.00 87.25  ?  669  ARG D C   1 
ATOM   11215 O O   . ARG D  1  669 ? 0.392   -46.110 5.486   1.00 89.08  ?  669  ARG D O   1 
ATOM   11216 C CB  . ARG D  1  669 ? 3.742   -45.726 5.252   1.00 91.07  ?  669  ARG D CB  1 
ATOM   11217 C CG  . ARG D  1  669 ? 4.850   -46.641 4.751   1.00 94.19  ?  669  ARG D CG  1 
ATOM   11218 C CD  . ARG D  1  669 ? 5.906   -46.882 5.817   1.00 97.65  ?  669  ARG D CD  1 
ATOM   11219 N NE  . ARG D  1  669 ? 6.728   -45.700 6.049   1.00 95.79  ?  669  ARG D NE  1 
ATOM   11220 C CZ  . ARG D  1  669 ? 6.575   -44.868 7.070   1.00 94.75  ?  669  ARG D CZ  1 
ATOM   11221 N NH1 . ARG D  1  669 ? 5.636   -45.058 7.983   1.00 95.38  ?  669  ARG D NH1 1 
ATOM   11222 N NH2 . ARG D  1  669 ? 7.384   -43.818 7.177   1.00 93.17  ?  669  ARG D NH2 1 
ATOM   11223 N N   . ASN D  1  670 ? 1.184   -44.006 5.492   1.00 89.98  ?  670  ASN D N   1 
ATOM   11224 C CA  . ASN D  1  670 ? 0.075   -43.469 6.270   1.00 88.91  ?  670  ASN D CA  1 
ATOM   11225 C C   . ASN D  1  670 ? -1.149  -43.147 5.424   1.00 86.10  ?  670  ASN D C   1 
ATOM   11226 O O   . ASN D  1  670 ? -2.133  -42.630 5.963   1.00 84.67  ?  670  ASN D O   1 
ATOM   11227 C CB  . ASN D  1  670 ? 0.521   -42.210 7.019   1.00 86.90  ?  670  ASN D CB  1 
ATOM   11228 C CG  . ASN D  1  670 ? 1.049   -42.515 8.407   1.00 90.11  ?  670  ASN D CG  1 
ATOM   11229 O OD1 . ASN D  1  670 ? 2.256   -42.476 8.647   1.00 91.58  ?  670  ASN D OD1 1 
ATOM   11230 N ND2 . ASN D  1  670 ? 0.144   -42.819 9.330   1.00 91.51  ?  670  ASN D ND2 1 
ATOM   11231 N N   . ALA D  1  671 ? -1.114  -43.428 4.128   1.00 83.33  ?  671  ALA D N   1 
ATOM   11232 C CA  . ALA D  1  671 ? -2.251  -43.122 3.269   1.00 80.72  ?  671  ALA D CA  1 
ATOM   11233 C C   . ALA D  1  671 ? -3.442  -43.999 3.643   1.00 82.65  ?  671  ALA D C   1 
ATOM   11234 O O   . ALA D  1  671 ? -3.285  -45.215 3.808   1.00 86.54  ?  671  ALA D O   1 
ATOM   11235 C CB  . ALA D  1  671 ? -1.883  -43.325 1.803   1.00 79.73  ?  671  ALA D CB  1 
ATOM   11236 N N   . PRO D  1  672 ? -4.634  -43.429 3.788   1.00 78.64  ?  672  PRO D N   1 
ATOM   11237 C CA  . PRO D  1  672 ? -5.818  -44.234 4.111   1.00 80.54  ?  672  PRO D CA  1 
ATOM   11238 C C   . PRO D  1  672 ? -6.214  -45.118 2.942   1.00 81.13  ?  672  PRO D C   1 
ATOM   11239 O O   . PRO D  1  672 ? -5.777  -44.888 1.804   1.00 79.33  ?  672  PRO D O   1 
ATOM   11240 C CB  . PRO D  1  672 ? -6.892  -43.175 4.407   1.00 77.92  ?  672  PRO D CB  1 
ATOM   11241 C CG  . PRO D  1  672 ? -6.428  -41.952 3.693   1.00 74.22  ?  672  PRO D CG  1 
ATOM   11242 C CD  . PRO D  1  672 ? -4.933  -41.988 3.734   1.00 74.93  ?  672  PRO D CD  1 
ATOM   11243 N N   . PRO D  1  673 ? -7.034  -46.147 3.183   1.00 79.47  ?  673  PRO D N   1 
ATOM   11244 C CA  . PRO D  1  673 ? -7.383  -47.078 2.094   1.00 80.40  ?  673  PRO D CA  1 
ATOM   11245 C C   . PRO D  1  673 ? -8.095  -46.428 0.920   1.00 77.09  ?  673  PRO D C   1 
ATOM   11246 O O   . PRO D  1  673 ? -7.998  -46.938 -0.204  1.00 77.12  ?  673  PRO D O   1 
ATOM   11247 C CB  . PRO D  1  673 ? -8.279  -48.111 2.793   1.00 83.80  ?  673  PRO D CB  1 
ATOM   11248 C CG  . PRO D  1  673 ? -7.895  -48.031 4.234   1.00 85.64  ?  673  PRO D CG  1 
ATOM   11249 C CD  . PRO D  1  673 ? -7.583  -46.587 4.478   1.00 82.18  ?  673  PRO D CD  1 
ATOM   11250 N N   . ASP D  1  674 ? -8.812  -45.322 1.136   1.00 83.96  ?  674  ASP D N   1 
ATOM   11251 C CA  . ASP D  1  674 ? -9.529  -44.689 0.035   1.00 81.08  ?  674  ASP D CA  1 
ATOM   11252 C C   . ASP D  1  674 ? -8.600  -43.938 -0.909  1.00 78.16  ?  674  ASP D C   1 
ATOM   11253 O O   . ASP D  1  674 ? -9.014  -43.608 -2.025  1.00 76.57  ?  674  ASP D O   1 
ATOM   11254 C CB  . ASP D  1  674 ? -10.602 -43.736 0.563   1.00 78.77  ?  674  ASP D CB  1 
ATOM   11255 C CG  . ASP D  1  674 ? -10.139 -42.943 1.765   1.00 78.28  ?  674  ASP D CG  1 
ATOM   11256 O OD1 . ASP D  1  674 ? -8.916  -42.756 1.917   1.00 78.15  ?  674  ASP D OD1 1 
ATOM   11257 O OD2 . ASP D  1  674 ? -11.000 -42.502 2.556   1.00 78.17  -1 674  ASP D OD2 1 
ATOM   11258 N N   . ALA D  1  675 ? -7.367  -43.652 -0.488  1.00 73.18  ?  675  ALA D N   1 
ATOM   11259 C CA  . ALA D  1  675 ? -6.407  -42.964 -1.345  1.00 71.02  ?  675  ALA D CA  1 
ATOM   11260 C C   . ALA D  1  675 ? -5.862  -43.847 -2.460  1.00 72.36  ?  675  ALA D C   1 
ATOM   11261 O O   . ALA D  1  675 ? -5.004  -43.388 -3.223  1.00 70.83  ?  675  ALA D O   1 
ATOM   11262 C CB  . ALA D  1  675 ? -5.250  -42.420 -0.504  1.00 71.05  ?  675  ALA D CB  1 
ATOM   11263 N N   . PHE D  1  676 ? -6.338  -45.089 -2.580  1.00 67.14  ?  676  PHE D N   1 
ATOM   11264 C CA  . PHE D  1  676 ? -5.916  -45.997 -3.639  1.00 68.52  ?  676  PHE D CA  1 
ATOM   11265 C C   . PHE D  1  676 ? -7.105  -46.668 -4.313  1.00 69.10  ?  676  PHE D C   1 
ATOM   11266 O O   . PHE D  1  676 ? -6.920  -47.661 -5.027  1.00 70.99  ?  676  PHE D O   1 
ATOM   11267 C CB  . PHE D  1  676 ? -4.970  -47.070 -3.089  1.00 72.15  ?  676  PHE D CB  1 
ATOM   11268 C CG  . PHE D  1  676 ? -3.762  -46.518 -2.394  1.00 72.10  ?  676  PHE D CG  1 
ATOM   11269 C CD1 . PHE D  1  676 ? -2.658  -46.102 -3.117  1.00 71.06  ?  676  PHE D CD1 1 
ATOM   11270 C CD2 . PHE D  1  676 ? -3.730  -46.423 -1.013  1.00 73.30  ?  676  PHE D CD2 1 
ATOM   11271 C CE1 . PHE D  1  676 ? -1.544  -45.597 -2.473  1.00 71.21  ?  676  PHE D CE1 1 
ATOM   11272 C CE2 . PHE D  1  676 ? -2.621  -45.921 -0.365  1.00 73.41  ?  676  PHE D CE2 1 
ATOM   11273 C CZ  . PHE D  1  676 ? -1.526  -45.506 -1.095  1.00 72.36  ?  676  PHE D CZ  1 
ATOM   11274 N N   . GLU D  1  677 ? -8.313  -46.152 -4.104  1.00 73.10  ?  677  GLU D N   1 
ATOM   11275 C CA  . GLU D  1  677 ? -9.526  -46.802 -4.573  1.00 74.01  ?  677  GLU D CA  1 
ATOM   11276 C C   . GLU D  1  677 ? -9.583  -46.842 -6.098  1.00 72.79  ?  677  GLU D C   1 
ATOM   11277 O O   . GLU D  1  677 ? -8.924  -46.069 -6.798  1.00 70.51  ?  677  GLU D O   1 
ATOM   11278 C CB  . GLU D  1  677 ? -10.757 -46.069 -4.043  1.00 72.58  ?  677  GLU D CB  1 
ATOM   11279 C CG  . GLU D  1  677 ? -11.262 -46.557 -2.699  1.00 75.03  ?  677  GLU D CG  1 
ATOM   11280 C CD  . GLU D  1  677 ? -12.511 -45.818 -2.259  1.00 73.71  ?  677  GLU D CD  1 
ATOM   11281 O OE1 . GLU D  1  677 ? -13.127 -45.137 -3.107  1.00 71.31  ?  677  GLU D OE1 1 
ATOM   11282 O OE2 . GLU D  1  677 ? -12.875 -45.915 -1.069  1.00 75.22  -1 677  GLU D OE2 1 
ATOM   11283 N N   . GLY D  1  678 ? -10.389 -47.772 -6.605  1.00 76.04  ?  678  GLY D N   1 
ATOM   11284 C CA  . GLY D  1  678 ? -10.781 -47.793 -8.001  1.00 74.96  ?  678  GLY D CA  1 
ATOM   11285 C C   . GLY D  1  678 ? -9.658  -47.806 -9.016  1.00 74.42  ?  678  GLY D C   1 
ATOM   11286 O O   . GLY D  1  678 ? -9.707  -47.058 -9.996  1.00 72.00  ?  678  GLY D O   1 
ATOM   11287 N N   . ASN D  1  679 ? -8.643  -48.634 -8.798  1.00 75.98  ?  679  ASN D N   1 
ATOM   11288 C CA  . ASN D  1  679 ? -7.576  -48.831 -9.768  1.00 76.12  ?  679  ASN D CA  1 
ATOM   11289 C C   . ASN D  1  679 ? -7.680  -50.240 -10.347 1.00 79.23  ?  679  ASN D C   1 
ATOM   11290 O O   . ASN D  1  679 ? -8.570  -51.018 -9.990  1.00 81.17  ?  679  ASN D O   1 
ATOM   11291 C CB  . ASN D  1  679 ? -6.212  -48.577 -9.123  1.00 76.47  ?  679  ASN D CB  1 
ATOM   11292 C CG  . ASN D  1  679 ? -5.887  -47.097 -9.020  1.00 73.08  ?  679  ASN D CG  1 
ATOM   11293 O OD1 . ASN D  1  679 ? -5.008  -46.591 -9.717  1.00 71.87  ?  679  ASN D OD1 1 
ATOM   11294 N ND2 . ASN D  1  679 ? -6.601  -46.394 -8.148  1.00 71.69  ?  679  ASN D ND2 1 
ATOM   11295 N N   . LYS D  1  680 ? -6.761  -50.576 -11.253 1.00 82.73  ?  680  LYS D N   1 
ATOM   11296 C CA  . LYS D  1  680 ? -6.892  -51.849 -11.957 1.00 85.71  ?  680  LYS D CA  1 
ATOM   11297 C C   . LYS D  1  680 ? -6.361  -53.012 -11.124 1.00 89.86  ?  680  LYS D C   1 
ATOM   11298 O O   . LYS D  1  680 ? -7.114  -53.928 -10.774 1.00 92.13  ?  680  LYS D O   1 
ATOM   11299 C CB  . LYS D  1  680 ? -6.171  -51.775 -13.307 1.00 84.89  ?  680  LYS D CB  1 
ATOM   11300 C CG  . LYS D  1  680 ? -6.251  -53.045 -14.153 1.00 88.18  ?  680  LYS D CG  1 
ATOM   11301 C CD  . LYS D  1  680 ? -7.642  -53.668 -14.127 1.00 89.55  ?  680  LYS D CD  1 
ATOM   11302 C CE  . LYS D  1  680 ? -8.527  -53.110 -15.231 1.00 86.73  ?  680  LYS D CE  1 
ATOM   11303 N NZ  . LYS D  1  680 ? -9.957  -53.055 -14.818 1.00 86.18  ?  680  LYS D NZ  1 
ATOM   11304 N N   . ASP D  1  681 ? -5.067  -52.998 -10.794 1.00 88.47  ?  681  ASP D N   1 
ATOM   11305 C CA  . ASP D  1  681 ? -4.512  -54.007 -9.891  1.00 92.22  ?  681  ASP D CA  1 
ATOM   11306 C C   . ASP D  1  681 ? -3.328  -53.386 -9.153  1.00 91.84  ?  681  ASP D C   1 
ATOM   11307 O O   . ASP D  1  681 ? -2.198  -53.429 -9.650  1.00 92.42  ?  681  ASP D O   1 
ATOM   11308 C CB  . ASP D  1  681 ? -4.104  -55.253 -10.670 1.00 95.41  ?  681  ASP D CB  1 
ATOM   11309 C CG  . ASP D  1  681 ? -3.651  -56.382 -9.770  1.00 99.68  ?  681  ASP D CG  1 
ATOM   11310 O OD1 . ASP D  1  681 ? -4.411  -56.757 -8.853  1.00 101.04 ?  681  ASP D OD1 1 
ATOM   11311 O OD2 . ASP D  1  681 ? -2.531  -56.894 -9.979  1.00 101.86 -1 681  ASP D OD2 1 
ATOM   11312 N N   . LEU D  1  682 ? -3.571  -52.888 -7.946  1.00 93.74  ?  682  LEU D N   1 
ATOM   11313 C CA  . LEU D  1  682 ? -2.503  -52.317 -7.139  1.00 93.23  ?  682  LEU D CA  1 
ATOM   11314 C C   . LEU D  1  682 ? -1.930  -53.379 -6.200  1.00 97.50  ?  682  LEU D C   1 
ATOM   11315 O O   . LEU D  1  682 ? -2.281  -54.560 -6.273  1.00 101.09 ?  682  LEU D O   1 
ATOM   11316 C CB  . LEU D  1  682 ? -3.004  -51.087 -6.384  1.00 90.23  ?  682  LEU D CB  1 
ATOM   11317 C CG  . LEU D  1  682 ? -2.548  -49.736 -6.949  1.00 86.75  ?  682  LEU D CG  1 
ATOM   11318 C CD1 . LEU D  1  682 ? -2.826  -49.641 -8.444  1.00 85.53  ?  682  LEU D CD1 1 
ATOM   11319 C CD2 . LEU D  1  682 ? -3.207  -48.586 -6.205  1.00 83.59  ?  682  LEU D CD2 1 
ATOM   11320 N N   . CYS D  1  683 ? -1.040  -52.956 -5.303  1.00 96.07  ?  683  CYS D N   1 
ATOM   11321 C CA  . CYS D  1  683 ? -0.408  -53.836 -4.320  1.00 100.16 ?  683  CYS D CA  1 
ATOM   11322 C C   . CYS D  1  683 ? 0.280   -55.029 -4.980  1.00 103.66 ?  683  CYS D C   1 
ATOM   11323 O O   . CYS D  1  683 ? 1.182   -54.859 -5.800  1.00 103.24 ?  683  CYS D O   1 
ATOM   11324 C CB  . CYS D  1  683 ? -1.437  -54.324 -3.295  1.00 101.80 ?  683  CYS D CB  1 
ATOM   11325 S SG  . CYS D  1  683 ? -2.653  -53.076 -2.807  1.00 97.73  ?  683  CYS D SG  1 
ATOM   11326 N N   . ASN E  2  26  ? -0.164  -4.270  13.290  1.00 36.17  ?  26   ASN E N   1 
ATOM   11327 C CA  . ASN E  2  26  ? -0.078  -4.934  14.586  1.00 36.59  ?  26   ASN E CA  1 
ATOM   11328 C C   . ASN E  2  26  ? 1.347   -5.394  14.868  1.00 36.80  ?  26   ASN E C   1 
ATOM   11329 O O   . ASN E  2  26  ? 2.290   -4.956  14.210  1.00 36.85  ?  26   ASN E O   1 
ATOM   11330 C CB  . ASN E  2  26  ? -1.037  -6.124  14.647  1.00 36.33  ?  26   ASN E CB  1 
ATOM   11331 C CG  . ASN E  2  26  ? -0.697  -7.201  13.635  1.00 35.76  ?  26   ASN E CG  1 
ATOM   11332 O OD1 . ASN E  2  26  ? 0.032   -6.959  12.672  1.00 35.43  ?  26   ASN E OD1 1 
ATOM   11333 N ND2 . ASN E  2  26  ? -1.221  -8.401  13.851  1.00 35.87  ?  26   ASN E ND2 1 
ATOM   11334 N N   . ALA E  2  27  ? 1.493   -6.289  15.849  1.00 35.55  ?  27   ALA E N   1 
ATOM   11335 C CA  . ALA E  2  27  ? 2.816   -6.781  16.221  1.00 35.90  ?  27   ALA E CA  1 
ATOM   11336 C C   . ALA E  2  27  ? 3.509   -7.448  15.039  1.00 35.42  ?  27   ALA E C   1 
ATOM   11337 O O   . ALA E  2  27  ? 4.660   -7.129  14.719  1.00 35.76  ?  27   ALA E O   1 
ATOM   11338 C CB  . ALA E  2  27  ? 2.702   -7.751  17.398  1.00 36.30  ?  27   ALA E CB  1 
ATOM   11339 N N   . GLU E  2  28  ? 2.816   -8.375  14.373  1.00 39.22  ?  28   GLU E N   1 
ATOM   11340 C CA  . GLU E  2  28  ? 3.410   -9.068  13.233  1.00 38.97  ?  28   GLU E CA  1 
ATOM   11341 C C   . GLU E  2  28  ? 3.731   -8.101  12.101  1.00 38.78  ?  28   GLU E C   1 
ATOM   11342 O O   . GLU E  2  28  ? 4.771   -8.227  11.443  1.00 39.04  ?  28   GLU E O   1 
ATOM   11343 C CB  . GLU E  2  28  ? 2.470   -10.167 12.740  1.00 38.68  ?  28   GLU E CB  1 
ATOM   11344 C CG  . GLU E  2  28  ? 2.199   -11.265 13.751  1.00 39.11  ?  28   GLU E CG  1 
ATOM   11345 C CD  . GLU E  2  28  ? 1.530   -12.469 13.122  1.00 39.20  ?  28   GLU E CD  1 
ATOM   11346 O OE1 . GLU E  2  28  ? 0.798   -12.285 12.127  1.00 38.86  ?  28   GLU E OE1 1 
ATOM   11347 O OE2 . GLU E  2  28  ? 1.736   -13.597 13.617  1.00 39.77  -1 28   GLU E OE2 1 
ATOM   11348 N N   . GLY E  2  29  ? 2.851   -7.128  11.859  1.00 36.68  ?  29   GLY E N   1 
ATOM   11349 C CA  . GLY E  2  29  ? 3.091   -6.182  10.782  1.00 36.64  ?  29   GLY E CA  1 
ATOM   11350 C C   . GLY E  2  29  ? 4.288   -5.289  11.043  1.00 37.42  ?  29   GLY E C   1 
ATOM   11351 O O   . GLY E  2  29  ? 5.058   -4.984  10.128  1.00 37.73  ?  29   GLY E O   1 
ATOM   11352 N N   . ASP E  2  30  ? 4.461   -4.855  12.294  1.00 36.47  ?  30   ASP E N   1 
ATOM   11353 C CA  . ASP E  2  30  ? 5.629   -4.050  12.636  1.00 37.54  ?  30   ASP E CA  1 
ATOM   11354 C C   . ASP E  2  30  ? 6.912   -4.864  12.523  1.00 37.96  ?  30   ASP E C   1 
ATOM   11355 O O   . ASP E  2  30  ? 7.950   -4.339  12.103  1.00 38.85  ?  30   ASP E O   1 
ATOM   11356 C CB  . ASP E  2  30  ? 5.476   -3.471  14.042  1.00 38.24  ?  30   ASP E CB  1 
ATOM   11357 C CG  . ASP E  2  30  ? 4.467   -2.339  14.101  1.00 38.34  ?  30   ASP E CG  1 
ATOM   11358 O OD1 . ASP E  2  30  ? 4.719   -1.285  13.479  1.00 38.89  ?  30   ASP E OD1 1 
ATOM   11359 O OD2 . ASP E  2  30  ? 3.427   -2.498  14.773  1.00 38.07  -1 30   ASP E OD2 1 
ATOM   11360 N N   . ALA E  2  31  ? 6.860   -6.145  12.895  1.00 37.20  ?  31   ALA E N   1 
ATOM   11361 C CA  . ALA E  2  31  ? 8.035   -7.005  12.779  1.00 37.70  ?  31   ALA E CA  1 
ATOM   11362 C C   . ALA E  2  31  ? 8.489   -7.123  11.328  1.00 37.72  ?  31   ALA E C   1 
ATOM   11363 O O   . ALA E  2  31  ? 9.669   -6.926  11.016  1.00 38.70  ?  31   ALA E O   1 
ATOM   11364 C CB  . ALA E  2  31  ? 7.735   -8.384  13.365  1.00 37.34  ?  31   ALA E CB  1 
ATOM   11365 N N   . LEU E  2  32  ? 7.560   -7.447  10.425  1.00 36.50  ?  32   LEU E N   1 
ATOM   11366 C CA  . LEU E  2  32  ? 7.903   -7.537  9.008   1.00 36.62  ?  32   LEU E CA  1 
ATOM   11367 C C   . LEU E  2  32  ? 8.312   -6.183  8.441   1.00 37.22  ?  32   LEU E C   1 
ATOM   11368 O O   . LEU E  2  32  ? 9.102   -6.123  7.491   1.00 37.92  ?  32   LEU E O   1 
ATOM   11369 C CB  . LEU E  2  32  ? 6.733   -8.118  8.215   1.00 35.71  ?  32   LEU E CB  1 
ATOM   11370 C CG  . LEU E  2  32  ? 6.422   -9.595  8.466   1.00 35.50  ?  32   LEU E CG  1 
ATOM   11371 C CD1 . LEU E  2  32  ? 5.283   -10.063 7.574   1.00 34.94  ?  32   LEU E CD1 1 
ATOM   11372 C CD2 . LEU E  2  32  ? 7.661   -10.447 8.246   1.00 36.35  ?  32   LEU E CD2 1 
ATOM   11373 N N   . SER E  2  33  ? 7.787   -5.090  9.002   1.00 37.00  ?  33   SER E N   1 
ATOM   11374 C CA  . SER E  2  33  ? 8.204   -3.764  8.557   1.00 37.88  ?  33   SER E CA  1 
ATOM   11375 C C   . SER E  2  33  ? 9.649   -3.476  8.946   1.00 39.39  ?  33   SER E C   1 
ATOM   11376 O O   . SER E  2  33  ? 10.346  -2.744  8.234   1.00 40.50  ?  33   SER E O   1 
ATOM   11377 C CB  . SER E  2  33  ? 7.276   -2.695  9.136   1.00 37.71  ?  33   SER E CB  1 
ATOM   11378 O OG  . SER E  2  33  ? 5.964   -2.816  8.615   1.00 36.57  ?  33   SER E OG  1 
ATOM   11379 N N   . ALA E  2  34  ? 10.112  -4.036  10.067  1.00 39.75  ?  34   ALA E N   1 
ATOM   11380 C CA  . ALA E  2  34  ? 11.512  -3.878  10.449  1.00 41.34  ?  34   ALA E CA  1 
ATOM   11381 C C   . ALA E  2  34  ? 12.439  -4.512  9.419   1.00 41.96  ?  34   ALA E C   1 
ATOM   11382 O O   . ALA E  2  34  ? 13.468  -3.930  9.055   1.00 43.55  ?  34   ALA E O   1 
ATOM   11383 C CB  . ALA E  2  34  ? 11.752  -4.483  11.831  1.00 41.45  ?  34   ALA E CB  1 
ATOM   11384 N N   . LEU E  2  35  ? 12.089  -5.707  8.937   1.00 40.70  ?  35   LEU E N   1 
ATOM   11385 C CA  . LEU E  2  35  ? 12.885  -6.349  7.896   1.00 41.41  ?  35   LEU E CA  1 
ATOM   11386 C C   . LEU E  2  35  ? 12.845  -5.543  6.604   1.00 41.81  ?  35   LEU E C   1 
ATOM   11387 O O   . LEU E  2  35  ? 13.854  -5.440  5.896   1.00 43.25  ?  35   LEU E O   1 
ATOM   11388 C CB  . LEU E  2  35  ? 12.396  -7.785  7.676   1.00 40.43  ?  35   LEU E CB  1 
ATOM   11389 C CG  . LEU E  2  35  ? 13.082  -8.702  6.656   1.00 41.18  ?  35   LEU E CG  1 
ATOM   11390 C CD1 . LEU E  2  35  ? 12.853  -10.146 7.026   1.00 40.70  ?  35   LEU E CD1 1 
ATOM   11391 C CD2 . LEU E  2  35  ? 12.544  -8.468  5.257   1.00 40.89  ?  35   LEU E CD2 1 
ATOM   11392 N N   . LYS E  2  36  ? 11.681  -4.976  6.274   1.00 39.92  ?  36   LYS E N   1 
ATOM   11393 C CA  . LYS E  2  36  ? 11.548  -4.181  5.057   1.00 40.30  ?  36   LYS E CA  1 
ATOM   11394 C C   . LYS E  2  36  ? 12.506  -2.994  5.047   1.00 42.11  ?  36   LYS E C   1 
ATOM   11395 O O   . LYS E  2  36  ? 12.964  -2.576  3.976   1.00 43.17  ?  36   LYS E O   1 
ATOM   11396 C CB  . LYS E  2  36  ? 10.102  -3.705  4.908   1.00 38.91  ?  36   LYS E CB  1 
ATOM   11397 C CG  . LYS E  2  36  ? 9.858   -2.771  3.735   1.00 39.29  ?  36   LYS E CG  1 
ATOM   11398 C CD  . LYS E  2  36  ? 8.414   -2.305  3.704   1.00 38.02  ?  36   LYS E CD  1 
ATOM   11399 C CE  . LYS E  2  36  ? 8.317   -0.811  3.458   1.00 38.83  ?  36   LYS E CE  1 
ATOM   11400 N NZ  . LYS E  2  36  ? 7.657   -0.511  2.158   1.00 38.55  ?  36   LYS E NZ  1 
ATOM   11401 N N   . ASN E  2  37  ? 12.828  -2.445  6.220   1.00 46.50  ?  37   ASN E N   1 
ATOM   11402 C CA  . ASN E  2  37  ? 13.731  -1.303  6.288   1.00 48.55  ?  37   ASN E CA  1 
ATOM   11403 C C   . ASN E  2  37  ? 15.200  -1.701  6.295   1.00 50.38  ?  37   ASN E C   1 
ATOM   11404 O O   . ASN E  2  37  ? 16.051  -0.875  5.946   1.00 52.43  ?  37   ASN E O   1 
ATOM   11405 C CB  . ASN E  2  37  ? 13.435  -0.467  7.535   1.00 48.76  ?  37   ASN E CB  1 
ATOM   11406 C CG  . ASN E  2  37  ? 12.070  0.185   7.490   1.00 47.51  ?  37   ASN E CG  1 
ATOM   11407 O OD1 . ASN E  2  37  ? 11.923  1.309   7.012   1.00 48.35  ?  37   ASN E OD1 1 
ATOM   11408 N ND2 . ASN E  2  37  ? 11.062  -0.518  7.992   1.00 45.68  ?  37   ASN E ND2 1 
ATOM   11409 N N   . SER E  2  38  ? 15.520  -2.935  6.676   1.00 51.67  ?  38   SER E N   1 
ATOM   11410 C CA  . SER E  2  38  ? 16.902  -3.391  6.705   1.00 53.49  ?  38   SER E CA  1 
ATOM   11411 C C   . SER E  2  38  ? 17.339  -4.047  5.404   1.00 54.02  ?  38   SER E C   1 
ATOM   11412 O O   . SER E  2  38  ? 18.510  -4.420  5.278   1.00 55.78  ?  38   SER E O   1 
ATOM   11413 C CB  . SER E  2  38  ? 17.112  -4.366  7.866   1.00 53.01  ?  38   SER E CB  1 
ATOM   11414 O OG  . SER E  2  38  ? 18.084  -5.347  7.544   1.00 54.01  ?  38   SER E OG  1 
ATOM   11415 N N   . LEU E  2  39  ? 16.436  -4.198  4.441   1.00 50.44  ?  39   LEU E N   1 
ATOM   11416 C CA  . LEU E  2  39  ? 16.761  -4.767  3.143   1.00 51.06  ?  39   LEU E CA  1 
ATOM   11417 C C   . LEU E  2  39  ? 16.665  -3.701  2.061   1.00 51.90  ?  39   LEU E C   1 
ATOM   11418 O O   . LEU E  2  39  ? 15.723  -2.903  2.043   1.00 50.86  ?  39   LEU E O   1 
ATOM   11419 C CB  . LEU E  2  39  ? 15.832  -5.934  2.794   1.00 49.20  ?  39   LEU E CB  1 
ATOM   11420 C CG  . LEU E  2  39  ? 16.263  -7.351  3.183   1.00 49.21  ?  39   LEU E CG  1 
ATOM   11421 C CD1 . LEU E  2  39  ? 16.708  -7.433  4.637   1.00 49.34  ?  39   LEU E CD1 1 
ATOM   11422 C CD2 . LEU E  2  39  ? 15.157  -8.354  2.888   1.00 47.49  ?  39   LEU E CD2 1 
ATOM   11423 N N   . ALA E  2  40  ? 17.645  -3.694  1.162   1.00 51.71  ?  40   ALA E N   1 
ATOM   11424 C CA  . ALA E  2  40  ? 17.557  -2.890  -0.047  1.00 52.63  ?  40   ALA E CA  1 
ATOM   11425 C C   . ALA E  2  40  ? 16.754  -3.654  -1.091  1.00 51.32  ?  40   ALA E C   1 
ATOM   11426 O O   . ALA E  2  40  ? 17.044  -4.819  -1.376  1.00 51.40  ?  40   ALA E O   1 
ATOM   11427 C CB  . ALA E  2  40  ? 18.951  -2.561  -0.577  1.00 55.68  ?  40   ALA E CB  1 
ATOM   11428 N N   . ASP E  2  41  ? 15.746  -2.996  -1.666  1.00 52.32  ?  41   ASP E N   1 
ATOM   11429 C CA  . ASP E  2  41  ? 14.778  -3.637  -2.554  1.00 50.94  ?  41   ASP E CA  1 
ATOM   11430 C C   . ASP E  2  41  ? 14.823  -2.941  -3.909  1.00 52.19  ?  41   ASP E C   1 
ATOM   11431 O O   . ASP E  2  41  ? 13.996  -2.062  -4.195  1.00 51.52  ?  41   ASP E O   1 
ATOM   11432 C CB  . ASP E  2  41  ? 13.371  -3.592  -1.957  1.00 48.49  ?  41   ASP E CB  1 
ATOM   11433 C CG  . ASP E  2  41  ? 12.380  -4.454  -2.719  1.00 47.17  ?  41   ASP E CG  1 
ATOM   11434 O OD1 . ASP E  2  41  ? 12.722  -4.955  -3.811  1.00 48.15  ?  41   ASP E OD1 1 
ATOM   11435 O OD2 . ASP E  2  41  ? 11.247  -4.626  -2.225  1.00 45.35  -1 41   ASP E OD2 1 
ATOM   11436 N N   . PRO E  2  42  ? 15.765  -3.320  -4.777  1.00 50.46  ?  42   PRO E N   1 
ATOM   11437 C CA  . PRO E  2  42  ? 15.848  -2.656  -6.087  1.00 52.30  ?  42   PRO E CA  1 
ATOM   11438 C C   . PRO E  2  42  ? 14.693  -3.000  -7.010  1.00 50.39  ?  42   PRO E C   1 
ATOM   11439 O O   . PRO E  2  42  ? 14.358  -2.193  -7.886  1.00 51.11  ?  42   PRO E O   1 
ATOM   11440 C CB  . PRO E  2  42  ? 17.188  -3.154  -6.646  1.00 55.74  ?  42   PRO E CB  1 
ATOM   11441 C CG  . PRO E  2  42  ? 17.398  -4.474  -5.986  1.00 54.77  ?  42   PRO E CG  1 
ATOM   11442 C CD  . PRO E  2  42  ? 16.793  -4.362  -4.612  1.00 52.11  ?  42   PRO E CD  1 
ATOM   11443 N N   . ASN E  2  43  ? 14.073  -4.166  -6.842  1.00 51.05  ?  43   ASN E N   1 
ATOM   11444 C CA  . ASN E  2  43  ? 12.971  -4.596  -7.691  1.00 51.19  ?  43   ASN E CA  1 
ATOM   11445 C C   . ASN E  2  43  ? 11.606  -4.218  -7.127  1.00 50.07  ?  43   ASN E C   1 
ATOM   11446 O O   . ASN E  2  43  ? 10.584  -4.604  -7.704  1.00 49.38  ?  43   ASN E O   1 
ATOM   11447 C CB  . ASN E  2  43  ? 13.039  -6.109  -7.913  1.00 49.37  ?  43   ASN E CB  1 
ATOM   11448 C CG  . ASN E  2  43  ? 14.112  -6.504  -8.909  1.00 52.28  ?  43   ASN E CG  1 
ATOM   11449 O OD1 . ASN E  2  43  ? 14.938  -7.376  -8.636  1.00 53.43  ?  43   ASN E OD1 1 
ATOM   11450 N ND2 . ASN E  2  43  ? 14.110  -5.858  -10.069 1.00 53.87  ?  43   ASN E ND2 1 
ATOM   11451 N N   . LYS E  2  44  ? 11.573  -3.474  -6.018  1.00 48.61  ?  44   LYS E N   1 
ATOM   11452 C CA  . LYS E  2  44  ? 10.327  -3.003  -5.407  1.00 47.20  ?  44   LYS E CA  1 
ATOM   11453 C C   . LYS E  2  44  ? 9.399   -4.168  -5.064  1.00 44.57  ?  44   LYS E C   1 
ATOM   11454 O O   . LYS E  2  44  ? 8.178   -4.080  -5.209  1.00 44.03  ?  44   LYS E O   1 
ATOM   11455 C CB  . LYS E  2  44  ? 9.618   -1.981  -6.302  1.00 49.85  ?  44   LYS E CB  1 
ATOM   11456 C CG  . LYS E  2  44  ? 10.342  -0.639  -6.455  1.00 52.53  ?  44   LYS E CG  1 
ATOM   11457 C CD  . LYS E  2  44  ? 11.398  -0.413  -5.378  1.00 50.94  ?  44   LYS E CD  1 
ATOM   11458 C CE  . LYS E  2  44  ? 11.445  1.038   -4.931  1.00 51.79  ?  44   LYS E CE  1 
ATOM   11459 N NZ  . LYS E  2  44  ? 12.170  1.190   -3.639  1.00 48.08  ?  44   LYS E NZ  1 
ATOM   11460 N N   . VAL E  2  45  ? 9.991   -5.276  -4.614  1.00 42.57  ?  45   VAL E N   1 
ATOM   11461 C CA  . VAL E  2  45  ? 9.207   -6.441  -4.217  1.00 40.82  ?  45   VAL E CA  1 
ATOM   11462 C C   . VAL E  2  45  ? 8.377   -6.130  -2.976  1.00 38.82  ?  45   VAL E C   1 
ATOM   11463 O O   . VAL E  2  45  ? 7.189   -6.467  -2.905  1.00 37.19  ?  45   VAL E O   1 
ATOM   11464 C CB  . VAL E  2  45  ? 10.134  -7.650  -3.995  1.00 41.90  ?  45   VAL E CB  1 
ATOM   11465 C CG1 . VAL E  2  45  ? 9.425   -8.731  -3.197  1.00 40.28  ?  45   VAL E CG1 1 
ATOM   11466 C CG2 . VAL E  2  45  ? 10.622  -8.197  -5.328  1.00 43.66  ?  45   VAL E CG2 1 
ATOM   11467 N N   . LEU E  2  46  ? 8.983   -5.477  -1.986  1.00 39.65  ?  46   LEU E N   1 
ATOM   11468 C CA  . LEU E  2  46  ? 8.324   -5.123  -0.733  1.00 36.91  ?  46   LEU E CA  1 
ATOM   11469 C C   . LEU E  2  46  ? 7.424   -3.898  -0.857  1.00 37.04  ?  46   LEU E C   1 
ATOM   11470 O O   . LEU E  2  46  ? 6.998   -3.358  0.170   1.00 34.84  ?  46   LEU E O   1 
ATOM   11471 C CB  . LEU E  2  46  ? 9.369   -4.887  0.360   1.00 37.59  ?  46   LEU E CB  1 
ATOM   11472 C CG  . LEU E  2  46  ? 10.341  -6.040  0.606   1.00 38.71  ?  46   LEU E CG  1 
ATOM   11473 C CD1 . LEU E  2  46  ? 11.457  -5.609  1.542   1.00 40.23  ?  46   LEU E CD1 1 
ATOM   11474 C CD2 . LEU E  2  46  ? 9.604   -7.246  1.162   1.00 37.25  ?  46   LEU E CD2 1 
ATOM   11475 N N   . GLN E  2  47  ? 7.141   -3.452  -2.085  1.00 35.54  ?  47   GLN E N   1 
ATOM   11476 C CA  . GLN E  2  47  ? 6.331   -2.255  -2.298  1.00 36.98  ?  47   GLN E CA  1 
ATOM   11477 C C   . GLN E  2  47  ? 4.989   -2.352  -1.582  1.00 33.65  ?  47   GLN E C   1 
ATOM   11478 O O   . GLN E  2  47  ? 4.533   -1.385  -0.961  1.00 32.38  ?  47   GLN E O   1 
ATOM   11479 C CB  . GLN E  2  47  ? 6.117   -2.045  -3.799  1.00 40.73  ?  47   GLN E CB  1 
ATOM   11480 C CG  . GLN E  2  47  ? 5.079   -0.998  -4.167  1.00 42.43  ?  47   GLN E CG  1 
ATOM   11481 C CD  . GLN E  2  47  ? 5.656   0.404   -4.202  1.00 46.04  ?  47   GLN E CD  1 
ATOM   11482 O OE1 . GLN E  2  47  ? 6.867   0.586   -4.334  1.00 46.57  ?  47   GLN E OE1 1 
ATOM   11483 N NE2 . GLN E  2  47  ? 4.789   1.406   -4.093  1.00 46.64  ?  47   GLN E NE2 1 
ATOM   11484 N N   . SER E  2  48  ? 4.349   -3.521  -1.650  1.00 33.02  ?  48   SER E N   1 
ATOM   11485 C CA  . SER E  2  48  ? 3.014   -3.702  -1.094  1.00 31.48  ?  48   SER E CA  1 
ATOM   11486 C C   . SER E  2  48  ? 2.978   -3.598  0.426   1.00 30.82  ?  48   SER E C   1 
ATOM   11487 O O   . SER E  2  48  ? 1.893   -3.438  0.996   1.00 29.83  ?  48   SER E O   1 
ATOM   11488 C CB  . SER E  2  48  ? 2.460   -5.059  -1.529  1.00 31.10  ?  48   SER E CB  1 
ATOM   11489 O OG  . SER E  2  48  ? 1.331   -5.433  -0.761  1.00 30.00  ?  48   SER E OG  1 
ATOM   11490 N N   . TRP E  2  49  ? 4.127   -3.669  1.094   1.00 30.97  ?  49   TRP E N   1 
ATOM   11491 C CA  . TRP E  2  49  ? 4.179   -3.780  2.552   1.00 30.59  ?  49   TRP E CA  1 
ATOM   11492 C C   . TRP E  2  49  ? 3.896   -2.412  3.167   1.00 30.50  ?  49   TRP E C   1 
ATOM   11493 O O   . TRP E  2  49  ? 4.805   -1.636  3.465   1.00 31.58  ?  49   TRP E O   1 
ATOM   11494 C CB  . TRP E  2  49  ? 5.529   -4.332  2.993   1.00 31.72  ?  49   TRP E CB  1 
ATOM   11495 C CG  . TRP E  2  49  ? 5.718   -5.792  2.669   1.00 31.83  ?  49   TRP E CG  1 
ATOM   11496 C CD1 . TRP E  2  49  ? 5.095   -6.499  1.681   1.00 31.45  ?  49   TRP E CD1 1 
ATOM   11497 C CD2 . TRP E  2  49  ? 6.584   -6.719  3.339   1.00 32.59  ?  49   TRP E CD2 1 
ATOM   11498 N NE1 . TRP E  2  49  ? 5.518   -7.806  1.694   1.00 31.94  ?  49   TRP E NE1 1 
ATOM   11499 C CE2 . TRP E  2  49  ? 6.432   -7.967  2.701   1.00 32.62  ?  49   TRP E CE2 1 
ATOM   11500 C CE3 . TRP E  2  49  ? 7.471   -6.616  4.415   1.00 33.44  ?  49   TRP E CE3 1 
ATOM   11501 C CZ2 . TRP E  2  49  ? 7.134   -9.102  3.103   1.00 33.45  ?  49   TRP E CZ2 1 
ATOM   11502 C CZ3 . TRP E  2  49  ? 8.168   -7.745  4.813   1.00 34.25  ?  49   TRP E CZ3 1 
ATOM   11503 C CH2 . TRP E  2  49  ? 7.995   -8.971  4.157   1.00 34.24  ?  49   TRP E CH2 1 
ATOM   11504 N N   . ASP E  2  50  ? 2.610   -2.119  3.367   1.00 28.17  ?  50   ASP E N   1 
ATOM   11505 C CA  . ASP E  2  50  ? 2.168   -0.836  3.910   1.00 28.13  ?  50   ASP E CA  1 
ATOM   11506 C C   . ASP E  2  50  ? 2.080   -0.955  5.428   1.00 27.90  ?  50   ASP E C   1 
ATOM   11507 O O   . ASP E  2  50  ? 1.206   -1.650  5.955   1.00 27.11  ?  50   ASP E O   1 
ATOM   11508 C CB  . ASP E  2  50  ? 0.825   -0.437  3.302   1.00 27.41  ?  50   ASP E CB  1 
ATOM   11509 C CG  . ASP E  2  50  ? 0.222   0.801   3.950   1.00 27.42  ?  50   ASP E CG  1 
ATOM   11510 O OD1 . ASP E  2  50  ? 0.960   1.573   4.600   1.00 28.18  ?  50   ASP E OD1 1 
ATOM   11511 O OD2 . ASP E  2  50  ? -1.002  1.005   3.803   1.00 26.86  -1 50   ASP E OD2 1 
ATOM   11512 N N   . ALA E  2  51  ? 2.983   -0.262  6.129   1.00 28.42  ?  51   ALA E N   1 
ATOM   11513 C CA  . ALA E  2  51  ? 3.053   -0.375  7.584   1.00 28.52  ?  51   ALA E CA  1 
ATOM   11514 C C   . ALA E  2  51  ? 1.785   0.123   8.267   1.00 27.82  ?  51   ALA E C   1 
ATOM   11515 O O   . ALA E  2  51  ? 1.479   -0.305  9.386   1.00 27.70  ?  51   ALA E O   1 
ATOM   11516 C CB  . ALA E  2  51  ? 4.268   0.390   8.108   1.00 30.02  ?  51   ALA E CB  1 
ATOM   11517 N N   . THR E  2  52  ? 1.037   1.017   7.622   1.00 26.44  ?  52   THR E N   1 
ATOM   11518 C CA  . THR E  2  52  ? -0.117  1.649   8.251   1.00 26.12  ?  52   THR E CA  1 
ATOM   11519 C C   . THR E  2  52  ? -1.381  0.798   8.186   1.00 25.19  ?  52   THR E C   1 
ATOM   11520 O O   . THR E  2  52  ? -2.472  1.320   8.438   1.00 25.06  ?  52   THR E O   1 
ATOM   11521 C CB  . THR E  2  52  ? -0.382  3.013   7.609   1.00 26.57  ?  52   THR E CB  1 
ATOM   11522 O OG1 . THR E  2  52  ? -0.844  2.829   6.264   1.00 26.11  ?  52   THR E OG1 1 
ATOM   11523 C CG2 . THR E  2  52  ? 0.888   3.845   7.591   1.00 27.89  ?  52   THR E CG2 1 
ATOM   11524 N N   . LEU E  2  53  ? -1.264  -0.484  7.861   1.00 24.62  ?  53   LEU E N   1 
ATOM   11525 C CA  . LEU E  2  53  ? -2.397  -1.396  7.898   1.00 24.13  ?  53   LEU E CA  1 
ATOM   11526 C C   . LEU E  2  53  ? -2.460  -2.106  9.247   1.00 24.39  ?  53   LEU E C   1 
ATOM   11527 O O   . LEU E  2  53  ? -1.457  -2.235  9.955   1.00 24.82  ?  53   LEU E O   1 
ATOM   11528 C CB  . LEU E  2  53  ? -2.313  -2.416  6.761   1.00 23.86  ?  53   LEU E CB  1 
ATOM   11529 C CG  . LEU E  2  53  ? -2.237  -1.841  5.345   1.00 23.83  ?  53   LEU E CG  1 
ATOM   11530 C CD1 . LEU E  2  53  ? -2.145  -2.957  4.319   1.00 23.77  ?  53   LEU E CD1 1 
ATOM   11531 C CD2 . LEU E  2  53  ? -3.442  -0.954  5.067   1.00 23.73  ?  53   LEU E CD2 1 
ATOM   11532 N N   . VAL E  2  54  ? -3.669  -2.550  9.608   1.00 25.72  ?  54   VAL E N   1 
ATOM   11533 C CA  . VAL E  2  54  ? -3.861  -3.263  10.871  1.00 26.25  ?  54   VAL E CA  1 
ATOM   11534 C C   . VAL E  2  54  ? -2.955  -4.486  10.930  1.00 26.42  ?  54   VAL E C   1 
ATOM   11535 O O   . VAL E  2  54  ? -2.114  -4.620  11.826  1.00 26.91  ?  54   VAL E O   1 
ATOM   11536 C CB  . VAL E  2  54  ? -5.338  -3.655  11.057  1.00 26.57  ?  54   VAL E CB  1 
ATOM   11537 C CG1 . VAL E  2  54  ? -5.588  -4.103  12.487  1.00 27.47  ?  54   VAL E CG1 1 
ATOM   11538 C CG2 . VAL E  2  54  ? -6.248  -2.496  10.704  1.00 26.49  ?  54   VAL E CG2 1 
ATOM   11539 N N   . THR E  2  55  ? -3.110  -5.389  9.973   1.00 29.54  ?  55   THR E N   1 
ATOM   11540 C CA  . THR E  2  55  ? -2.291  -6.581  9.857   1.00 29.83  ?  55   THR E CA  1 
ATOM   11541 C C   . THR E  2  55  ? -1.629  -6.613  8.486   1.00 29.45  ?  55   THR E C   1 
ATOM   11542 O O   . THR E  2  55  ? -2.114  -5.984  7.538   1.00 29.01  ?  55   THR E O   1 
ATOM   11543 C CB  . THR E  2  55  ? -3.128  -7.855  10.061  1.00 30.40  ?  55   THR E CB  1 
ATOM   11544 O OG1 . THR E  2  55  ? -3.819  -8.180  8.848   1.00 30.18  ?  55   THR E OG1 1 
ATOM   11545 C CG2 . THR E  2  55  ? -4.135  -7.669  11.190  1.00 30.97  ?  55   THR E CG2 1 
ATOM   11546 N N   . PRO E  2  56  ? -0.515  -7.332  8.343   1.00 31.45  ?  56   PRO E N   1 
ATOM   11547 C CA  . PRO E  2  56  ? 0.153   -7.437  7.041   1.00 31.40  ?  56   PRO E CA  1 
ATOM   11548 C C   . PRO E  2  56  ? -0.453  -8.474  6.109   1.00 31.45  ?  56   PRO E C   1 
ATOM   11549 O O   . PRO E  2  56  ? 0.179   -8.827  5.110   1.00 31.68  ?  56   PRO E O   1 
ATOM   11550 C CB  . PRO E  2  56  ? 1.583   -7.836  7.438   1.00 32.14  ?  56   PRO E CB  1 
ATOM   11551 C CG  . PRO E  2  56  ? 1.402   -8.632  8.671   1.00 32.58  ?  56   PRO E CG  1 
ATOM   11552 C CD  . PRO E  2  56  ? 0.268   -7.978  9.413   1.00 32.18  ?  56   PRO E CD  1 
ATOM   11553 N N   . CYS E  2  57  ? -1.656  -8.965  6.416   1.00 32.63  ?  57   CYS E N   1 
ATOM   11554 C CA  . CYS E  2  57  ? -2.239  -10.080 5.680   1.00 33.07  ?  57   CYS E CA  1 
ATOM   11555 C C   . CYS E  2  57  ? -2.617  -9.713  4.251   1.00 32.79  ?  57   CYS E C   1 
ATOM   11556 O O   . CYS E  2  57  ? -2.679  -10.602 3.395   1.00 33.31  ?  57   CYS E O   1 
ATOM   11557 C CB  . CYS E  2  57  ? -3.464  -10.599 6.429   1.00 33.59  ?  57   CYS E CB  1 
ATOM   11558 S SG  . CYS E  2  57  ? -3.062  -11.233 8.063   1.00 34.34  ?  57   CYS E SG  1 
ATOM   11559 N N   . THR E  2  58  ? -2.870  -8.438  3.971   1.00 29.09  ?  58   THR E N   1 
ATOM   11560 C CA  . THR E  2  58  ? -3.188  -8.001  2.620   1.00 29.00  ?  58   THR E CA  1 
ATOM   11561 C C   . THR E  2  58  ? -1.946  -7.634  1.821   1.00 29.07  ?  58   THR E C   1 
ATOM   11562 O O   . THR E  2  58  ? -2.069  -7.135  0.697   1.00 29.16  ?  58   THR E O   1 
ATOM   11563 C CB  . THR E  2  58  ? -4.147  -6.811  2.661   1.00 28.62  ?  58   THR E CB  1 
ATOM   11564 O OG1 . THR E  2  58  ? -3.490  -5.692  3.266   1.00 28.24  ?  58   THR E OG1 1 
ATOM   11565 C CG2 . THR E  2  58  ? -5.374  -7.160  3.475   1.00 28.89  ?  58   THR E CG2 1 
ATOM   11566 N N   . TRP E  2  59  ? -0.761  -7.866  2.374   1.00 29.25  ?  59   TRP E N   1 
ATOM   11567 C CA  . TRP E  2  59  ? 0.473   -7.636  1.646   1.00 29.74  ?  59   TRP E CA  1 
ATOM   11568 C C   . TRP E  2  59  ? 0.718   -8.770  0.657   1.00 30.42  ?  59   TRP E C   1 
ATOM   11569 O O   . TRP E  2  59  ? 0.216   -9.887  0.813   1.00 30.61  ?  59   TRP E O   1 
ATOM   11570 C CB  . TRP E  2  59  ? 1.659   -7.519  2.607   1.00 30.08  ?  59   TRP E CB  1 
ATOM   11571 C CG  . TRP E  2  59  ? 1.550   -6.390  3.593   1.00 29.69  ?  59   TRP E CG  1 
ATOM   11572 C CD1 . TRP E  2  59  ? 0.543   -5.474  3.687   1.00 29.09  ?  59   TRP E CD1 1 
ATOM   11573 C CD2 . TRP E  2  59  ? 2.487   -6.061  4.625   1.00 30.13  ?  59   TRP E CD2 1 
ATOM   11574 N NE1 . TRP E  2  59  ? 0.794   -4.596  4.713   1.00 29.10  ?  59   TRP E NE1 1 
ATOM   11575 C CE2 . TRP E  2  59  ? 1.982   -4.935  5.305   1.00 29.75  ?  59   TRP E CE2 1 
ATOM   11576 C CE3 . TRP E  2  59  ? 3.703   -6.610  5.043   1.00 31.02  ?  59   TRP E CE3 1 
ATOM   11577 C CZ2 . TRP E  2  59  ? 2.651   -4.348  6.376   1.00 30.23  ?  59   TRP E CZ2 1 
ATOM   11578 C CZ3 . TRP E  2  59  ? 4.366   -6.023  6.105   1.00 31.51  ?  59   TRP E CZ3 1 
ATOM   11579 C CH2 . TRP E  2  59  ? 3.839   -4.905  6.759   1.00 31.12  ?  59   TRP E CH2 1 
ATOM   11580 N N   . PHE E  2  60  ? 1.504   -8.473  -0.371  1.00 30.12  ?  60   PHE E N   1 
ATOM   11581 C CA  . PHE E  2  60  ? 1.912   -9.510  -1.302  1.00 31.03  ?  60   PHE E CA  1 
ATOM   11582 C C   . PHE E  2  60  ? 3.109   -10.264 -0.739  1.00 31.77  ?  60   PHE E C   1 
ATOM   11583 O O   . PHE E  2  60  ? 3.883   -9.731  0.063   1.00 31.82  ?  60   PHE E O   1 
ATOM   11584 C CB  . PHE E  2  60  ? 2.248   -8.914  -2.670  1.00 31.71  ?  60   PHE E CB  1 
ATOM   11585 C CG  . PHE E  2  60  ? 1.122   -8.126  -3.280  1.00 31.22  ?  60   PHE E CG  1 
ATOM   11586 C CD1 . PHE E  2  60  ? -0.197  -8.464  -3.023  1.00 30.58  ?  60   PHE E CD1 1 
ATOM   11587 C CD2 . PHE E  2  60  ? 1.381   -7.054  -4.117  1.00 33.61  ?  60   PHE E CD2 1 
ATOM   11588 C CE1 . PHE E  2  60  ? -1.235  -7.743  -3.582  1.00 30.36  ?  60   PHE E CE1 1 
ATOM   11589 C CE2 . PHE E  2  60  ? 0.347   -6.328  -4.677  1.00 32.78  ?  60   PHE E CE2 1 
ATOM   11590 C CZ  . PHE E  2  60  ? -0.962  -6.676  -4.411  1.00 30.72  ?  60   PHE E CZ  1 
ATOM   11591 N N   . HIS E  2  61  ? 3.237   -11.527 -1.148  1.00 32.31  ?  61   HIS E N   1 
ATOM   11592 C CA  . HIS E  2  61  ? 4.251   -12.474 -0.692  1.00 33.26  ?  61   HIS E CA  1 
ATOM   11593 C C   . HIS E  2  61  ? 4.046   -12.872 0.766   1.00 32.84  ?  61   HIS E C   1 
ATOM   11594 O O   . HIS E  2  61  ? 4.842   -13.656 1.299   1.00 33.71  ?  61   HIS E O   1 
ATOM   11595 C CB  . HIS E  2  61  ? 5.680   -11.945 -0.890  1.00 34.72  ?  61   HIS E CB  1 
ATOM   11596 C CG  . HIS E  2  61  ? 5.863   -11.171 -2.160  1.00 36.57  ?  61   HIS E CG  1 
ATOM   11597 N ND1 . HIS E  2  61  ? 5.745   -11.747 -3.407  1.00 36.97  ?  61   HIS E ND1 1 
ATOM   11598 C CD2 . HIS E  2  61  ? 6.141   -9.864  -2.375  1.00 37.61  ?  61   HIS E CD2 1 
ATOM   11599 C CE1 . HIS E  2  61  ? 5.949   -10.829 -4.335  1.00 38.05  ?  61   HIS E CE1 1 
ATOM   11600 N NE2 . HIS E  2  61  ? 6.192   -9.677  -3.735  1.00 38.53  ?  61   HIS E NE2 1 
ATOM   11601 N N   . VAL E  2  62  ? 3.011   -12.358 1.427   1.00 34.66  ?  62   VAL E N   1 
ATOM   11602 C CA  . VAL E  2  62  ? 2.670   -12.699 2.803   1.00 34.64  ?  62   VAL E CA  1 
ATOM   11603 C C   . VAL E  2  62  ? 1.293   -13.349 2.803   1.00 35.37  ?  62   VAL E C   1 
ATOM   11604 O O   . VAL E  2  62  ? 0.347   -12.804 2.223   1.00 36.06  ?  62   VAL E O   1 
ATOM   11605 C CB  . VAL E  2  62  ? 2.685   -11.458 3.715   1.00 34.41  ?  62   VAL E CB  1 
ATOM   11606 C CG1 . VAL E  2  62  ? 1.976   -11.749 5.033   1.00 35.08  ?  62   VAL E CG1 1 
ATOM   11607 C CG2 . VAL E  2  62  ? 4.111   -10.988 3.958   1.00 34.41  ?  62   VAL E CG2 1 
ATOM   11608 N N   . THR E  2  63  ? 1.181   -14.512 3.443   1.00 37.49  ?  63   THR E N   1 
ATOM   11609 C CA  . THR E  2  63  ? -0.091  -15.208 3.584   1.00 39.19  ?  63   THR E CA  1 
ATOM   11610 C C   . THR E  2  63  ? -0.392  -15.432 5.060   1.00 40.32  ?  63   THR E C   1 
ATOM   11611 O O   . THR E  2  63  ? 0.503   -15.763 5.844   1.00 40.17  ?  63   THR E O   1 
ATOM   11612 C CB  . THR E  2  63  ? -0.092  -16.555 2.844   1.00 39.46  ?  63   THR E CB  1 
ATOM   11613 O OG1 . THR E  2  63  ? 0.407   -17.581 3.710   1.00 41.11  ?  63   THR E OG1 1 
ATOM   11614 C CG2 . THR E  2  63  ? 0.772   -16.487 1.592   1.00 38.02  ?  63   THR E CG2 1 
ATOM   11615 N N   . CYS E  2  64  ? -1.653  -15.242 5.432   1.00 39.49  ?  64   CYS E N   1 
ATOM   11616 C CA  . CYS E  2  64  ? -2.119  -15.401 6.801   1.00 41.08  ?  64   CYS E CA  1 
ATOM   11617 C C   . CYS E  2  64  ? -3.066  -16.590 6.905   1.00 42.78  ?  64   CYS E C   1 
ATOM   11618 O O   . CYS E  2  64  ? -3.566  -17.113 5.905   1.00 43.16  ?  64   CYS E O   1 
ATOM   11619 C CB  . CYS E  2  64  ? -2.827  -14.133 7.292   1.00 41.38  ?  64   CYS E CB  1 
ATOM   11620 S SG  . CYS E  2  64  ? -1.753  -12.739 7.689   1.00 40.22  ?  64   CYS E SG  1 
ATOM   11621 N N   . ASN E  2  65  ? -3.307  -17.014 8.142   1.00 40.28  ?  65   ASN E N   1 
ATOM   11622 C CA  . ASN E  2  65  ? -4.299  -18.039 8.424   1.00 41.77  ?  65   ASN E CA  1 
ATOM   11623 C C   . ASN E  2  65  ? -5.634  -17.363 8.744   1.00 41.20  ?  65   ASN E C   1 
ATOM   11624 O O   . ASN E  2  65  ? -5.775  -16.141 8.643   1.00 39.60  ?  65   ASN E O   1 
ATOM   11625 C CB  . ASN E  2  65  ? -3.819  -18.959 9.548   1.00 44.04  ?  65   ASN E CB  1 
ATOM   11626 C CG  . ASN E  2  65  ? -3.536  -18.217 10.846  1.00 44.39  ?  65   ASN E CG  1 
ATOM   11627 O OD1 . ASN E  2  65  ? -3.814  -17.025 10.975  1.00 42.95  ?  65   ASN E OD1 1 
ATOM   11628 N ND2 . ASN E  2  65  ? -2.989  -18.932 11.822  1.00 46.61  ?  65   ASN E ND2 1 
ATOM   11629 N N   . SER E  2  66  ? -6.634  -18.157 9.136   1.00 44.62  ?  66   SER E N   1 
ATOM   11630 C CA  . SER E  2  66  ? -7.958  -17.608 9.410   1.00 43.66  ?  66   SER E CA  1 
ATOM   11631 C C   . SER E  2  66  ? -7.966  -16.656 10.601  1.00 43.52  ?  66   SER E C   1 
ATOM   11632 O O   . SER E  2  66  ? -8.935  -15.908 10.771  1.00 41.94  ?  66   SER E O   1 
ATOM   11633 C CB  . SER E  2  66  ? -8.957  -18.742 9.647   1.00 43.21  ?  66   SER E CB  1 
ATOM   11634 O OG  . SER E  2  66  ? -8.487  -19.635 10.642  1.00 45.03  ?  66   SER E OG  1 
ATOM   11635 N N   . ASP E  2  67  ? -6.918  -16.664 11.421  1.00 45.01  ?  67   ASP E N   1 
ATOM   11636 C CA  . ASP E  2  67  ? -6.796  -15.751 12.549  1.00 44.75  ?  67   ASP E CA  1 
ATOM   11637 C C   . ASP E  2  67  ? -6.030  -14.482 12.203  1.00 44.17  ?  67   ASP E C   1 
ATOM   11638 O O   . ASP E  2  67  ? -5.791  -13.660 13.095  1.00 43.92  ?  67   ASP E O   1 
ATOM   11639 C CB  . ASP E  2  67  ? -6.115  -16.453 13.728  1.00 46.13  ?  67   ASP E CB  1 
ATOM   11640 C CG  . ASP E  2  67  ? -6.848  -17.705 14.164  1.00 47.00  ?  67   ASP E CG  1 
ATOM   11641 O OD1 . ASP E  2  67  ? -8.068  -17.799 13.915  1.00 46.11  ?  67   ASP E OD1 1 
ATOM   11642 O OD2 . ASP E  2  67  ? -6.204  -18.594 14.759  1.00 48.28  -1 67   ASP E OD2 1 
ATOM   11643 N N   . ASN E  2  68  ? -5.631  -14.315 10.938  1.00 41.86  ?  68   ASN E N   1 
ATOM   11644 C CA  . ASN E  2  68  ? -4.821  -13.186 10.478  1.00 40.91  ?  68   ASN E CA  1 
ATOM   11645 C C   . ASN E  2  68  ? -3.430  -13.184 11.105  1.00 40.57  ?  68   ASN E C   1 
ATOM   11646 O O   . ASN E  2  68  ? -2.838  -12.124 11.322  1.00 39.17  ?  68   ASN E O   1 
ATOM   11647 C CB  . ASN E  2  68  ? -5.523  -11.845 10.722  1.00 39.50  ?  68   ASN E CB  1 
ATOM   11648 C CG  . ASN E  2  68  ? -6.913  -11.800 10.122  1.00 38.97  ?  68   ASN E CG  1 
ATOM   11649 O OD1 . ASN E  2  68  ? -7.084  -11.486 8.944   1.00 38.70  ?  68   ASN E OD1 1 
ATOM   11650 N ND2 . ASN E  2  68  ? -7.916  -12.119 10.931  1.00 38.73  ?  68   ASN E ND2 1 
ATOM   11651 N N   . SER E  2  69  ? -2.903  -14.368 11.403  1.00 43.42  ?  69   SER E N   1 
ATOM   11652 C CA  . SER E  2  69  ? -1.518  -14.533 11.818  1.00 42.78  ?  69   SER E CA  1 
ATOM   11653 C C   . SER E  2  69  ? -0.676  -14.937 10.616  1.00 42.10  ?  69   SER E C   1 
ATOM   11654 O O   . SER E  2  69  ? -1.091  -15.774 9.809   1.00 42.81  ?  69   SER E O   1 
ATOM   11655 C CB  . SER E  2  69  ? -1.392  -15.583 12.925  1.00 44.26  ?  69   SER E CB  1 
ATOM   11656 O OG  . SER E  2  69  ? -0.267  -15.324 13.748  1.00 43.53  ?  69   SER E OG  1 
ATOM   11657 N N   . VAL E  2  70  ? 0.505   -14.331 10.496  1.00 43.88  ?  70   VAL E N   1 
ATOM   11658 C CA  . VAL E  2  70  ? 1.383   -14.611 9.367   1.00 42.33  ?  70   VAL E CA  1 
ATOM   11659 C C   . VAL E  2  70  ? 1.881   -16.048 9.453   1.00 43.37  ?  70   VAL E C   1 
ATOM   11660 O O   . VAL E  2  70  ? 2.407   -16.480 10.487  1.00 43.93  ?  70   VAL E O   1 
ATOM   11661 C CB  . VAL E  2  70  ? 2.552   -13.616 9.335   1.00 40.68  ?  70   VAL E CB  1 
ATOM   11662 C CG1 . VAL E  2  70  ? 3.601   -14.055 8.324   1.00 40.15  ?  70   VAL E CG1 1 
ATOM   11663 C CG2 . VAL E  2  70  ? 2.049   -12.220 9.011   1.00 40.37  ?  70   VAL E CG2 1 
ATOM   11664 N N   . THR E  2  71  ? 1.705   -16.800 8.365   1.00 42.11  ?  71   THR E N   1 
ATOM   11665 C CA  . THR E  2  71  ? 2.160   -18.179 8.288   1.00 43.76  ?  71   THR E CA  1 
ATOM   11666 C C   . THR E  2  71  ? 3.152   -18.434 7.163   1.00 43.81  ?  71   THR E C   1 
ATOM   11667 O O   . THR E  2  71  ? 3.779   -19.500 7.149   1.00 45.55  ?  71   THR E O   1 
ATOM   11668 C CB  . THR E  2  71  ? 0.969   -19.137 8.118   1.00 44.40  ?  71   THR E CB  1 
ATOM   11669 O OG1 . THR E  2  71  ? 0.261   -18.817 6.914   1.00 43.37  ?  71   THR E OG1 1 
ATOM   11670 C CG2 . THR E  2  71  ? 0.022   -19.035 9.305   1.00 45.44  ?  71   THR E CG2 1 
ATOM   11671 N N   . ARG E  2  72  ? 3.313   -17.503 6.225   1.00 42.13  ?  72   ARG E N   1 
ATOM   11672 C CA  . ARG E  2  72  ? 4.222   -17.680 5.102   1.00 41.28  ?  72   ARG E CA  1 
ATOM   11673 C C   . ARG E  2  72  ? 4.862   -16.349 4.741   1.00 40.33  ?  72   ARG E C   1 
ATOM   11674 O O   . ARG E  2  72  ? 4.218   -15.298 4.817   1.00 40.01  ?  72   ARG E O   1 
ATOM   11675 C CB  . ARG E  2  72  ? 3.503   -18.244 3.867   1.00 41.40  ?  72   ARG E CB  1 
ATOM   11676 C CG  . ARG E  2  72  ? 3.099   -19.705 3.973   1.00 42.69  ?  72   ARG E CG  1 
ATOM   11677 C CD  . ARG E  2  72  ? 2.757   -20.285 2.608   1.00 42.66  ?  72   ARG E CD  1 
ATOM   11678 N NE  . ARG E  2  72  ? 3.920   -20.349 1.731   1.00 42.47  ?  72   ARG E NE  1 
ATOM   11679 C CZ  . ARG E  2  72  ? 4.510   -21.474 1.351   1.00 43.95  ?  72   ARG E CZ  1 
ATOM   11680 N NH1 . ARG E  2  72  ? 4.074   -22.655 1.760   1.00 45.35  ?  72   ARG E NH1 1 
ATOM   11681 N NH2 . ARG E  2  72  ? 5.565   -21.414 0.544   1.00 44.72  ?  72   ARG E NH2 1 
ATOM   11682 N N   . VAL E  2  73  ? 6.134   -16.404 4.353   1.00 40.82  ?  73   VAL E N   1 
ATOM   11683 C CA  . VAL E  2  73  ? 6.845   -15.274 3.760   1.00 40.22  ?  73   VAL E CA  1 
ATOM   11684 C C   . VAL E  2  73  ? 7.593   -15.839 2.557   1.00 41.36  ?  73   VAL E C   1 
ATOM   11685 O O   . VAL E  2  73  ? 8.657   -16.449 2.708   1.00 43.01  ?  73   VAL E O   1 
ATOM   11686 C CB  . VAL E  2  73  ? 7.806   -14.591 4.740   1.00 40.73  ?  73   VAL E CB  1 
ATOM   11687 C CG1 . VAL E  2  73  ? 8.505   -13.425 4.062   1.00 40.34  ?  73   VAL E CG1 1 
ATOM   11688 C CG2 . VAL E  2  73  ? 7.063   -14.111 5.980   1.00 40.03  ?  73   VAL E CG2 1 
ATOM   11689 N N   . ASP E  2  74  ? 7.039   -15.640 1.362   1.00 41.37  ?  74   ASP E N   1 
ATOM   11690 C CA  . ASP E  2  74  ? 7.577   -16.211 0.127   1.00 42.19  ?  74   ASP E CA  1 
ATOM   11691 C C   . ASP E  2  74  ? 8.347   -15.120 -0.613  1.00 42.93  ?  74   ASP E C   1 
ATOM   11692 O O   . ASP E  2  74  ? 7.811   -14.442 -1.491  1.00 43.01  ?  74   ASP E O   1 
ATOM   11693 C CB  . ASP E  2  74  ? 6.456   -16.794 -0.724  1.00 42.22  ?  74   ASP E CB  1 
ATOM   11694 C CG  . ASP E  2  74  ? 5.764   -17.969 -0.054  1.00 42.43  ?  74   ASP E CG  1 
ATOM   11695 O OD1 . ASP E  2  74  ? 4.804   -17.740 0.714   1.00 41.91  ?  74   ASP E OD1 1 
ATOM   11696 O OD2 . ASP E  2  74  ? 6.181   -19.121 -0.296  1.00 43.28  -1 74   ASP E OD2 1 
ATOM   11697 N N   . LEU E  2  75  ? 9.619   -14.948 -0.249  1.00 43.13  ?  75   LEU E N   1 
ATOM   11698 C CA  . LEU E  2  75  ? 10.475  -13.927 -0.844  1.00 43.61  ?  75   LEU E CA  1 
ATOM   11699 C C   . LEU E  2  75  ? 11.663  -14.537 -1.584  1.00 45.93  ?  75   LEU E C   1 
ATOM   11700 O O   . LEU E  2  75  ? 12.747  -13.951 -1.617  1.00 46.99  ?  75   LEU E O   1 
ATOM   11701 C CB  . LEU E  2  75  ? 10.960  -12.945 0.221   1.00 43.09  ?  75   LEU E CB  1 
ATOM   11702 C CG  . LEU E  2  75  ? 9.927   -11.939 0.730   1.00 41.02  ?  75   LEU E CG  1 
ATOM   11703 C CD1 . LEU E  2  75  ? 10.478  -11.154 1.909   1.00 40.99  ?  75   LEU E CD1 1 
ATOM   11704 C CD2 . LEU E  2  75  ? 9.503   -11.006 -0.388  1.00 40.41  ?  75   LEU E CD2 1 
ATOM   11705 N N   . GLY E  2  76  ? 11.477  -15.712 -2.177  1.00 52.45  ?  76   GLY E N   1 
ATOM   11706 C CA  . GLY E  2  76  ? 12.553  -16.329 -2.934  1.00 53.24  ?  76   GLY E CA  1 
ATOM   11707 C C   . GLY E  2  76  ? 12.786  -15.623 -4.260  1.00 53.01  ?  76   GLY E C   1 
ATOM   11708 O O   . GLY E  2  76  ? 11.852  -15.159 -4.916  1.00 52.87  ?  76   GLY E O   1 
ATOM   11709 N N   . ASN E  2  77  ? 14.062  -15.538 -4.649  1.00 53.92  ?  77   ASN E N   1 
ATOM   11710 C CA  . ASN E  2  77  ? 14.464  -15.015 -5.958  1.00 55.52  ?  77   ASN E CA  1 
ATOM   11711 C C   . ASN E  2  77  ? 13.977  -13.581 -6.163  1.00 54.11  ?  77   ASN E C   1 
ATOM   11712 O O   . ASN E  2  77  ? 13.387  -13.241 -7.191  1.00 54.34  ?  77   ASN E O   1 
ATOM   11713 C CB  . ASN E  2  77  ? 13.967  -15.923 -7.086  1.00 56.82  ?  77   ASN E CB  1 
ATOM   11714 C CG  . ASN E  2  77  ? 14.344  -17.374 -6.878  1.00 58.29  ?  77   ASN E CG  1 
ATOM   11715 O OD1 . ASN E  2  77  ? 13.534  -18.179 -6.417  1.00 57.30  ?  77   ASN E OD1 1 
ATOM   11716 N ND2 . ASN E  2  77  ? 15.574  -17.722 -7.237  1.00 60.92  ?  77   ASN E ND2 1 
ATOM   11717 N N   . ALA E  2  78  ? 14.228  -12.733 -5.170  1.00 55.01  ?  78   ALA E N   1 
ATOM   11718 C CA  . ALA E  2  78  ? 13.728  -11.367 -5.185  1.00 53.60  ?  78   ALA E CA  1 
ATOM   11719 C C   . ALA E  2  78  ? 14.825  -10.318 -5.307  1.00 55.02  ?  78   ALA E C   1 
ATOM   11720 O O   . ALA E  2  78  ? 14.514  -9.121  -5.315  1.00 54.17  ?  78   ALA E O   1 
ATOM   11721 C CB  . ALA E  2  78  ? 12.891  -11.105 -3.928  1.00 51.36  ?  78   ALA E CB  1 
ATOM   11722 N N   . ASN E  2  79  ? 16.092  -10.729 -5.407  1.00 54.24  ?  79   ASN E N   1 
ATOM   11723 C CA  . ASN E  2  79  ? 17.231  -9.809  -5.503  1.00 56.04  ?  79   ASN E CA  1 
ATOM   11724 C C   . ASN E  2  79  ? 17.286  -8.843  -4.321  1.00 54.62  ?  79   ASN E C   1 
ATOM   11725 O O   . ASN E  2  79  ? 17.704  -7.691  -4.464  1.00 55.34  ?  79   ASN E O   1 
ATOM   11726 C CB  . ASN E  2  79  ? 17.221  -9.035  -6.826  1.00 57.48  ?  79   ASN E CB  1 
ATOM   11727 C CG  . ASN E  2  79  ? 16.955  -9.927  -8.021  1.00 58.89  ?  79   ASN E CG  1 
ATOM   11728 O OD1 . ASN E  2  79  ? 16.967  -11.153 -7.909  1.00 59.12  ?  79   ASN E OD1 1 
ATOM   11729 N ND2 . ASN E  2  79  ? 16.718  -9.316  -9.177  1.00 60.15  ?  79   ASN E ND2 1 
ATOM   11730 N N   . LEU E  2  80  ? 16.862  -9.306  -3.148  1.00 55.97  ?  80   LEU E N   1 
ATOM   11731 C CA  . LEU E  2  80  ? 16.892  -8.490  -1.940  1.00 55.63  ?  80   LEU E CA  1 
ATOM   11732 C C   . LEU E  2  80  ? 18.266  -8.582  -1.288  1.00 57.49  ?  80   LEU E C   1 
ATOM   11733 O O   . LEU E  2  80  ? 18.736  -9.677  -0.962  1.00 58.28  ?  80   LEU E O   1 
ATOM   11734 C CB  . LEU E  2  80  ? 15.803  -8.941  -0.967  1.00 54.14  ?  80   LEU E CB  1 
ATOM   11735 C CG  . LEU E  2  80  ? 14.475  -8.178  -0.954  1.00 53.94  ?  80   LEU E CG  1 
ATOM   11736 C CD1 . LEU E  2  80  ? 14.679  -6.758  -0.476  1.00 55.56  ?  80   LEU E CD1 1 
ATOM   11737 C CD2 . LEU E  2  80  ? 13.841  -8.162  -2.326  1.00 53.23  ?  80   LEU E CD2 1 
ATOM   11738 N N   . SER E  2  81  ? 18.910  -7.435  -1.100  1.00 57.63  ?  81   SER E N   1 
ATOM   11739 C CA  . SER E  2  81  ? 20.163  -7.347  -0.368  1.00 59.48  ?  81   SER E CA  1 
ATOM   11740 C C   . SER E  2  81  ? 19.936  -6.609  0.945   1.00 59.13  ?  81   SER E C   1 
ATOM   11741 O O   . SER E  2  81  ? 19.068  -5.737  1.044   1.00 57.87  ?  81   SER E O   1 
ATOM   11742 C CB  . SER E  2  81  ? 21.243  -6.637  -1.191  1.00 61.29  ?  81   SER E CB  1 
ATOM   11743 O OG  . SER E  2  81  ? 20.804  -5.362  -1.623  1.00 60.79  ?  81   SER E OG  1 
ATOM   11744 N N   . GLY E  2  82  ? 20.715  -6.970  1.951   1.00 60.70  ?  82   GLY E N   1 
ATOM   11745 C CA  . GLY E  2  82  ? 20.580  -6.377  3.264   1.00 60.69  ?  82   GLY E CA  1 
ATOM   11746 C C   . GLY E  2  82  ? 20.968  -7.373  4.339   1.00 61.43  ?  82   GLY E C   1 
ATOM   11747 O O   . GLY E  2  82  ? 21.720  -8.310  4.091   1.00 62.56  ?  82   GLY E O   1 
ATOM   11748 N N   . GLN E  2  83  ? 20.444  -7.136  5.539   1.00 61.02  ?  83   GLN E N   1 
ATOM   11749 C CA  . GLN E  2  83  ? 20.732  -7.956  6.707   1.00 61.80  ?  83   GLN E CA  1 
ATOM   11750 C C   . GLN E  2  83  ? 19.430  -8.420  7.342   1.00 60.01  ?  83   GLN E C   1 
ATOM   11751 O O   . GLN E  2  83  ? 18.445  -7.676  7.369   1.00 58.52  ?  83   GLN E O   1 
ATOM   11752 C CB  . GLN E  2  83  ? 21.564  -7.182  7.738   1.00 63.59  ?  83   GLN E CB  1 
ATOM   11753 C CG  . GLN E  2  83  ? 22.627  -6.281  7.133   1.00 65.24  ?  83   GLN E CG  1 
ATOM   11754 C CD  . GLN E  2  83  ? 24.030  -6.678  7.545   1.00 67.76  ?  83   GLN E CD  1 
ATOM   11755 O OE1 . GLN E  2  83  ? 24.217  -7.451  8.484   1.00 68.39  ?  83   GLN E OE1 1 
ATOM   11756 N NE2 . GLN E  2  83  ? 25.026  -6.154  6.840   1.00 69.36  ?  83   GLN E NE2 1 
ATOM   11757 N N   . LEU E  2  84  ? 19.429  -9.651  7.851   1.00 57.52  ?  84   LEU E N   1 
ATOM   11758 C CA  . LEU E  2  84  ? 18.276  -10.148 8.585   1.00 56.19  ?  84   LEU E CA  1 
ATOM   11759 C C   . LEU E  2  84  ? 18.051  -9.314  9.847   1.00 56.36  ?  84   LEU E C   1 
ATOM   11760 O O   . LEU E  2  84  ? 18.889  -8.508  10.258  1.00 57.77  ?  84   LEU E O   1 
ATOM   11761 C CB  . LEU E  2  84  ? 18.456  -11.623 8.947   1.00 56.91  ?  84   LEU E CB  1 
ATOM   11762 C CG  . LEU E  2  84  ? 17.874  -12.660 7.980   1.00 55.99  ?  84   LEU E CG  1 
ATOM   11763 C CD1 . LEU E  2  84  ? 18.506  -12.558 6.608   1.00 56.36  ?  84   LEU E CD1 1 
ATOM   11764 C CD2 . LEU E  2  84  ? 18.026  -14.070 8.526   1.00 56.97  ?  84   LEU E CD2 1 
ATOM   11765 N N   . VAL E  2  85  ? 16.895  -9.526  10.470  1.00 53.56  ?  85   VAL E N   1 
ATOM   11766 C CA  . VAL E  2  85  ? 16.434  -8.694  11.573  1.00 53.47  ?  85   VAL E CA  1 
ATOM   11767 C C   . VAL E  2  85  ? 15.958  -9.597  12.702  1.00 53.64  ?  85   VAL E C   1 
ATOM   11768 O O   . VAL E  2  85  ? 15.275  -10.598 12.462  1.00 52.73  ?  85   VAL E O   1 
ATOM   11769 C CB  . VAL E  2  85  ? 15.307  -7.739  11.121  1.00 51.59  ?  85   VAL E CB  1 
ATOM   11770 C CG1 . VAL E  2  85  ? 14.718  -6.998  12.303  1.00 51.53  ?  85   VAL E CG1 1 
ATOM   11771 C CG2 . VAL E  2  85  ? 15.823  -6.760  10.088  1.00 51.73  ?  85   VAL E CG2 1 
ATOM   11772 N N   . MET E  2  86  ? 16.328  -9.241  13.935  1.00 59.06  ?  86   MET E N   1 
ATOM   11773 C CA  . MET E  2  86  ? 15.903  -10.006 15.103  1.00 59.48  ?  86   MET E CA  1 
ATOM   11774 C C   . MET E  2  86  ? 14.390  -9.989  15.292  1.00 57.61  ?  86   MET E C   1 
ATOM   11775 O O   . MET E  2  86  ? 13.858  -10.842 16.009  1.00 57.70  ?  86   MET E O   1 
ATOM   11776 C CB  . MET E  2  86  ? 16.610  -9.476  16.356  1.00 61.47  ?  86   MET E CB  1 
ATOM   11777 C CG  . MET E  2  86  ? 16.205  -8.068  16.795  1.00 61.22  ?  86   MET E CG  1 
ATOM   11778 S SD  . MET E  2  86  ? 14.720  -7.982  17.821  1.00 60.13  ?  86   MET E SD  1 
ATOM   11779 C CE  . MET E  2  86  ? 14.976  -6.417  18.653  1.00 61.39  ?  86   MET E CE  1 
ATOM   11780 N N   . GLN E  2  87  ? 13.691  -9.031  14.677  1.00 54.57  ?  87   GLN E N   1 
ATOM   11781 C CA  . GLN E  2  87  ? 12.240  -8.952  14.806  1.00 52.84  ?  87   GLN E CA  1 
ATOM   11782 C C   . GLN E  2  87  ? 11.528  -10.166 14.221  1.00 51.76  ?  87   GLN E C   1 
ATOM   11783 O O   . GLN E  2  87  ? 10.354  -10.389 14.536  1.00 50.71  ?  87   GLN E O   1 
ATOM   11784 C CB  . GLN E  2  87  ? 11.725  -7.682  14.129  1.00 51.55  ?  87   GLN E CB  1 
ATOM   11785 C CG  . GLN E  2  87  ? 11.560  -6.499  15.064  1.00 52.06  ?  87   GLN E CG  1 
ATOM   11786 C CD  . GLN E  2  87  ? 12.817  -5.658  15.164  1.00 53.79  ?  87   GLN E CD  1 
ATOM   11787 O OE1 . GLN E  2  87  ? 13.926  -6.185  15.241  1.00 55.28  ?  87   GLN E OE1 1 
ATOM   11788 N NE2 . GLN E  2  87  ? 12.650  -4.341  15.156  1.00 53.75  ?  87   GLN E NE2 1 
ATOM   11789 N N   . LEU E  2  88  ? 12.206  -10.954 13.382  1.00 53.00  ?  88   LEU E N   1 
ATOM   11790 C CA  . LEU E  2  88  ? 11.567  -12.093 12.730  1.00 52.19  ?  88   LEU E CA  1 
ATOM   11791 C C   . LEU E  2  88  ? 11.096  -13.163 13.705  1.00 52.77  ?  88   LEU E C   1 
ATOM   11792 O O   . LEU E  2  88  ? 10.419  -14.104 13.277  1.00 52.21  ?  88   LEU E O   1 
ATOM   11793 C CB  . LEU E  2  88  ? 12.520  -12.720 11.712  1.00 52.91  ?  88   LEU E CB  1 
ATOM   11794 C CG  . LEU E  2  88  ? 12.677  -11.961 10.399  1.00 52.07  ?  88   LEU E CG  1 
ATOM   11795 C CD1 . LEU E  2  88  ? 13.630  -12.699 9.475   1.00 53.04  ?  88   LEU E CD1 1 
ATOM   11796 C CD2 . LEU E  2  88  ? 11.314  -11.791 9.753   1.00 50.31  ?  88   LEU E CD2 1 
ATOM   11797 N N   . GLY E  2  89  ? 11.429  -13.052 14.987  1.00 54.45  ?  89   GLY E N   1 
ATOM   11798 C CA  . GLY E  2  89  ? 10.914  -13.965 15.982  1.00 55.11  ?  89   GLY E CA  1 
ATOM   11799 C C   . GLY E  2  89  ? 9.562   -13.593 16.539  1.00 53.96  ?  89   GLY E C   1 
ATOM   11800 O O   . GLY E  2  89  ? 9.073   -14.256 17.460  1.00 54.62  ?  89   GLY E O   1 
ATOM   11801 N N   . GLN E  2  90  ? 8.938   -12.543 16.008  1.00 53.42  ?  90   GLN E N   1 
ATOM   11802 C CA  . GLN E  2  90  ? 7.640   -12.073 16.471  1.00 52.31  ?  90   GLN E CA  1 
ATOM   11803 C C   . GLN E  2  90  ? 6.474   -12.695 15.712  1.00 51.29  ?  90   GLN E C   1 
ATOM   11804 O O   . GLN E  2  90  ? 5.335   -12.249 15.881  1.00 51.48  ?  90   GLN E O   1 
ATOM   11805 C CB  . GLN E  2  90  ? 7.566   -10.547 16.367  1.00 52.09  ?  90   GLN E CB  1 
ATOM   11806 C CG  . GLN E  2  90  ? 8.012   -9.823  17.624  1.00 53.03  ?  90   GLN E CG  1 
ATOM   11807 C CD  . GLN E  2  90  ? 9.499   -9.526  17.625  1.00 54.49  ?  90   GLN E CD  1 
ATOM   11808 O OE1 . GLN E  2  90  ? 9.942   -8.525  17.062  1.00 54.29  ?  90   GLN E OE1 1 
ATOM   11809 N NE2 . GLN E  2  90  ? 10.278  -10.399 18.253  1.00 56.16  ?  90   GLN E NE2 1 
ATOM   11810 N N   . LEU E  2  91  ? 6.730   -13.695 14.873  1.00 50.08  ?  91   LEU E N   1 
ATOM   11811 C CA  . LEU E  2  91  ? 5.664   -14.342 14.121  1.00 49.52  ?  91   LEU E CA  1 
ATOM   11812 C C   . LEU E  2  91  ? 5.469   -15.766 14.629  1.00 50.02  ?  91   LEU E C   1 
ATOM   11813 O O   . LEU E  2  91  ? 5.991   -16.715 14.032  1.00 50.74  ?  91   LEU E O   1 
ATOM   11814 C CB  . LEU E  2  91  ? 5.991   -14.332 12.627  1.00 49.49  ?  91   LEU E CB  1 
ATOM   11815 C CG  . LEU E  2  91  ? 6.563   -13.005 12.120  1.00 49.71  ?  91   LEU E CG  1 
ATOM   11816 C CD1 . LEU E  2  91  ? 7.240   -13.166 10.769  1.00 49.47  ?  91   LEU E CD1 1 
ATOM   11817 C CD2 . LEU E  2  91  ? 5.483   -11.942 12.052  1.00 49.90  ?  91   LEU E CD2 1 
ATOM   11818 N N   . PRO E  2  92  ? 4.720   -15.953 15.722  1.00 51.48  ?  92   PRO E N   1 
ATOM   11819 C CA  . PRO E  2  92  ? 4.626   -17.296 16.325  1.00 52.95  ?  92   PRO E CA  1 
ATOM   11820 C C   . PRO E  2  92  ? 4.069   -18.356 15.390  1.00 52.73  ?  92   PRO E C   1 
ATOM   11821 O O   . PRO E  2  92  ? 4.523   -19.506 15.425  1.00 54.18  ?  92   PRO E O   1 
ATOM   11822 C CB  . PRO E  2  92  ? 3.711   -17.068 17.537  1.00 53.10  ?  92   PRO E CB  1 
ATOM   11823 C CG  . PRO E  2  92  ? 2.918   -15.851 17.191  1.00 51.32  ?  92   PRO E CG  1 
ATOM   11824 C CD  . PRO E  2  92  ? 3.835   -14.981 16.387  1.00 51.25  ?  92   PRO E CD  1 
ATOM   11825 N N   . ASN E  2  93  ? 3.097   -18.003 14.553  1.00 50.04  ?  93   ASN E N   1 
ATOM   11826 C CA  . ASN E  2  93  ? 2.450   -18.959 13.664  1.00 49.92  ?  93   ASN E CA  1 
ATOM   11827 C C   . ASN E  2  93  ? 3.148   -19.091 12.316  1.00 49.69  ?  93   ASN E C   1 
ATOM   11828 O O   . ASN E  2  93  ? 2.685   -19.866 11.473  1.00 49.78  ?  93   ASN E O   1 
ATOM   11829 C CB  . ASN E  2  93  ? 0.982   -18.574 13.455  1.00 48.92  ?  93   ASN E CB  1 
ATOM   11830 C CG  . ASN E  2  93  ? 0.110   -18.944 14.641  1.00 49.19  ?  93   ASN E CG  1 
ATOM   11831 O OD1 . ASN E  2  93  ? -0.550  -18.091 15.233  1.00 48.59  ?  93   ASN E OD1 1 
ATOM   11832 N ND2 . ASN E  2  93  ? 0.111   -20.223 14.999  1.00 50.81  ?  93   ASN E ND2 1 
ATOM   11833 N N   . LEU E  2  94  ? 4.229   -18.346 12.090  1.00 50.38  ?  94   LEU E N   1 
ATOM   11834 C CA  . LEU E  2  94  ? 4.979   -18.448 10.843  1.00 50.15  ?  94   LEU E CA  1 
ATOM   11835 C C   . LEU E  2  94  ? 5.440   -19.881 10.617  1.00 51.37  ?  94   LEU E C   1 
ATOM   11836 O O   . LEU E  2  94  ? 6.224   -20.421 11.403  1.00 52.91  ?  94   LEU E O   1 
ATOM   11837 C CB  . LEU E  2  94  ? 6.182   -17.508 10.882  1.00 50.27  ?  94   LEU E CB  1 
ATOM   11838 C CG  . LEU E  2  94  ? 7.039   -17.432 9.618   1.00 50.29  ?  94   LEU E CG  1 
ATOM   11839 C CD1 . LEU E  2  94  ? 6.197   -17.036 8.412   1.00 49.95  ?  94   LEU E CD1 1 
ATOM   11840 C CD2 . LEU E  2  94  ? 8.197   -16.473 9.818   1.00 50.37  ?  94   LEU E CD2 1 
ATOM   11841 N N   . GLN E  2  95  ? 4.949   -20.496 9.543   1.00 50.01  ?  95   GLN E N   1 
ATOM   11842 C CA  . GLN E  2  95  ? 5.286   -21.874 9.207   1.00 51.67  ?  95   GLN E CA  1 
ATOM   11843 C C   . GLN E  2  95  ? 6.363   -21.982 8.138   1.00 52.20  ?  95   GLN E C   1 
ATOM   11844 O O   . GLN E  2  95  ? 7.209   -22.879 8.208   1.00 53.93  ?  95   GLN E O   1 
ATOM   11845 C CB  . GLN E  2  95  ? 4.032   -22.621 8.743   1.00 51.58  ?  95   GLN E CB  1 
ATOM   11846 C CG  . GLN E  2  95  ? 2.922   -22.663 9.778   1.00 51.34  ?  95   GLN E CG  1 
ATOM   11847 C CD  . GLN E  2  95  ? 1.675   -23.356 9.267   1.00 51.36  ?  95   GLN E CD  1 
ATOM   11848 O OE1 . GLN E  2  95  ? 1.608   -23.761 8.106   1.00 51.49  ?  95   GLN E OE1 1 
ATOM   11849 N NE2 . GLN E  2  95  ? 0.678   -23.495 10.133  1.00 51.39  ?  95   GLN E NE2 1 
ATOM   11850 N N   . TYR E  2  96  ? 6.353   -21.094 7.145   1.00 49.09  ?  96   TYR E N   1 
ATOM   11851 C CA  . TYR E  2  96  ? 7.318   -21.130 6.053   1.00 49.54  ?  96   TYR E CA  1 
ATOM   11852 C C   . TYR E  2  96  ? 8.014   -19.783 5.953   1.00 49.28  ?  96   TYR E C   1 
ATOM   11853 O O   . TYR E  2  96  ? 7.355   -18.751 5.785   1.00 48.54  ?  96   TYR E O   1 
ATOM   11854 C CB  . TYR E  2  96  ? 6.638   -21.486 4.726   1.00 49.56  ?  96   TYR E CB  1 
ATOM   11855 C CG  . TYR E  2  96  ? 6.078   -22.891 4.686   1.00 50.24  ?  96   TYR E CG  1 
ATOM   11856 C CD1 . TYR E  2  96  ? 4.854   -23.192 5.271   1.00 49.98  ?  96   TYR E CD1 1 
ATOM   11857 C CD2 . TYR E  2  96  ? 6.778   -23.918 4.070   1.00 51.40  ?  96   TYR E CD2 1 
ATOM   11858 C CE1 . TYR E  2  96  ? 4.343   -24.476 5.237   1.00 50.83  ?  96   TYR E CE1 1 
ATOM   11859 C CE2 . TYR E  2  96  ? 6.276   -25.205 4.033   1.00 52.27  ?  96   TYR E CE2 1 
ATOM   11860 C CZ  . TYR E  2  96  ? 5.058   -25.479 4.617   1.00 51.97  ?  96   TYR E CZ  1 
ATOM   11861 O OH  . TYR E  2  96  ? 4.551   -26.758 4.582   1.00 53.06  ?  96   TYR E OH  1 
ATOM   11862 N N   . LEU E  2  97  ? 9.340   -19.797 6.055   1.00 49.53  ?  97   LEU E N   1 
ATOM   11863 C CA  . LEU E  2  97  ? 10.176  -18.609 5.905   1.00 49.71  ?  97   LEU E CA  1 
ATOM   11864 C C   . LEU E  2  97  ? 11.077  -18.846 4.697   1.00 50.54  ?  97   LEU E C   1 
ATOM   11865 O O   . LEU E  2  97  ? 12.071  -19.572 4.789   1.00 51.78  ?  97   LEU E O   1 
ATOM   11866 C CB  . LEU E  2  97  ? 10.980  -18.343 7.175   1.00 50.51  ?  97   LEU E CB  1 
ATOM   11867 C CG  . LEU E  2  97  ? 11.630  -16.964 7.293   1.00 50.84  ?  97   LEU E CG  1 
ATOM   11868 C CD1 . LEU E  2  97  ? 10.580  -15.866 7.179   1.00 49.66  ?  97   LEU E CD1 1 
ATOM   11869 C CD2 . LEU E  2  97  ? 12.407  -16.837 8.595   1.00 52.09  ?  97   LEU E CD2 1 
ATOM   11870 N N   . GLU E  2  98  ? 10.725  -18.247 3.562   1.00 51.66  ?  98   GLU E N   1 
ATOM   11871 C CA  . GLU E  2  98  ? 11.388  -18.510 2.287   1.00 52.59  ?  98   GLU E CA  1 
ATOM   11872 C C   . GLU E  2  98  ? 12.095  -17.235 1.826   1.00 52.89  ?  98   GLU E C   1 
ATOM   11873 O O   . GLU E  2  98  ? 11.527  -16.423 1.094   1.00 52.36  ?  98   GLU E O   1 
ATOM   11874 C CB  . GLU E  2  98  ? 10.375  -18.992 1.247   1.00 52.32  ?  98   GLU E CB  1 
ATOM   11875 C CG  . GLU E  2  98  ? 9.361   -20.000 1.779   1.00 51.91  ?  98   GLU E CG  1 
ATOM   11876 C CD  . GLU E  2  98  ? 9.909   -21.412 1.866   1.00 53.06  ?  98   GLU E CD  1 
ATOM   11877 O OE1 . GLU E  2  98  ? 11.111  -21.607 1.597   1.00 54.22  ?  98   GLU E OE1 1 
ATOM   11878 O OE2 . GLU E  2  98  ? 9.135   -22.330 2.211   1.00 53.02  -1 98   GLU E OE2 1 
ATOM   11879 N N   . LEU E  2  99  ? 13.348  -17.069 2.255   1.00 52.24  ?  99   LEU E N   1 
ATOM   11880 C CA  . LEU E  2  99  ? 14.191  -15.957 1.831   1.00 52.98  ?  99   LEU E CA  1 
ATOM   11881 C C   . LEU E  2  99  ? 15.340  -16.416 0.939   1.00 54.71  ?  99   LEU E C   1 
ATOM   11882 O O   . LEU E  2  99  ? 16.314  -15.679 0.758   1.00 55.87  ?  99   LEU E O   1 
ATOM   11883 C CB  . LEU E  2  99  ? 14.735  -15.201 3.043   1.00 53.35  ?  99   LEU E CB  1 
ATOM   11884 C CG  . LEU E  2  99  ? 13.800  -14.179 3.694   1.00 52.10  ?  99   LEU E CG  1 
ATOM   11885 C CD1 . LEU E  2  99  ? 13.125  -14.784 4.901   1.00 51.45  ?  99   LEU E CD1 1 
ATOM   11886 C CD2 . LEU E  2  99  ? 14.555  -12.918 4.083   1.00 53.03  ?  99   LEU E CD2 1 
ATOM   11887 N N   . TYR E  2  100 ? 15.241  -17.620 0.384   1.00 57.95  ?  100  TYR E N   1 
ATOM   11888 C CA  . TYR E  2  100 ? 16.326  -18.215 -0.379  1.00 59.93  ?  100  TYR E CA  1 
ATOM   11889 C C   . TYR E  2  100 ? 16.612  -17.423 -1.654  1.00 60.57  ?  100  TYR E C   1 
ATOM   11890 O O   . TYR E  2  100 ? 15.777  -16.660 -2.149  1.00 59.44  ?  100  TYR E O   1 
ATOM   11891 C CB  . TYR E  2  100 ? 15.999  -19.669 -0.724  1.00 60.38  ?  100  TYR E CB  1 
ATOM   11892 C CG  . TYR E  2  100 ? 14.731  -19.862 -1.532  1.00 59.35  ?  100  TYR E CG  1 
ATOM   11893 C CD1 . TYR E  2  100 ? 14.746  -19.780 -2.921  1.00 60.24  ?  100  TYR E CD1 1 
ATOM   11894 C CD2 . TYR E  2  100 ? 13.520  -20.136 -0.908  1.00 57.80  ?  100  TYR E CD2 1 
ATOM   11895 C CE1 . TYR E  2  100 ? 13.592  -19.960 -3.662  1.00 59.70  ?  100  TYR E CE1 1 
ATOM   11896 C CE2 . TYR E  2  100 ? 12.361  -20.317 -1.641  1.00 57.23  ?  100  TYR E CE2 1 
ATOM   11897 C CZ  . TYR E  2  100 ? 12.403  -20.228 -3.017  1.00 58.23  ?  100  TYR E CZ  1 
ATOM   11898 O OH  . TYR E  2  100 ? 11.252  -20.407 -3.750  1.00 58.04  ?  100  TYR E OH  1 
ATOM   11899 N N   . SER E  2  101 ? 17.822  -17.623 -2.183  1.00 61.85  ?  101  SER E N   1 
ATOM   11900 C CA  . SER E  2  101 ? 18.252  -17.052 -3.461  1.00 63.02  ?  101  SER E CA  1 
ATOM   11901 C C   . SER E  2  101 ? 18.167  -15.523 -3.459  1.00 62.32  ?  101  SER E C   1 
ATOM   11902 O O   . SER E  2  101 ? 17.422  -14.910 -4.226  1.00 61.57  ?  101  SER E O   1 
ATOM   11903 C CB  . SER E  2  101 ? 17.447  -17.648 -4.619  1.00 62.96  ?  101  SER E CB  1 
ATOM   11904 O OG  . SER E  2  101 ? 17.695  -19.036 -4.753  1.00 64.19  ?  101  SER E OG  1 
ATOM   11905 N N   . ASN E  2  102 ? 18.951  -14.913 -2.570  1.00 62.52  ?  102  ASN E N   1 
ATOM   11906 C CA  . ASN E  2  102 ? 19.069  -13.464 -2.503  1.00 62.39  ?  102  ASN E CA  1 
ATOM   11907 C C   . ASN E  2  102 ? 20.503  -13.101 -2.132  1.00 64.63  ?  102  ASN E C   1 
ATOM   11908 O O   . ASN E  2  102 ? 21.363  -13.970 -1.958  1.00 66.27  ?  102  ASN E O   1 
ATOM   11909 C CB  . ASN E  2  102 ? 18.071  -12.870 -1.502  1.00 60.33  ?  102  ASN E CB  1 
ATOM   11910 C CG  . ASN E  2  102 ? 16.683  -12.705 -2.089  1.00 58.56  ?  102  ASN E CG  1 
ATOM   11911 O OD1 . ASN E  2  102 ? 16.461  -11.865 -2.962  1.00 58.67  ?  102  ASN E OD1 1 
ATOM   11912 N ND2 . ASN E  2  102 ? 15.738  -13.503 -1.607  1.00 57.17  ?  102  ASN E ND2 1 
ATOM   11913 N N   . ASN E  2  103 ? 20.760  -11.800 -2.019  1.00 59.93  ?  103  ASN E N   1 
ATOM   11914 C CA  . ASN E  2  103 ? 22.076  -11.265 -1.686  1.00 62.32  ?  103  ASN E CA  1 
ATOM   11915 C C   . ASN E  2  103 ? 22.106  -10.726 -0.259  1.00 62.13  ?  103  ASN E C   1 
ATOM   11916 O O   . ASN E  2  103 ? 22.747  -9.713  0.031   1.00 63.55  ?  103  ASN E O   1 
ATOM   11917 C CB  . ASN E  2  103 ? 22.496  -10.186 -2.681  1.00 63.54  ?  103  ASN E CB  1 
ATOM   11918 C CG  . ASN E  2  103 ? 23.992  -9.927  -2.663  1.00 66.67  ?  103  ASN E CG  1 
ATOM   11919 O OD1 . ASN E  2  103 ? 24.792  -10.855 -2.542  1.00 68.33  ?  103  ASN E OD1 1 
ATOM   11920 N ND2 . ASN E  2  103 ? 24.377  -8.661  -2.779  1.00 67.74  ?  103  ASN E ND2 1 
ATOM   11921 N N   . ILE E  2  104 ? 21.395  -11.392 0.644   1.00 66.50  ?  104  ILE E N   1 
ATOM   11922 C CA  . ILE E  2  104 ? 21.288  -10.932 2.023   1.00 66.35  ?  104  ILE E CA  1 
ATOM   11923 C C   . ILE E  2  104 ? 22.540  -11.344 2.785   1.00 68.94  ?  104  ILE E C   1 
ATOM   11924 O O   . ILE E  2  104 ? 22.987  -12.494 2.697   1.00 69.81  ?  104  ILE E O   1 
ATOM   11925 C CB  . ILE E  2  104 ? 20.025  -11.500 2.688   1.00 63.94  ?  104  ILE E CB  1 
ATOM   11926 C CG1 . ILE E  2  104 ? 18.864  -11.522 1.695   1.00 61.86  ?  104  ILE E CG1 1 
ATOM   11927 C CG2 . ILE E  2  104 ? 19.649  -10.672 3.896   1.00 63.59  ?  104  ILE E CG2 1 
ATOM   11928 C CD1 . ILE E  2  104 ? 17.624  -12.207 2.222   1.00 59.79  ?  104  ILE E CD1 1 
ATOM   11929 N N   . THR E  2  105 ? 23.110  -10.404 3.531   1.00 67.03  ?  105  THR E N   1 
ATOM   11930 C CA  . THR E  2  105 ? 24.321  -10.616 4.307   1.00 69.99  ?  105  THR E CA  1 
ATOM   11931 C C   . THR E  2  105 ? 24.009  -10.496 5.796   1.00 69.95  ?  105  THR E C   1 
ATOM   11932 O O   . THR E  2  105 ? 22.859  -10.317 6.207   1.00 67.58  ?  105  THR E O   1 
ATOM   11933 C CB  . THR E  2  105 ? 25.412  -9.623  3.895   1.00 72.69  ?  105  THR E CB  1 
ATOM   11934 O OG1 . THR E  2  105 ? 26.583  -9.840  4.692   1.00 75.94  ?  105  THR E OG1 1 
ATOM   11935 C CG2 . THR E  2  105 ? 24.934  -8.192  4.088   1.00 72.06  ?  105  THR E CG2 1 
ATOM   11936 N N   . GLY E  2  106 ? 25.052  -10.602 6.608   1.00 74.89  ?  106  GLY E N   1 
ATOM   11937 C CA  . GLY E  2  106 ? 24.913  -10.535 8.048   1.00 75.56  ?  106  GLY E CA  1 
ATOM   11938 C C   . GLY E  2  106 ? 24.804  -11.906 8.682   1.00 75.46  ?  106  GLY E C   1 
ATOM   11939 O O   . GLY E  2  106 ? 25.065  -12.945 8.069   1.00 75.51  ?  106  GLY E O   1 
ATOM   11940 N N   . THR E  2  107 ? 24.405  -11.893 9.949   1.00 73.47  ?  107  THR E N   1 
ATOM   11941 C CA  . THR E  2  107 ? 24.289  -13.102 10.750  1.00 73.72  ?  107  THR E CA  1 
ATOM   11942 C C   . THR E  2  107 ? 22.850  -13.608 10.760  1.00 70.20  ?  107  THR E C   1 
ATOM   11943 O O   . THR E  2  107 ? 21.918  -12.936 10.312  1.00 67.76  ?  107  THR E O   1 
ATOM   11944 C CB  . THR E  2  107 ? 24.772  -12.844 12.182  1.00 76.48  ?  107  THR E CB  1 
ATOM   11945 O OG1 . THR E  2  107 ? 25.016  -14.094 12.837  1.00 77.70  ?  107  THR E OG1 1 
ATOM   11946 C CG2 . THR E  2  107 ? 23.727  -12.059 12.965  1.00 74.93  ?  107  THR E CG2 1 
ATOM   11947 N N   . ILE E  2  108 ? 22.682  -14.823 11.274  1.00 70.84  ?  108  ILE E N   1 
ATOM   11948 C CA  . ILE E  2  108 ? 21.360  -15.421 11.443  1.00 68.01  ?  108  ILE E CA  1 
ATOM   11949 C C   . ILE E  2  108 ? 20.894  -15.081 12.853  1.00 68.40  ?  108  ILE E C   1 
ATOM   11950 O O   . ILE E  2  108 ? 21.612  -15.364 13.822  1.00 71.06  ?  108  ILE E O   1 
ATOM   11951 C CB  . ILE E  2  108 ? 21.376  -16.942 11.210  1.00 67.96  ?  108  ILE E CB  1 
ATOM   11952 C CG1 . ILE E  2  108 ? 21.285  -17.297 9.720   1.00 66.64  ?  108  ILE E CG1 1 
ATOM   11953 C CG2 . ILE E  2  108 ? 20.220  -17.608 11.941  1.00 66.25  ?  108  ILE E CG2 1 
ATOM   11954 C CD1 . ILE E  2  108 ? 22.299  -16.634 8.822   1.00 68.12  ?  108  ILE E CD1 1 
ATOM   11955 N N   . PRO E  2  109 ? 19.720  -14.473 13.022  1.00 66.89  ?  109  PRO E N   1 
ATOM   11956 C CA  . PRO E  2  109 ? 19.293  -14.037 14.359  1.00 67.59  ?  109  PRO E CA  1 
ATOM   11957 C C   . PRO E  2  109 ? 18.905  -15.231 15.218  1.00 67.73  ?  109  PRO E C   1 
ATOM   11958 O O   . PRO E  2  109 ? 18.039  -16.027 14.846  1.00 65.56  ?  109  PRO E O   1 
ATOM   11959 C CB  . PRO E  2  109 ? 18.089  -13.124 14.075  1.00 66.50  ?  109  PRO E CB  1 
ATOM   11960 C CG  . PRO E  2  109 ? 17.910  -13.113 12.566  1.00 64.17  ?  109  PRO E CG  1 
ATOM   11961 C CD  . PRO E  2  109 ? 18.661  -14.279 12.022  1.00 63.82  ?  109  PRO E CD  1 
ATOM   11962 N N   . GLU E  2  110 ? 19.561  -15.353 16.376  1.00 69.40  ?  110  GLU E N   1 
ATOM   11963 C CA  . GLU E  2  110 ? 19.258  -16.437 17.302  1.00 70.01  ?  110  GLU E CA  1 
ATOM   11964 C C   . GLU E  2  110 ? 17.832  -16.357 17.826  1.00 67.92  ?  110  GLU E C   1 
ATOM   11965 O O   . GLU E  2  110 ? 17.329  -17.340 18.380  1.00 68.28  ?  110  GLU E O   1 
ATOM   11966 C CB  . GLU E  2  110 ? 20.242  -16.416 18.471  1.00 73.89  ?  110  GLU E CB  1 
ATOM   11967 C CG  . GLU E  2  110 ? 20.000  -15.276 19.449  1.00 75.08  ?  110  GLU E CG  1 
ATOM   11968 C CD  . GLU E  2  110 ? 20.962  -15.291 20.618  1.00 79.32  ?  110  GLU E CD  1 
ATOM   11969 O OE1 . GLU E  2  110 ? 22.094  -15.793 20.452  1.00 81.66  ?  110  GLU E OE1 1 
ATOM   11970 O OE2 . GLU E  2  110 ? 20.588  -14.798 21.704  1.00 80.60  -1 110  GLU E OE2 1 
ATOM   11971 N N   . GLN E  2  111 ? 17.171  -15.210 17.662  1.00 68.16  ?  111  GLN E N   1 
ATOM   11972 C CA  . GLN E  2  111 ? 15.770  -15.072 18.033  1.00 68.08  ?  111  GLN E CA  1 
ATOM   11973 C C   . GLN E  2  111 ? 14.840  -15.833 17.097  1.00 66.72  ?  111  GLN E C   1 
ATOM   11974 O O   . GLN E  2  111 ? 13.643  -15.929 17.386  1.00 66.31  ?  111  GLN E O   1 
ATOM   11975 C CB  . GLN E  2  111 ? 15.386  -13.593 18.080  1.00 68.12  ?  111  GLN E CB  1 
ATOM   11976 C CG  . GLN E  2  111 ? 15.877  -12.877 19.332  1.00 69.80  ?  111  GLN E CG  1 
ATOM   11977 C CD  . GLN E  2  111 ? 15.967  -13.796 20.542  1.00 71.19  ?  111  GLN E CD  1 
ATOM   11978 O OE1 . GLN E  2  111 ? 17.056  -14.068 21.049  1.00 72.86  ?  111  GLN E OE1 1 
ATOM   11979 N NE2 . GLN E  2  111 ? 14.818  -14.259 21.022  1.00 70.24  ?  111  GLN E NE2 1 
ATOM   11980 N N   . LEU E  2  112 ? 15.356  -16.368 15.986  1.00 67.21  ?  112  LEU E N   1 
ATOM   11981 C CA  . LEU E  2  112 ? 14.552  -17.214 15.114  1.00 65.44  ?  112  LEU E CA  1 
ATOM   11982 C C   . LEU E  2  112 ? 14.159  -18.526 15.777  1.00 65.98  ?  112  LEU E C   1 
ATOM   11983 O O   . LEU E  2  112 ? 13.283  -19.225 15.256  1.00 63.52  ?  112  LEU E O   1 
ATOM   11984 C CB  . LEU E  2  112 ? 15.302  -17.507 13.812  1.00 62.48  ?  112  LEU E CB  1 
ATOM   11985 C CG  . LEU E  2  112 ? 14.960  -16.654 12.587  1.00 60.46  ?  112  LEU E CG  1 
ATOM   11986 C CD1 . LEU E  2  112 ? 14.810  -15.191 12.967  1.00 62.75  ?  112  LEU E CD1 1 
ATOM   11987 C CD2 . LEU E  2  112 ? 16.010  -16.826 11.498  1.00 59.42  ?  112  LEU E CD2 1 
ATOM   11988 N N   . GLY E  2  113 ? 14.780  -18.876 16.904  1.00 66.00  ?  113  GLY E N   1 
ATOM   11989 C CA  . GLY E  2  113 ? 14.350  -20.024 17.678  1.00 66.54  ?  113  GLY E CA  1 
ATOM   11990 C C   . GLY E  2  113 ? 13.011  -19.848 18.361  1.00 68.01  ?  113  GLY E C   1 
ATOM   11991 O O   . GLY E  2  113 ? 12.465  -20.830 18.874  1.00 67.90  ?  113  GLY E O   1 
ATOM   11992 N N   . ASN E  2  114 ? 12.476  -18.627 18.384  1.00 69.60  ?  114  ASN E N   1 
ATOM   11993 C CA  . ASN E  2  114 ? 11.160  -18.375 18.955  1.00 66.87  ?  114  ASN E CA  1 
ATOM   11994 C C   . ASN E  2  114 ? 10.026  -18.718 17.999  1.00 62.28  ?  114  ASN E C   1 
ATOM   11995 O O   . ASN E  2  114 ? 8.863   -18.711 18.416  1.00 60.26  ?  114  ASN E O   1 
ATOM   11996 C CB  . ASN E  2  114 ? 11.046  -16.909 19.383  1.00 66.57  ?  114  ASN E CB  1 
ATOM   11997 C CG  . ASN E  2  114 ? 11.899  -16.587 20.595  1.00 70.25  ?  114  ASN E CG  1 
ATOM   11998 O OD1 . ASN E  2  114 ? 12.807  -17.341 20.947  1.00 72.43  ?  114  ASN E OD1 1 
ATOM   11999 N ND2 . ASN E  2  114 ? 11.615  -15.460 21.236  1.00 69.74  ?  114  ASN E ND2 1 
ATOM   12000 N N   . LEU E  2  115 ? 10.333  -19.014 16.735  1.00 63.40  ?  115  LEU E N   1 
ATOM   12001 C CA  . LEU E  2  115 ? 9.320   -19.383 15.745  1.00 62.44  ?  115  LEU E CA  1 
ATOM   12002 C C   . LEU E  2  115 ? 8.906   -20.829 15.998  1.00 62.64  ?  115  LEU E C   1 
ATOM   12003 O O   . LEU E  2  115 ? 9.390   -21.774 15.370  1.00 61.46  ?  115  LEU E O   1 
ATOM   12004 C CB  . LEU E  2  115 ? 9.852   -19.182 14.332  1.00 60.48  ?  115  LEU E CB  1 
ATOM   12005 C CG  . LEU E  2  115 ? 10.284  -17.750 14.010  1.00 59.46  ?  115  LEU E CG  1 
ATOM   12006 C CD1 . LEU E  2  115 ? 10.756  -17.628 12.568  1.00 57.70  ?  115  LEU E CD1 1 
ATOM   12007 C CD2 . LEU E  2  115 ? 9.144   -16.791 14.293  1.00 60.78  ?  115  LEU E CD2 1 
ATOM   12008 N N   . THR E  2  116 ? 7.983   -20.993 16.949  1.00 62.86  ?  116  THR E N   1 
ATOM   12009 C CA  . THR E  2  116 ? 7.588   -22.326 17.394  1.00 64.46  ?  116  THR E CA  1 
ATOM   12010 C C   . THR E  2  116 ? 6.987   -23.142 16.255  1.00 62.71  ?  116  THR E C   1 
ATOM   12011 O O   . THR E  2  116 ? 7.327   -24.317 16.069  1.00 63.64  ?  116  THR E O   1 
ATOM   12012 C CB  . THR E  2  116 ? 6.595   -22.214 18.553  1.00 66.57  ?  116  THR E CB  1 
ATOM   12013 O OG1 . THR E  2  116 ? 7.247   -21.636 19.691  1.00 69.00  ?  116  THR E OG1 1 
ATOM   12014 C CG2 . THR E  2  116 ? 6.049   -23.584 18.928  1.00 68.53  ?  116  THR E CG2 1 
ATOM   12015 N N   . GLU E  2  117 ? 6.098   -22.533 15.474  1.00 63.07  ?  117  GLU E N   1 
ATOM   12016 C CA  . GLU E  2  117 ? 5.359   -23.241 14.438  1.00 61.77  ?  117  GLU E CA  1 
ATOM   12017 C C   . GLU E  2  117 ? 6.118   -23.332 13.119  1.00 60.32  ?  117  GLU E C   1 
ATOM   12018 O O   . GLU E  2  117 ? 5.556   -23.817 12.130  1.00 59.46  ?  117  GLU E O   1 
ATOM   12019 C CB  . GLU E  2  117 ? 3.999   -22.571 14.217  1.00 62.63  ?  117  GLU E CB  1 
ATOM   12020 C CG  . GLU E  2  117 ? 2.877   -23.542 13.872  1.00 63.35  ?  117  GLU E CG  1 
ATOM   12021 C CD  . GLU E  2  117 ? 2.363   -24.305 15.083  1.00 64.61  ?  117  GLU E CD  1 
ATOM   12022 O OE1 . GLU E  2  117 ? 2.870   -24.072 16.201  1.00 65.59  ?  117  GLU E OE1 1 
ATOM   12023 O OE2 . GLU E  2  117 ? 1.452   -25.142 14.914  1.00 66.07  -1 117  GLU E OE2 1 
ATOM   12024 N N   . LEU E  2  118 ? 7.368   -22.872 13.078  1.00 60.17  ?  118  LEU E N   1 
ATOM   12025 C CA  . LEU E  2  118 ? 8.141   -22.894 11.842  1.00 59.40  ?  118  LEU E CA  1 
ATOM   12026 C C   . LEU E  2  118 ? 8.321   -24.322 11.341  1.00 58.94  ?  118  LEU E C   1 
ATOM   12027 O O   . LEU E  2  118 ? 8.644   -25.229 12.113  1.00 60.55  ?  118  LEU E O   1 
ATOM   12028 C CB  . LEU E  2  118 ? 9.503   -22.234 12.059  1.00 59.62  ?  118  LEU E CB  1 
ATOM   12029 C CG  . LEU E  2  118 ? 10.282  -21.896 10.786  1.00 58.86  ?  118  LEU E CG  1 
ATOM   12030 C CD1 . LEU E  2  118 ? 9.444   -21.023 9.864   1.00 57.97  ?  118  LEU E CD1 1 
ATOM   12031 C CD2 . LEU E  2  118 ? 11.601  -21.218 11.119  1.00 58.98  ?  118  LEU E CD2 1 
ATOM   12032 N N   . VAL E  2  119 ? 8.117   -24.515 10.037  1.00 58.16  ?  119  VAL E N   1 
ATOM   12033 C CA  . VAL E  2  119 ? 8.201   -25.826 9.412   1.00 59.36  ?  119  VAL E CA  1 
ATOM   12034 C C   . VAL E  2  119 ? 9.322   -25.893 8.383   1.00 59.69  ?  119  VAL E C   1 
ATOM   12035 O O   . VAL E  2  119 ? 10.077  -26.872 8.343   1.00 61.67  ?  119  VAL E O   1 
ATOM   12036 C CB  . VAL E  2  119 ? 6.850   -26.219 8.771   1.00 58.81  ?  119  VAL E CB  1 
ATOM   12037 C CG1 . VAL E  2  119 ? 7.034   -27.317 7.735   1.00 60.02  ?  119  VAL E CG1 1 
ATOM   12038 C CG2 . VAL E  2  119 ? 5.861   -26.649 9.844   1.00 59.83  ?  119  VAL E CG2 1 
ATOM   12039 N N   . SER E  2  120 ? 9.463   -24.861 7.554   1.00 61.28  ?  120  SER E N   1 
ATOM   12040 C CA  . SER E  2  120 ? 10.514  -24.790 6.549   1.00 60.48  ?  120  SER E CA  1 
ATOM   12041 C C   . SER E  2  120 ? 11.304  -23.503 6.731   1.00 59.58  ?  120  SER E C   1 
ATOM   12042 O O   . SER E  2  120 ? 10.719  -22.420 6.846   1.00 58.98  ?  120  SER E O   1 
ATOM   12043 C CB  . SER E  2  120 ? 9.934   -24.859 5.134   1.00 60.13  ?  120  SER E CB  1 
ATOM   12044 O OG  . SER E  2  120 ? 10.950  -24.689 4.159   1.00 59.85  ?  120  SER E OG  1 
ATOM   12045 N N   . LEU E  2  121 ? 12.628  -23.626 6.754   1.00 58.69  ?  121  LEU E N   1 
ATOM   12046 C CA  . LEU E  2  121 ? 13.542  -22.495 6.890   1.00 59.11  ?  121  LEU E CA  1 
ATOM   12047 C C   . LEU E  2  121 ? 14.507  -22.559 5.710   1.00 60.76  ?  121  LEU E C   1 
ATOM   12048 O O   . LEU E  2  121 ? 15.478  -23.324 5.734   1.00 63.11  ?  121  LEU E O   1 
ATOM   12049 C CB  . LEU E  2  121 ? 14.268  -22.545 8.236   1.00 60.58  ?  121  LEU E CB  1 
ATOM   12050 C CG  . LEU E  2  121 ? 14.884  -21.270 8.824   1.00 61.03  ?  121  LEU E CG  1 
ATOM   12051 C CD1 . LEU E  2  121 ? 15.280  -21.505 10.272  1.00 62.61  ?  121  LEU E CD1 1 
ATOM   12052 C CD2 . LEU E  2  121 ? 16.087  -20.796 8.027   1.00 62.76  ?  121  LEU E CD2 1 
ATOM   12053 N N   . ASP E  2  122 ? 14.242  -21.763 4.678   1.00 60.25  ?  122  ASP E N   1 
ATOM   12054 C CA  . ASP E  2  122 ? 15.026  -21.778 3.444   1.00 62.18  ?  122  ASP E CA  1 
ATOM   12055 C C   . ASP E  2  122 ? 15.772  -20.450 3.328   1.00 63.01  ?  122  ASP E C   1 
ATOM   12056 O O   . ASP E  2  122 ? 15.235  -19.456 2.836   1.00 61.90  ?  122  ASP E O   1 
ATOM   12057 C CB  . ASP E  2  122 ? 14.134  -22.022 2.229   1.00 61.47  ?  122  ASP E CB  1 
ATOM   12058 C CG  . ASP E  2  122 ? 13.597  -23.439 2.173   1.00 61.70  ?  122  ASP E CG  1 
ATOM   12059 O OD1 . ASP E  2  122 ? 13.756  -24.179 3.167   1.00 62.04  ?  122  ASP E OD1 1 
ATOM   12060 O OD2 . ASP E  2  122 ? 13.014  -23.813 1.133   1.00 61.94  -1 122  ASP E OD2 1 
ATOM   12061 N N   . LEU E  2  123 ? 17.022  -20.446 3.791   1.00 64.84  ?  123  LEU E N   1 
ATOM   12062 C CA  . LEU E  2  123 ? 17.934  -19.320 3.630   1.00 65.27  ?  123  LEU E CA  1 
ATOM   12063 C C   . LEU E  2  123 ? 19.049  -19.627 2.636   1.00 66.01  ?  123  LEU E C   1 
ATOM   12064 O O   . LEU E  2  123 ? 20.057  -18.914 2.599   1.00 66.80  ?  123  LEU E O   1 
ATOM   12065 C CB  . LEU E  2  123 ? 18.522  -18.909 4.982   1.00 66.08  ?  123  LEU E CB  1 
ATOM   12066 C CG  . LEU E  2  123 ? 17.802  -17.833 5.805   1.00 65.74  ?  123  LEU E CG  1 
ATOM   12067 C CD1 . LEU E  2  123 ? 16.292  -18.007 5.793   1.00 64.65  ?  123  LEU E CD1 1 
ATOM   12068 C CD2 . LEU E  2  123 ? 18.325  -17.829 7.236   1.00 66.81  ?  123  LEU E CD2 1 
ATOM   12069 N N   . TYR E  2  124 ? 18.889  -20.679 1.836   1.00 67.30  ?  124  TYR E N   1 
ATOM   12070 C CA  . TYR E  2  124 ? 19.949  -21.144 0.956   1.00 68.26  ?  124  TYR E CA  1 
ATOM   12071 C C   . TYR E  2  124 ? 20.207  -20.145 -0.173  1.00 68.27  ?  124  TYR E C   1 
ATOM   12072 O O   . TYR E  2  124 ? 19.378  -19.286 -0.484  1.00 67.33  ?  124  TYR E O   1 
ATOM   12073 C CB  . TYR E  2  124 ? 19.604  -22.534 0.406   1.00 68.35  ?  124  TYR E CB  1 
ATOM   12074 C CG  . TYR E  2  124 ? 18.404  -22.623 -0.526  1.00 67.47  ?  124  TYR E CG  1 
ATOM   12075 C CD1 . TYR E  2  124 ? 18.447  -22.108 -1.817  1.00 67.48  ?  124  TYR E CD1 1 
ATOM   12076 C CD2 . TYR E  2  124 ? 17.226  -23.227 -0.108  1.00 66.82  ?  124  TYR E CD2 1 
ATOM   12077 C CE1 . TYR E  2  124 ? 17.355  -22.199 -2.663  1.00 66.84  ?  124  TYR E CE1 1 
ATOM   12078 C CE2 . TYR E  2  124 ? 16.130  -23.320 -0.944  1.00 66.23  ?  124  TYR E CE2 1 
ATOM   12079 C CZ  . TYR E  2  124 ? 16.199  -22.804 -2.219  1.00 66.23  ?  124  TYR E CZ  1 
ATOM   12080 O OH  . TYR E  2  124 ? 15.107  -22.896 -3.052  1.00 65.80  ?  124  TYR E OH  1 
ATOM   12081 N N   . LEU E  2  125 ? 21.387  -20.274 -0.785  1.00 69.18  ?  125  LEU E N   1 
ATOM   12082 C CA  . LEU E  2  125 ? 21.826  -19.410 -1.883  1.00 69.57  ?  125  LEU E CA  1 
ATOM   12083 C C   . LEU E  2  125 ? 21.823  -17.937 -1.464  1.00 69.29  ?  125  LEU E C   1 
ATOM   12084 O O   . LEU E  2  125 ? 21.111  -17.101 -2.021  1.00 68.47  ?  125  LEU E O   1 
ATOM   12085 C CB  . LEU E  2  125 ? 20.972  -19.632 -3.137  1.00 68.95  ?  125  LEU E CB  1 
ATOM   12086 C CG  . LEU E  2  125 ? 21.348  -20.836 -4.003  1.00 69.88  ?  125  LEU E CG  1 
ATOM   12087 C CD1 . LEU E  2  125 ? 20.148  -21.342 -4.787  1.00 69.12  ?  125  LEU E CD1 1 
ATOM   12088 C CD2 . LEU E  2  125 ? 22.492  -20.480 -4.940  1.00 71.30  ?  125  LEU E CD2 1 
ATOM   12089 N N   . ASN E  2  126 ? 22.646  -17.634 -0.463  1.00 73.52  ?  126  ASN E N   1 
ATOM   12090 C CA  . ASN E  2  126 ? 22.767  -16.280 0.060   1.00 73.62  ?  126  ASN E CA  1 
ATOM   12091 C C   . ASN E  2  126 ? 24.238  -16.014 0.365   1.00 75.45  ?  126  ASN E C   1 
ATOM   12092 O O   . ASN E  2  126 ? 25.120  -16.806 0.020   1.00 76.56  ?  126  ASN E O   1 
ATOM   12093 C CB  . ASN E  2  126 ? 21.883  -16.095 1.301   1.00 72.72  ?  126  ASN E CB  1 
ATOM   12094 C CG  . ASN E  2  126 ? 20.444  -15.772 0.952   1.00 71.12  ?  126  ASN E CG  1 
ATOM   12095 O OD1 . ASN E  2  126 ? 20.141  -14.689 0.453   1.00 70.74  ?  126  ASN E OD1 1 
ATOM   12096 N ND2 . ASN E  2  126 ? 19.546  -16.714 1.215   1.00 70.31  ?  126  ASN E ND2 1 
ATOM   12097 N N   . ASN E  2  127 ? 24.500  -14.884 1.020   1.00 78.02  ?  127  ASN E N   1 
ATOM   12098 C CA  . ASN E  2  127 ? 25.840  -14.504 1.450   1.00 80.24  ?  127  ASN E CA  1 
ATOM   12099 C C   . ASN E  2  127 ? 25.881  -14.277 2.958   1.00 80.35  ?  127  ASN E C   1 
ATOM   12100 O O   . ASN E  2  127 ? 26.645  -13.446 3.453   1.00 81.87  ?  127  ASN E O   1 
ATOM   12101 C CB  . ASN E  2  127 ? 26.323  -13.262 0.703   1.00 80.78  ?  127  ASN E CB  1 
ATOM   12102 C CG  . ASN E  2  127 ? 27.835  -13.198 0.597   1.00 83.33  ?  127  ASN E CG  1 
ATOM   12103 O OD1 . ASN E  2  127 ? 28.447  -12.168 0.882   1.00 84.59  ?  127  ASN E OD1 1 
ATOM   12104 N ND2 . ASN E  2  127 ? 28.447  -14.303 0.187   1.00 83.77  ?  127  ASN E ND2 1 
ATOM   12105 N N   . LEU E  2  128 ? 25.047  -15.010 3.689   1.00 81.10  ?  128  LEU E N   1 
ATOM   12106 C CA  . LEU E  2  128 ? 25.009  -14.907 5.139   1.00 81.62  ?  128  LEU E CA  1 
ATOM   12107 C C   . LEU E  2  128 ? 26.306  -15.427 5.749   1.00 83.45  ?  128  LEU E C   1 
ATOM   12108 O O   . LEU E  2  128 ? 26.983  -16.292 5.187   1.00 84.27  ?  128  LEU E O   1 
ATOM   12109 C CB  . LEU E  2  128 ? 23.815  -15.686 5.690   1.00 80.35  ?  128  LEU E CB  1 
ATOM   12110 C CG  . LEU E  2  128 ? 22.441  -15.271 5.157   1.00 79.15  ?  128  LEU E CG  1 
ATOM   12111 C CD1 . LEU E  2  128 ? 21.439  -16.407 5.293   1.00 77.27  ?  128  LEU E CD1 1 
ATOM   12112 C CD2 . LEU E  2  128 ? 21.945  -14.025 5.875   1.00 78.91  ?  128  LEU E CD2 1 
ATOM   12113 N N   . SER E  2  129 ? 26.653  -14.881 6.913   1.00 81.13  ?  129  SER E N   1 
ATOM   12114 C CA  . SER E  2  129 ? 27.885  -15.255 7.596   1.00 83.16  ?  129  SER E CA  1 
ATOM   12115 C C   . SER E  2  129 ? 27.622  -15.537 9.070   1.00 83.51  ?  129  SER E C   1 
ATOM   12116 O O   . SER E  2  129 ? 26.467  -15.570 9.506   1.00 82.14  ?  129  SER E O   1 
ATOM   12117 C CB  . SER E  2  129 ? 28.937  -14.154 7.446   1.00 85.05  ?  129  SER E CB  1 
ATOM   12118 O OG  . SER E  2  129 ? 28.619  -13.031 8.250   1.00 85.42  ?  129  SER E OG  1 
ATOM   12119 N N   . GLY E  2  130 ? 28.685  -15.742 9.842   1.00 85.68  ?  130  GLY E N   1 
ATOM   12120 C CA  . GLY E  2  130 ? 28.554  -16.041 11.246  1.00 86.35  ?  130  GLY E CA  1 
ATOM   12121 C C   . GLY E  2  130 ? 28.193  -17.491 11.491  1.00 85.53  ?  130  GLY E C   1 
ATOM   12122 O O   . GLY E  2  130 ? 28.239  -18.329 10.585  1.00 84.76  ?  130  GLY E O   1 
ATOM   12123 N N   . PRO E  2  131 ? 27.826  -17.816 12.729  1.00 83.14  ?  131  PRO E N   1 
ATOM   12124 C CA  . PRO E  2  131 ? 27.540  -19.215 13.066  1.00 82.63  ?  131  PRO E CA  1 
ATOM   12125 C C   . PRO E  2  131 ? 26.098  -19.612 12.792  1.00 80.47  ?  131  PRO E C   1 
ATOM   12126 O O   . PRO E  2  131 ? 25.296  -18.802 12.315  1.00 79.28  ?  131  PRO E O   1 
ATOM   12127 C CB  . PRO E  2  131 ? 27.859  -19.279 14.564  1.00 84.29  ?  131  PRO E CB  1 
ATOM   12128 C CG  . PRO E  2  131 ? 27.662  -17.859 15.066  1.00 84.91  ?  131  PRO E CG  1 
ATOM   12129 C CD  . PRO E  2  131 ? 27.613  -16.920 13.878  1.00 84.09  ?  131  PRO E CD  1 
ATOM   12130 N N   . ILE E  2  132 ? 25.768  -20.865 13.092  1.00 78.99  ?  132  ILE E N   1 
ATOM   12131 C CA  . ILE E  2  132 ? 24.393  -21.356 13.059  1.00 77.33  ?  132  ILE E CA  1 
ATOM   12132 C C   . ILE E  2  132 ? 23.899  -21.385 14.503  1.00 77.96  ?  132  ILE E C   1 
ATOM   12133 O O   . ILE E  2  132 ? 24.367  -22.229 15.286  1.00 79.04  ?  132  ILE E O   1 
ATOM   12134 C CB  . ILE E  2  132 ? 24.288  -22.743 12.408  1.00 76.66  ?  132  ILE E CB  1 
ATOM   12135 C CG1 . ILE E  2  132 ? 24.528  -22.691 10.890  1.00 75.94  ?  132  ILE E CG1 1 
ATOM   12136 C CG2 . ILE E  2  132 ? 22.921  -23.358 12.688  1.00 75.47  ?  132  ILE E CG2 1 
ATOM   12137 C CD1 . ILE E  2  132 ? 25.959  -22.417 10.465  1.00 77.34  ?  132  ILE E CD1 1 
ATOM   12138 N N   . PRO E  2  133 ? 23.006  -20.481 14.907  1.00 75.34  ?  133  PRO E N   1 
ATOM   12139 C CA  . PRO E  2  133 ? 22.646  -20.382 16.327  1.00 76.36  ?  133  PRO E CA  1 
ATOM   12140 C C   . PRO E  2  133 ? 22.137  -21.703 16.884  1.00 76.25  ?  133  PRO E C   1 
ATOM   12141 O O   . PRO E  2  133 ? 21.394  -22.435 16.227  1.00 74.88  ?  133  PRO E O   1 
ATOM   12142 C CB  . PRO E  2  133 ? 21.546  -19.314 16.345  1.00 75.52  ?  133  PRO E CB  1 
ATOM   12143 C CG  . PRO E  2  133 ? 21.671  -18.568 15.057  1.00 74.49  ?  133  PRO E CG  1 
ATOM   12144 C CD  . PRO E  2  133 ? 22.647  -19.268 14.156  1.00 74.49  ?  133  PRO E CD  1 
ATOM   12145 N N   . SER E  2  134 ? 22.559  -22.007 18.112  1.00 81.31  ?  134  SER E N   1 
ATOM   12146 C CA  . SER E  2  134 ? 22.092  -23.202 18.800  1.00 81.50  ?  134  SER E CA  1 
ATOM   12147 C C   . SER E  2  134 ? 20.610  -23.138 19.143  1.00 80.68  ?  134  SER E C   1 
ATOM   12148 O O   . SER E  2  134 ? 20.030  -24.167 19.505  1.00 80.62  ?  134  SER E O   1 
ATOM   12149 C CB  . SER E  2  134 ? 22.910  -23.423 20.073  1.00 83.65  ?  134  SER E CB  1 
ATOM   12150 O OG  . SER E  2  134 ? 22.712  -22.363 20.992  1.00 84.75  ?  134  SER E OG  1 
ATOM   12151 N N   . THR E  2  135 ? 19.989  -21.962 19.034  1.00 76.52  ?  135  THR E N   1 
ATOM   12152 C CA  . THR E  2  135 ? 18.569  -21.815 19.321  1.00 75.88  ?  135  THR E CA  1 
ATOM   12153 C C   . THR E  2  135 ? 17.684  -22.392 18.224  1.00 74.03  ?  135  THR E C   1 
ATOM   12154 O O   . THR E  2  135 ? 16.478  -22.542 18.447  1.00 73.62  ?  135  THR E O   1 
ATOM   12155 C CB  . THR E  2  135 ? 18.223  -20.340 19.533  1.00 76.09  ?  135  THR E CB  1 
ATOM   12156 O OG1 . THR E  2  135 ? 18.853  -19.550 18.516  1.00 75.42  ?  135  THR E OG1 1 
ATOM   12157 C CG2 . THR E  2  135 ? 18.701  -19.873 20.900  1.00 78.25  ?  135  THR E CG2 1 
ATOM   12158 N N   . LEU E  2  136 ? 18.243  -22.715 17.054  1.00 73.59  ?  136  LEU E N   1 
ATOM   12159 C CA  . LEU E  2  136 ? 17.449  -23.333 15.998  1.00 72.08  ?  136  LEU E CA  1 
ATOM   12160 C C   . LEU E  2  136 ? 16.910  -24.699 16.403  1.00 72.30  ?  136  LEU E C   1 
ATOM   12161 O O   . LEU E  2  136 ? 16.002  -25.215 15.743  1.00 71.33  ?  136  LEU E O   1 
ATOM   12162 C CB  . LEU E  2  136 ? 18.270  -23.456 14.711  1.00 71.41  ?  136  LEU E CB  1 
ATOM   12163 C CG  . LEU E  2  136 ? 18.283  -22.231 13.790  1.00 70.56  ?  136  LEU E CG  1 
ATOM   12164 C CD1 . LEU E  2  136 ? 19.424  -21.287 14.120  1.00 71.64  ?  136  LEU E CD1 1 
ATOM   12165 C CD2 . LEU E  2  136 ? 18.354  -22.657 12.334  1.00 69.50  ?  136  LEU E CD2 1 
ATOM   12166 N N   . GLY E  2  137 ? 17.444  -25.295 17.469  1.00 75.81  ?  137  GLY E N   1 
ATOM   12167 C CA  . GLY E  2  137 ? 16.913  -26.549 17.972  1.00 76.22  ?  137  GLY E CA  1 
ATOM   12168 C C   . GLY E  2  137 ? 15.582  -26.426 18.686  1.00 76.40  ?  137  GLY E C   1 
ATOM   12169 O O   . GLY E  2  137 ? 14.992  -27.454 19.036  1.00 76.77  ?  137  GLY E O   1 
ATOM   12170 N N   . ARG E  2  138 ? 15.104  -25.202 18.916  1.00 74.09  ?  138  ARG E N   1 
ATOM   12171 C CA  . ARG E  2  138 ? 13.799  -24.988 19.528  1.00 74.36  ?  138  ARG E CA  1 
ATOM   12172 C C   . ARG E  2  138 ? 12.647  -25.207 18.557  1.00 73.01  ?  138  ARG E C   1 
ATOM   12173 O O   . ARG E  2  138 ? 11.499  -25.324 19.000  1.00 73.35  ?  138  ARG E O   1 
ATOM   12174 C CB  . ARG E  2  138 ? 13.714  -23.572 20.104  1.00 74.90  ?  138  ARG E CB  1 
ATOM   12175 C CG  . ARG E  2  138 ? 14.796  -23.242 21.116  1.00 76.52  ?  138  ARG E CG  1 
ATOM   12176 C CD  . ARG E  2  138 ? 14.255  -22.359 22.227  1.00 77.85  ?  138  ARG E CD  1 
ATOM   12177 N NE  . ARG E  2  138 ? 15.214  -21.331 22.614  1.00 78.84  ?  138  ARG E NE  1 
ATOM   12178 C CZ  . ARG E  2  138 ? 14.929  -20.039 22.708  1.00 79.03  ?  138  ARG E CZ  1 
ATOM   12179 N NH1 . ARG E  2  138 ? 13.717  -19.577 22.447  1.00 78.24  ?  138  ARG E NH1 1 
ATOM   12180 N NH2 . ARG E  2  138 ? 15.886  -19.189 23.070  1.00 80.17  ?  138  ARG E NH2 1 
ATOM   12181 N N   . LEU E  2  139 ? 12.920  -25.257 17.252  1.00 74.85  ?  139  LEU E N   1 
ATOM   12182 C CA  . LEU E  2  139 ? 11.884  -25.453 16.238  1.00 73.69  ?  139  LEU E CA  1 
ATOM   12183 C C   . LEU E  2  139 ? 11.564  -26.944 16.157  1.00 73.99  ?  139  LEU E C   1 
ATOM   12184 O O   . LEU E  2  139 ? 12.018  -27.670 15.270  1.00 73.50  ?  139  LEU E O   1 
ATOM   12185 C CB  . LEU E  2  139 ? 12.335  -24.896 14.894  1.00 72.39  ?  139  LEU E CB  1 
ATOM   12186 C CG  . LEU E  2  139 ? 13.254  -23.671 14.927  1.00 72.38  ?  139  LEU E CG  1 
ATOM   12187 C CD1 . LEU E  2  139 ? 13.739  -23.326 13.528  1.00 71.26  ?  139  LEU E CD1 1 
ATOM   12188 C CD2 . LEU E  2  139 ? 12.550  -22.479 15.558  1.00 72.59  ?  139  LEU E CD2 1 
ATOM   12189 N N   . LYS E  2  140 ? 10.762  -27.404 17.122  1.00 74.94  ?  140  LYS E N   1 
ATOM   12190 C CA  . LYS E  2  140 ? 10.395  -28.814 17.189  1.00 75.51  ?  140  LYS E CA  1 
ATOM   12191 C C   . LYS E  2  140 ? 9.549   -29.260 16.002  1.00 74.63  ?  140  LYS E C   1 
ATOM   12192 O O   . LYS E  2  140 ? 9.496   -30.460 15.713  1.00 74.96  ?  140  LYS E O   1 
ATOM   12193 C CB  . LYS E  2  140 ? 9.651   -29.099 18.494  1.00 76.97  ?  140  LYS E CB  1 
ATOM   12194 C CG  . LYS E  2  140 ? 10.448  -28.763 19.746  1.00 78.17  ?  140  LYS E CG  1 
ATOM   12195 C CD  . LYS E  2  140 ? 11.872  -29.293 19.659  1.00 78.27  ?  140  LYS E CD  1 
ATOM   12196 C CE  . LYS E  2  140 ? 12.691  -28.887 20.875  1.00 79.60  ?  140  LYS E CE  1 
ATOM   12197 N NZ  . LYS E  2  140 ? 12.244  -29.584 22.111  1.00 81.26  ?  140  LYS E NZ  1 
ATOM   12198 N N   . LYS E  2  141 ? 8.893   -28.331 15.310  1.00 70.18  ?  141  LYS E N   1 
ATOM   12199 C CA  . LYS E  2  141 ? 8.074   -28.655 14.150  1.00 69.47  ?  141  LYS E CA  1 
ATOM   12200 C C   . LYS E  2  141 ? 8.828   -28.508 12.835  1.00 68.33  ?  141  LYS E C   1 
ATOM   12201 O O   . LYS E  2  141 ? 8.258   -28.794 11.777  1.00 67.82  ?  141  LYS E O   1 
ATOM   12202 C CB  . LYS E  2  141 ? 6.822   -27.770 14.121  1.00 69.23  ?  141  LYS E CB  1 
ATOM   12203 C CG  . LYS E  2  141 ? 5.884   -27.975 15.300  1.00 70.57  ?  141  LYS E CG  1 
ATOM   12204 C CD  . LYS E  2  141 ? 4.831   -29.030 14.999  1.00 71.21  ?  141  LYS E CD  1 
ATOM   12205 C CE  . LYS E  2  141 ? 3.911   -28.592 13.871  1.00 70.38  ?  141  LYS E CE  1 
ATOM   12206 N NZ  . LYS E  2  141 ? 2.474   -28.724 14.243  1.00 71.44  ?  141  LYS E NZ  1 
ATOM   12207 N N   . LEU E  2  142 ? 10.082  -28.065 12.878  1.00 70.39  ?  142  LEU E N   1 
ATOM   12208 C CA  . LEU E  2  142 ? 10.856  -27.861 11.660  1.00 69.52  ?  142  LEU E CA  1 
ATOM   12209 C C   . LEU E  2  142 ? 11.066  -29.176 10.921  1.00 69.74  ?  142  LEU E C   1 
ATOM   12210 O O   . LEU E  2  142 ? 11.464  -30.182 11.515  1.00 70.64  ?  142  LEU E O   1 
ATOM   12211 C CB  . LEU E  2  142 ? 12.205  -27.227 11.997  1.00 69.63  ?  142  LEU E CB  1 
ATOM   12212 C CG  . LEU E  2  142 ? 13.075  -26.836 10.803  1.00 68.91  ?  142  LEU E CG  1 
ATOM   12213 C CD1 . LEU E  2  142 ? 12.657  -25.479 10.258  1.00 67.98  ?  142  LEU E CD1 1 
ATOM   12214 C CD2 . LEU E  2  142 ? 14.538  -26.833 11.196  1.00 69.58  ?  142  LEU E CD2 1 
ATOM   12215 N N   . ARG E  2  143 ? 10.796  -29.164 9.618   1.00 70.44  ?  143  ARG E N   1 
ATOM   12216 C CA  . ARG E  2  143 ? 10.997  -30.322 8.756   1.00 70.75  ?  143  ARG E CA  1 
ATOM   12217 C C   . ARG E  2  143 ? 12.097  -30.125 7.728   1.00 70.37  ?  143  ARG E C   1 
ATOM   12218 O O   . ARG E  2  143 ? 12.814  -31.077 7.409   1.00 70.97  ?  143  ARG E O   1 
ATOM   12219 C CB  . ARG E  2  143 ? 9.700   -30.667 8.018   1.00 70.69  ?  143  ARG E CB  1 
ATOM   12220 C CG  . ARG E  2  143 ? 8.881   -31.782 8.637   1.00 71.74  ?  143  ARG E CG  1 
ATOM   12221 C CD  . ARG E  2  143 ? 7.855   -32.279 7.638   1.00 71.93  ?  143  ARG E CD  1 
ATOM   12222 N NE  . ARG E  2  143 ? 6.796   -31.300 7.428   1.00 71.33  ?  143  ARG E NE  1 
ATOM   12223 C CZ  . ARG E  2  143 ? 6.064   -31.215 6.326   1.00 71.14  ?  143  ARG E CZ  1 
ATOM   12224 N NH1 . ARG E  2  143 ? 6.261   -32.028 5.301   1.00 71.53  ?  143  ARG E NH1 1 
ATOM   12225 N NH2 . ARG E  2  143 ? 5.116   -30.285 6.246   1.00 70.66  ?  143  ARG E NH2 1 
ATOM   12226 N N   . PHE E  2  144 ? 12.252  -28.913 7.201   1.00 68.84  ?  144  PHE E N   1 
ATOM   12227 C CA  . PHE E  2  144 ? 13.193  -28.642 6.122   1.00 68.59  ?  144  PHE E CA  1 
ATOM   12228 C C   . PHE E  2  144 ? 14.064  -27.460 6.510   1.00 68.33  ?  144  PHE E C   1 
ATOM   12229 O O   . PHE E  2  144 ? 13.549  -26.386 6.835   1.00 67.76  ?  144  PHE E O   1 
ATOM   12230 C CB  . PHE E  2  144 ? 12.463  -28.355 4.806   1.00 67.98  ?  144  PHE E CB  1 
ATOM   12231 C CG  . PHE E  2  144 ? 11.235  -29.190 4.602   1.00 68.25  ?  144  PHE E CG  1 
ATOM   12232 C CD1 . PHE E  2  144 ? 11.324  -30.438 4.014   1.00 69.04  ?  144  PHE E CD1 1 
ATOM   12233 C CD2 . PHE E  2  144 ? 9.989   -28.719 4.981   1.00 67.91  ?  144  PHE E CD2 1 
ATOM   12234 C CE1 . PHE E  2  144 ? 10.199  -31.210 3.823   1.00 69.53  ?  144  PHE E CE1 1 
ATOM   12235 C CE2 . PHE E  2  144 ? 8.857   -29.487 4.788   1.00 68.39  ?  144  PHE E CE2 1 
ATOM   12236 C CZ  . PHE E  2  144 ? 8.964   -30.733 4.207   1.00 69.22  ?  144  PHE E CZ  1 
ATOM   12237 N N   . LEU E  2  145 ? 15.379  -27.658 6.469   1.00 69.13  ?  145  LEU E N   1 
ATOM   12238 C CA  . LEU E  2  145 ? 16.347  -26.607 6.761   1.00 69.20  ?  145  LEU E CA  1 
ATOM   12239 C C   . LEU E  2  145 ? 17.403  -26.627 5.666   1.00 69.48  ?  145  LEU E C   1 
ATOM   12240 O O   . LEU E  2  145 ? 18.197  -27.570 5.580   1.00 70.32  ?  145  LEU E O   1 
ATOM   12241 C CB  . LEU E  2  145 ? 16.977  -26.802 8.140   1.00 70.07  ?  145  LEU E CB  1 
ATOM   12242 C CG  . LEU E  2  145 ? 17.887  -25.674 8.625   1.00 70.41  ?  145  LEU E CG  1 
ATOM   12243 C CD1 . LEU E  2  145 ? 17.594  -25.340 10.070  1.00 70.85  ?  145  LEU E CD1 1 
ATOM   12244 C CD2 . LEU E  2  145 ? 19.342  -26.064 8.460   1.00 71.40  ?  145  LEU E CD2 1 
ATOM   12245 N N   . ARG E  2  146 ? 17.412  -25.589 4.833   1.00 68.08  ?  146  ARG E N   1 
ATOM   12246 C CA  . ARG E  2  146 ? 18.333  -25.487 3.706   1.00 68.45  ?  146  ARG E CA  1 
ATOM   12247 C C   . ARG E  2  146 ? 19.130  -24.199 3.857   1.00 68.59  ?  146  ARG E C   1 
ATOM   12248 O O   . ARG E  2  146 ? 18.580  -23.102 3.714   1.00 67.82  ?  146  ARG E O   1 
ATOM   12249 C CB  . ARG E  2  146 ? 17.582  -25.509 2.376   1.00 67.85  ?  146  ARG E CB  1 
ATOM   12250 C CG  . ARG E  2  146 ? 16.890  -26.821 2.044   1.00 68.04  ?  146  ARG E CG  1 
ATOM   12251 C CD  . ARG E  2  146 ? 15.546  -26.559 1.378   1.00 67.21  ?  146  ARG E CD  1 
ATOM   12252 N NE  . ARG E  2  146 ? 14.681  -27.732 1.375   1.00 67.49  ?  146  ARG E NE  1 
ATOM   12253 C CZ  . ARG E  2  146 ? 13.369  -27.696 1.565   1.00 66.99  ?  146  ARG E CZ  1 
ATOM   12254 N NH1 . ARG E  2  146 ? 12.734  -26.558 1.792   1.00 66.11  ?  146  ARG E NH1 1 
ATOM   12255 N NH2 . ARG E  2  146 ? 12.675  -28.830 1.519   1.00 67.52  ?  146  ARG E NH2 1 
ATOM   12256 N N   . LEU E  2  147 ? 20.427  -24.336 4.137   1.00 75.55  ?  147  LEU E N   1 
ATOM   12257 C CA  . LEU E  2  147 ? 21.328  -23.203 4.320   1.00 75.68  ?  147  LEU E CA  1 
ATOM   12258 C C   . LEU E  2  147 ? 22.480  -23.231 3.323   1.00 76.92  ?  147  LEU E C   1 
ATOM   12259 O O   . LEU E  2  147 ? 23.493  -22.556 3.531   1.00 77.71  ?  147  LEU E O   1 
ATOM   12260 C CB  . LEU E  2  147 ? 21.875  -23.172 5.751   1.00 77.15  ?  147  LEU E CB  1 
ATOM   12261 C CG  . LEU E  2  147 ? 20.931  -23.250 6.955   1.00 76.68  ?  147  LEU E CG  1 
ATOM   12262 C CD1 . LEU E  2  147 ? 21.619  -22.715 8.198   1.00 78.13  ?  147  LEU E CD1 1 
ATOM   12263 C CD2 . LEU E  2  147 ? 19.642  -22.481 6.714   1.00 75.51  ?  147  LEU E CD2 1 
ATOM   12264 N N   . ASN E  2  148 ? 22.347  -23.999 2.244   1.00 77.67  ?  148  ASN E N   1 
ATOM   12265 C CA  . ASN E  2  148 ? 23.474  -24.258 1.364   1.00 79.41  ?  148  ASN E CA  1 
ATOM   12266 C C   . ASN E  2  148 ? 23.819  -23.021 0.535   1.00 78.38  ?  148  ASN E C   1 
ATOM   12267 O O   . ASN E  2  148 ? 23.070  -22.041 0.478   1.00 76.35  ?  148  ASN E O   1 
ATOM   12268 C CB  . ASN E  2  148 ? 23.179  -25.455 0.457   1.00 80.43  ?  148  ASN E CB  1 
ATOM   12269 C CG  . ASN E  2  148 ? 21.893  -25.292 -0.334  1.00 78.43  ?  148  ASN E CG  1 
ATOM   12270 O OD1 . ASN E  2  148 ? 21.726  -24.332 -1.085  1.00 77.15  ?  148  ASN E OD1 1 
ATOM   12271 N ND2 . ASN E  2  148 ? 20.973  -26.235 -0.163  1.00 78.37  ?  148  ASN E ND2 1 
ATOM   12272 N N   . ASN E  2  149 ? 24.978  -23.090 -0.121  1.00 80.19  ?  149  ASN E N   1 
ATOM   12273 C CA  . ASN E  2  149 ? 25.517  -22.003 -0.938  1.00 79.74  ?  149  ASN E CA  1 
ATOM   12274 C C   . ASN E  2  149 ? 25.535  -20.687 -0.158  1.00 78.43  ?  149  ASN E C   1 
ATOM   12275 O O   . ASN E  2  149 ? 24.899  -19.698 -0.526  1.00 76.73  ?  149  ASN E O   1 
ATOM   12276 C CB  . ASN E  2  149 ? 24.733  -21.866 -2.245  1.00 78.74  ?  149  ASN E CB  1 
ATOM   12277 C CG  . ASN E  2  149 ? 25.400  -22.586 -3.400  1.00 80.72  ?  149  ASN E CG  1 
ATOM   12278 O OD1 . ASN E  2  149 ? 26.167  -21.992 -4.157  1.00 81.34  ?  149  ASN E OD1 1 
ATOM   12279 N ND2 . ASN E  2  149 ? 25.116  -23.877 -3.537  1.00 81.93  ?  149  ASN E ND2 1 
ATOM   12280 N N   . ASN E  2  150 ? 26.288  -20.697 0.942   1.00 84.28  ?  150  ASN E N   1 
ATOM   12281 C CA  . ASN E  2  150 ? 26.375  -19.558 1.845   1.00 83.57  ?  150  ASN E CA  1 
ATOM   12282 C C   . ASN E  2  150 ? 27.812  -19.415 2.333   1.00 85.61  ?  150  ASN E C   1 
ATOM   12283 O O   . ASN E  2  150 ? 28.713  -20.147 1.911   1.00 87.45  ?  150  ASN E O   1 
ATOM   12284 C CB  . ASN E  2  150 ? 25.406  -19.710 3.023   1.00 82.78  ?  150  ASN E CB  1 
ATOM   12285 C CG  . ASN E  2  150 ? 24.131  -18.916 2.832   1.00 80.42  ?  150  ASN E CG  1 
ATOM   12286 O OD1 . ASN E  2  150 ? 24.090  -17.715 3.098   1.00 79.70  ?  150  ASN E OD1 1 
ATOM   12287 N ND2 . ASN E  2  150 ? 23.080  -19.583 2.370   1.00 79.42  ?  150  ASN E ND2 1 
ATOM   12288 N N   . SER E  2  151 ? 28.023  -18.449 3.226   1.00 84.24  ?  151  SER E N   1 
ATOM   12289 C CA  . SER E  2  151 ? 29.325  -18.190 3.829   1.00 86.22  ?  151  SER E CA  1 
ATOM   12290 C C   . SER E  2  151 ? 29.312  -18.461 5.332   1.00 87.43  ?  151  SER E C   1 
ATOM   12291 O O   . SER E  2  151 ? 30.031  -17.810 6.095   1.00 88.59  ?  151  SER E O   1 
ATOM   12292 C CB  . SER E  2  151 ? 29.767  -16.756 3.545   1.00 85.60  ?  151  SER E CB  1 
ATOM   12293 O OG  . SER E  2  151 ? 31.141  -16.577 3.837   1.00 87.63  ?  151  SER E OG  1 
ATOM   12294 N N   . LEU E  2  152 ? 28.491  -19.416 5.766   1.00 90.04  ?  152  LEU E N   1 
ATOM   12295 C CA  . LEU E  2  152 ? 28.371  -19.742 7.181   1.00 91.36  ?  152  LEU E CA  1 
ATOM   12296 C C   . LEU E  2  152 ? 29.610  -20.486 7.673   1.00 94.57  ?  152  LEU E C   1 
ATOM   12297 O O   . LEU E  2  152 ? 30.237  -21.253 6.938   1.00 95.75  ?  152  LEU E O   1 
ATOM   12298 C CB  . LEU E  2  152 ? 27.115  -20.584 7.422   1.00 90.41  ?  152  LEU E CB  1 
ATOM   12299 C CG  . LEU E  2  152 ? 25.795  -19.876 7.752   1.00 88.07  ?  152  LEU E CG  1 
ATOM   12300 C CD1 . LEU E  2  152 ? 25.594  -18.628 6.918   1.00 86.40  ?  152  LEU E CD1 1 
ATOM   12301 C CD2 . LEU E  2  152 ? 24.631  -20.827 7.548   1.00 87.80  ?  152  LEU E CD2 1 
ATOM   12302 N N   . SER E  2  153 ? 29.961  -20.251 8.938   1.00 93.33  ?  153  SER E N   1 
ATOM   12303 C CA  . SER E  2  153 ? 31.171  -20.816 9.520   1.00 96.74  ?  153  SER E CA  1 
ATOM   12304 C C   . SER E  2  153 ? 30.926  -21.150 10.985  1.00 98.64  ?  153  SER E C   1 
ATOM   12305 O O   . SER E  2  153 ? 30.283  -20.380 11.704  1.00 97.68  ?  153  SER E O   1 
ATOM   12306 C CB  . SER E  2  153 ? 32.353  -19.848 9.388   1.00 97.59  ?  153  SER E CB  1 
ATOM   12307 O OG  . SER E  2  153 ? 32.119  -18.660 10.123  1.00 96.93  ?  153  SER E OG  1 
ATOM   12308 N N   . GLY E  2  154 ? 31.444  -22.286 11.415  1.00 96.34  ?  154  GLY E N   1 
ATOM   12309 C CA  . GLY E  2  154 ? 31.310  -22.719 12.791  1.00 98.77  ?  154  GLY E CA  1 
ATOM   12310 C C   . GLY E  2  154 ? 31.228  -24.240 12.874  1.00 100.86 ?  154  GLY E C   1 
ATOM   12311 O O   . GLY E  2  154 ? 31.943  -24.949 12.163  1.00 102.24 ?  154  GLY E O   1 
ATOM   12312 N N   . GLU E  2  155 ? 30.370  -24.713 13.777  1.00 101.16 ?  155  GLU E N   1 
ATOM   12313 C CA  . GLU E  2  155 ? 30.107  -26.133 13.966  1.00 103.14 ?  155  GLU E CA  1 
ATOM   12314 C C   . GLU E  2  155 ? 28.602  -26.334 14.094  1.00 100.64 ?  155  GLU E C   1 
ATOM   12315 O O   . GLU E  2  155 ? 27.880  -25.422 14.506  1.00 98.55  ?  155  GLU E O   1 
ATOM   12316 C CB  . GLU E  2  155 ? 30.841  -26.674 15.206  1.00 107.77 ?  155  GLU E CB  1 
ATOM   12317 C CG  . GLU E  2  155 ? 30.860  -28.190 15.338  1.00 110.73 ?  155  GLU E CG  1 
ATOM   12318 C CD  . GLU E  2  155 ? 31.976  -28.678 16.244  1.00 115.88 ?  155  GLU E CD  1 
ATOM   12319 O OE1 . GLU E  2  155 ? 32.189  -28.064 17.310  1.00 117.39 ?  155  GLU E OE1 1 
ATOM   12320 O OE2 . GLU E  2  155 ? 32.632  -29.682 15.900  1.00 118.69 -1 155  GLU E OE2 1 
ATOM   12321 N N   . ILE E  2  156 ? 28.129  -27.528 13.737  1.00 101.04 ?  156  ILE E N   1 
ATOM   12322 C CA  . ILE E  2  156 ? 26.696  -27.823 13.794  1.00 98.76  ?  156  ILE E CA  1 
ATOM   12323 C C   . ILE E  2  156 ? 26.266  -27.914 15.252  1.00 100.50 ?  156  ILE E C   1 
ATOM   12324 O O   . ILE E  2  156 ? 26.833  -28.713 16.012  1.00 104.36 ?  156  ILE E O   1 
ATOM   12325 C CB  . ILE E  2  156 ? 26.334  -29.131 13.066  1.00 99.14  ?  156  ILE E CB  1 
ATOM   12326 C CG1 . ILE E  2  156 ? 26.601  -29.041 11.564  1.00 97.37  ?  156  ILE E CG1 1 
ATOM   12327 C CG2 . ILE E  2  156 ? 24.878  -29.489 13.320  1.00 97.26  ?  156  ILE E CG2 1 
ATOM   12328 C CD1 . ILE E  2  156 ? 27.991  -29.443 11.180  1.00 100.36 ?  156  ILE E CD1 1 
ATOM   12329 N N   . PRO E  2  157 ? 25.289  -27.119 15.689  1.00 98.09  ?  157  PRO E N   1 
ATOM   12330 C CA  . PRO E  2  157 ? 24.761  -27.285 17.049  1.00 99.83  ?  157  PRO E CA  1 
ATOM   12331 C C   . PRO E  2  157 ? 24.198  -28.685 17.250  1.00 101.29 ?  157  PRO E C   1 
ATOM   12332 O O   . PRO E  2  157 ? 23.566  -29.254 16.359  1.00 99.30  ?  157  PRO E O   1 
ATOM   12333 C CB  . PRO E  2  157 ? 23.657  -26.223 17.150  1.00 96.39  ?  157  PRO E CB  1 
ATOM   12334 C CG  . PRO E  2  157 ? 23.675  -25.450 15.882  1.00 93.07  ?  157  PRO E CG  1 
ATOM   12335 C CD  . PRO E  2  157 ? 24.788  -25.911 15.013  1.00 94.22  ?  157  PRO E CD  1 
ATOM   12336 N N   . ARG E  2  158 ? 24.435  -29.239 18.442  1.00 105.06 ?  158  ARG E N   1 
ATOM   12337 C CA  . ARG E  2  158 ? 23.872  -30.541 18.778  1.00 106.85 ?  158  ARG E CA  1 
ATOM   12338 C C   . ARG E  2  158 ? 22.351  -30.507 18.850  1.00 103.79 ?  158  ARG E C   1 
ATOM   12339 O O   . ARG E  2  158 ? 21.714  -31.557 18.709  1.00 104.06 ?  158  ARG E O   1 
ATOM   12340 C CB  . ARG E  2  158 ? 24.449  -31.044 20.106  1.00 111.87 ?  158  ARG E CB  1 
ATOM   12341 C CG  . ARG E  2  158 ? 23.688  -30.581 21.341  1.00 112.23 ?  158  ARG E CG  1 
ATOM   12342 C CD  . ARG E  2  158 ? 22.836  -31.701 21.924  1.00 113.81 ?  158  ARG E CD  1 
ATOM   12343 N NE  . ARG E  2  158 ? 21.825  -31.195 22.845  1.00 112.97 ?  158  ARG E NE  1 
ATOM   12344 C CZ  . ARG E  2  158 ? 20.733  -31.860 23.196  1.00 112.68 ?  158  ARG E CZ  1 
ATOM   12345 N NH1 . ARG E  2  158 ? 20.478  -33.070 22.725  1.00 113.20 ?  158  ARG E NH1 1 
ATOM   12346 N NH2 . ARG E  2  158 ? 19.873  -31.296 24.040  1.00 112.03 ?  158  ARG E NH2 1 
ATOM   12347 N N   . SER E  2  159 ? 21.760  -29.329 19.075  1.00 101.12 ?  159  SER E N   1 
ATOM   12348 C CA  . SER E  2  159 ? 20.310  -29.228 19.204  1.00 98.41  ?  159  SER E CA  1 
ATOM   12349 C C   . SER E  2  159 ? 19.594  -29.672 17.936  1.00 95.22  ?  159  SER E C   1 
ATOM   12350 O O   . SER E  2  159 ? 18.459  -30.159 18.005  1.00 93.98  ?  159  SER E O   1 
ATOM   12351 C CB  . SER E  2  159 ? 19.918  -27.794 19.558  1.00 96.34  ?  159  SER E CB  1 
ATOM   12352 O OG  . SER E  2  159 ? 20.481  -26.870 18.643  1.00 94.28  ?  159  SER E OG  1 
ATOM   12353 N N   . LEU E  2  160 ? 20.232  -29.517 16.774  1.00 94.67  ?  160  LEU E N   1 
ATOM   12354 C CA  . LEU E  2  160 ? 19.605  -29.908 15.518  1.00 91.99  ?  160  LEU E CA  1 
ATOM   12355 C C   . LEU E  2  160 ? 19.414  -31.415 15.393  1.00 93.91  ?  160  LEU E C   1 
ATOM   12356 O O   . LEU E  2  160 ? 18.717  -31.855 14.474  1.00 91.95  ?  160  LEU E O   1 
ATOM   12357 C CB  . LEU E  2  160 ? 20.431  -29.394 14.337  1.00 90.85  ?  160  LEU E CB  1 
ATOM   12358 C CG  . LEU E  2  160 ? 20.631  -27.879 14.255  1.00 88.83  ?  160  LEU E CG  1 
ATOM   12359 C CD1 . LEU E  2  160 ? 21.567  -27.518 13.111  1.00 88.30  ?  160  LEU E CD1 1 
ATOM   12360 C CD2 . LEU E  2  160 ? 19.295  -27.166 14.108  1.00 85.34  ?  160  LEU E CD2 1 
ATOM   12361 N N   . THR E  2  161 ? 20.022  -32.211 16.274  1.00 97.31  ?  161  THR E N   1 
ATOM   12362 C CA  . THR E  2  161 ? 19.812  -33.653 16.263  1.00 99.59  ?  161  THR E CA  1 
ATOM   12363 C C   . THR E  2  161 ? 18.643  -34.099 17.133  1.00 99.62  ?  161  THR E C   1 
ATOM   12364 O O   . THR E  2  161 ? 18.180  -35.236 16.984  1.00 100.69 ?  161  THR E O   1 
ATOM   12365 C CB  . THR E  2  161 ? 21.082  -34.379 16.722  1.00 104.45 ?  161  THR E CB  1 
ATOM   12366 O OG1 . THR E  2  161 ? 21.562  -33.788 17.936  1.00 106.49 ?  161  THR E OG1 1 
ATOM   12367 C CG2 . THR E  2  161 ? 22.163  -34.285 15.657  1.00 104.68 ?  161  THR E CG2 1 
ATOM   12368 N N   . ALA E  2  162 ? 18.155  -33.241 18.027  1.00 98.64  ?  162  ALA E N   1 
ATOM   12369 C CA  . ALA E  2  162 ? 17.067  -33.588 18.931  1.00 98.84  ?  162  ALA E CA  1 
ATOM   12370 C C   . ALA E  2  162 ? 15.700  -33.157 18.417  1.00 94.48  ?  162  ALA E C   1 
ATOM   12371 O O   . ALA E  2  162 ? 14.702  -33.347 19.120  1.00 94.24  ?  162  ALA E O   1 
ATOM   12372 C CB  . ALA E  2  162 ? 17.313  -32.972 20.313  1.00 101.00 ?  162  ALA E CB  1 
ATOM   12373 N N   . VAL E  2  163 ? 15.630  -32.582 17.216  1.00 94.67  ?  163  VAL E N   1 
ATOM   12374 C CA  . VAL E  2  163 ? 14.362  -32.066 16.709  1.00 90.71  ?  163  VAL E CA  1 
ATOM   12375 C C   . VAL E  2  163 ? 13.413  -33.206 16.355  1.00 90.33  ?  163  VAL E C   1 
ATOM   12376 O O   . VAL E  2  163 ? 12.196  -33.096 16.544  1.00 89.29  ?  163  VAL E O   1 
ATOM   12377 C CB  . VAL E  2  163 ? 14.622  -31.138 15.507  1.00 88.56  ?  163  VAL E CB  1 
ATOM   12378 C CG1 . VAL E  2  163 ? 15.555  -31.811 14.516  1.00 89.07  ?  163  VAL E CG1 1 
ATOM   12379 C CG2 . VAL E  2  163 ? 13.315  -30.732 14.840  1.00 86.80  ?  163  VAL E CG2 1 
ATOM   12380 N N   . LEU E  2  164 ? 13.950  -34.297 15.803  1.00 91.91  ?  164  LEU E N   1 
ATOM   12381 C CA  . LEU E  2  164 ? 13.287  -35.551 15.439  1.00 92.48  ?  164  LEU E CA  1 
ATOM   12382 C C   . LEU E  2  164 ? 12.304  -35.384 14.284  1.00 88.84  ?  164  LEU E C   1 
ATOM   12383 O O   . LEU E  2  164 ? 11.690  -36.374 13.867  1.00 89.10  ?  164  LEU E O   1 
ATOM   12384 C CB  . LEU E  2  164 ? 12.581  -36.230 16.629  1.00 94.26  ?  164  LEU E CB  1 
ATOM   12385 C CG  . LEU E  2  164 ? 11.230  -35.821 17.235  1.00 91.98  ?  164  LEU E CG  1 
ATOM   12386 C CD1 . LEU E  2  164 ? 10.043  -36.479 16.536  1.00 90.01  ?  164  LEU E CD1 1 
ATOM   12387 C CD2 . LEU E  2  164 ? 11.206  -36.119 18.729  1.00 94.99  ?  164  LEU E CD2 1 
ATOM   12388 N N   . THR E  2  165 ? 12.149  -34.177 13.736  1.00 85.37  ?  165  THR E N   1 
ATOM   12389 C CA  . THR E  2  165 ? 11.234  -33.946 12.629  1.00 82.19  ?  165  THR E CA  1 
ATOM   12390 C C   . THR E  2  165 ? 11.939  -33.661 11.310  1.00 81.51  ?  165  THR E C   1 
ATOM   12391 O O   . THR E  2  165 ? 11.300  -33.750 10.257  1.00 79.72  ?  165  THR E O   1 
ATOM   12392 C CB  . THR E  2  165 ? 10.291  -32.776 12.958  1.00 79.21  ?  165  THR E CB  1 
ATOM   12393 O OG1 . THR E  2  165 ? 9.894   -32.860 14.331  1.00 80.33  ?  165  THR E OG1 1 
ATOM   12394 C CG2 . THR E  2  165 ? 9.038   -32.826 12.096  1.00 76.49  ?  165  THR E CG2 1 
ATOM   12395 N N   . LEU E  2  166 ? 13.234  -33.340 11.339  1.00 84.02  ?  166  LEU E N   1 
ATOM   12396 C CA  . LEU E  2  166 ? 13.980  -33.036 10.123  1.00 82.69  ?  166  LEU E CA  1 
ATOM   12397 C C   . LEU E  2  166 ? 13.982  -34.193 9.132   1.00 83.91  ?  166  LEU E C   1 
ATOM   12398 O O   . LEU E  2  166 ? 14.548  -35.258 9.401   1.00 87.05  ?  166  LEU E O   1 
ATOM   12399 C CB  . LEU E  2  166 ? 15.421  -32.640 10.463  1.00 84.70  ?  166  LEU E CB  1 
ATOM   12400 C CG  . LEU E  2  166 ? 15.733  -31.151 10.639  1.00 82.95  ?  166  LEU E CG  1 
ATOM   12401 C CD1 . LEU E  2  166 ? 15.890  -30.497 9.283   1.00 80.98  ?  166  LEU E CD1 1 
ATOM   12402 C CD2 . LEU E  2  166 ? 14.649  -30.447 11.428  1.00 83.00  ?  166  LEU E CD2 1 
ATOM   12403 N N   . GLN E  2  167 ? 13.352  -33.981 7.979   1.00 86.22  ?  167  GLN E N   1 
ATOM   12404 C CA  . GLN E  2  167 ? 13.420  -34.901 6.853   1.00 85.58  ?  167  GLN E CA  1 
ATOM   12405 C C   . GLN E  2  167 ? 14.457  -34.481 5.822   1.00 86.00  ?  167  GLN E C   1 
ATOM   12406 O O   . GLN E  2  167 ? 15.207  -35.325 5.321   1.00 88.65  ?  167  GLN E O   1 
ATOM   12407 C CB  . GLN E  2  167 ? 12.050  -35.013 6.175   1.00 83.35  ?  167  GLN E CB  1 
ATOM   12408 C CG  . GLN E  2  167 ? 10.941  -35.533 7.076   1.00 82.96  ?  167  GLN E CG  1 
ATOM   12409 C CD  . GLN E  2  167 ? 10.358  -36.845 6.584   1.00 84.33  ?  167  GLN E CD  1 
ATOM   12410 O OE1 . GLN E  2  167 ? 11.069  -37.687 6.034   1.00 86.94  ?  167  GLN E OE1 1 
ATOM   12411 N NE2 . GLN E  2  167 ? 9.056   -37.022 6.774   1.00 82.74  ?  167  GLN E NE2 1 
ATOM   12412 N N   . VAL E  2  168 ? 14.516  -33.190 5.502   1.00 78.29  ?  168  VAL E N   1 
ATOM   12413 C CA  . VAL E  2  168 ? 15.417  -32.650 4.493   1.00 78.41  ?  168  VAL E CA  1 
ATOM   12414 C C   . VAL E  2  168 ? 16.380  -31.683 5.169   1.00 78.47  ?  168  VAL E C   1 
ATOM   12415 O O   . VAL E  2  168 ? 15.952  -30.768 5.882   1.00 76.64  ?  168  VAL E O   1 
ATOM   12416 C CB  . VAL E  2  168 ? 14.645  -31.951 3.359   1.00 75.86  ?  168  VAL E CB  1 
ATOM   12417 C CG1 . VAL E  2  168 ? 15.599  -31.519 2.257   1.00 76.45  ?  168  VAL E CG1 1 
ATOM   12418 C CG2 . VAL E  2  168 ? 13.570  -32.874 2.808   1.00 75.80  ?  168  VAL E CG2 1 
ATOM   12419 N N   . LEU E  2  169 ? 17.676  -31.894 4.947   1.00 83.83  ?  169  LEU E N   1 
ATOM   12420 C CA  . LEU E  2  169 ? 18.721  -31.042 5.492   1.00 84.28  ?  169  LEU E CA  1 
ATOM   12421 C C   . LEU E  2  169 ? 19.799  -30.869 4.433   1.00 85.28  ?  169  LEU E C   1 
ATOM   12422 O O   . LEU E  2  169 ? 20.176  -31.833 3.760   1.00 87.38  ?  169  LEU E O   1 
ATOM   12423 C CB  . LEU E  2  169 ? 19.303  -31.647 6.785   1.00 86.99  ?  169  LEU E CB  1 
ATOM   12424 C CG  . LEU E  2  169 ? 20.422  -30.992 7.611   1.00 88.32  ?  169  LEU E CG  1 
ATOM   12425 C CD1 . LEU E  2  169 ? 21.806  -31.102 6.972   1.00 90.46  ?  169  LEU E CD1 1 
ATOM   12426 C CD2 . LEU E  2  169 ? 20.082  -29.541 7.901   1.00 85.55  ?  169  LEU E CD2 1 
ATOM   12427 N N   . ASP E  2  170 ? 20.282  -29.637 4.280   1.00 84.78  ?  170  ASP E N   1 
ATOM   12428 C CA  . ASP E  2  170 ? 21.365  -29.363 3.337   1.00 85.74  ?  170  ASP E CA  1 
ATOM   12429 C C   . ASP E  2  170 ? 22.063  -28.081 3.768   1.00 84.97  ?  170  ASP E C   1 
ATOM   12430 O O   . ASP E  2  170 ? 21.454  -27.007 3.743   1.00 82.45  ?  170  ASP E O   1 
ATOM   12431 C CB  . ASP E  2  170 ? 20.835  -29.248 1.913   1.00 84.43  ?  170  ASP E CB  1 
ATOM   12432 C CG  . ASP E  2  170 ? 21.945  -29.202 0.881   1.00 85.99  ?  170  ASP E CG  1 
ATOM   12433 O OD1 . ASP E  2  170 ? 23.080  -29.606 1.211   1.00 88.49  ?  170  ASP E OD1 1 
ATOM   12434 O OD2 . ASP E  2  170 ? 21.685  -28.761 -0.258  1.00 84.91  -1 170  ASP E OD2 1 
ATOM   12435 N N   . LEU E  2  171 ? 23.328  -28.196 4.162   1.00 85.12  ?  171  LEU E N   1 
ATOM   12436 C CA  . LEU E  2  171 ? 24.169  -27.059 4.518   1.00 87.02  ?  171  LEU E CA  1 
ATOM   12437 C C   . LEU E  2  171 ? 25.476  -27.099 3.736   1.00 89.24  ?  171  LEU E C   1 
ATOM   12438 O O   . LEU E  2  171 ? 26.544  -26.750 4.243   1.00 91.50  ?  171  LEU E O   1 
ATOM   12439 C CB  . LEU E  2  171 ? 24.406  -27.013 6.029   1.00 87.79  ?  171  LEU E CB  1 
ATOM   12440 C CG  . LEU E  2  171 ? 24.922  -28.243 6.790   1.00 88.41  ?  171  LEU E CG  1 
ATOM   12441 C CD1 . LEU E  2  171 ? 26.444  -28.332 6.837   1.00 91.22  ?  171  LEU E CD1 1 
ATOM   12442 C CD2 . LEU E  2  171 ? 24.345  -28.261 8.199   1.00 87.97  ?  171  LEU E CD2 1 
ATOM   12443 N N   . SER E  2  172 ? 25.401  -27.528 2.479   1.00 88.41  ?  172  SER E N   1 
ATOM   12444 C CA  . SER E  2  172 ? 26.582  -27.620 1.635   1.00 90.77  ?  172  SER E CA  1 
ATOM   12445 C C   . SER E  2  172 ? 27.084  -26.233 1.233   1.00 92.41  ?  172  SER E C   1 
ATOM   12446 O O   . SER E  2  172 ? 26.373  -25.231 1.326   1.00 91.45  ?  172  SER E O   1 
ATOM   12447 C CB  . SER E  2  172 ? 26.277  -28.443 0.383   1.00 90.13  ?  172  SER E CB  1 
ATOM   12448 O OG  . SER E  2  172 ? 25.931  -29.776 0.718   1.00 89.12  ?  172  SER E OG  1 
ATOM   12449 N N   . ASN E  2  173 ? 28.338  -26.193 0.777   1.00 94.25  ?  173  ASN E N   1 
ATOM   12450 C CA  . ASN E  2  173 ? 28.928  -25.006 0.152   1.00 96.34  ?  173  ASN E CA  1 
ATOM   12451 C C   . ASN E  2  173 ? 29.051  -23.834 1.129   1.00 97.13  ?  173  ASN E C   1 
ATOM   12452 O O   . ASN E  2  173 ? 28.712  -22.693 0.807   1.00 97.23  ?  173  ASN E O   1 
ATOM   12453 C CB  . ASN E  2  173 ? 28.140  -24.594 -1.097  1.00 95.15  ?  173  ASN E CB  1 
ATOM   12454 C CG  . ASN E  2  173 ? 28.134  -25.669 -2.166  1.00 95.00  ?  173  ASN E CG  1 
ATOM   12455 O OD1 . ASN E  2  173 ? 29.087  -25.802 -2.934  1.00 97.56  ?  173  ASN E OD1 1 
ATOM   12456 N ND2 . ASN E  2  173 ? 27.053  -26.439 -2.226  1.00 92.30  ?  173  ASN E ND2 1 
ATOM   12457 N N   . ASN E  2  174 ? 29.539  -24.122 2.340   1.00 98.80  ?  174  ASN E N   1 
ATOM   12458 C CA  . ASN E  2  174 ? 29.946  -23.069 3.273   1.00 100.47 ?  174  ASN E CA  1 
ATOM   12459 C C   . ASN E  2  174 ? 31.019  -23.606 4.210   1.00 102.71 ?  174  ASN E C   1 
ATOM   12460 O O   . ASN E  2  174 ? 30.938  -24.769 4.632   1.00 101.78 ?  174  ASN E O   1 
ATOM   12461 C CB  . ASN E  2  174 ? 28.778  -22.496 4.090   1.00 98.30  ?  174  ASN E CB  1 
ATOM   12462 C CG  . ASN E  2  174 ? 27.783  -23.547 4.510   1.00 95.38  ?  174  ASN E CG  1 
ATOM   12463 O OD1 . ASN E  2  174 ? 27.238  -24.260 3.676   1.00 93.64  ?  174  ASN E OD1 1 
ATOM   12464 N ND2 . ASN E  2  174 ? 27.532  -23.645 5.812   1.00 95.05  ?  174  ASN E ND2 1 
ATOM   12465 N N   . PRO E  2  175 ? 32.022  -22.793 4.552   1.00 105.01 ?  175  PRO E N   1 
ATOM   12466 C CA  . PRO E  2  175 ? 33.176  -23.298 5.312   1.00 107.76 ?  175  PRO E CA  1 
ATOM   12467 C C   . PRO E  2  175 ? 32.886  -23.566 6.781   1.00 107.05 ?  175  PRO E C   1 
ATOM   12468 O O   . PRO E  2  175 ? 33.206  -22.749 7.648   1.00 108.77 ?  175  PRO E O   1 
ATOM   12469 C CB  . PRO E  2  175 ? 34.207  -22.173 5.150   1.00 111.48 ?  175  PRO E CB  1 
ATOM   12470 C CG  . PRO E  2  175 ? 33.376  -20.950 4.968   1.00 110.25 ?  175  PRO E CG  1 
ATOM   12471 C CD  . PRO E  2  175 ? 32.224  -21.400 4.117   1.00 106.69 ?  175  PRO E CD  1 
ATOM   12472 N N   . LEU E  2  176 ? 32.273  -24.710 7.067   1.00 105.98 ?  176  LEU E N   1 
ATOM   12473 C CA  . LEU E  2  176 ? 31.953  -25.099 8.429   1.00 105.36 ?  176  LEU E CA  1 
ATOM   12474 C C   . LEU E  2  176 ? 33.100  -25.940 8.990   1.00 108.07 ?  176  LEU E C   1 
ATOM   12475 O O   . LEU E  2  176 ? 34.016  -26.334 8.267   1.00 110.12 ?  176  LEU E O   1 
ATOM   12476 C CB  . LEU E  2  176 ? 30.629  -25.865 8.449   1.00 101.67 ?  176  LEU E CB  1 
ATOM   12477 C CG  . LEU E  2  176 ? 29.715  -25.723 9.664   1.00 100.18 ?  176  LEU E CG  1 
ATOM   12478 C CD1 . LEU E  2  176 ? 29.443  -24.254 9.939   1.00 100.70 ?  176  LEU E CD1 1 
ATOM   12479 C CD2 . LEU E  2  176 ? 28.406  -26.451 9.411   1.00 96.80  ?  176  LEU E CD2 1 
ATOM   12480 N N   . THR E  2  177 ? 33.052  -26.218 10.295  1.00 107.13 ?  177  THR E N   1 
ATOM   12481 C CA  . THR E  2  177 ? 34.106  -26.982 10.956  1.00 109.94 ?  177  THR E CA  1 
ATOM   12482 C C   . THR E  2  177 ? 33.502  -28.044 11.869  1.00 108.39 ?  177  THR E C   1 
ATOM   12483 O O   . THR E  2  177 ? 32.349  -27.946 12.296  1.00 105.69 ?  177  THR E O   1 
ATOM   12484 C CB  . THR E  2  177 ? 35.049  -26.086 11.786  1.00 113.48 ?  177  THR E CB  1 
ATOM   12485 O OG1 . THR E  2  177 ? 34.346  -25.559 12.918  1.00 112.55 ?  177  THR E OG1 1 
ATOM   12486 C CG2 . THR E  2  177 ? 35.603  -24.936 10.950  1.00 115.27 ?  177  THR E CG2 1 
ATOM   12487 N N   . GLY E  2  178 ? 34.306  -29.060 12.173  1.00 112.77 ?  178  GLY E N   1 
ATOM   12488 C CA  . GLY E  2  178 ? 33.903  -30.129 13.067  1.00 111.99 ?  178  GLY E CA  1 
ATOM   12489 C C   . GLY E  2  178 ? 33.496  -31.387 12.326  1.00 110.29 ?  178  GLY E C   1 
ATOM   12490 O O   . GLY E  2  178 ? 33.546  -31.479 11.096  1.00 109.76 ?  178  GLY E O   1 
ATOM   12491 N N   . ASP E  2  179 ? 33.096  -32.383 13.110  1.00 112.44 ?  179  ASP E N   1 
ATOM   12492 C CA  . ASP E  2  179 ? 32.646  -33.667 12.592  1.00 111.07 ?  179  ASP E CA  1 
ATOM   12493 C C   . ASP E  2  179 ? 31.128  -33.689 12.465  1.00 107.24 ?  179  ASP E C   1 
ATOM   12494 O O   . ASP E  2  179 ? 30.413  -33.008 13.205  1.00 107.75 ?  179  ASP E O   1 
ATOM   12495 C CB  . ASP E  2  179 ? 33.110  -34.813 13.493  1.00 113.10 ?  179  ASP E CB  1 
ATOM   12496 C CG  . ASP E  2  179 ? 34.500  -35.304 13.139  1.00 116.86 ?  179  ASP E CG  1 
ATOM   12497 O OD1 . ASP E  2  179 ? 35.328  -34.480 12.698  1.00 118.76 ?  179  ASP E OD1 1 
ATOM   12498 O OD2 . ASP E  2  179 ? 34.763  -36.515 13.297  1.00 118.18 -1 179  ASP E OD2 1 
ATOM   12499 N N   . ILE E  2  180 ? 30.643  -34.480 11.513  1.00 109.42 ?  180  ILE E N   1 
ATOM   12500 C CA  . ILE E  2  180 ? 29.209  -34.597 11.255  1.00 107.43 ?  180  ILE E CA  1 
ATOM   12501 C C   . ILE E  2  180 ? 28.550  -35.400 12.372  1.00 108.59 ?  180  ILE E C   1 
ATOM   12502 O O   . ILE E  2  180 ? 28.902  -36.569 12.588  1.00 109.03 ?  180  ILE E O   1 
ATOM   12503 C CB  . ILE E  2  180 ? 28.940  -35.234 9.880   1.00 104.97 ?  180  ILE E CB  1 
ATOM   12504 C CG1 . ILE E  2  180 ? 29.848  -36.448 9.657   1.00 106.15 ?  180  ILE E CG1 1 
ATOM   12505 C CG2 . ILE E  2  180 ? 29.129  -34.214 8.769   1.00 103.74 ?  180  ILE E CG2 1 
ATOM   12506 C CD1 . ILE E  2  180 ? 29.703  -37.075 8.288   1.00 105.27 ?  180  ILE E CD1 1 
ATOM   12507 N N   . PRO E  2  181 ? 27.604  -34.820 13.108  1.00 106.04 ?  181  PRO E N   1 
ATOM   12508 C CA  . PRO E  2  181 ? 26.885  -35.594 14.125  1.00 107.26 ?  181  PRO E CA  1 
ATOM   12509 C C   . PRO E  2  181 ? 25.945  -36.603 13.485  1.00 105.36 ?  181  PRO E C   1 
ATOM   12510 O O   . PRO E  2  181 ? 25.392  -36.373 12.408  1.00 104.05 ?  181  PRO E O   1 
ATOM   12511 C CB  . PRO E  2  181 ? 26.104  -34.525 14.902  1.00 108.59 ?  181  PRO E CB  1 
ATOM   12512 C CG  . PRO E  2  181 ? 26.763  -33.222 14.547  1.00 108.75 ?  181  PRO E CG  1 
ATOM   12513 C CD  . PRO E  2  181 ? 27.233  -33.397 13.139  1.00 106.61 ?  181  PRO E CD  1 
ATOM   12514 N N   . VAL E  2  182 ? 25.806  -37.755 14.142  1.00 107.14 ?  182  VAL E N   1 
ATOM   12515 C CA  . VAL E  2  182 ? 24.856  -38.781 13.721  1.00 105.71 ?  182  VAL E CA  1 
ATOM   12516 C C   . VAL E  2  182 ? 23.973  -39.123 14.922  1.00 105.82 ?  182  VAL E C   1 
ATOM   12517 O O   . VAL E  2  182 ? 23.455  -40.240 15.033  1.00 103.87 ?  182  VAL E O   1 
ATOM   12518 C CB  . VAL E  2  182 ? 25.590  -40.019 13.173  1.00 103.89 ?  182  VAL E CB  1 
ATOM   12519 C CG1 . VAL E  2  182 ? 24.647  -40.949 12.411  1.00 101.71 ?  182  VAL E CG1 1 
ATOM   12520 C CG2 . VAL E  2  182 ? 26.768  -39.610 12.289  1.00 103.86 ?  182  VAL E CG2 1 
ATOM   12521 N N   . ASN E  2  183 ? 23.802  -38.166 15.839  1.00 103.96 ?  183  ASN E N   1 
ATOM   12522 C CA  . ASN E  2  183 ? 23.370  -38.521 17.188  1.00 104.41 ?  183  ASN E CA  1 
ATOM   12523 C C   . ASN E  2  183 ? 21.890  -38.898 17.259  1.00 103.09 ?  183  ASN E C   1 
ATOM   12524 O O   . ASN E  2  183 ? 21.545  -40.045 17.567  1.00 101.83 ?  183  ASN E O   1 
ATOM   12525 C CB  . ASN E  2  183 ? 23.649  -37.345 18.127  1.00 106.35 ?  183  ASN E CB  1 
ATOM   12526 C CG  . ASN E  2  183 ? 23.536  -37.722 19.593  1.00 106.94 ?  183  ASN E CG  1 
ATOM   12527 O OD1 . ASN E  2  183 ? 23.325  -38.884 19.936  1.00 105.81 ?  183  ASN E OD1 1 
ATOM   12528 N ND2 . ASN E  2  183 ? 23.666  -36.728 20.468  1.00 108.64 ?  183  ASN E ND2 1 
ATOM   12529 N N   . GLY E  2  184 ? 20.993  -37.951 16.990  1.00 105.33 ?  184  GLY E N   1 
ATOM   12530 C CA  . GLY E  2  184 ? 19.584  -38.248 17.163  1.00 104.03 ?  184  GLY E CA  1 
ATOM   12531 C C   . GLY E  2  184 ? 18.738  -38.368 15.912  1.00 103.95 ?  184  GLY E C   1 
ATOM   12532 O O   . GLY E  2  184 ? 17.877  -39.249 15.803  1.00 102.55 ?  184  GLY E O   1 
ATOM   12533 N N   . SER E  2  185 ? 18.994  -37.487 14.950  1.00 104.49 ?  185  SER E N   1 
ATOM   12534 C CA  . SER E  2  185 ? 18.185  -37.376 13.743  1.00 103.44 ?  185  SER E CA  1 
ATOM   12535 C C   . SER E  2  185 ? 18.999  -37.433 12.465  1.00 102.38 ?  185  SER E C   1 
ATOM   12536 O O   . SER E  2  185 ? 18.427  -37.691 11.398  1.00 100.57 ?  185  SER E O   1 
ATOM   12537 C CB  . SER E  2  185 ? 17.379  -36.069 13.765  1.00 104.66 ?  185  SER E CB  1 
ATOM   12538 O OG  . SER E  2  185 ? 16.776  -35.821 12.511  1.00 104.15 ?  185  SER E OG  1 
ATOM   12539 N N   . PHE E  2  186 ? 20.304  -37.193 12.532  1.00 105.20 ?  186  PHE E N   1 
ATOM   12540 C CA  . PHE E  2  186 ? 21.181  -37.240 11.373  1.00 104.73 ?  186  PHE E CA  1 
ATOM   12541 C C   . PHE E  2  186 ? 21.516  -38.667 10.963  1.00 104.76 ?  186  PHE E C   1 
ATOM   12542 O O   . PHE E  2  186 ? 22.307  -38.858 10.035  1.00 104.53 ?  186  PHE E O   1 
ATOM   12543 C CB  . PHE E  2  186 ? 22.471  -36.467 11.665  1.00 104.84 ?  186  PHE E CB  1 
ATOM   12544 C CG  . PHE E  2  186 ? 22.307  -34.963 11.697  1.00 104.87 ?  186  PHE E CG  1 
ATOM   12545 C CD1 . PHE E  2  186 ? 21.160  -34.373 12.208  1.00 105.09 ?  186  PHE E CD1 1 
ATOM   12546 C CD2 . PHE E  2  186 ? 23.323  -34.141 11.241  1.00 104.85 ?  186  PHE E CD2 1 
ATOM   12547 C CE1 . PHE E  2  186 ? 21.023  -32.997 12.240  1.00 105.28 ?  186  PHE E CE1 1 
ATOM   12548 C CE2 . PHE E  2  186 ? 23.192  -32.765 11.271  1.00 105.07 ?  186  PHE E CE2 1 
ATOM   12549 C CZ  . PHE E  2  186 ? 22.041  -32.193 11.772  1.00 105.29 ?  186  PHE E CZ  1 
ATOM   12550 N N   . SER E  2  187 ? 20.942  -39.664 11.644  1.00 106.97 ?  187  SER E N   1 
ATOM   12551 C CA  . SER E  2  187 ? 21.205  -41.057 11.300  1.00 107.21 ?  187  SER E CA  1 
ATOM   12552 C C   . SER E  2  187 ? 20.720  -41.393 9.896   1.00 106.92 ?  187  SER E C   1 
ATOM   12553 O O   . SER E  2  187 ? 21.331  -42.221 9.211   1.00 107.05 ?  187  SER E O   1 
ATOM   12554 C CB  . SER E  2  187 ? 20.545  -41.981 12.324  1.00 107.91 ?  187  SER E CB  1 
ATOM   12555 O OG  . SER E  2  187 ? 19.182  -41.644 12.513  1.00 107.98 ?  187  SER E OG  1 
ATOM   12556 N N   . LEU E  2  188 ? 19.632  -40.770 9.453   1.00 103.58 ?  188  LEU E N   1 
ATOM   12557 C CA  . LEU E  2  188 ? 19.097  -40.997 8.118   1.00 103.37 ?  188  LEU E CA  1 
ATOM   12558 C C   . LEU E  2  188 ? 19.735  -40.098 7.069   1.00 102.88 ?  188  LEU E C   1 
ATOM   12559 O O   . LEU E  2  188 ? 19.417  -40.232 5.883   1.00 102.78 ?  188  LEU E O   1 
ATOM   12560 C CB  . LEU E  2  188 ? 17.577  -40.787 8.108   1.00 103.38 ?  188  LEU E CB  1 
ATOM   12561 C CG  . LEU E  2  188 ? 16.704  -41.526 9.129   1.00 103.99 ?  188  LEU E CG  1 
ATOM   12562 C CD1 . LEU E  2  188 ? 16.603  -40.762 10.446  1.00 104.13 ?  188  LEU E CD1 1 
ATOM   12563 C CD2 . LEU E  2  188 ? 15.321  -41.788 8.553   1.00 104.13 ?  188  LEU E CD2 1 
ATOM   12564 N N   . PHE E  2  189 ? 20.622  -39.194 7.472   1.00 102.70 ?  189  PHE E N   1 
ATOM   12565 C CA  . PHE E  2  189 ? 21.210  -38.225 6.561   1.00 102.38 ?  189  PHE E CA  1 
ATOM   12566 C C   . PHE E  2  189 ? 22.449  -38.801 5.885   1.00 102.53 ?  189  PHE E C   1 
ATOM   12567 O O   . PHE E  2  189 ? 23.170  -39.625 6.455   1.00 102.84 ?  189  PHE E O   1 
ATOM   12568 C CB  . PHE E  2  189 ? 21.559  -36.934 7.306   1.00 102.33 ?  189  PHE E CB  1 
ATOM   12569 C CG  . PHE E  2  189 ? 20.353  -36.161 7.776   1.00 102.28 ?  189  PHE E CG  1 
ATOM   12570 C CD1 . PHE E  2  189 ? 19.073  -36.548 7.405   1.00 102.19 ?  189  PHE E CD1 1 
ATOM   12571 C CD2 . PHE E  2  189 ? 20.498  -35.054 8.595   1.00 102.46 ?  189  PHE E CD2 1 
ATOM   12572 C CE1 . PHE E  2  189 ? 17.964  -35.845 7.836   1.00 102.23 ?  189  PHE E CE1 1 
ATOM   12573 C CE2 . PHE E  2  189 ? 19.390  -34.346 9.032   1.00 102.56 ?  189  PHE E CE2 1 
ATOM   12574 C CZ  . PHE E  2  189 ? 18.123  -34.743 8.650   1.00 102.42 ?  189  PHE E CZ  1 
ATOM   12575 N N   . THR E  2  190 ? 22.690  -38.352 4.659   1.00 102.41 ?  190  THR E N   1 
ATOM   12576 C CA  . THR E  2  190 ? 23.752  -38.848 3.801   1.00 102.68 ?  190  THR E CA  1 
ATOM   12577 C C   . THR E  2  190 ? 24.724  -37.719 3.473   1.00 102.64 ?  190  THR E C   1 
ATOM   12578 O O   . THR E  2  190 ? 24.386  -36.538 3.620   1.00 102.42 ?  190  THR E O   1 
ATOM   12579 C CB  . THR E  2  190 ? 23.169  -39.438 2.505   1.00 102.85 ?  190  THR E CB  1 
ATOM   12580 O OG1 . THR E  2  190 ? 23.028  -38.404 1.525   1.00 102.68 ?  190  THR E OG1 1 
ATOM   12581 C CG2 . THR E  2  190 ? 21.811  -40.077 2.765   1.00 102.85 ?  190  THR E CG2 1 
ATOM   12582 N N   . PRO E  2  191 ? 25.949  -38.045 3.040   1.00 102.98 ?  191  PRO E N   1 
ATOM   12583 C CA  . PRO E  2  191 ? 26.968  -36.998 2.834   1.00 103.10 ?  191  PRO E CA  1 
ATOM   12584 C C   . PRO E  2  191 ? 26.581  -35.888 1.861   1.00 103.04 ?  191  PRO E C   1 
ATOM   12585 O O   . PRO E  2  191 ? 27.321  -34.900 1.775   1.00 103.25 ?  191  PRO E O   1 
ATOM   12586 C CB  . PRO E  2  191 ? 28.175  -37.788 2.313   1.00 103.60 ?  191  PRO E CB  1 
ATOM   12587 C CG  . PRO E  2  191 ? 28.013  -39.133 2.919   1.00 103.70 ?  191  PRO E CG  1 
ATOM   12588 C CD  . PRO E  2  191 ? 26.532  -39.396 2.925   1.00 103.40 ?  191  PRO E CD  1 
ATOM   12589 N N   . ILE E  2  192 ? 25.472  -36.004 1.126   1.00 102.88 ?  192  ILE E N   1 
ATOM   12590 C CA  . ILE E  2  192 ? 25.085  -34.906 0.243   1.00 102.88 ?  192  ILE E CA  1 
ATOM   12591 C C   . ILE E  2  192 ? 24.596  -33.714 1.059   1.00 102.63 ?  192  ILE E C   1 
ATOM   12592 O O   . ILE E  2  192 ? 24.666  -32.566 0.601   1.00 102.80 ?  192  ILE E O   1 
ATOM   12593 C CB  . ILE E  2  192 ? 24.028  -35.375 -0.777  1.00 102.86 ?  192  ILE E CB  1 
ATOM   12594 C CG1 . ILE E  2  192 ? 23.776  -34.297 -1.836  1.00 103.02 ?  192  ILE E CG1 1 
ATOM   12595 C CG2 . ILE E  2  192 ? 22.723  -35.719 -0.082  1.00 102.45 ?  192  ILE E CG2 1 
ATOM   12596 C CD1 . ILE E  2  192 ? 25.040  -33.711 -2.435  1.00 103.56 ?  192  ILE E CD1 1 
ATOM   12597 N N   . SER E  2  193 ? 24.103  -33.958 2.275   1.00 102.37 ?  193  SER E N   1 
ATOM   12598 C CA  . SER E  2  193 ? 23.654  -32.862 3.127   1.00 102.31 ?  193  SER E CA  1 
ATOM   12599 C C   . SER E  2  193 ? 24.817  -32.008 3.617   1.00 102.70 ?  193  SER E C   1 
ATOM   12600 O O   . SER E  2  193 ? 24.627  -30.829 3.933   1.00 102.91 ?  193  SER E O   1 
ATOM   12601 C CB  . SER E  2  193 ? 22.869  -33.414 4.317   1.00 102.12 ?  193  SER E CB  1 
ATOM   12602 O OG  . SER E  2  193 ? 21.808  -34.246 3.885   1.00 101.89 ?  193  SER E OG  1 
ATOM   12603 N N   . PHE E  2  194 ? 26.020  -32.579 3.686   1.00 102.92 ?  194  PHE E N   1 
ATOM   12604 C CA  . PHE E  2  194 ? 27.177  -31.916 4.275   1.00 103.36 ?  194  PHE E CA  1 
ATOM   12605 C C   . PHE E  2  194 ? 28.323  -31.781 3.277   1.00 103.78 ?  194  PHE E C   1 
ATOM   12606 O O   . PHE E  2  194 ? 29.488  -31.702 3.671   1.00 104.19 ?  194  PHE E O   1 
ATOM   12607 C CB  . PHE E  2  194 ? 27.653  -32.655 5.526   1.00 103.40 ?  194  PHE E CB  1 
ATOM   12608 C CG  . PHE E  2  194 ? 26.541  -33.093 6.437   1.00 103.10 ?  194  PHE E CG  1 
ATOM   12609 C CD1 . PHE E  2  194 ? 25.855  -34.275 6.204   1.00 102.78 ?  194  PHE E CD1 1 
ATOM   12610 C CD2 . PHE E  2  194 ? 26.180  -32.320 7.528   1.00 103.32 ?  194  PHE E CD2 1 
ATOM   12611 C CE1 . PHE E  2  194 ? 24.834  -34.678 7.040   1.00 102.65 ?  194  PHE E CE1 1 
ATOM   12612 C CE2 . PHE E  2  194 ? 25.159  -32.718 8.367   1.00 103.19 ?  194  PHE E CE2 1 
ATOM   12613 C CZ  . PHE E  2  194 ? 24.485  -33.898 8.121   1.00 102.84 ?  194  PHE E CZ  1 
ATOM   12614 N N   . ALA E  2  195 ? 28.010  -31.763 1.984   1.00 103.78 ?  195  ALA E N   1 
ATOM   12615 C CA  . ALA E  2  195 ? 29.048  -31.684 0.967   1.00 104.33 ?  195  ALA E CA  1 
ATOM   12616 C C   . ALA E  2  195 ? 29.763  -30.339 1.025   1.00 104.94 ?  195  ALA E C   1 
ATOM   12617 O O   . ALA E  2  195 ? 29.193  -29.324 1.431   1.00 104.98 ?  195  ALA E O   1 
ATOM   12618 C CB  . ALA E  2  195 ? 28.451  -31.900 -0.423  1.00 104.35 ?  195  ALA E CB  1 
ATOM   12619 N N   . ASN E  2  196 ? 31.036  -30.347 0.625   1.00 105.57 ?  196  ASN E N   1 
ATOM   12620 C CA  . ASN E  2  196 ? 31.884  -29.155 0.582   1.00 106.38 ?  196  ASN E CA  1 
ATOM   12621 C C   . ASN E  2  196 ? 32.065  -28.516 1.957   1.00 106.50 ?  196  ASN E C   1 
ATOM   12622 O O   . ASN E  2  196 ? 32.374  -27.324 2.055   1.00 107.20 ?  196  ASN E O   1 
ATOM   12623 C CB  . ASN E  2  196 ? 31.334  -28.123 -0.412  1.00 106.74 ?  196  ASN E CB  1 
ATOM   12624 C CG  . ASN E  2  196 ? 32.411  -27.209 -0.964  1.00 107.85 ?  196  ASN E CG  1 
ATOM   12625 O OD1 . ASN E  2  196 ? 32.500  -26.040 -0.590  1.00 108.41 ?  196  ASN E OD1 1 
ATOM   12626 N ND2 . ASN E  2  196 ? 33.234  -27.738 -1.862  1.00 108.32 ?  196  ASN E ND2 1 
ATOM   12627 N N   . THR E  2  197 ? 31.876  -29.284 3.032   1.00 105.98 ?  197  THR E N   1 
ATOM   12628 C CA  . THR E  2  197 ? 32.028  -28.779 4.390   1.00 106.20 ?  197  THR E CA  1 
ATOM   12629 C C   . THR E  2  197 ? 32.733  -29.812 5.257   1.00 106.08 ?  197  THR E C   1 
ATOM   12630 O O   . THR E  2  197 ? 32.407  -31.002 5.209   1.00 105.50 ?  197  THR E O   1 
ATOM   12631 C CB  . THR E  2  197 ? 30.677  -28.431 5.046   1.00 105.79 ?  197  THR E CB  1 
ATOM   12632 O OG1 . THR E  2  197 ? 30.025  -29.633 5.474   1.00 105.05 ?  197  THR E OG1 1 
ATOM   12633 C CG2 . THR E  2  197 ? 29.763  -27.668 4.094   1.00 105.75 ?  197  THR E CG2 1 
ATOM   12634 N N   . LYS E  2  198 ? 33.694  -29.344 6.047   1.00 106.73 ?  198  LYS E N   1 
ATOM   12635 C CA  . LYS E  2  198 ? 34.276  -30.090 7.173   1.00 106.75 ?  198  LYS E CA  1 
ATOM   12636 C C   . LYS E  2  198 ? 34.898  -31.396 6.674   1.00 106.51 ?  198  LYS E C   1 
ATOM   12637 O O   . LYS E  2  198 ? 35.403  -31.474 5.547   1.00 106.71 ?  198  LYS E O   1 
ATOM   12638 C CB  . LYS E  2  198 ? 33.222  -30.292 8.243   1.00 106.34 ?  198  LYS E CB  1 
ATOM   12639 C CG  . LYS E  2  198 ? 32.240  -29.153 8.438   1.00 106.47 ?  198  LYS E CG  1 
ATOM   12640 C CD  . LYS E  2  198 ? 31.350  -29.438 9.634   1.00 106.27 ?  198  LYS E CD  1 
ATOM   12641 C CE  . LYS E  2  198 ? 30.707  -30.821 9.539   1.00 105.45 ?  198  LYS E CE  1 
ATOM   12642 N NZ  . LYS E  2  198 ? 30.231  -31.158 8.163   1.00 104.89 ?  198  LYS E NZ  1 
ATOM   12643 N N   . LEU E  2  199 ? 34.860  -32.419 7.525   1.00 106.21 ?  199  LEU E N   1 
ATOM   12644 C CA  . LEU E  2  199 ? 35.336  -33.758 7.202   1.00 106.06 ?  199  LEU E CA  1 
ATOM   12645 C C   . LEU E  2  199 ? 34.717  -34.776 8.154   1.00 105.66 ?  199  LEU E C   1 
ATOM   12646 O O   . LEU E  2  199 ? 34.365  -35.885 7.752   1.00 105.35 ?  199  LEU E O   1 
ATOM   12647 C CB  . LEU E  2  199 ? 36.860  -33.830 7.274   1.00 106.75 ?  199  LEU E CB  1 
ATOM   12648 C CG  . LEU E  2  199 ? 37.494  -34.951 6.448   1.00 106.84 ?  199  LEU E CG  1 
ATOM   12649 C CD1 . LEU E  2  199 ? 37.295  -34.704 4.961   1.00 106.89 ?  199  LEU E CD1 1 
ATOM   12650 C CD2 . LEU E  2  199 ? 38.970  -35.099 6.781   1.00 107.55 ?  199  LEU E CD2 1 
ATOM   12651 N N   . GLU F  3  1   ? 16.499  18.579  22.925  1.00 61.46  ?  1    GLU F N   1 
ATOM   12652 C CA  . GLU F  3  1   ? 16.218  19.093  21.587  1.00 62.05  ?  1    GLU F CA  1 
ATOM   12653 C C   . GLU F  3  1   ? 14.725  19.349  21.377  1.00 60.03  ?  1    GLU F C   1 
ATOM   12654 O O   . GLU F  3  1   ? 14.291  19.621  20.254  1.00 60.05  ?  1    GLU F O   1 
ATOM   12655 C CB  . GLU F  3  1   ? 16.734  18.119  20.514  1.00 61.09  ?  1    GLU F CB  1 
ATOM   12656 C CG  . GLU F  3  1   ? 18.240  18.194  20.202  1.00 64.09  ?  1    GLU F CG  1 
ATOM   12657 C CD  . GLU F  3  1   ? 19.151  17.897  21.389  1.00 65.11  ?  1    GLU F CD  1 
ATOM   12658 O OE1 . GLU F  3  1   ? 18.658  17.548  22.483  1.00 63.42  ?  1    GLU F OE1 1 
ATOM   12659 O OE2 . GLU F  3  1   ? 20.382  18.019  21.219  1.00 67.88  -1 1    GLU F OE2 1 
ATOM   12660 N N   . SER F  3  2   ? 13.956  19.246  22.466  1.00 58.48  ?  2    SER F N   1 
ATOM   12661 C CA  . SER F  3  2   ? 12.496  19.348  22.475  1.00 56.41  ?  2    SER F CA  1 
ATOM   12662 C C   . SER F  3  2   ? 11.853  18.239  21.649  1.00 53.28  ?  2    SER F C   1 
ATOM   12663 O O   . SER F  3  2   ? 12.428  17.782  20.658  1.00 53.35  ?  2    SER F O   1 
ATOM   12664 C CB  . SER F  3  2   ? 12.051  20.720  21.963  1.00 58.66  ?  2    SER F CB  1 
ATOM   12665 O OG  . SER F  3  2   ? 10.639  20.840  21.966  1.00 56.88  ?  2    SER F OG  1 
ATOM   12666 N N   . SER F  3  3   ? 10.670  17.771  22.047  1.00 50.71  ?  3    SER F N   1 
ATOM   12667 C CA  . SER F  3  3   ? 10.034  16.706  21.278  1.00 47.96  ?  3    SER F CA  1 
ATOM   12668 C C   . SER F  3  3   ? 8.672   17.038  20.689  1.00 46.96  ?  3    SER F C   1 
ATOM   12669 O O   . SER F  3  3   ? 8.502   16.966  19.466  1.00 46.89  ?  3    SER F O   1 
ATOM   12670 C CB  . SER F  3  3   ? 9.893   15.489  22.179  1.00 45.59  ?  3    SER F CB  1 
ATOM   12671 O OG  . SER F  3  3   ? 9.222   15.843  23.376  1.00 45.40  ?  3    SER F OG  1 
ATOM   12672 N N   . SER F  3  4   ? 7.709   17.434  21.519  1.00 46.47  ?  4    SER F N   1 
ATOM   12673 C CA  . SER F  3  4   ? 6.296   17.443  21.140  1.00 45.03  ?  4    SER F CA  1 
ATOM   12674 C C   . SER F  3  4   ? 5.917   16.128  20.454  1.00 42.45  ?  4    SER F C   1 
ATOM   12675 O O   . SER F  3  4   ? 5.566   16.099  19.275  1.00 42.34  ?  4    SER F O   1 
ATOM   12676 C CB  . SER F  3  4   ? 5.967   18.643  20.248  1.00 47.11  ?  4    SER F CB  1 
ATOM   12677 O OG  . SER F  3  4   ? 4.738   18.446  19.567  1.00 45.74  ?  4    SER F OG  1 
ATOM   12678 N N   . SER F  3  5   ? 6.037   15.027  21.207  1.00 40.63  ?  5    SER F N   1 
ATOM   12679 C CA  . SER F  3  5   ? 5.847   13.690  20.647  1.00 38.43  ?  5    SER F CA  1 
ATOM   12680 C C   . SER F  3  5   ? 4.516   13.577  19.911  1.00 37.24  ?  5    SER F C   1 
ATOM   12681 O O   . SER F  3  5   ? 3.540   14.263  20.228  1.00 37.44  ?  5    SER F O   1 
ATOM   12682 C CB  . SER F  3  5   ? 5.915   12.626  21.749  1.00 36.85  ?  5    SER F CB  1 
ATOM   12683 O OG  . SER F  3  5   ? 5.221   13.037  22.915  1.00 36.82  ?  5    SER F OG  1 
ATOM   12684 N N   . HIS F  3  6   ? 4.477   12.678  18.928  1.00 36.13  ?  6    HIS F N   1 
ATOM   12685 C CA  . HIS F  3  6   ? 3.407   12.630  17.940  1.00 35.57  ?  6    HIS F CA  1 
ATOM   12686 C C   . HIS F  3  6   ? 2.603   11.343  18.058  1.00 33.25  ?  6    HIS F C   1 
ATOM   12687 O O   . HIS F  3  6   ? 3.165   10.245  17.997  1.00 32.25  ?  6    HIS F O   1 
ATOM   12688 C CB  . HIS F  3  6   ? 3.971   12.757  16.523  1.00 36.74  ?  6    HIS F CB  1 
ATOM   12689 C CG  . HIS F  3  6   ? 2.938   13.084  15.491  1.00 37.01  ?  6    HIS F CG  1 
ATOM   12690 N ND1 . HIS F  3  6   ? 2.304   12.116  14.742  1.00 35.66  ?  6    HIS F ND1 1 
ATOM   12691 C CD2 . HIS F  3  6   ? 2.426   14.270  15.084  1.00 38.72  ?  6    HIS F CD2 1 
ATOM   12692 C CE1 . HIS F  3  6   ? 1.445   12.691  13.919  1.00 36.51  ?  6    HIS F CE1 1 
ATOM   12693 N NE2 . HIS F  3  6   ? 1.500   13.997  14.106  1.00 38.36  ?  6    HIS F NE2 1 
ATOM   12694 N N   . SER F  3  7   ? 1.288   11.488  18.216  1.00 32.62  ?  7    SER F N   1 
ATOM   12695 C CA  . SER F  3  7   ? 0.370   10.359  18.147  1.00 30.80  ?  7    SER F CA  1 
ATOM   12696 C C   . SER F  3  7   ? 0.057   10.027  16.694  1.00 30.83  ?  7    SER F C   1 
ATOM   12697 O O   . SER F  3  7   ? -0.343  10.903  15.921  1.00 32.08  ?  7    SER F O   1 
ATOM   12698 C CB  . SER F  3  7   ? -0.920  10.671  18.897  1.00 30.42  ?  7    SER F CB  1 
ATOM   12699 O OG  . SER F  3  7   ? -1.865  9.625   18.737  1.00 28.99  ?  7    SER F OG  1 
ATOM   12700 N N   . GLU F  3  8   ? 0.231   8.763   16.329  1.00 29.65  ?  8    GLU F N   1 
ATOM   12701 C CA  . GLU F  3  8   ? 0.077   8.320   14.952  1.00 29.82  ?  8    GLU F CA  1 
ATOM   12702 C C   . GLU F  3  8   ? -1.255  7.609   14.766  1.00 28.77  ?  8    GLU F C   1 
ATOM   12703 O O   . GLU F  3  8   ? -1.693  6.849   15.635  1.00 27.50  ?  8    GLU F O   1 
ATOM   12704 C CB  . GLU F  3  8   ? 1.233   7.406   14.551  1.00 29.60  ?  8    GLU F CB  1 
ATOM   12705 C CG  . GLU F  3  8   ? 2.587   8.033   14.815  1.00 30.78  ?  8    GLU F CG  1 
ATOM   12706 C CD  . GLU F  3  8   ? 3.528   7.903   13.642  1.00 31.90  ?  8    GLU F CD  1 
ATOM   12707 O OE1 . GLU F  3  8   ? 3.515   6.842   12.984  1.00 31.24  ?  8    GLU F OE1 1 
ATOM   12708 O OE2 . GLU F  3  8   ? 4.274   8.867   13.371  1.00 33.66  -1 8    GLU F OE2 1 
ATOM   12709 N N   . ARG F  3  9   ? -1.898  7.876   13.632  1.00 29.57  ?  9    ARG F N   1 
ATOM   12710 C CA  . ARG F  3  9   ? -3.215  7.328   13.349  1.00 29.02  ?  9    ARG F CA  1 
ATOM   12711 C C   . ARG F  3  9   ? -3.197  5.804   13.421  1.00 27.65  ?  9    ARG F C   1 
ATOM   12712 O O   . ARG F  3  9   ? -2.161  5.154   13.254  1.00 27.38  ?  9    ARG F O   1 
ATOM   12713 C CB  . ARG F  3  9   ? -3.689  7.782   11.968  1.00 30.44  ?  9    ARG F CB  1 
ATOM   12714 C CG  . ARG F  3  9   ? -3.731  9.290   11.796  1.00 32.15  ?  9    ARG F CG  1 
ATOM   12715 C CD  . ARG F  3  9   ? -4.247  9.682   10.422  1.00 33.78  ?  9    ARG F CD  1 
ATOM   12716 N NE  . ARG F  3  9   ? -3.388  10.672  9.785   1.00 35.68  ?  9    ARG F NE  1 
ATOM   12717 C CZ  . ARG F  3  9   ? -2.454  10.389  8.887   1.00 36.42  ?  9    ARG F CZ  1 
ATOM   12718 N NH1 . ARG F  3  9   ? -2.227  9.147   8.494   1.00 35.39  ?  9    ARG F NH1 1 
ATOM   12719 N NH2 . ARG F  3  9   ? -1.727  11.378  8.373   1.00 38.43  ?  9    ARG F NH2 1 
ATOM   12720 N N   . ALA F  3  10  ? -4.373  5.233   13.665  1.00 26.99  ?  10   ALA F N   1 
ATOM   12721 C CA  . ALA F  3  10  ? -4.494  3.792   13.790  1.00 25.94  ?  10   ALA F CA  1 
ATOM   12722 C C   . ALA F  3  10  ? -4.407  3.138   12.413  1.00 26.47  ?  10   ALA F C   1 
ATOM   12723 O O   . ALA F  3  10  ? -4.296  3.805   11.380  1.00 27.66  ?  10   ALA F O   1 
ATOM   12724 C CB  . ALA F  3  10  ? -5.798  3.427   14.494  1.00 25.42  ?  10   ALA F CB  1 
ATOM   12725 N N   . GLY F  3  11  ? -4.478  1.813   12.398  1.00 25.79  ?  11   GLY F N   1 
ATOM   12726 C CA  . GLY F  3  11  ? -4.330  1.066   11.169  1.00 26.37  ?  11   GLY F CA  1 
ATOM   12727 C C   . GLY F  3  11  ? -5.639  0.907   10.417  1.00 27.09  ?  11   GLY F C   1 
ATOM   12728 O O   . GLY F  3  11  ? -6.710  0.787   11.008  1.00 26.78  ?  11   GLY F O   1 
ATOM   12729 N N   . GLY F  3  12  ? -5.535  0.919   9.090   1.00 28.28  ?  12   GLY F N   1 
ATOM   12730 C CA  . GLY F  3  12  ? -6.658  0.641   8.228   1.00 29.28  ?  12   GLY F CA  1 
ATOM   12731 C C   . GLY F  3  12  ? -6.604  -0.783  7.707   1.00 29.33  ?  12   GLY F C   1 
ATOM   12732 O O   . GLY F  3  12  ? -5.572  -1.447  7.763   1.00 28.85  ?  12   GLY F O   1 
ATOM   12733 N N   . ARG F  3  13  ? -7.738  -1.255  7.205   1.00 30.59  ?  13   ARG F N   1 
ATOM   12734 C CA  . ARG F  3  13  ? -7.821  -2.625  6.716   1.00 30.93  ?  13   ARG F CA  1 
ATOM   12735 C C   . ARG F  3  13  ? -7.670  -2.674  5.201   1.00 32.65  ?  13   ARG F C   1 
ATOM   12736 O O   . ARG F  3  13  ? -6.903  -1.908  4.619   1.00 33.24  ?  13   ARG F O   1 
ATOM   12737 C CB  . ARG F  3  13  ? -9.141  -3.267  7.138   1.00 31.02  ?  13   ARG F CB  1 
ATOM   12738 C CG  . ARG F  3  13  ? -9.388  -4.632  6.522   1.00 31.85  ?  13   ARG F CG  1 
ATOM   12739 C CD  . ARG F  3  13  ? -10.630 -5.269  7.112   1.00 32.02  ?  13   ARG F CD  1 
ATOM   12740 N NE  . ARG F  3  13  ? -10.410 -5.742  8.472   1.00 30.59  ?  13   ARG F NE  1 
ATOM   12741 C CZ  . ARG F  3  13  ? -10.426 -7.018  8.831   1.00 30.59  ?  13   ARG F CZ  1 
ATOM   12742 N NH1 . ARG F  3  13  ? -10.673 -7.980  7.956   1.00 31.91  ?  13   ARG F NH1 1 
ATOM   12743 N NH2 . ARG F  3  13  ? -10.192 -7.338  10.100  1.00 29.45  ?  13   ARG F NH2 1 
HETATM 12744 C C1  . NAG G  4  .   ? 52.162  -11.981 110.498 1.00 66.80  ?  1    NAG G C1  1 
HETATM 12745 C C2  . NAG G  4  .   ? 53.190  -11.176 111.291 1.00 65.57  ?  1    NAG G C2  1 
HETATM 12746 C C3  . NAG G  4  .   ? 52.782  -11.128 112.766 1.00 64.48  ?  1    NAG G C3  1 
HETATM 12747 C C4  . NAG G  4  .   ? 51.355  -10.612 112.916 1.00 63.88  ?  1    NAG G C4  1 
HETATM 12748 C C5  . NAG G  4  .   ? 50.412  -11.433 112.029 1.00 64.43  ?  1    NAG G C5  1 
HETATM 12749 C C6  . NAG G  4  .   ? 48.987  -10.928 112.002 1.00 63.50  ?  1    NAG G C6  1 
HETATM 12750 C C7  . NAG G  4  .   ? 55.443  -11.271 110.299 1.00 66.10  ?  1    NAG G C7  1 
HETATM 12751 C C8  . NAG G  4  .   ? 55.043  -10.070 109.492 1.00 65.66  ?  1    NAG G C8  1 
HETATM 12752 N N2  . NAG G  4  .   ? 54.519  -11.751 111.141 1.00 66.12  ?  1    NAG G N2  1 
HETATM 12753 O O3  . NAG G  4  .   ? 53.687  -10.384 113.581 1.00 63.84  ?  1    NAG G O3  1 
HETATM 12754 O O4  . NAG G  4  .   ? 50.975  -10.733 114.284 1.00 63.50  ?  1    NAG G O4  1 
HETATM 12755 O O5  . NAG G  4  .   ? 50.873  -11.409 110.671 1.00 65.60  ?  1    NAG G O5  1 
HETATM 12756 O O6  . NAG G  4  .   ? 48.937  -9.532  111.740 1.00 63.12  ?  1    NAG G O6  1 
HETATM 12757 O O7  . NAG G  4  .   ? 56.555  -11.780 110.198 1.00 66.30  ?  1    NAG G O7  1 
HETATM 12758 C C1  . FUC G  4  .   ? 54.297  -9.222  112.986 1.00 69.32  ?  2    FUC G C1  1 
HETATM 12759 C C2  . FUC G  4  .   ? 54.063  -8.030  113.957 1.00 68.79  ?  2    FUC G C2  1 
HETATM 12760 C C3  . FUC G  4  .   ? 54.996  -6.805  113.702 1.00 68.51  ?  2    FUC G C3  1 
HETATM 12761 C C4  . FUC G  4  .   ? 56.342  -7.191  113.057 1.00 68.56  ?  2    FUC G C4  1 
HETATM 12762 C C5  . FUC G  4  .   ? 56.651  -8.650  113.342 1.00 68.93  ?  2    FUC G C5  1 
HETATM 12763 C C6  . FUC G  4  .   ? 57.998  -9.096  112.787 1.00 68.86  ?  2    FUC G C6  1 
HETATM 12764 O O2  . FUC G  4  .   ? 54.113  -8.433  115.326 1.00 68.70  ?  2    FUC G O2  1 
HETATM 12765 O O3  . FUC G  4  .   ? 54.351  -5.859  112.849 1.00 68.40  ?  2    FUC G O3  1 
HETATM 12766 O O4  . FUC G  4  .   ? 56.288  -6.978  111.655 1.00 68.59  ?  2    FUC G O4  1 
HETATM 12767 O O5  . FUC G  4  .   ? 55.663  -9.506  112.740 1.00 69.28  ?  2    FUC G O5  1 
HETATM 12768 C C1  . NAG G  4  .   ? 50.211  -9.601  114.780 1.00 72.96  ?  3    NAG G C1  1 
HETATM 12769 C C2  . NAG G  4  .   ? 49.767  -9.934  116.205 1.00 72.93  ?  3    NAG G C2  1 
HETATM 12770 C C3  . NAG G  4  .   ? 48.933  -8.790  116.772 1.00 73.08  ?  3    NAG G C3  1 
HETATM 12771 C C4  . NAG G  4  .   ? 49.693  -7.474  116.662 1.00 72.80  ?  3    NAG G C4  1 
HETATM 12772 C C5  . NAG G  4  .   ? 50.173  -7.245  115.229 1.00 72.68  ?  3    NAG G C5  1 
HETATM 12773 C C6  . NAG G  4  .   ? 51.046  -6.021  115.086 1.00 72.54  ?  3    NAG G C6  1 
HETATM 12774 C C7  . NAG G  4  .   ? 49.606  -12.376 116.389 1.00 72.80  ?  3    NAG G C7  1 
HETATM 12775 C C8  . NAG G  4  .   ? 48.686  -13.559 116.407 1.00 72.74  ?  3    NAG G C8  1 
HETATM 12776 N N2  . NAG G  4  .   ? 49.022  -11.182 116.243 1.00 72.85  ?  3    NAG G N2  1 
HETATM 12777 O O3  . NAG G  4  .   ? 48.619  -9.061  118.133 1.00 75.71  ?  3    NAG G O3  1 
HETATM 12778 O O4  . NAG G  4  .   ? 48.850  -6.395  117.050 1.00 72.74  ?  3    NAG G O4  1 
HETATM 12779 O O5  . NAG G  4  .   ? 50.952  -8.366  114.783 1.00 72.79  ?  3    NAG G O5  1 
HETATM 12780 O O6  . NAG G  4  .   ? 51.540  -5.887  113.760 1.00 72.46  ?  3    NAG G O6  1 
HETATM 12781 O O7  . NAG G  4  .   ? 50.822  -12.495 116.500 1.00 72.79  ?  3    NAG G O7  1 
HETATM 12782 C C1  . FUC G  4  .   ? 47.623  -9.181  111.255 1.00 72.06  ?  4    FUC G C1  1 
HETATM 12783 C C2  . FUC G  4  .   ? 47.799  -8.018  110.247 1.00 71.85  ?  4    FUC G C2  1 
HETATM 12784 C C3  . FUC G  4  .   ? 46.962  -8.243  108.980 1.00 71.66  ?  4    FUC G C3  1 
HETATM 12785 C C4  . FUC G  4  .   ? 45.559  -8.733  109.350 1.00 71.67  ?  4    FUC G C4  1 
HETATM 12786 C C5  . FUC G  4  .   ? 45.666  -10.078 110.087 1.00 71.98  ?  4    FUC G C5  1 
HETATM 12787 C C6  . FUC G  4  .   ? 44.663  -10.229 111.226 1.00 71.98  ?  4    FUC G C6  1 
HETATM 12788 O O2  . FUC G  4  .   ? 49.165  -7.791  109.920 1.00 71.90  ?  4    FUC G O2  1 
HETATM 12789 O O3  . FUC G  4  .   ? 46.822  -7.022  108.260 1.00 71.54  ?  4    FUC G O3  1 
HETATM 12790 O O4  . FUC G  4  .   ? 44.904  -7.774  110.168 1.00 71.58  ?  4    FUC G O4  1 
HETATM 12791 O O5  . FUC G  4  .   ? 46.985  -10.300 110.657 1.00 72.23  ?  4    FUC G O5  1 
HETATM 12792 C C1  . NAG H  5  .   ? 35.284  17.187  61.838  1.00 57.51  ?  1    NAG H C1  1 
HETATM 12793 C C2  . NAG H  5  .   ? 36.257  17.752  62.868  1.00 56.97  ?  1    NAG H C2  1 
HETATM 12794 C C3  . NAG H  5  .   ? 37.178  18.780  62.214  1.00 55.89  ?  1    NAG H C3  1 
HETATM 12795 C C4  . NAG H  5  .   ? 37.841  18.199  60.969  1.00 54.97  ?  1    NAG H C4  1 
HETATM 12796 C C5  . NAG H  5  .   ? 36.795  17.581  60.045  1.00 57.00  ?  1    NAG H C5  1 
HETATM 12797 C C6  . NAG H  5  .   ? 37.397  16.856  58.865  1.00 56.11  ?  1    NAG H C6  1 
HETATM 12798 C C7  . NAG H  5  .   ? 35.609  17.862  65.235  1.00 57.93  ?  1    NAG H C7  1 
HETATM 12799 C C8  . NAG H  5  .   ? 34.811  18.601  66.267  1.00 60.07  ?  1    NAG H C8  1 
HETATM 12800 N N2  . NAG H  5  .   ? 35.545  18.344  63.989  1.00 58.19  ?  1    NAG H N2  1 
HETATM 12801 O O3  . NAG H  5  .   ? 38.161  19.190  63.158  1.00 54.26  ?  1    NAG H O3  1 
HETATM 12802 O O4  . NAG H  5  .   ? 38.511  19.224  60.243  1.00 54.98  ?  1    NAG H O4  1 
HETATM 12803 O O5  . NAG H  5  .   ? 36.009  16.619  60.761  1.00 56.58  ?  1    NAG H O5  1 
HETATM 12804 O O6  . NAG H  5  .   ? 36.391  16.345  58.001  1.00 56.21  ?  1    NAG H O6  1 
HETATM 12805 O O7  . NAG H  5  .   ? 36.280  16.874  65.516  1.00 56.77  ?  1    NAG H O7  1 
HETATM 12806 C C1  . NAG H  5  .   ? 39.903  19.303  60.603  1.00 64.19  ?  2    NAG H C1  1 
HETATM 12807 C C2  . NAG H  5  .   ? 40.765  19.246  59.341  1.00 64.02  ?  2    NAG H C2  1 
HETATM 12808 C C3  . NAG H  5  .   ? 42.239  19.428  59.696  1.00 62.17  ?  2    NAG H C3  1 
HETATM 12809 C C4  . NAG H  5  .   ? 42.438  20.699  60.511  1.00 61.52  ?  2    NAG H C4  1 
HETATM 12810 C C5  . NAG H  5  .   ? 41.521  20.687  61.729  1.00 61.69  ?  2    NAG H C5  1 
HETATM 12811 C C6  . NAG H  5  .   ? 41.579  21.970  62.525  1.00 60.54  ?  2    NAG H C6  1 
HETATM 12812 C C7  . NAG H  5  .   ? 40.391  17.933  57.300  1.00 65.26  ?  2    NAG H C7  1 
HETATM 12813 C C8  . NAG H  5  .   ? 40.210  16.560  56.725  1.00 64.52  ?  2    NAG H C8  1 
HETATM 12814 N N2  . NAG H  5  .   ? 40.567  17.996  58.625  1.00 64.53  ?  2    NAG H N2  1 
HETATM 12815 O O3  . NAG H  5  .   ? 43.009  19.490  58.501  1.00 61.62  ?  2    NAG H O3  1 
HETATM 12816 O O4  . NAG H  5  .   ? 43.791  20.795  60.942  1.00 60.48  ?  2    NAG H O4  1 
HETATM 12817 O O5  . NAG H  5  .   ? 40.159  20.524  61.308  1.00 62.96  ?  2    NAG H O5  1 
HETATM 12818 O O6  . NAG H  5  .   ? 42.158  23.025  61.769  1.00 59.95  ?  2    NAG H O6  1 
HETATM 12819 O O7  . NAG H  5  .   ? 40.378  18.939  56.598  1.00 65.96  ?  2    NAG H O7  1 
HETATM 12820 C C1  . NAG I  5  .   ? 47.222  -45.785 119.804 1.00 50.21  ?  1    NAG I C1  1 
HETATM 12821 C C2  . NAG I  5  .   ? 48.023  -46.993 119.311 1.00 47.79  ?  1    NAG I C2  1 
HETATM 12822 C C3  . NAG I  5  .   ? 48.438  -47.868 120.488 1.00 45.10  ?  1    NAG I C3  1 
HETATM 12823 C C4  . NAG I  5  .   ? 49.183  -47.034 121.521 1.00 43.68  ?  1    NAG I C4  1 
HETATM 12824 C C5  . NAG I  5  .   ? 48.328  -45.843 121.943 1.00 45.00  ?  1    NAG I C5  1 
HETATM 12825 C C6  . NAG I  5  .   ? 49.037  -44.913 122.899 1.00 43.70  ?  1    NAG I C6  1 
HETATM 12826 C C7  . NAG I  5  .   ? 47.510  -47.717 117.025 1.00 49.26  ?  1    NAG I C7  1 
HETATM 12827 C C8  . NAG I  5  .   ? 46.638  -48.576 116.162 1.00 47.08  ?  1    NAG I C8  1 
HETATM 12828 N N2  . NAG I  5  .   ? 47.266  -47.765 118.339 1.00 48.46  ?  1    NAG I N2  1 
HETATM 12829 O O3  . NAG I  5  .   ? 49.268  -48.927 120.025 1.00 43.80  ?  1    NAG I O3  1 
HETATM 12830 O O4  . NAG I  5  .   ? 49.518  -47.825 122.655 1.00 41.57  ?  1    NAG I O4  1 
HETATM 12831 O O5  . NAG I  5  .   ? 47.986  -45.064 120.786 1.00 48.23  ?  1    NAG I O5  1 
HETATM 12832 O O6  . NAG I  5  .   ? 50.240  -44.410 122.334 1.00 43.32  ?  1    NAG I O6  1 
HETATM 12833 O O7  . NAG I  5  .   ? 48.397  -47.012 116.554 1.00 50.90  ?  1    NAG I O7  1 
HETATM 12834 C C1  . NAG I  5  .   ? 50.955  -47.951 122.655 1.00 56.35  ?  2    NAG I C1  1 
HETATM 12835 C C2  . NAG I  5  .   ? 51.414  -48.493 124.007 1.00 55.52  ?  2    NAG I C2  1 
HETATM 12836 C C3  . NAG I  5  .   ? 52.929  -48.682 124.010 1.00 54.79  ?  2    NAG I C3  1 
HETATM 12837 C C4  . NAG I  5  .   ? 53.362  -49.538 122.827 1.00 54.64  ?  2    NAG I C4  1 
HETATM 12838 C C5  . NAG I  5  .   ? 52.815  -48.962 121.524 1.00 55.16  ?  2    NAG I C5  1 
HETATM 12839 C C6  . NAG I  5  .   ? 53.102  -49.834 120.323 1.00 54.93  ?  2    NAG I C6  1 
HETATM 12840 C C7  . NAG I  5  .   ? 49.836  -47.724 125.723 1.00 55.21  ?  2    NAG I C7  1 
HETATM 12841 C C8  . NAG I  5  .   ? 49.580  -46.726 126.813 1.00 54.66  ?  2    NAG I C8  1 
HETATM 12842 N N2  . NAG I  5  .   ? 51.007  -47.610 125.088 1.00 55.30  ?  2    NAG I N2  1 
HETATM 12843 O O3  . NAG I  5  .   ? 53.328  -49.296 125.230 1.00 54.49  ?  2    NAG I O3  1 
HETATM 12844 O O4  . NAG I  5  .   ? 54.783  -49.585 122.756 1.00 54.35  ?  2    NAG I O4  1 
HETATM 12845 O O5  . NAG I  5  .   ? 51.388  -48.833 121.609 1.00 56.01  ?  2    NAG I O5  1 
HETATM 12846 O O6  . NAG I  5  .   ? 52.329  -49.439 119.198 1.00 55.39  ?  2    NAG I O6  1 
HETATM 12847 O O7  . NAG I  5  .   ? 49.020  -48.592 125.432 1.00 55.16  ?  2    NAG I O7  1 
HETATM 12848 C C1  . NAG J  5  .   ? 37.347  -37.342 103.233 1.00 55.34  ?  1    NAG J C1  1 
HETATM 12849 C C2  . NAG J  5  .   ? 37.620  -38.551 102.346 1.00 54.50  ?  1    NAG J C2  1 
HETATM 12850 C C3  . NAG J  5  .   ? 37.520  -38.155 100.877 1.00 53.70  ?  1    NAG J C3  1 
HETATM 12851 C C4  . NAG J  5  .   ? 36.181  -37.484 100.594 1.00 53.06  ?  1    NAG J C4  1 
HETATM 12852 C C5  . NAG J  5  .   ? 35.931  -36.343 101.579 1.00 53.20  ?  1    NAG J C5  1 
HETATM 12853 C C6  . NAG J  5  .   ? 34.547  -35.749 101.453 1.00 52.96  ?  1    NAG J C6  1 
HETATM 12854 C C7  . NAG J  5  .   ? 39.092  -40.165 103.464 1.00 57.59  ?  1    NAG J C7  1 
HETATM 12855 C C8  . NAG J  5  .   ? 40.504  -40.637 103.645 1.00 61.47  ?  1    NAG J C8  1 
HETATM 12856 N N2  . NAG J  5  .   ? 38.922  -39.131 102.634 1.00 56.12  ?  1    NAG J N2  1 
HETATM 12857 O O3  . NAG J  5  .   ? 37.672  -39.318 100.070 1.00 53.35  ?  1    NAG J O3  1 
HETATM 12858 O O4  . NAG J  5  .   ? 36.177  -36.945 99.277  1.00 52.66  ?  1    NAG J O4  1 
HETATM 12859 O O5  . NAG J  5  .   ? 36.058  -36.810 102.931 1.00 54.10  ?  1    NAG J O5  1 
HETATM 12860 O O6  . NAG J  5  .   ? 33.845  -35.804 102.688 1.00 54.30  ?  1    NAG J O6  1 
HETATM 12861 O O7  . NAG J  5  .   ? 38.150  -40.695 104.044 1.00 57.07  ?  1    NAG J O7  1 
HETATM 12862 C C1  . NAG J  5  .   ? 35.508  -37.838 98.367  1.00 69.43  ?  2    NAG J C1  1 
HETATM 12863 C C2  . NAG J  5  .   ? 34.902  -37.018 97.229  1.00 69.33  ?  2    NAG J C2  1 
HETATM 12864 C C3  . NAG J  5  .   ? 34.247  -37.940 96.204  1.00 69.30  ?  2    NAG J C3  1 
HETATM 12865 C C4  . NAG J  5  .   ? 35.234  -38.999 95.732  1.00 69.32  ?  2    NAG J C4  1 
HETATM 12866 C C5  . NAG J  5  .   ? 35.824  -39.739 96.929  1.00 69.36  ?  2    NAG J C5  1 
HETATM 12867 C C6  . NAG J  5  .   ? 36.905  -40.721 96.543  1.00 69.35  ?  2    NAG J C6  1 
HETATM 12868 C C7  . NAG J  5  .   ? 34.183  -34.739 97.807  1.00 69.26  ?  2    NAG J C7  1 
HETATM 12869 C C8  . NAG J  5  .   ? 35.531  -34.290 97.326  1.00 69.25  ?  2    NAG J C8  1 
HETATM 12870 N N2  . NAG J  5  .   ? 33.940  -36.052 97.736  1.00 69.31  ?  2    NAG J N2  1 
HETATM 12871 O O3  . NAG J  5  .   ? 33.794  -37.170 95.096  1.00 69.29  ?  2    NAG J O3  1 
HETATM 12872 O O4  . NAG J  5  .   ? 34.578  -39.933 94.881  1.00 69.32  ?  2    NAG J O4  1 
HETATM 12873 O O5  . NAG J  5  .   ? 36.424  -38.800 97.834  1.00 69.41  ?  2    NAG J O5  1 
HETATM 12874 O O6  . NAG J  5  .   ? 38.117  -40.056 96.214  1.00 69.36  ?  2    NAG J O6  1 
HETATM 12875 O O7  . NAG J  5  .   ? 33.351  -33.947 98.239  1.00 69.26  ?  2    NAG J O7  1 
HETATM 12876 C C1  . NAG K  5  .   ? 56.141  -27.615 54.828  1.00 86.57  ?  1    NAG K C1  1 
HETATM 12877 C C2  . NAG K  5  .   ? 57.593  -28.090 54.975  1.00 81.89  ?  1    NAG K C2  1 
HETATM 12878 C C3  . NAG K  5  .   ? 57.952  -29.092 53.883  1.00 77.15  ?  1    NAG K C3  1 
HETATM 12879 C C4  . NAG K  5  .   ? 57.139  -30.368 54.051  1.00 75.51  ?  1    NAG K C4  1 
HETATM 12880 C C5  . NAG K  5  .   ? 55.680  -30.065 54.416  1.00 79.75  ?  1    NAG K C5  1 
HETATM 12881 C C6  . NAG K  5  .   ? 55.319  -30.421 55.843  1.00 80.45  ?  1    NAG K C6  1 
HETATM 12882 C C7  . NAG K  5  .   ? 58.855  -26.044 54.148  1.00 80.08  ?  1    NAG K C7  1 
HETATM 12883 C C8  . NAG K  5  .   ? 58.105  -26.063 52.840  1.00 79.58  ?  1    NAG K C8  1 
HETATM 12884 N N2  . NAG K  5  .   ? 58.564  -26.998 55.060  1.00 81.16  ?  1    NAG K N2  1 
HETATM 12885 O O3  . NAG K  5  .   ? 59.342  -29.389 53.948  1.00 75.25  ?  1    NAG K O3  1 
HETATM 12886 O O4  . NAG K  5  .   ? 57.169  -31.091 52.823  1.00 73.17  ?  1    NAG K O4  1 
HETATM 12887 O O5  . NAG K  5  .   ? 55.322  -28.683 54.209  1.00 83.87  ?  1    NAG K O5  1 
HETATM 12888 O O6  . NAG K  5  .   ? 54.171  -31.256 55.897  1.00 78.74  ?  1    NAG K O6  1 
HETATM 12889 O O7  . NAG K  5  .   ? 59.705  -25.189 54.378  1.00 78.95  ?  1    NAG K O7  1 
HETATM 12890 C C1  . NAG K  5  .   ? 57.208  -32.541 52.954  1.00 82.41  ?  2    NAG K C1  1 
HETATM 12891 C C2  . NAG K  5  .   ? 58.488  -32.979 53.683  1.00 81.32  ?  2    NAG K C2  1 
HETATM 12892 C C3  . NAG K  5  .   ? 58.512  -34.500 53.831  1.00 80.22  ?  2    NAG K C3  1 
HETATM 12893 C C4  . NAG K  5  .   ? 57.229  -34.997 54.485  1.00 80.14  ?  2    NAG K C4  1 
HETATM 12894 C C5  . NAG K  5  .   ? 56.009  -34.480 53.728  1.00 80.99  ?  2    NAG K C5  1 
HETATM 12895 C C6  . NAG K  5  .   ? 54.701  -34.849 54.389  1.00 80.65  ?  2    NAG K C6  1 
HETATM 12896 C C7  . NAG K  5  .   ? 60.880  -32.428 53.549  1.00 80.46  ?  2    NAG K C7  1 
HETATM 12897 C C8  . NAG K  5  .   ? 61.987  -31.930 52.670  1.00 79.79  ?  2    NAG K C8  1 
HETATM 12898 N N2  . NAG K  5  .   ? 59.673  -32.515 52.979  1.00 80.95  ?  2    NAG K N2  1 
HETATM 12899 O O3  . NAG K  5  .   ? 59.634  -34.893 54.614  1.00 79.81  ?  2    NAG K O3  1 
HETATM 12900 O O4  . NAG K  5  .   ? 57.206  -36.420 54.488  1.00 79.57  ?  2    NAG K O4  1 
HETATM 12901 O O5  . NAG K  5  .   ? 56.049  -33.047 53.660  1.00 82.18  ?  2    NAG K O5  1 
HETATM 12902 O O6  . NAG K  5  .   ? 54.324  -36.184 54.084  1.00 79.45  ?  2    NAG K O6  1 
HETATM 12903 O O7  . NAG K  5  .   ? 61.070  -32.740 54.721  1.00 80.29  ?  2    NAG K O7  1 
HETATM 12904 C C1  . NAG L  6  .   ? 17.529  -7.184  53.195  1.00 75.92  ?  1    NAG L C1  1 
HETATM 12905 C C2  . NAG L  6  .   ? 17.343  -7.379  51.692  1.00 74.18  ?  1    NAG L C2  1 
HETATM 12906 C C3  . NAG L  6  .   ? 15.869  -7.231  51.317  1.00 72.48  ?  1    NAG L C3  1 
HETATM 12907 C C4  . NAG L  6  .   ? 14.986  -8.128  52.177  1.00 71.44  ?  1    NAG L C4  1 
HETATM 12908 C C5  . NAG L  6  .   ? 15.303  -7.930  53.662  1.00 72.50  ?  1    NAG L C5  1 
HETATM 12909 C C6  . NAG L  6  .   ? 14.583  -8.903  54.568  1.00 71.35  ?  1    NAG L C6  1 
HETATM 12910 C C7  . NAG L  6  .   ? 19.120  -6.803  50.096  1.00 73.69  ?  1    NAG L C7  1 
HETATM 12911 C C8  . NAG L  6  .   ? 19.853  -5.690  49.410  1.00 72.32  ?  1    NAG L C8  1 
HETATM 12912 N N2  . NAG L  6  .   ? 18.154  -6.433  50.944  1.00 74.12  ?  1    NAG L N2  1 
HETATM 12913 O O3  . NAG L  6  .   ? 15.694  -7.554  49.942  1.00 71.67  ?  1    NAG L O3  1 
HETATM 12914 O O4  . NAG L  6  .   ? 13.625  -7.783  51.933  1.00 70.56  ?  1    NAG L O4  1 
HETATM 12915 O O5  . NAG L  6  .   ? 16.707  -8.110  53.901  1.00 74.35  ?  1    NAG L O5  1 
HETATM 12916 O O6  . NAG L  6  .   ? 15.487  -9.602  55.413  1.00 71.56  ?  1    NAG L O6  1 
HETATM 12917 O O7  . NAG L  6  .   ? 19.389  -7.983  49.893  1.00 73.78  ?  1    NAG L O7  1 
HETATM 12918 C C1  . NAG L  6  .   ? 12.763  -8.926  51.696  1.00 83.21  ?  2    NAG L C1  1 
HETATM 12919 C C2  . NAG L  6  .   ? 11.354  -8.390  51.420  1.00 82.83  ?  2    NAG L C2  1 
HETATM 12920 C C3  . NAG L  6  .   ? 10.388  -9.545  51.169  1.00 82.54  ?  2    NAG L C3  1 
HETATM 12921 C C4  . NAG L  6  .   ? 10.923  -10.452 50.068  1.00 82.45  ?  2    NAG L C4  1 
HETATM 12922 C C5  . NAG L  6  .   ? 12.351  -10.895 50.383  1.00 82.59  ?  2    NAG L C5  1 
HETATM 12923 C C6  . NAG L  6  .   ? 12.980  -11.699 49.269  1.00 82.39  ?  2    NAG L C6  1 
HETATM 12924 C C7  . NAG L  6  .   ? 10.715  -7.934  53.768  1.00 82.72  ?  2    NAG L C7  1 
HETATM 12925 C C8  . NAG L  6  .   ? 10.214  -6.889  54.720  1.00 82.53  ?  2    NAG L C8  1 
HETATM 12926 N N2  . NAG L  6  .   ? 10.879  -7.536  52.499  1.00 82.74  ?  2    NAG L N2  1 
HETATM 12927 O O3  . NAG L  6  .   ? 9.114   -9.029  50.802  1.00 82.44  ?  2    NAG L O3  1 
HETATM 12928 O O4  . NAG L  6  .   ? 10.093  -11.602 49.942  1.00 82.34  ?  2    NAG L O4  1 
HETATM 12929 O O5  . NAG L  6  .   ? 13.191  -9.748  50.593  1.00 82.98  ?  2    NAG L O5  1 
HETATM 12930 O O6  . NAG L  6  .   ? 13.285  -13.021 49.692  1.00 82.30  ?  2    NAG L O6  1 
HETATM 12931 O O7  . NAG L  6  .   ? 10.956  -9.081  54.134  1.00 82.78  ?  2    NAG L O7  1 
HETATM 12932 C C1  . FUC L  6  .   ? 15.627  -10.972 54.970  1.00 79.25  ?  3    FUC L C1  1 
HETATM 12933 C C2  . FUC L  6  .   ? 15.483  -11.883 56.220  1.00 78.71  ?  3    FUC L C2  1 
HETATM 12934 C C3  . FUC L  6  .   ? 14.918  -13.273 55.863  1.00 78.37  ?  3    FUC L C3  1 
HETATM 12935 C C4  . FUC L  6  .   ? 15.293  -13.689 54.429  1.00 78.35  ?  3    FUC L C4  1 
HETATM 12936 C C5  . FUC L  6  .   ? 14.750  -12.652 53.423  1.00 78.65  ?  3    FUC L C5  1 
HETATM 12937 C C6  . FUC L  6  .   ? 15.578  -12.548 52.148  1.00 78.62  ?  3    FUC L C6  1 
HETATM 12938 O O2  . FUC L  6  .   ? 14.702  -11.269 57.239  1.00 78.58  ?  3    FUC L O2  1 
HETATM 12939 O O3  . FUC L  6  .   ? 15.442  -14.257 56.753  1.00 78.19  ?  3    FUC L O3  1 
HETATM 12940 O O4  . FUC L  6  .   ? 16.704  -13.833 54.296  1.00 78.24  ?  3    FUC L O4  1 
HETATM 12941 O O5  . FUC L  6  .   ? 14.664  -11.310 53.980  1.00 78.94  ?  3    FUC L O5  1 
HETATM 12942 C C1  . NAG M  7  .   ? 40.666  -16.326 68.739  1.00 25.61  ?  1    NAG M C1  1 
HETATM 12943 C C2  . NAG M  7  .   ? 40.825  -16.924 70.109  1.00 40.59  ?  1    NAG M C2  1 
HETATM 12944 C C3  . NAG M  7  .   ? 39.514  -16.875 70.847  1.00 52.49  ?  1    NAG M C3  1 
HETATM 12945 C C4  . NAG M  7  .   ? 38.999  -15.474 71.014  1.00 34.47  ?  1    NAG M C4  1 
HETATM 12946 C C5  . NAG M  7  .   ? 39.300  -14.602 69.808  1.00 27.20  ?  1    NAG M C5  1 
HETATM 12947 C C6  . NAG M  7  .   ? 40.474  -13.676 70.065  1.00 32.22  ?  1    NAG M C6  1 
HETATM 12948 C C7  . NAG M  7  .   ? 42.390  -18.710 70.247  1.00 48.06  ?  1    NAG M C7  1 
HETATM 12949 C C8  . NAG M  7  .   ? 43.127  -17.828 71.203  1.00 37.13  ?  1    NAG M C8  1 
HETATM 12950 N N2  . NAG M  7  .   ? 41.180  -18.301 69.947  1.00 34.77  ?  1    NAG M N2  1 
HETATM 12951 O O3  . NAG M  7  .   ? 39.712  -17.388 72.161  1.00 63.55  ?  1    NAG M O3  1 
HETATM 12952 O O4  . NAG M  7  .   ? 37.594  -15.621 71.146  1.00 32.72  ?  1    NAG M O4  1 
HETATM 12953 O O5  . NAG M  7  .   ? 39.592  -15.397 68.664  1.00 29.71  ?  1    NAG M O5  1 
HETATM 12954 O O6  . NAG M  7  .   ? 40.091  -12.753 71.078  1.00 40.33  ?  1    NAG M O6  1 
HETATM 12955 O O7  . NAG M  7  .   ? 42.857  -19.726 69.785  1.00 76.94  ?  1    NAG M O7  1 
HETATM 12956 C C1  . NAG M  7  .   ? 37.113  -15.285 72.454  1.00 38.37  ?  2    NAG M C1  1 
HETATM 12957 C C2  . NAG M  7  .   ? 35.611  -15.457 72.430  1.00 38.37  ?  2    NAG M C2  1 
HETATM 12958 C C3  . NAG M  7  .   ? 35.008  -15.110 73.767  1.00 38.37  ?  2    NAG M C3  1 
HETATM 12959 C C4  . NAG M  7  .   ? 35.712  -15.859 74.858  1.00 38.37  ?  2    NAG M C4  1 
HETATM 12960 C C5  . NAG M  7  .   ? 37.200  -15.638 74.747  1.00 38.37  ?  2    NAG M C5  1 
HETATM 12961 C C6  . NAG M  7  .   ? 37.922  -16.403 75.833  1.00 38.37  ?  2    NAG M C6  1 
HETATM 12962 C C7  . NAG M  7  .   ? 34.848  -15.031 70.213  1.00 38.37  ?  2    NAG M C7  1 
HETATM 12963 C C8  . NAG M  7  .   ? 33.893  -14.236 69.393  1.00 38.37  ?  2    NAG M C8  1 
HETATM 12964 N N2  . NAG M  7  .   ? 35.053  -14.586 71.433  1.00 38.37  ?  2    NAG M N2  1 
HETATM 12965 O O3  . NAG M  7  .   ? 33.645  -15.517 73.795  1.00 38.37  ?  2    NAG M O3  1 
HETATM 12966 O O4  . NAG M  7  .   ? 35.230  -15.313 76.073  1.00 38.37  ?  2    NAG M O4  1 
HETATM 12967 O O5  . NAG M  7  .   ? 37.633  -16.108 73.483  1.00 38.37  ?  2    NAG M O5  1 
HETATM 12968 O O6  . NAG M  7  .   ? 37.566  -17.775 75.693  1.00 38.37  ?  2    NAG M O6  1 
HETATM 12969 O O7  . NAG M  7  .   ? 35.395  -16.028 69.799  1.00 38.37  ?  2    NAG M O7  1 
HETATM 12970 C C1  . BMA M  7  .   ? 34.685  -16.355 76.886  1.00 43.09  ?  3    BMA M C1  1 
HETATM 12971 C C2  . BMA M  7  .   ? 34.853  -15.897 78.314  1.00 43.09  ?  3    BMA M C2  1 
HETATM 12972 C C3  . BMA M  7  .   ? 34.367  -16.970 79.249  1.00 43.09  ?  3    BMA M C3  1 
HETATM 12973 C C4  . BMA M  7  .   ? 32.925  -17.262 78.914  1.00 43.09  ?  3    BMA M C4  1 
HETATM 12974 C C5  . BMA M  7  .   ? 32.776  -17.620 77.454  1.00 43.09  ?  3    BMA M C5  1 
HETATM 12975 C C6  . BMA M  7  .   ? 31.301  -17.807 77.150  1.00 43.09  ?  3    BMA M C6  1 
HETATM 12976 O O2  . BMA M  7  .   ? 34.066  -14.728 78.505  1.00 43.09  ?  3    BMA M O2  1 
HETATM 12977 O O3  . BMA M  7  .   ? 34.487  -16.489 80.586  1.00 43.09  ?  3    BMA M O3  1 
HETATM 12978 O O4  . BMA M  7  .   ? 32.487  -18.376 79.678  1.00 43.09  ?  3    BMA M O4  1 
HETATM 12979 O O5  . BMA M  7  .   ? 33.303  -16.581 76.642  1.00 43.09  ?  3    BMA M O5  1 
HETATM 12980 O O6  . BMA M  7  .   ? 31.129  -18.308 75.824  1.00 43.09  ?  3    BMA M O6  1 
HETATM 12981 C C1  . NAG N  7  .   ? -5.290  6.014   1.816   1.00 26.61  ?  1    NAG N C1  1 
HETATM 12982 C C2  . NAG N  7  .   ? -4.268  6.833   2.597   1.00 28.95  ?  1    NAG N C2  1 
HETATM 12983 C C3  . NAG N  7  .   ? -2.944  6.843   1.864   1.00 30.14  ?  1    NAG N C3  1 
HETATM 12984 C C4  . NAG N  7  .   ? -2.337  5.449   1.832   1.00 29.78  ?  1    NAG N C4  1 
HETATM 12985 C C5  . NAG N  7  .   ? -3.392  4.348   1.729   1.00 25.22  ?  1    NAG N C5  1 
HETATM 12986 C C6  . NAG N  7  .   ? -3.663  3.622   3.030   1.00 25.06  ?  1    NAG N C6  1 
HETATM 12987 C C7  . NAG N  7  .   ? -4.895  8.771   3.984   1.00 25.80  ?  1    NAG N C7  1 
HETATM 12988 C C8  . NAG N  7  .   ? -4.512  7.938   5.173   1.00 24.28  ?  1    NAG N C8  1 
HETATM 12989 N N2  . NAG N  7  .   ? -4.752  8.192   2.787   1.00 24.68  ?  1    NAG N N2  1 
HETATM 12990 O O3  . NAG N  7  .   ? -2.054  7.743   2.516   1.00 44.68  ?  1    NAG N O3  1 
HETATM 12991 O O4  . NAG N  7  .   ? -1.553  5.360   0.651   1.00 27.78  ?  1    NAG N O4  1 
HETATM 12992 O O5  . NAG N  7  .   ? -4.648  4.829   1.220   1.00 27.20  ?  1    NAG N O5  1 
HETATM 12993 O O6  . NAG N  7  .   ? -3.274  2.257   2.958   1.00 25.31  ?  1    NAG N O6  1 
HETATM 12994 O O7  . NAG N  7  .   ? -5.317  9.916   4.102   1.00 26.22  ?  1    NAG N O7  1 
HETATM 12995 C C1  . NAG N  7  .   ? -0.237  4.907   1.060   1.00 29.74  ?  2    NAG N C1  1 
HETATM 12996 C C2  . NAG N  7  .   ? 0.700   5.018   -0.119  1.00 31.64  ?  2    NAG N C2  1 
HETATM 12997 C C3  . NAG N  7  .   ? 2.100   4.567   0.243   1.00 26.58  ?  2    NAG N C3  1 
HETATM 12998 C C4  . NAG N  7  .   ? 2.575   5.245   1.500   1.00 35.66  ?  2    NAG N C4  1 
HETATM 12999 C C5  . NAG N  7  .   ? 1.550   5.040   2.586   1.00 32.09  ?  2    NAG N C5  1 
HETATM 13000 C C6  . NAG N  7  .   ? 1.993   5.708   3.875   1.00 35.12  ?  2    NAG N C6  1 
HETATM 13001 C C7  . NAG N  7  .   ? -0.642  4.785   -2.062  1.00 34.01  ?  2    NAG N C7  1 
HETATM 13002 C C8  . NAG N  7  .   ? -1.022  3.966   -3.247  1.00 22.09  ?  2    NAG N C8  1 
HETATM 13003 N N2  . NAG N  7  .   ? 0.166   4.213   -1.190  1.00 35.04  ?  2    NAG N N2  1 
HETATM 13004 O O3  . NAG N  7  .   ? 3.007   4.937   -0.793  1.00 33.13  ?  2    NAG N O3  1 
HETATM 13005 O O4  . NAG N  7  .   ? 3.808   4.641   1.869   1.00 46.44  ?  2    NAG N O4  1 
HETATM 13006 O O5  . NAG N  7  .   ? 0.337   5.623   2.148   1.00 31.59  ?  2    NAG N O5  1 
HETATM 13007 O O6  . NAG N  7  .   ? 2.276   7.082   3.616   1.00 44.13  ?  2    NAG N O6  1 
HETATM 13008 O O7  . NAG N  7  .   ? -1.038  5.919   -1.912  1.00 36.78  ?  2    NAG N O7  1 
HETATM 13009 C C1  . BMA N  7  .   ? 4.784   5.658   2.107   1.00 40.96  ?  3    BMA N C1  1 
HETATM 13010 C C2  . BMA N  7  .   ? 5.683   5.182   3.228   1.00 40.96  ?  3    BMA N C2  1 
HETATM 13011 C C3  . BMA N  7  .   ? 6.731   6.229   3.527   1.00 40.96  ?  3    BMA N C3  1 
HETATM 13012 C C4  . BMA N  7  .   ? 7.479   6.533   2.254   1.00 40.96  ?  3    BMA N C4  1 
HETATM 13013 C C5  . BMA N  7  .   ? 6.509   6.968   1.177   1.00 40.96  ?  3    BMA N C5  1 
HETATM 13014 C C6  . BMA N  7  .   ? 7.260   7.247   -0.110  1.00 40.96  ?  3    BMA N C6  1 
HETATM 13015 O O2  . BMA N  7  .   ? 6.330   3.984   2.818   1.00 40.96  ?  3    BMA N O2  1 
HETATM 13016 O O3  . BMA N  7  .   ? 7.645   5.736   4.505   1.00 40.96  ?  3    BMA N O3  1 
HETATM 13017 O O4  . BMA N  7  .   ? 8.403   7.585   2.507   1.00 40.96  ?  3    BMA N O4  1 
HETATM 13018 O O5  . BMA N  7  .   ? 5.566   5.930   0.955   1.00 40.96  ?  3    BMA N O5  1 
HETATM 13019 O O6  . BMA N  7  .   ? 6.371   7.847   -1.051  1.00 40.96  ?  3    BMA N O6  1 
HETATM 13020 C C1  . NAG O  8  .   ? 20.762  1.151   36.595  1.00 35.17  ?  1    NAG O C1  1 
HETATM 13021 C C2  . NAG O  8  .   ? 20.761  -0.176  37.331  1.00 36.79  ?  1    NAG O C2  1 
HETATM 13022 C C3  . NAG O  8  .   ? 22.068  -0.261  38.113  1.00 46.91  ?  1    NAG O C3  1 
HETATM 13023 C C4  . NAG O  8  .   ? 23.202  -0.310  37.111  1.00 51.89  ?  1    NAG O C4  1 
HETATM 13024 C C5  . NAG O  8  .   ? 23.160  0.944   36.253  1.00 47.90  ?  1    NAG O C5  1 
HETATM 13025 C C6  . NAG O  8  .   ? 24.152  0.853   35.102  1.00 49.16  ?  1    NAG O C6  1 
HETATM 13026 C C7  . NAG O  8  .   ? 18.975  0.614   38.872  1.00 38.93  ?  1    NAG O C7  1 
HETATM 13027 C C8  . NAG O  8  .   ? 19.817  1.555   39.674  1.00 41.03  ?  1    NAG O C8  1 
HETATM 13028 N N2  . NAG O  8  .   ? 19.601  -0.336  38.190  1.00 33.97  ?  1    NAG O N2  1 
HETATM 13029 O O3  . NAG O  8  .   ? 22.118  -1.400  38.986  1.00 47.78  ?  1    NAG O O3  1 
HETATM 13030 O O4  . NAG O  8  .   ? 24.421  -0.369  37.850  1.00 67.26  ?  1    NAG O O4  1 
HETATM 13031 O O5  . NAG O  8  .   ? 21.866  1.168   35.695  1.00 31.00  ?  1    NAG O O5  1 
HETATM 13032 O O6  . NAG O  8  .   ? 23.480  0.623   33.859  1.00 48.81  ?  1    NAG O O6  1 
HETATM 13033 O O7  . NAG O  8  .   ? 17.764  0.696   38.865  1.00 38.30  ?  1    NAG O O7  1 
HETATM 13034 C C1  . NAG O  8  .   ? 25.500  -1.044  37.177  1.00 58.62  ?  2    NAG O C1  1 
HETATM 13035 C C2  . NAG O  8  .   ? 26.797  -0.362  37.581  1.00 58.62  ?  2    NAG O C2  1 
HETATM 13036 C C3  . NAG O  8  .   ? 27.975  -1.110  36.998  1.00 58.62  ?  2    NAG O C3  1 
HETATM 13037 C C4  . NAG O  8  .   ? 27.919  -2.555  37.436  1.00 58.62  ?  2    NAG O C4  1 
HETATM 13038 C C5  . NAG O  8  .   ? 26.608  -3.134  36.937  1.00 58.62  ?  2    NAG O C5  1 
HETATM 13039 C C6  . NAG O  8  .   ? 26.432  -4.582  37.341  1.00 58.62  ?  2    NAG O C6  1 
HETATM 13040 C C7  . NAG O  8  .   ? 26.527  2.059   37.849  1.00 58.62  ?  2    NAG O C7  1 
HETATM 13041 C C8  . NAG O  8  .   ? 27.410  3.255   37.677  1.00 58.62  ?  2    NAG O C8  1 
HETATM 13042 N N2  . NAG O  8  .   ? 26.838  1.002   37.101  1.00 58.62  ?  2    NAG O N2  1 
HETATM 13043 O O3  . NAG O  8  .   ? 29.199  -0.531  37.450  1.00 58.62  ?  2    NAG O O3  1 
HETATM 13044 O O4  . NAG O  8  .   ? 29.059  -3.225  36.892  1.00 58.62  ?  2    NAG O O4  1 
HETATM 13045 O O5  . NAG O  8  .   ? 25.539  -2.417  37.528  1.00 58.62  ?  2    NAG O O5  1 
HETATM 13046 O O6  . NAG O  8  .   ? 25.063  -4.943  37.166  1.00 58.62  ?  2    NAG O O6  1 
HETATM 13047 O O7  . NAG O  8  .   ? 25.588  2.073   38.621  1.00 58.62  ?  2    NAG O O7  1 
HETATM 13048 C C1  . BMA O  8  .   ? 29.650  -4.066  37.894  1.00 60.69  ?  3    BMA O C1  1 
HETATM 13049 C C2  . BMA O  8  .   ? 29.513  -5.490  37.391  1.00 60.69  ?  3    BMA O C2  1 
HETATM 13050 C C3  . BMA O  8  .   ? 30.075  -6.462  38.411  1.00 60.69  ?  3    BMA O C3  1 
HETATM 13051 C C4  . BMA O  8  .   ? 31.507  -6.076  38.705  1.00 60.69  ?  3    BMA O C4  1 
HETATM 13052 C C5  . BMA O  8  .   ? 31.596  -4.625  39.136  1.00 60.69  ?  3    BMA O C5  1 
HETATM 13053 C C6  . BMA O  8  .   ? 33.060  -4.284  39.356  1.00 60.69  ?  3    BMA O C6  1 
HETATM 13054 O O2  . BMA O  8  .   ? 30.223  -5.594  36.156  1.00 60.69  ?  3    BMA O O2  1 
HETATM 13055 O O3  . BMA O  8  .   ? 30.029  -7.801  37.902  1.00 60.69  ?  3    BMA O O3  1 
HETATM 13056 O O4  . BMA O  8  .   ? 31.995  -6.904  39.757  1.00 60.69  ?  3    BMA O O4  1 
HETATM 13057 O O5  . BMA O  8  .   ? 31.028  -3.784  38.134  1.00 60.69  ?  3    BMA O O5  1 
HETATM 13058 O O6  . BMA O  8  .   ? 33.197  -2.962  39.870  1.00 60.69  ?  3    BMA O O6  1 
HETATM 13059 C C1  . FUC O  8  .   ? 23.231  -0.763  33.522  1.00 54.13  ?  4    FUC O C1  1 
HETATM 13060 C C2  . FUC O  8  .   ? 22.996  -0.775  31.976  1.00 54.13  ?  4    FUC O C2  1 
HETATM 13061 C C3  . FUC O  8  .   ? 23.731  -1.953  31.304  1.00 54.13  ?  4    FUC O C3  1 
HETATM 13062 C C4  . FUC O  8  .   ? 23.574  -3.238  32.131  1.00 54.13  ?  4    FUC O C4  1 
HETATM 13063 C C5  . FUC O  8  .   ? 24.132  -3.019  33.551  1.00 54.13  ?  4    FUC O C5  1 
HETATM 13064 C C6  . FUC O  8  .   ? 23.242  -3.601  34.641  1.00 54.13  ?  4    FUC O C6  1 
HETATM 13065 O O2  . FUC O  8  .   ? 23.334  0.460   31.356  1.00 54.13  ?  4    FUC O O2  1 
HETATM 13066 O O3  . FUC O  8  .   ? 23.193  -2.202  30.004  1.00 54.13  ?  4    FUC O O3  1 
HETATM 13067 O O4  . FUC O  8  .   ? 22.206  -3.625  32.190  1.00 54.13  ?  4    FUC O O4  1 
HETATM 13068 O O5  . FUC O  8  .   ? 24.313  -1.614  33.870  1.00 54.13  ?  4    FUC O O5  1 
HETATM 13069 C C1  . NAG P  5  .   ? -8.121  -27.127 -4.823  1.00 47.07  ?  1    NAG P C1  1 
HETATM 13070 C C2  . NAG P  5  .   ? -9.570  -27.236 -5.286  1.00 46.22  ?  1    NAG P C2  1 
HETATM 13071 C C3  . NAG P  5  .   ? -10.431 -27.837 -4.172  1.00 44.96  ?  1    NAG P C3  1 
HETATM 13072 C C4  . NAG P  5  .   ? -9.811  -29.105 -3.587  1.00 44.44  ?  1    NAG P C4  1 
HETATM 13073 C C5  . NAG P  5  .   ? -8.314  -28.932 -3.317  1.00 44.85  ?  1    NAG P C5  1 
HETATM 13074 C C6  . NAG P  5  .   ? -7.624  -30.225 -2.950  1.00 44.54  ?  1    NAG P C6  1 
HETATM 13075 C C7  . NAG P  5  .   ? -11.246 -25.779 -6.342  1.00 47.46  ?  1    NAG P C7  1 
HETATM 13076 C C8  . NAG P  5  .   ? -11.637 -24.367 -6.652  1.00 47.70  ?  1    NAG P C8  1 
HETATM 13077 N N2  . NAG P  5  .   ? -10.093 -25.938 -5.681  1.00 46.81  ?  1    NAG P N2  1 
HETATM 13078 O O3  . NAG P  5  .   ? -11.719 -28.125 -4.705  1.00 45.06  ?  1    NAG P O3  1 
HETATM 13079 O O4  . NAG P  5  .   ? -10.408 -29.399 -2.325  1.00 43.06  ?  1    NAG P O4  1 
HETATM 13080 O O5  . NAG P  5  .   ? -7.640  -28.410 -4.471  1.00 46.30  ?  1    NAG P O5  1 
HETATM 13081 O O6  . NAG P  5  .   ? -7.725  -30.492 -1.558  1.00 43.00  ?  1    NAG P O6  1 
HETATM 13082 O O7  . NAG P  5  .   ? -11.940 -26.734 -6.680  1.00 47.91  ?  1    NAG P O7  1 
HETATM 13083 C C1  . NAG P  5  .   ? -11.737 -29.968 -2.346  1.00 52.72  ?  2    NAG P C1  1 
HETATM 13084 C C2  . NAG P  5  .   ? -11.992 -30.665 -1.005  1.00 51.73  ?  2    NAG P C2  1 
HETATM 13085 C C3  . NAG P  5  .   ? -13.425 -31.197 -0.934  1.00 51.16  ?  2    NAG P C3  1 
HETATM 13086 C C4  . NAG P  5  .   ? -14.423 -30.094 -1.254  1.00 51.17  ?  2    NAG P C4  1 
HETATM 13087 C C5  . NAG P  5  .   ? -14.082 -29.460 -2.598  1.00 52.26  ?  2    NAG P C5  1 
HETATM 13088 C C6  . NAG P  5  .   ? -14.971 -28.288 -2.942  1.00 51.61  ?  2    NAG P C6  1 
HETATM 13089 C C7  . NAG P  5  .   ? -10.904 -32.826 -1.522  1.00 51.62  ?  2    NAG P C7  1 
HETATM 13090 C C8  . NAG P  5  .   ? -9.851  -33.802 -1.092  1.00 51.85  ?  2    NAG P C8  1 
HETATM 13091 N N2  . NAG P  5  .   ? -11.030 -31.731 -0.761  1.00 51.60  ?  2    NAG P N2  1 
HETATM 13092 O O3  . NAG P  5  .   ? -13.674 -31.712 0.369   1.00 50.80  ?  2    NAG P O3  1 
HETATM 13093 O O4  . NAG P  5  .   ? -15.742 -30.626 -1.307  1.00 50.74  ?  2    NAG P O4  1 
HETATM 13094 O O5  . NAG P  5  .   ? -12.737 -28.962 -2.565  1.00 52.70  ?  2    NAG P O5  1 
HETATM 13095 O O6  . NAG P  5  .   ? -15.028 -28.073 -4.345  1.00 53.13  ?  2    NAG P O6  1 
HETATM 13096 O O7  . NAG P  5  .   ? -11.604 -33.023 -2.513  1.00 52.18  ?  2    NAG P O7  1 
HETATM 13097 C C1  . NAG Q  5  .   ? 25.102  26.684  20.162  1.00 44.81  ?  1    NAG Q C1  1 
HETATM 13098 C C2  . NAG Q  5  .   ? 24.341  27.982  19.920  1.00 44.04  ?  1    NAG Q C2  1 
HETATM 13099 C C3  . NAG Q  5  .   ? 23.194  27.746  18.943  1.00 43.34  ?  1    NAG Q C3  1 
HETATM 13100 C C4  . NAG Q  5  .   ? 23.705  27.092  17.665  1.00 42.71  ?  1    NAG Q C4  1 
HETATM 13101 C C5  . NAG Q  5  .   ? 24.532  25.848  17.988  1.00 42.88  ?  1    NAG Q C5  1 
HETATM 13102 C C6  . NAG Q  5  .   ? 25.203  25.253  16.772  1.00 42.50  ?  1    NAG Q C6  1 
HETATM 13103 C C7  . NAG Q  5  .   ? 24.385  29.606  21.767  1.00 46.67  ?  1    NAG Q C7  1 
HETATM 13104 C C8  . NAG Q  5  .   ? 25.561  30.227  21.072  1.00 46.18  ?  1    NAG Q C8  1 
HETATM 13105 N N2  . NAG Q  5  .   ? 23.844  28.538  21.170  1.00 44.71  ?  1    NAG Q N2  1 
HETATM 13106 O O3  . NAG Q  5  .   ? 22.572  28.989  18.638  1.00 43.04  ?  1    NAG Q O3  1 
HETATM 13107 O O4  . NAG Q  5  .   ? 22.599  26.709  16.855  1.00 42.09  ?  1    NAG Q O4  1 
HETATM 13108 O O5  . NAG Q  5  .   ? 25.578  26.170  18.919  1.00 43.98  ?  1    NAG Q O5  1 
HETATM 13109 O O6  . NAG Q  5  .   ? 26.608  25.466  16.796  1.00 42.74  ?  1    NAG Q O6  1 
HETATM 13110 O O7  . NAG Q  5  .   ? 23.945  30.051  22.822  1.00 48.87  ?  1    NAG Q O7  1 
HETATM 13111 C C1  . NAG Q  5  .   ? 22.558  27.496  15.648  1.00 55.42  ?  2    NAG Q C1  1 
HETATM 13112 C C2  . NAG Q  5  .   ? 21.987  26.621  14.532  1.00 55.22  ?  2    NAG Q C2  1 
HETATM 13113 C C3  . NAG Q  5  .   ? 21.872  27.421  13.239  1.00 55.09  ?  2    NAG Q C3  1 
HETATM 13114 C C4  . NAG Q  5  .   ? 21.074  28.697  13.474  1.00 55.06  ?  2    NAG Q C4  1 
HETATM 13115 C C5  . NAG Q  5  .   ? 21.679  29.491  14.629  1.00 55.15  ?  2    NAG Q C5  1 
HETATM 13116 C C6  . NAG Q  5  .   ? 20.866  30.711  14.997  1.00 55.08  ?  2    NAG Q C6  1 
HETATM 13117 C C7  . NAG Q  5  .   ? 22.422  24.212  14.713  1.00 55.17  ?  2    NAG Q C7  1 
HETATM 13118 C C8  . NAG Q  5  .   ? 23.386  23.101  14.422  1.00 55.14  ?  2    NAG Q C8  1 
HETATM 13119 N N2  . NAG Q  5  .   ? 22.803  25.434  14.329  1.00 55.19  ?  2    NAG Q N2  1 
HETATM 13120 O O3  . NAG Q  5  .   ? 21.237  26.626  12.244  1.00 55.05  ?  2    NAG Q O3  1 
HETATM 13121 O O4  . NAG Q  5  .   ? 21.080  29.499  12.298  1.00 55.02  ?  2    NAG Q O4  1 
HETATM 13122 O O5  . NAG Q  5  .   ? 21.746  28.669  15.804  1.00 55.31  ?  2    NAG Q O5  1 
HETATM 13123 O O6  . NAG Q  5  .   ? 19.745  30.366  15.798  1.00 55.08  ?  2    NAG Q O6  1 
HETATM 13124 O O7  . NAG Q  5  .   ? 21.347  24.011  15.270  1.00 55.15  ?  2    NAG Q O7  1 
HETATM 13125 C C1  . NAG R  5  .   ? -23.898 18.745  6.259   1.00 55.69  ?  1    NAG R C1  1 
HETATM 13126 C C2  . NAG R  5  .   ? -25.323 18.706  6.786   1.00 51.67  ?  1    NAG R C2  1 
HETATM 13127 C C3  . NAG R  5  .   ? -26.066 19.958  6.343   1.00 48.29  ?  1    NAG R C3  1 
HETATM 13128 C C4  . NAG R  5  .   ? -25.286 21.215  6.702   1.00 46.62  ?  1    NAG R C4  1 
HETATM 13129 C C5  . NAG R  5  .   ? -23.821 21.104  6.289   1.00 49.96  ?  1    NAG R C5  1 
HETATM 13130 C C6  . NAG R  5  .   ? -22.995 22.265  6.829   1.00 48.21  ?  1    NAG R C6  1 
HETATM 13131 C C7  . NAG R  5  .   ? -25.819 16.329  6.879   1.00 51.90  ?  1    NAG R C7  1 
HETATM 13132 C C8  . NAG R  5  .   ? -26.080 15.140  6.003   1.00 51.84  ?  1    NAG R C8  1 
HETATM 13133 N N2  . NAG R  5  .   ? -26.006 17.518  6.311   1.00 52.04  ?  1    NAG R N2  1 
HETATM 13134 O O3  . NAG R  5  .   ? -27.347 20.001  6.981   1.00 46.62  ?  1    NAG R O3  1 
HETATM 13135 O O4  . NAG R  5  .   ? -25.894 22.314  6.017   1.00 43.99  ?  1    NAG R O4  1 
HETATM 13136 O O5  . NAG R  5  .   ? -23.249 19.896  6.786   1.00 54.15  ?  1    NAG R O5  1 
HETATM 13137 O O6  . NAG R  5  .   ? -21.682 22.218  6.261   1.00 50.24  ?  1    NAG R O6  1 
HETATM 13138 O O7  . NAG R  5  .   ? -25.451 16.214  8.037   1.00 50.42  ?  1    NAG R O7  1 
HETATM 13139 C C1  . NAG R  5  .   ? -26.093 23.418  6.918   1.00 54.98  ?  2    NAG R C1  1 
HETATM 13140 C C2  . NAG R  5  .   ? -26.675 24.600  6.154   1.00 53.84  ?  2    NAG R C2  1 
HETATM 13141 C C3  . NAG R  5  .   ? -26.803 25.801  7.079   1.00 52.45  ?  2    NAG R C3  1 
HETATM 13142 C C4  . NAG R  5  .   ? -27.613 25.417  8.310   1.00 52.01  ?  2    NAG R C4  1 
HETATM 13143 C C5  . NAG R  5  .   ? -27.017 24.171  8.959   1.00 52.73  ?  2    NAG R C5  1 
HETATM 13144 C C6  . NAG R  5  .   ? -27.846 23.721  10.155  1.00 52.16  ?  2    NAG R C6  1 
HETATM 13145 C C7  . NAG R  5  .   ? -24.543 24.746  4.959   1.00 54.18  ?  2    NAG R C7  1 
HETATM 13146 C C8  . NAG R  5  .   ? -23.700 25.749  5.689   1.00 53.98  ?  2    NAG R C8  1 
HETATM 13147 N N2  . NAG R  5  .   ? -25.859 24.939  5.001   1.00 54.15  ?  2    NAG R N2  1 
HETATM 13148 O O3  . NAG R  5  .   ? -27.431 26.867  6.361   1.00 52.02  ?  2    NAG R O3  1 
HETATM 13149 O O4  . NAG R  5  .   ? -27.610 26.489  9.260   1.00 51.23  ?  2    NAG R O4  1 
HETATM 13150 O O5  . NAG R  5  .   ? -26.955 23.105  8.010   1.00 54.18  ?  2    NAG R O5  1 
HETATM 13151 O O6  . NAG R  5  .   ? -27.878 24.758  11.140  1.00 51.48  ?  2    NAG R O6  1 
HETATM 13152 O O7  . NAG R  5  .   ? -24.052 23.809  4.351   1.00 53.74  ?  2    NAG R O7  1 
HETATM 13153 C C1  . NAG S  9  .   ? -16.089 22.130  34.628  1.00 64.78  ?  1    NAG S C1  1 
HETATM 13154 C C2  . NAG S  9  .   ? -16.786 21.058  35.469  1.00 63.07  ?  1    NAG S C2  1 
HETATM 13155 C C3  . NAG S  9  .   ? -18.054 21.622  36.103  1.00 61.07  ?  1    NAG S C3  1 
HETATM 13156 C C4  . NAG S  9  .   ? -17.734 22.884  36.893  1.00 59.59  ?  1    NAG S C4  1 
HETATM 13157 C C5  . NAG S  9  .   ? -16.992 23.890  36.017  1.00 60.28  ?  1    NAG S C5  1 
HETATM 13158 C C6  . NAG S  9  .   ? -16.515 25.095  36.793  1.00 57.71  ?  1    NAG S C6  1 
HETATM 13159 C C7  . NAG S  9  .   ? -17.892 19.834  33.625  1.00 64.13  ?  1    NAG S C7  1 
HETATM 13160 C C8  . NAG S  9  .   ? -18.058 18.497  32.972  1.00 65.69  ?  1    NAG S C8  1 
HETATM 13161 N N2  . NAG S  9  .   ? -17.080 19.864  34.690  1.00 64.59  ?  1    NAG S N2  1 
HETATM 13162 O O3  . NAG S  9  .   ? -18.632 20.644  36.961  1.00 60.52  ?  1    NAG S O3  1 
HETATM 13163 O O4  . NAG S  9  .   ? -18.937 23.475  37.370  1.00 58.50  ?  1    NAG S O4  1 
HETATM 13164 O O5  . NAG S  9  .   ? -15.822 23.284  35.443  1.00 62.01  ?  1    NAG S O5  1 
HETATM 13165 O O6  . NAG S  9  .   ? -15.366 24.776  37.565  1.00 56.63  ?  1    NAG S O6  1 
HETATM 13166 O O7  . NAG S  9  .   ? -18.466 20.836  33.206  1.00 64.06  ?  1    NAG S O7  1 
HETATM 13167 C C1  . FUC S  9  .   ? -15.412 25.473  38.824  1.00 63.83  ?  2    FUC S C1  1 
HETATM 13168 C C2  . FUC S  9  .   ? -14.931 24.505  39.911  1.00 63.55  ?  2    FUC S C2  1 
HETATM 13169 C C3  . FUC S  9  .   ? -13.483 24.087  39.630  1.00 63.44  ?  2    FUC S C3  1 
HETATM 13170 C C4  . FUC S  9  .   ? -12.582 25.330  39.506  1.00 63.12  ?  2    FUC S C4  1 
HETATM 13171 C C5  . FUC S  9  .   ? -13.188 26.340  38.509  1.00 62.75  ?  2    FUC S C5  1 
HETATM 13172 C C6  . FUC S  9  .   ? -12.486 27.689  38.528  1.00 62.25  ?  2    FUC S C6  1 
HETATM 13173 O O2  . FUC S  9  .   ? -15.775 23.367  40.039  1.00 63.82  ?  2    FUC S O2  1 
HETATM 13174 O O3  . FUC S  9  .   ? -12.983 23.295  40.703  1.00 63.20  ?  2    FUC S O3  1 
HETATM 13175 O O4  . FUC S  9  .   ? -12.423 25.941  40.775  1.00 62.48  ?  2    FUC S O4  1 
HETATM 13176 O O5  . FUC S  9  .   ? -14.585 26.605  38.779  1.00 63.23  ?  2    FUC S O5  1 
HETATM 13177 C C1  . NAG T  9  .   ? -3.499  -3.775  -25.228 1.00 66.17  ?  1    NAG T C1  1 
HETATM 13178 C C2  . NAG T  9  .   ? -4.538  -3.530  -26.326 1.00 64.16  ?  1    NAG T C2  1 
HETATM 13179 C C3  . NAG T  9  .   ? -3.927  -3.783  -27.703 1.00 62.66  ?  1    NAG T C3  1 
HETATM 13180 C C4  . NAG T  9  .   ? -2.644  -2.981  -27.877 1.00 61.34  ?  1    NAG T C4  1 
HETATM 13181 C C5  . NAG T  9  .   ? -1.688  -3.270  -26.725 1.00 61.80  ?  1    NAG T C5  1 
HETATM 13182 C C6  . NAG T  9  .   ? -0.425  -2.442  -26.778 1.00 59.56  ?  1    NAG T C6  1 
HETATM 13183 C C7  . NAG T  9  .   ? -6.925  -3.879  -25.868 1.00 64.79  ?  1    NAG T C7  1 
HETATM 13184 C C8  . NAG T  9  .   ? -8.016  -4.892  -25.693 1.00 63.86  ?  1    NAG T C8  1 
HETATM 13185 N N2  . NAG T  9  .   ? -5.708  -4.369  -26.127 1.00 64.50  ?  1    NAG T N2  1 
HETATM 13186 O O3  . NAG T  9  .   ? -4.865  -3.425  -28.711 1.00 62.25  ?  1    NAG T O3  1 
HETATM 13187 O O4  . NAG T  9  .   ? -2.017  -3.324  -29.107 1.00 60.30  ?  1    NAG T O4  1 
HETATM 13188 O O5  . NAG T  9  .   ? -2.331  -2.972  -25.477 1.00 63.45  ?  1    NAG T O5  1 
HETATM 13189 O O6  . NAG T  9  .   ? -0.667  -1.099  -26.385 1.00 57.84  ?  1    NAG T O6  1 
HETATM 13190 O O7  . NAG T  9  .   ? -7.136  -2.674  -25.780 1.00 65.60  ?  1    NAG T O7  1 
HETATM 13191 C C1  . FUC T  9  .   ? 0.138   -0.223  -27.203 1.00 78.02  ?  2    FUC T C1  1 
HETATM 13192 C C2  . FUC T  9  .   ? -0.792  0.862   -27.783 1.00 77.66  ?  2    FUC T C2  1 
HETATM 13193 C C3  . FUC T  9  .   ? -0.693  2.198   -27.003 1.00 76.57  ?  2    FUC T C3  1 
HETATM 13194 C C4  . FUC T  9  .   ? -0.437  2.001   -25.486 1.00 76.39  ?  2    FUC T C4  1 
HETATM 13195 C C5  . FUC T  9  .   ? 0.713   1.005   -25.232 1.00 76.52  ?  2    FUC T C5  1 
HETATM 13196 C C6  . FUC T  9  .   ? 1.941   1.655   -24.604 1.00 75.90  ?  2    FUC T C6  1 
HETATM 13197 O O2  . FUC T  9  .   ? -2.144  0.423   -27.869 1.00 78.55  ?  2    FUC T O2  1 
HETATM 13198 O O3  . FUC T  9  .   ? 0.362   3.002   -27.531 1.00 76.18  ?  2    FUC T O3  1 
HETATM 13199 O O4  . FUC T  9  .   ? -0.118  3.248   -24.890 1.00 75.95  ?  2    FUC T O4  1 
HETATM 13200 O O5  . FUC T  9  .   ? 1.157   0.365   -26.438 1.00 77.18  ?  2    FUC T O5  1 
HETATM 13201 C C1  . NAG U  5  .   ? 6.339   -1.352  30.400  1.00 65.21  ?  1    NAG U C1  1 
HETATM 13202 C C2  . NAG U  5  .   ? 6.756   -2.662  31.061  1.00 63.47  ?  1    NAG U C2  1 
HETATM 13203 C C3  . NAG U  5  .   ? 7.195   -3.658  30.002  1.00 60.62  ?  1    NAG U C3  1 
HETATM 13204 C C4  . NAG U  5  .   ? 6.088   -3.811  28.973  1.00 59.58  ?  1    NAG U C4  1 
HETATM 13205 C C5  . NAG U  5  .   ? 5.692   -2.453  28.410  1.00 60.66  ?  1    NAG U C5  1 
HETATM 13206 C C6  . NAG U  5  .   ? 4.552   -2.591  27.408  1.00 59.01  ?  1    NAG U C6  1 
HETATM 13207 C C7  . NAG U  5  .   ? 7.546   -2.107  33.277  1.00 63.03  ?  1    NAG U C7  1 
HETATM 13208 C C8  . NAG U  5  .   ? 8.540   -1.210  33.952  1.00 60.51  ?  1    NAG U C8  1 
HETATM 13209 N N2  . NAG U  5  .   ? 7.821   -2.432  32.017  1.00 63.10  ?  1    NAG U N2  1 
HETATM 13210 O O3  . NAG U  5  .   ? 7.472   -4.921  30.613  1.00 59.27  ?  1    NAG U O3  1 
HETATM 13211 O O4  . NAG U  5  .   ? 6.540   -4.651  27.911  1.00 57.21  ?  1    NAG U O4  1 
HETATM 13212 O O5  . NAG U  5  .   ? 5.284   -1.593  29.472  1.00 64.08  ?  1    NAG U O5  1 
HETATM 13213 O O6  . NAG U  5  .   ? 4.288   -1.316  26.812  1.00 58.62  ?  1    NAG U O6  1 
HETATM 13214 O O7  . NAG U  5  .   ? 6.547   -2.513  33.846  1.00 63.29  ?  1    NAG U O7  1 
HETATM 13215 C C1  . NAG U  5  .   ? 5.817   -5.891  27.989  1.00 75.11  ?  2    NAG U C1  1 
HETATM 13216 C C2  . NAG U  5  .   ? 5.302   -6.273  26.613  1.00 74.40  ?  2    NAG U C2  1 
HETATM 13217 C C3  . NAG U  5  .   ? 6.460   -6.692  25.725  1.00 74.14  ?  2    NAG U C3  1 
HETATM 13218 C C4  . NAG U  5  .   ? 7.237   -7.817  26.399  1.00 73.90  ?  2    NAG U C4  1 
HETATM 13219 C C5  . NAG U  5  .   ? 7.656   -7.475  27.833  1.00 74.22  ?  2    NAG U C5  1 
HETATM 13220 C C6  . NAG U  5  .   ? 8.821   -6.486  27.857  1.00 74.34  ?  2    NAG U C6  1 
HETATM 13221 C C7  . NAG U  5  .   ? 3.084   -7.103  27.087  1.00 73.50  ?  2    NAG U C7  1 
HETATM 13222 C C8  . NAG U  5  .   ? 2.496   -5.832  26.547  1.00 73.77  ?  2    NAG U C8  1 
HETATM 13223 N N2  . NAG U  5  .   ? 4.341   -7.348  26.735  1.00 73.83  ?  2    NAG U N2  1 
HETATM 13224 O O3  . NAG U  5  .   ? 7.309   -5.566  25.475  1.00 74.42  ?  2    NAG U O3  1 
HETATM 13225 O O4  . NAG U  5  .   ? 6.428   -8.999  26.420  1.00 73.62  ?  2    NAG U O4  1 
HETATM 13226 O O5  . NAG U  5  .   ? 6.553   -6.957  28.594  1.00 74.54  ?  2    NAG U O5  1 
HETATM 13227 O O6  . NAG U  5  .   ? 9.282   -6.329  29.203  1.00 74.44  ?  2    NAG U O6  1 
HETATM 13228 O O7  . NAG U  5  .   ? 2.450   -7.860  27.803  1.00 73.09  ?  2    NAG U O7  1 
HETATM 13229 C C1  . NAG V  10 .   ? 47.158  6.519   55.510  1.00 66.43  ?  1601 NAG A C1  1 
HETATM 13230 C C2  . NAG V  10 .   ? 47.318  7.345   54.221  1.00 65.03  ?  1601 NAG A C2  1 
HETATM 13231 C C3  . NAG V  10 .   ? 47.692  8.794   54.546  1.00 63.74  ?  1601 NAG A C3  1 
HETATM 13232 C C4  . NAG V  10 .   ? 48.921  8.867   55.447  1.00 62.48  ?  1601 NAG A C4  1 
HETATM 13233 C C5  . NAG V  10 .   ? 48.851  7.814   56.546  1.00 62.99  ?  1601 NAG A C5  1 
HETATM 13234 C C6  . NAG V  10 .   ? 49.202  8.356   57.912  1.00 61.35  ?  1601 NAG A C6  1 
HETATM 13235 C C7  . NAG V  10 .   ? 48.021  5.794   52.451  1.00 64.59  ?  1601 NAG A C7  1 
HETATM 13236 C C8  . NAG V  10 .   ? 49.169  5.299   51.623  1.00 62.10  ?  1601 NAG A C8  1 
HETATM 13237 N N2  . NAG V  10 .   ? 48.310  6.750   53.340  1.00 64.02  ?  1601 NAG A N2  1 
HETATM 13238 O O3  . NAG V  10 .   ? 46.591  9.439   55.177  1.00 63.97  ?  1601 NAG A O3  1 
HETATM 13239 O O4  . NAG V  10 .   ? 50.102  8.663   54.679  1.00 61.16  ?  1601 NAG A O4  1 
HETATM 13240 O O5  . NAG V  10 .   ? 47.511  7.314   56.633  1.00 64.51  ?  1601 NAG A O5  1 
HETATM 13241 O O6  . NAG V  10 .   ? 48.175  8.085   58.856  1.00 61.11  ?  1601 NAG A O6  1 
HETATM 13242 O O7  . NAG V  10 .   ? 46.885  5.349   52.320  1.00 66.21  ?  1601 NAG A O7  1 
HETATM 13243 C C1  . NAG W  10 .   ? 62.416  -40.613 87.724  1.00 68.09  ?  1602 NAG A C1  1 
HETATM 13244 C C2  . NAG W  10 .   ? 63.880  -40.971 87.940  1.00 65.35  ?  1602 NAG A C2  1 
HETATM 13245 C C3  . NAG W  10 .   ? 64.051  -42.478 88.029  1.00 63.58  ?  1602 NAG A C3  1 
HETATM 13246 C C4  . NAG W  10 .   ? 63.123  -43.033 89.097  1.00 63.40  ?  1602 NAG A C4  1 
HETATM 13247 C C5  . NAG W  10 .   ? 61.690  -42.591 88.826  1.00 65.99  ?  1602 NAG A C5  1 
HETATM 13248 C C6  . NAG W  10 .   ? 60.741  -43.085 89.911  1.00 64.66  ?  1602 NAG A C6  1 
HETATM 13249 C C7  . NAG W  10 .   ? 65.094  -39.168 86.870  1.00 61.69  ?  1602 NAG A C7  1 
HETATM 13250 C C8  . NAG W  10 .   ? 66.083  -38.815 87.940  1.00 60.22  ?  1602 NAG A C8  1 
HETATM 13251 N N2  . NAG W  10 .   ? 64.687  -40.434 86.862  1.00 64.08  ?  1602 NAG A N2  1 
HETATM 13252 O O3  . NAG W  10 .   ? 65.408  -42.791 88.356  1.00 61.93  ?  1602 NAG A O3  1 
HETATM 13253 O O4  . NAG W  10 .   ? 63.201  -44.462 89.097  1.00 62.06  ?  1602 NAG A O4  1 
HETATM 13254 O O5  . NAG W  10 .   ? 61.633  -41.167 88.780  1.00 67.22  ?  1602 NAG A O5  1 
HETATM 13255 O O6  . NAG W  10 .   ? 60.808  -44.512 90.001  1.00 63.01  ?  1602 NAG A O6  1 
HETATM 13256 O O7  . NAG W  10 .   ? 64.685  -38.348 86.065  1.00 60.78  ?  1602 NAG A O7  1 
HETATM 13257 C C1  . NAG X  10 .   ? 73.414  -30.511 79.117  1.00 76.43  ?  1603 NAG A C1  1 
HETATM 13258 C C2  . NAG X  10 .   ? 74.231  -31.756 78.751  1.00 73.39  ?  1603 NAG A C2  1 
HETATM 13259 C C3  . NAG X  10 .   ? 75.666  -31.360 78.407  1.00 71.10  ?  1603 NAG A C3  1 
HETATM 13260 C C4  . NAG X  10 .   ? 75.679  -30.272 77.340  1.00 69.99  ?  1603 NAG A C4  1 
HETATM 13261 C C5  . NAG X  10 .   ? 74.794  -29.100 77.757  1.00 71.77  ?  1603 NAG A C5  1 
HETATM 13262 C C6  . NAG X  10 .   ? 74.672  -28.040 76.687  1.00 70.34  ?  1603 NAG A C6  1 
HETATM 13263 C C7  . NAG X  10 .   ? 74.437  -34.035 79.639  1.00 71.70  ?  1603 NAG A C7  1 
HETATM 13264 C C8  . NAG X  10 .   ? 74.380  -34.898 80.864  1.00 70.98  ?  1603 NAG A C8  1 
HETATM 13265 N N2  . NAG X  10 .   ? 74.213  -32.731 79.830  1.00 73.15  ?  1603 NAG A N2  1 
HETATM 13266 O O3  . NAG X  10 .   ? 76.380  -32.498 77.940  1.00 69.63  ?  1603 NAG A O3  1 
HETATM 13267 O O4  . NAG X  10 .   ? 77.009  -29.806 77.138  1.00 68.56  ?  1603 NAG A O4  1 
HETATM 13268 O O5  . NAG X  10 .   ? 73.465  -29.566 78.035  1.00 74.51  ?  1603 NAG A O5  1 
HETATM 13269 O O6  . NAG X  10 .   ? 74.781  -26.734 77.237  1.00 71.64  ?  1603 NAG A O6  1 
HETATM 13270 O O7  . NAG X  10 .   ? 74.676  -34.498 78.528  1.00 70.95  ?  1603 NAG A O7  1 
HETATM 13271 C C1  . NAG Y  10 .   ? 32.539  35.022  38.317  1.00 42.29  ?  1401 NAG D C1  1 
HETATM 13272 C C2  . NAG Y  10 .   ? 31.762  36.322  38.516  1.00 40.21  ?  1401 NAG D C2  1 
HETATM 13273 C C3  . NAG Y  10 .   ? 32.466  37.198  39.547  1.00 37.90  ?  1401 NAG D C3  1 
HETATM 13274 C C4  . NAG Y  10 .   ? 32.683  36.423  40.840  1.00 37.28  ?  1401 NAG D C4  1 
HETATM 13275 C C5  . NAG Y  10 .   ? 33.398  35.102  40.559  1.00 38.16  ?  1401 NAG D C5  1 
HETATM 13276 C C6  . NAG Y  10 .   ? 33.517  34.226  41.784  1.00 37.06  ?  1401 NAG D C6  1 
HETATM 13277 C C7  . NAG Y  10 .   ? 30.461  37.013  36.556  1.00 39.96  ?  1401 NAG D C7  1 
HETATM 13278 C C8  . NAG Y  10 .   ? 30.459  37.807  35.287  1.00 37.62  ?  1401 NAG D C8  1 
HETATM 13279 N N2  . NAG Y  10 .   ? 31.597  37.036  37.261  1.00 40.11  ?  1401 NAG D N2  1 
HETATM 13280 O O3  . NAG Y  10 .   ? 31.683  38.359  39.801  1.00 36.97  ?  1401 NAG D O3  1 
HETATM 13281 O O4  . NAG Y  10 .   ? 33.463  37.196  41.745  1.00 35.30  ?  1401 NAG D O4  1 
HETATM 13282 O O5  . NAG Y  10 .   ? 32.674  34.345  39.576  1.00 40.91  ?  1401 NAG D O5  1 
HETATM 13283 O O6  . NAG Y  10 .   ? 32.279  34.135  42.477  1.00 36.28  ?  1401 NAG D O6  1 
HETATM 13284 O O7  . NAG Y  10 .   ? 29.480  36.378  36.928  1.00 40.63  ?  1401 NAG D O7  1 
HETATM 13285 C C1  . NAG Z  10 .   ? -2.732  30.548  31.151  1.00 64.50  ?  1402 NAG D C1  1 
HETATM 13286 C C2  . NAG Z  10 .   ? -2.740  30.817  32.663  1.00 61.23  ?  1402 NAG D C2  1 
HETATM 13287 C C3  . NAG Z  10 .   ? -1.634  31.804  33.049  1.00 59.64  ?  1402 NAG D C3  1 
HETATM 13288 C C4  . NAG Z  10 .   ? -1.717  33.086  32.229  1.00 58.08  ?  1402 NAG D C4  1 
HETATM 13289 C C5  . NAG Z  10 .   ? -2.007  32.775  30.766  1.00 59.22  ?  1402 NAG D C5  1 
HETATM 13290 C C6  . NAG Z  10 .   ? -1.120  33.542  29.812  1.00 57.04  ?  1402 NAG D C6  1 
HETATM 13291 C C7  . NAG Z  10 .   ? -4.868  30.600  33.874  1.00 57.51  ?  1402 NAG D C7  1 
HETATM 13292 C C8  . NAG Z  10 .   ? -4.391  29.238  34.282  1.00 58.33  ?  1402 NAG D C8  1 
HETATM 13293 N N2  . NAG Z  10 .   ? -4.037  31.308  33.100  1.00 59.15  ?  1402 NAG D N2  1 
HETATM 13294 O O3  . NAG Z  10 .   ? -0.364  31.189  32.860  1.00 60.99  ?  1402 NAG D O3  1 
HETATM 13295 O O4  . NAG Z  10 .   ? -2.743  33.927  32.743  1.00 56.17  ?  1402 NAG D O4  1 
HETATM 13296 O O5  . NAG Z  10 .   ? -1.771  31.383  30.521  1.00 61.89  ?  1402 NAG D O5  1 
HETATM 13297 O O6  . NAG Z  10 .   ? 0.216   33.059  29.844  1.00 56.66  ?  1402 NAG D O6  1 
HETATM 13298 O O7  . NAG Z  10 .   ? -5.957  31.040  34.229  1.00 55.14  ?  1402 NAG D O7  1 
HETATM 13299 C C1  . NAG AA 10 .   ? 37.024  4.590   20.336  1.00 61.45  ?  1403 NAG D C1  1 
HETATM 13300 C C2  . NAG AA 10 .   ? 37.292  3.692   19.130  1.00 58.99  ?  1403 NAG D C2  1 
HETATM 13301 C C3  . NAG AA 10 .   ? 38.091  2.453   19.547  1.00 57.78  ?  1403 NAG D C3  1 
HETATM 13302 C C4  . NAG AA 10 .   ? 37.610  1.896   20.884  1.00 57.36  ?  1403 NAG D C4  1 
HETATM 13303 C C5  . NAG AA 10 .   ? 37.584  2.977   21.963  1.00 58.41  ?  1403 NAG D C5  1 
HETATM 13304 C C6  . NAG AA 10 .   ? 38.583  2.731   23.070  1.00 57.34  ?  1403 NAG D C6  1 
HETATM 13305 C C7  . NAG AA 10 .   ? 35.866  3.315   17.160  1.00 56.30  ?  1403 NAG D C7  1 
HETATM 13306 C C8  . NAG AA 10 .   ? 37.036  3.765   16.336  1.00 56.72  ?  1403 NAG D C8  1 
HETATM 13307 N N2  . NAG AA 10 .   ? 36.048  3.302   18.485  1.00 57.57  ?  1403 NAG D N2  1 
HETATM 13308 O O3  . NAG AA 10 .   ? 39.472  2.787   19.631  1.00 57.86  ?  1403 NAG D O3  1 
HETATM 13309 O O4  . NAG AA 10 .   ? 36.305  1.348   20.740  1.00 56.24  ?  1403 NAG D O4  1 
HETATM 13310 O O5  . NAG AA 10 .   ? 37.907  4.249   21.388  1.00 60.16  ?  1403 NAG D O5  1 
HETATM 13311 O O6  . NAG AA 10 .   ? 39.018  3.950   23.656  1.00 57.97  ?  1403 NAG D O6  1 
HETATM 13312 O O7  . NAG AA 10 .   ? 34.803  2.978   16.648  1.00 54.79  ?  1403 NAG D O7  1 
HETATM 13313 C C1  . NAG BA 10 .   ? -9.229  -44.793 -20.725 1.00 86.03  ?  1404 NAG D C1  1 
HETATM 13314 C C2  . NAG BA 10 .   ? -8.400  -46.072 -20.903 1.00 86.19  ?  1404 NAG D C2  1 
HETATM 13315 C C3  . NAG BA 10 .   ? -9.312  -47.308 -20.926 1.00 85.57  ?  1404 NAG D C3  1 
HETATM 13316 C C4  . NAG BA 10 .   ? -10.596 -47.063 -21.717 1.00 83.49  ?  1404 NAG D C4  1 
HETATM 13317 C C5  . NAG BA 10 .   ? -11.292 -45.778 -21.274 1.00 83.86  ?  1404 NAG D C5  1 
HETATM 13318 C C6  . NAG BA 10 .   ? -12.669 -46.014 -20.697 1.00 83.23  ?  1404 NAG D C6  1 
HETATM 13319 C C7  . NAG BA 10 .   ? -6.370  -46.523 -22.226 1.00 85.22  ?  1404 NAG D C7  1 
HETATM 13320 C C8  . NAG BA 10 .   ? -5.816  -47.185 -20.998 1.00 89.05  ?  1404 NAG D C8  1 
HETATM 13321 N N2  . NAG BA 10 .   ? -7.601  -46.008 -22.117 1.00 85.21  ?  1404 NAG D N2  1 
HETATM 13322 O O3  . NAG BA 10 .   ? -9.630  -47.688 -19.592 1.00 88.29  ?  1404 NAG D O3  1 
HETATM 13323 O O4  . NAG BA 10 .   ? -10.326 -46.980 -23.113 1.00 82.60  ?  1404 NAG D O4  1 
HETATM 13324 O O5  . NAG BA 10 .   ? -10.520 -45.128 -20.256 1.00 85.15  ?  1404 NAG D O5  1 
HETATM 13325 O O6  . NAG BA 10 .   ? -13.436 -44.818 -20.688 1.00 83.14  ?  1404 NAG D O6  1 
HETATM 13326 O O7  . NAG BA 10 .   ? -5.729  -46.453 -23.270 1.00 84.65  ?  1404 NAG D O7  1 
HETATM 13327 C C1  . NAG CA 10 .   ? -19.504 -1.063  30.302  1.00 61.15  ?  1405 NAG D C1  1 
HETATM 13328 C C2  . NAG CA 10 .   ? -20.744 -1.877  30.681  1.00 59.52  ?  1405 NAG D C2  1 
HETATM 13329 C C3  . NAG CA 10 .   ? -20.986 -1.810  32.186  1.00 58.23  ?  1405 NAG D C3  1 
HETATM 13330 C C4  . NAG CA 10 .   ? -19.734 -2.229  32.945  1.00 57.63  ?  1405 NAG D C4  1 
HETATM 13331 C C5  . NAG CA 10 .   ? -18.543 -1.392  32.490  1.00 58.29  ?  1405 NAG D C5  1 
HETATM 13332 C C6  . NAG CA 10 .   ? -17.240 -1.825  33.122  1.00 57.27  ?  1405 NAG D C6  1 
HETATM 13333 C C7  . NAG CA 10 .   ? -22.540 -2.150  29.029  1.00 59.04  ?  1405 NAG D C7  1 
HETATM 13334 C C8  . NAG CA 10 .   ? -23.732 -1.515  28.380  1.00 57.77  ?  1405 NAG D C8  1 
HETATM 13335 N N2  . NAG CA 10 .   ? -21.915 -1.414  29.954  1.00 59.40  ?  1405 NAG D N2  1 
HETATM 13336 O O3  . NAG CA 10 .   ? -22.070 -2.666  32.530  1.00 57.59  ?  1405 NAG D O3  1 
HETATM 13337 O O4  . NAG CA 10 .   ? -19.929 -2.051  34.343  1.00 56.80  ?  1405 NAG D O4  1 
HETATM 13338 O O5  . NAG CA 10 .   ? -18.376 -1.515  31.070  1.00 59.78  ?  1405 NAG D O5  1 
HETATM 13339 O O6  . NAG CA 10 .   ? -17.460 -2.521  34.341  1.00 56.45  ?  1405 NAG D O6  1 
HETATM 13340 O O7  . NAG CA 10 .   ? -22.159 -3.277  28.729  1.00 59.03  ?  1405 NAG D O7  1 
HETATM 13341 C C1  . NAG DA 10 .   ? -20.385 -16.802 -0.621  1.00 57.88  ?  1406 NAG D C1  1 
HETATM 13342 C C2  . NAG DA 10 .   ? -20.179 -17.426 0.761   1.00 56.22  ?  1406 NAG D C2  1 
HETATM 13343 C C3  . NAG DA 10 .   ? -21.456 -18.125 1.224   1.00 55.44  ?  1406 NAG D C3  1 
HETATM 13344 C C4  . NAG DA 10 .   ? -22.645 -17.177 1.148   1.00 54.70  ?  1406 NAG D C4  1 
HETATM 13345 C C5  . NAG DA 10 .   ? -22.750 -16.580 -0.251  1.00 56.24  ?  1406 NAG D C5  1 
HETATM 13346 C C6  . NAG DA 10 .   ? -23.844 -15.544 -0.373  1.00 56.28  ?  1406 NAG D C6  1 
HETATM 13347 C C7  . NAG DA 10 .   ? -17.847 -18.053 1.208   1.00 55.38  ?  1406 NAG D C7  1 
HETATM 13348 C C8  . NAG DA 10 .   ? -16.818 -19.139 1.117   1.00 53.61  ?  1406 NAG D C8  1 
HETATM 13349 N N2  . NAG DA 10 .   ? -19.064 -18.359 0.748   1.00 55.86  ?  1406 NAG D N2  1 
HETATM 13350 O O3  . NAG DA 10 .   ? -21.287 -18.584 2.561   1.00 54.12  ?  1406 NAG D O3  1 
HETATM 13351 O O4  . NAG DA 10 .   ? -23.846 -17.875 1.452   1.00 53.94  ?  1406 NAG D O4  1 
HETATM 13352 O O5  . NAG DA 10 .   ? -21.520 -15.924 -0.590  1.00 57.14  ?  1406 NAG D O5  1 
HETATM 13353 O O6  . NAG DA 10 .   ? -24.064 -15.177 -1.728  1.00 59.88  ?  1406 NAG D O6  1 
HETATM 13354 O O7  . NAG DA 10 .   ? -17.588 -16.949 1.676   1.00 55.36  ?  1406 NAG D O7  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . THR A 47  ? 0.9296 0.4804 0.4938 0.1512  -0.0539 0.0617  47  THR A N   
2     C CA  . THR A 47  ? 0.9044 0.4803 0.4956 0.1407  -0.0261 0.0812  47  THR A CA  
3     C C   . THR A 47  ? 0.9483 0.5229 0.5107 0.1546  -0.0028 0.0851  47  THR A C   
4     O O   . THR A 47  ? 0.9394 0.5441 0.5370 0.1557  0.0047  0.0773  47  THR A O   
5     C CB  . THR A 47  ? 0.9256 0.5050 0.5227 0.1226  -0.0081 0.1043  47  THR A CB  
6     O OG1 . THR A 47  ? 1.0010 0.5555 0.5449 0.1292  0.0159  0.1180  47  THR A OG1 
7     C CG2 . THR A 47  ? 0.9174 0.4889 0.5244 0.1129  -0.0302 0.0986  47  THR A CG2 
8     N N   . VAL A 48  ? 0.9120 0.4508 0.4102 0.1639  0.0099  0.0957  48  VAL A N   
9     C CA  . VAL A 48  ? 0.9684 0.5053 0.4373 0.1743  0.0365  0.0969  48  VAL A CA  
10    C C   . VAL A 48  ? 0.9755 0.5120 0.4380 0.1932  0.0196  0.0724  48  VAL A C   
11    O O   . VAL A 48  ? 0.9927 0.5531 0.4753 0.1972  0.0375  0.0668  48  VAL A O   
12    C CB  . VAL A 48  ? 1.0369 0.5273 0.4301 0.1782  0.0540  0.1107  48  VAL A CB  
13    C CG1 . VAL A 48  ? 1.1017 0.5719 0.4412 0.1953  0.0721  0.1054  48  VAL A CG1 
14    C CG2 . VAL A 48  ? 1.0428 0.5432 0.4547 0.1569  0.0872  0.1332  48  VAL A CG2 
15    N N   . GLU A 49  ? 1.0051 0.5156 0.4452 0.2053  -0.0152 0.0550  49  GLU A N   
16    C CA  . GLU A 49  ? 1.0047 0.5184 0.4507 0.2211  -0.0321 0.0268  49  GLU A CA  
17    C C   . GLU A 49  ? 0.9221 0.4776 0.4446 0.2101  -0.0326 0.0159  49  GLU A C   
18    O O   . GLU A 49  ? 0.9067 0.4759 0.4453 0.2181  -0.0262 0.0010  49  GLU A O   
19    C CB  . GLU A 49  ? 1.0232 0.5011 0.4354 0.2366  -0.0714 0.0066  49  GLU A CB  
20    C CG  . GLU A 49  ? 1.1091 0.5439 0.4420 0.2493  -0.0733 0.0109  49  GLU A CG  
21    C CD  . GLU A 49  ? 1.1277 0.5516 0.4553 0.2335  -0.0720 0.0275  49  GLU A CD  
22    O OE1 . GLU A 49  ? 1.0906 0.5281 0.4613 0.2223  -0.0928 0.0209  49  GLU A OE1 
23    O OE2 . GLU A 49  ? 1.1834 0.5842 0.4648 0.2314  -0.0484 0.0461  49  GLU A OE2 
24    N N   . GLU A 50  ? 0.9023 0.4741 0.4686 0.1917  -0.0389 0.0232  50  GLU A N   
25    C CA  . GLU A 50  ? 0.8268 0.4302 0.4548 0.1800  -0.0377 0.0155  50  GLU A CA  
26    C C   . GLU A 50  ? 0.8286 0.4622 0.4802 0.1758  -0.0095 0.0310  50  GLU A C   
27    O O   . GLU A 50  ? 0.8013 0.4488 0.4774 0.1804  -0.0046 0.0205  50  GLU A O   
28    C CB  . GLU A 50  ? 0.7889 0.3989 0.4512 0.1604  -0.0506 0.0193  50  GLU A CB  
29    C CG  . GLU A 50  ? 0.7954 0.3940 0.4576 0.1581  -0.0783 -0.0022 50  GLU A CG  
30    C CD  . GLU A 50  ? 0.7625 0.3749 0.4631 0.1352  -0.0858 0.0013  50  GLU A CD  
31    O OE1 . GLU A 50  ? 0.7649 0.3809 0.4673 0.1250  -0.0732 0.0260  50  GLU A OE1 
32    O OE2 . GLU A 50  ? 0.7281 0.3530 0.4615 0.1255  -0.1016 -0.0208 50  GLU A OE2 
33    N N   . ALA A 51  ? 0.7927 0.4356 0.4402 0.1674  0.0096  0.0543  51  ALA A N   
34    C CA  . ALA A 51  ? 0.8015 0.4774 0.4821 0.1635  0.0342  0.0659  51  ALA A CA  
35    C C   . ALA A 51  ? 0.8416 0.5164 0.5054 0.1808  0.0501  0.0576  51  ALA A C   
36    O O   . ALA A 51  ? 0.8179 0.5166 0.5179 0.1841  0.0579  0.0542  51  ALA A O   
37    C CB  . ALA A 51  ? 0.8397 0.5247 0.5226 0.1504  0.0539  0.0873  51  ALA A CB  
38    N N   . ASN A 52  ? 0.8244 0.4685 0.4305 0.1927  0.0547  0.0541  52  ASN A N   
39    C CA  . ASN A 52  ? 0.8642 0.5049 0.4504 0.2087  0.0706  0.0437  52  ASN A CA  
40    C C   . ASN A 52  ? 0.8057 0.4492 0.4108 0.2196  0.0545  0.0205  52  ASN A C   
41    O O   . ASN A 52  ? 0.7988 0.4558 0.4199 0.2283  0.0694  0.0132  52  ASN A O   
42    C CB  . ASN A 52  ? 0.9520 0.5514 0.4613 0.2191  0.0755  0.0435  52  ASN A CB  
43    C CG  . ASN A 52  ? 1.0083 0.6021 0.4960 0.2094  0.1077  0.0647  52  ASN A CG  
44    O OD1 . ASN A 52  ? 1.0241 0.6493 0.5530 0.2024  0.1354  0.0712  52  ASN A OD1 
45    N ND2 . ASN A 52  ? 1.0336 0.5850 0.4579 0.2092  0.1046  0.0742  52  ASN A ND2 
46    N N   . ALA A 53  ? 0.8134 0.4433 0.4200 0.2186  0.0262  0.0067  53  ALA A N   
47    C CA  . ALA A 53  ? 0.7916 0.4221 0.4214 0.2256  0.0147  -0.0180 53  ALA A CA  
48    C C   . ALA A 53  ? 0.7447 0.4015 0.4293 0.2164  0.0230  -0.0124 53  ALA A C   
49    O O   . ALA A 53  ? 0.7350 0.4025 0.4401 0.2201  0.0294  -0.0237 53  ALA A O   
50    C CB  . ALA A 53  ? 0.7848 0.4026 0.4139 0.2205  -0.0154 -0.0363 53  ALA A CB  
51    N N   . LEU A 54  ? 0.7402 0.4120 0.4504 0.1997  0.0212  0.0058  54  LEU A N   
52    C CA  . LEU A 54  ? 0.7047 0.3980 0.4582 0.1929  0.0269  0.0137  54  LEU A CA  
53    C C   . LEU A 54  ? 0.7284 0.4424 0.4948 0.2028  0.0485  0.0228  54  LEU A C   
54    O O   . LEU A 54  ? 0.7042 0.4241 0.4940 0.2097  0.0526  0.0185  54  LEU A O   
55    C CB  . LEU A 54  ? 0.6923 0.3989 0.4672 0.1737  0.0197  0.0305  54  LEU A CB  
56    C CG  . LEU A 54  ? 0.6509 0.3456 0.4390 0.1600  0.0019  0.0212  54  LEU A CG  
57    C CD1 . LEU A 54  ? 0.6376 0.3325 0.4454 0.1591  0.0032  0.0093  54  LEU A CD1 
58    C CD2 . LEU A 54  ? 0.6616 0.3347 0.4283 0.1592  -0.0130 0.0041  54  LEU A CD2 
59    N N   . LEU A 55  ? 0.6893 0.4115 0.4412 0.2034  0.0642  0.0345  55  LEU A N   
60    C CA  . LEU A 55  ? 0.7003 0.4434 0.4701 0.2117  0.0879  0.0392  55  LEU A CA  
61    C C   . LEU A 55  ? 0.7186 0.4509 0.4768 0.2295  0.0952  0.0213  55  LEU A C   
62    O O   . LEU A 55  ? 0.7139 0.4638 0.5035 0.2379  0.1077  0.0204  55  LEU A O   
63    C CB  . LEU A 55  ? 0.7376 0.4826 0.4865 0.2069  0.1086  0.0506  55  LEU A CB  
64    C CG  . LEU A 55  ? 0.7363 0.5120 0.5270 0.1925  0.1179  0.0674  55  LEU A CG  
65    C CD1 . LEU A 55  ? 0.7976 0.5613 0.5564 0.1831  0.1370  0.0775  55  LEU A CD1 
66    C CD2 . LEU A 55  ? 0.7259 0.5357 0.5692 0.1994  0.1327  0.0664  55  LEU A CD2 
67    N N   . LYS A 56  ? 0.7306 0.4344 0.4469 0.2363  0.0860  0.0050  56  LYS A N   
68    C CA  . LYS A 56  ? 0.7469 0.4404 0.4548 0.2523  0.0912  -0.0160 56  LYS A CA  
69    C C   . LYS A 56  ? 0.7093 0.4164 0.4614 0.2432  0.0794  -0.0233 56  LYS A C   
70    O O   . LYS A 56  ? 0.7083 0.4281 0.4830 0.2459  0.0881  -0.0298 56  LYS A O   
71    C CB  . LYS A 56  ? 0.7794 0.4463 0.4377 0.2570  0.0778  -0.0332 56  LYS A CB  
72    C CG  . LYS A 56  ? 0.7724 0.4509 0.4485 0.2519  0.0679  -0.0544 56  LYS A CG  
73    C CD  . LYS A 56  ? 0.8218 0.4833 0.4496 0.2624  0.0674  -0.0669 56  LYS A CD  
74    C CE  . LYS A 56  ? 0.8111 0.4847 0.4631 0.2552  0.0517  -0.0899 56  LYS A CE  
75    N NZ  . LYS A 56  ? 0.8520 0.5221 0.4801 0.2656  0.0632  -0.1010 56  LYS A NZ  
76    N N   . TRP A 57  ? 0.7167 0.4215 0.4819 0.2281  0.0606  -0.0221 57  TRP A N   
77    C CA  . TRP A 57  ? 0.6881 0.4021 0.4894 0.2147  0.0536  -0.0274 57  TRP A CA  
78    C C   . TRP A 57  ? 0.6812 0.4068 0.5095 0.2208  0.0628  -0.0115 57  TRP A C   
79    O O   . TRP A 57  ? 0.6775 0.4068 0.5271 0.2193  0.0647  -0.0162 57  TRP A O   
80    C CB  . TRP A 57  ? 0.6641 0.3723 0.4715 0.1958  0.0363  -0.0305 57  TRP A CB  
81    C CG  . TRP A 57  ? 0.6436 0.3542 0.4803 0.1815  0.0345  -0.0355 57  TRP A CG  
82    C CD1 . TRP A 57  ? 0.6434 0.3574 0.4983 0.1778  0.0398  -0.0498 57  TRP A CD1 
83    C CD2 . TRP A 57  ? 0.6268 0.3327 0.4745 0.1691  0.0287  -0.0259 57  TRP A CD2 
84    N NE1 . TRP A 57  ? 0.6311 0.3395 0.5038 0.1650  0.0391  -0.0490 57  TRP A NE1 
85    C CE2 . TRP A 57  ? 0.6227 0.3249 0.4881 0.1597  0.0321  -0.0345 57  TRP A CE2 
86    C CE3 . TRP A 57  ? 0.6182 0.3214 0.4616 0.1642  0.0213  -0.0107 57  TRP A CE3 
87    C CZ2 . TRP A 57  ? 0.6165 0.3078 0.4866 0.1473  0.0291  -0.0285 57  TRP A CZ2 
88    C CZ3 . TRP A 57  ? 0.6074 0.3039 0.4604 0.1504  0.0166  -0.0057 57  TRP A CZ3 
89    C CH2 . TRP A 57  ? 0.6096 0.2979 0.4716 0.1428  0.0209  -0.0144 57  TRP A CH2 
90    N N   . LYS A 58  ? 0.6602 0.3921 0.4916 0.2276  0.0672  0.0076  58  LYS A N   
91    C CA  . LYS A 58  ? 0.6548 0.4048 0.5204 0.2355  0.0724  0.0218  58  LYS A CA  
92    C C   . LYS A 58  ? 0.6716 0.4339 0.5521 0.2500  0.0893  0.0152  58  LYS A C   
93    O O   . LYS A 58  ? 0.6689 0.4415 0.5801 0.2546  0.0875  0.0184  58  LYS A O   
94    C CB  . LYS A 58  ? 0.6454 0.4206 0.5262 0.2273  0.0728  0.0399  58  LYS A CB  
95    C CG  . LYS A 58  ? 0.6381 0.4422 0.5644 0.2326  0.0730  0.0511  58  LYS A CG  
96    C CD  . LYS A 58  ? 0.6712 0.5076 0.6203 0.2219  0.0789  0.0626  58  LYS A CD  
97    C CE  . LYS A 58  ? 0.6829 0.5538 0.6834 0.2329  0.0884  0.0643  58  LYS A CE  
98    N NZ  . LYS A 58  ? 0.7242 0.6263 0.7500 0.2220  0.1037  0.0692  58  LYS A NZ  
99    N N   . SER A 59  ? 0.6841 0.4430 0.5410 0.2572  0.1047  0.0053  59  SER A N   
100   C CA  . SER A 59  ? 0.7020 0.4727 0.5726 0.2678  0.1225  -0.0036 59  SER A CA  
101   C C   . SER A 59  ? 0.6962 0.4635 0.5827 0.2624  0.1133  -0.0158 59  SER A C   
102   O O   . SER A 59  ? 0.7041 0.4834 0.6182 0.2707  0.1225  -0.0190 59  SER A O   
103   C CB  . SER A 59  ? 0.7341 0.4944 0.5637 0.2726  0.1385  -0.0139 59  SER A CB  
104   O OG  . SER A 59  ? 0.7516 0.5195 0.5905 0.2777  0.1517  -0.0272 59  SER A OG  
105   N N   . THR A 60  ? 0.7058 0.4576 0.5796 0.2480  0.0972  -0.0240 60  THR A N   
106   C CA  . THR A 60  ? 0.7022 0.4488 0.5928 0.2409  0.0929  -0.0359 60  THR A CA  
107   C C   . THR A 60  ? 0.6990 0.4452 0.6155 0.2441  0.0888  -0.0237 60  THR A C   
108   O O   . THR A 60  ? 0.7081 0.4503 0.6407 0.2460  0.0915  -0.0304 60  THR A O   
109   C CB  . THR A 60  ? 0.6882 0.4228 0.5683 0.2228  0.0803  -0.0483 60  THR A CB  
110   O OG1 . THR A 60  ? 0.6985 0.4347 0.5631 0.2222  0.0816  -0.0653 60  THR A OG1 
111   C CG2 . THR A 60  ? 0.6819 0.4087 0.5832 0.2124  0.0776  -0.0560 60  THR A CG2 
112   N N   . PHE A 61  ? 0.6867 0.4360 0.6073 0.2461  0.0812  -0.0060 61  PHE A N   
113   C CA  . PHE A 61  ? 0.6890 0.4328 0.6269 0.2481  0.0706  0.0059  61  PHE A CA  
114   C C   . PHE A 61  ? 0.7059 0.4616 0.6745 0.2651  0.0766  0.0063  61  PHE A C   
115   O O   . PHE A 61  ? 0.7096 0.4883 0.6965 0.2772  0.0890  0.0050  61  PHE A O   
116   C CB  . PHE A 61  ? 0.6778 0.4289 0.6185 0.2473  0.0589  0.0237  61  PHE A CB  
117   C CG  . PHE A 61  ? 0.6620 0.4000 0.5765 0.2296  0.0513  0.0232  61  PHE A CG  
118   C CD1 . PHE A 61  ? 0.6585 0.3784 0.5547 0.2150  0.0518  0.0074  61  PHE A CD1 
119   C CD2 . PHE A 61  ? 0.6500 0.3972 0.5653 0.2269  0.0435  0.0369  61  PHE A CD2 
120   C CE1 . PHE A 61  ? 0.6434 0.3547 0.5240 0.1988  0.0443  0.0040  61  PHE A CE1 
121   C CE2 . PHE A 61  ? 0.6364 0.3712 0.5309 0.2099  0.0361  0.0352  61  PHE A CE2 
122   C CZ  . PHE A 61  ? 0.6333 0.3500 0.5109 0.1963  0.0363  0.0180  61  PHE A CZ  
123   N N   . THR A 62  ? 0.7101 0.4480 0.6843 0.2659  0.0692  0.0075  62  THR A N   
124   C CA  . THR A 62  ? 0.7303 0.4741 0.7346 0.2822  0.0711  0.0067  62  THR A CA  
125   C C   . THR A 62  ? 0.7430 0.4836 0.7633 0.2915  0.0517  0.0236  62  THR A C   
126   O O   . THR A 62  ? 0.7421 0.4658 0.7409 0.2822  0.0376  0.0347  62  THR A O   
127   C CB  . THR A 62  ? 0.7461 0.4683 0.7440 0.2782  0.0779  -0.0066 62  THR A CB  
128   O OG1 . THR A 62  ? 0.7617 0.4518 0.7426 0.2722  0.0670  0.0015  62  THR A OG1 
129   C CG2 . THR A 62  ? 0.7321 0.4541 0.7106 0.2635  0.0885  -0.0240 62  THR A CG2 
130   N N   . ASN A 63  ? 0.7694 0.5272 0.8295 0.3101  0.0497  0.0237  63  ASN A N   
131   C CA  . ASN A 63  ? 0.7876 0.5454 0.8713 0.3226  0.0267  0.0373  63  ASN A CA  
132   C C   . ASN A 63  ? 0.7706 0.5449 0.8560 0.3191  0.0115  0.0504  63  ASN A C   
133   O O   . ASN A 63  ? 0.7849 0.5448 0.8616 0.3184  -0.0109 0.0638  63  ASN A O   
134   C CB  . ASN A 63  ? 0.8198 0.5335 0.8762 0.3201  0.0162  0.0438  63  ASN A CB  
135   C CG  . ASN A 63  ? 0.8427 0.5436 0.9107 0.3286  0.0274  0.0324  63  ASN A CG  
136   O OD1 . ASN A 63  ? 0.8303 0.5518 0.9165 0.3309  0.0454  0.0167  63  ASN A OD1 
137   N ND2 . ASN A 63  ? 0.8808 0.5457 0.9355 0.3332  0.0175  0.0404  63  ASN A ND2 
138   N N   . GLN A 64  ? 0.8378 0.6418 0.9324 0.3163  0.0250  0.0467  64  GLN A N   
139   C CA  . GLN A 64  ? 0.8171 0.6402 0.9162 0.3119  0.0148  0.0576  64  GLN A CA  
140   C C   . GLN A 64  ? 0.8142 0.6823 0.9767 0.3299  0.0098  0.0575  64  GLN A C   
141   O O   . GLN A 64  ? 0.8120 0.7062 1.0101 0.3401  0.0303  0.0457  64  GLN A O   
142   C CB  . GLN A 64  ? 0.7974 0.6239 0.8697 0.2986  0.0342  0.0548  64  GLN A CB  
143   C CG  . GLN A 64  ? 0.7875 0.6100 0.8391 0.2849  0.0209  0.0667  64  GLN A CG  
144   C CD  . GLN A 64  ? 0.7882 0.5698 0.7969 0.2686  0.0066  0.0691  64  GLN A CD  
145   O OE1 . GLN A 64  ? 0.7825 0.5396 0.7605 0.2576  0.0177  0.0590  64  GLN A OE1 
146   N NE2 . GLN A 64  ? 0.7979 0.5735 0.8062 0.2665  -0.0166 0.0808  64  GLN A NE2 
147   N N   . THR A 65  ? 0.7944 0.6737 0.9738 0.3323  -0.0165 0.0682  65  THR A N   
148   C CA  . THR A 65  ? 0.7910 0.7186 1.0402 0.3488  -0.0262 0.0650  65  THR A CA  
149   C C   . THR A 65  ? 0.7554 0.7229 1.0270 0.3405  -0.0122 0.0676  65  THR A C   
150   O O   . THR A 65  ? 0.7414 0.6933 0.9680 0.3182  -0.0099 0.0748  65  THR A O   
151   C CB  . THR A 65  ? 0.8131 0.7337 1.0750 0.3558  -0.0644 0.0756  65  THR A CB  
152   O OG1 . THR A 65  ? 0.8079 0.7279 1.0451 0.3430  -0.0815 0.0872  65  THR A OG1 
153   C CG2 . THR A 65  ? 0.8527 0.7207 1.0702 0.3546  -0.0711 0.0829  65  THR A CG2 
154   N N   . SER A 66  ? 0.7033 0.7236 1.0478 0.3450  -0.0034 0.0557  66  SER A N   
155   C CA  . SER A 66  ? 0.7117 0.7712 1.0823 0.3221  0.0124  0.0518  66  SER A CA  
156   C C   . SER A 66  ? 0.7103 0.7782 1.0799 0.3104  -0.0182 0.0610  66  SER A C   
157   O O   . SER A 66  ? 0.7161 0.8055 1.0922 0.2875  -0.0058 0.0607  66  SER A O   
158   C CB  . SER A 66  ? 0.7136 0.8262 1.1694 0.3291  0.0323  0.0330  66  SER A CB  
159   O OG  . SER A 66  ? 0.7102 0.8452 1.2268 0.3536  0.0010  0.0263  66  SER A OG  
160   N N   . SER A 67  ? 0.6950 0.7425 1.0525 0.3254  -0.0571 0.0689  67  SER A N   
161   C CA  . SER A 67  ? 0.6977 0.7470 1.0455 0.3153  -0.0888 0.0771  67  SER A CA  
162   C C   . SER A 67  ? 0.6972 0.6976 0.9623 0.2950  -0.0895 0.0913  67  SER A C   
163   O O   . SER A 67  ? 0.7025 0.6953 0.9484 0.2854  -0.1147 0.0985  67  SER A O   
164   C CB  . SER A 67  ? 0.7103 0.7548 1.0743 0.3412  -0.1314 0.0788  67  SER A CB  
165   O OG  . SER A 67  ? 0.7481 0.7357 1.0471 0.3469  -0.1321 0.0911  67  SER A OG  
166   N N   . SER A 68  ? 0.7009 0.6688 0.9200 0.2885  -0.0631 0.0927  68  SER A N   
167   C CA  . SER A 68  ? 0.7004 0.6227 0.8496 0.2702  -0.0628 0.1012  68  SER A CA  
168   C C   . SER A 68  ? 0.6986 0.6415 0.8480 0.2425  -0.0579 0.1028  68  SER A C   
169   O O   . SER A 68  ? 0.7101 0.6957 0.9030 0.2350  -0.0419 0.0971  68  SER A O   
170   C CB  . SER A 68  ? 0.6838 0.5737 0.7954 0.2712  -0.0365 0.0967  68  SER A CB  
171   O OG  . SER A 68  ? 0.6727 0.5270 0.7295 0.2515  -0.0336 0.0995  68  SER A OG  
172   N N   . LYS A 69  ? 0.6574 0.5663 0.7575 0.2264  -0.0692 0.1098  69  LYS A N   
173   C CA  . LYS A 69  ? 0.6612 0.5836 0.7582 0.1999  -0.0655 0.1113  69  LYS A CA  
174   C C   . LYS A 69  ? 0.6584 0.5815 0.7442 0.1883  -0.0354 0.1072  69  LYS A C   
175   O O   . LYS A 69  ? 0.6671 0.6083 0.7616 0.1695  -0.0278 0.1082  69  LYS A O   
176   C CB  . LYS A 69  ? 0.6495 0.5315 0.6964 0.1854  -0.0826 0.1170  69  LYS A CB  
177   C CG  . LYS A 69  ? 0.6713 0.5528 0.7212 0.1907  -0.1149 0.1224  69  LYS A CG  
178   C CD  . LYS A 69  ? 0.6827 0.6182 0.7856 0.1813  -0.1244 0.1200  69  LYS A CD  
179   C CE  . LYS A 69  ? 0.6881 0.6128 0.7728 0.1739  -0.1556 0.1240  69  LYS A CE  
180   N NZ  . LYS A 69  ? 0.7020 0.5655 0.7238 0.1844  -0.1714 0.1311  69  LYS A NZ  
181   N N   . LEU A 70  ? 0.6240 0.5249 0.6879 0.1997  -0.0190 0.1023  70  LEU A N   
182   C CA  . LEU A 70  ? 0.6319 0.5269 0.6755 0.1920  0.0055  0.0975  70  LEU A CA  
183   C C   . LEU A 70  ? 0.6640 0.5957 0.7443 0.1947  0.0287  0.0942  70  LEU A C   
184   O O   . LEU A 70  ? 0.6816 0.6033 0.7380 0.1921  0.0507  0.0905  70  LEU A O   
185   C CB  . LEU A 70  ? 0.6148 0.4715 0.6204 0.2030  0.0131  0.0899  70  LEU A CB  
186   C CG  . LEU A 70  ? 0.5892 0.4043 0.5495 0.1911  0.0050  0.0867  70  LEU A CG  
187   C CD1 . LEU A 70  ? 0.5806 0.3851 0.5362 0.1799  -0.0167 0.0940  70  LEU A CD1 
188   C CD2 . LEU A 70  ? 0.6005 0.3813 0.5362 0.2044  0.0120  0.0759  70  LEU A CD2 
189   N N   . SER A 71  ? 0.5622 0.5335 0.6988 0.1999  0.0248  0.0936  71  SER A N   
190   C CA  . SER A 71  ? 0.5877 0.5946 0.7655 0.1976  0.0515  0.0876  71  SER A CA  
191   C C   . SER A 71  ? 0.6209 0.6299 0.7851 0.1739  0.0669  0.0919  71  SER A C   
192   O O   . SER A 71  ? 0.6605 0.6793 0.8326 0.1690  0.0978  0.0881  71  SER A O   
193   C CB  . SER A 71  ? 0.5837 0.6361 0.8352 0.2070  0.0408  0.0815  71  SER A CB  
194   O OG  . SER A 71  ? 0.5697 0.6133 0.8280 0.2299  0.0177  0.0806  71  SER A OG  
195   N N   . SER A 72  ? 0.5954 0.5913 0.7371 0.1587  0.0480  0.0994  72  SER A N   
196   C CA  . SER A 72  ? 0.5907 0.5849 0.7198 0.1367  0.0600  0.1042  72  SER A CA  
197   C C   . SER A 72  ? 0.6089 0.5648 0.6785 0.1343  0.0774  0.1059  72  SER A C   
198   O O   . SER A 72  ? 0.6154 0.5635 0.6686 0.1189  0.0900  0.1107  72  SER A O   
199   C CB  . SER A 72  ? 0.5706 0.5605 0.6942 0.1220  0.0334  0.1097  72  SER A CB  
200   O OG  . SER A 72  ? 0.5703 0.5270 0.6561 0.1287  0.0124  0.1104  72  SER A OG  
201   N N   . TRP A 73  ? 0.6194 0.5493 0.6555 0.1499  0.0770  0.1011  73  TRP A N   
202   C CA  . TRP A 73  ? 0.6415 0.5350 0.6204 0.1511  0.0886  0.0992  73  TRP A CA  
203   C C   . TRP A 73  ? 0.6726 0.5715 0.6501 0.1565  0.1219  0.0962  73  TRP A C   
204   O O   . TRP A 73  ? 0.6882 0.5834 0.6610 0.1723  0.1323  0.0879  73  TRP A O   
205   C CB  . TRP A 73  ? 0.6422 0.5068 0.5906 0.1643  0.0742  0.0913  73  TRP A CB  
206   C CG  . TRP A 73  ? 0.6206 0.4702 0.5619 0.1563  0.0477  0.0918  73  TRP A CG  
207   C CD1 . TRP A 73  ? 0.5998 0.4642 0.5647 0.1425  0.0326  0.0989  73  TRP A CD1 
208   C CD2 . TRP A 73  ? 0.6217 0.4372 0.5311 0.1605  0.0359  0.0821  73  TRP A CD2 
209   N NE1 . TRP A 73  ? 0.5908 0.4292 0.5355 0.1369  0.0140  0.0953  73  TRP A NE1 
210   C CE2 . TRP A 73  ? 0.6032 0.4118 0.5167 0.1473  0.0169  0.0843  73  TRP A CE2 
211   C CE3 . TRP A 73  ? 0.6386 0.4288 0.5185 0.1732  0.0411  0.0692  73  TRP A CE3 
212   C CZ2 . TRP A 73  ? 0.6022 0.3779 0.4929 0.1450  0.0064  0.0736  73  TRP A CZ2 
213   C CZ3 . TRP A 73  ? 0.6344 0.3955 0.4965 0.1719  0.0283  0.0574  73  TRP A CZ3 
214   C CH2 . TRP A 73  ? 0.6168 0.3702 0.4851 0.1572  0.0128  0.0595  73  TRP A CH2 
215   N N   . VAL A 74  ? 0.6765 0.5817 0.6573 0.1418  0.1417  0.1020  74  VAL A N   
216   C CA  . VAL A 74  ? 0.7356 0.6420 0.7135 0.1429  0.1794  0.0986  74  VAL A CA  
217   C C   . VAL A 74  ? 0.7891 0.6516 0.6966 0.1353  0.1951  0.1054  74  VAL A C   
218   O O   . VAL A 74  ? 0.8078 0.6399 0.6640 0.1458  0.2085  0.1011  74  VAL A O   
219   C CB  . VAL A 74  ? 0.7406 0.6919 0.7900 0.1327  0.1981  0.0963  74  VAL A CB  
220   C CG1 . VAL A 74  ? 0.7527 0.7114 0.8153 0.1374  0.2381  0.0864  74  VAL A CG1 
221   C CG2 . VAL A 74  ? 0.6869 0.6778 0.8009 0.1386  0.1691  0.0925  74  VAL A CG2 
222   N N   . ASN A 75  ? 0.8952 0.7509 0.7968 0.1182  0.1921  0.1155  75  ASN A N   
223   C CA  . ASN A 75  ? 0.9060 0.7163 0.7411 0.1112  0.2079  0.1240  75  ASN A CA  
224   C C   . ASN A 75  ? 0.8665 0.6407 0.6502 0.1158  0.1743  0.1265  75  ASN A C   
225   O O   . ASN A 75  ? 0.8227 0.6094 0.6326 0.1078  0.1480  0.1283  75  ASN A O   
226   C CB  . ASN A 75  ? 0.9050 0.7252 0.7654 0.0896  0.2289  0.1326  75  ASN A CB  
227   C CG  . ASN A 75  ? 0.9237 0.6886 0.7098 0.0824  0.2423  0.1445  75  ASN A CG  
228   O OD1 . ASN A 75  ? 0.9553 0.6754 0.6696 0.0940  0.2501  0.1452  75  ASN A OD1 
229   N ND2 . ASN A 75  ? 0.9052 0.6702 0.7059 0.0641  0.2440  0.1536  75  ASN A ND2 
230   N N   . PRO A 76  ? 0.9654 0.6949 0.6782 0.1284  0.1735  0.1240  76  PRO A N   
231   C CA  . PRO A 76  ? 0.9270 0.6248 0.5994 0.1345  0.1389  0.1211  76  PRO A CA  
232   C C   . PRO A 76  ? 0.9213 0.5904 0.5647 0.1224  0.1324  0.1330  76  PRO A C   
233   O O   . PRO A 76  ? 0.8839 0.5319 0.5073 0.1260  0.1014  0.1285  76  PRO A O   
234   C CB  . PRO A 76  ? 0.9675 0.6299 0.5768 0.1540  0.1411  0.1115  76  PRO A CB  
235   C CG  . PRO A 76  ? 1.0441 0.6985 0.6321 0.1516  0.1830  0.1178  76  PRO A CG  
236   C CD  . PRO A 76  ? 1.0322 0.7401 0.7021 0.1391  0.2023  0.1198  76  PRO A CD  
237   N N   . ASN A 77  ? 0.9981 0.6643 0.6414 0.1083  0.1618  0.1460  77  ASN A N   
238   C CA  . ASN A 77  ? 0.9836 0.6202 0.6016 0.0964  0.1574  0.1583  77  ASN A CA  
239   C C   . ASN A 77  ? 0.9185 0.5863 0.5944 0.0836  0.1303  0.1568  77  ASN A C   
240   O O   . ASN A 77  ? 0.8880 0.6044 0.6295 0.0775  0.1277  0.1516  77  ASN A O   
241   C CB  . ASN A 77  ? 1.0230 0.6511 0.6362 0.0811  0.2007  0.1710  77  ASN A CB  
242   C CG  . ASN A 77  ? 1.0943 0.6702 0.6259 0.0909  0.2287  0.1752  77  ASN A CG  
243   O OD1 . ASN A 77  ? 1.1052 0.6436 0.5728 0.1100  0.2094  0.1708  77  ASN A OD1 
244   N ND2 . ASN A 77  ? 1.1327 0.7045 0.6657 0.0773  0.2755  0.1817  77  ASN A ND2 
245   N N   . THR A 78  ? 0.9975 0.6338 0.6461 0.0806  0.1090  0.1606  78  THR A N   
246   C CA  . THR A 78  ? 0.9331 0.5934 0.6316 0.0667  0.0853  0.1576  78  THR A CA  
247   C C   . THR A 78  ? 0.9224 0.6213 0.6795 0.0447  0.1055  0.1654  78  THR A C   
248   O O   . THR A 78  ? 0.8730 0.6035 0.6810 0.0328  0.0887  0.1608  78  THR A O   
249   C CB  . THR A 78  ? 0.9200 0.5370 0.5804 0.0675  0.0621  0.1591  78  THR A CB  
250   O OG1 . THR A 78  ? 0.9481 0.5282 0.5485 0.0885  0.0491  0.1507  78  THR A OG1 
251   C CG2 . THR A 78  ? 0.8498 0.4870 0.5549 0.0598  0.0309  0.1465  78  THR A CG2 
252   N N   . SER A 79  ? 0.8644 0.5602 0.6156 0.0385  0.1424  0.1748  79  SER A N   
253   C CA  . SER A 79  ? 0.8602 0.5962 0.6747 0.0180  0.1644  0.1775  79  SER A CA  
254   C C   . SER A 79  ? 0.8582 0.6540 0.7421 0.0189  0.1601  0.1663  79  SER A C   
255   O O   . SER A 79  ? 0.8622 0.6986 0.8078 0.0038  0.1709  0.1642  79  SER A O   
256   C CB  . SER A 79  ? 0.9213 0.6347 0.7119 0.0110  0.2101  0.1865  79  SER A CB  
257   O OG  . SER A 79  ? 0.9658 0.6668 0.7226 0.0265  0.2287  0.1832  79  SER A OG  
258   N N   . SER A 80  ? 0.8042 0.6049 0.6795 0.0373  0.1455  0.1582  80  SER A N   
259   C CA  . SER A 80  ? 0.7845 0.6327 0.7175 0.0410  0.1315  0.1487  80  SER A CA  
260   C C   . SER A 80  ? 0.7374 0.5765 0.6548 0.0534  0.0982  0.1414  80  SER A C   
261   O O   . SER A 80  ? 0.7159 0.5845 0.6734 0.0532  0.0810  0.1360  80  SER A O   
262   C CB  . SER A 80  ? 0.8317 0.7032 0.7882 0.0506  0.1573  0.1434  80  SER A CB  
263   O OG  . SER A 80  ? 0.8676 0.7010 0.7636 0.0647  0.1716  0.1440  80  SER A OG  
264   N N   . PHE A 81  ? 0.8256 0.6226 0.6854 0.0646  0.0891  0.1396  81  PHE A N   
265   C CA  . PHE A 81  ? 0.7840 0.5714 0.6333 0.0757  0.0624  0.1284  81  PHE A CA  
266   C C   . PHE A 81  ? 0.7284 0.5241 0.6041 0.0615  0.0382  0.1251  81  PHE A C   
267   O O   . PHE A 81  ? 0.7059 0.5169 0.6049 0.0630  0.0249  0.1184  81  PHE A O   
268   C CB  . PHE A 81  ? 0.7956 0.5375 0.5831 0.0894  0.0561  0.1234  81  PHE A CB  
269   C CG  . PHE A 81  ? 0.7481 0.4779 0.5293 0.0982  0.0302  0.1074  81  PHE A CG  
270   C CD1 . PHE A 81  ? 0.7396 0.4840 0.5377 0.1086  0.0289  0.0983  81  PHE A CD1 
271   C CD2 . PHE A 81  ? 0.7215 0.4234 0.4826 0.0961  0.0086  0.0995  81  PHE A CD2 
272   C CE1 . PHE A 81  ? 0.6991 0.4287 0.4923 0.1146  0.0102  0.0818  81  PHE A CE1 
273   C CE2 . PHE A 81  ? 0.6855 0.3770 0.4480 0.1023  -0.0115 0.0802  81  PHE A CE2 
274   C CZ  . PHE A 81  ? 0.6733 0.3776 0.4507 0.1106  -0.0088 0.0715  81  PHE A CZ  
275   N N   . CYS A 82  ? 0.7693 0.5516 0.6393 0.0473  0.0339  0.1297  82  CYS A N   
276   C CA  . CYS A 82  ? 0.7208 0.5041 0.6097 0.0332  0.0121  0.1236  82  CYS A CA  
277   C C   . CYS A 82  ? 0.7111 0.5323 0.6500 0.0156  0.0129  0.1276  82  CYS A C   
278   O O   . CYS A 82  ? 0.6775 0.5003 0.6317 0.0019  -0.0032 0.1221  82  CYS A O   
279   C CB  . CYS A 82  ? 0.7174 0.4679 0.5808 0.0270  0.0048  0.1244  82  CYS A CB  
280   S SG  . CYS A 82  ? 0.7094 0.4146 0.5206 0.0479  -0.0123 0.1108  82  CYS A SG  
281   N N   . THR A 83  ? 0.6265 0.4781 0.5929 0.0154  0.0310  0.1344  83  THR A N   
282   C CA  . THR A 83  ? 0.6145 0.5051 0.6325 0.0002  0.0292  0.1352  83  THR A CA  
283   C C   . THR A 83  ? 0.6373 0.5629 0.6892 0.0108  0.0286  0.1322  83  THR A C   
284   O O   . THR A 83  ? 0.6276 0.5770 0.7104 0.0044  0.0121  0.1287  83  THR A O   
285   C CB  . THR A 83  ? 0.6338 0.5335 0.6701 -0.0152 0.0510  0.1426  83  THR A CB  
286   O OG1 . THR A 83  ? 0.6842 0.5989 0.7323 -0.0076 0.0781  0.1452  83  THR A OG1 
287   C CG2 . THR A 83  ? 0.6339 0.4899 0.6271 -0.0197 0.0533  0.1479  83  THR A CG2 
288   N N   . SER A 84  ? 0.5838 0.5111 0.6296 0.0275  0.0449  0.1325  84  SER A N   
289   C CA  . SER A 84  ? 0.5783 0.5409 0.6645 0.0389  0.0456  0.1283  84  SER A CA  
290   C C   . SER A 84  ? 0.5831 0.5316 0.6477 0.0603  0.0356  0.1242  84  SER A C   
291   O O   . SER A 84  ? 0.5798 0.5535 0.6767 0.0722  0.0303  0.1206  84  SER A O   
292   C CB  . SER A 84  ? 0.5975 0.5816 0.7114 0.0390  0.0779  0.1283  84  SER A CB  
293   O OG  . SER A 84  ? 0.6293 0.5836 0.6992 0.0509  0.0980  0.1302  84  SER A OG  
294   N N   . TRP A 85  ? 0.6434 0.5525 0.6578 0.0664  0.0320  0.1229  85  TRP A N   
295   C CA  . TRP A 85  ? 0.6256 0.5187 0.6207 0.0849  0.0242  0.1168  85  TRP A CA  
296   C C   . TRP A 85  ? 0.5830 0.4707 0.5812 0.0818  -0.0007 0.1141  85  TRP A C   
297   O O   . TRP A 85  ? 0.5570 0.4261 0.5393 0.0673  -0.0120 0.1122  85  TRP A O   
298   C CB  . TRP A 85  ? 0.6165 0.4707 0.5612 0.0918  0.0283  0.1122  85  TRP A CB  
299   C CG  . TRP A 85  ? 0.6694 0.5194 0.5965 0.1022  0.0524  0.1134  85  TRP A CG  
300   C CD1 . TRP A 85  ? 0.7288 0.5962 0.6717 0.0965  0.0759  0.1200  85  TRP A CD1 
301   C CD2 . TRP A 85  ? 0.6803 0.5039 0.5682 0.1188  0.0580  0.1058  85  TRP A CD2 
302   N NE1 . TRP A 85  ? 0.7723 0.6218 0.6823 0.1080  0.0972  0.1184  85  TRP A NE1 
303   C CE2 . TRP A 85  ? 0.7442 0.5681 0.6196 0.1226  0.0847  0.1097  85  TRP A CE2 
304   C CE3 . TRP A 85  ? 0.6449 0.4438 0.5079 0.1300  0.0446  0.0940  85  TRP A CE3 
305   C CZ2 . TRP A 85  ? 0.7795 0.5791 0.6132 0.1378  0.0961  0.1032  85  TRP A CZ2 
306   C CZ3 . TRP A 85  ? 0.6719 0.4510 0.5007 0.1456  0.0545  0.0860  85  TRP A CZ3 
307   C CH2 . TRP A 85  ? 0.7394 0.5188 0.5514 0.1499  0.0788  0.0911  85  TRP A CH2 
308   N N   . TYR A 86  ? 0.6429 0.5429 0.6592 0.0953  -0.0085 0.1133  86  TYR A N   
309   C CA  . TYR A 86  ? 0.6220 0.5077 0.6301 0.0937  -0.0307 0.1124  86  TYR A CA  
310   C C   . TYR A 86  ? 0.5886 0.4289 0.5527 0.0926  -0.0330 0.1050  86  TYR A C   
311   O O   . TYR A 86  ? 0.5858 0.4092 0.5316 0.1057  -0.0228 0.0991  86  TYR A O   
312   C CB  . TYR A 86  ? 0.6349 0.5338 0.6633 0.1133  -0.0394 0.1136  86  TYR A CB  
313   C CG  . TYR A 86  ? 0.6202 0.4929 0.6268 0.1141  -0.0618 0.1147  86  TYR A CG  
314   C CD1 . TYR A 86  ? 0.6285 0.5148 0.6482 0.1040  -0.0814 0.1182  86  TYR A CD1 
315   C CD2 . TYR A 86  ? 0.6041 0.4346 0.5734 0.1243  -0.0617 0.1114  86  TYR A CD2 
316   C CE1 . TYR A 86  ? 0.6301 0.4840 0.6180 0.1046  -0.1009 0.1201  86  TYR A CE1 
317   C CE2 . TYR A 86  ? 0.6055 0.4025 0.5461 0.1237  -0.0778 0.1133  86  TYR A CE2 
318   C CZ  . TYR A 86  ? 0.6210 0.4276 0.5668 0.1141  -0.0976 0.1185  86  TYR A CZ  
319   O OH  . TYR A 86  ? 0.6269 0.3923 0.5330 0.1134  -0.1128 0.1213  86  TYR A OH  
320   N N   . GLY A 87  ? 0.6047 0.4259 0.5549 0.0759  -0.0452 0.1025  87  GLY A N   
321   C CA  . GLY A 87  ? 0.5772 0.3557 0.4941 0.0724  -0.0464 0.0915  87  GLY A CA  
322   C C   . GLY A 87  ? 0.5560 0.3191 0.4608 0.0639  -0.0403 0.0810  87  GLY A C   
323   O O   . GLY A 87  ? 0.5529 0.2831 0.4383 0.0611  -0.0403 0.0666  87  GLY A O   
324   N N   . VAL A 88  ? 0.5552 0.3378 0.4708 0.0602  -0.0350 0.0861  88  VAL A N   
325   C CA  . VAL A 88  ? 0.5543 0.3190 0.4555 0.0546  -0.0343 0.0772  88  VAL A CA  
326   C C   . VAL A 88  ? 0.5397 0.3144 0.4558 0.0335  -0.0391 0.0820  88  VAL A C   
327   O O   . VAL A 88  ? 0.5325 0.3361 0.4714 0.0268  -0.0366 0.0943  88  VAL A O   
328   C CB  . VAL A 88  ? 0.5717 0.3366 0.4581 0.0713  -0.0232 0.0789  88  VAL A CB  
329   C CG1 . VAL A 88  ? 0.5848 0.3495 0.4654 0.0918  -0.0155 0.0764  88  VAL A CG1 
330   C CG2 . VAL A 88  ? 0.5746 0.3637 0.4734 0.0668  -0.0127 0.0941  88  VAL A CG2 
331   N N   . ALA A 89  ? 0.5434 0.2953 0.4520 0.0227  -0.0460 0.0694  89  ALA A N   
332   C CA  . ALA A 89  ? 0.5288 0.2850 0.4512 0.0035  -0.0502 0.0713  89  ALA A CA  
333   C C   . ALA A 89  ? 0.5298 0.2606 0.4380 0.0067  -0.0558 0.0592  89  ALA A C   
334   O O   . ALA A 89  ? 0.5297 0.2473 0.4317 0.0127  -0.0592 0.0392  89  ALA A O   
335   C CB  . ALA A 89  ? 0.5063 0.2607 0.4421 -0.0178 -0.0574 0.0650  89  ALA A CB  
336   N N   . CYS A 90  ? 0.5291 0.2618 0.4370 0.0032  -0.0546 0.0686  90  CYS A N   
337   C CA  . CYS A 90  ? 0.5466 0.2562 0.4360 0.0116  -0.0622 0.0595  90  CYS A CA  
338   C C   . CYS A 90  ? 0.5274 0.2453 0.4412 -0.0058 -0.0687 0.0483  90  CYS A C   
339   O O   . CYS A 90  ? 0.5048 0.2433 0.4453 -0.0247 -0.0649 0.0496  90  CYS A O   
340   C CB  . CYS A 90  ? 0.5819 0.2829 0.4419 0.0245  -0.0527 0.0780  90  CYS A CB  
341   S SG  . CYS A 90  ? 0.6102 0.3209 0.4490 0.0455  -0.0360 0.0860  90  CYS A SG  
342   N N   . SER A 91  ? 0.5101 0.2141 0.4134 0.0030  -0.0790 0.0356  91  SER A N   
343   C CA  . SER A 91  ? 0.5012 0.2111 0.4233 -0.0073 -0.0856 0.0273  91  SER A CA  
344   C C   . SER A 91  ? 0.5428 0.2241 0.4327 0.0098  -0.0972 0.0297  91  SER A C   
345   O O   . SER A 91  ? 0.5639 0.2308 0.4300 0.0278  -0.1067 0.0191  91  SER A O   
346   C CB  . SER A 91  ? 0.4680 0.2027 0.4210 -0.0147 -0.0866 0.0017  91  SER A CB  
347   O OG  . SER A 91  ? 0.4604 0.2051 0.4322 -0.0212 -0.0899 -0.0049 91  SER A OG  
348   N N   . LEU A 92  ? 0.5058 0.1787 0.3925 0.0045  -0.0956 0.0430  92  LEU A N   
349   C CA  . LEU A 92  ? 0.5572 0.1981 0.4033 0.0210  -0.1035 0.0502  92  LEU A CA  
350   C C   . LEU A 92  ? 0.5959 0.2189 0.3940 0.0398  -0.0952 0.0627  92  LEU A C   
351   O O   . LEU A 92  ? 0.6391 0.2367 0.3966 0.0588  -0.1066 0.0573  92  LEU A O   
352   C CB  . LEU A 92  ? 0.5646 0.1976 0.4142 0.0297  -0.1293 0.0254  92  LEU A CB  
353   C CG  . LEU A 92  ? 0.5257 0.1850 0.4257 0.0126  -0.1338 0.0114  92  LEU A CG  
354   C CD1 . LEU A 92  ? 0.5373 0.1945 0.4438 0.0241  -0.1587 -0.0104 92  LEU A CD1 
355   C CD2 . LEU A 92  ? 0.5299 0.1863 0.4371 -0.0006 -0.1221 0.0297  92  LEU A CD2 
356   N N   . GLY A 93  ? 0.6431 0.2815 0.4460 0.0345  -0.0752 0.0780  93  GLY A N   
357   C CA  . GLY A 93  ? 0.6763 0.3047 0.4396 0.0500  -0.0611 0.0902  93  GLY A CA  
358   C C   . GLY A 93  ? 0.6716 0.3003 0.4257 0.0655  -0.0686 0.0737  93  GLY A C   
359   O O   . GLY A 93  ? 0.6958 0.3196 0.4209 0.0782  -0.0546 0.0826  93  GLY A O   
360   N N   . SER A 94  ? 0.6805 0.3160 0.4609 0.0636  -0.0867 0.0487  94  SER A N   
361   C CA  . SER A 94  ? 0.6756 0.3113 0.4514 0.0768  -0.0920 0.0299  94  SER A CA  
362   C C   . SER A 94  ? 0.6327 0.2925 0.4490 0.0633  -0.0852 0.0232  94  SER A C   
363   O O   . SER A 94  ? 0.5991 0.2746 0.4505 0.0435  -0.0866 0.0191  94  SER A O   
364   C CB  . SER A 94  ? 0.6863 0.3127 0.4592 0.0856  -0.1156 0.0026  94  SER A CB  
365   O OG  . SER A 94  ? 0.6695 0.3089 0.4562 0.0909  -0.1174 -0.0182 94  SER A OG  
366   N N   . ILE A 95  ? 0.6167 0.2786 0.4248 0.0743  -0.0766 0.0217  95  ILE A N   
367   C CA  . ILE A 95  ? 0.5844 0.2632 0.4213 0.0639  -0.0689 0.0181  95  ILE A CA  
368   C C   . ILE A 95  ? 0.5558 0.2482 0.4240 0.0508  -0.0751 -0.0082 95  ILE A C   
369   O O   . ILE A 95  ? 0.5598 0.2549 0.4290 0.0583  -0.0812 -0.0274 95  ILE A O   
370   C CB  . ILE A 95  ? 0.5971 0.2744 0.4183 0.0812  -0.0579 0.0213  95  ILE A CB  
371   C CG1 . ILE A 95  ? 0.5718 0.2609 0.4176 0.0716  -0.0517 0.0174  95  ILE A CG1 
372   C CG2 . ILE A 95  ? 0.6188 0.2852 0.4191 0.0986  -0.0635 0.0019  95  ILE A CG2 
373   C CD1 . ILE A 95  ? 0.5839 0.2739 0.4196 0.0884  -0.0402 0.0241  95  ILE A CD1 
374   N N   . ILE A 96  ? 0.5258 0.2339 0.4221 0.0302  -0.0704 -0.0076 96  ILE A N   
375   C CA  . ILE A 96  ? 0.4973 0.2279 0.4249 0.0165  -0.0633 -0.0274 96  ILE A CA  
376   C C   . ILE A 96  ? 0.4859 0.2216 0.4206 0.0084  -0.0493 -0.0264 96  ILE A C   
377   O O   . ILE A 96  ? 0.4687 0.2203 0.4251 -0.0018 -0.0347 -0.0412 96  ILE A O   
378   C CB  . ILE A 96  ? 0.4782 0.2253 0.4288 0.0010  -0.0636 -0.0308 96  ILE A CB  
379   C CG1 . ILE A 96  ? 0.4690 0.2196 0.4232 -0.0127 -0.0602 -0.0148 96  ILE A CG1 
380   C CG2 . ILE A 96  ? 0.4972 0.2332 0.4377 0.0107  -0.0810 -0.0308 96  ILE A CG2 
381   C CD1 . ILE A 96  ? 0.4461 0.2194 0.4247 -0.0285 -0.0527 -0.0213 96  ILE A CD1 
382   N N   . ARG A 97  ? 0.5524 0.2740 0.4682 0.0136  -0.0504 -0.0079 97  ARG A N   
383   C CA  . ARG A 97  ? 0.5499 0.2708 0.4660 0.0064  -0.0430 -0.0029 97  ARG A CA  
384   C C   . ARG A 97  ? 0.5730 0.2790 0.4671 0.0254  -0.0420 0.0102  97  ARG A C   
385   O O   . ARG A 97  ? 0.5848 0.2900 0.4689 0.0371  -0.0452 0.0286  97  ARG A O   
386   C CB  . ARG A 97  ? 0.5418 0.2703 0.4644 -0.0098 -0.0463 0.0100  97  ARG A CB  
387   C CG  . ARG A 97  ? 0.5395 0.2724 0.4664 -0.0232 -0.0390 0.0049  97  ARG A CG  
388   C CD  . ARG A 97  ? 0.5375 0.2843 0.4736 -0.0395 -0.0427 0.0123  97  ARG A CD  
389   N NE  . ARG A 97  ? 0.5093 0.2791 0.4716 -0.0500 -0.0310 -0.0057 97  ARG A NE  
390   C CZ  . ARG A 97  ? 0.4966 0.2837 0.4721 -0.0617 -0.0290 -0.0055 97  ARG A CZ  
391   N NH1 . ARG A 97  ? 0.5042 0.2900 0.4699 -0.0686 -0.0402 0.0109  97  ARG A NH1 
392   N NH2 . ARG A 97  ? 0.4862 0.2839 0.4788 -0.0684 -0.0225 -0.0207 97  ARG A NH2 
393   N N   . LEU A 98  ? 0.5410 0.2416 0.4322 0.0293  -0.0338 0.0016  98  LEU A N   
394   C CA  . LEU A 98  ? 0.5595 0.2508 0.4347 0.0483  -0.0305 0.0127  98  LEU A CA  
395   C C   . LEU A 98  ? 0.5696 0.2511 0.4385 0.0419  -0.0273 0.0169  98  LEU A C   
396   O O   . LEU A 98  ? 0.5712 0.2477 0.4431 0.0342  -0.0186 0.0019  98  LEU A O   
397   C CB  . LEU A 98  ? 0.5652 0.2561 0.4388 0.0622  -0.0242 -0.0025 98  LEU A CB  
398   C CG  . LEU A 98  ? 0.5846 0.2715 0.4469 0.0828  -0.0178 0.0061  98  LEU A CG  
399   C CD1 . LEU A 98  ? 0.5935 0.2890 0.4493 0.0988  -0.0196 0.0273  98  LEU A CD1 
400   C CD2 . LEU A 98  ? 0.5878 0.2771 0.4529 0.0907  -0.0110 -0.0128 98  LEU A CD2 
401   N N   . ASN A 99  ? 0.5970 0.2793 0.4595 0.0458  -0.0347 0.0381  99  ASN A N   
402   C CA  . ASN A 99  ? 0.6160 0.2856 0.4650 0.0414  -0.0371 0.0449  99  ASN A CA  
403   C C   . ASN A 99  ? 0.6358 0.3089 0.4814 0.0654  -0.0403 0.0602  99  ASN A C   
404   O O   . ASN A 99  ? 0.6346 0.3285 0.4924 0.0751  -0.0506 0.0772  99  ASN A O   
405   C CB  . ASN A 99  ? 0.6116 0.2869 0.4622 0.0240  -0.0482 0.0540  99  ASN A CB  
406   C CG  . ASN A 99  ? 0.6385 0.2934 0.4652 0.0161  -0.0512 0.0558  99  ASN A CG  
407   O OD1 . ASN A 99  ? 0.6615 0.2953 0.4694 0.0222  -0.0430 0.0503  99  ASN A OD1 
408   N ND2 . ASN A 99  ? 0.6406 0.2997 0.4652 0.0022  -0.0632 0.0635  99  ASN A ND2 
409   N N   . LEU A 100 ? 0.4624 0.2817 0.4975 0.1020  -0.0756 -0.0321 100 LEU A N   
410   C CA  . LEU A 100 ? 0.4712 0.2849 0.5150 0.1055  -0.0680 -0.0302 100 LEU A CA  
411   C C   . LEU A 100 ? 0.4712 0.2860 0.5163 0.1045  -0.0743 -0.0309 100 LEU A C   
412   O O   . LEU A 100 ? 0.4790 0.2871 0.5247 0.1066  -0.0685 -0.0303 100 LEU A O   
413   C CB  . LEU A 100 ? 0.4810 0.2840 0.5181 0.1078  -0.0565 -0.0305 100 LEU A CB  
414   C CG  . LEU A 100 ? 0.4848 0.2840 0.5231 0.1099  -0.0474 -0.0289 100 LEU A CG  
415   C CD1 . LEU A 100 ? 0.4967 0.2831 0.5279 0.1113  -0.0359 -0.0303 100 LEU A CD1 
416   C CD2 . LEU A 100 ? 0.4871 0.2881 0.5409 0.1133  -0.0428 -0.0250 100 LEU A CD2 
417   N N   . THR A 101 ? 0.4744 0.2963 0.5199 0.1013  -0.0856 -0.0320 101 THR A N   
418   C CA  . THR A 101 ? 0.4752 0.2978 0.5222 0.1004  -0.0920 -0.0322 101 THR A CA  
419   C C   . THR A 101 ? 0.4817 0.3033 0.5451 0.1039  -0.0886 -0.0283 101 THR A C   
420   O O   . THR A 101 ? 0.4816 0.3064 0.5571 0.1051  -0.0878 -0.0261 101 THR A O   
421   C CB  . THR A 101 ? 0.4680 0.2963 0.5111 0.0963  -0.1039 -0.0344 101 THR A CB  
422   O OG1 . THR A 101 ? 0.4628 0.2919 0.4922 0.0938  -0.1058 -0.0372 101 THR A OG1 
423   C CG2 . THR A 101 ? 0.4702 0.2975 0.5118 0.0953  -0.1104 -0.0347 101 THR A CG2 
424   N N   . ASN A 102 ? 0.4751 0.2923 0.5398 0.1058  -0.0864 -0.0270 102 ASN A N   
425   C CA  . ASN A 102 ? 0.4820 0.2987 0.5625 0.1093  -0.0849 -0.0225 102 ASN A CA  
426   C C   . ASN A 102 ? 0.4888 0.3027 0.5809 0.1141  -0.0740 -0.0191 102 ASN A C   
427   O O   . ASN A 102 ? 0.4910 0.3087 0.5988 0.1160  -0.0759 -0.0154 102 ASN A O   
428   C CB  . ASN A 102 ? 0.4775 0.3015 0.5651 0.1065  -0.0979 -0.0219 102 ASN A CB  
429   C CG  . ASN A 102 ? 0.4849 0.3084 0.5856 0.1094  -0.0995 -0.0171 102 ASN A CG  
430   O OD1 . ASN A 102 ? 0.4924 0.3099 0.5932 0.1129  -0.0922 -0.0151 102 ASN A OD1 
431   N ND2 . ASN A 102 ? 0.4840 0.3132 0.5960 0.1079  -0.1090 -0.0151 102 ASN A ND2 
432   N N   . THR A 103 ? 0.5097 0.3161 0.5937 0.1159  -0.0627 -0.0202 103 THR A N   
433   C CA  . THR A 103 ? 0.5191 0.3194 0.6097 0.1209  -0.0504 -0.0174 103 THR A CA  
434   C C   . THR A 103 ? 0.5351 0.3230 0.6266 0.1267  -0.0379 -0.0150 103 THR A C   
435   O O   . THR A 103 ? 0.5472 0.3269 0.6411 0.1322  -0.0270 -0.0129 103 THR A O   
436   C CB  . THR A 103 ? 0.5174 0.3145 0.5969 0.1197  -0.0445 -0.0199 103 THR A CB  
437   O OG1 . THR A 103 ? 0.5038 0.3107 0.5785 0.1144  -0.0562 -0.0227 103 THR A OG1 
438   C CG2 . THR A 103 ? 0.5252 0.3182 0.6115 0.1244  -0.0348 -0.0170 103 THR A CG2 
439   N N   . GLY A 104 ? 0.5621 0.3470 0.6502 0.1262  -0.0393 -0.0155 104 GLY A N   
440   C CA  . GLY A 104 ? 0.5839 0.3550 0.6711 0.1320  -0.0269 -0.0135 104 GLY A CA  
441   C C   . GLY A 104 ? 0.5922 0.3468 0.6647 0.1336  -0.0113 -0.0163 104 GLY A C   
442   O O   . GLY A 104 ? 0.6127 0.3512 0.6797 0.1404  0.0008  -0.0150 104 GLY A O   
443   N N   . ILE A 105 ? 0.5882 0.3450 0.6518 0.1278  -0.0125 -0.0207 105 ILE A N   
444   C CA  . ILE A 105 ? 0.5985 0.3405 0.6513 0.1271  0.0016  -0.0242 105 ILE A CA  
445   C C   . ILE A 105 ? 0.6066 0.3384 0.6540 0.1251  0.0072  -0.0276 105 ILE A C   
446   O O   . ILE A 105 ? 0.5982 0.3378 0.6442 0.1215  -0.0041 -0.0292 105 ILE A O   
447   C CB  . ILE A 105 ? 0.5855 0.3352 0.6324 0.1212  -0.0049 -0.0283 105 ILE A CB  
448   C CG1 . ILE A 105 ? 0.5857 0.3432 0.6387 0.1234  -0.0074 -0.0249 105 ILE A CG1 
449   C CG2 . ILE A 105 ? 0.5949 0.3320 0.6348 0.1183  0.0064  -0.0338 105 ILE A CG2 
450   C CD1 . ILE A 105 ? 0.5664 0.3349 0.6137 0.1184  -0.0185 -0.0274 105 ILE A CD1 
451   N N   . GLU A 106 ? 0.6428 0.3620 0.6858 0.1247  0.0226  -0.0293 106 GLU A N   
452   C CA  . GLU A 106 ? 0.6510 0.3624 0.6928 0.1204  0.0292  -0.0339 106 GLU A CA  
453   C C   . GLU A 106 ? 0.6508 0.3611 0.6990 0.1119  0.0342  -0.0442 106 GLU A C   
454   O O   . GLU A 106 ? 0.6536 0.3668 0.7200 0.1096  0.0415  -0.0474 106 GLU A O   
455   C CB  . GLU A 106 ? 0.6773 0.3737 0.7052 0.1286  0.0387  -0.0286 106 GLU A CB  
456   C CG  . GLU A 106 ? 0.6844 0.3742 0.7119 0.1257  0.0433  -0.0311 106 GLU A CG  
457   C CD  . GLU A 106 ? 0.7351 0.3905 0.7034 0.1436  0.0261  -0.0365 106 GLU A CD  
458   O OE1 . GLU A 106 ? 0.7324 0.3964 0.7285 0.1425  -0.0139 -0.0617 106 GLU A OE1 
459   O OE2 . GLU A 106 ? 0.7358 0.3950 0.7216 0.1496  0.0177  -0.0346 106 GLU A OE2 
460   N N   . GLY A 107 ? 0.5966 0.3045 0.6336 0.1077  0.0254  -0.0518 107 GLY A N   
461   C CA  . GLY A 107 ? 0.6025 0.3045 0.6326 0.1025  0.0246  -0.0632 107 GLY A CA  
462   C C   . GLY A 107 ? 0.6032 0.3009 0.6059 0.0997  0.0131  -0.0673 107 GLY A C   
463   O O   . GLY A 107 ? 0.5958 0.2983 0.5964 0.0991  0.0083  -0.0640 107 GLY A O   
464   N N   . THR A 108 ? 0.6025 0.2927 0.5809 0.0978  0.0069  -0.0736 108 THR A N   
465   C CA  . THR A 108 ? 0.6064 0.2937 0.5561 0.0944  -0.0056 -0.0768 108 THR A CA  
466   C C   . THR A 108 ? 0.6035 0.2939 0.5363 0.0952  -0.0161 -0.0752 108 THR A C   
467   O O   . THR A 108 ? 0.6035 0.2945 0.5425 0.0979  -0.0120 -0.0735 108 THR A O   
468   C CB  . THR A 108 ? 0.6333 0.3014 0.5625 0.0903  -0.0019 -0.0872 108 THR A CB  
469   O OG1 . THR A 108 ? 0.6550 0.3090 0.5627 0.0899  0.0000  -0.0928 108 THR A OG1 
470   C CG2 . THR A 108 ? 0.6398 0.3032 0.5909 0.0905  0.0105  -0.0907 108 THR A CG2 
471   N N   . PHE A 109 ? 0.6048 0.2970 0.5180 0.0930  -0.0297 -0.0756 109 PHE A N   
472   C CA  . PHE A 109 ? 0.6047 0.2980 0.5009 0.0938  -0.0409 -0.0745 109 PHE A CA  
473   C C   . PHE A 109 ? 0.6351 0.3067 0.4981 0.0911  -0.0424 -0.0818 109 PHE A C   
474   O O   . PHE A 109 ? 0.6392 0.3085 0.4829 0.0909  -0.0544 -0.0812 109 PHE A O   
475   C CB  . PHE A 109 ? 0.5852 0.2934 0.4814 0.0931  -0.0557 -0.0701 109 PHE A CB  
476   C CG  . PHE A 109 ? 0.5589 0.2870 0.4807 0.0945  -0.0556 -0.0633 109 PHE A CG  
477   C CD1 . PHE A 109 ? 0.5488 0.2850 0.4884 0.0971  -0.0493 -0.0587 109 PHE A CD1 
478   C CD2 . PHE A 109 ? 0.5466 0.2838 0.4725 0.0927  -0.0618 -0.0614 109 PHE A CD2 
479   C CE1 . PHE A 109 ? 0.5287 0.2808 0.4873 0.0975  -0.0499 -0.0529 109 PHE A CE1 
480   C CE2 . PHE A 109 ? 0.5267 0.2795 0.4710 0.0933  -0.0622 -0.0558 109 PHE A CE2 
481   C CZ  . PHE A 109 ? 0.5192 0.2787 0.4783 0.0957  -0.0571 -0.0518 109 PHE A CZ  
482   N N   . GLU A 110 ? 0.7184 0.3732 0.5734 0.0885  -0.0304 -0.0889 110 GLU A N   
483   C CA  . GLU A 110 ? 0.7522 0.3843 0.5702 0.0839  -0.0308 -0.0964 110 GLU A CA  
484   C C   . GLU A 110 ? 0.7660 0.3887 0.5686 0.0866  -0.0293 -0.0959 110 GLU A C   
485   O O   . GLU A 110 ? 0.7878 0.3969 0.5572 0.0835  -0.0373 -0.0982 110 GLU A O   
486   C CB  . GLU A 110 ? 0.7751 0.3923 0.5886 0.0795  -0.0172 -0.1047 110 GLU A CB  
487   C CG  . GLU A 110 ? 0.8138 0.4076 0.5855 0.0718  -0.0171 -0.1130 110 GLU A CG  
488   C CD  . GLU A 110 ? 0.8423 0.4246 0.6104 0.0661  -0.0063 -0.1212 110 GLU A CD  
489   O OE1 . GLU A 110 ? 0.8504 0.4261 0.6293 0.0684  0.0085  -0.1241 110 GLU A OE1 
490   O OE2 . GLU A 110 ? 0.8482 0.4285 0.6041 0.0596  -0.0129 -0.1244 110 GLU A OE2 
491   N N   . ASP A 111 ? 0.7350 0.3645 0.5614 0.0919  -0.0194 -0.0925 111 ASP A N   
492   C CA  . ASP A 111 ? 0.7455 0.3677 0.5615 0.0954  -0.0168 -0.0910 111 ASP A CA  
493   C C   . ASP A 111 ? 0.7156 0.3586 0.5527 0.1006  -0.0255 -0.0820 111 ASP A C   
494   O O   . ASP A 111 ? 0.7124 0.3582 0.5610 0.1047  -0.0194 -0.0787 111 ASP A O   
495   C CB  . ASP A 111 ? 0.7614 0.3755 0.5890 0.0973  0.0012  -0.0938 111 ASP A CB  
496   C CG  . ASP A 111 ? 0.7992 0.3860 0.5912 0.0918  0.0107  -0.1029 111 ASP A CG  
497   O OD1 . ASP A 111 ? 0.8247 0.3965 0.5776 0.0864  0.0032  -0.1063 111 ASP A OD1 
498   O OD2 . ASP A 111 ? 0.8166 0.3971 0.6194 0.0924  0.0252  -0.1065 111 ASP A OD2 
499   N N   . PHE A 112 ? 0.6622 0.3201 0.5049 0.0999  -0.0392 -0.0781 112 PHE A N   
500   C CA  . PHE A 112 ? 0.6362 0.3136 0.4953 0.1034  -0.0479 -0.0703 112 PHE A CA  
501   C C   . PHE A 112 ? 0.6517 0.3180 0.4841 0.1053  -0.0570 -0.0697 112 PHE A C   
502   O O   . PHE A 112 ? 0.6723 0.3233 0.4744 0.1025  -0.0660 -0.0736 112 PHE A O   
503   C CB  . PHE A 112 ? 0.6120 0.3074 0.4837 0.1015  -0.0584 -0.0670 112 PHE A CB  
504   C CG  . PHE A 112 ? 0.5840 0.3014 0.4768 0.1034  -0.0637 -0.0597 112 PHE A CG  
505   C CD1 . PHE A 112 ? 0.5657 0.2972 0.4867 0.1041  -0.0550 -0.0554 112 PHE A CD1 
506   C CD2 . PHE A 112 ? 0.5781 0.3009 0.4621 0.1039  -0.0768 -0.0571 112 PHE A CD2 
507   C CE1 . PHE A 112 ? 0.5434 0.2931 0.4802 0.1042  -0.0589 -0.0495 112 PHE A CE1 
508   C CE2 . PHE A 112 ? 0.5540 0.2965 0.4571 0.1043  -0.0795 -0.0513 112 PHE A CE2 
509   C CZ  . PHE A 112 ? 0.5374 0.2928 0.4653 0.1040  -0.0704 -0.0479 112 PHE A CZ  
510   N N   . PRO A 113 ? 0.6403 0.3126 0.4826 0.1097  -0.0550 -0.0648 113 PRO A N   
511   C CA  . PRO A 113 ? 0.6593 0.3176 0.4747 0.1125  -0.0621 -0.0636 113 PRO A CA  
512   C C   . PRO A 113 ? 0.6465 0.3148 0.4597 0.1129  -0.0795 -0.0593 113 PRO A C   
513   O O   . PRO A 113 ? 0.6279 0.3116 0.4574 0.1160  -0.0830 -0.0526 113 PRO A O   
514   C CB  . PRO A 113 ? 0.6514 0.3164 0.4860 0.1170  -0.0517 -0.0589 113 PRO A CB  
515   C CG  . PRO A 113 ? 0.6167 0.3085 0.4928 0.1157  -0.0474 -0.0551 113 PRO A CG  
516   C CD  . PRO A 113 ? 0.6157 0.3071 0.4943 0.1117  -0.0459 -0.0596 113 PRO A CD  
517   N N   . PHE A 114 ? 0.6493 0.3092 0.4437 0.1090  -0.0898 -0.0632 114 PHE A N   
518   C CA  . PHE A 114 ? 0.6391 0.3071 0.4327 0.1093  -0.1064 -0.0593 114 PHE A CA  
519   C C   . PHE A 114 ? 0.6549 0.3110 0.4304 0.1136  -0.1146 -0.0547 114 PHE A C   
520   O O   . PHE A 114 ? 0.6342 0.3084 0.4277 0.1164  -0.1210 -0.0469 114 PHE A O   
521   C CB  . PHE A 114 ? 0.6523 0.3100 0.4272 0.1034  -0.1156 -0.0648 114 PHE A CB  
522   C CG  . PHE A 114 ? 0.6364 0.3061 0.4301 0.1000  -0.1083 -0.0673 114 PHE A CG  
523   C CD1 . PHE A 114 ? 0.6050 0.2986 0.4256 0.1002  -0.1117 -0.0629 114 PHE A CD1 
524   C CD2 . PHE A 114 ? 0.6551 0.3111 0.4379 0.0959  -0.0974 -0.0740 114 PHE A CD2 
525   C CE1 . PHE A 114 ? 0.5933 0.2953 0.4283 0.0973  -0.1055 -0.0645 114 PHE A CE1 
526   C CE2 . PHE A 114 ? 0.6417 0.3074 0.4427 0.0935  -0.0907 -0.0754 114 PHE A CE2 
527   C CZ  . PHE A 114 ? 0.6111 0.2993 0.4375 0.0945  -0.0954 -0.0703 114 PHE A CZ  
528   N N   . SER A 115 ? 0.7082 0.3408 0.4498 0.1110  -0.1121 -0.0582 115 SER A N   
529   C CA  . SER A 115 ? 0.7176 0.3588 0.4470 0.1081  -0.1167 -0.0487 115 SER A CA  
530   C C   . SER A 115 ? 0.7058 0.3520 0.4536 0.1175  -0.1092 -0.0419 115 SER A C   
531   O O   . SER A 115 ? 0.7097 0.3672 0.4569 0.1176  -0.1142 -0.0318 115 SER A O   
532   C CB  . SER A 115 ? 0.7557 0.3821 0.4460 0.0978  -0.1128 -0.0524 115 SER A CB  
533   O OG  . SER A 115 ? 0.7741 0.3792 0.4550 0.0982  -0.0972 -0.0629 115 SER A OG  
534   N N   . SER A 116 ? 0.6786 0.3182 0.4445 0.1248  -0.0971 -0.0464 116 SER A N   
535   C CA  . SER A 116 ? 0.6676 0.3179 0.4529 0.1295  -0.0866 -0.0403 116 SER A CA  
536   C C   . SER A 116 ? 0.6256 0.3116 0.4534 0.1288  -0.0869 -0.0338 116 SER A C   
537   O O   . SER A 116 ? 0.6156 0.3117 0.4606 0.1314  -0.0796 -0.0284 116 SER A O   
538   C CB  . SER A 116 ? 0.6747 0.3184 0.4649 0.1288  -0.0682 -0.0458 116 SER A CB  
539   O OG  . SER A 116 ? 0.7108 0.3249 0.4642 0.1255  -0.0646 -0.0546 116 SER A OG  
540   N N   . LEU A 117 ? 0.6197 0.3231 0.4626 0.1244  -0.0939 -0.0347 117 LEU A N   
541   C CA  . LEU A 117 ? 0.5841 0.3170 0.4620 0.1214  -0.0913 -0.0307 117 LEU A CA  
542   C C   . LEU A 117 ? 0.5738 0.3174 0.4529 0.1194  -0.1032 -0.0271 117 LEU A C   
543   O O   . LEU A 117 ? 0.5580 0.3128 0.4466 0.1150  -0.1064 -0.0293 117 LEU A O   
544   C CB  . LEU A 117 ? 0.5669 0.3106 0.4636 0.1170  -0.0845 -0.0348 117 LEU A CB  
545   C CG  . LEU A 117 ? 0.5784 0.3113 0.4757 0.1179  -0.0724 -0.0386 117 LEU A CG  
546   C CD1 . LEU A 117 ? 0.5598 0.3058 0.4789 0.1138  -0.0669 -0.0400 117 LEU A CD1 
547   C CD2 . LEU A 117 ? 0.5804 0.3129 0.4877 0.1214  -0.0625 -0.0348 117 LEU A CD2 
548   N N   . PRO A 118 ? 0.5940 0.3351 0.4648 0.1225  -0.1090 -0.0203 118 PRO A N   
549   C CA  . PRO A 118 ? 0.5844 0.3377 0.4600 0.1198  -0.1186 -0.0156 118 PRO A CA  
550   C C   . PRO A 118 ? 0.5529 0.3306 0.4586 0.1154  -0.1123 -0.0140 118 PRO A C   
551   O O   . PRO A 118 ? 0.5430 0.3290 0.4535 0.1117  -0.1174 -0.0142 118 PRO A O   
552   C CB  . PRO A 118 ? 0.6002 0.3493 0.4649 0.1237  -0.1230 -0.0058 118 PRO A CB  
553   C CG  . PRO A 118 ? 0.6049 0.3484 0.4722 0.1281  -0.1116 -0.0050 118 PRO A CG  
554   C CD  . PRO A 118 ? 0.6108 0.3416 0.4722 0.1280  -0.1050 -0.0150 118 PRO A CD  
555   N N   . ASN A 119 ? 0.5762 0.3633 0.5007 0.1155  -0.1010 -0.0123 119 ASN A N   
556   C CA  . ASN A 119 ? 0.5528 0.3582 0.5003 0.1118  -0.0952 -0.0092 119 ASN A CA  
557   C C   . ASN A 119 ? 0.5380 0.3506 0.4955 0.1071  -0.0916 -0.0146 119 ASN A C   
558   O O   . ASN A 119 ? 0.5272 0.3509 0.5005 0.1045  -0.0856 -0.0126 119 ASN A O   
559   C CB  . ASN A 119 ? 0.5542 0.3645 0.5156 0.1142  -0.0858 -0.0035 119 ASN A CB  
560   C CG  . ASN A 119 ? 0.5619 0.3684 0.5163 0.1187  -0.0889 0.0043  119 ASN A CG  
561   O OD1 . ASN A 119 ? 0.5674 0.3745 0.5139 0.1187  -0.0973 0.0080  119 ASN A OD1 
562   N ND2 . ASN A 119 ? 0.5683 0.3718 0.5270 0.1224  -0.0817 0.0081  119 ASN A ND2 
563   N N   . LEU A 120 ? 0.4924 0.2976 0.4397 0.1062  -0.0952 -0.0206 120 LEU A N   
564   C CA  . LEU A 120 ? 0.4792 0.2914 0.4357 0.1021  -0.0922 -0.0241 120 LEU A CA  
565   C C   . LEU A 120 ? 0.4670 0.2883 0.4276 0.0982  -0.0961 -0.0238 120 LEU A C   
566   O O   . LEU A 120 ? 0.4723 0.2904 0.4234 0.0978  -0.1037 -0.0245 120 LEU A O   
567   C CB  . LEU A 120 ? 0.4895 0.2917 0.4352 0.1024  -0.0942 -0.0295 120 LEU A CB  
568   C CG  . LEU A 120 ? 0.5003 0.2934 0.4455 0.1054  -0.0866 -0.0307 120 LEU A CG  
569   C CD1 . LEU A 120 ? 0.5097 0.2935 0.4461 0.1049  -0.0869 -0.0358 120 LEU A CD1 
570   C CD2 . LEU A 120 ? 0.4869 0.2902 0.4530 0.1045  -0.0768 -0.0277 120 LEU A CD2 
571   N N   . THR A 121 ? 0.4319 0.2623 0.4051 0.0956  -0.0916 -0.0231 121 THR A N   
572   C CA  . THR A 121 ? 0.4259 0.2607 0.4004 0.0928  -0.0963 -0.0246 121 THR A CA  
573   C C   . THR A 121 ? 0.4233 0.2588 0.3989 0.0906  -0.0992 -0.0294 121 THR A C   
574   O O   . THR A 121 ? 0.4207 0.2573 0.3934 0.0884  -0.1036 -0.0314 121 THR A O   
575   C CB  . THR A 121 ? 0.4218 0.2615 0.4055 0.0933  -0.0934 -0.0208 121 THR A CB  
576   O OG1 . THR A 121 ? 0.4195 0.2607 0.4110 0.0930  -0.0912 -0.0226 121 THR A OG1 
577   C CG2 . THR A 121 ? 0.4250 0.2649 0.4108 0.0964  -0.0891 -0.0145 121 THR A CG2 
578   N N   . PHE A 122 ? 0.4627 0.2973 0.4431 0.0916  -0.0965 -0.0307 122 PHE A N   
579   C CA  . PHE A 122 ? 0.4615 0.2967 0.4442 0.0900  -0.0995 -0.0341 122 PHE A CA  
580   C C   . PHE A 122 ? 0.4672 0.2977 0.4486 0.0916  -0.0968 -0.0351 122 PHE A C   
581   O O   . PHE A 122 ? 0.4708 0.2992 0.4573 0.0941  -0.0907 -0.0334 122 PHE A O   
582   C CB  . PHE A 122 ? 0.4585 0.2971 0.4516 0.0897  -0.0988 -0.0339 122 PHE A CB  
583   C CG  . PHE A 122 ? 0.4606 0.2995 0.4569 0.0884  -0.1027 -0.0366 122 PHE A CG  
584   C CD1 . PHE A 122 ? 0.4564 0.2963 0.4493 0.0859  -0.1087 -0.0388 122 PHE A CD1 
585   C CD2 . PHE A 122 ? 0.4634 0.3010 0.4667 0.0901  -0.0998 -0.0364 122 PHE A CD2 
586   C CE1 . PHE A 122 ? 0.4574 0.2969 0.4530 0.0850  -0.1129 -0.0408 122 PHE A CE1 
587   C CE2 . PHE A 122 ? 0.4637 0.3015 0.4713 0.0893  -0.1037 -0.0380 122 PHE A CE2 
588   C CZ  . PHE A 122 ? 0.4639 0.3028 0.4673 0.0866  -0.1107 -0.0402 122 PHE A CZ  
589   N N   . VAL A 123 ? 0.4268 0.2550 0.4022 0.0905  -0.1002 -0.0376 123 VAL A N   
590   C CA  . VAL A 123 ? 0.4335 0.2560 0.4082 0.0921  -0.0966 -0.0385 123 VAL A CA  
591   C C   . VAL A 123 ? 0.4324 0.2562 0.4098 0.0908  -0.1005 -0.0405 123 VAL A C   
592   O O   . VAL A 123 ? 0.4306 0.2549 0.4014 0.0888  -0.1058 -0.0420 123 VAL A O   
593   C CB  . VAL A 123 ? 0.4400 0.2555 0.4030 0.0924  -0.0956 -0.0392 123 VAL A CB  
594   C CG1 . VAL A 123 ? 0.4480 0.2564 0.4098 0.0934  -0.0916 -0.0411 123 VAL A CG1 
595   C CG2 . VAL A 123 ? 0.4439 0.2561 0.4043 0.0944  -0.0910 -0.0369 123 VAL A CG2 
596   N N   . ASP A 124 ? 0.4481 0.2720 0.4358 0.0922  -0.0976 -0.0399 124 ASP A N   
597   C CA  . ASP A 124 ? 0.4488 0.2730 0.4404 0.0917  -0.1009 -0.0408 124 ASP A CA  
598   C C   . ASP A 124 ? 0.4566 0.2753 0.4550 0.0947  -0.0932 -0.0397 124 ASP A C   
599   O O   . ASP A 124 ? 0.4581 0.2774 0.4678 0.0967  -0.0886 -0.0377 124 ASP A O   
600   C CB  . ASP A 124 ? 0.4440 0.2737 0.4433 0.0902  -0.1061 -0.0408 124 ASP A CB  
601   C CG  . ASP A 124 ? 0.4451 0.2746 0.4457 0.0892  -0.1115 -0.0417 124 ASP A CG  
602   O OD1 . ASP A 124 ? 0.4498 0.2753 0.4485 0.0903  -0.1096 -0.0418 124 ASP A OD1 
603   O OD2 . ASP A 124 ? 0.4425 0.2747 0.4457 0.0874  -0.1173 -0.0424 124 ASP A OD2 
604   N N   . LEU A 125 ? 0.4377 0.2503 0.4299 0.0951  -0.0910 -0.0409 125 LEU A N   
605   C CA  . LEU A 125 ? 0.4473 0.2523 0.4454 0.0979  -0.0819 -0.0400 125 LEU A CA  
606   C C   . LEU A 125 ? 0.4496 0.2536 0.4511 0.0980  -0.0842 -0.0400 125 LEU A C   
607   O O   . LEU A 125 ? 0.4583 0.2542 0.4590 0.0994  -0.0777 -0.0404 125 LEU A O   
608   C CB  . LEU A 125 ? 0.4558 0.2513 0.4438 0.0984  -0.0750 -0.0418 125 LEU A CB  
609   C CG  . LEU A 125 ? 0.4552 0.2503 0.4382 0.0985  -0.0730 -0.0415 125 LEU A CG  
610   C CD1 . LEU A 125 ? 0.4654 0.2496 0.4355 0.0980  -0.0682 -0.0440 125 LEU A CD1 
611   C CD2 . LEU A 125 ? 0.4565 0.2522 0.4524 0.1012  -0.0657 -0.0387 125 LEU A CD2 
612   N N   . SER A 126 ? 0.4681 0.2791 0.4732 0.0965  -0.0928 -0.0397 126 SER A N   
613   C CA  . SER A 126 ? 0.4704 0.2803 0.4772 0.0963  -0.0963 -0.0394 126 SER A CA  
614   C C   . SER A 126 ? 0.4761 0.2846 0.4984 0.0996  -0.0918 -0.0360 126 SER A C   
615   O O   . SER A 126 ? 0.4765 0.2867 0.5091 0.1015  -0.0881 -0.0339 126 SER A O   
616   C CB  . SER A 126 ? 0.4633 0.2792 0.4655 0.0931  -0.1072 -0.0407 126 SER A CB  
617   O OG  . SER A 126 ? 0.4592 0.2804 0.4694 0.0925  -0.1109 -0.0399 126 SER A OG  
618   N N   . MET A 127 ? 0.4915 0.2964 0.5161 0.1007  -0.0916 -0.0349 127 MET A N   
619   C CA  . MET A 127 ? 0.4980 0.3015 0.5379 0.1043  -0.0882 -0.0306 127 MET A CA  
620   C C   . MET A 127 ? 0.5066 0.3036 0.5549 0.1086  -0.0747 -0.0283 127 MET A C   
621   O O   . MET A 127 ? 0.5083 0.3075 0.5696 0.1114  -0.0722 -0.0249 127 MET A O   
622   C CB  . MET A 127 ? 0.4930 0.3044 0.5420 0.1033  -0.0975 -0.0289 127 MET A CB  
623   C CG  . MET A 127 ? 0.4870 0.3021 0.5262 0.0990  -0.1094 -0.0315 127 MET A CG  
624   S SD  . MET A 127 ? 0.4868 0.3068 0.5375 0.0980  -0.1195 -0.0291 127 MET A SD  
625   C CE  . MET A 127 ? 0.4974 0.3142 0.5640 0.1032  -0.1145 -0.0228 127 MET A CE  
626   N N   . ASN A 128 ? 0.5295 0.3171 0.5696 0.1092  -0.0656 -0.0304 128 ASN A N   
627   C CA  . ASN A 128 ? 0.5411 0.3186 0.5859 0.1130  -0.0505 -0.0291 128 ASN A CA  
628   C C   . ASN A 128 ? 0.5530 0.3180 0.5932 0.1138  -0.0413 -0.0305 128 ASN A C   
629   O O   . ASN A 128 ? 0.5551 0.3208 0.5916 0.1123  -0.0469 -0.0313 128 ASN A O   
630   C CB  . ASN A 128 ? 0.5389 0.3156 0.5767 0.1115  -0.0472 -0.0317 128 ASN A CB  
631   C CG  . ASN A 128 ? 0.5305 0.3170 0.5759 0.1118  -0.0524 -0.0295 128 ASN A CG  
632   O OD1 . ASN A 128 ? 0.5366 0.3222 0.5944 0.1158  -0.0464 -0.0257 128 ASN A OD1 
633   N ND2 . ASN A 128 ? 0.5189 0.3140 0.5565 0.1078  -0.0631 -0.0319 128 ASN A ND2 
634   N N   . ARG A 129 ? 0.5719 0.3240 0.6121 0.1161  -0.0260 -0.0313 129 ARG A N   
635   C CA  . ARG A 129 ? 0.5864 0.3237 0.6236 0.1165  -0.0142 -0.0334 129 ARG A CA  
636   C C   . ARG A 129 ? 0.5921 0.3216 0.6173 0.1115  -0.0094 -0.0408 129 ARG A C   
637   O O   . ARG A 129 ? 0.6051 0.3203 0.6322 0.1113  0.0054  -0.0441 129 ARG A O   
638   C CB  . ARG A 129 ? 0.6042 0.3287 0.6502 0.1237  0.0016  -0.0284 129 ARG A CB  
639   C CG  . ARG A 129 ? 0.6031 0.3350 0.6597 0.1293  -0.0055 -0.0213 129 ARG A CG  
640   C CD  . ARG A 129 ? 0.6288 0.3436 0.6839 0.1384  0.0072  -0.0171 129 ARG A CD  
641   N NE  . ARG A 129 ? 0.6523 0.3527 0.6935 0.1355  0.0199  -0.0215 129 ARG A NE  
642   C CZ  . ARG A 129 ? 0.6563 0.3507 0.6949 0.1350  0.0219  -0.0219 129 ARG A CZ  
643   N NH1 . ARG A 129 ? 0.6425 0.3438 0.6910 0.1375  0.0122  -0.0178 129 ARG A NH1 
644   N NH2 . ARG A 129 ? 0.6667 0.3471 0.6920 0.1315  0.0344  -0.0266 129 ARG A NH2 
645   N N   . PHE A 130 ? 0.5353 0.2739 0.5482 0.1073  -0.0222 -0.0438 130 PHE A N   
646   C CA  . PHE A 130 ? 0.5399 0.2719 0.5377 0.1028  -0.0212 -0.0505 130 PHE A CA  
647   C C   . PHE A 130 ? 0.5470 0.2716 0.5361 0.0997  -0.0211 -0.0549 130 PHE A C   
648   O O   . PHE A 130 ? 0.5394 0.2707 0.5263 0.0993  -0.0307 -0.0530 130 PHE A O   
649   C CB  . PHE A 130 ? 0.5265 0.2696 0.5132 0.1006  -0.0345 -0.0507 130 PHE A CB  
650   C CG  . PHE A 130 ? 0.5221 0.2699 0.5152 0.1026  -0.0328 -0.0480 130 PHE A CG  
651   C CD1 . PHE A 130 ? 0.5329 0.2707 0.5260 0.1028  -0.0213 -0.0505 130 PHE A CD1 
652   C CD2 . PHE A 130 ? 0.5082 0.2699 0.5076 0.1038  -0.0425 -0.0438 130 PHE A CD2 
653   C CE1 . PHE A 130 ? 0.5294 0.2710 0.5289 0.1049  -0.0190 -0.0477 130 PHE A CE1 
654   C CE2 . PHE A 130 ? 0.5049 0.2704 0.5106 0.1055  -0.0403 -0.0415 130 PHE A CE2 
655   C CZ  . PHE A 130 ? 0.5153 0.2708 0.5210 0.1065  -0.0283 -0.0428 130 PHE A CZ  
656   N N   . SER A 131 ? 0.5521 0.2627 0.5372 0.0969  -0.0102 -0.0614 131 SER A N   
657   C CA  . SER A 131 ? 0.5615 0.2635 0.5383 0.0930  -0.0088 -0.0670 131 SER A CA  
658   C C   . SER A 131 ? 0.5731 0.2666 0.5271 0.0882  -0.0129 -0.0753 131 SER A C   
659   O O   . SER A 131 ? 0.5802 0.2694 0.5269 0.0886  -0.0122 -0.0778 131 SER A O   
660   C CB  . SER A 131 ? 0.5761 0.2662 0.5691 0.0941  0.0067  -0.0693 131 SER A CB  
661   O OG  . SER A 131 ? 0.5856 0.2691 0.5890 0.0939  0.0173  -0.0743 131 SER A OG  
662   N N   . GLY A 132 ? 0.5584 0.2472 0.4980 0.0844  -0.0184 -0.0793 132 GLY A N   
663   C CA  . GLY A 132 ? 0.5744 0.2528 0.4872 0.0801  -0.0250 -0.0865 132 GLY A CA  
664   C C   . GLY A 132 ? 0.5630 0.2504 0.4643 0.0786  -0.0406 -0.0836 132 GLY A C   
665   O O   . GLY A 132 ? 0.5484 0.2457 0.4600 0.0793  -0.0441 -0.0791 132 GLY A O   
666   N N   . THR A 133 ? 0.5584 0.2415 0.4388 0.0766  -0.0501 -0.0861 133 THR A N   
667   C CA  . THR A 133 ? 0.5507 0.2404 0.4209 0.0751  -0.0651 -0.0840 133 THR A CA  
668   C C   . THR A 133 ? 0.5376 0.2377 0.4070 0.0786  -0.0753 -0.0790 133 THR A C   
669   O O   . THR A 133 ? 0.5380 0.2378 0.4103 0.0814  -0.0710 -0.0781 133 THR A O   
670   C CB  . THR A 133 ? 0.5749 0.2490 0.4207 0.0686  -0.0686 -0.0914 133 THR A CB  
671   O OG1 . THR A 133 ? 0.5970 0.2569 0.4243 0.0666  -0.0655 -0.0965 133 THR A OG1 
672   C CG2 . THR A 133 ? 0.5860 0.2517 0.4345 0.0645  -0.0589 -0.0965 133 THR A CG2 
673   N N   . ILE A 134 ? 0.5407 0.2497 0.4076 0.0785  -0.0883 -0.0758 134 ILE A N   
674   C CA  . ILE A 134 ? 0.5292 0.2476 0.3956 0.0813  -0.0986 -0.0715 134 ILE A CA  
675   C C   . ILE A 134 ? 0.5501 0.2543 0.3926 0.0790  -0.1070 -0.0751 134 ILE A C   
676   O O   . ILE A 134 ? 0.5571 0.2571 0.3897 0.0754  -0.1152 -0.0765 134 ILE A O   
677   C CB  . ILE A 134 ? 0.5067 0.2420 0.3850 0.0821  -0.1068 -0.0663 134 ILE A CB  
678   C CG1 . ILE A 134 ? 0.4893 0.2371 0.3877 0.0834  -0.0993 -0.0627 134 ILE A CG1 
679   C CG2 . ILE A 134 ? 0.4978 0.2410 0.3749 0.0842  -0.1167 -0.0629 134 ILE A CG2 
680   C CD1 . ILE A 134 ? 0.4735 0.2333 0.3793 0.0825  -0.1048 -0.0594 134 ILE A CD1 
681   N N   . SER A 135 ? 0.5682 0.2641 0.4007 0.0804  -0.1050 -0.0764 135 SER A N   
682   C CA  . SER A 135 ? 0.5931 0.2727 0.3986 0.0771  -0.1126 -0.0801 135 SER A CA  
683   C C   . SER A 135 ? 0.5848 0.2710 0.3886 0.0784  -0.1292 -0.0755 135 SER A C   
684   O O   . SER A 135 ? 0.5606 0.2634 0.3828 0.0834  -0.1326 -0.0696 135 SER A O   
685   C CB  . SER A 135 ? 0.6077 0.2767 0.4025 0.0791  -0.1062 -0.0818 135 SER A CB  
686   O OG  . SER A 135 ? 0.6370 0.2880 0.4006 0.0739  -0.1127 -0.0861 135 SER A OG  
687   N N   . PRO A 136 ? 0.5766 0.2509 0.3592 0.0725  -0.1392 -0.0783 136 PRO A N   
688   C CA  . PRO A 136 ? 0.5721 0.2504 0.3535 0.0737  -0.1555 -0.0737 136 PRO A CA  
689   C C   . PRO A 136 ? 0.5714 0.2486 0.3503 0.0795  -0.1594 -0.0703 136 PRO A C   
690   O O   . PRO A 136 ? 0.5610 0.2446 0.3472 0.0830  -0.1709 -0.0652 136 PRO A O   
691   C CB  . PRO A 136 ? 0.5987 0.2659 0.3564 0.0626  -0.1633 -0.0778 136 PRO A CB  
692   C CG  . PRO A 136 ? 0.6102 0.2708 0.3629 0.0566  -0.1508 -0.0844 136 PRO A CG  
693   C CD  . PRO A 136 ? 0.6047 0.2638 0.3654 0.0627  -0.1357 -0.0857 136 PRO A CD  
694   N N   . GLU A 137 ? 0.6518 0.3202 0.4216 0.0808  -0.1494 -0.0729 137 GLU A N   
695   C CA  . GLU A 137 ? 0.6514 0.3183 0.4200 0.0869  -0.1511 -0.0695 137 GLU A CA  
696   C C   . GLU A 137 ? 0.6166 0.3076 0.4173 0.0938  -0.1483 -0.0623 137 GLU A C   
697   O O   . GLU A 137 ? 0.6111 0.3066 0.4165 0.0981  -0.1507 -0.0576 137 GLU A O   
698   C CB  . GLU A 137 ? 0.6706 0.3238 0.4250 0.0866  -0.1378 -0.0738 137 GLU A CB  
699   C CG  . GLU A 137 ? 0.7057 0.3394 0.4274 0.0763  -0.1357 -0.0818 137 GLU A CG  
700   C CD  . GLU A 137 ? 0.7353 0.3542 0.4233 0.0718  -0.1433 -0.0832 137 GLU A CD  
701   O OE1 . GLU A 137 ? 0.7294 0.3632 0.4186 0.0692  -0.1573 -0.0753 137 GLU A OE1 
702   O OE2 . GLU A 137 ? 0.7595 0.3632 0.4269 0.0692  -0.1323 -0.0877 137 GLU A OE2 
703   N N   . TRP A 138 ? 0.5739 0.2818 0.3960 0.0928  -0.1421 -0.0616 138 TRP A N   
704   C CA  . TRP A 138 ? 0.5433 0.2753 0.3918 0.0945  -0.1386 -0.0566 138 TRP A CA  
705   C C   . TRP A 138 ? 0.5342 0.2746 0.3872 0.0947  -0.1490 -0.0527 138 TRP A C   
706   O O   . TRP A 138 ? 0.5157 0.2719 0.3853 0.0952  -0.1446 -0.0488 138 TRP A O   
707   C CB  . TRP A 138 ? 0.5270 0.2708 0.3910 0.0920  -0.1321 -0.0570 138 TRP A CB  
708   C CG  . TRP A 138 ? 0.5270 0.2700 0.3985 0.0922  -0.1186 -0.0585 138 TRP A CG  
709   C CD1 . TRP A 138 ? 0.5392 0.2719 0.4057 0.0904  -0.1119 -0.0626 138 TRP A CD1 
710   C CD2 . TRP A 138 ? 0.5152 0.2676 0.4023 0.0941  -0.1095 -0.0558 138 TRP A CD2 
711   N NE1 . TRP A 138 ? 0.5356 0.2706 0.4148 0.0915  -0.0993 -0.0624 138 TRP A NE1 
712   C CE2 . TRP A 138 ? 0.5211 0.2679 0.4129 0.0938  -0.0983 -0.0580 138 TRP A CE2 
713   C CE3 . TRP A 138 ? 0.5011 0.2655 0.3997 0.0954  -0.1090 -0.0517 138 TRP A CE3 
714   C CZ2 . TRP A 138 ? 0.5134 0.2661 0.4216 0.0953  -0.0879 -0.0558 138 TRP A CZ2 
715   C CZ3 . TRP A 138 ? 0.4937 0.2638 0.4072 0.0964  -0.0986 -0.0497 138 TRP A CZ3 
716   C CH2 . TRP A 138 ? 0.4998 0.2642 0.4182 0.0966  -0.0888 -0.0516 138 TRP A CH2 
717   N N   . GLY A 139 ? 0.5371 0.2670 0.3771 0.0932  -0.1615 -0.0535 139 GLY A N   
718   C CA  . GLY A 139 ? 0.5303 0.2678 0.3772 0.0924  -0.1699 -0.0491 139 GLY A CA  
719   C C   . GLY A 139 ? 0.5389 0.2739 0.3813 0.0949  -0.1729 -0.0436 139 GLY A C   
720   O O   . GLY A 139 ? 0.5292 0.2779 0.3845 0.0931  -0.1748 -0.0369 139 GLY A O   
721   N N   . ARG A 140 ? 0.5846 0.3046 0.4108 0.0985  -0.1709 -0.0447 140 ARG A N   
722   C CA  . ARG A 140 ? 0.5940 0.3130 0.4144 0.1014  -0.1735 -0.0372 140 ARG A CA  
723   C C   . ARG A 140 ? 0.5679 0.3099 0.4148 0.1026  -0.1613 -0.0327 140 ARG A C   
724   O O   . ARG A 140 ? 0.5691 0.3179 0.4189 0.1038  -0.1619 -0.0246 140 ARG A O   
725   C CB  . ARG A 140 ? 0.6233 0.3182 0.4156 0.1029  -0.1717 -0.0408 140 ARG A CB  
726   C CG  . ARG A 140 ? 0.6517 0.3422 0.4164 0.0905  -0.1775 -0.0435 140 ARG A CG  
727   C CD  . ARG A 140 ? 0.6784 0.3530 0.4169 0.0867  -0.1682 -0.0492 140 ARG A CD  
728   N NE  . ARG A 140 ? 0.7171 0.3977 0.4491 0.0875  -0.1678 -0.0403 140 ARG A NE  
729   C CZ  . ARG A 140 ? 0.7293 0.3973 0.4417 0.0864  -0.1579 -0.0429 140 ARG A CZ  
730   N NH1 . ARG A 140 ? 0.7290 0.3771 0.4271 0.0846  -0.1467 -0.0544 140 ARG A NH1 
731   N NH2 . ARG A 140 ? 0.7462 0.4208 0.4536 0.0872  -0.1583 -0.0335 140 ARG A NH2 
732   N N   . PHE A 141 ? 0.5401 0.2953 0.4056 0.1013  -0.1505 -0.0363 141 PHE A N   
733   C CA  . PHE A 141 ? 0.5188 0.2920 0.4062 0.1015  -0.1394 -0.0322 141 PHE A CA  
734   C C   . PHE A 141 ? 0.5027 0.2918 0.4064 0.0986  -0.1394 -0.0269 141 PHE A C   
735   O O   . PHE A 141 ? 0.4864 0.2856 0.4021 0.0952  -0.1357 -0.0285 141 PHE A O   
736   C CB  . PHE A 141 ? 0.5044 0.2848 0.4034 0.0999  -0.1294 -0.0360 141 PHE A CB  
737   C CG  . PHE A 141 ? 0.5187 0.2859 0.4073 0.1025  -0.1252 -0.0397 141 PHE A CG  
738   C CD1 . PHE A 141 ? 0.5288 0.2891 0.4135 0.1064  -0.1204 -0.0377 141 PHE A CD1 
739   C CD2 . PHE A 141 ? 0.5230 0.2842 0.4066 0.1009  -0.1242 -0.0446 141 PHE A CD2 
740   C CE1 . PHE A 141 ? 0.5436 0.2904 0.4193 0.1084  -0.1139 -0.0414 141 PHE A CE1 
741   C CE2 . PHE A 141 ? 0.5368 0.2859 0.4132 0.1026  -0.1170 -0.0478 141 PHE A CE2 
742   C CZ  . PHE A 141 ? 0.5475 0.2888 0.4197 0.1061  -0.1115 -0.0465 141 PHE A CZ  
743   N N   . SER A 142 ? 0.5123 0.3039 0.4163 0.0999  -0.1428 -0.0192 142 SER A N   
744   C CA  . SER A 142 ? 0.5005 0.3066 0.4200 0.0974  -0.1423 -0.0125 142 SER A CA  
745   C C   . SER A 142 ? 0.4785 0.2984 0.4180 0.0963  -0.1304 -0.0114 142 SER A C   
746   O O   . SER A 142 ? 0.4675 0.2952 0.4172 0.0936  -0.1284 -0.0104 142 SER A O   
747   C CB  . SER A 142 ? 0.5105 0.3207 0.4291 0.0990  -0.1466 -0.0018 142 SER A CB  
748   O OG  . SER A 142 ? 0.5125 0.3221 0.4316 0.1030  -0.1406 0.0012  142 SER A OG  
749   N N   . LYS A 143 ? 0.4957 0.3174 0.4401 0.0982  -0.1225 -0.0113 143 LYS A N   
750   C CA  . LYS A 143 ? 0.4778 0.3105 0.4388 0.0967  -0.1122 -0.0096 143 LYS A CA  
751   C C   . LYS A 143 ? 0.4692 0.3028 0.4316 0.0935  -0.1093 -0.0164 143 LYS A C   
752   O O   . LYS A 143 ? 0.4581 0.2987 0.4313 0.0918  -0.1023 -0.0155 143 LYS A O   
753   C CB  . LYS A 143 ? 0.4777 0.3123 0.4449 0.0998  -0.1053 -0.0053 143 LYS A CB  
754   C CG  . LYS A 143 ? 0.4854 0.3223 0.4543 0.1031  -0.1069 0.0041  143 LYS A CG  
755   C CD  . LYS A 143 ? 0.4841 0.3270 0.4661 0.1055  -0.0971 0.0100  143 LYS A CD  
756   C CE  . LYS A 143 ? 0.5001 0.3355 0.4770 0.1080  -0.0943 0.0072  143 LYS A CE  
757   N NZ  . LYS A 143 ? 0.5064 0.3303 0.4651 0.1116  -0.1026 0.0081  143 LYS A NZ  
758   N N   . LEU A 144 ? 0.4399 0.2658 0.3910 0.0927  -0.1147 -0.0225 144 LEU A N   
759   C CA  . LEU A 144 ? 0.4321 0.2599 0.3852 0.0901  -0.1120 -0.0273 144 LEU A CA  
760   C C   . LEU A 144 ? 0.4211 0.2558 0.3809 0.0867  -0.1108 -0.0271 144 LEU A C   
761   O O   . LEU A 144 ? 0.4228 0.2569 0.3805 0.0858  -0.1150 -0.0265 144 LEU A O   
762   C CB  . LEU A 144 ? 0.4429 0.2609 0.3831 0.0906  -0.1176 -0.0325 144 LEU A CB  
763   C CG  . LEU A 144 ? 0.4374 0.2571 0.3808 0.0890  -0.1136 -0.0356 144 LEU A CG  
764   C CD1 . LEU A 144 ? 0.4380 0.2575 0.3869 0.0911  -0.1066 -0.0346 144 LEU A CD1 
765   C CD2 . LEU A 144 ? 0.4471 0.2582 0.3793 0.0890  -0.1188 -0.0398 144 LEU A CD2 
766   N N   . GLU A 145 ? 0.4036 0.2404 0.3684 0.0861  -0.1094 -0.0295 145 GLU A N   
767   C CA  . GLU A 145 ? 0.3998 0.2387 0.3672 0.0841  -0.1109 -0.0309 145 GLU A CA  
768   C C   . GLU A 145 ? 0.3998 0.2372 0.3638 0.0826  -0.1141 -0.0356 145 GLU A C   
769   O O   . GLU A 145 ? 0.3989 0.2359 0.3609 0.0810  -0.1167 -0.0369 145 GLU A O   
770   C CB  . GLU A 145 ? 0.3971 0.2390 0.3731 0.0848  -0.1069 -0.0286 145 GLU A CB  
771   C CG  . GLU A 145 ? 0.3972 0.2414 0.3789 0.0869  -0.1029 -0.0225 145 GLU A CG  
772   C CD  . GLU A 145 ? 0.3957 0.2418 0.3863 0.0881  -0.0977 -0.0201 145 GLU A CD  
773   O OE1 . GLU A 145 ? 0.3944 0.2399 0.3869 0.0868  -0.0978 -0.0226 145 GLU A OE1 
774   O OE2 . GLU A 145 ? 0.3968 0.2444 0.3921 0.0906  -0.0936 -0.0156 145 GLU A OE2 
775   N N   . TYR A 146 ? 0.3867 0.2229 0.3509 0.0835  -0.1135 -0.0372 146 TYR A N   
776   C CA  . TYR A 146 ? 0.3875 0.2227 0.3508 0.0827  -0.1161 -0.0403 146 TYR A CA  
777   C C   . TYR A 146 ? 0.3921 0.2236 0.3516 0.0839  -0.1153 -0.0412 146 TYR A C   
778   O O   . TYR A 146 ? 0.3949 0.2247 0.3561 0.0859  -0.1113 -0.0400 146 TYR A O   
779   C CB  . TYR A 146 ? 0.3861 0.2234 0.3571 0.0829  -0.1153 -0.0406 146 TYR A CB  
780   C CG  . TYR A 146 ? 0.3872 0.2237 0.3586 0.0819  -0.1191 -0.0429 146 TYR A CG  
781   C CD1 . TYR A 146 ? 0.3903 0.2253 0.3643 0.0832  -0.1183 -0.0435 146 TYR A CD1 
782   C CD2 . TYR A 146 ? 0.3865 0.2229 0.3561 0.0802  -0.1227 -0.0440 146 TYR A CD2 
783   C CE1 . TYR A 146 ? 0.3921 0.2262 0.3679 0.0827  -0.1218 -0.0448 146 TYR A CE1 
784   C CE2 . TYR A 146 ? 0.3888 0.2237 0.3581 0.0796  -0.1267 -0.0456 146 TYR A CE2 
785   C CZ  . TYR A 146 ? 0.3913 0.2254 0.3643 0.0808  -0.1266 -0.0459 146 TYR A CZ  
786   O OH  . TYR A 146 ? 0.3944 0.2267 0.3683 0.0804  -0.1305 -0.0469 146 TYR A OH  
787   N N   . PHE A 147 ? 0.3917 0.2206 0.3459 0.0830  -0.1182 -0.0431 147 PHE A N   
788   C CA  . PHE A 147 ? 0.3977 0.2215 0.3478 0.0841  -0.1166 -0.0440 147 PHE A CA  
789   C C   . PHE A 147 ? 0.3992 0.2220 0.3510 0.0839  -0.1180 -0.0455 147 PHE A C   
790   O O   . PHE A 147 ? 0.3982 0.2212 0.3466 0.0824  -0.1217 -0.0464 147 PHE A O   
791   C CB  . PHE A 147 ? 0.4006 0.2207 0.3420 0.0834  -0.1183 -0.0440 147 PHE A CB  
792   C CG  . PHE A 147 ? 0.4095 0.2217 0.3450 0.0847  -0.1157 -0.0450 147 PHE A CG  
793   C CD1 . PHE A 147 ? 0.4140 0.2230 0.3526 0.0869  -0.1097 -0.0447 147 PHE A CD1 
794   C CD2 . PHE A 147 ? 0.4194 0.2236 0.3442 0.0847  -0.1213 -0.0473 147 PHE A CD2 
795   C CE1 . PHE A 147 ? 0.4290 0.2261 0.3592 0.0890  -0.1082 -0.0472 147 PHE A CE1 
796   C CE2 . PHE A 147 ? 0.4348 0.2268 0.3502 0.0865  -0.1209 -0.0498 147 PHE A CE2 
797   C CZ  . PHE A 147 ? 0.4400 0.2280 0.3577 0.0886  -0.1137 -0.0500 147 PHE A CZ  
798   N N   . ASP A 148 ? 0.4269 0.2482 0.3847 0.0857  -0.1143 -0.0453 148 ASP A N   
799   C CA  . ASP A 148 ? 0.4290 0.2494 0.3911 0.0860  -0.1152 -0.0459 148 ASP A CA  
800   C C   . ASP A 148 ? 0.4368 0.2511 0.4014 0.0883  -0.1088 -0.0456 148 ASP A C   
801   O O   . ASP A 148 ? 0.4391 0.2524 0.4105 0.0903  -0.1033 -0.0445 148 ASP A O   
802   C CB  . ASP A 148 ? 0.4255 0.2504 0.3964 0.0858  -0.1173 -0.0453 148 ASP A CB  
803   C CG  . ASP A 148 ? 0.4276 0.2516 0.4013 0.0855  -0.1208 -0.0457 148 ASP A CG  
804   O OD1 . ASP A 148 ? 0.4324 0.2523 0.4043 0.0863  -0.1193 -0.0458 148 ASP A OD1 
805   O OD2 . ASP A 148 ? 0.4255 0.2521 0.4031 0.0844  -0.1248 -0.0458 148 ASP A OD2 
806   N N   . LEU A 149 ? 0.4107 0.2198 0.3704 0.0882  -0.1083 -0.0466 149 LEU A N   
807   C CA  . LEU A 149 ? 0.4202 0.2214 0.3824 0.0902  -0.1008 -0.0468 149 LEU A CA  
808   C C   . LEU A 149 ? 0.4229 0.2227 0.3899 0.0907  -0.1014 -0.0464 149 LEU A C   
809   O O   . LEU A 149 ? 0.4314 0.2235 0.3982 0.0917  -0.0957 -0.0469 149 LEU A O   
810   C CB  . LEU A 149 ? 0.4274 0.2206 0.3789 0.0895  -0.0975 -0.0487 149 LEU A CB  
811   C CG  . LEU A 149 ? 0.4280 0.2198 0.3738 0.0894  -0.0960 -0.0489 149 LEU A CG  
812   C CD1 . LEU A 149 ? 0.4389 0.2203 0.3717 0.0883  -0.0950 -0.0517 149 LEU A CD1 
813   C CD2 . LEU A 149 ? 0.4311 0.2213 0.3851 0.0919  -0.0885 -0.0477 149 LEU A CD2 
814   N N   . SER A 150 ? 0.4528 0.2589 0.4239 0.0899  -0.1079 -0.0455 150 SER A N   
815   C CA  . SER A 150 ? 0.4557 0.2602 0.4296 0.0902  -0.1100 -0.0448 150 SER A CA  
816   C C   . SER A 150 ? 0.4628 0.2634 0.4489 0.0934  -0.1035 -0.0425 150 SER A C   
817   O O   . SER A 150 ? 0.4639 0.2647 0.4580 0.0953  -0.0984 -0.0413 150 SER A O   
818   C CB  . SER A 150 ? 0.4499 0.2601 0.4236 0.0883  -0.1184 -0.0447 150 SER A CB  
819   O OG  . SER A 150 ? 0.4442 0.2573 0.4085 0.0858  -0.1226 -0.0463 150 SER A OG  
820   N N   . ILE A 151 ? 0.4547 0.2514 0.4431 0.0944  -0.1030 -0.0413 151 ILE A N   
821   C CA  . ILE A 151 ? 0.4627 0.2551 0.4640 0.0980  -0.0965 -0.0381 151 ILE A CA  
822   C C   . ILE A 151 ? 0.4696 0.2554 0.4748 0.1003  -0.0847 -0.0382 151 ILE A C   
823   O O   . ILE A 151 ? 0.4694 0.2570 0.4834 0.1022  -0.0811 -0.0364 151 ILE A O   
824   C CB  . ILE A 151 ? 0.4599 0.2584 0.4727 0.0989  -0.1018 -0.0351 151 ILE A CB  
825   C CG1 . ILE A 151 ? 0.4560 0.2580 0.4626 0.0962  -0.1126 -0.0358 151 ILE A CG1 
826   C CG2 . ILE A 151 ? 0.4690 0.2634 0.4967 0.1034  -0.0953 -0.0304 151 ILE A CG2 
827   C CD1 . ILE A 151 ? 0.4491 0.2577 0.4560 0.0939  -0.1202 -0.0368 151 ILE A CD1 
828   N N   . ASN A 152 ? 0.4763 0.2532 0.4743 0.1000  -0.0781 -0.0405 152 ASN A N   
829   C CA  . ASN A 152 ? 0.4863 0.2533 0.4852 0.1014  -0.0656 -0.0418 152 ASN A CA  
830   C C   . ASN A 152 ? 0.4983 0.2535 0.4948 0.1014  -0.0575 -0.0435 152 ASN A C   
831   O O   . ASN A 152 ? 0.4986 0.2541 0.4961 0.1015  -0.0609 -0.0421 152 ASN A O   
832   C CB  . ASN A 152 ? 0.4827 0.2507 0.4705 0.0988  -0.0670 -0.0451 152 ASN A CB  
833   C CG  . ASN A 152 ? 0.4775 0.2514 0.4721 0.1002  -0.0668 -0.0432 152 ASN A CG  
834   O OD1 . ASN A 152 ? 0.4834 0.2538 0.4898 0.1035  -0.0582 -0.0407 152 ASN A OD1 
835   N ND2 . ASN A 152 ? 0.4671 0.2495 0.4551 0.0980  -0.0755 -0.0440 152 ASN A ND2 
836   N N   . GLN A 153 ? 0.5350 0.2787 0.5283 0.1008  -0.0462 -0.0469 153 GLN A N   
837   C CA  . GLN A 153 ? 0.5486 0.2790 0.5390 0.0996  -0.0369 -0.0502 153 GLN A CA  
838   C C   . GLN A 153 ? 0.5526 0.2775 0.5264 0.0944  -0.0376 -0.0570 153 GLN A C   
839   O O   . GLN A 153 ? 0.5673 0.2788 0.5383 0.0922  -0.0266 -0.0623 153 GLN A O   
840   C CB  . GLN A 153 ? 0.5632 0.2816 0.5667 0.1030  -0.0202 -0.0491 153 GLN A CB  
841   C CG  . GLN A 153 ? 0.5618 0.2847 0.5808 0.1091  -0.0195 -0.0411 153 GLN A CG  
842   C CD  . GLN A 153 ? 0.5703 0.2872 0.5999 0.1136  -0.0070 -0.0380 153 GLN A CD  
843   O OE1 . GLN A 153 ? 0.5645 0.2900 0.6021 0.1175  -0.0115 -0.0324 153 GLN A OE1 
844   N NE2 . GLN A 153 ? 0.5851 0.2870 0.6153 0.1125  0.0089  -0.0424 153 GLN A NE2 
845   N N   . LEU A 154 ? 0.5276 0.2622 0.4907 0.0921  -0.0505 -0.0571 154 LEU A N   
846   C CA  . LEU A 154 ? 0.5311 0.2615 0.4781 0.0875  -0.0531 -0.0621 154 LEU A CA  
847   C C   . LEU A 154 ? 0.5373 0.2618 0.4775 0.0844  -0.0537 -0.0650 154 LEU A C   
848   O O   . LEU A 154 ? 0.5319 0.2610 0.4770 0.0857  -0.0579 -0.0619 154 LEU A O   
849   C CB  . LEU A 154 ? 0.5165 0.2594 0.4571 0.0870  -0.0656 -0.0600 154 LEU A CB  
850   C CG  . LEU A 154 ? 0.5140 0.2592 0.4536 0.0878  -0.0649 -0.0597 154 LEU A CG  
851   C CD1 . LEU A 154 ? 0.5173 0.2607 0.4708 0.0914  -0.0555 -0.0577 154 LEU A CD1 
852   C CD2 . LEU A 154 ? 0.4978 0.2571 0.4363 0.0880  -0.0771 -0.0564 154 LEU A CD2 
853   N N   . VAL A 155 ? 0.5478 0.2608 0.4755 0.0800  -0.0500 -0.0715 155 VAL A N   
854   C CA  . VAL A 155 ? 0.5573 0.2627 0.4766 0.0762  -0.0510 -0.0755 155 VAL A CA  
855   C C   . VAL A 155 ? 0.5659 0.2666 0.4646 0.0724  -0.0608 -0.0799 155 VAL A C   
856   O O   . VAL A 155 ? 0.5659 0.2678 0.4568 0.0732  -0.0660 -0.0798 155 VAL A O   
857   C CB  . VAL A 155 ? 0.5760 0.2662 0.4996 0.0743  -0.0363 -0.0810 155 VAL A CB  
858   C CG1 . VAL A 155 ? 0.5709 0.2638 0.5135 0.0790  -0.0298 -0.0755 155 VAL A CG1 
859   C CG2 . VAL A 155 ? 0.5919 0.2711 0.5114 0.0735  -0.0279 -0.0867 155 VAL A CG2 
860   N N   . GLY A 156 ? 0.5838 0.2785 0.4740 0.0682  -0.0635 -0.0833 156 GLY A N   
861   C CA  . GLY A 156 ? 0.5939 0.2835 0.4653 0.0639  -0.0735 -0.0869 156 GLY A CA  
862   C C   . GLY A 156 ? 0.5767 0.2792 0.4497 0.0655  -0.0872 -0.0812 156 GLY A C   
863   O O   . GLY A 156 ? 0.5589 0.2733 0.4453 0.0686  -0.0883 -0.0757 156 GLY A O   
864   N N   . GLU A 157 ? 0.5795 0.2788 0.4383 0.0629  -0.0976 -0.0827 157 GLU A N   
865   C CA  . GLU A 157 ? 0.5660 0.2756 0.4269 0.0642  -0.1105 -0.0779 157 GLU A CA  
866   C C   . GLU A 157 ? 0.5530 0.2725 0.4165 0.0689  -0.1174 -0.0732 157 GLU A C   
867   O O   . GLU A 157 ? 0.5570 0.2737 0.4177 0.0706  -0.1136 -0.0741 157 GLU A O   
868   C CB  . GLU A 157 ? 0.5826 0.2827 0.4291 0.0581  -0.1186 -0.0817 157 GLU A CB  
869   C CG  . GLU A 157 ? 0.6004 0.2886 0.4412 0.0513  -0.1108 -0.0884 157 GLU A CG  
870   C CD  . GLU A 157 ? 0.6047 0.2918 0.4425 0.0464  -0.1192 -0.0890 157 GLU A CD  
871   O OE1 . GLU A 157 ? 0.5922 0.2881 0.4348 0.0491  -0.1304 -0.0836 157 GLU A OE1 
872   O OE2 . GLU A 157 ? 0.6213 0.2986 0.4531 0.0394  -0.1140 -0.0952 157 GLU A OE2 
873   N N   . ILE A 158 ? 0.4786 0.2092 0.3482 0.0708  -0.1267 -0.0685 158 ILE A N   
874   C CA  . ILE A 158 ? 0.4674 0.2070 0.3394 0.0742  -0.1340 -0.0646 158 ILE A CA  
875   C C   . ILE A 158 ? 0.4826 0.2122 0.3404 0.0724  -0.1450 -0.0661 158 ILE A C   
876   O O   . ILE A 158 ? 0.4873 0.2139 0.3427 0.0697  -0.1523 -0.0661 158 ILE A O   
877   C CB  . ILE A 158 ? 0.4461 0.2015 0.3313 0.0757  -0.1368 -0.0599 158 ILE A CB  
878   C CG1 . ILE A 158 ? 0.4341 0.1977 0.3310 0.0766  -0.1270 -0.0583 158 ILE A CG1 
879   C CG2 . ILE A 158 ? 0.4369 0.2004 0.3242 0.0777  -0.1433 -0.0572 158 ILE A CG2 
880   C CD1 . ILE A 158 ? 0.4193 0.1939 0.3250 0.0761  -0.1280 -0.0551 158 ILE A CD1 
881   N N   . PRO A 159 ? 0.5083 0.2314 0.3562 0.0734  -0.1467 -0.0672 159 PRO A N   
882   C CA  . PRO A 159 ? 0.5259 0.2379 0.3581 0.0706  -0.1583 -0.0682 159 PRO A CA  
883   C C   . PRO A 159 ? 0.5137 0.2342 0.3546 0.0732  -0.1706 -0.0629 159 PRO A C   
884   O O   . PRO A 159 ? 0.4925 0.2281 0.3478 0.0774  -0.1692 -0.0592 159 PRO A O   
885   C CB  . PRO A 159 ? 0.5355 0.2409 0.3573 0.0725  -0.1559 -0.0694 159 PRO A CB  
886   C CG  . PRO A 159 ? 0.5152 0.2336 0.3538 0.0777  -0.1457 -0.0669 159 PRO A CG  
887   C CD  . PRO A 159 ? 0.5046 0.2299 0.3555 0.0765  -0.1381 -0.0671 159 PRO A CD  
888   N N   . PRO A 160 ? 0.5577 0.2703 0.3913 0.0686  -0.1817 -0.0631 160 PRO A N   
889   C CA  . PRO A 160 ? 0.5486 0.2669 0.3920 0.0711  -0.1941 -0.0578 160 PRO A CA  
890   C C   . PRO A 160 ? 0.5471 0.2660 0.3890 0.0755  -0.2001 -0.0550 160 PRO A C   
891   O O   . PRO A 160 ? 0.5337 0.2632 0.3882 0.0757  -0.2041 -0.0532 160 PRO A O   
892   C CB  . PRO A 160 ? 0.5667 0.2774 0.4025 0.0618  -0.2033 -0.0590 160 PRO A CB  
893   C CG  . PRO A 160 ? 0.5824 0.2862 0.4049 0.0542  -0.1942 -0.0656 160 PRO A CG  
894   C CD  . PRO A 160 ? 0.5826 0.2832 0.3990 0.0585  -0.1828 -0.0684 160 PRO A CD  
895   N N   . GLU A 161 ? 0.5566 0.2665 0.3839 0.0753  -0.1964 -0.0576 161 GLU A N   
896   C CA  . GLU A 161 ? 0.5571 0.2657 0.3817 0.0799  -0.2011 -0.0551 161 GLU A CA  
897   C C   . GLU A 161 ? 0.5275 0.2593 0.3741 0.0829  -0.1894 -0.0533 161 GLU A C   
898   O O   . GLU A 161 ? 0.5199 0.2599 0.3749 0.0838  -0.1870 -0.0497 161 GLU A O   
899   C CB  . GLU A 161 ? 0.5772 0.2737 0.3810 0.0774  -0.1953 -0.0596 161 GLU A CB  
900   C CG  . GLU A 161 ? 0.6027 0.2962 0.3843 0.0653  -0.2028 -0.0604 161 GLU A CG  
901   C CD  . GLU A 161 ? 0.6165 0.3051 0.3889 0.0558  -0.1976 -0.0659 161 GLU A CD  
902   O OE1 . GLU A 161 ? 0.6042 0.2935 0.3896 0.0589  -0.1905 -0.0679 161 GLU A OE1 
903   O OE2 . GLU A 161 ? 0.6399 0.3264 0.3922 0.0445  -0.2002 -0.0675 161 GLU A OE2 
904   N N   . LEU A 162 ? 0.5063 0.2504 0.3646 0.0827  -0.1787 -0.0542 162 LEU A N   
905   C CA  . LEU A 162 ? 0.4811 0.2450 0.3585 0.0827  -0.1680 -0.0521 162 LEU A CA  
906   C C   . LEU A 162 ? 0.4699 0.2434 0.3602 0.0804  -0.1694 -0.0491 162 LEU A C   
907   O O   . LEU A 162 ? 0.4541 0.2406 0.3575 0.0804  -0.1610 -0.0460 162 LEU A O   
908   C CB  . LEU A 162 ? 0.4697 0.2411 0.3547 0.0819  -0.1590 -0.0529 162 LEU A CB  
909   C CG  . LEU A 162 ? 0.4748 0.2415 0.3562 0.0834  -0.1508 -0.0546 162 LEU A CG  
910   C CD1 . LEU A 162 ? 0.4585 0.2369 0.3534 0.0824  -0.1411 -0.0535 162 LEU A CD1 
911   C CD2 . LEU A 162 ? 0.4794 0.2432 0.3573 0.0860  -0.1485 -0.0543 162 LEU A CD2 
912   N N   . GLY A 163 ? 0.5196 0.2864 0.4078 0.0782  -0.1785 -0.0489 163 GLY A N   
913   C CA  . GLY A 163 ? 0.5096 0.2866 0.4136 0.0761  -0.1771 -0.0437 163 GLY A CA  
914   C C   . GLY A 163 ? 0.5085 0.2924 0.4198 0.0770  -0.1760 -0.0364 163 GLY A C   
915   O O   . GLY A 163 ? 0.4994 0.2970 0.4272 0.0766  -0.1700 -0.0301 163 GLY A O   
916   N N   . LYS A 164 ? 0.4889 0.2642 0.3875 0.0786  -0.1814 -0.0359 164 LYS A N   
917   C CA  . LYS A 164 ? 0.4876 0.2731 0.3931 0.0795  -0.1798 -0.0270 164 LYS A CA  
918   C C   . LYS A 164 ? 0.4749 0.2674 0.3862 0.0828  -0.1687 -0.0274 164 LYS A C   
919   O O   . LYS A 164 ? 0.4768 0.2743 0.3900 0.0846  -0.1673 -0.0212 164 LYS A O   
920   C CB  . LYS A 164 ? 0.5107 0.2874 0.3986 0.0781  -0.1913 -0.0238 164 LYS A CB  
921   C CG  . LYS A 164 ? 0.5269 0.2848 0.3918 0.0813  -0.1933 -0.0306 164 LYS A CG  
922   C CD  . LYS A 164 ? 0.5546 0.3009 0.3946 0.0761  -0.2061 -0.0301 164 LYS A CD  
923   C CE  . LYS A 164 ? 0.5744 0.3067 0.3891 0.0781  -0.2074 -0.0326 164 LYS A CE  
924   N NZ  . LYS A 164 ? 0.6010 0.3322 0.3910 0.0668  -0.2157 -0.0318 164 LYS A NZ  
925   N N   . LEU A 165 ? 0.4503 0.2454 0.3652 0.0829  -0.1607 -0.0330 165 LEU A N   
926   C CA  . LEU A 165 ? 0.4361 0.2412 0.3602 0.0843  -0.1497 -0.0317 165 LEU A CA  
927   C C   . LEU A 165 ? 0.4208 0.2395 0.3623 0.0831  -0.1425 -0.0260 165 LEU A C   
928   O O   . LEU A 165 ? 0.4092 0.2332 0.3567 0.0815  -0.1362 -0.0277 165 LEU A O   
929   C CB  . LEU A 165 ? 0.4308 0.2350 0.3516 0.0841  -0.1452 -0.0376 165 LEU A CB  
930   C CG  . LEU A 165 ? 0.4453 0.2371 0.3511 0.0864  -0.1487 -0.0420 165 LEU A CG  
931   C CD1 . LEU A 165 ? 0.4384 0.2329 0.3460 0.0856  -0.1431 -0.0451 165 LEU A CD1 
932   C CD2 . LEU A 165 ? 0.4501 0.2401 0.3540 0.0897  -0.1457 -0.0396 165 LEU A CD2 
933   N N   . SER A 166 ? 0.4499 0.2740 0.3987 0.0840  -0.1436 -0.0179 166 SER A N   
934   C CA  . SER A 166 ? 0.4393 0.2746 0.4043 0.0837  -0.1373 -0.0111 166 SER A CA  
935   C C   . SER A 166 ? 0.4259 0.2673 0.3988 0.0841  -0.1258 -0.0113 166 SER A C   
936   O O   . SER A 166 ? 0.4183 0.2640 0.3996 0.0834  -0.1202 -0.0095 166 SER A O   
937   C CB  . SER A 166 ? 0.4441 0.2869 0.4171 0.0853  -0.1396 -0.0004 166 SER A CB  
938   O OG  . SER A 166 ? 0.4461 0.2902 0.4174 0.0879  -0.1370 0.0024  166 SER A OG  
939   N N   . ASN A 167 ? 0.4307 0.2715 0.4008 0.0854  -0.1225 -0.0131 167 ASN A N   
940   C CA  . ASN A 167 ? 0.4201 0.2661 0.3979 0.0854  -0.1128 -0.0125 167 ASN A CA  
941   C C   . ASN A 167 ? 0.4176 0.2600 0.3897 0.0833  -0.1133 -0.0204 167 ASN A C   
942   O O   . ASN A 167 ? 0.4153 0.2584 0.3905 0.0836  -0.1103 -0.0219 167 ASN A O   
943   C CB  . ASN A 167 ? 0.4232 0.2705 0.4028 0.0880  -0.1096 -0.0095 167 ASN A CB  
944   C CG  . ASN A 167 ? 0.4215 0.2754 0.4120 0.0907  -0.1059 0.0002  167 ASN A CG  
945   O OD1 . ASN A 167 ? 0.4202 0.2774 0.4200 0.0911  -0.1012 0.0033  167 ASN A OD1 
946   N ND2 . ASN A 167 ? 0.4303 0.2836 0.4181 0.0933  -0.1098 0.0046  167 ASN A ND2 
947   N N   . LEU A 168 ? 0.4086 0.2471 0.3725 0.0815  -0.1178 -0.0248 168 LEU A N   
948   C CA  . LEU A 168 ? 0.4079 0.2439 0.3668 0.0803  -0.1191 -0.0308 168 LEU A CA  
949   C C   . LEU A 168 ? 0.4052 0.2423 0.3675 0.0793  -0.1181 -0.0316 168 LEU A C   
950   O O   . LEU A 168 ? 0.4049 0.2423 0.3698 0.0787  -0.1180 -0.0295 168 LEU A O   
951   C CB  . LEU A 168 ? 0.4116 0.2430 0.3619 0.0791  -0.1233 -0.0342 168 LEU A CB  
952   C CG  . LEU A 168 ? 0.4128 0.2419 0.3586 0.0791  -0.1240 -0.0385 168 LEU A CG  
953   C CD1 . LEU A 168 ? 0.4153 0.2432 0.3603 0.0811  -0.1215 -0.0384 168 LEU A CD1 
954   C CD2 . LEU A 168 ? 0.4165 0.2414 0.3557 0.0780  -0.1274 -0.0410 168 LEU A CD2 
955   N N   . ASP A 169 ? 0.4334 0.2706 0.3960 0.0793  -0.1173 -0.0340 169 ASP A N   
956   C CA  . ASP A 169 ? 0.4329 0.2695 0.3964 0.0785  -0.1168 -0.0349 169 ASP A CA  
957   C C   . ASP A 169 ? 0.4347 0.2688 0.3915 0.0774  -0.1210 -0.0389 169 ASP A C   
958   O O   . ASP A 169 ? 0.4360 0.2680 0.3905 0.0766  -0.1217 -0.0392 169 ASP A O   
959   C CB  . ASP A 169 ? 0.4320 0.2697 0.4007 0.0794  -0.1136 -0.0341 169 ASP A CB  
960   C CG  . ASP A 169 ? 0.4374 0.2725 0.4042 0.0786  -0.1144 -0.0360 169 ASP A CG  
961   O OD1 . ASP A 169 ? 0.4385 0.2713 0.4031 0.0781  -0.1141 -0.0356 169 ASP A OD1 
962   O OD2 . ASP A 169 ? 0.4507 0.2856 0.4186 0.0786  -0.1153 -0.0376 169 ASP A OD2 
963   N N   . THR A 170 ? 0.3969 0.2308 0.3516 0.0776  -0.1229 -0.0410 170 THR A N   
964   C CA  . THR A 170 ? 0.3993 0.2310 0.3497 0.0772  -0.1262 -0.0437 170 THR A CA  
965   C C   . THR A 170 ? 0.4015 0.2317 0.3488 0.0778  -0.1269 -0.0445 170 THR A C   
966   O O   . THR A 170 ? 0.4018 0.2324 0.3505 0.0789  -0.1249 -0.0439 170 THR A O   
967   C CB  . THR A 170 ? 0.3997 0.2319 0.3532 0.0775  -0.1270 -0.0447 170 THR A CB  
968   O OG1 . THR A 170 ? 0.3997 0.2314 0.3541 0.0769  -0.1267 -0.0441 170 THR A OG1 
969   C CG2 . THR A 170 ? 0.4029 0.2330 0.3540 0.0775  -0.1303 -0.0465 170 THR A CG2 
970   N N   . LEU A 171 ? 0.3888 0.2163 0.3316 0.0772  -0.1291 -0.0457 171 LEU A N   
971   C CA  . LEU A 171 ? 0.3926 0.2170 0.3322 0.0779  -0.1291 -0.0465 171 LEU A CA  
972   C C   . LEU A 171 ? 0.3958 0.2181 0.3351 0.0784  -0.1300 -0.0476 171 LEU A C   
973   O O   . LEU A 171 ? 0.3968 0.2177 0.3337 0.0776  -0.1320 -0.0478 171 LEU A O   
974   C CB  . LEU A 171 ? 0.3940 0.2161 0.3293 0.0769  -0.1302 -0.0461 171 LEU A CB  
975   C CG  . LEU A 171 ? 0.3999 0.2168 0.3305 0.0774  -0.1301 -0.0470 171 LEU A CG  
976   C CD1 . LEU A 171 ? 0.4030 0.2178 0.3328 0.0790  -0.1274 -0.0470 171 LEU A CD1 
977   C CD2 . LEU A 171 ? 0.4016 0.2159 0.3287 0.0759  -0.1322 -0.0466 171 LEU A CD2 
978   N N   . HIS A 172 ? 0.4247 0.2458 0.3671 0.0800  -0.1279 -0.0478 172 HIS A N   
979   C CA  . HIS A 172 ? 0.4285 0.2474 0.3735 0.0809  -0.1279 -0.0482 172 HIS A CA  
980   C C   . HIS A 172 ? 0.4347 0.2485 0.3793 0.0825  -0.1237 -0.0483 172 HIS A C   
981   O O   . HIS A 172 ? 0.4366 0.2493 0.3845 0.0840  -0.1196 -0.0480 172 HIS A O   
982   C CB  . HIS A 172 ? 0.4272 0.2487 0.3796 0.0815  -0.1283 -0.0479 172 HIS A CB  
983   C CG  . HIS A 172 ? 0.4244 0.2480 0.3759 0.0799  -0.1323 -0.0482 172 HIS A CG  
984   N ND1 . HIS A 172 ? 0.4235 0.2489 0.3809 0.0799  -0.1337 -0.0481 172 HIS A ND1 
985   C CD2 . HIS A 172 ? 0.4235 0.2465 0.3692 0.0785  -0.1346 -0.0484 172 HIS A CD2 
986   C CE1 . HIS A 172 ? 0.4229 0.2480 0.3767 0.0785  -0.1368 -0.0485 172 HIS A CE1 
987   N NE2 . HIS A 172 ? 0.4230 0.2466 0.3698 0.0777  -0.1369 -0.0485 172 HIS A NE2 
988   N N   . LEU A 173 ? 0.4219 0.2314 0.3628 0.0823  -0.1237 -0.0486 173 LEU A N   
989   C CA  . LEU A 173 ? 0.4300 0.2324 0.3702 0.0835  -0.1186 -0.0491 173 LEU A CA  
990   C C   . LEU A 173 ? 0.4347 0.2338 0.3781 0.0843  -0.1176 -0.0487 173 LEU A C   
991   O O   . LEU A 173 ? 0.4408 0.2339 0.3812 0.0842  -0.1153 -0.0493 173 LEU A O   
992   C CB  . LEU A 173 ? 0.4330 0.2312 0.3650 0.0821  -0.1185 -0.0501 173 LEU A CB  
993   C CG  . LEU A 173 ? 0.4306 0.2303 0.3593 0.0816  -0.1192 -0.0501 173 LEU A CG  
994   C CD1 . LEU A 173 ? 0.4329 0.2294 0.3541 0.0797  -0.1223 -0.0506 173 LEU A CD1 
995   C CD2 . LEU A 173 ? 0.4371 0.2316 0.3664 0.0833  -0.1129 -0.0507 173 LEU A CD2 
996   N N   . VAL A 174 ? 0.4607 0.2630 0.4107 0.0852  -0.1195 -0.0476 174 VAL A N   
997   C CA  . VAL A 174 ? 0.4643 0.2644 0.4167 0.0857  -0.1210 -0.0466 174 VAL A CA  
998   C C   . VAL A 174 ? 0.4722 0.2670 0.4330 0.0885  -0.1146 -0.0452 174 VAL A C   
999   O O   . VAL A 174 ? 0.4740 0.2680 0.4411 0.0902  -0.1095 -0.0448 174 VAL A O   
1000  C CB  . VAL A 174 ? 0.4601 0.2649 0.4145 0.0850  -0.1271 -0.0461 174 VAL A CB  
1001  C CG1 . VAL A 174 ? 0.4647 0.2662 0.4179 0.0851  -0.1298 -0.0451 174 VAL A CG1 
1002  C CG2 . VAL A 174 ? 0.4532 0.2625 0.4013 0.0826  -0.1308 -0.0473 174 VAL A CG2 
1003  N N   . GLU A 175 ? 0.4644 0.2545 0.4258 0.0892  -0.1139 -0.0442 175 GLU A N   
1004  C CA  . GLU A 175 ? 0.4730 0.2575 0.4442 0.0923  -0.1075 -0.0419 175 GLU A CA  
1005  C C   . GLU A 175 ? 0.4794 0.2573 0.4527 0.0935  -0.0976 -0.0430 175 GLU A C   
1006  O O   . GLU A 175 ? 0.4835 0.2594 0.4668 0.0962  -0.0913 -0.0414 175 GLU A O   
1007  C CB  . GLU A 175 ? 0.4720 0.2606 0.4540 0.0941  -0.1102 -0.0390 175 GLU A CB  
1008  C CG  . GLU A 175 ? 0.4715 0.2618 0.4515 0.0932  -0.1184 -0.0377 175 GLU A CG  
1009  C CD  . GLU A 175 ? 0.4739 0.2662 0.4658 0.0951  -0.1210 -0.0343 175 GLU A CD  
1010  O OE1 . GLU A 175 ? 0.4779 0.2691 0.4820 0.0983  -0.1146 -0.0316 175 GLU A OE1 
1011  O OE2 . GLU A 175 ? 0.4730 0.2671 0.4620 0.0936  -0.1291 -0.0340 175 GLU A OE2 
1012  N N   . ASN A 176 ? 0.4741 0.2477 0.4376 0.0914  -0.0958 -0.0459 176 ASN A N   
1013  C CA  . ASN A 176 ? 0.4834 0.2476 0.4456 0.0915  -0.0861 -0.0483 176 ASN A CA  
1014  C C   . ASN A 176 ? 0.4921 0.2474 0.4496 0.0901  -0.0822 -0.0501 176 ASN A C   
1015  O O   . ASN A 176 ? 0.4906 0.2474 0.4480 0.0900  -0.0863 -0.0485 176 ASN A O   
1016  C CB  . ASN A 176 ? 0.4797 0.2459 0.4334 0.0893  -0.0878 -0.0508 176 ASN A CB  
1017  C CG  . ASN A 176 ? 0.4765 0.2466 0.4366 0.0912  -0.0859 -0.0497 176 ASN A CG  
1018  O OD1 . ASN A 176 ? 0.4852 0.2480 0.4502 0.0928  -0.0762 -0.0502 176 ASN A OD1 
1019  N ND2 . ASN A 176 ? 0.4652 0.2458 0.4257 0.0907  -0.0941 -0.0483 176 ASN A ND2 
1020  N N   . LYS A 177 ? 0.4951 0.2399 0.4484 0.0885  -0.0737 -0.0538 177 LYS A N   
1021  C CA  . LYS A 177 ? 0.5052 0.2401 0.4541 0.0862  -0.0689 -0.0567 177 LYS A CA  
1022  C C   . LYS A 177 ? 0.5077 0.2393 0.4434 0.0815  -0.0709 -0.0614 177 LYS A C   
1023  O O   . LYS A 177 ? 0.5213 0.2410 0.4523 0.0783  -0.0631 -0.0663 177 LYS A O   
1024  C CB  . LYS A 177 ? 0.5203 0.2423 0.4774 0.0877  -0.0550 -0.0579 177 LYS A CB  
1025  C CG  . LYS A 177 ? 0.5200 0.2439 0.4913 0.0928  -0.0528 -0.0520 177 LYS A CG  
1026  C CD  . LYS A 177 ? 0.5178 0.2437 0.4889 0.0930  -0.0583 -0.0494 177 LYS A CD  
1027  C CE  . LYS A 177 ? 0.5118 0.2456 0.4925 0.0971  -0.0638 -0.0431 177 LYS A CE  
1028  N NZ  . LYS A 177 ? 0.4985 0.2450 0.4776 0.0968  -0.0741 -0.0421 177 LYS A NZ  
1029  N N   . LEU A 178 ? 0.5070 0.2487 0.4371 0.0806  -0.0812 -0.0601 178 LEU A N   
1030  C CA  . LEU A 178 ? 0.5090 0.2484 0.4278 0.0765  -0.0844 -0.0633 178 LEU A CA  
1031  C C   . LEU A 178 ? 0.5124 0.2483 0.4277 0.0735  -0.0859 -0.0645 178 LEU A C   
1032  O O   . LEU A 178 ? 0.5043 0.2467 0.4230 0.0749  -0.0912 -0.0611 178 LEU A O   
1033  C CB  . LEU A 178 ? 0.4953 0.2464 0.4119 0.0770  -0.0940 -0.0606 178 LEU A CB  
1034  C CG  . LEU A 178 ? 0.4891 0.2462 0.4110 0.0800  -0.0938 -0.0586 178 LEU A CG  
1035  C CD1 . LEU A 178 ? 0.4757 0.2442 0.3963 0.0801  -0.1030 -0.0561 178 LEU A CD1 
1036  C CD2 . LEU A 178 ? 0.5020 0.2488 0.4195 0.0797  -0.0865 -0.0622 178 LEU A CD2 
1037  N N   . ASN A 179 ? 0.6265 0.3492 0.5321 0.0698  -0.0834 -0.0703 179 ASN A N   
1038  C CA  . ASN A 179 ? 0.6334 0.3505 0.5349 0.0663  -0.0848 -0.0725 179 ASN A CA  
1039  C C   . ASN A 179 ? 0.6390 0.3538 0.5280 0.0630  -0.0953 -0.0749 179 ASN A C   
1040  O O   . ASN A 179 ? 0.6443 0.3568 0.5246 0.0626  -0.0995 -0.0766 179 ASN A O   
1041  C CB  . ASN A 179 ? 0.6516 0.3541 0.5528 0.0632  -0.0728 -0.0781 179 ASN A CB  
1042  C CG  . ASN A 179 ? 0.6698 0.3603 0.5608 0.0599  -0.0679 -0.0851 179 ASN A CG  
1043  O OD1 . ASN A 179 ? 0.6675 0.3608 0.5541 0.0615  -0.0715 -0.0845 179 ASN A OD1 
1044  N ND2 . ASN A 179 ? 0.6895 0.3657 0.5760 0.0548  -0.0593 -0.0924 179 ASN A ND2 
1045  N N   . GLY A 180 ? 0.5837 0.2983 0.4722 0.0608  -0.0996 -0.0747 180 GLY A N   
1046  C CA  . GLY A 180 ? 0.5894 0.3018 0.4689 0.0575  -0.1103 -0.0761 180 GLY A CA  
1047  C C   . GLY A 180 ? 0.5724 0.2969 0.4592 0.0604  -0.1188 -0.0701 180 GLY A C   
1048  O O   . GLY A 180 ? 0.5574 0.2917 0.4538 0.0640  -0.1160 -0.0656 180 GLY A O   
1049  N N   . SER A 181 ? 0.5898 0.3125 0.4714 0.0581  -0.1290 -0.0705 181 SER A N   
1050  C CA  . SER A 181 ? 0.5760 0.3086 0.4649 0.0604  -0.1367 -0.0655 181 SER A CA  
1051  C C   . SER A 181 ? 0.5660 0.3069 0.4555 0.0640  -0.1432 -0.0624 181 SER A C   
1052  O O   . SER A 181 ? 0.5742 0.3102 0.4556 0.0639  -0.1457 -0.0643 181 SER A O   
1053  C CB  . SER A 181 ? 0.5867 0.3125 0.4732 0.0558  -0.1446 -0.0671 181 SER A CB  
1054  O OG  . SER A 181 ? 0.5936 0.3134 0.4820 0.0524  -0.1380 -0.0697 181 SER A OG  
1055  N N   . ILE A 182 ? 0.5280 0.2808 0.4263 0.0666  -0.1447 -0.0580 182 ILE A N   
1056  C CA  . ILE A 182 ? 0.5184 0.2795 0.4185 0.0690  -0.1497 -0.0556 182 ILE A CA  
1057  C C   . ILE A 182 ? 0.5279 0.2831 0.4242 0.0677  -0.1616 -0.0558 182 ILE A C   
1058  O O   . ILE A 182 ? 0.5309 0.2837 0.4309 0.0657  -0.1661 -0.0552 182 ILE A O   
1059  C CB  . ILE A 182 ? 0.5012 0.2750 0.4107 0.0700  -0.1459 -0.0521 182 ILE A CB  
1060  C CG1 . ILE A 182 ? 0.4944 0.2724 0.4068 0.0710  -0.1366 -0.0514 182 ILE A CG1 
1061  C CG2 . ILE A 182 ? 0.4930 0.2742 0.4050 0.0710  -0.1495 -0.0506 182 ILE A CG2 
1062  C CD1 . ILE A 182 ? 0.4817 0.2689 0.4002 0.0711  -0.1330 -0.0484 182 ILE A CD1 
1063  N N   . PRO A 183 ? 0.5211 0.2723 0.4102 0.0687  -0.1673 -0.0564 183 PRO A N   
1064  C CA  . PRO A 183 ? 0.5333 0.2765 0.4181 0.0669  -0.1806 -0.0561 183 PRO A CA  
1065  C C   . PRO A 183 ? 0.5216 0.2741 0.4189 0.0673  -0.1859 -0.0526 183 PRO A C   
1066  O O   . PRO A 183 ? 0.5047 0.2699 0.4105 0.0689  -0.1783 -0.0510 183 PRO A O   
1067  C CB  . PRO A 183 ? 0.5408 0.2792 0.4154 0.0686  -0.1835 -0.0567 183 PRO A CB  
1068  C CG  . PRO A 183 ? 0.5375 0.2777 0.4098 0.0700  -0.1707 -0.0589 183 PRO A CG  
1069  C CD  . PRO A 183 ? 0.5197 0.2722 0.4046 0.0710  -0.1620 -0.0573 183 PRO A CD  
1070  N N   . SER A 184 ? 0.5646 0.3096 0.4639 0.0643  -0.1972 -0.0516 184 SER A N   
1071  C CA  . SER A 184 ? 0.5554 0.3084 0.4697 0.0633  -0.2003 -0.0480 184 SER A CA  
1072  C C   . SER A 184 ? 0.5484 0.3084 0.4664 0.0646  -0.1988 -0.0459 184 SER A C   
1073  O O   . SER A 184 ? 0.5340 0.3069 0.4671 0.0651  -0.1905 -0.0411 184 SER A O   
1074  C CB  . SER A 184 ? 0.5705 0.3130 0.4886 0.0588  -0.2147 -0.0461 184 SER A CB  
1075  O OG  . SER A 184 ? 0.5899 0.3222 0.5000 0.0555  -0.2146 -0.0495 184 SER A OG  
1076  N N   . GLU A 185 ? 0.5596 0.3113 0.4640 0.0654  -0.2045 -0.0481 185 GLU A N   
1077  C CA  . GLU A 185 ? 0.5544 0.3124 0.4628 0.0665  -0.2014 -0.0446 185 GLU A CA  
1078  C C   . GLU A 185 ? 0.5343 0.3069 0.4495 0.0695  -0.1867 -0.0445 185 GLU A C   
1079  O O   . GLU A 185 ? 0.5274 0.3082 0.4496 0.0706  -0.1821 -0.0403 185 GLU A O   
1080  C CB  . GLU A 185 ? 0.5745 0.3167 0.4638 0.0667  -0.2104 -0.0468 185 GLU A CB  
1081  C CG  . GLU A 185 ? 0.5943 0.3329 0.4780 0.0605  -0.2224 -0.0416 185 GLU A CG  
1082  C CD  . GLU A 185 ? 0.6081 0.3347 0.4809 0.0561  -0.2255 -0.0477 185 GLU A CD  
1083  O OE1 . GLU A 185 ? 0.6091 0.3304 0.4794 0.0614  -0.2168 -0.0518 185 GLU A OE1 
1084  O OE2 . GLU A 185 ? 0.6179 0.3515 0.4887 0.0452  -0.2313 -0.0458 185 GLU A OE2 
1085  N N   . ILE A 186 ? 0.5245 0.3016 0.4390 0.0704  -0.1789 -0.0471 186 ILE A N   
1086  C CA  . ILE A 186 ? 0.5072 0.2970 0.4287 0.0717  -0.1663 -0.0457 186 ILE A CA  
1087  C C   . ILE A 186 ? 0.4963 0.2956 0.4324 0.0711  -0.1603 -0.0406 186 ILE A C   
1088  O O   . ILE A 186 ? 0.4859 0.2935 0.4278 0.0720  -0.1523 -0.0381 186 ILE A O   
1089  C CB  . ILE A 186 ? 0.5020 0.2939 0.4211 0.0720  -0.1598 -0.0474 186 ILE A CB  
1090  C CG1 . ILE A 186 ? 0.5132 0.2964 0.4207 0.0733  -0.1626 -0.0504 186 ILE A CG1 
1091  C CG2 . ILE A 186 ? 0.4873 0.2897 0.4124 0.0724  -0.1495 -0.0458 186 ILE A CG2 
1092  C CD1 . ILE A 186 ? 0.5163 0.2979 0.4183 0.0752  -0.1628 -0.0512 186 ILE A CD1 
1093  N N   . GLY A 187 ? 0.5122 0.3100 0.4551 0.0697  -0.1636 -0.0381 187 GLY A N   
1094  C CA  . GLY A 187 ? 0.5042 0.3106 0.4622 0.0700  -0.1574 -0.0315 187 GLY A CA  
1095  C C   . GLY A 187 ? 0.5024 0.3154 0.4687 0.0712  -0.1567 -0.0253 187 GLY A C   
1096  O O   . GLY A 187 ? 0.4974 0.3187 0.4770 0.0724  -0.1496 -0.0187 187 GLY A O   
1097  N N   . ARG A 188 ? 0.5151 0.3244 0.4738 0.0714  -0.1631 -0.0265 188 ARG A N   
1098  C CA  . ARG A 188 ? 0.5135 0.3307 0.4797 0.0728  -0.1617 -0.0194 188 ARG A CA  
1099  C C   . ARG A 188 ? 0.5043 0.3280 0.4723 0.0750  -0.1506 -0.0194 188 ARG A C   
1100  O O   . ARG A 188 ? 0.4991 0.3305 0.4754 0.0767  -0.1472 -0.0126 188 ARG A O   
1101  C CB  . ARG A 188 ? 0.5303 0.3405 0.4856 0.0721  -0.1728 -0.0196 188 ARG A CB  
1102  C CG  . ARG A 188 ? 0.5467 0.3525 0.5011 0.0686  -0.1855 -0.0168 188 ARG A CG  
1103  C CD  . ARG A 188 ? 0.5581 0.3599 0.5001 0.0668  -0.1958 -0.0145 188 ARG A CD  
1104  N NE  . ARG A 188 ? 0.5759 0.3774 0.5161 0.0610  -0.2085 -0.0107 188 ARG A NE  
1105  C CZ  . ARG A 188 ? 0.5829 0.3950 0.5223 0.0561  -0.2166 -0.0021 188 ARG A CZ  
1106  N NH1 . ARG A 188 ? 0.5817 0.4032 0.5217 0.0578  -0.2136 0.0039  188 ARG A NH1 
1107  N NH2 . ARG A 188 ? 0.5955 0.4105 0.5334 0.0484  -0.2277 0.0008  188 ARG A NH2 
1108  N N   . LEU A 189 ? 0.5056 0.3275 0.4672 0.0747  -0.1452 -0.0255 189 LEU A N   
1109  C CA  . LEU A 189 ? 0.4922 0.3196 0.4550 0.0758  -0.1365 -0.0256 189 LEU A CA  
1110  C C   . LEU A 189 ? 0.4825 0.3167 0.4565 0.0763  -0.1269 -0.0208 189 LEU A C   
1111  O O   . LEU A 189 ? 0.4807 0.3153 0.4532 0.0755  -0.1215 -0.0231 189 LEU A O   
1112  C CB  . LEU A 189 ? 0.4937 0.3179 0.4463 0.0750  -0.1360 -0.0323 189 LEU A CB  
1113  C CG  . LEU A 189 ? 0.4992 0.3146 0.4394 0.0754  -0.1440 -0.0372 189 LEU A CG  
1114  C CD1 . LEU A 189 ? 0.4973 0.3132 0.4323 0.0754  -0.1405 -0.0410 189 LEU A CD1 
1115  C CD2 . LEU A 189 ? 0.5061 0.3192 0.4442 0.0772  -0.1472 -0.0354 189 LEU A CD2 
1116  N N   . THR A 190 ? 0.4707 0.3101 0.4562 0.0780  -0.1250 -0.0131 190 THR A N   
1117  C CA  . THR A 190 ? 0.4657 0.3096 0.4624 0.0795  -0.1154 -0.0075 190 THR A CA  
1118  C C   . THR A 190 ? 0.4645 0.3076 0.4595 0.0804  -0.1093 -0.0100 190 THR A C   
1119  O O   . THR A 190 ? 0.4673 0.3082 0.4654 0.0813  -0.1038 -0.0093 190 THR A O   
1120  C CB  . THR A 190 ? 0.4702 0.3206 0.4804 0.0821  -0.1147 0.0024  190 THR A CB  
1121  O OG1 . THR A 190 ? 0.4695 0.3236 0.4796 0.0834  -0.1162 0.0050  190 THR A OG1 
1122  C CG2 . THR A 190 ? 0.4795 0.3296 0.4930 0.0810  -0.1241 0.0049  190 THR A CG2 
1123  N N   . LYS A 191 ? 0.4154 0.2587 0.4050 0.0803  -0.1108 -0.0129 191 LYS A N   
1124  C CA  . LYS A 191 ? 0.4144 0.2565 0.4030 0.0811  -0.1071 -0.0153 191 LYS A CA  
1125  C C   . LYS A 191 ? 0.4147 0.2527 0.3925 0.0792  -0.1104 -0.0229 191 LYS A C   
1126  O O   . LYS A 191 ? 0.4146 0.2516 0.3911 0.0795  -0.1087 -0.0249 191 LYS A O   
1127  C CB  . LYS A 191 ? 0.4135 0.2590 0.4050 0.0827  -0.1059 -0.0127 191 LYS A CB  
1128  C CG  . LYS A 191 ? 0.4137 0.2642 0.4178 0.0858  -0.1005 -0.0036 191 LYS A CG  
1129  C CD  . LYS A 191 ? 0.4135 0.2668 0.4200 0.0877  -0.0985 -0.0009 191 LYS A CD  
1130  C CE  . LYS A 191 ? 0.4148 0.2746 0.4335 0.0912  -0.0942 0.0099  191 LYS A CE  
1131  N NZ  . LYS A 191 ? 0.4154 0.2781 0.4360 0.0935  -0.0924 0.0134  191 LYS A NZ  
1132  N N   . VAL A 192 ? 0.4329 0.2684 0.4036 0.0775  -0.1152 -0.0265 192 VAL A N   
1133  C CA  . VAL A 192 ? 0.4339 0.2664 0.3957 0.0764  -0.1184 -0.0321 192 VAL A CA  
1134  C C   . VAL A 192 ? 0.4357 0.2654 0.3964 0.0763  -0.1162 -0.0325 192 VAL A C   
1135  O O   . VAL A 192 ? 0.4370 0.2655 0.4018 0.0767  -0.1127 -0.0296 192 VAL A O   
1136  C CB  . VAL A 192 ? 0.4357 0.2661 0.3910 0.0751  -0.1231 -0.0348 192 VAL A CB  
1137  C CG1 . VAL A 192 ? 0.4375 0.2653 0.3925 0.0742  -0.1232 -0.0343 192 VAL A CG1 
1138  C CG2 . VAL A 192 ? 0.4388 0.2678 0.3874 0.0750  -0.1258 -0.0390 192 VAL A CG2 
1139  N N   . THR A 193 ? 0.4312 0.2594 0.3869 0.0762  -0.1178 -0.0356 193 THR A N   
1140  C CA  . THR A 193 ? 0.4351 0.2590 0.3870 0.0762  -0.1169 -0.0363 193 THR A CA  
1141  C C   . THR A 193 ? 0.4381 0.2593 0.3817 0.0754  -0.1219 -0.0395 193 THR A C   
1142  O O   . THR A 193 ? 0.4427 0.2592 0.3818 0.0754  -0.1214 -0.0394 193 THR A O   
1143  C CB  . THR A 193 ? 0.4360 0.2592 0.3898 0.0769  -0.1147 -0.0362 193 THR A CB  
1144  O OG1 . THR A 193 ? 0.4333 0.2598 0.3877 0.0767  -0.1178 -0.0382 193 THR A OG1 
1145  C CG2 . THR A 193 ? 0.4352 0.2592 0.3979 0.0782  -0.1076 -0.0319 193 THR A CG2 
1146  N N   . GLU A 194 ? 0.4419 0.2651 0.3838 0.0752  -0.1258 -0.0418 194 GLU A N   
1147  C CA  . GLU A 194 ? 0.4476 0.2684 0.3838 0.0750  -0.1298 -0.0439 194 GLU A CA  
1148  C C   . GLU A 194 ? 0.4482 0.2703 0.3843 0.0749  -0.1312 -0.0447 194 GLU A C   
1149  O O   . GLU A 194 ? 0.4415 0.2664 0.3806 0.0752  -0.1307 -0.0449 194 GLU A O   
1150  C CB  . GLU A 194 ? 0.4468 0.2672 0.3826 0.0753  -0.1325 -0.0453 194 GLU A CB  
1151  C CG  . GLU A 194 ? 0.4505 0.2686 0.3829 0.0755  -0.1363 -0.0468 194 GLU A CG  
1152  C CD  . GLU A 194 ? 0.4566 0.2730 0.3891 0.0756  -0.1396 -0.0477 194 GLU A CD  
1153  O OE1 . GLU A 194 ? 0.4628 0.2747 0.3903 0.0754  -0.1409 -0.0474 194 GLU A OE1 
1154  O OE2 . GLU A 194 ? 0.4562 0.2750 0.3940 0.0760  -0.1407 -0.0484 194 GLU A OE2 
1155  N N   . ILE A 195 ? 0.4216 0.2406 0.3538 0.0747  -0.1324 -0.0451 195 ILE A N   
1156  C CA  . ILE A 195 ? 0.4227 0.2410 0.3538 0.0748  -0.1333 -0.0459 195 ILE A CA  
1157  C C   . ILE A 195 ? 0.4274 0.2423 0.3556 0.0754  -0.1348 -0.0467 195 ILE A C   
1158  O O   . ILE A 195 ? 0.4308 0.2423 0.3558 0.0752  -0.1349 -0.0462 195 ILE A O   
1159  C CB  . ILE A 195 ? 0.4227 0.2400 0.3539 0.0739  -0.1327 -0.0449 195 ILE A CB  
1160  C CG1 . ILE A 195 ? 0.4188 0.2393 0.3546 0.0735  -0.1313 -0.0434 195 ILE A CG1 
1161  C CG2 . ILE A 195 ? 0.4261 0.2406 0.3548 0.0740  -0.1336 -0.0459 195 ILE A CG2 
1162  C CD1 . ILE A 195 ? 0.4192 0.2386 0.3573 0.0724  -0.1312 -0.0416 195 ILE A CD1 
1163  N N   . ALA A 196 ? 0.4251 0.2402 0.3550 0.0764  -0.1351 -0.0476 196 ALA A N   
1164  C CA  . ALA A 196 ? 0.4303 0.2418 0.3597 0.0774  -0.1358 -0.0478 196 ALA A CA  
1165  C C   . ALA A 196 ? 0.4332 0.2426 0.3641 0.0784  -0.1332 -0.0481 196 ALA A C   
1166  O O   . ALA A 196 ? 0.4325 0.2432 0.3668 0.0794  -0.1314 -0.0484 196 ALA A O   
1167  C CB  . ALA A 196 ? 0.4308 0.2433 0.3635 0.0780  -0.1376 -0.0481 196 ALA A CB  
1168  N N   . ILE A 197 ? 0.4431 0.2481 0.3712 0.0784  -0.1322 -0.0479 197 ILE A N   
1169  C CA  . ILE A 197 ? 0.4485 0.2489 0.3772 0.0793  -0.1287 -0.0483 197 ILE A CA  
1170  C C   . ILE A 197 ? 0.4553 0.2503 0.3848 0.0803  -0.1270 -0.0477 197 ILE A C   
1171  O O   . ILE A 197 ? 0.4614 0.2507 0.3904 0.0805  -0.1233 -0.0481 197 ILE A O   
1172  C CB  . ILE A 197 ? 0.4491 0.2475 0.3740 0.0779  -0.1281 -0.0488 197 ILE A CB  
1173  C CG1 . ILE A 197 ? 0.4421 0.2460 0.3667 0.0767  -0.1307 -0.0484 197 ILE A CG1 
1174  C CG2 . ILE A 197 ? 0.4553 0.2484 0.3797 0.0785  -0.1239 -0.0500 197 ILE A CG2 
1175  C CD1 . ILE A 197 ? 0.4427 0.2448 0.3648 0.0750  -0.1316 -0.0483 197 ILE A CD1 
1176  N N   . TYR A 198 ? 0.4699 0.2656 0.4003 0.0808  -0.1295 -0.0468 198 TYR A N   
1177  C CA  . TYR A 198 ? 0.4771 0.2672 0.4081 0.0819  -0.1283 -0.0457 198 TYR A CA  
1178  C C   . TYR A 198 ? 0.4825 0.2694 0.4209 0.0842  -0.1241 -0.0450 198 TYR A C   
1179  O O   . TYR A 198 ? 0.4806 0.2699 0.4237 0.0850  -0.1222 -0.0455 198 TYR A O   
1180  C CB  . TYR A 198 ? 0.4780 0.2680 0.4064 0.0818  -0.1327 -0.0447 198 TYR A CB  
1181  C CG  . TYR A 198 ? 0.4761 0.2694 0.4085 0.0822  -0.1360 -0.0447 198 TYR A CG  
1182  C CD1 . TYR A 198 ? 0.4812 0.2724 0.4205 0.0842  -0.1359 -0.0432 198 TYR A CD1 
1183  C CD2 . TYR A 198 ? 0.4698 0.2680 0.4006 0.0808  -0.1387 -0.0459 198 TYR A CD2 
1184  C CE1 . TYR A 198 ? 0.4800 0.2740 0.4244 0.0844  -0.1393 -0.0430 198 TYR A CE1 
1185  C CE2 . TYR A 198 ? 0.4688 0.2692 0.4038 0.0809  -0.1415 -0.0461 198 TYR A CE2 
1186  C CZ  . TYR A 198 ? 0.4738 0.2722 0.4156 0.0825  -0.1422 -0.0447 198 TYR A CZ  
1187  O OH  . TYR A 198 ? 0.4732 0.2738 0.4206 0.0825  -0.1455 -0.0447 198 TYR A OH  
1188  N N   . ASP A 199 ? 0.4678 0.2486 0.4080 0.0856  -0.1214 -0.0436 199 ASP A N   
1189  C CA  . ASP A 199 ? 0.4751 0.2510 0.4238 0.0882  -0.1154 -0.0422 199 ASP A CA  
1190  C C   . ASP A 199 ? 0.4775 0.2500 0.4269 0.0880  -0.1086 -0.0443 199 ASP A C   
1191  O O   . ASP A 199 ? 0.4783 0.2509 0.4334 0.0894  -0.1048 -0.0444 199 ASP A O   
1192  C CB  . ASP A 199 ? 0.4743 0.2536 0.4315 0.0901  -0.1174 -0.0402 199 ASP A CB  
1193  C CG  . ASP A 199 ? 0.4834 0.2572 0.4512 0.0936  -0.1120 -0.0369 199 ASP A CG  
1194  O OD1 . ASP A 199 ? 0.4904 0.2571 0.4597 0.0946  -0.1044 -0.0369 199 ASP A OD1 
1195  O OD2 . ASP A 199 ? 0.4845 0.2605 0.4599 0.0953  -0.1149 -0.0340 199 ASP A OD2 
1196  N N   . ASN A 200 ? 0.4841 0.2523 0.4271 0.0861  -0.1068 -0.0461 200 ASN A N   
1197  C CA  . ASN A 200 ? 0.4888 0.2516 0.4294 0.0849  -0.1010 -0.0490 200 ASN A CA  
1198  C C   . ASN A 200 ? 0.4980 0.2516 0.4360 0.0835  -0.0962 -0.0503 200 ASN A C   
1199  O O   . ASN A 200 ? 0.5009 0.2522 0.4410 0.0845  -0.0960 -0.0483 200 ASN A O   
1200  C CB  . ASN A 200 ? 0.4810 0.2497 0.4151 0.0826  -0.1059 -0.0505 200 ASN A CB  
1201  C CG  . ASN A 200 ? 0.4775 0.2500 0.4145 0.0838  -0.1055 -0.0506 200 ASN A CG  
1202  O OD1 . ASN A 200 ? 0.4841 0.2507 0.4211 0.0840  -0.0991 -0.0524 200 ASN A OD1 
1203  N ND2 . ASN A 200 ? 0.4685 0.2498 0.4078 0.0843  -0.1112 -0.0490 200 ASN A ND2 
1204  N N   . LEU A 201 ? 0.4638 0.2111 0.3970 0.0809  -0.0921 -0.0539 201 LEU A N   
1205  C CA  . LEU A 201 ? 0.4740 0.2114 0.4045 0.0784  -0.0868 -0.0565 201 LEU A CA  
1206  C C   . LEU A 201 ? 0.4716 0.2102 0.3941 0.0743  -0.0916 -0.0586 201 LEU A C   
1207  O O   . LEU A 201 ? 0.4818 0.2113 0.4001 0.0705  -0.0871 -0.0628 201 LEU A O   
1208  C CB  . LEU A 201 ? 0.4883 0.2135 0.4208 0.0777  -0.0755 -0.0602 201 LEU A CB  
1209  C CG  . LEU A 201 ? 0.4923 0.2150 0.4356 0.0821  -0.0688 -0.0575 201 LEU A CG  
1210  C CD1 . LEU A 201 ? 0.5073 0.2171 0.4527 0.0810  -0.0560 -0.0620 201 LEU A CD1 
1211  C CD2 . LEU A 201 ? 0.4939 0.2156 0.4435 0.0847  -0.0685 -0.0535 201 LEU A CD2 
1212  N N   . LEU A 202 ? 0.4942 0.2432 0.4152 0.0746  -0.1003 -0.0560 202 LEU A N   
1213  C CA  . LEU A 202 ? 0.4912 0.2419 0.4072 0.0714  -0.1049 -0.0570 202 LEU A CA  
1214  C C   . LEU A 202 ? 0.4964 0.2418 0.4122 0.0690  -0.1034 -0.0576 202 LEU A C   
1215  O O   . LEU A 202 ? 0.4975 0.2417 0.4166 0.0707  -0.1017 -0.0556 202 LEU A O   
1216  C CB  . LEU A 202 ? 0.4776 0.2400 0.3942 0.0726  -0.1128 -0.0539 202 LEU A CB  
1217  C CG  . LEU A 202 ? 0.4716 0.2401 0.3892 0.0746  -0.1145 -0.0534 202 LEU A CG  
1218  C CD1 . LEU A 202 ? 0.4601 0.2384 0.3781 0.0746  -0.1211 -0.0513 202 LEU A CD1 
1219  C CD2 . LEU A 202 ? 0.4791 0.2415 0.3924 0.0733  -0.1117 -0.0564 202 LEU A CD2 
1220  N N   . THR A 203 ? 0.5202 0.2596 0.4302 0.0657  -0.1068 -0.0608 203 THR A N   
1221  C CA  . THR A 203 ? 0.5278 0.2606 0.4374 0.0628  -0.1062 -0.0622 203 THR A CA  
1222  C C   . THR A 203 ? 0.5259 0.2611 0.4334 0.0613  -0.1161 -0.0617 203 THR A C   
1223  O O   . THR A 203 ? 0.5178 0.2604 0.4247 0.0630  -0.1228 -0.0597 203 THR A O   
1224  C CB  . THR A 203 ? 0.5465 0.2650 0.4514 0.0587  -0.1002 -0.0684 203 THR A CB  
1225  O OG1 . THR A 203 ? 0.5564 0.2698 0.4517 0.0555  -0.1056 -0.0727 203 THR A OG1 
1226  C CG2 . THR A 203 ? 0.5497 0.2646 0.4589 0.0605  -0.0893 -0.0689 203 THR A CG2 
1227  N N   . GLY A 204 ? 0.5810 0.3097 0.4887 0.0581  -0.1166 -0.0632 204 GLY A N   
1228  C CA  . GLY A 204 ? 0.5814 0.3109 0.4894 0.0564  -0.1259 -0.0626 204 GLY A CA  
1229  C C   . GLY A 204 ? 0.5660 0.3064 0.4810 0.0597  -0.1276 -0.0572 204 GLY A C   
1230  O O   . GLY A 204 ? 0.5591 0.3061 0.4770 0.0625  -0.1219 -0.0542 204 GLY A O   
1231  N N   . PRO A 205 ? 0.5554 0.2967 0.4734 0.0586  -0.1352 -0.0561 205 PRO A N   
1232  C CA  . PRO A 205 ? 0.5431 0.2932 0.4681 0.0608  -0.1345 -0.0515 205 PRO A CA  
1233  C C   . PRO A 205 ? 0.5318 0.2917 0.4567 0.0634  -0.1374 -0.0496 205 PRO A C   
1234  O O   . PRO A 205 ? 0.5336 0.2934 0.4538 0.0638  -0.1421 -0.0512 205 PRO A O   
1235  C CB  . PRO A 205 ? 0.5497 0.2952 0.4803 0.0582  -0.1411 -0.0514 205 PRO A CB  
1236  C CG  . PRO A 205 ? 0.5623 0.3002 0.4873 0.0550  -0.1507 -0.0552 205 PRO A CG  
1237  C CD  . PRO A 205 ? 0.5688 0.3016 0.4847 0.0543  -0.1444 -0.0591 205 PRO A CD  
1238  N N   . ILE A 206 ? 0.5335 0.3007 0.4632 0.0648  -0.1334 -0.0461 206 ILE A N   
1239  C CA  . ILE A 206 ? 0.5239 0.2996 0.4552 0.0661  -0.1353 -0.0445 206 ILE A CA  
1240  C C   . ILE A 206 ? 0.5272 0.3019 0.4633 0.0652  -0.1437 -0.0440 206 ILE A C   
1241  O O   . ILE A 206 ? 0.5316 0.3026 0.4741 0.0639  -0.1446 -0.0427 206 ILE A O   
1242  C CB  . ILE A 206 ? 0.5151 0.2964 0.4492 0.0672  -0.1276 -0.0413 206 ILE A CB  
1243  C CG1 . ILE A 206 ? 0.5142 0.2956 0.4435 0.0682  -0.1230 -0.0416 206 ILE A CG1 
1244  C CG2 . ILE A 206 ? 0.5068 0.2956 0.4438 0.0679  -0.1282 -0.0398 206 ILE A CG2 
1245  C CD1 . ILE A 206 ? 0.5157 0.2957 0.4431 0.0698  -0.1201 -0.0398 206 ILE A CD1 
1246  N N   . PRO A 207 ? 0.5466 0.3234 0.4808 0.0657  -0.1502 -0.0448 207 PRO A N   
1247  C CA  . PRO A 207 ? 0.5521 0.3271 0.4921 0.0646  -0.1597 -0.0436 207 PRO A CA  
1248  C C   . PRO A 207 ? 0.5435 0.3249 0.4957 0.0651  -0.1543 -0.0389 207 PRO A C   
1249  O O   . PRO A 207 ? 0.5333 0.3222 0.4870 0.0666  -0.1464 -0.0369 207 PRO A O   
1250  C CB  . PRO A 207 ? 0.5517 0.3280 0.4858 0.0656  -0.1652 -0.0450 207 PRO A CB  
1251  C CG  . PRO A 207 ? 0.5512 0.3268 0.4756 0.0668  -0.1603 -0.0477 207 PRO A CG  
1252  C CD  . PRO A 207 ? 0.5446 0.3246 0.4722 0.0671  -0.1496 -0.0464 207 PRO A CD  
1253  N N   . SER A 208 ? 0.5612 0.3387 0.5229 0.0636  -0.1581 -0.0365 208 SER A N   
1254  C CA  . SER A 208 ? 0.5554 0.3386 0.5310 0.0647  -0.1516 -0.0305 208 SER A CA  
1255  C C   . SER A 208 ? 0.5502 0.3409 0.5329 0.0658  -0.1532 -0.0266 208 SER A C   
1256  O O   . SER A 208 ? 0.5442 0.3409 0.5373 0.0676  -0.1445 -0.0210 208 SER A O   
1257  C CB  . SER A 208 ? 0.5638 0.3418 0.5513 0.0628  -0.1559 -0.0276 208 SER A CB  
1258  O OG  . SER A 208 ? 0.5796 0.3532 0.5704 0.0599  -0.1718 -0.0277 208 SER A OG  
1259  N N   . SER A 209 ? 0.5425 0.3321 0.5193 0.0650  -0.1630 -0.0289 209 SER A N   
1260  C CA  . SER A 209 ? 0.5375 0.3346 0.5194 0.0661  -0.1629 -0.0251 209 SER A CA  
1261  C C   . SER A 209 ? 0.5260 0.3295 0.5035 0.0684  -0.1508 -0.0258 209 SER A C   
1262  O O   . SER A 209 ? 0.5213 0.3312 0.5035 0.0697  -0.1484 -0.0224 209 SER A O   
1263  C CB  . SER A 209 ? 0.5472 0.3389 0.5208 0.0646  -0.1760 -0.0276 209 SER A CB  
1264  O OG  . SER A 209 ? 0.5500 0.3349 0.5061 0.0649  -0.1767 -0.0353 209 SER A OG  
1265  N N   . PHE A 210 ? 0.5208 0.3230 0.4903 0.0686  -0.1437 -0.0293 210 PHE A N   
1266  C CA  . PHE A 210 ? 0.5115 0.3191 0.4777 0.0699  -0.1342 -0.0293 210 PHE A CA  
1267  C C   . PHE A 210 ? 0.5072 0.3189 0.4839 0.0715  -0.1246 -0.0235 210 PHE A C   
1268  O O   . PHE A 210 ? 0.5038 0.3191 0.4794 0.0724  -0.1181 -0.0228 210 PHE A O   
1269  C CB  . PHE A 210 ? 0.5105 0.3157 0.4672 0.0695  -0.1305 -0.0328 210 PHE A CB  
1270  C CG  . PHE A 210 ? 0.5121 0.3168 0.4591 0.0692  -0.1348 -0.0371 210 PHE A CG  
1271  C CD1 . PHE A 210 ? 0.5165 0.3186 0.4605 0.0691  -0.1435 -0.0392 210 PHE A CD1 
1272  C CD2 . PHE A 210 ? 0.5078 0.3136 0.4490 0.0694  -0.1303 -0.0385 210 PHE A CD2 
1273  C CE1 . PHE A 210 ? 0.5187 0.3190 0.4539 0.0695  -0.1458 -0.0426 210 PHE A CE1 
1274  C CE2 . PHE A 210 ? 0.5082 0.3137 0.4432 0.0697  -0.1329 -0.0412 210 PHE A CE2 
1275  C CZ  . PHE A 210 ? 0.5136 0.3164 0.4456 0.0700  -0.1397 -0.0432 210 PHE A CZ  
1276  N N   . GLY A 211 ? 0.5056 0.3157 0.4927 0.0720  -0.1233 -0.0191 211 GLY A N   
1277  C CA  . GLY A 211 ? 0.5033 0.3162 0.5015 0.0744  -0.1133 -0.0126 211 GLY A CA  
1278  C C   . GLY A 211 ? 0.4995 0.3193 0.5051 0.0760  -0.1129 -0.0083 211 GLY A C   
1279  O O   . GLY A 211 ? 0.4969 0.3186 0.5081 0.0784  -0.1027 -0.0040 211 GLY A O   
1280  N N   . ASN A 212 ? 0.5190 0.3415 0.5241 0.0748  -0.1234 -0.0092 212 ASN A N   
1281  C CA  . ASN A 212 ? 0.5162 0.3456 0.5276 0.0764  -0.1232 -0.0046 212 ASN A CA  
1282  C C   . ASN A 212 ? 0.5097 0.3406 0.5128 0.0768  -0.1173 -0.0080 212 ASN A C   
1283  O O   . ASN A 212 ? 0.5131 0.3494 0.5215 0.0784  -0.1150 -0.0040 212 ASN A O   
1284  C CB  . ASN A 212 ? 0.5222 0.3524 0.5336 0.0746  -0.1367 -0.0043 212 ASN A CB  
1285  C CG  . ASN A 212 ? 0.5288 0.3610 0.5539 0.0738  -0.1438 0.0022  212 ASN A CG  
1286  O OD1 . ASN A 212 ? 0.5354 0.3677 0.5705 0.0749  -0.1378 0.0060  212 ASN A OD1 
1287  N ND2 . ASN A 212 ? 0.5360 0.3696 0.5619 0.0714  -0.1567 0.0043  212 ASN A ND2 
1288  N N   . LEU A 213 ? 0.4400 0.4524 0.4598 0.2189  -0.1002 0.0206  213 LEU A N   
1289  C CA  . LEU A 213 ? 0.4421 0.4196 0.4399 0.2140  -0.0959 0.0099  213 LEU A CA  
1290  C C   . LEU A 213 ? 0.4545 0.4287 0.4415 0.2250  -0.0877 0.0056  213 LEU A C   
1291  O O   . LEU A 213 ? 0.4532 0.4153 0.4302 0.2224  -0.0837 0.0012  213 LEU A O   
1292  C CB  . LEU A 213 ? 0.4296 0.3911 0.4225 0.2004  -0.0976 0.0071  213 LEU A CB  
1293  C CG  . LEU A 213 ? 0.4203 0.3842 0.4213 0.1899  -0.1065 0.0108  213 LEU A CG  
1294  C CD1 . LEU A 213 ? 0.4104 0.3603 0.4068 0.1785  -0.1076 0.0083  213 LEU A CD1 
1295  C CD2 . LEU A 213 ? 0.4228 0.3709 0.4156 0.1853  -0.1096 0.0074  213 LEU A CD2 
1296  N N   . THR A 214 ? 0.4805 0.4646 0.4681 0.2374  -0.0858 0.0067  214 THR A N   
1297  C CA  . THR A 214 ? 0.4966 0.4823 0.4739 0.2508  -0.0787 0.0037  214 THR A CA  
1298  C C   . THR A 214 ? 0.5022 0.4559 0.4570 0.2462  -0.0766 -0.0061 214 THR A C   
1299  O O   . THR A 214 ? 0.5120 0.4637 0.4562 0.2533  -0.0716 -0.0090 214 THR A O   
1300  C CB  . THR A 214 ? 0.5123 0.5104 0.4922 0.2642  -0.0779 0.0061  214 THR A CB  
1301  O OG1 . THR A 214 ? 0.5139 0.4921 0.4876 0.2585  -0.0823 0.0023  214 THR A OG1 
1302  C CG2 . THR A 214 ? 0.5074 0.5428 0.5118 0.2690  -0.0797 0.0175  214 THR A CG2 
1303  N N   . LYS A 215 ? 0.4952 0.4257 0.4427 0.2341  -0.0804 -0.0103 215 LYS A N   
1304  C CA  . LYS A 215 ? 0.4995 0.4034 0.4287 0.2279  -0.0797 -0.0176 215 LYS A CA  
1305  C C   . LYS A 215 ? 0.4863 0.3806 0.4121 0.2162  -0.0786 -0.0194 215 LYS A C   
1306  O O   . LYS A 215 ? 0.4880 0.3630 0.4007 0.2096  -0.0783 -0.0241 215 LYS A O   
1307  C CB  . LYS A 215 ? 0.4981 0.3860 0.4235 0.2196  -0.0837 -0.0195 215 LYS A CB  
1308  C CG  . LYS A 215 ? 0.5129 0.4063 0.4396 0.2308  -0.0850 -0.0184 215 LYS A CG  
1309  C CD  . LYS A 215 ? 0.5350 0.4222 0.4477 0.2435  -0.0826 -0.0226 215 LYS A CD  
1310  C CE  . LYS A 215 ? 0.5506 0.4551 0.4688 0.2600  -0.0814 -0.0195 215 LYS A CE  
1311  N NZ  . LYS A 215 ? 0.5708 0.4603 0.4761 0.2669  -0.0831 -0.0236 215 LYS A NZ  
1312  N N   . LEU A 216 ? 0.4732 0.3813 0.4115 0.2131  -0.0786 -0.0149 216 LEU A N   
1313  C CA  . LEU A 216 ? 0.4605 0.3595 0.3967 0.2017  -0.0777 -0.0161 216 LEU A CA  
1314  C C   . LEU A 216 ? 0.4695 0.3647 0.3946 0.2074  -0.0729 -0.0193 216 LEU A C   
1315  O O   . LEU A 216 ? 0.4810 0.3924 0.4073 0.2220  -0.0694 -0.0175 216 LEU A O   
1316  C CB  . LEU A 216 ? 0.4478 0.3643 0.4006 0.1991  -0.0799 -0.0099 216 LEU A CB  
1317  C CG  . LEU A 216 ? 0.4332 0.3391 0.3859 0.1851  -0.0807 -0.0103 216 LEU A CG  
1318  C CD1 . LEU A 216 ? 0.4252 0.3117 0.3718 0.1709  -0.0836 -0.0134 216 LEU A CD1 
1319  C CD2 . LEU A 216 ? 0.4249 0.3519 0.3950 0.1857  -0.0841 -0.0031 216 LEU A CD2 
1320  N N   . VAL A 217 ? 0.4783 0.3541 0.3929 0.1962  -0.0727 -0.0232 217 VAL A N   
1321  C CA  . VAL A 217 ? 0.4866 0.3568 0.3895 0.2000  -0.0693 -0.0262 217 VAL A CA  
1322  C C   . VAL A 217 ? 0.4708 0.3381 0.3774 0.1886  -0.0680 -0.0250 217 VAL A C   
1323  O O   . VAL A 217 ? 0.4752 0.3453 0.3773 0.1935  -0.0646 -0.0253 217 VAL A O   
1324  C CB  . VAL A 217 ? 0.4985 0.3492 0.3849 0.1984  -0.0711 -0.0314 217 VAL A CB  
1325  C CG1 . VAL A 217 ? 0.5147 0.3667 0.3977 0.2093  -0.0729 -0.0325 217 VAL A CG1 
1326  C CG2 . VAL A 217 ? 0.4907 0.3237 0.3704 0.1831  -0.0762 -0.0335 217 VAL A CG2 
1327  N N   . ASN A 218 ? 0.4528 0.3147 0.3666 0.1740  -0.0705 -0.0234 218 ASN A N   
1328  C CA  . ASN A 218 ? 0.4380 0.2947 0.3545 0.1616  -0.0694 -0.0224 218 ASN A CA  
1329  C C   . ASN A 218 ? 0.4255 0.2896 0.3553 0.1559  -0.0722 -0.0184 218 ASN A C   
1330  O O   . ASN A 218 ? 0.4207 0.2809 0.3523 0.1496  -0.0753 -0.0183 218 ASN A O   
1331  C CB  . ASN A 218 ? 0.4331 0.2724 0.3396 0.1485  -0.0705 -0.0253 218 ASN A CB  
1332  C CG  . ASN A 218 ? 0.4501 0.2788 0.3391 0.1542  -0.0710 -0.0297 218 ASN A CG  
1333  O OD1 . ASN A 218 ? 0.4564 0.2924 0.3456 0.1638  -0.0669 -0.0294 218 ASN A OD1 
1334  N ND2 . ASN A 218 ? 0.4584 0.2706 0.3323 0.1489  -0.0767 -0.0331 218 ASN A ND2 
1335  N N   . LEU A 219 ? 0.4149 0.2899 0.3537 0.1583  -0.0718 -0.0147 219 LEU A N   
1336  C CA  . LEU A 219 ? 0.4047 0.2857 0.3558 0.1523  -0.0765 -0.0104 219 LEU A CA  
1337  C C   . LEU A 219 ? 0.3944 0.2666 0.3454 0.1411  -0.0753 -0.0099 219 LEU A C   
1338  O O   . LEU A 219 ? 0.3954 0.2750 0.3492 0.1461  -0.0727 -0.0078 219 LEU A O   
1339  C CB  . LEU A 219 ? 0.4086 0.3165 0.3752 0.1650  -0.0795 -0.0036 219 LEU A CB  
1340  C CG  . LEU A 219 ? 0.4011 0.3173 0.3811 0.1589  -0.0881 0.0017  219 LEU A CG  
1341  C CD1 . LEU A 219 ? 0.3999 0.2984 0.3724 0.1498  -0.0916 -0.0026 219 LEU A CD1 
1342  C CD2 . LEU A 219 ? 0.4039 0.3547 0.4024 0.1705  -0.0920 0.0105  219 LEU A CD2 
1343  N N   . TYR A 220 ? 0.4238 0.2823 0.3719 0.1264  -0.0766 -0.0115 220 TYR A N   
1344  C CA  . TYR A 220 ? 0.4133 0.2636 0.3614 0.1141  -0.0749 -0.0109 220 TYR A CA  
1345  C C   . TYR A 220 ? 0.4088 0.2569 0.3630 0.1063  -0.0813 -0.0089 220 TYR A C   
1346  O O   . TYR A 220 ? 0.4060 0.2479 0.3562 0.0995  -0.0830 -0.0108 220 TYR A O   
1347  C CB  . TYR A 220 ? 0.4051 0.2452 0.3443 0.1032  -0.0695 -0.0137 220 TYR A CB  
1348  C CG  . TYR A 220 ? 0.4123 0.2515 0.3440 0.1096  -0.0661 -0.0161 220 TYR A CG  
1349  C CD1 . TYR A 220 ? 0.4219 0.2653 0.3520 0.1202  -0.0645 -0.0162 220 TYR A CD1 
1350  C CD2 . TYR A 220 ? 0.4199 0.2496 0.3388 0.1084  -0.0690 -0.0199 220 TYR A CD2 
1351  C CE1 . TYR A 220 ? 0.4322 0.2725 0.3522 0.1265  -0.0625 -0.0192 220 TYR A CE1 
1352  C CE2 . TYR A 220 ? 0.4341 0.2583 0.3409 0.1155  -0.0697 -0.0231 220 TYR A CE2 
1353  C CZ  . TYR A 220 ? 0.4384 0.2681 0.3467 0.1237  -0.0655 -0.0227 220 TYR A CZ  
1354  O OH  . TYR A 220 ? 0.4556 0.2781 0.3490 0.1315  -0.0669 -0.0265 220 TYR A OH  
1355  N N   . LEU A 221 ? 0.4226 0.2768 0.3868 0.1072  -0.0861 -0.0044 221 LEU A N   
1356  C CA  . LEU A 221 ? 0.4212 0.2714 0.3915 0.0983  -0.0952 -0.0021 221 LEU A CA  
1357  C C   . LEU A 221 ? 0.4167 0.2629 0.3928 0.0896  -0.0968 0.0014  221 LEU A C   
1358  O O   . LEU A 221 ? 0.4208 0.2701 0.4084 0.0847  -0.1079 0.0066  221 LEU A O   
1359  C CB  . LEU A 221 ? 0.4278 0.2960 0.4114 0.1069  -0.1061 0.0033  221 LEU A CB  
1360  C CG  . LEU A 221 ? 0.4336 0.3099 0.4150 0.1167  -0.1057 0.0017  221 LEU A CG  
1361  C CD1 . LEU A 221 ? 0.4370 0.3444 0.4368 0.1273  -0.1136 0.0100  221 LEU A CD1 
1362  C CD2 . LEU A 221 ? 0.4345 0.2946 0.4066 0.1080  -0.1090 -0.0029 221 LEU A CD2 
1363  N N   . PHE A 222 ? 0.4648 0.3054 0.4349 0.0858  -0.0873 -0.0004 222 PHE A N   
1364  C CA  . PHE A 222 ? 0.4718 0.3140 0.4505 0.0824  -0.0890 0.0048  222 PHE A CA  
1365  C C   . PHE A 222 ? 0.4683 0.2988 0.4495 0.0652  -0.0934 0.0058  222 PHE A C   
1366  O O   . PHE A 222 ? 0.4963 0.3308 0.4919 0.0612  -0.1050 0.0130  222 PHE A O   
1367  C CB  . PHE A 222 ? 0.4655 0.3065 0.4375 0.0846  -0.0783 0.0033  222 PHE A CB  
1368  C CG  . PHE A 222 ? 0.4510 0.2849 0.4108 0.0783  -0.0689 -0.0026 222 PHE A CG  
1369  C CD1 . PHE A 222 ? 0.4550 0.2916 0.4083 0.0864  -0.0667 -0.0059 222 PHE A CD1 
1370  C CD2 . PHE A 222 ? 0.4381 0.2677 0.3961 0.0647  -0.0628 -0.0029 222 PHE A CD2 
1371  C CE1 . PHE A 222 ? 0.4473 0.2809 0.3938 0.0799  -0.0609 -0.0086 222 PHE A CE1 
1372  C CE2 . PHE A 222 ? 0.4301 0.2615 0.3831 0.0601  -0.0557 -0.0050 222 PHE A CE2 
1373  C CZ  . PHE A 222 ? 0.4375 0.2685 0.3833 0.0677  -0.0570 -0.0081 222 PHE A CZ  
1374  N N   . ILE A 223 ? 0.4709 0.2932 0.4413 0.0545  -0.0850 0.0008  223 ILE A N   
1375  C CA  . ILE A 223 ? 0.4636 0.2806 0.4356 0.0400  -0.0862 0.0016  223 ILE A CA  
1376  C C   . ILE A 223 ? 0.4734 0.2854 0.4454 0.0368  -0.0972 0.0008  223 ILE A C   
1377  O O   . ILE A 223 ? 0.4728 0.2838 0.4354 0.0367  -0.0941 -0.0032 223 ILE A O   
1378  C CB  . ILE A 223 ? 0.4456 0.2659 0.4105 0.0331  -0.0724 -0.0007 223 ILE A CB  
1379  C CG1 . ILE A 223 ? 0.4387 0.2629 0.4049 0.0345  -0.0637 0.0007  223 ILE A CG1 
1380  C CG2 . ILE A 223 ? 0.4414 0.2606 0.4072 0.0220  -0.0721 0.0001  223 ILE A CG2 
1381  C CD1 . ILE A 223 ? 0.4305 0.2580 0.3896 0.0342  -0.0563 -0.0017 223 ILE A CD1 
1382  N N   . ASN A 224 ? 0.4458 0.2562 0.4307 0.0336  -0.1112 0.0066  224 ASN A N   
1383  C CA  . ASN A 224 ? 0.4599 0.2654 0.4474 0.0304  -0.1253 0.0077  224 ASN A CA  
1384  C C   . ASN A 224 ? 0.4895 0.3103 0.4965 0.0182  -0.1342 0.0166  224 ASN A C   
1385  O O   . ASN A 224 ? 0.4975 0.3302 0.5147 0.0127  -0.1288 0.0214  224 ASN A O   
1386  C CB  . ASN A 224 ? 0.4691 0.2829 0.4569 0.0451  -0.1296 0.0074  224 ASN A CB  
1387  C CG  . ASN A 224 ? 0.4564 0.2636 0.4265 0.0468  -0.1220 -0.0014 224 ASN A CG  
1388  O OD1 . ASN A 224 ? 0.4568 0.2554 0.4183 0.0384  -0.1235 -0.0045 224 ASN A OD1 
1389  N ND2 . ASN A 224 ? 0.4542 0.2686 0.4197 0.0579  -0.1137 -0.0039 224 ASN A ND2 
1390  N N   . SER A 225 ? 0.4406 0.2697 0.4533 0.0118  -0.1452 0.0184  225 SER A N   
1391  C CA  . SER A 225 ? 0.4503 0.3037 0.4832 -0.0028 -0.1527 0.0269  225 SER A CA  
1392  C C   . SER A 225 ? 0.4502 0.3364 0.4982 0.0012  -0.1590 0.0330  225 SER A C   
1393  O O   . SER A 225 ? 0.4547 0.3508 0.5128 -0.0106 -0.1710 0.0377  225 SER A O   
1394  C CB  . SER A 225 ? 0.4535 0.2813 0.4787 -0.0185 -0.1628 0.0243  225 SER A CB  
1395  O OG  . SER A 225 ? 0.4502 0.2597 0.4710 -0.0258 -0.1571 0.0234  225 SER A OG  
1396  N N   . LEU A 226 ? 0.4338 0.3365 0.4831 0.0182  -0.1516 0.0331  226 LEU A N   
1397  C CA  . LEU A 226 ? 0.4329 0.3699 0.4979 0.0241  -0.1558 0.0400  226 LEU A CA  
1398  C C   . LEU A 226 ? 0.4299 0.4051 0.5222 0.0133  -0.1580 0.0534  226 LEU A C   
1399  O O   . LEU A 226 ? 0.4262 0.4085 0.5256 0.0086  -0.1511 0.0576  226 LEU A O   
1400  C CB  . LEU A 226 ? 0.4274 0.3736 0.4879 0.0457  -0.1458 0.0377  226 LEU A CB  
1401  C CG  . LEU A 226 ? 0.4281 0.3398 0.4642 0.0575  -0.1440 0.0263  226 LEU A CG  
1402  C CD1 . LEU A 226 ? 0.4269 0.3501 0.4606 0.0783  -0.1362 0.0252  226 LEU A CD1 
1403  C CD2 . LEU A 226 ? 0.4378 0.3353 0.4664 0.0527  -0.1557 0.0230  226 LEU A CD2 
1404  N N   . SER A 227 ? 0.4362 0.4371 0.5445 0.0090  -0.1681 0.0614  227 SER A N   
1405  C CA  . SER A 227 ? 0.4297 0.4660 0.5658 -0.0046 -0.1737 0.0760  227 SER A CA  
1406  C C   . SER A 227 ? 0.4203 0.5022 0.5771 0.0063  -0.1720 0.0874  227 SER A C   
1407  O O   . SER A 227 ? 0.4213 0.5050 0.5698 0.0239  -0.1674 0.0828  227 SER A O   
1408  C CB  . SER A 227 ? 0.4321 0.4547 0.5702 -0.0253 -0.1912 0.0773  227 SER A CB  
1409  O OG  . SER A 227 ? 0.4355 0.4847 0.5988 -0.0414 -0.1967 0.0911  227 SER A OG  
1410  N N   . GLY A 228 ? 0.4286 0.5484 0.6134 -0.0043 -0.1758 0.1032  228 GLY A N   
1411  C CA  . GLY A 228 ? 0.4171 0.5849 0.6256 0.0041  -0.1749 0.1171  228 GLY A CA  
1412  C C   . GLY A 228 ? 0.4108 0.6008 0.6202 0.0259  -0.1570 0.1190  228 GLY A C   
1413  O O   . GLY A 228 ? 0.4192 0.5876 0.6112 0.0339  -0.1456 0.1097  228 GLY A O   
1414  N N   . SER A 229 ? 0.3951 0.6289 0.6247 0.0362  -0.1549 0.1318  229 SER A N   
1415  C CA  . SER A 229 ? 0.3907 0.6499 0.6219 0.0587  -0.1384 0.1351  229 SER A CA  
1416  C C   . SER A 229 ? 0.4009 0.6335 0.6053 0.0805  -0.1317 0.1196  229 SER A C   
1417  O O   . SER A 229 ? 0.4102 0.6157 0.6009 0.0794  -0.1403 0.1100  229 SER A O   
1418  C CB  . SER A 229 ? 0.3896 0.7067 0.6523 0.0633  -0.1380 0.1556  229 SER A CB  
1419  O OG  . SER A 229 ? 0.3863 0.7290 0.6758 0.0419  -0.1455 0.1717  229 SER A OG  
1420  N N   . ILE A 230 ? 0.3877 0.6280 0.5843 0.1007  -0.1169 0.1177  230 ILE A N   
1421  C CA  . ILE A 230 ? 0.3959 0.6120 0.5676 0.1227  -0.1106 0.1041  230 ILE A CA  
1422  C C   . ILE A 230 ? 0.3985 0.6445 0.5815 0.1374  -0.1120 0.1111  230 ILE A C   
1423  O O   . ILE A 230 ? 0.3974 0.6901 0.6030 0.1436  -0.1073 0.1266  230 ILE A O   
1424  C CB  . ILE A 230 ? 0.3971 0.6080 0.5545 0.1388  -0.0957 0.0991  230 ILE A CB  
1425  C CG1 . ILE A 230 ? 0.4033 0.5967 0.5574 0.1222  -0.0942 0.0972  230 ILE A CG1 
1426  C CG2 . ILE A 230 ? 0.4025 0.5773 0.5309 0.1576  -0.0921 0.0830  230 ILE A CG2 
1427  C CD1 . ILE A 230 ? 0.4062 0.5838 0.5407 0.1361  -0.0815 0.0894  230 ILE A CD1 
1428  N N   . PRO A 231 ? 0.3777 0.6001 0.5467 0.1434  -0.1181 0.1015  231 PRO A N   
1429  C CA  . PRO A 231 ? 0.3829 0.6330 0.5623 0.1580  -0.1195 0.1082  231 PRO A CA  
1430  C C   . PRO A 231 ? 0.3896 0.6582 0.5656 0.1822  -0.1040 0.1093  231 PRO A C   
1431  O O   . PRO A 231 ? 0.3950 0.6349 0.5469 0.1948  -0.0950 0.0968  231 PRO A O   
1432  C CB  . PRO A 231 ? 0.3887 0.5992 0.5466 0.1607  -0.1270 0.0941  231 PRO A CB  
1433  C CG  . PRO A 231 ? 0.3857 0.5556 0.5292 0.1413  -0.1331 0.0841  231 PRO A CG  
1434  C CD  . PRO A 231 ? 0.3799 0.5504 0.5235 0.1373  -0.1239 0.0851  231 PRO A CD  
1435  N N   . SER A 232 ? 0.3982 0.7078 0.5950 0.1847  -0.0999 0.1223  232 SER A N   
1436  C CA  . SER A 232 ? 0.4105 0.7345 0.6012 0.2049  -0.0839 0.1225  232 SER A CA  
1437  C C   . SER A 232 ? 0.4239 0.7163 0.5895 0.2216  -0.0803 0.1077  232 SER A C   
1438  O O   . SER A 232 ? 0.4359 0.7204 0.5841 0.2380  -0.0677 0.1014  232 SER A O   
1439  C CB  . SER A 232 ? 0.4151 0.7886 0.6326 0.2040  -0.0811 0.1404  232 SER A CB  
1440  O OG  . SER A 232 ? 0.4040 0.8018 0.6474 0.1818  -0.0900 0.1544  232 SER A OG  
1441  N N   . GLU A 233 ? 0.4281 0.7015 0.5906 0.2166  -0.0915 0.1024  233 GLU A N   
1442  C CA  . GLU A 233 ? 0.4405 0.6833 0.5810 0.2292  -0.0887 0.0896  233 GLU A CA  
1443  C C   . GLU A 233 ? 0.4438 0.6431 0.5551 0.2339  -0.0828 0.0739  233 GLU A C   
1444  O O   . GLU A 233 ? 0.4575 0.6352 0.5493 0.2455  -0.0767 0.0643  233 GLU A O   
1445  C CB  . GLU A 233 ? 0.4382 0.6680 0.5813 0.2203  -0.1024 0.0877  233 GLU A CB  
1446  C CG  . GLU A 233 ? 0.4398 0.7076 0.6081 0.2169  -0.1088 0.1013  233 GLU A CG  
1447  C CD  . GLU A 233 ? 0.4286 0.7276 0.6220 0.1995  -0.1169 0.1151  233 GLU A CD  
1448  O OE1 . GLU A 233 ? 0.4181 0.7006 0.6085 0.1859  -0.1247 0.1125  233 GLU A OE1 
1449  O OE2 . GLU A 233 ? 0.4318 0.7709 0.6475 0.1984  -0.1154 0.1292  233 GLU A OE2 
1450  N N   . ILE A 234 ? 0.4251 0.6107 0.5330 0.2239  -0.0851 0.0717  234 ILE A N   
1451  C CA  . ILE A 234 ? 0.4285 0.5728 0.5095 0.2261  -0.0799 0.0576  234 ILE A CA  
1452  C C   . ILE A 234 ? 0.4426 0.5908 0.5108 0.2420  -0.0661 0.0547  234 ILE A C   
1453  O O   . ILE A 234 ? 0.4540 0.5686 0.4971 0.2477  -0.0618 0.0422  234 ILE A O   
1454  C CB  . ILE A 234 ? 0.4143 0.5473 0.4965 0.2124  -0.0850 0.0576  234 ILE A CB  
1455  C CG1 . ILE A 234 ? 0.4079 0.5149 0.4866 0.1987  -0.0980 0.0530  234 ILE A CG1 
1456  C CG2 . ILE A 234 ? 0.4184 0.5222 0.4781 0.2160  -0.0765 0.0474  234 ILE A CG2 
1457  C CD1 . ILE A 234 ? 0.3989 0.4811 0.4701 0.1862  -0.1027 0.0486  234 ILE A CD1 
1458  N N   . GLY A 235 ? 0.4684 0.6581 0.5529 0.2486  -0.0593 0.0668  235 GLY A N   
1459  C CA  . GLY A 235 ? 0.4851 0.6813 0.5560 0.2653  -0.0461 0.0651  235 GLY A CA  
1460  C C   . GLY A 235 ? 0.5053 0.6916 0.5611 0.2797  -0.0424 0.0587  235 GLY A C   
1461  O O   . GLY A 235 ? 0.5235 0.7052 0.5605 0.2941  -0.0328 0.0541  235 GLY A O   
1462  N N   . ASN A 236 ? 0.4739 0.6569 0.5366 0.2762  -0.0502 0.0586  236 ASN A N   
1463  C CA  . ASN A 236 ? 0.4925 0.6694 0.5442 0.2891  -0.0474 0.0543  236 ASN A CA  
1464  C C   . ASN A 236 ? 0.4973 0.6272 0.5265 0.2853  -0.0524 0.0397  236 ASN A C   
1465  O O   . ASN A 236 ? 0.5090 0.6323 0.5328 0.2917  -0.0534 0.0369  236 ASN A O   
1466  C CB  . ASN A 236 ? 0.4900 0.7012 0.5669 0.2889  -0.0517 0.0665  236 ASN A CB  
1467  C CG  . ASN A 236 ? 0.4907 0.7514 0.5887 0.2942  -0.0446 0.0825  236 ASN A CG  
1468  O OD1 . ASN A 236 ? 0.4752 0.7645 0.5993 0.2816  -0.0503 0.0948  236 ASN A OD1 
1469  N ND2 . ASN A 236 ? 0.5103 0.7817 0.5966 0.3120  -0.0325 0.0831  236 ASN A ND2 
1470  N N   . LEU A 237 ? 0.5111 0.6095 0.5279 0.2741  -0.0554 0.0313  237 LEU A N   
1471  C CA  . LEU A 237 ? 0.5171 0.5731 0.5116 0.2696  -0.0584 0.0186  237 LEU A CA  
1472  C C   . LEU A 237 ? 0.5389 0.5793 0.5088 0.2820  -0.0512 0.0107  237 LEU A C   
1473  O O   . LEU A 237 ? 0.5416 0.5793 0.5020 0.2843  -0.0463 0.0088  237 LEU A O   
1474  C CB  . LEU A 237 ? 0.5013 0.5306 0.4914 0.2524  -0.0635 0.0136  237 LEU A CB  
1475  C CG  . LEU A 237 ? 0.4856 0.5142 0.4898 0.2390  -0.0730 0.0171  237 LEU A CG  
1476  C CD1 . LEU A 237 ? 0.4930 0.5191 0.4973 0.2420  -0.0764 0.0164  237 LEU A CD1 
1477  C CD2 . LEU A 237 ? 0.4727 0.5359 0.5023 0.2356  -0.0770 0.0293  237 LEU A CD2 
1478  N N   . PRO A 238 ? 0.5625 0.5923 0.5208 0.2903  -0.0513 0.0062  238 PRO A N   
1479  C CA  . PRO A 238 ? 0.5872 0.6055 0.5217 0.3040  -0.0457 -0.0001 238 PRO A CA  
1480  C C   . PRO A 238 ? 0.5905 0.5709 0.5021 0.2954  -0.0482 -0.0107 238 PRO A C   
1481  O O   . PRO A 238 ? 0.6051 0.5795 0.4995 0.3032  -0.0439 -0.0142 238 PRO A O   
1482  C CB  . PRO A 238 ? 0.6034 0.6223 0.5353 0.3139  -0.0468 -0.0006 238 PRO A CB  
1483  C CG  . PRO A 238 ? 0.5856 0.6068 0.5361 0.3019  -0.0541 0.0029  238 PRO A CG  
1484  C CD  . PRO A 238 ? 0.5608 0.5831 0.5242 0.2859  -0.0577 0.0056  238 PRO A CD  
1485  N N   . ASN A 239 ? 0.6222 0.5788 0.5335 0.2792  -0.0552 -0.0149 239 ASN A N   
1486  C CA  . ASN A 239 ? 0.6245 0.5481 0.5168 0.2692  -0.0582 -0.0232 239 ASN A CA  
1487  C C   . ASN A 239 ? 0.6056 0.5223 0.5010 0.2550  -0.0586 -0.0232 239 ASN A C   
1488  O O   . ASN A 239 ? 0.6046 0.4968 0.4871 0.2446  -0.0612 -0.0285 239 ASN A O   
1489  C CB  . ASN A 239 ? 0.6226 0.5265 0.5126 0.2598  -0.0646 -0.0265 239 ASN A CB  
1490  C CG  . ASN A 239 ? 0.6439 0.5495 0.5277 0.2736  -0.0649 -0.0275 239 ASN A CG  
1491  O OD1 . ASN A 239 ? 0.6667 0.5655 0.5331 0.2855  -0.0631 -0.0315 239 ASN A OD1 
1492  N ND2 . ASN A 239 ? 0.6379 0.5521 0.5353 0.2724  -0.0675 -0.0238 239 ASN A ND2 
1493  N N   . LEU A 240 ? 0.5527 0.4916 0.4661 0.2537  -0.0565 -0.0164 240 LEU A N   
1494  C CA  . LEU A 240 ? 0.5352 0.4675 0.4525 0.2404  -0.0571 -0.0159 240 LEU A CA  
1495  C C   . LEU A 240 ? 0.5449 0.4653 0.4446 0.2430  -0.0535 -0.0204 240 LEU A C   
1496  O O   . LEU A 240 ? 0.5616 0.4945 0.4538 0.2586  -0.0481 -0.0197 240 LEU A O   
1497  C CB  . LEU A 240 ? 0.5207 0.4829 0.4611 0.2411  -0.0562 -0.0066 240 LEU A CB  
1498  C CG  . LEU A 240 ? 0.5011 0.4551 0.4483 0.2255  -0.0590 -0.0054 240 LEU A CG  
1499  C CD1 . LEU A 240 ? 0.4905 0.4225 0.4370 0.2099  -0.0654 -0.0086 240 LEU A CD1 
1500  C CD2 . LEU A 240 ? 0.4893 0.4759 0.4595 0.2272  -0.0591 0.0052  240 LEU A CD2 
1501  N N   . ARG A 241 ? 0.5976 0.4950 0.4904 0.2278  -0.0563 -0.0243 241 ARG A N   
1502  C CA  . ARG A 241 ? 0.6048 0.4894 0.4820 0.2273  -0.0543 -0.0280 241 ARG A CA  
1503  C C   . ARG A 241 ? 0.5866 0.4722 0.4723 0.2164  -0.0530 -0.0252 241 ARG A C   
1504  O O   . ARG A 241 ? 0.5939 0.4830 0.4731 0.2220  -0.0490 -0.0250 241 ARG A O   
1505  C CB  . ARG A 241 ? 0.6117 0.4691 0.4725 0.2190  -0.0592 -0.0342 241 ARG A CB  
1506  C CG  . ARG A 241 ? 0.6538 0.5031 0.4929 0.2327  -0.0588 -0.0388 241 ARG A CG  
1507  C CD  . ARG A 241 ? 0.6568 0.4843 0.4844 0.2266  -0.0654 -0.0432 241 ARG A CD  
1508  N NE  . ARG A 241 ? 0.6817 0.5120 0.5055 0.2391  -0.0665 -0.0444 241 ARG A NE  
1509  C CZ  . ARG A 241 ? 0.6936 0.5108 0.5120 0.2359  -0.0731 -0.0469 241 ARG A CZ  
1510  N NH1 . ARG A 241 ? 0.6819 0.4831 0.4965 0.2218  -0.0797 -0.0483 241 ARG A NH1 
1511  N NH2 . ARG A 241 ? 0.7072 0.5280 0.5227 0.2485  -0.0735 -0.0477 241 ARG A NH2 
1512  N N   . GLU A 242 ? 0.5113 0.3934 0.4102 0.2013  -0.0564 -0.0230 242 GLU A N   
1513  C CA  . GLU A 242 ? 0.4946 0.3743 0.4008 0.1895  -0.0560 -0.0205 242 GLU A CA  
1514  C C   . GLU A 242 ? 0.4798 0.3742 0.4062 0.1856  -0.0584 -0.0143 242 GLU A C   
1515  O O   . GLU A 242 ? 0.4742 0.3644 0.4054 0.1792  -0.0626 -0.0144 242 GLU A O   
1516  C CB  . GLU A 242 ? 0.4855 0.3417 0.3841 0.1717  -0.0584 -0.0241 242 GLU A CB  
1517  C CG  . GLU A 242 ? 0.4999 0.3419 0.3801 0.1739  -0.0587 -0.0290 242 GLU A CG  
1518  C CD  . GLU A 242 ? 0.4880 0.3159 0.3654 0.1575  -0.0596 -0.0296 242 GLU A CD  
1519  O OE1 . GLU A 242 ? 0.4683 0.2969 0.3574 0.1440  -0.0593 -0.0265 242 GLU A OE1 
1520  O OE2 . GLU A 242 ? 0.5025 0.3184 0.3629 0.1600  -0.0617 -0.0331 242 GLU A OE2 
1521  N N   . LEU A 243 ? 0.4348 0.3476 0.3731 0.1895  -0.0565 -0.0082 243 LEU A N   
1522  C CA  . LEU A 243 ? 0.4217 0.3515 0.3805 0.1858  -0.0611 -0.0005 243 LEU A CA  
1523  C C   . LEU A 243 ? 0.4096 0.3328 0.3727 0.1748  -0.0620 0.0021  243 LEU A C   
1524  O O   . LEU A 243 ? 0.4108 0.3456 0.3751 0.1808  -0.0575 0.0054  243 LEU A O   
1525  C CB  . LEU A 243 ? 0.4255 0.3942 0.4004 0.2011  -0.0594 0.0084  243 LEU A CB  
1526  C CG  . LEU A 243 ? 0.4125 0.4067 0.4118 0.1967  -0.0666 0.0188  243 LEU A CG  
1527  C CD1 . LEU A 243 ? 0.4094 0.3868 0.4084 0.1874  -0.0747 0.0155  243 LEU A CD1 
1528  C CD2 . LEU A 243 ? 0.4156 0.4553 0.4328 0.2100  -0.0633 0.0295  243 LEU A CD2 
1529  N N   . CYS A 244 ? 0.4294 0.3348 0.3940 0.1590  -0.0672 0.0008  244 CYS A N   
1530  C CA  . CYS A 244 ? 0.4191 0.3133 0.3859 0.1462  -0.0683 0.0024  244 CYS A CA  
1531  C C   . CYS A 244 ? 0.4114 0.3121 0.3933 0.1391  -0.0778 0.0083  244 CYS A C   
1532  O O   . CYS A 244 ? 0.4077 0.2912 0.3859 0.1271  -0.0815 0.0049  244 CYS A O   
1533  C CB  . CYS A 244 ? 0.4143 0.2814 0.3669 0.1313  -0.0651 -0.0046 244 CYS A CB  
1534  S SG  . CYS A 244 ? 0.4241 0.2834 0.3596 0.1365  -0.0586 -0.0105 244 CYS A SG  
1535  N N   . LEU A 245 ? 0.4005 0.3311 0.4004 0.1437  -0.0812 0.0179  245 LEU A N   
1536  C CA  . LEU A 245 ? 0.4006 0.3464 0.4189 0.1254  -0.0875 0.0247  245 LEU A CA  
1537  C C   . LEU A 245 ? 0.4115 0.3571 0.4373 0.1072  -0.0858 0.0289  245 LEU A C   
1538  O O   . LEU A 245 ? 0.4225 0.3866 0.4661 0.0922  -0.0905 0.0365  245 LEU A O   
1539  C CB  . LEU A 245 ? 0.4106 0.4004 0.4495 0.1303  -0.0881 0.0345  245 LEU A CB  
1540  C CG  . LEU A 245 ? 0.4009 0.3952 0.4351 0.1486  -0.0897 0.0317  245 LEU A CG  
1541  C CD1 . LEU A 245 ? 0.4043 0.4468 0.4607 0.1546  -0.0883 0.0436  245 LEU A CD1 
1542  C CD2 . LEU A 245 ? 0.4023 0.3709 0.4291 0.1426  -0.0996 0.0258  245 LEU A CD2 
1543  N N   . ASP A 246 ? 0.4539 0.3783 0.4665 0.1080  -0.0801 0.0245  246 ASP A N   
1544  C CA  . ASP A 246 ? 0.4649 0.3910 0.4845 0.0927  -0.0773 0.0291  246 ASP A CA  
1545  C C   . ASP A 246 ? 0.4568 0.3613 0.4779 0.0734  -0.0848 0.0279  246 ASP A C   
1546  O O   . ASP A 246 ? 0.4438 0.3271 0.4561 0.0730  -0.0912 0.0223  246 ASP A O   
1547  C CB  . ASP A 246 ? 0.4594 0.3652 0.4626 0.0990  -0.0702 0.0242  246 ASP A CB  
1548  C CG  . ASP A 246 ? 0.4277 0.2925 0.4086 0.1057  -0.0728 0.0138  246 ASP A CG  
1549  O OD1 . ASP A 246 ? 0.4180 0.2865 0.3919 0.1153  -0.0701 0.0091  246 ASP A OD1 
1550  O OD2 . ASP A 246 ? 0.4071 0.2531 0.3821 0.0896  -0.0693 0.0106  246 ASP A OD2 
1551  N N   . ARG A 247 ? 0.4874 0.3980 0.5191 0.0577  -0.0841 0.0338  247 ARG A N   
1552  C CA  . ARG A 247 ? 0.4772 0.3641 0.5078 0.0399  -0.0901 0.0324  247 ARG A CA  
1553  C C   . ARG A 247 ? 0.4810 0.3689 0.5168 0.0337  -0.1007 0.0324  247 ARG A C   
1554  O O   . ARG A 247 ? 0.4639 0.3223 0.4859 0.0321  -0.1057 0.0254  247 ARG A O   
1555  C CB  . ARG A 247 ? 0.4472 0.2927 0.4562 0.0418  -0.0879 0.0236  247 ARG A CB  
1556  C CG  . ARG A 247 ? 0.4364 0.2753 0.4425 0.0388  -0.0803 0.0250  247 ARG A CG  
1557  C CD  . ARG A 247 ? 0.3964 0.2199 0.3840 0.0368  -0.0697 0.0157  247 ARG A CD  
1558  N NE  . ARG A 247 ? 0.3994 0.2251 0.3767 0.0502  -0.0634 0.0113  247 ARG A NE  
1559  C CZ  . ARG A 247 ? 0.3795 0.2059 0.3480 0.0476  -0.0544 0.0057  247 ARG A CZ  
1560  N NH1 . ARG A 247 ? 0.3616 0.1904 0.3304 0.0361  -0.0490 0.0044  247 ARG A NH1 
1561  N NH2 . ARG A 247 ? 0.3794 0.2077 0.3413 0.0573  -0.0516 0.0028  247 ARG A NH2 
1562  N N   . ASN A 248 ? 0.4530 0.3764 0.5091 0.0300  -0.1044 0.0413  248 ASN A N   
1563  C CA  . ASN A 248 ? 0.4552 0.3842 0.5183 0.0237  -0.1157 0.0428  248 ASN A CA  
1564  C C   . ASN A 248 ? 0.4655 0.4233 0.5528 0.0076  -0.1213 0.0547  248 ASN A C   
1565  O O   . ASN A 248 ? 0.4680 0.4358 0.5647 0.0002  -0.1165 0.0608  248 ASN A O   
1566  C CB  . ASN A 248 ? 0.4504 0.3952 0.5131 0.0404  -0.1160 0.0419  248 ASN A CB  
1567  C CG  . ASN A 248 ? 0.4393 0.3503 0.4799 0.0494  -0.1180 0.0308  248 ASN A CG  
1568  O OD1 . ASN A 248 ? 0.4386 0.3302 0.4728 0.0414  -0.1266 0.0272  248 ASN A OD1 
1569  N ND2 . ASN A 248 ? 0.4285 0.3318 0.4567 0.0664  -0.1106 0.0256  248 ASN A ND2 
1570  N N   . ASN A 249 ? 0.4631 0.4341 0.5610 0.0016  -0.1323 0.0588  249 ASN A N   
1571  C CA  . ASN A 249 ? 0.4595 0.4583 0.5820 -0.0146 -0.1405 0.0714  249 ASN A CA  
1572  C C   . ASN A 249 ? 0.4509 0.4944 0.5939 -0.0070 -0.1415 0.0822  249 ASN A C   
1573  O O   . ASN A 249 ? 0.4489 0.5105 0.6083 -0.0177 -0.1533 0.0905  249 ASN A O   
1574  C CB  . ASN A 249 ? 0.4638 0.4378 0.5817 -0.0314 -0.1553 0.0683  249 ASN A CB  
1575  C CG  . ASN A 249 ? 0.4784 0.4165 0.5828 -0.0421 -0.1545 0.0621  249 ASN A CG  
1576  O OD1 . ASN A 249 ? 0.4816 0.3832 0.5623 -0.0366 -0.1520 0.0504  249 ASN A OD1 
1577  N ND2 . ASN A 249 ? 0.4668 0.4160 0.5872 -0.0571 -0.1566 0.0709  249 ASN A ND2 
1578  N N   . LEU A 250 ? 0.4088 0.4700 0.5504 0.0122  -0.1293 0.0826  250 LEU A N   
1579  C CA  . LEU A 250 ? 0.4088 0.5108 0.5667 0.0238  -0.1282 0.0919  250 LEU A CA  
1580  C C   . LEU A 250 ? 0.4037 0.5512 0.5912 0.0160  -0.1269 0.1099  250 LEU A C   
1581  O O   . LEU A 250 ? 0.3979 0.5529 0.5884 0.0158  -0.1176 0.1136  250 LEU A O   
1582  C CB  . LEU A 250 ? 0.4087 0.5098 0.5516 0.0487  -0.1157 0.0851  250 LEU A CB  
1583  C CG  . LEU A 250 ? 0.4153 0.5003 0.5432 0.0620  -0.1190 0.0758  250 LEU A CG  
1584  C CD1 . LEU A 250 ? 0.4194 0.4604 0.5292 0.0515  -0.1278 0.0644  250 LEU A CD1 
1585  C CD2 . LEU A 250 ? 0.4172 0.4956 0.5283 0.0854  -0.1071 0.0685  250 LEU A CD2 
1586  N N   . THR A 251 ? 0.4015 0.5801 0.6115 0.0094  -0.1366 0.1221  251 THR A N   
1587  C CA  . THR A 251 ? 0.3813 0.6079 0.6231 0.0017  -0.1369 0.1420  251 THR A CA  
1588  C C   . THR A 251 ? 0.3801 0.6505 0.6348 0.0219  -0.1285 0.1518  251 THR A C   
1589  O O   . THR A 251 ? 0.3834 0.6446 0.6218 0.0411  -0.1236 0.1424  251 THR A O   
1590  C CB  . THR A 251 ? 0.3868 0.6184 0.6472 -0.0222 -0.1555 0.1512  251 THR A CB  
1591  O OG1 . THR A 251 ? 0.3931 0.6349 0.6577 -0.0180 -0.1645 0.1526  251 THR A OG1 
1592  C CG2 . THR A 251 ? 0.3924 0.5737 0.6337 -0.0385 -0.1643 0.1383  251 THR A CG2 
1593  N N   . GLY A 252 ? 0.3645 0.6836 0.6491 0.0182  -0.1267 0.1719  252 GLY A N   
1594  C CA  . GLY A 252 ? 0.3645 0.7305 0.6651 0.0365  -0.1195 0.1843  252 GLY A CA  
1595  C C   . GLY A 252 ? 0.3628 0.7410 0.6529 0.0603  -0.1000 0.1827  252 GLY A C   
1596  O O   . GLY A 252 ? 0.3608 0.7130 0.6323 0.0621  -0.0920 0.1726  252 GLY A O   
1597  N N   . LYS A 253 ? 0.3737 0.7926 0.6755 0.0796  -0.0926 0.1932  253 LYS A N   
1598  C CA  . LYS A 253 ? 0.3763 0.8111 0.6680 0.1051  -0.0743 0.1929  253 LYS A CA  
1599  C C   . LYS A 253 ? 0.3839 0.7789 0.6405 0.1262  -0.0689 0.1714  253 LYS A C   
1600  O O   . LYS A 253 ? 0.3865 0.7499 0.6304 0.1231  -0.0783 0.1594  253 LYS A O   
1601  C CB  . LYS A 253 ? 0.3880 0.8662 0.6944 0.1140  -0.0650 0.2071  253 LYS A CB  
1602  C CG  . LYS A 253 ? 0.3878 0.8998 0.7225 0.0937  -0.0665 0.2272  253 LYS A CG  
1603  C CD  . LYS A 253 ? 0.3998 0.9529 0.7415 0.1088  -0.0504 0.2413  253 LYS A CD  
1604  C CE  . LYS A 253 ? 0.4124 0.9783 0.7516 0.1256  -0.0475 0.2414  253 LYS A CE  
1605  N NZ  . LYS A 253 ? 0.4268 1.0313 0.7701 0.1417  -0.0313 0.2553  253 LYS A NZ  
1606  N N   . ILE A 254 ? 0.4018 0.7979 0.6418 0.1479  -0.0539 0.1670  254 ILE A N   
1607  C CA  . ILE A 254 ? 0.4122 0.7746 0.6198 0.1704  -0.0484 0.1486  254 ILE A CA  
1608  C C   . ILE A 254 ? 0.4250 0.8106 0.6351 0.1881  -0.0437 0.1521  254 ILE A C   
1609  O O   . ILE A 254 ? 0.4332 0.8548 0.6533 0.1953  -0.0330 0.1638  254 ILE A O   
1610  C CB  . ILE A 254 ? 0.4178 0.7638 0.6020 0.1840  -0.0356 0.1402  254 ILE A CB  
1611  C CG1 . ILE A 254 ? 0.4142 0.7273 0.5913 0.1620  -0.0394 0.1335  254 ILE A CG1 
1612  C CG2 . ILE A 254 ? 0.4318 0.7449 0.5836 0.2084  -0.0312 0.1227  254 ILE A CG2 
1613  C CD1 . ILE A 254 ? 0.4222 0.7219 0.5790 0.1725  -0.0278 0.1272  254 ILE A CD1 
1614  N N   . PRO A 255 ? 0.4175 0.7805 0.6167 0.1933  -0.0506 0.1418  255 PRO A N   
1615  C CA  . PRO A 255 ? 0.4314 0.8135 0.6335 0.2059  -0.0468 0.1450  255 PRO A CA  
1616  C C   . PRO A 255 ? 0.4494 0.8382 0.6338 0.2295  -0.0299 0.1423  255 PRO A C   
1617  O O   . PRO A 255 ? 0.4576 0.8126 0.6128 0.2422  -0.0244 0.1271  255 PRO A O   
1618  C CB  . PRO A 255 ? 0.4335 0.7788 0.6200 0.2081  -0.0567 0.1306  255 PRO A CB  
1619  C CG  . PRO A 255 ? 0.4182 0.7377 0.6046 0.1899  -0.0692 0.1264  255 PRO A CG  
1620  C CD  . PRO A 255 ? 0.4120 0.7302 0.5952 0.1871  -0.0621 0.1275  255 PRO A CD  
1621  N N   . SER A 256 ? 0.4222 0.8538 0.6230 0.2347  -0.0222 0.1576  256 SER A N   
1622  C CA  . SER A 256 ? 0.4434 0.8837 0.6263 0.2582  -0.0065 0.1565  256 SER A CA  
1623  C C   . SER A 256 ? 0.4599 0.8685 0.6161 0.2756  -0.0058 0.1403  256 SER A C   
1624  O O   . SER A 256 ? 0.4798 0.8784 0.6107 0.2951  0.0052  0.1331  256 SER A O   
1625  C CB  . SER A 256 ? 0.4508 0.9437 0.6575 0.2596  0.0005  0.1778  256 SER A CB  
1626  O OG  . SER A 256 ? 0.4480 0.9561 0.6756 0.2508  -0.0090 0.1854  256 SER A OG  
1627  N N   . SER A 257 ? 0.4843 0.8758 0.6444 0.2682  -0.0178 0.1347  257 SER A N   
1628  C CA  . SER A 257 ? 0.4988 0.8570 0.6347 0.2815  -0.0186 0.1195  257 SER A CA  
1629  C C   . SER A 257 ? 0.5049 0.8144 0.6071 0.2877  -0.0168 0.1003  257 SER A C   
1630  O O   . SER A 257 ? 0.5217 0.8031 0.6001 0.2998  -0.0154 0.0878  257 SER A O   
1631  C CB  . SER A 257 ? 0.4889 0.8380 0.6369 0.2695  -0.0329 0.1181  257 SER A CB  
1632  O OG  . SER A 257 ? 0.4709 0.7956 0.6201 0.2523  -0.0441 0.1126  257 SER A OG  
1633  N N   . PHE A 258 ? 0.4968 0.7951 0.5968 0.2785  -0.0175 0.0983  258 PHE A N   
1634  C CA  . PHE A 258 ? 0.5029 0.7542 0.5717 0.2820  -0.0167 0.0810  258 PHE A CA  
1635  C C   . PHE A 258 ? 0.5287 0.7728 0.5703 0.3022  -0.0049 0.0746  258 PHE A C   
1636  O O   . PHE A 258 ? 0.5401 0.7418 0.5523 0.3061  -0.0057 0.0591  258 PHE A O   
1637  C CB  . PHE A 258 ? 0.4854 0.7319 0.5596 0.2687  -0.0189 0.0826  258 PHE A CB  
1638  C CG  . PHE A 258 ? 0.4675 0.6894 0.5476 0.2509  -0.0324 0.0783  258 PHE A CG  
1639  C CD1 . PHE A 258 ? 0.4620 0.6873 0.5555 0.2439  -0.0424 0.0806  258 PHE A CD1 
1640  C CD2 . PHE A 258 ? 0.4579 0.6527 0.5289 0.2416  -0.0353 0.0721  258 PHE A CD2 
1641  C CE1 . PHE A 258 ? 0.4485 0.6503 0.5443 0.2285  -0.0550 0.0766  258 PHE A CE1 
1642  C CE2 . PHE A 258 ? 0.4443 0.6153 0.5181 0.2262  -0.0475 0.0684  258 PHE A CE2 
1643  C CZ  . PHE A 258 ? 0.4403 0.6145 0.5255 0.2200  -0.0573 0.0704  258 PHE A CZ  
1644  N N   . GLY A 259 ? 0.5430 0.8270 0.5926 0.3142  0.0052  0.0869  259 GLY A N   
1645  C CA  . GLY A 259 ? 0.5716 0.8496 0.5932 0.3350  0.0156  0.0815  259 GLY A CA  
1646  C C   . GLY A 259 ? 0.5914 0.8375 0.5897 0.3452  0.0126  0.0683  259 GLY A C   
1647  O O   . GLY A 259 ? 0.6166 0.8417 0.5842 0.3597  0.0174  0.0590  259 GLY A O   
1648  N N   . ASN A 260 ? 0.5800 0.8218 0.5917 0.3373  0.0038  0.0676  260 ASN A N   
1649  C CA  . ASN A 260 ? 0.5974 0.8110 0.5900 0.3453  0.0005  0.0565  260 ASN A CA  
1650  C C   . ASN A 260 ? 0.5992 0.7590 0.5662 0.3382  -0.0067 0.0390  260 ASN A C   
1651  O O   . ASN A 260 ? 0.6182 0.7515 0.5638 0.3455  -0.0085 0.0291  260 ASN A O   
1652  C CB  . ASN A 260 ? 0.5867 0.8158 0.6033 0.3389  -0.0065 0.0630  260 ASN A CB  
1653  C CG  . ASN A 260 ? 0.5879 0.8702 0.6299 0.3450  -0.0003 0.0813  260 ASN A CG  
1654  O OD1 . ASN A 260 ? 0.6087 0.9097 0.6416 0.3620  0.0105  0.0860  260 ASN A OD1 
1655  N ND2 . ASN A 260 ? 0.5673 0.8739 0.6406 0.3307  -0.0076 0.0923  260 ASN A ND2 
1656  N N   . LEU A 261 ? 0.6022 0.7460 0.5712 0.3235  -0.0109 0.0358  261 LEU A N   
1657  C CA  . LEU A 261 ? 0.6022 0.6970 0.5496 0.3140  -0.0179 0.0211  261 LEU A CA  
1658  C C   . LEU A 261 ? 0.6259 0.6996 0.5419 0.3248  -0.0129 0.0126  261 LEU A C   
1659  O O   . LEU A 261 ? 0.6226 0.6872 0.5306 0.3208  -0.0112 0.0105  261 LEU A O   
1660  C CB  . LEU A 261 ? 0.5761 0.6618 0.5363 0.2950  -0.0239 0.0217  261 LEU A CB  
1661  C CG  . LEU A 261 ? 0.5545 0.6564 0.5428 0.2828  -0.0315 0.0295  261 LEU A CG  
1662  C CD1 . LEU A 261 ? 0.5334 0.6573 0.5430 0.2722  -0.0326 0.0394  261 LEU A CD1 
1663  C CD2 . LEU A 261 ? 0.5492 0.6136 0.5294 0.2705  -0.0410 0.0199  261 LEU A CD2 
1664  N N   . LYS A 262 ? 0.6727 0.7382 0.5702 0.3388  -0.0114 0.0079  262 LYS A N   
1665  C CA  . LYS A 262 ? 0.7002 0.7444 0.5655 0.3504  -0.0088 -0.0002 262 LYS A CA  
1666  C C   . LYS A 262 ? 0.7023 0.6994 0.5472 0.3381  -0.0181 -0.0130 262 LYS A C   
1667  O O   . LYS A 262 ? 0.7240 0.7006 0.5423 0.3447  -0.0183 -0.0197 262 LYS A O   
1668  C CB  . LYS A 262 ? 0.7294 0.7826 0.5823 0.3704  -0.0047 0.0004  262 LYS A CB  
1669  C CG  . LYS A 262 ? 0.7500 0.8307 0.5942 0.3899  0.0065  0.0073  262 LYS A CG  
1670  C CD  . LYS A 262 ? 0.7328 0.8647 0.6092 0.3912  0.0145  0.0238  262 LYS A CD  
1671  C CE  . LYS A 262 ? 0.7554 0.9176 0.6231 0.4113  0.0267  0.0325  262 LYS A CE  
1672  N NZ  . LYS A 262 ? 0.7412 0.9574 0.6423 0.4123  0.0344  0.0510  262 LYS A NZ  
1673  N N   . ASN A 263 ? 0.7348 0.7161 0.5917 0.3203  -0.0260 -0.0155 263 ASN A N   
1674  C CA  . ASN A 263 ? 0.7338 0.6755 0.5756 0.3063  -0.0344 -0.0251 263 ASN A CA  
1675  C C   . ASN A 263 ? 0.7102 0.6417 0.5593 0.2882  -0.0367 -0.0252 263 ASN A C   
1676  O O   . ASN A 263 ? 0.7086 0.6106 0.5460 0.2757  -0.0427 -0.0316 263 ASN A O   
1677  C CB  . ASN A 263 ? 0.7296 0.6591 0.5769 0.2989  -0.0413 -0.0275 263 ASN A CB  
1678  C CG  . ASN A 263 ? 0.7598 0.6717 0.5855 0.3094  -0.0441 -0.0337 263 ASN A CG  
1679  O OD1 . ASN A 263 ? 0.7876 0.6823 0.5901 0.3150  -0.0449 -0.0391 263 ASN A OD1 
1680  N ND2 . ASN A 263 ? 0.7602 0.6760 0.5932 0.3122  -0.0462 -0.0327 263 ASN A ND2 
1681  N N   . VAL A 264 ? 0.6320 0.5887 0.5012 0.2862  -0.0324 -0.0174 264 VAL A N   
1682  C CA  . VAL A 264 ? 0.6090 0.5569 0.4874 0.2690  -0.0349 -0.0167 264 VAL A CA  
1683  C C   . VAL A 264 ? 0.6175 0.5526 0.4781 0.2700  -0.0324 -0.0202 264 VAL A C   
1684  O O   . VAL A 264 ? 0.6316 0.5843 0.4854 0.2851  -0.0252 -0.0173 264 VAL A O   
1685  C CB  . VAL A 264 ? 0.5882 0.5688 0.4953 0.2669  -0.0326 -0.0060 264 VAL A CB  
1686  C CG1 . VAL A 264 ? 0.5710 0.5471 0.4840 0.2549  -0.0329 -0.0041 264 VAL A CG1 
1687  C CG2 . VAL A 264 ? 0.5750 0.5580 0.4991 0.2585  -0.0390 -0.0037 264 VAL A CG2 
1688  N N   . THR A 265 ? 0.5977 0.5039 0.4509 0.2536  -0.0380 -0.0255 265 THR A N   
1689  C CA  . THR A 265 ? 0.6033 0.4959 0.4413 0.2516  -0.0369 -0.0283 265 THR A CA  
1690  C C   . THR A 265 ? 0.5796 0.4738 0.4320 0.2377  -0.0363 -0.0245 265 THR A C   
1691  O O   . THR A 265 ? 0.5831 0.4750 0.4272 0.2391  -0.0332 -0.0244 265 THR A O   
1692  C CB  . THR A 265 ? 0.6139 0.4740 0.4321 0.2434  -0.0442 -0.0360 265 THR A CB  
1693  O OG1 . THR A 265 ? 0.5933 0.4409 0.4232 0.2241  -0.0500 -0.0364 265 THR A OG1 
1694  C CG2 . THR A 265 ? 0.6411 0.4972 0.4425 0.2584  -0.0457 -0.0399 265 THR A CG2 
1695  N N   . LEU A 266 ? 0.5564 0.4537 0.4290 0.2250  -0.0393 -0.0211 266 LEU A N   
1696  C CA  . LEU A 266 ? 0.5346 0.4318 0.4207 0.2116  -0.0396 -0.0172 266 LEU A CA  
1697  C C   . LEU A 266 ? 0.5195 0.4427 0.4308 0.2124  -0.0397 -0.0087 266 LEU A C   
1698  O O   . LEU A 266 ? 0.5157 0.4409 0.4351 0.2101  -0.0438 -0.0084 266 LEU A O   
1699  C CB  . LEU A 266 ? 0.5223 0.3917 0.4056 0.1907  -0.0455 -0.0214 266 LEU A CB  
1700  C CG  . LEU A 266 ? 0.4999 0.3679 0.3985 0.1754  -0.0465 -0.0171 266 LEU A CG  
1701  C CD1 . LEU A 266 ? 0.5003 0.3710 0.3969 0.1768  -0.0424 -0.0146 266 LEU A CD1 
1702  C CD2 . LEU A 266 ? 0.4878 0.3360 0.3858 0.1557  -0.0506 -0.0198 266 LEU A CD2 
1703  N N   . LEU A 267 ? 0.4751 0.4201 0.3996 0.2150  -0.0361 -0.0006 267 LEU A N   
1704  C CA  . LEU A 267 ? 0.4595 0.4344 0.4109 0.2139  -0.0381 0.0103  267 LEU A CA  
1705  C C   . LEU A 267 ? 0.4432 0.4143 0.4043 0.2013  -0.0404 0.0152  267 LEU A C   
1706  O O   . LEU A 267 ? 0.4416 0.4313 0.4071 0.2062  -0.0349 0.0218  267 LEU A O   
1707  C CB  . LEU A 267 ? 0.4653 0.4850 0.4292 0.2307  -0.0310 0.0203  267 LEU A CB  
1708  C CG  . LEU A 267 ? 0.4481 0.5082 0.4442 0.2271  -0.0339 0.0349  267 LEU A CG  
1709  C CD1 . LEU A 267 ? 0.4419 0.4920 0.4455 0.2189  -0.0437 0.0329  267 LEU A CD1 
1710  C CD2 . LEU A 267 ? 0.4545 0.5624 0.4639 0.2413  -0.0251 0.0462  267 LEU A CD2 
1711  N N   . ASN A 268 ? 0.4524 0.4001 0.4161 0.1850  -0.0481 0.0124  268 ASN A N   
1712  C CA  . ASN A 268 ? 0.4391 0.3781 0.4103 0.1715  -0.0519 0.0166  268 ASN A CA  
1713  C C   . ASN A 268 ? 0.4263 0.3901 0.4223 0.1575  -0.0569 0.0254  268 ASN A C   
1714  O O   . ASN A 268 ? 0.4249 0.3770 0.4219 0.1535  -0.0645 0.0226  268 ASN A O   
1715  C CB  . ASN A 268 ? 0.4357 0.3343 0.3930 0.1536  -0.0539 0.0073  268 ASN A CB  
1716  C CG  . ASN A 268 ? 0.4420 0.3247 0.3821 0.1526  -0.0480 0.0016  268 ASN A CG  
1717  O OD1 . ASN A 268 ? 0.4497 0.3457 0.3865 0.1646  -0.0429 0.0043  268 ASN A OD1 
1718  N ND2 . ASN A 268 ? 0.4379 0.2969 0.3681 0.1380  -0.0487 -0.0050 268 ASN A ND2 
1719  N N   . MET A 269 ? 0.4097 0.4077 0.4256 0.1486  -0.0529 0.0365  269 MET A N   
1720  C CA  . MET A 269 ? 0.3991 0.4210 0.4397 0.1319  -0.0587 0.0459  269 MET A CA  
1721  C C   . MET A 269 ? 0.3887 0.4187 0.4427 0.1121  -0.0577 0.0535  269 MET A C   
1722  O O   . MET A 269 ? 0.3819 0.4414 0.4596 0.0997  -0.0609 0.0646  269 MET A O   
1723  C CB  . MET A 269 ? 0.4015 0.4683 0.4600 0.1428  -0.0568 0.0560  269 MET A CB  
1724  C CG  . MET A 269 ? 0.4094 0.4702 0.4610 0.1565  -0.0612 0.0505  269 MET A CG  
1725  S SD  . MET A 269 ? 0.4118 0.5274 0.4868 0.1688  -0.0592 0.0639  269 MET A SD  
1726  C CE  . MET A 269 ? 0.4118 0.5652 0.4966 0.1754  -0.0464 0.0753  269 MET A CE  
1727  N N   . PHE A 270 ? 0.4264 0.4307 0.4664 0.1086  -0.0540 0.0482  270 PHE A N   
1728  C CA  . PHE A 270 ? 0.4302 0.4401 0.4813 0.0910  -0.0523 0.0551  270 PHE A CA  
1729  C C   . PHE A 270 ? 0.4258 0.4194 0.4852 0.0692  -0.0619 0.0553  270 PHE A C   
1730  O O   . PHE A 270 ? 0.4203 0.3936 0.4731 0.0682  -0.0692 0.0488  270 PHE A O   
1731  C CB  . PHE A 270 ? 0.4305 0.4148 0.4626 0.0941  -0.0463 0.0489  270 PHE A CB  
1732  C CG  . PHE A 270 ? 0.4236 0.3606 0.4337 0.0944  -0.0506 0.0365  270 PHE A CG  
1733  C CD1 . PHE A 270 ? 0.4166 0.3274 0.4265 0.0765  -0.0556 0.0347  270 PHE A CD1 
1734  C CD2 . PHE A 270 ? 0.4354 0.3540 0.4250 0.1131  -0.0499 0.0274  270 PHE A CD2 
1735  C CE1 . PHE A 270 ? 0.4198 0.2901 0.4110 0.0772  -0.0589 0.0253  270 PHE A CE1 
1736  C CE2 . PHE A 270 ? 0.4387 0.3156 0.4102 0.1126  -0.0545 0.0180  270 PHE A CE2 
1737  C CZ  . PHE A 270 ? 0.4303 0.2843 0.4032 0.0948  -0.0586 0.0176  270 PHE A CZ  
1738  N N   . GLU A 271 ? 0.4684 0.4708 0.5417 0.0521  -0.0619 0.0631  271 GLU A N   
1739  C CA  . GLU A 271 ? 0.4635 0.4487 0.5433 0.0312  -0.0709 0.0635  271 GLU A CA  
1740  C C   . GLU A 271 ? 0.4616 0.4596 0.5535 0.0267  -0.0808 0.0664  271 GLU A C   
1741  O O   . GLU A 271 ? 0.4584 0.4292 0.5402 0.0230  -0.0884 0.0588  271 GLU A O   
1742  C CB  . GLU A 271 ? 0.4518 0.3892 0.5093 0.0286  -0.0722 0.0518  271 GLU A CB  
1743  C CG  . GLU A 271 ? 0.4442 0.3674 0.4972 0.0210  -0.0667 0.0524  271 GLU A CG  
1744  C CD  . GLU A 271 ? 0.4198 0.2980 0.4530 0.0183  -0.0682 0.0428  271 GLU A CD  
1745  O OE1 . GLU A 271 ? 0.4034 0.2633 0.4369 0.0063  -0.0750 0.0410  271 GLU A OE1 
1746  O OE2 . GLU A 271 ? 0.4188 0.2799 0.4359 0.0284  -0.0628 0.0374  271 GLU A OE2 
1747  N N   . ASN A 272 ? 0.4486 0.4898 0.5627 0.0274  -0.0808 0.0786  272 ASN A N   
1748  C CA  . ASN A 272 ? 0.4418 0.5012 0.5708 0.0227  -0.0906 0.0839  272 ASN A CA  
1749  C C   . ASN A 272 ? 0.4288 0.5271 0.5874 0.0086  -0.0937 0.1007  272 ASN A C   
1750  O O   . ASN A 272 ? 0.4313 0.5396 0.5976 0.0022  -0.0882 0.1074  272 ASN A O   
1751  C CB  . ASN A 272 ? 0.4421 0.5174 0.5674 0.0437  -0.0877 0.0822  272 ASN A CB  
1752  C CG  . ASN A 272 ? 0.4502 0.4892 0.5539 0.0505  -0.0924 0.0683  272 ASN A CG  
1753  O OD1 . ASN A 272 ? 0.4480 0.4758 0.5532 0.0404  -0.1031 0.0666  272 ASN A OD1 
1754  N ND2 . ASN A 272 ? 0.4506 0.4705 0.5334 0.0676  -0.0850 0.0588  272 ASN A ND2 
1755  N N   . GLN A 273 ? 0.4591 0.5801 0.6351 0.0033  -0.1033 0.1086  273 GLN A N   
1756  C CA  . GLN A 273 ? 0.4382 0.6001 0.6454 -0.0098 -0.1080 0.1269  273 GLN A CA  
1757  C C   . GLN A 273 ? 0.4207 0.6311 0.6452 0.0050  -0.1030 0.1389  273 GLN A C   
1758  O O   . GLN A 273 ? 0.4023 0.6469 0.6532 -0.0044 -0.1109 0.1539  273 GLN A O   
1759  C CB  . GLN A 273 ? 0.4375 0.5880 0.6538 -0.0311 -0.1254 0.1290  273 GLN A CB  
1760  C CG  . GLN A 273 ? 0.4450 0.5451 0.6412 -0.0434 -0.1307 0.1162  273 GLN A CG  
1761  C CD  . GLN A 273 ? 0.4424 0.5346 0.6497 -0.0661 -0.1477 0.1208  273 GLN A CD  
1762  O OE1 . GLN A 273 ? 0.4235 0.5425 0.6557 -0.0803 -0.1529 0.1357  273 GLN A OE1 
1763  N NE2 . GLN A 273 ? 0.4481 0.5027 0.6363 -0.0694 -0.1571 0.1085  273 GLN A NE2 
1764  N N   . LEU A 274 ? 0.3977 0.6110 0.6074 0.0285  -0.0904 0.1329  274 LEU A N   
1765  C CA  . LEU A 274 ? 0.3820 0.6402 0.6053 0.0460  -0.0837 0.1438  274 LEU A CA  
1766  C C   . LEU A 274 ? 0.3599 0.6656 0.6114 0.0402  -0.0790 0.1641  274 LEU A C   
1767  O O   . LEU A 274 ? 0.3609 0.6624 0.6128 0.0317  -0.0746 0.1663  274 LEU A O   
1768  C CB  . LEU A 274 ? 0.3943 0.6412 0.5925 0.0727  -0.0709 0.1323  274 LEU A CB  
1769  C CG  . LEU A 274 ? 0.4033 0.6290 0.5836 0.0874  -0.0737 0.1198  274 LEU A CG  
1770  C CD1 . LEU A 274 ? 0.4151 0.6010 0.5860 0.0716  -0.0868 0.1093  274 LEU A CD1 
1771  C CD2 . LEU A 274 ? 0.4136 0.6165 0.5654 0.1098  -0.0627 0.1067  274 LEU A CD2 
1772  N N   . SER A 275 ? 0.3243 0.6769 0.6004 0.0449  -0.0799 0.1802  275 SER A N   
1773  C CA  . SER A 275 ? 0.3195 0.7224 0.6274 0.0376  -0.0773 0.2029  275 SER A CA  
1774  C C   . SER A 275 ? 0.3225 0.7730 0.6405 0.0619  -0.0657 0.2146  275 SER A C   
1775  O O   . SER A 275 ? 0.3290 0.7688 0.6262 0.0846  -0.0590 0.2031  275 SER A O   
1776  C CB  . SER A 275 ? 0.3179 0.7327 0.6535 0.0108  -0.0949 0.2160  275 SER A CB  
1777  O OG  . SER A 275 ? 0.3228 0.7413 0.6629 0.0125  -0.1050 0.2157  275 SER A OG  
1778  N N   . GLY A 276 ? 0.3553 0.8474 0.6967 0.0557  -0.0614 0.2340  276 GLY A N   
1779  C CA  . GLY A 276 ? 0.3671 0.8935 0.7083 0.0772  -0.0465 0.2421  276 GLY A CA  
1780  C C   . GLY A 276 ? 0.3687 0.8952 0.6900 0.0992  -0.0295 0.2365  276 GLY A C   
1781  O O   . GLY A 276 ? 0.3596 0.8698 0.6746 0.0941  -0.0281 0.2320  276 GLY A O   
1782  N N   . GLU A 277 ? 0.3918 0.9356 0.7018 0.1242  -0.0166 0.2366  277 GLU A N   
1783  C CA  . GLU A 277 ? 0.4003 0.9435 0.6869 0.1479  -0.0002 0.2308  277 GLU A CA  
1784  C C   . GLU A 277 ? 0.4079 0.9180 0.6635 0.1713  0.0022  0.2100  277 GLU A C   
1785  O O   . GLU A 277 ? 0.4102 0.9107 0.6650 0.1735  -0.0052 0.2043  277 GLU A O   
1786  C CB  . GLU A 277 ? 0.4169 1.0028 0.7097 0.1594  0.0136  0.2476  277 GLU A CB  
1787  C CG  . GLU A 277 ? 0.4160 1.0363 0.7421 0.1369  0.0078  0.2704  277 GLU A CG  
1788  C CD  . GLU A 277 ? 0.4307 1.0899 0.7614 0.1453  0.0219  0.2890  277 GLU A CD  
1789  O OE1 . GLU A 277 ? 0.4441 1.1063 0.7514 0.1710  0.0364  0.2839  277 GLU A OE1 
1790  O OE2 . GLU A 277 ? 0.4315 1.1163 0.7872 0.1264  0.0179  0.3088  277 GLU A OE2 
1791  N N   . ILE A 278 ? 0.4064 0.8967 0.6350 0.1882  0.0120  0.1985  278 ILE A N   
1792  C CA  . ILE A 278 ? 0.4193 0.8733 0.6139 0.2107  0.0147  0.1781  278 ILE A CA  
1793  C C   . ILE A 278 ? 0.4404 0.9157 0.6290 0.2300  0.0234  0.1816  278 ILE A C   
1794  O O   . ILE A 278 ? 0.4538 0.9584 0.6413 0.2407  0.0359  0.1921  278 ILE A O   
1795  C CB  . ILE A 278 ? 0.4253 0.8511 0.5903 0.2232  0.0224  0.1655  278 ILE A CB  
1796  C CG1 . ILE A 278 ? 0.4074 0.8078 0.5764 0.2005  0.0142  0.1620  278 ILE A CG1 
1797  C CG2 . ILE A 278 ? 0.4431 0.8263 0.5711 0.2439  0.0234  0.1441  278 ILE A CG2 
1798  C CD1 . ILE A 278 ? 0.4144 0.7897 0.5572 0.2067  0.0221  0.1524  278 ILE A CD1 
1799  N N   . PRO A 279 ? 0.4546 0.9165 0.6389 0.2349  0.0172  0.1739  279 PRO A N   
1800  C CA  . PRO A 279 ? 0.4748 0.9575 0.6553 0.2524  0.0248  0.1782  279 PRO A CA  
1801  C C   . PRO A 279 ? 0.4994 0.9701 0.6453 0.2784  0.0384  0.1689  279 PRO A C   
1802  O O   . PRO A 279 ? 0.5053 0.9324 0.6212 0.2869  0.0375  0.1497  279 PRO A O   
1803  C CB  . PRO A 279 ? 0.4733 0.9319 0.6511 0.2515  0.0137  0.1675  279 PRO A CB  
1804  C CG  . PRO A 279 ? 0.4582 0.8741 0.6263 0.2404  0.0030  0.1529  279 PRO A CG  
1805  C CD  . PRO A 279 ? 0.4420 0.8700 0.6257 0.2238  0.0023  0.1623  279 PRO A CD  
1806  N N   . PRO A 280 ? 0.5072 1.0141 0.6547 0.2910  0.0505  0.1823  280 PRO A N   
1807  C CA  . PRO A 280 ? 0.5353 1.0302 0.6466 0.3167  0.0627  0.1738  280 PRO A CA  
1808  C C   . PRO A 280 ? 0.5538 1.0118 0.6357 0.3332  0.0605  0.1551  280 PRO A C   
1809  O O   . PRO A 280 ? 0.5760 1.0067 0.6222 0.3506  0.0659  0.1420  280 PRO A O   
1810  C CB  . PRO A 280 ? 0.5501 1.0959 0.6740 0.3251  0.0741  0.1954  280 PRO A CB  
1811  C CG  . PRO A 280 ? 0.5265 1.1080 0.6923 0.2998  0.0688  0.2154  280 PRO A CG  
1812  C CD  . PRO A 280 ? 0.5038 1.0628 0.6848 0.2810  0.0530  0.2071  280 PRO A CD  
1813  N N   . GLU A 281 ? 0.5798 1.0351 0.6750 0.3274  0.0520  0.1538  281 GLU A N   
1814  C CA  . GLU A 281 ? 0.5962 1.0153 0.6655 0.3404  0.0487  0.1366  281 GLU A CA  
1815  C C   . GLU A 281 ? 0.5934 0.9566 0.6365 0.3374  0.0414  0.1150  281 GLU A C   
1816  O O   . GLU A 281 ? 0.6107 0.9391 0.6274 0.3480  0.0390  0.0998  281 GLU A O   
1817  C CB  . GLU A 281 ? 0.5872 1.0174 0.6794 0.3325  0.0403  0.1413  281 GLU A CB  
1818  C CG  . GLU A 281 ? 0.5877 1.0731 0.7105 0.3309  0.0449  0.1644  281 GLU A CG  
1819  C CD  . GLU A 281 ? 0.5633 1.0805 0.7216 0.3077  0.0407  0.1816  281 GLU A CD  
1820  O OE1 . GLU A 281 ? 0.5485 1.0507 0.7058 0.2965  0.0378  0.1772  281 GLU A OE1 
1821  O OE2 . GLU A 281 ? 0.5603 1.1167 0.7475 0.2999  0.0397  0.1999  281 GLU A OE2 
1822  N N   . ILE A 282 ? 0.5709 0.9246 0.6212 0.3223  0.0373  0.1140  282 ILE A N   
1823  C CA  . ILE A 282 ? 0.5702 0.8712 0.5946 0.3194  0.0312  0.0949  282 ILE A CA  
1824  C C   . ILE A 282 ? 0.6001 0.8764 0.5851 0.3386  0.0385  0.0833  282 ILE A C   
1825  O O   . ILE A 282 ? 0.6107 0.8395 0.5680 0.3404  0.0327  0.0658  282 ILE A O   
1826  C CB  . ILE A 282 ? 0.5446 0.8456 0.5851 0.3009  0.0271  0.0989  282 ILE A CB  
1827  C CG1 . ILE A 282 ? 0.5199 0.8174 0.5852 0.2810  0.0139  0.1010  282 ILE A CG1 
1828  C CG2 . ILE A 282 ? 0.5511 0.8072 0.5609 0.3029  0.0266  0.0831  282 ILE A CG2 
1829  C CD1 . ILE A 282 ? 0.4973 0.7845 0.5732 0.2628  0.0075  0.1022  282 ILE A CD1 
1830  N N   . GLY A 283 ? 0.6032 0.9109 0.5844 0.3524  0.0504  0.0936  283 GLY A N   
1831  C CA  . GLY A 283 ? 0.6356 0.9215 0.5776 0.3718  0.0563  0.0837  283 GLY A CA  
1832  C C   . GLY A 283 ? 0.6602 0.9162 0.5767 0.3842  0.0524  0.0707  283 GLY A C   
1833  O O   . GLY A 283 ? 0.6843 0.9035 0.5651 0.3939  0.0508  0.0570  283 GLY A O   
1834  N N   . ASN A 284 ? 0.7029 0.9742 0.6378 0.3831  0.0499  0.0755  284 ASN A N   
1835  C CA  . ASN A 284 ? 0.7244 0.9684 0.6381 0.3933  0.0457  0.0640  284 ASN A CA  
1836  C C   . ASN A 284 ? 0.7186 0.9094 0.6170 0.3815  0.0334  0.0461  284 ASN A C   
1837  O O   . ASN A 284 ? 0.7386 0.9007 0.6153 0.3887  0.0289  0.0353  284 ASN A O   
1838  C CB  . ASN A 284 ? 0.7191 0.9946 0.6585 0.3941  0.0459  0.0747  284 ASN A CB  
1839  C CG  . ASN A 284 ? 0.7384 1.0587 0.6820 0.4115  0.0583  0.0903  284 ASN A CG  
1840  O OD1 . ASN A 284 ? 0.7709 1.0826 0.6847 0.4315  0.0640  0.0860  284 ASN A OD1 
1841  N ND2 . ASN A 284 ? 0.7198 1.0878 0.7003 0.4033  0.0614  0.1092  284 ASN A ND2 
1842  N N   . MET A 285 ? 0.6898 0.8670 0.5990 0.3632  0.0277  0.0436  285 MET A N   
1843  C CA  . MET A 285 ? 0.6839 0.8117 0.5794 0.3502  0.0164  0.0284  285 MET A CA  
1844  C C   . MET A 285 ? 0.7079 0.7997 0.5663 0.3570  0.0159  0.0163  285 MET A C   
1845  O O   . MET A 285 ? 0.7008 0.7739 0.5526 0.3476  0.0137  0.0121  285 MET A O   
1846  C CB  . MET A 285 ? 0.6508 0.7777 0.5697 0.3294  0.0108  0.0312  285 MET A CB  
1847  C CG  . MET A 285 ? 0.6322 0.7865 0.5855 0.3196  0.0068  0.0416  285 MET A CG  
1848  S SD  . MET A 285 ? 0.5963 0.7414 0.5711 0.2954  -0.0024 0.0433  285 MET A SD  
1849  C CE  . MET A 285 ? 0.5940 0.6914 0.5565 0.2852  -0.0145 0.0288  285 MET A CE  
1850  N N   . THR A 286 ? 0.6904 0.7725 0.5244 0.3734  0.0170  0.0112  286 THR A N   
1851  C CA  . THR A 286 ? 0.7196 0.7743 0.5176 0.3836  0.0165  0.0023  286 THR A CA  
1852  C C   . THR A 286 ? 0.7188 0.7238 0.4994 0.3692  0.0045  -0.0113 286 THR A C   
1853  O O   . THR A 286 ? 0.7401 0.7209 0.4928 0.3740  0.0020  -0.0181 286 THR A O   
1854  C CB  . THR A 286 ? 0.7550 0.8136 0.5326 0.4056  0.0199  0.0016  286 THR A CB  
1855  O OG1 . THR A 286 ? 0.7530 0.8045 0.5383 0.4028  0.0143  -0.0013 286 THR A OG1 
1856  C CG2 . THR A 286 ? 0.7617 0.8697 0.5505 0.4217  0.0333  0.0164  286 THR A CG2 
1857  N N   . ALA A 287 ? 0.6913 0.6819 0.4877 0.3513  -0.0034 -0.0144 287 ALA A N   
1858  C CA  . ALA A 287 ? 0.6875 0.6359 0.4716 0.3351  -0.0143 -0.0247 287 ALA A CA  
1859  C C   . ALA A 287 ? 0.6586 0.6014 0.4573 0.3159  -0.0162 -0.0235 287 ALA A C   
1860  O O   . ALA A 287 ? 0.6505 0.5625 0.4443 0.2996  -0.0247 -0.0299 287 ALA A O   
1861  C CB  . ALA A 287 ? 0.6844 0.6181 0.4733 0.3281  -0.0219 -0.0289 287 ALA A CB  
1862  N N   . LEU A 288 ? 0.6594 0.6332 0.4771 0.3172  -0.0084 -0.0142 288 LEU A N   
1863  C CA  . LEU A 288 ? 0.6337 0.6042 0.4676 0.2996  -0.0103 -0.0119 288 LEU A CA  
1864  C C   . LEU A 288 ? 0.6391 0.5822 0.4518 0.2946  -0.0125 -0.0180 288 LEU A C   
1865  O O   . LEU A 288 ? 0.6600 0.6072 0.4544 0.3084  -0.0075 -0.0180 288 LEU A O   
1866  C CB  . LEU A 288 ? 0.6187 0.6335 0.4796 0.3032  -0.0018 0.0015  288 LEU A CB  
1867  C CG  . LEU A 288 ? 0.5836 0.6017 0.4691 0.2850  -0.0050 0.0066  288 LEU A CG  
1868  C CD1 . LEU A 288 ? 0.5688 0.5712 0.4659 0.2711  -0.0143 0.0035  288 LEU A CD1 
1869  C CD2 . LEU A 288 ? 0.5697 0.6376 0.4831 0.2891  0.0028  0.0224  288 LEU A CD2 
1870  N N   . ASP A 289 ? 0.6552 0.5713 0.4706 0.2745  -0.0202 -0.0224 289 ASP A N   
1871  C CA  . ASP A 289 ? 0.6577 0.5484 0.4576 0.2657  -0.0235 -0.0270 289 ASP A CA  
1872  C C   . ASP A 289 ? 0.6351 0.5331 0.4519 0.2544  -0.0207 -0.0215 289 ASP A C   
1873  O O   . ASP A 289 ? 0.6396 0.5333 0.4457 0.2561  -0.0181 -0.0214 289 ASP A O   
1874  C CB  . ASP A 289 ? 0.6568 0.5138 0.4478 0.2500  -0.0341 -0.0343 289 ASP A CB  
1875  C CG  . ASP A 289 ? 0.6649 0.4986 0.4431 0.2390  -0.0383 -0.0373 289 ASP A CG  
1876  O OD1 . ASP A 289 ? 0.6915 0.5265 0.4546 0.2495  -0.0347 -0.0373 289 ASP A OD1 
1877  O OD2 . ASP A 289 ? 0.6476 0.4640 0.4316 0.2198  -0.0448 -0.0389 289 ASP A OD2 
1878  N N   . THR A 290 ? 0.6138 0.5221 0.4562 0.2434  -0.0218 -0.0166 290 THR A N   
1879  C CA  . THR A 290 ? 0.5855 0.4987 0.4451 0.2316  -0.0208 -0.0107 290 THR A CA  
1880  C C   . THR A 290 ? 0.5671 0.5140 0.4558 0.2334  -0.0185 -0.0003 290 THR A C   
1881  O O   . THR A 290 ? 0.5608 0.5070 0.4596 0.2284  -0.0234 -0.0008 290 THR A O   
1882  C CB  . THR A 290 ? 0.5701 0.4512 0.4296 0.2088  -0.0287 -0.0156 290 THR A CB  
1883  O OG1 . THR A 290 ? 0.5873 0.4433 0.4236 0.2057  -0.0318 -0.0226 290 THR A OG1 
1884  C CG2 . THR A 290 ? 0.5514 0.4355 0.4275 0.1968  -0.0280 -0.0092 290 THR A CG2 
1885  N N   . LEU A 291 ? 0.5085 0.4877 0.4119 0.2396  -0.0117 0.0105  291 LEU A N   
1886  C CA  . LEU A 291 ? 0.4907 0.5106 0.4258 0.2395  -0.0104 0.0242  291 LEU A CA  
1887  C C   . LEU A 291 ? 0.4698 0.4960 0.4224 0.2240  -0.0117 0.0328  291 LEU A C   
1888  O O   . LEU A 291 ? 0.4711 0.5051 0.4207 0.2229  -0.0053 0.0364  291 LEU A O   
1889  C CB  . LEU A 291 ? 0.5004 0.5661 0.4430 0.2573  -0.0003 0.0338  291 LEU A CB  
1890  C CG  . LEU A 291 ? 0.4811 0.5994 0.4610 0.2544  0.0017  0.0521  291 LEU A CG  
1891  C CD1 . LEU A 291 ? 0.4690 0.5845 0.4647 0.2445  -0.0082 0.0525  291 LEU A CD1 
1892  C CD2 . LEU A 291 ? 0.4946 0.6554 0.4786 0.2709  0.0127  0.0611  291 LEU A CD2 
1893  N N   . SER A 292 ? 0.4612 0.4825 0.4311 0.2034  -0.0193 0.0350  292 SER A N   
1894  C CA  . SER A 292 ? 0.4436 0.4633 0.4282 0.1777  -0.0214 0.0405  292 SER A CA  
1895  C C   . SER A 292 ? 0.4285 0.4795 0.4435 0.1627  -0.0251 0.0518  292 SER A C   
1896  O O   . SER A 292 ? 0.4243 0.4627 0.4431 0.1561  -0.0334 0.0484  292 SER A O   
1897  C CB  . SER A 292 ? 0.4409 0.4111 0.4104 0.1658  -0.0288 0.0299  292 SER A CB  
1898  O OG  . SER A 292 ? 0.4256 0.3939 0.4082 0.1426  -0.0301 0.0353  292 SER A OG  
1899  N N   . LEU A 293 ? 0.4253 0.5170 0.4618 0.1569  -0.0197 0.0657  293 LEU A N   
1900  C CA  . LEU A 293 ? 0.4157 0.5368 0.4827 0.1393  -0.0247 0.0782  293 LEU A CA  
1901  C C   . LEU A 293 ? 0.4219 0.5437 0.5025 0.1158  -0.0260 0.0850  293 LEU A C   
1902  O O   . LEU A 293 ? 0.4147 0.5688 0.5223 0.1023  -0.0283 0.0987  293 LEU A O   
1903  C CB  . LEU A 293 ? 0.4027 0.5767 0.4891 0.1516  -0.0189 0.0920  293 LEU A CB  
1904  C CG  . LEU A 293 ? 0.3984 0.5774 0.4705 0.1793  -0.0147 0.0868  293 LEU A CG  
1905  C CD1 . LEU A 293 ? 0.3907 0.6264 0.4847 0.1909  -0.0077 0.1032  293 LEU A CD1 
1906  C CD2 . LEU A 293 ? 0.3980 0.5502 0.4635 0.1790  -0.0246 0.0769  293 LEU A CD2 
1907  N N   . HIS A 294 ? 0.4283 0.5149 0.4912 0.1103  -0.0251 0.0766  294 HIS A N   
1908  C CA  . HIS A 294 ? 0.4180 0.5058 0.4925 0.0903  -0.0249 0.0835  294 HIS A CA  
1909  C C   . HIS A 294 ? 0.4078 0.4860 0.4979 0.0672  -0.0356 0.0856  294 HIS A C   
1910  O O   . HIS A 294 ? 0.4092 0.4696 0.4951 0.0664  -0.0433 0.0789  294 HIS A O   
1911  C CB  . HIS A 294 ? 0.4213 0.4735 0.4726 0.0910  -0.0215 0.0742  294 HIS A CB  
1912  C CG  . HIS A 294 ? 0.4203 0.4245 0.4560 0.0832  -0.0289 0.0619  294 HIS A CG  
1913  N ND1 . HIS A 294 ? 0.4103 0.3983 0.4552 0.0617  -0.0354 0.0631  294 HIS A ND1 
1914  C CD2 . HIS A 294 ? 0.4294 0.3982 0.4406 0.0946  -0.0308 0.0491  294 HIS A CD2 
1915  C CE1 . HIS A 294 ? 0.4126 0.3595 0.4397 0.0610  -0.0400 0.0520  294 HIS A CE1 
1916  N NE2 . HIS A 294 ? 0.4235 0.3585 0.4310 0.0800  -0.0376 0.0439  294 HIS A NE2 
1917  N N   . THR A 295 ? 0.4318 0.5220 0.5395 0.0487  -0.0364 0.0956  295 THR A N   
1918  C CA  . THR A 295 ? 0.4264 0.5073 0.5485 0.0260  -0.0470 0.0985  295 THR A CA  
1919  C C   . THR A 295 ? 0.4194 0.5229 0.5582 0.0246  -0.0549 0.1041  295 THR A C   
1920  O O   . THR A 295 ? 0.4209 0.5010 0.5537 0.0203  -0.0638 0.0964  295 THR A O   
1921  C CB  . THR A 295 ? 0.4332 0.4625 0.5348 0.0192  -0.0519 0.0848  295 THR A CB  
1922  O OG1 . THR A 295 ? 0.4435 0.4522 0.5268 0.0254  -0.0442 0.0789  295 THR A OG1 
1923  C CG2 . THR A 295 ? 0.4332 0.4513 0.5472 -0.0044 -0.0605 0.0886  295 THR A CG2 
1924  N N   . ASN A 296 ? 0.4198 0.5709 0.5801 0.0287  -0.0514 0.1186  296 ASN A N   
1925  C CA  . ASN A 296 ? 0.3998 0.5793 0.5796 0.0275  -0.0586 0.1270  296 ASN A CA  
1926  C C   . ASN A 296 ? 0.3782 0.6021 0.5906 0.0142  -0.0600 0.1473  296 ASN A C   
1927  O O   . ASN A 296 ? 0.3746 0.6024 0.5934 0.0042  -0.0564 0.1536  296 ASN A O   
1928  C CB  . ASN A 296 ? 0.4038 0.5990 0.5752 0.0529  -0.0523 0.1241  296 ASN A CB  
1929  C CG  . ASN A 296 ? 0.4182 0.5774 0.5691 0.0596  -0.0583 0.1086  296 ASN A CG  
1930  O OD1 . ASN A 296 ? 0.4118 0.5720 0.5718 0.0521  -0.0685 0.1097  296 ASN A OD1 
1931  N ND2 . ASN A 296 ? 0.4297 0.5571 0.5529 0.0737  -0.0525 0.0946  296 ASN A ND2 
1932  N N   . LYS A 297 ? 0.4009 0.6592 0.6351 0.0135  -0.0656 0.1589  297 LYS A N   
1933  C CA  . LYS A 297 ? 0.3725 0.6778 0.6409 0.0015  -0.0680 0.1809  297 LYS A CA  
1934  C C   . LYS A 297 ? 0.3554 0.7121 0.6375 0.0212  -0.0583 0.1941  297 LYS A C   
1935  O O   . LYS A 297 ? 0.3467 0.7461 0.6592 0.0143  -0.0631 0.2129  297 LYS A O   
1936  C CB  . LYS A 297 ? 0.3590 0.6621 0.6458 -0.0208 -0.0858 0.1865  297 LYS A CB  
1937  C CG  . LYS A 297 ? 0.3685 0.6280 0.6466 -0.0421 -0.0951 0.1779  297 LYS A CG  
1938  C CD  . LYS A 297 ? 0.3626 0.6168 0.6551 -0.0627 -0.1139 0.1823  297 LYS A CD  
1939  C CE  . LYS A 297 ? 0.3733 0.5788 0.6518 -0.0804 -0.1226 0.1713  297 LYS A CE  
1940  N NZ  . LYS A 297 ? 0.3783 0.5676 0.6608 -0.0964 -0.1413 0.1701  297 LYS A NZ  
1941  N N   . LEU A 298 ? 0.3447 0.6974 0.6044 0.0461  -0.0451 0.1850  298 LEU A N   
1942  C CA  . LEU A 298 ? 0.3417 0.7402 0.6097 0.0685  -0.0343 0.1961  298 LEU A CA  
1943  C C   . LEU A 298 ? 0.3373 0.7830 0.6302 0.0647  -0.0268 0.2174  298 LEU A C   
1944  O O   . LEU A 298 ? 0.3325 0.7684 0.6254 0.0520  -0.0254 0.2188  298 LEU A O   
1945  C CB  . LEU A 298 ? 0.3527 0.7294 0.5867 0.0958  -0.0226 0.1798  298 LEU A CB  
1946  C CG  . LEU A 298 ? 0.3739 0.7049 0.5825 0.1021  -0.0289 0.1594  298 LEU A CG  
1947  C CD1 . LEU A 298 ? 0.3851 0.7062 0.5659 0.1318  -0.0181 0.1481  298 LEU A CD1 
1948  C CD2 . LEU A 298 ? 0.3639 0.7082 0.5904 0.0956  -0.0402 0.1648  298 LEU A CD2 
1949  N N   . THR A 299 ? 0.3253 0.8242 0.6401 0.0763  -0.0217 0.2353  299 THR A N   
1950  C CA  . THR A 299 ? 0.3314 0.8669 0.6607 0.0724  -0.0125 0.2537  299 THR A CA  
1951  C C   . THR A 299 ? 0.3476 0.9097 0.6646 0.1008  0.0037  0.2570  299 THR A C   
1952  O O   . THR A 299 ? 0.3543 0.9066 0.6538 0.1216  0.0067  0.2453  299 THR A O   
1953  C CB  . THR A 299 ? 0.3346 0.8871 0.6912 0.0468  -0.0236 0.2702  299 THR A CB  
1954  O OG1 . THR A 299 ? 0.3404 0.8976 0.7020 0.0497  -0.0307 0.2697  299 THR A OG1 
1955  C CG2 . THR A 299 ? 0.3243 0.8475 0.6889 0.0182  -0.0383 0.2673  299 THR A CG2 
1956  N N   . GLY A 300 ? 0.3664 0.9599 0.6904 0.1018  0.0140  0.2732  300 GLY A N   
1957  C CA  . GLY A 300 ? 0.3851 1.0044 0.6962 0.1280  0.0296  0.2783  300 GLY A CA  
1958  C C   . GLY A 300 ? 0.3905 0.9937 0.6705 0.1511  0.0421  0.2647  300 GLY A C   
1959  O O   . GLY A 300 ? 0.3782 0.9508 0.6479 0.1470  0.0389  0.2516  300 GLY A O   
1960  N N   . PRO A 301 ? 0.3923 1.0139 0.6551 0.1761  0.0561  0.2676  301 PRO A N   
1961  C CA  . PRO A 301 ? 0.4033 1.0088 0.6331 0.1987  0.0679  0.2553  301 PRO A CA  
1962  C C   . PRO A 301 ? 0.4080 0.9727 0.6082 0.2170  0.0663  0.2308  301 PRO A C   
1963  O O   . PRO A 301 ? 0.4060 0.9604 0.6094 0.2170  0.0586  0.2245  301 PRO A O   
1964  C CB  . PRO A 301 ? 0.4287 1.0693 0.6510 0.2176  0.0815  0.2693  301 PRO A CB  
1965  C CG  . PRO A 301 ? 0.4334 1.0958 0.6739 0.2157  0.0775  0.2792  301 PRO A CG  
1966  C CD  . PRO A 301 ? 0.4097 1.0678 0.6817 0.1847  0.0615  0.2834  301 PRO A CD  
1967  N N   . ILE A 302 ? 0.4500 0.9893 0.6196 0.2324  0.0730  0.2171  302 ILE A N   
1968  C CA  . ILE A 302 ? 0.4628 0.9597 0.5974 0.2526  0.0723  0.1939  302 ILE A CA  
1969  C C   . ILE A 302 ? 0.4893 0.9990 0.6089 0.2748  0.0795  0.1944  302 ILE A C   
1970  O O   . ILE A 302 ? 0.5073 1.0475 0.6229 0.2864  0.0906  0.2068  302 ILE A O   
1971  C CB  . ILE A 302 ? 0.4716 0.9376 0.5740 0.2642  0.0776  0.1802  302 ILE A CB  
1972  C CG1 . ILE A 302 ? 0.4470 0.8853 0.5571 0.2455  0.0683  0.1737  302 ILE A CG1 
1973  C CG2 . ILE A 302 ? 0.4987 0.9266 0.5585 0.2894  0.0797  0.1596  302 ILE A CG2 
1974  C CD1 . ILE A 302 ? 0.4237 0.8870 0.5709 0.2151  0.0635  0.1910  302 ILE A CD1 
1975  N N   . PRO A 303 ? 0.4998 0.9879 0.6106 0.2815  0.0736  0.1824  303 PRO A N   
1976  C CA  . PRO A 303 ? 0.5264 1.0256 0.6223 0.3029  0.0804  0.1829  303 PRO A CA  
1977  C C   . PRO A 303 ? 0.5567 1.0347 0.6096 0.3281  0.0897  0.1711  303 PRO A C   
1978  O O   . PRO A 303 ? 0.5617 0.9936 0.5863 0.3333  0.0858  0.1514  303 PRO A O   
1979  C CB  . PRO A 303 ? 0.5218 0.9945 0.6169 0.3011  0.0699  0.1702  303 PRO A CB  
1980  C CG  . PRO A 303 ? 0.5027 0.9346 0.5937 0.2879  0.0595  0.1559  303 PRO A CG  
1981  C CD  . PRO A 303 ? 0.4828 0.9345 0.5958 0.2700  0.0600  0.1684  303 PRO A CD  
1982  N N   . SER A 304 ? 0.5543 1.0650 0.6015 0.3435  0.1009  0.1841  304 SER A N   
1983  C CA  . SER A 304 ? 0.5879 1.0802 0.5927 0.3685  0.1087  0.1745  304 SER A CA  
1984  C C   . SER A 304 ? 0.6092 1.0588 0.5811 0.3843  0.1042  0.1536  304 SER A C   
1985  O O   . SER A 304 ? 0.6359 1.0545 0.5686 0.4012  0.1058  0.1401  304 SER A O   
1986  C CB  . SER A 304 ? 0.6102 1.1477 0.6163 0.3828  0.1205  0.1942  304 SER A CB  
1987  O OG  . SER A 304 ? 0.6191 1.1786 0.6362 0.3893  0.1217  0.2024  304 SER A OG  
1988  N N   . THR A 305 ? 0.6086 1.0551 0.5956 0.3782  0.0974  0.1511  305 THR A N   
1989  C CA  . THR A 305 ? 0.6272 1.0342 0.5866 0.3903  0.0920  0.1326  305 THR A CA  
1990  C C   . THR A 305 ? 0.6220 0.9720 0.5595 0.3837  0.0820  0.1106  305 THR A C   
1991  O O   . THR A 305 ? 0.6379 0.9509 0.5515 0.3912  0.0760  0.0949  305 THR A O   
1992  C CB  . THR A 305 ? 0.6159 1.0389 0.6011 0.3837  0.0873  0.1382  305 THR A CB  
1993  O OG1 . THR A 305 ? 0.5807 0.9995 0.5951 0.3592  0.0771  0.1384  305 THR A OG1 
1994  C CG2 . THR A 305 ? 0.6215 1.1012 0.6301 0.3884  0.0964  0.1617  305 THR A CG2 
1995  N N   . LEU A 306 ? 0.6349 0.9765 0.5800 0.3692  0.0796  0.1097  306 LEU A N   
1996  C CA  . LEU A 306 ? 0.6329 0.9196 0.5553 0.3633  0.0704  0.0898  306 LEU A CA  
1997  C C   . LEU A 306 ? 0.6685 0.9204 0.5449 0.3814  0.0717  0.0760  306 LEU A C   
1998  O O   . LEU A 306 ? 0.6759 0.8780 0.5284 0.3789  0.0623  0.0584  306 LEU A O   
1999  C CB  . LEU A 306 ? 0.6039 0.8919 0.5455 0.3445  0.0681  0.0938  306 LEU A CB  
2000  C CG  . LEU A 306 ? 0.5685 0.8776 0.5524 0.3226  0.0617  0.1043  306 LEU A CG  
2001  C CD1 . LEU A 306 ? 0.5441 0.8451 0.5406 0.3052  0.0579  0.1058  306 LEU A CD1 
2002  C CD2 . LEU A 306 ? 0.5651 0.8461 0.5480 0.3184  0.0510  0.0931  306 LEU A CD2 
2003  N N   . GLY A 307 ? 0.6724 0.9491 0.5359 0.3985  0.0819  0.0846  307 GLY A N   
2004  C CA  . GLY A 307 ? 0.7097 0.9542 0.5287 0.4166  0.0815  0.0726  307 GLY A CA  
2005  C C   . GLY A 307 ? 0.7349 0.9467 0.5288 0.4272  0.0746  0.0591  307 GLY A C   
2006  O O   . GLY A 307 ? 0.7601 0.9288 0.5182 0.4341  0.0679  0.0446  307 GLY A O   
2007  N N   . ASN A 308 ? 0.7420 0.9739 0.5550 0.4278  0.0753  0.0646  308 ASN A N   
2008  C CA  . ASN A 308 ? 0.7662 0.9707 0.5573 0.4382  0.0694  0.0533  308 ASN A CA  
2009  C C   . ASN A 308 ? 0.7598 0.9104 0.5382 0.4245  0.0554  0.0351  308 ASN A C   
2010  O O   . ASN A 308 ? 0.7860 0.9030 0.5364 0.4328  0.0487  0.0232  308 ASN A O   
2011  C CB  . ASN A 308 ? 0.7585 0.9976 0.5761 0.4400  0.0729  0.0641  308 ASN A CB  
2012  C CG  . ASN A 308 ? 0.7603 1.0571 0.5972 0.4491  0.0861  0.0853  308 ASN A CG  
2013  O OD1 . ASN A 308 ? 0.7349 1.0630 0.5998 0.4369  0.0904  0.0983  308 ASN A OD1 
2014  N ND2 . ASN A 308 ? 0.7912 1.1029 0.6141 0.4702  0.0923  0.0902  308 ASN A ND2 
2015  N N   . ILE A 309 ? 0.7377 0.8799 0.5366 0.4031  0.0504  0.0336  309 ILE A N   
2016  C CA  . ILE A 309 ? 0.7313 0.8238 0.5193 0.3885  0.0373  0.0182  309 ILE A CA  
2017  C C   . ILE A 309 ? 0.7519 0.8092 0.5064 0.3914  0.0334  0.0083  309 ILE A C   
2018  O O   . ILE A 309 ? 0.7387 0.7955 0.4968 0.3832  0.0349  0.0102  309 ILE A O   
2019  C CB  . ILE A 309 ? 0.6914 0.7858 0.5110 0.3657  0.0329  0.0206  309 ILE A CB  
2020  C CG1 . ILE A 309 ? 0.6724 0.8048 0.5264 0.3629  0.0356  0.0322  309 ILE A CG1 
2021  C CG2 . ILE A 309 ? 0.6871 0.7312 0.4947 0.3508  0.0198  0.0060  309 ILE A CG2 
2022  C CD1 . ILE A 309 ? 0.6429 0.8164 0.5325 0.3526  0.0409  0.0479  309 ILE A CD1 
2023  N N   . LYS A 310 ? 0.7491 0.7768 0.4714 0.4027  0.0276  -0.0015 310 LYS A N   
2024  C CA  . LYS A 310 ? 0.7723 0.7651 0.4618 0.4055  0.0216  -0.0104 310 LYS A CA  
2025  C C   . LYS A 310 ? 0.7591 0.7085 0.4449 0.3841  0.0083  -0.0213 310 LYS A C   
2026  O O   . LYS A 310 ? 0.7732 0.6941 0.4365 0.3822  0.0021  -0.0274 310 LYS A O   
2027  C CB  . LYS A 310 ? 0.8164 0.7972 0.4731 0.4274  0.0199  -0.0149 310 LYS A CB  
2028  C CG  . LYS A 310 ? 0.8333 0.8571 0.4918 0.4499  0.0331  -0.0033 310 LYS A CG  
2029  C CD  . LYS A 310 ? 0.8181 0.8798 0.4929 0.4507  0.0449  0.0094  310 LYS A CD  
2030  C CE  . LYS A 310 ? 0.8467 0.9427 0.5112 0.4756  0.0565  0.0202  310 LYS A CE  
2031  N NZ  . LYS A 310 ? 0.8384 0.9646 0.5115 0.4770  0.0662  0.0317  310 LYS A NZ  
2032  N N   . THR A 311 ? 0.7452 0.6898 0.4528 0.3680  0.0034  -0.0228 311 THR A N   
2033  C CA  . THR A 311 ? 0.7300 0.6383 0.4380 0.3461  -0.0084 -0.0308 311 THR A CA  
2034  C C   . THR A 311 ? 0.6952 0.6089 0.4268 0.3277  -0.0069 -0.0268 311 THR A C   
2035  O O   . THR A 311 ? 0.6822 0.5675 0.4143 0.3089  -0.0157 -0.0320 311 THR A O   
2036  C CB  . THR A 311 ? 0.7242 0.6219 0.4407 0.3390  -0.0153 -0.0346 311 THR A CB  
2037  O OG1 . THR A 311 ? 0.7135 0.6465 0.4526 0.3460  -0.0074 -0.0269 311 THR A OG1 
2038  C CG2 . THR A 311 ? 0.7588 0.6320 0.4465 0.3498  -0.0225 -0.0422 311 THR A CG2 
2039  N N   . LEU A 312 ? 0.6947 0.6458 0.4469 0.3321  0.0038  -0.0165 312 LEU A N   
2040  C CA  . LEU A 312 ? 0.6615 0.6198 0.4388 0.3152  0.0048  -0.0115 312 LEU A CA  
2041  C C   . LEU A 312 ? 0.6637 0.5987 0.4259 0.3082  0.0024  -0.0152 312 LEU A C   
2042  O O   . LEU A 312 ? 0.6802 0.6256 0.4283 0.3212  0.0088  -0.0125 312 LEU A O   
2043  C CB  . LEU A 312 ? 0.6459 0.6548 0.4511 0.3220  0.0164  0.0028  312 LEU A CB  
2044  C CG  . LEU A 312 ? 0.6098 0.6316 0.4476 0.3044  0.0159  0.0103  312 LEU A CG  
2045  C CD1 . LEU A 312 ? 0.5936 0.5973 0.4442 0.2897  0.0063  0.0058  312 LEU A CD1 
2046  C CD2 . LEU A 312 ? 0.5960 0.6736 0.4631 0.3103  0.0264  0.0274  312 LEU A CD2 
2047  N N   . ALA A 313 ? 0.6414 0.5463 0.4069 0.2874  -0.0066 -0.0205 313 ALA A N   
2048  C CA  . ALA A 313 ? 0.6406 0.5229 0.3949 0.2776  -0.0098 -0.0231 313 ALA A CA  
2049  C C   . ALA A 313 ? 0.6099 0.5007 0.3889 0.2630  -0.0070 -0.0167 313 ALA A C   
2050  O O   . ALA A 313 ? 0.6095 0.4914 0.3818 0.2590  -0.0060 -0.0161 313 ALA A O   
2051  C CB  . ALA A 313 ? 0.6468 0.4894 0.3858 0.2636  -0.0225 -0.0321 313 ALA A CB  
2052  N N   . VAL A 314 ? 0.5882 0.4948 0.3950 0.2551  -0.0066 -0.0115 314 VAL A N   
2053  C CA  . VAL A 314 ? 0.5604 0.4747 0.3916 0.2414  -0.0056 -0.0041 314 VAL A CA  
2054  C C   . VAL A 314 ? 0.5455 0.5042 0.4057 0.2485  0.0008  0.0082  314 VAL A C   
2055  O O   . VAL A 314 ? 0.5420 0.5087 0.4125 0.2490  -0.0019 0.0081  314 VAL A O   
2056  C CB  . VAL A 314 ? 0.5433 0.4270 0.3809 0.2179  -0.0155 -0.0090 314 VAL A CB  
2057  C CG1 . VAL A 314 ? 0.5179 0.4084 0.3792 0.2048  -0.0152 -0.0005 314 VAL A CG1 
2058  C CG2 . VAL A 314 ? 0.5539 0.4031 0.3690 0.2080  -0.0220 -0.0175 314 VAL A CG2 
2059  N N   . LEU A 315 ? 0.5110 0.5021 0.3868 0.2527  0.0087  0.0203  315 LEU A N   
2060  C CA  . LEU A 315 ? 0.4924 0.5335 0.4023 0.2508  0.0137  0.0359  315 LEU A CA  
2061  C C   . LEU A 315 ? 0.4909 0.5379 0.4231 0.2219  0.0122  0.0444  315 LEU A C   
2062  O O   . LEU A 315 ? 0.5077 0.5577 0.4362 0.2173  0.0171  0.0479  315 LEU A O   
2063  C CB  . LEU A 315 ? 0.5050 0.5906 0.4164 0.2717  0.0259  0.0452  315 LEU A CB  
2064  C CG  . LEU A 315 ? 0.4886 0.6302 0.4364 0.2666  0.0309  0.0629  315 LEU A CG  
2065  C CD1 . LEU A 315 ? 0.4855 0.6292 0.4433 0.2697  0.0248  0.0613  315 LEU A CD1 
2066  C CD2 . LEU A 315 ? 0.5020 0.6879 0.4501 0.2879  0.0442  0.0736  315 LEU A CD2 
2067  N N   . HIS A 316 ? 0.4770 0.5247 0.4311 0.2029  0.0053  0.0476  316 HIS A N   
2068  C CA  . HIS A 316 ? 0.4557 0.5064 0.4310 0.1754  0.0026  0.0552  316 HIS A CA  
2069  C C   . HIS A 316 ? 0.4414 0.5374 0.4505 0.1660  0.0030  0.0700  316 HIS A C   
2070  O O   . HIS A 316 ? 0.4344 0.5284 0.4548 0.1591  -0.0043 0.0694  316 HIS A O   
2071  C CB  . HIS A 316 ? 0.4484 0.4534 0.4166 0.1597  -0.0075 0.0454  316 HIS A CB  
2072  C CG  . HIS A 316 ? 0.4600 0.4222 0.3996 0.1640  -0.0090 0.0341  316 HIS A CG  
2073  N ND1 . HIS A 316 ? 0.4562 0.3763 0.3866 0.1529  -0.0172 0.0259  316 HIS A ND1 
2074  C CD2 . HIS A 316 ? 0.4766 0.4321 0.3947 0.1782  -0.0040 0.0304  316 HIS A CD2 
2075  C CE1 . HIS A 316 ? 0.4692 0.3589 0.3754 0.1590  -0.0177 0.0185  316 HIS A CE1 
2076  N NE2 . HIS A 316 ? 0.4824 0.3914 0.3797 0.1742  -0.0102 0.0204  316 HIS A NE2 
2077  N N   . LEU A 317 ? 0.4225 0.5591 0.4477 0.1654  0.0111  0.0839  317 LEU A N   
2078  C CA  . LEU A 317 ? 0.4037 0.5869 0.4633 0.1555  0.0113  0.1007  317 LEU A CA  
2079  C C   . LEU A 317 ? 0.3995 0.5899 0.4806 0.1288  0.0087  0.1108  317 LEU A C   
2080  O O   . LEU A 317 ? 0.3837 0.6140 0.4947 0.1186  0.0084  0.1269  317 LEU A O   
2081  C CB  . LEU A 317 ? 0.4130 0.6441 0.4785 0.1766  0.0225  0.1122  317 LEU A CB  
2082  C CG  . LEU A 317 ? 0.4302 0.6651 0.4805 0.2044  0.0256  0.1060  317 LEU A CG  
2083  C CD1 . LEU A 317 ? 0.4336 0.7277 0.5038 0.2186  0.0351  0.1235  317 LEU A CD1 
2084  C CD2 . LEU A 317 ? 0.4264 0.6382 0.4775 0.1996  0.0148  0.0975  317 LEU A CD2 
2085  N N   . TYR A 318 ? 0.4247 0.5776 0.4923 0.1170  0.0062  0.1026  318 TYR A N   
2086  C CA  . TYR A 318 ? 0.4230 0.5820 0.5081 0.0944  0.0053  0.1121  318 TYR A CA  
2087  C C   . TYR A 318 ? 0.4128 0.5707 0.5210 0.0715  -0.0055 0.1167  318 TYR A C   
2088  O O   . TYR A 318 ? 0.4101 0.5569 0.5176 0.0724  -0.0126 0.1108  318 TYR A O   
2089  C CB  . TYR A 318 ? 0.4397 0.5581 0.5027 0.0896  0.0058  0.1021  318 TYR A CB  
2090  C CG  . TYR A 318 ? 0.4470 0.5149 0.4930 0.0839  -0.0028 0.0871  318 TYR A CG  
2091  C CD1 . TYR A 318 ? 0.4417 0.4916 0.4995 0.0616  -0.0109 0.0874  318 TYR A CD1 
2092  C CD2 . TYR A 318 ? 0.4543 0.4923 0.4720 0.1014  -0.0030 0.0731  318 TYR A CD2 
2093  C CE1 . TYR A 318 ? 0.4402 0.4462 0.4825 0.0577  -0.0177 0.0750  318 TYR A CE1 
2094  C CE2 . TYR A 318 ? 0.4524 0.4466 0.4562 0.0962  -0.0107 0.0614  318 TYR A CE2 
2095  C CZ  . TYR A 318 ? 0.4464 0.4261 0.4628 0.0747  -0.0174 0.0628  318 TYR A CZ  
2096  O OH  . TYR A 318 ? 0.4400 0.3783 0.4427 0.0707  -0.0241 0.0524  318 TYR A OH  
2097  N N   . LEU A 319 ? 0.4028 0.5719 0.5308 0.0511  -0.0071 0.1276  319 LEU A N   
2098  C CA  . LEU A 319 ? 0.3932 0.5588 0.5419 0.0278  -0.0182 0.1324  319 LEU A CA  
2099  C C   . LEU A 319 ? 0.3930 0.5916 0.5627 0.0291  -0.0231 0.1413  319 LEU A C   
2100  O O   . LEU A 319 ? 0.3937 0.5749 0.5618 0.0254  -0.0323 0.1345  319 LEU A O   
2101  C CB  . LEU A 319 ? 0.3928 0.5053 0.5231 0.0195  -0.0260 0.1168  319 LEU A CB  
2102  C CG  . LEU A 319 ? 0.3870 0.4733 0.5152 0.0020  -0.0273 0.1158  319 LEU A CG  
2103  C CD1 . LEU A 319 ? 0.3872 0.4259 0.5005 -0.0057 -0.0352 0.1026  319 LEU A CD1 
2104  C CD2 . LEU A 319 ? 0.3794 0.4934 0.5370 -0.0176 -0.0304 0.1320  319 LEU A CD2 
2105  N N   . ASN A 320 ? 0.3951 0.6435 0.5849 0.0347  -0.0169 0.1577  320 ASN A N   
2106  C CA  . ASN A 320 ? 0.3663 0.6537 0.5791 0.0371  -0.0204 0.1696  320 ASN A CA  
2107  C C   . ASN A 320 ? 0.3393 0.6777 0.5837 0.0287  -0.0171 0.1927  320 ASN A C   
2108  O O   . ASN A 320 ? 0.3316 0.6699 0.5811 0.0170  -0.0147 0.1983  320 ASN A O   
2109  C CB  . ASN A 320 ? 0.3758 0.6720 0.5730 0.0650  -0.0133 0.1634  320 ASN A CB  
2110  C CG  . ASN A 320 ? 0.3894 0.6536 0.5731 0.0678  -0.0220 0.1489  320 ASN A CG  
2111  O OD1 . ASN A 320 ? 0.3780 0.6572 0.5795 0.0610  -0.0305 0.1549  320 ASN A OD1 
2112  N ND2 . ASN A 320 ? 0.4130 0.6334 0.5654 0.0776  -0.0204 0.1306  320 ASN A ND2 
2113  N N   . GLN A 321 ? 0.3624 0.7458 0.6294 0.0344  -0.0172 0.2072  321 GLN A N   
2114  C CA  . GLN A 321 ? 0.3444 0.7817 0.6453 0.0268  -0.0149 0.2321  321 GLN A CA  
2115  C C   . GLN A 321 ? 0.3509 0.8358 0.6561 0.0526  -0.0017 0.2430  321 GLN A C   
2116  O O   . GLN A 321 ? 0.3541 0.8803 0.6833 0.0493  -0.0015 0.2617  321 GLN A O   
2117  C CB  . GLN A 321 ? 0.3391 0.7907 0.6714 0.0033  -0.0306 0.2447  321 GLN A CB  
2118  C CG  . GLN A 321 ? 0.3369 0.7384 0.6617 -0.0195 -0.0451 0.2320  321 GLN A CG  
2119  C CD  . GLN A 321 ? 0.3356 0.7512 0.6900 -0.0421 -0.0618 0.2449  321 GLN A CD  
2120  O OE1 . GLN A 321 ? 0.3493 0.7825 0.7161 -0.0534 -0.0617 0.2598  321 GLN A OE1 
2121  N NE2 . GLN A 321 ? 0.3398 0.7248 0.6846 -0.0470 -0.0737 0.2326  321 GLN A NE2 
2122  N N   . LEU A 322 ? 0.3445 0.8140 0.6182 0.0780  0.0098  0.2292  322 LEU A N   
2123  C CA  . LEU A 322 ? 0.3539 0.8667 0.6281 0.1050  0.0233  0.2389  322 LEU A CA  
2124  C C   . LEU A 322 ? 0.3566 0.9024 0.6403 0.1036  0.0339  0.2555  322 LEU A C   
2125  O O   . LEU A 322 ? 0.3494 0.8825 0.6293 0.0956  0.0357  0.2537  322 LEU A O   
2126  C CB  . LEU A 322 ? 0.3689 0.8506 0.6027 0.1328  0.0314  0.2181  322 LEU A CB  
2127  C CG  . LEU A 322 ? 0.3722 0.8109 0.5871 0.1356  0.0223  0.1984  322 LEU A CG  
2128  C CD1 . LEU A 322 ? 0.3910 0.7687 0.5779 0.1267  0.0173  0.1776  322 LEU A CD1 
2129  C CD2 . LEU A 322 ? 0.3879 0.8348 0.5851 0.1671  0.0301  0.1926  322 LEU A CD2 
2130  N N   . ASN A 323 ? 0.3547 0.9362 0.6455 0.1101  0.0405  0.2707  323 ASN A N   
2131  C CA  . ASN A 323 ? 0.3647 0.9747 0.6605 0.1085  0.0492  0.2880  323 ASN A CA  
2132  C C   . ASN A 323 ? 0.3866 1.0163 0.6597 0.1400  0.0652  0.2889  323 ASN A C   
2133  O O   . ASN A 323 ? 0.3945 1.0107 0.6457 0.1624  0.0693  0.2743  323 ASN A O   
2134  C CB  . ASN A 323 ? 0.3670 1.0002 0.6925 0.0854  0.0404  0.3087  323 ASN A CB  
2135  C CG  . ASN A 323 ? 0.3779 1.0334 0.7121 0.0930  0.0393  0.3159  323 ASN A CG  
2136  O OD1 . ASN A 323 ? 0.3930 1.0659 0.7129 0.1183  0.0509  0.3164  323 ASN A OD1 
2137  N ND2 . ASN A 323 ? 0.3726 1.0254 0.7288 0.0710  0.0247  0.3214  323 ASN A ND2 
2138  N N   . GLY A 324 ? 0.3810 1.0396 0.6569 0.1421  0.0732  0.3060  324 GLY A N   
2139  C CA  . GLY A 324 ? 0.4054 1.0839 0.6593 0.1712  0.0876  0.3092  324 GLY A CA  
2140  C C   . GLY A 324 ? 0.4120 1.0684 0.6324 0.1906  0.0968  0.2935  324 GLY A C   
2141  O O   . GLY A 324 ? 0.3966 1.0267 0.6134 0.1803  0.0935  0.2831  324 GLY A O   
2142  N N   . SER A 325 ? 0.4455 1.1112 0.6396 0.2195  0.1083  0.2919  325 SER A N   
2143  C CA  . SER A 325 ? 0.4600 1.1050 0.6176 0.2409  0.1169  0.2781  325 SER A CA  
2144  C C   . SER A 325 ? 0.4663 1.0719 0.5941 0.2593  0.1160  0.2527  325 SER A C   
2145  O O   . SER A 325 ? 0.4662 1.0680 0.5981 0.2621  0.1117  0.2481  325 SER A O   
2146  C CB  . SER A 325 ? 0.4902 1.1643 0.6320 0.2627  0.1283  0.2909  325 SER A CB  
2147  O OG  . SER A 325 ? 0.4879 1.2017 0.6599 0.2471  0.1278  0.3169  325 SER A OG  
2148  N N   . ILE A 326 ? 0.5190 1.0928 0.6155 0.2713  0.1192  0.2363  326 ILE A N   
2149  C CA  . ILE A 326 ? 0.5314 1.0608 0.5933 0.2898  0.1174  0.2115  326 ILE A CA  
2150  C C   . ILE A 326 ? 0.5670 1.1024 0.6010 0.3182  0.1244  0.2099  326 ILE A C   
2151  O O   . ILE A 326 ? 0.5898 1.1420 0.6079 0.3328  0.1329  0.2177  326 ILE A O   
2152  C CB  . ILE A 326 ? 0.5323 1.0235 0.5676 0.2931  0.1176  0.1954  326 ILE A CB  
2153  C CG1 . ILE A 326 ? 0.4971 0.9839 0.5617 0.2648  0.1108  0.1985  326 ILE A CG1 
2154  C CG2 . ILE A 326 ? 0.5501 0.9902 0.5470 0.3112  0.1134  0.1700  326 ILE A CG2 
2155  C CD1 . ILE A 326 ? 0.4988 0.9574 0.5424 0.2640  0.1128  0.1888  326 ILE A CD1 
2156  N N   . PRO A 327 ? 0.5458 1.0681 0.5733 0.3267  0.1207  0.2007  327 PRO A N   
2157  C CA  . PRO A 327 ? 0.5811 1.1075 0.5818 0.3534  0.1269  0.1992  327 PRO A CA  
2158  C C   . PRO A 327 ? 0.6114 1.1014 0.5643 0.3754  0.1294  0.1823  327 PRO A C   
2159  O O   . PRO A 327 ? 0.6090 1.0520 0.5413 0.3740  0.1227  0.1620  327 PRO A O   
2160  C CB  . PRO A 327 ? 0.5772 1.0869 0.5813 0.3533  0.1197  0.1891  327 PRO A CB  
2161  C CG  . PRO A 327 ? 0.5390 1.0554 0.5828 0.3247  0.1109  0.1945  327 PRO A CG  
2162  C CD  . PRO A 327 ? 0.5219 1.0277 0.5689 0.3112  0.1099  0.1933  327 PRO A CD  
2163  N N   . PRO A 328 ? 0.6241 1.1333 0.5579 0.3956  0.1378  0.1907  328 PRO A N   
2164  C CA  . PRO A 328 ? 0.6582 1.1304 0.5442 0.4177  0.1382  0.1744  328 PRO A CA  
2165  C C   . PRO A 328 ? 0.6776 1.1032 0.5324 0.4303  0.1309  0.1523  328 PRO A C   
2166  O O   . PRO A 328 ? 0.7012 1.0839 0.5175 0.4419  0.1266  0.1352  328 PRO A O   
2167  C CB  . PRO A 328 ? 0.6882 1.1976 0.5659 0.4378  0.1479  0.1912  328 PRO A CB  
2168  C CG  . PRO A 328 ? 0.6630 1.2271 0.5863 0.4199  0.1528  0.2173  328 PRO A CG  
2169  C CD  . PRO A 328 ? 0.6301 1.1947 0.5857 0.3981  0.1462  0.2166  328 PRO A CD  
2170  N N   . GLU A 329 ? 0.6956 1.1273 0.5659 0.4271  0.1284  0.1528  329 GLU A N   
2171  C CA  . GLU A 329 ? 0.7127 1.1010 0.5564 0.4367  0.1206  0.1329  329 GLU A CA  
2172  C C   . GLU A 329 ? 0.6951 1.0332 0.5317 0.4217  0.1094  0.1133  329 GLU A C   
2173  O O   . GLU A 329 ? 0.7125 1.0072 0.5220 0.4285  0.1013  0.0955  329 GLU A O   
2174  C CB  . GLU A 329 ? 0.7070 1.1196 0.5731 0.4361  0.1212  0.1407  329 GLU A CB  
2175  C CG  . GLU A 329 ? 0.7278 1.1884 0.5995 0.4520  0.1320  0.1606  329 GLU A CG  
2176  C CD  . GLU A 329 ? 0.7020 1.2174 0.6169 0.4359  0.1381  0.1857  329 GLU A CD  
2177  O OE1 . GLU A 329 ? 0.6755 1.1920 0.6077 0.4170  0.1360  0.1881  329 GLU A OE1 
2178  O OE2 . GLU A 329 ? 0.7094 1.2664 0.6413 0.4415  0.1443  0.2039  329 GLU A OE2 
2179  N N   . LEU A 330 ? 0.7005 1.0433 0.5614 0.4010  0.1081  0.1170  330 LEU A N   
2180  C CA  . LEU A 330 ? 0.6865 0.9805 0.5385 0.3880  0.0978  0.0993  330 LEU A CA  
2181  C C   . LEU A 330 ? 0.7157 0.9646 0.5232 0.3995  0.0941  0.0835  330 LEU A C   
2182  O O   . LEU A 330 ? 0.7152 0.9151 0.5060 0.3924  0.0836  0.0665  330 LEU A O   
2183  C CB  . LEU A 330 ? 0.6469 0.9581 0.5349 0.3646  0.0976  0.1086  330 LEU A CB  
2184  C CG  . LEU A 330 ? 0.6179 0.9692 0.5532 0.3477  0.0972  0.1244  330 LEU A CG  
2185  C CD1 . LEU A 330 ? 0.5787 0.9282 0.5426 0.3232  0.0916  0.1276  330 LEU A CD1 
2186  C CD2 . LEU A 330 ? 0.6184 0.9561 0.5538 0.3503  0.0905  0.1167  330 LEU A CD2 
2187  N N   . GLY A 331 ? 0.7162 0.9802 0.5047 0.4162  0.1013  0.0896  331 GLY A N   
2188  C CA  . GLY A 331 ? 0.7490 0.9698 0.4939 0.4287  0.0959  0.0752  331 GLY A CA  
2189  C C   . GLY A 331 ? 0.7800 0.9610 0.4928 0.4412  0.0868  0.0597  331 GLY A C   
2190  O O   . GLY A 331 ? 0.8039 0.9394 0.4827 0.4459  0.0778  0.0454  331 GLY A O   
2191  N N   . GLU A 332 ? 0.7832 0.9806 0.5073 0.4457  0.0881  0.0630  332 GLU A N   
2192  C CA  . GLU A 332 ? 0.8125 0.9774 0.5092 0.4577  0.0803  0.0503  332 GLU A CA  
2193  C C   . GLU A 332 ? 0.7955 0.9202 0.4951 0.4403  0.0678  0.0360  332 GLU A C   
2194  O O   . GLU A 332 ? 0.8170 0.9133 0.4964 0.4470  0.0600  0.0255  332 GLU A O   
2195  C CB  . GLU A 332 ? 0.8243 1.0282 0.5307 0.4726  0.0886  0.0620  332 GLU A CB  
2196  C CG  . GLU A 332 ? 0.8295 1.0859 0.5474 0.4838  0.1023  0.0819  332 GLU A CG  
2197  C CD  . GLU A 332 ? 0.8724 1.1174 0.5522 0.5066  0.1037  0.0796  332 GLU A CD  
2198  O OE1 . GLU A 332 ? 0.9038 1.1058 0.5485 0.5179  0.0947  0.0642  332 GLU A OE1 
2199  O OE2 . GLU A 332 ? 0.8753 1.1543 0.5612 0.5128  0.1131  0.0937  332 GLU A OE2 
2200  N N   . MET A 333 ? 0.8001 0.9225 0.5247 0.4184  0.0656  0.0361  333 MET A N   
2201  C CA  . MET A 333 ? 0.7833 0.8665 0.5108 0.4008  0.0533  0.0234  333 MET A CA  
2202  C C   . MET A 333 ? 0.8029 0.8337 0.4961 0.3986  0.0423  0.0089  333 MET A C   
2203  O O   . MET A 333 ? 0.7887 0.8042 0.4830 0.3859  0.0397  0.0068  333 MET A O   
2204  C CB  . MET A 333 ? 0.7382 0.8381 0.5040 0.3796  0.0545  0.0301  333 MET A CB  
2205  C CG  . MET A 333 ? 0.7228 0.8832 0.5247 0.3810  0.0661  0.0493  333 MET A CG  
2206  S SD  . MET A 333 ? 0.6716 0.8564 0.5215 0.3559  0.0660  0.0604  333 MET A SD  
2207  C CE  . MET A 333 ? 0.6600 0.7823 0.4981 0.3393  0.0506  0.0414  333 MET A CE  
2208  N N   . GLU A 334 ? 0.8027 0.8066 0.4658 0.4109  0.0352  -0.0002 334 GLU A N   
2209  C CA  . GLU A 334 ? 0.8297 0.7899 0.4582 0.4129  0.0247  -0.0110 334 GLU A CA  
2210  C C   . GLU A 334 ? 0.8093 0.7309 0.4411 0.3884  0.0126  -0.0199 334 GLU A C   
2211  O O   . GLU A 334 ? 0.8138 0.7127 0.4319 0.3826  0.0078  -0.0234 334 GLU A O   
2212  C CB  . GLU A 334 ? 0.8692 0.8103 0.4689 0.4299  0.0185  -0.0177 334 GLU A CB  
2213  C CG  . GLU A 334 ? 0.8973 0.8713 0.4869 0.4564  0.0295  -0.0092 334 GLU A CG  
2214  C CD  . GLU A 334 ? 0.9240 0.8916 0.4998 0.4705  0.0264  -0.0131 334 GLU A CD  
2215  O OE1 . GLU A 334 ? 0.9053 0.8723 0.4990 0.4601  0.0236  -0.0151 334 GLU A OE1 
2216  O OE2 . GLU A 334 ? 0.9677 0.9307 0.5148 0.4926  0.0267  -0.0139 334 GLU A OE2 
2217  N N   . SER A 335 ? 0.7682 0.6830 0.4187 0.3738  0.0076  -0.0229 335 SER A N   
2218  C CA  . SER A 335 ? 0.7513 0.6301 0.4047 0.3506  -0.0044 -0.0304 335 SER A CA  
2219  C C   . SER A 335 ? 0.7160 0.6019 0.3936 0.3326  -0.0012 -0.0260 335 SER A C   
2220  O O   . SER A 335 ? 0.6994 0.5586 0.3824 0.3121  -0.0102 -0.0306 335 SER A O   
2221  C CB  . SER A 335 ? 0.7426 0.6124 0.4066 0.3423  -0.0110 -0.0345 335 SER A CB  
2222  O OG  . SER A 335 ? 0.7763 0.6317 0.4159 0.3565  -0.0164 -0.0399 335 SER A OG  
2223  N N   . MET A 336 ? 0.7244 0.6476 0.4181 0.3394  0.0115  -0.0159 336 MET A N   
2224  C CA  . MET A 336 ? 0.6893 0.6240 0.4108 0.3232  0.0151  -0.0099 336 MET A CA  
2225  C C   . MET A 336 ? 0.6878 0.5893 0.3967 0.3101  0.0085  -0.0151 336 MET A C   
2226  O O   . MET A 336 ? 0.7112 0.6029 0.3954 0.3195  0.0085  -0.0169 336 MET A O   
2227  C CB  . MET A 336 ? 0.6793 0.6657 0.4211 0.3341  0.0301  0.0043  336 MET A CB  
2228  C CG  . MET A 336 ? 0.6443 0.6490 0.4190 0.3186  0.0341  0.0133  336 MET A CG  
2229  S SD  . MET A 336 ? 0.6167 0.5939 0.4117 0.2941  0.0223  0.0082  336 MET A SD  
2230  C CE  . MET A 336 ? 0.6089 0.6157 0.4237 0.3005  0.0240  0.0128  336 MET A CE  
2231  N N   . ILE A 337 ? 0.6750 0.5594 0.4012 0.2879  0.0024  -0.0165 337 ILE A N   
2232  C CA  . ILE A 337 ? 0.6705 0.5257 0.3904 0.2717  -0.0038 -0.0197 337 ILE A CA  
2233  C C   . ILE A 337 ? 0.6451 0.5156 0.3924 0.2603  0.0021  -0.0111 337 ILE A C   
2234  O O   . ILE A 337 ? 0.6466 0.5121 0.3891 0.2578  0.0044  -0.0086 337 ILE A O   
2235  C CB  . ILE A 337 ? 0.6645 0.4839 0.3799 0.2529  -0.0178 -0.0277 337 ILE A CB  
2236  C CG1 . ILE A 337 ? 0.6963 0.4965 0.3820 0.2635  -0.0254 -0.0348 337 ILE A CG1 
2237  C CG2 . ILE A 337 ? 0.6499 0.4477 0.3696 0.2315  -0.0230 -0.0278 337 ILE A CG2 
2238  C CD1 . ILE A 337 ? 0.6919 0.4671 0.3779 0.2471  -0.0378 -0.0401 337 ILE A CD1 
2239  N N   . ASP A 338 ? 0.6073 0.4964 0.3837 0.2537  0.0038  -0.0055 338 ASP A N   
2240  C CA  . ASP A 338 ? 0.5775 0.4787 0.3826 0.2408  0.0061  0.0043  338 ASP A CA  
2241  C C   . ASP A 338 ? 0.5641 0.5177 0.3973 0.2494  0.0156  0.0178  338 ASP A C   
2242  O O   . ASP A 338 ? 0.5557 0.5211 0.4041 0.2501  0.0136  0.0191  338 ASP A O   
2243  C CB  . ASP A 338 ? 0.5590 0.4325 0.3750 0.2174  -0.0042 0.0001  338 ASP A CB  
2244  C CG  . ASP A 338 ? 0.5321 0.4119 0.3738 0.2015  -0.0039 0.0103  338 ASP A CG  
2245  O OD1 . ASP A 338 ? 0.5252 0.4292 0.3765 0.1947  0.0032  0.0193  338 ASP A OD1 
2246  O OD2 . ASP A 338 ? 0.5161 0.3823 0.3707 0.1856  -0.0105 0.0093  338 ASP A OD2 
2247  N N   . LEU A 339 ? 0.5270 0.5156 0.3692 0.2491  0.0254  0.0286  339 LEU A N   
2248  C CA  . LEU A 339 ? 0.5201 0.5651 0.3913 0.2503  0.0346  0.0440  339 LEU A CA  
2249  C C   . LEU A 339 ? 0.5172 0.5808 0.4192 0.2217  0.0350  0.0566  339 LEU A C   
2250  O O   . LEU A 339 ? 0.5319 0.5949 0.4303 0.2144  0.0383  0.0602  339 LEU A O   
2251  C CB  . LEU A 339 ? 0.5302 0.6048 0.3873 0.2758  0.0463  0.0483  339 LEU A CB  
2252  C CG  . LEU A 339 ? 0.5205 0.6577 0.4072 0.2804  0.0568  0.0663  339 LEU A CG  
2253  C CD1 . LEU A 339 ? 0.5109 0.6616 0.4171 0.2809  0.0531  0.0683  339 LEU A CD1 
2254  C CD2 . LEU A 339 ? 0.5475 0.7093 0.4144 0.3102  0.0688  0.0690  339 LEU A CD2 
2255  N N   . GLU A 340 ? 0.4923 0.5710 0.4236 0.2057  0.0310  0.0633  340 GLU A N   
2256  C CA  . GLU A 340 ? 0.4816 0.5713 0.4412 0.1775  0.0289  0.0738  340 GLU A CA  
2257  C C   . GLU A 340 ? 0.4645 0.6036 0.4584 0.1721  0.0315  0.0894  340 GLU A C   
2258  O O   . GLU A 340 ? 0.4557 0.5968 0.4598 0.1715  0.0261  0.0881  340 GLU A O   
2259  C CB  . GLU A 340 ? 0.4771 0.5231 0.4353 0.1586  0.0177  0.0646  340 GLU A CB  
2260  C CG  . GLU A 340 ? 0.4835 0.4795 0.4082 0.1673  0.0128  0.0487  340 GLU A CG  
2261  C CD  . GLU A 340 ? 0.4746 0.4323 0.3998 0.1458  0.0044  0.0440  340 GLU A CD  
2262  O OE1 . GLU A 340 ? 0.4616 0.4130 0.4010 0.1339  -0.0017 0.0437  340 GLU A OE1 
2263  O OE2 . GLU A 340 ? 0.4791 0.4136 0.3901 0.1412  0.0041  0.0411  340 GLU A OE2 
2264  N N   . ILE A 341 ? 0.4771 0.6565 0.4895 0.1677  0.0391  0.1049  341 ILE A N   
2265  C CA  . ILE A 341 ? 0.4518 0.6814 0.4998 0.1605  0.0410  0.1228  341 ILE A CA  
2266  C C   . ILE A 341 ? 0.4469 0.6878 0.5201 0.1334  0.0390  0.1351  341 ILE A C   
2267  O O   . ILE A 341 ? 0.4229 0.7102 0.5243 0.1275  0.0429  0.1535  341 ILE A O   
2268  C CB  . ILE A 341 ? 0.4418 0.7181 0.4909 0.1850  0.0531  0.1334  341 ILE A CB  
2269  C CG1 . ILE A 341 ? 0.4572 0.7118 0.4714 0.2145  0.0560  0.1182  341 ILE A CG1 
2270  C CG2 . ILE A 341 ? 0.4208 0.7446 0.5045 0.1818  0.0529  0.1497  341 ILE A CG2 
2271  C CD1 . ILE A 341 ? 0.4562 0.7475 0.4611 0.2421  0.0694  0.1256  341 ILE A CD1 
2272  N N   . SER A 342 ? 0.4517 0.6510 0.5154 0.1170  0.0328  0.1260  342 SER A N   
2273  C CA  . SER A 342 ? 0.4387 0.6435 0.5220 0.0928  0.0313  0.1362  342 SER A CA  
2274  C C   . SER A 342 ? 0.4158 0.6370 0.5320 0.0716  0.0231  0.1465  342 SER A C   
2275  O O   . SER A 342 ? 0.4135 0.6354 0.5353 0.0738  0.0173  0.1437  342 SER A O   
2276  C CB  . SER A 342 ? 0.4599 0.6145 0.5236 0.0822  0.0269  0.1238  342 SER A CB  
2277  O OG  . SER A 342 ? 0.4876 0.6191 0.5180 0.1015  0.0312  0.1120  342 SER A OG  
2278  N N   . GLU A 343 ? 0.4371 0.6704 0.5746 0.0508  0.0218  0.1585  343 GLU A N   
2279  C CA  . GLU A 343 ? 0.4104 0.6535 0.5778 0.0275  0.0121  0.1682  343 GLU A CA  
2280  C C   . GLU A 343 ? 0.3902 0.6747 0.5795 0.0331  0.0107  0.1793  343 GLU A C   
2281  O O   . GLU A 343 ? 0.3916 0.6658 0.5856 0.0285  0.0016  0.1748  343 GLU A O   
2282  C CB  . GLU A 343 ? 0.4251 0.6180 0.5822 0.0139  0.0012  0.1537  343 GLU A CB  
2283  C CG  . GLU A 343 ? 0.4549 0.6027 0.5836 0.0160  0.0031  0.1394  343 GLU A CG  
2284  C CD  . GLU A 343 ? 0.4510 0.5577 0.5780 -0.0030 -0.0065 0.1318  343 GLU A CD  
2285  O OE1 . GLU A 343 ? 0.4178 0.5328 0.5675 -0.0227 -0.0128 0.1410  343 GLU A OE1 
2286  O OE2 . GLU A 343 ? 0.4775 0.5435 0.5803 0.0020  -0.0081 0.1172  343 GLU A OE2 
2287  N N   . ASN A 344 ? 0.3827 0.7157 0.5851 0.0438  0.0202  0.1949  344 ASN A N   
2288  C CA  . ASN A 344 ? 0.3585 0.7371 0.5828 0.0516  0.0209  0.2083  344 ASN A CA  
2289  C C   . ASN A 344 ? 0.3340 0.7659 0.5895 0.0442  0.0259  0.2332  344 ASN A C   
2290  O O   . ASN A 344 ? 0.3281 0.7577 0.5901 0.0297  0.0266  0.2391  344 ASN A O   
2291  C CB  . ASN A 344 ? 0.3787 0.7620 0.5798 0.0828  0.0298  0.1997  344 ASN A CB  
2292  C CG  . ASN A 344 ? 0.4005 0.7516 0.5878 0.0875  0.0216  0.1837  344 ASN A CG  
2293  O OD1 . ASN A 344 ? 0.3917 0.7576 0.5993 0.0799  0.0137  0.1898  344 ASN A OD1 
2294  N ND2 . ASN A 344 ? 0.4303 0.7370 0.5829 0.0997  0.0227  0.1637  344 ASN A ND2 
2295  N N   . LYS A 345 ? 0.3085 0.7898 0.5847 0.0544  0.0295  0.2489  345 LYS A N   
2296  C CA  . LYS A 345 ? 0.3102 0.8388 0.6106 0.0492  0.0344  0.2725  345 LYS A CA  
2297  C C   . LYS A 345 ? 0.3281 0.8867 0.6136 0.0782  0.0494  0.2774  345 LYS A C   
2298  O O   . LYS A 345 ? 0.3414 0.9314 0.6371 0.0796  0.0516  0.2935  345 LYS A O   
2299  C CB  . LYS A 345 ? 0.3128 0.8503 0.6370 0.0284  0.0214  0.2844  345 LYS A CB  
2300  C CG  . LYS A 345 ? 0.3025 0.8060 0.6366 -0.0009 0.0059  0.2800  345 LYS A CG  
2301  C CD  . LYS A 345 ? 0.3109 0.8208 0.6643 -0.0194 -0.0073 0.2916  345 LYS A CD  
2302  C CE  . LYS A 345 ? 0.3068 0.7764 0.6631 -0.0458 -0.0229 0.2848  345 LYS A CE  
2303  N NZ  . LYS A 345 ? 0.2935 0.7302 0.6404 -0.0461 -0.0282 0.2660  345 LYS A NZ  
2304  N N   . LEU A 346 ? 0.3514 0.8975 0.6102 0.1025  0.0593  0.2631  346 LEU A N   
2305  C CA  . LEU A 346 ? 0.3735 0.9398 0.6106 0.1314  0.0734  0.2648  346 LEU A CA  
2306  C C   . LEU A 346 ? 0.3831 0.9712 0.6207 0.1287  0.0809  0.2797  346 LEU A C   
2307  O O   . LEU A 346 ? 0.3723 0.9503 0.6180 0.1094  0.0774  0.2827  346 LEU A O   
2308  C CB  . LEU A 346 ? 0.3818 0.9157 0.5822 0.1567  0.0794  0.2425  346 LEU A CB  
2309  C CG  . LEU A 346 ? 0.3860 0.8806 0.5686 0.1627  0.0710  0.2228  346 LEU A CG  
2310  C CD1 . LEU A 346 ? 0.4089 0.8791 0.5494 0.1936  0.0789  0.2051  346 LEU A CD1 
2311  C CD2 . LEU A 346 ? 0.3806 0.9106 0.5917 0.1624  0.0669  0.2351  346 LEU A CD2 
2312  N N   . THR A 347 ? 0.3802 0.9969 0.6079 0.1489  0.0907  0.2893  347 THR A N   
2313  C CA  . THR A 347 ? 0.3931 1.0340 0.6206 0.1500  0.0972  0.3051  347 THR A CA  
2314  C C   . THR A 347 ? 0.4189 1.0671 0.6131 0.1839  0.1108  0.3003  347 THR A C   
2315  O O   . THR A 347 ? 0.4280 1.0603 0.5992 0.2049  0.1143  0.2847  347 THR A O   
2316  C CB  . THR A 347 ? 0.3976 1.0726 0.6544 0.1352  0.0920  0.3291  347 THR A CB  
2317  O OG1 . THR A 347 ? 0.4076 1.0998 0.6673 0.1471  0.0931  0.3324  347 THR A OG1 
2318  C CG2 . THR A 347 ? 0.3781 1.0393 0.6625 0.1009  0.0771  0.3333  347 THR A CG2 
2319  N N   . GLY A 348 ? 0.4662 1.1356 0.6560 0.1894  0.1171  0.3132  348 GLY A N   
2320  C CA  . GLY A 348 ? 0.4949 1.1731 0.6534 0.2210  0.1286  0.3111  348 GLY A CA  
2321  C C   . GLY A 348 ? 0.5005 1.1431 0.6236 0.2358  0.1331  0.2897  348 GLY A C   
2322  O O   . GLY A 348 ? 0.4804 1.0929 0.6041 0.2215  0.1284  0.2772  348 GLY A O   
2323  N N   . PRO A 349 ? 0.5099 1.1539 0.6002 0.2651  0.1418  0.2854  349 PRO A N   
2324  C CA  . PRO A 349 ? 0.5216 1.1290 0.5743 0.2803  0.1449  0.2653  349 PRO A CA  
2325  C C   . PRO A 349 ? 0.5276 1.0953 0.5531 0.2947  0.1430  0.2413  349 PRO A C   
2326  O O   . PRO A 349 ? 0.5298 1.1017 0.5600 0.3001  0.1412  0.2401  349 PRO A O   
2327  C CB  . PRO A 349 ? 0.5557 1.1825 0.5859 0.3056  0.1529  0.2727  349 PRO A CB  
2328  C CG  . PRO A 349 ? 0.5682 1.2292 0.6103 0.3149  0.1554  0.2874  349 PRO A CG  
2329  C CD  . PRO A 349 ? 0.5375 1.2164 0.6233 0.2852  0.1484  0.3003  349 PRO A CD  
2330  N N   . VAL A 350 ? 0.5791 1.1057 0.5754 0.3001  0.1424  0.2221  350 VAL A N   
2331  C CA  . VAL A 350 ? 0.5934 1.0749 0.5556 0.3169  0.1392  0.1978  350 VAL A CA  
2332  C C   . VAL A 350 ? 0.6369 1.1163 0.5635 0.3483  0.1432  0.1934  350 VAL A C   
2333  O O   . VAL A 350 ? 0.6601 1.1502 0.5719 0.3598  0.1481  0.1991  350 VAL A O   
2334  C CB  . VAL A 350 ? 0.5896 1.0250 0.5298 0.3118  0.1362  0.1798  350 VAL A CB  
2335  C CG1 . VAL A 350 ? 0.6127 0.9962 0.5152 0.3287  0.1303  0.1547  350 VAL A CG1 
2336  C CG2 . VAL A 350 ? 0.5543 0.9927 0.5306 0.2808  0.1327  0.1854  350 VAL A CG2 
2337  N N   . PRO A 351 ? 0.6273 1.0936 0.5403 0.3623  0.1407  0.1842  351 PRO A N   
2338  C CA  . PRO A 351 ? 0.6696 1.1318 0.5478 0.3919  0.1437  0.1802  351 PRO A CA  
2339  C C   . PRO A 351 ? 0.6973 1.1116 0.5301 0.4071  0.1403  0.1603  351 PRO A C   
2340  O O   . PRO A 351 ? 0.6897 1.0588 0.5084 0.3993  0.1329  0.1422  351 PRO A O   
2341  C CB  . PRO A 351 ? 0.6733 1.1265 0.5505 0.3978  0.1400  0.1732  351 PRO A CB  
2342  C CG  . PRO A 351 ? 0.6318 1.1034 0.5534 0.3710  0.1370  0.1816  351 PRO A CG  
2343  C CD  . PRO A 351 ? 0.6059 1.0653 0.5386 0.3510  0.1347  0.1795  351 PRO A CD  
2344  N N   . ASP A 352 ? 0.7538 1.1774 0.5635 0.4287  0.1448  0.1643  352 ASP A N   
2345  C CA  . ASP A 352 ? 0.7872 1.1645 0.5516 0.4455  0.1398  0.1457  352 ASP A CA  
2346  C C   . ASP A 352 ? 0.8079 1.1372 0.5417 0.4565  0.1305  0.1250  352 ASP A C   
2347  O O   . ASP A 352 ? 0.8306 1.1111 0.5292 0.4636  0.1224  0.1070  352 ASP A O   
2348  C CB  . ASP A 352 ? 0.8227 1.2224 0.5701 0.4688  0.1463  0.1551  352 ASP A CB  
2349  C CG  . ASP A 352 ? 0.8046 1.2578 0.5854 0.4587  0.1552  0.1789  352 ASP A CG  
2350  O OD1 . ASP A 352 ? 0.7942 1.2940 0.6044 0.4557  0.1609  0.1985  352 ASP A OD1 
2351  O OD2 . ASP A 352 ? 0.8017 1.2498 0.5796 0.4527  0.1559  0.1785  352 ASP A OD2 
2352  N N   . SER A 353 ? 0.7740 1.1157 0.5213 0.4565  0.1305  0.1277  353 SER A N   
2353  C CA  . SER A 353 ? 0.7916 1.0904 0.5137 0.4645  0.1213  0.1094  353 SER A CA  
2354  C C   . SER A 353 ? 0.7740 1.0224 0.4897 0.4471  0.1102  0.0910  353 SER A C   
2355  O O   . SER A 353 ? 0.7928 0.9968 0.4823 0.4526  0.1001  0.0743  353 SER A O   
2356  C CB  . SER A 353 ? 0.7824 1.1102 0.5272 0.4646  0.1245  0.1181  353 SER A CB  
2357  O OG  . SER A 353 ? 0.7378 1.0890 0.5251 0.4399  0.1258  0.1270  353 SER A OG  
2358  N N   . PHE A 354 ? 0.7655 1.0199 0.5050 0.4259  0.1115  0.0948  354 PHE A N   
2359  C CA  . PHE A 354 ? 0.7500 0.9566 0.4830 0.4097  0.1014  0.0786  354 PHE A CA  
2360  C C   . PHE A 354 ? 0.7829 0.9358 0.4720 0.4187  0.0918  0.0615  354 PHE A C   
2361  O O   . PHE A 354 ? 0.7797 0.8850 0.4563 0.4081  0.0804  0.0464  354 PHE A O   
2362  C CB  . PHE A 354 ? 0.7100 0.9367 0.4760 0.3871  0.1062  0.0880  354 PHE A CB  
2363  C CG  . PHE A 354 ? 0.6722 0.9281 0.4814 0.3703  0.1079  0.0978  354 PHE A CG  
2364  C CD1 . PHE A 354 ? 0.6702 0.9702 0.5017 0.3752  0.1134  0.1121  354 PHE A CD1 
2365  C CD2 . PHE A 354 ? 0.6402 0.8783 0.4685 0.3497  0.1028  0.0933  354 PHE A CD2 
2366  C CE1 . PHE A 354 ? 0.6370 0.9624 0.5092 0.3584  0.1127  0.1216  354 PHE A CE1 
2367  C CE2 . PHE A 354 ? 0.6068 0.8706 0.4766 0.3344  0.1017  0.1028  354 PHE A CE2 
2368  C CZ  . PHE A 354 ? 0.6053 0.9125 0.4970 0.3379  0.1062  0.1168  354 PHE A CZ  
2369  N N   . GLY A 355 ? 0.8207 0.9802 0.4878 0.4372  0.0951  0.0644  355 GLY A N   
2370  C CA  . GLY A 355 ? 0.8562 0.9648 0.4819 0.4470  0.0844  0.0489  355 GLY A CA  
2371  C C   . GLY A 355 ? 0.8807 0.9489 0.4816 0.4546  0.0723  0.0346  355 GLY A C   
2372  O O   . GLY A 355 ? 0.9003 0.9178 0.4733 0.4532  0.0592  0.0203  355 GLY A O   
2373  N N   . LYS A 356 ? 0.8157 0.9063 0.4277 0.4612  0.0758  0.0392  356 LYS A N   
2374  C CA  . LYS A 356 ? 0.8377 0.8940 0.4288 0.4675  0.0651  0.0269  356 LYS A CA  
2375  C C   . LYS A 356 ? 0.8128 0.8338 0.4121 0.4449  0.0540  0.0157  356 LYS A C   
2376  O O   . LYS A 356 ? 0.8300 0.8168 0.4115 0.4463  0.0429  0.0047  356 LYS A O   
2377  C CB  . LYS A 356 ? 0.8448 0.9381 0.4461 0.4817  0.0733  0.0361  356 LYS A CB  
2378  C CG  . LYS A 356 ? 0.8877 0.9958 0.4648 0.5098  0.0786  0.0414  356 LYS A CG  
2379  C CD  . LYS A 356 ? 0.8898 1.0427 0.4830 0.5218  0.0890  0.0545  356 LYS A CD  
2380  C CE  . LYS A 356 ? 0.8730 1.0858 0.4948 0.5227  0.1040  0.0757  356 LYS A CE  
2381  N NZ  . LYS A 356 ? 0.8620 1.1205 0.5106 0.5252  0.1129  0.0902  356 LYS A NZ  
2382  N N   . LEU A 357 ? 0.8478 0.8815 0.3960 0.4846  -0.0199 -0.0363 357 LEU A N   
2383  C CA  . LEU A 357 ? 0.8317 0.8181 0.3872 0.4607  -0.0235 -0.0409 357 LEU A CA  
2384  C C   . LEU A 357 ? 0.8466 0.7913 0.3863 0.4556  -0.0336 -0.0498 357 LEU A C   
2385  O O   . LEU A 357 ? 0.8265 0.7726 0.3779 0.4439  -0.0282 -0.0451 357 LEU A O   
2386  C CB  . LEU A 357 ? 0.7869 0.7953 0.3765 0.4413  -0.0095 -0.0280 357 LEU A CB  
2387  C CG  . LEU A 357 ? 0.7688 0.8290 0.3803 0.4456  0.0018  -0.0163 357 LEU A CG  
2388  C CD1 . LEU A 357 ? 0.7257 0.8027 0.3728 0.4250  0.0128  -0.0035 357 LEU A CD1 
2389  C CD2 . LEU A 357 ? 0.7846 0.8309 0.3871 0.4514  -0.0045 -0.0233 357 LEU A CD2 
2390  N N   . THR A 358 ? 0.8707 0.7776 0.3838 0.4643  -0.0493 -0.0628 358 THR A N   
2391  C CA  . THR A 358 ? 0.8918 0.7599 0.3882 0.4620  -0.0616 -0.0722 358 THR A CA  
2392  C C   . THR A 358 ? 0.8770 0.6993 0.3837 0.4346  -0.0649 -0.0744 358 THR A C   
2393  O O   . THR A 358 ? 0.8875 0.6809 0.3871 0.4280  -0.0733 -0.0801 358 THR A O   
2394  C CB  . THR A 358 ? 0.9405 0.7867 0.4052 0.4826  -0.0789 -0.0846 358 THR A CB  
2395  O OG1 . THR A 358 ? 0.9517 0.7557 0.4112 0.4718  -0.0885 -0.0914 358 THR A OG1 
2396  C CG2 . THR A 358 ? 0.9556 0.8459 0.4118 0.5093  -0.0755 -0.0816 358 THR A CG2 
2397  N N   . ALA A 359 ? 0.8454 0.6615 0.3697 0.4187  -0.0590 -0.0696 359 ALA A N   
2398  C CA  . ALA A 359 ? 0.8314 0.6075 0.3681 0.3929  -0.0612 -0.0696 359 ALA A CA  
2399  C C   . ALA A 359 ? 0.7871 0.5800 0.3536 0.3746  -0.0469 -0.0576 359 ALA A C   
2400  O O   . ALA A 359 ? 0.7712 0.5385 0.3521 0.3535  -0.0464 -0.0546 359 ALA A O   
2401  C CB  . ALA A 359 ? 0.8465 0.5939 0.3776 0.3886  -0.0687 -0.0741 359 ALA A CB  
2402  N N   . LEU A 360 ? 0.7873 0.6245 0.3645 0.3823  -0.0354 -0.0494 360 LEU A N   
2403  C CA  . LEU A 360 ? 0.7466 0.6022 0.3531 0.3665  -0.0229 -0.0371 360 LEU A CA  
2404  C C   . LEU A 360 ? 0.7334 0.5645 0.3481 0.3487  -0.0237 -0.0355 360 LEU A C   
2405  O O   . LEU A 360 ? 0.7494 0.5718 0.3502 0.3540  -0.0290 -0.0410 360 LEU A O   
2406  C CB  . LEU A 360 ? 0.7308 0.6448 0.3493 0.3795  -0.0108 -0.0271 360 LEU A CB  
2407  C CG  . LEU A 360 ? 0.6893 0.6301 0.3415 0.3654  0.0011  -0.0124 360 LEU A CG  
2408  C CD1 . LEU A 360 ? 0.6769 0.6164 0.3435 0.3581  0.0021  -0.0094 360 LEU A CD1 
2409  C CD2 . LEU A 360 ? 0.6764 0.6769 0.3415 0.3767  0.0123  -0.0008 360 LEU A CD2 
2410  N N   . GLU A 361 ? 0.7482 0.5680 0.3855 0.3277  -0.0194 -0.0276 361 GLU A N   
2411  C CA  . GLU A 361 ? 0.7325 0.5310 0.3816 0.3087  -0.0198 -0.0236 361 GLU A CA  
2412  C C   . GLU A 361 ? 0.6947 0.5195 0.3716 0.2982  -0.0095 -0.0086 361 GLU A C   
2413  O O   . GLU A 361 ? 0.6829 0.5095 0.3670 0.2916  -0.0081 -0.0031 361 GLU A O   
2414  C CB  . GLU A 361 ? 0.7372 0.4919 0.3885 0.2894  -0.0271 -0.0266 361 GLU A CB  
2415  C CG  . GLU A 361 ? 0.7746 0.5011 0.4027 0.2971  -0.0394 -0.0392 361 GLU A CG  
2416  C CD  . GLU A 361 ? 0.7777 0.4656 0.4134 0.2763  -0.0459 -0.0396 361 GLU A CD  
2417  O OE1 . GLU A 361 ? 0.7508 0.4350 0.4087 0.2562  -0.0406 -0.0306 361 GLU A OE1 
2418  O OE2 . GLU A 361 ? 0.8071 0.4712 0.4283 0.2803  -0.0564 -0.0481 361 GLU A OE2 
2419  N N   . TRP A 362 ? 0.7062 0.5510 0.3995 0.2959  -0.0040 -0.0012 362 TRP A N   
2420  C CA  . TRP A 362 ? 0.6719 0.5450 0.3937 0.2859  0.0030  0.0145  362 TRP A CA  
2421  C C   . TRP A 362 ? 0.6652 0.5892 0.3970 0.3016  0.0094  0.0210  362 TRP A C   
2422  O O   . TRP A 362 ? 0.6740 0.6018 0.4020 0.3089  0.0090  0.0162  362 TRP A O   
2423  C CB  . TRP A 362 ? 0.6541 0.5055 0.3920 0.2646  0.0019  0.0188  362 TRP A CB  
2424  C CG  . TRP A 362 ? 0.6547 0.4658 0.3909 0.2455  -0.0025 0.0162  362 TRP A CG  
2425  C CD1 . TRP A 362 ? 0.6349 0.4408 0.3858 0.2278  -0.0017 0.0248  362 TRP A CD1 
2426  C CD2 . TRP A 362 ? 0.6749 0.4501 0.3978 0.2405  -0.0084 0.0062  362 TRP A CD2 
2427  N NE1 . TRP A 362 ? 0.6409 0.4122 0.3894 0.2129  -0.0059 0.0201  362 TRP A NE1 
2428  C CE2 . TRP A 362 ? 0.6648 0.4180 0.3978 0.2200  -0.0100 0.0097  362 TRP A CE2 
2429  C CE3 . TRP A 362 ? 0.7005 0.4627 0.4058 0.2508  -0.0131 -0.0038 362 TRP A CE3 
2430  C CZ2 . TRP A 362 ? 0.6778 0.4007 0.4075 0.2098  -0.0153 0.0045  362 TRP A CZ2 
2431  C CZ3 . TRP A 362 ? 0.7147 0.4435 0.4149 0.2403  -0.0193 -0.0088 362 TRP A CZ3 
2432  C CH2 . TRP A 362 ? 0.7027 0.4138 0.4166 0.2201  -0.0199 -0.0041 362 TRP A CH2 
2433  N N   . LEU A 363 ? 0.6002 0.5662 0.3468 0.3027  0.0150  0.0332  363 LEU A N   
2434  C CA  . LEU A 363 ? 0.5886 0.6113 0.3538 0.3106  0.0220  0.0440  363 LEU A CA  
2435  C C   . LEU A 363 ? 0.5537 0.6001 0.3539 0.2852  0.0240  0.0623  363 LEU A C   
2436  O O   . LEU A 363 ? 0.5417 0.6034 0.3508 0.2716  0.0265  0.0708  363 LEU A O   
2437  C CB  . LEU A 363 ? 0.6044 0.6633 0.3569 0.3289  0.0278  0.0429  363 LEU A CB  
2438  C CG  . LEU A 363 ? 0.5947 0.7166 0.3678 0.3389  0.0362  0.0558  363 LEU A CG  
2439  C CD1 . LEU A 363 ? 0.6090 0.7282 0.3749 0.3531  0.0346  0.0474  363 LEU A CD1 
2440  C CD2 . LEU A 363 ? 0.6080 0.7695 0.3704 0.3546  0.0438  0.0586  363 LEU A CD2 
2441  N N   . PHE A 364 ? 0.5387 0.5863 0.3574 0.2798  0.0214  0.0677  364 PHE A N   
2442  C CA  . PHE A 364 ? 0.5092 0.5732 0.3601 0.2571  0.0198  0.0835  364 PHE A CA  
2443  C C   . PHE A 364 ? 0.4986 0.6195 0.3760 0.2618  0.0233  0.0967  364 PHE A C   
2444  O O   . PHE A 364 ? 0.5013 0.6285 0.3847 0.2723  0.0210  0.0951  364 PHE A O   
2445  C CB  . PHE A 364 ? 0.5039 0.5264 0.3562 0.2483  0.0126  0.0804  364 PHE A CB  
2446  C CG  . PHE A 364 ? 0.5006 0.4814 0.3445 0.2321  0.0097  0.0778  364 PHE A CG  
2447  C CD1 . PHE A 364 ? 0.5211 0.4646 0.3381 0.2372  0.0095  0.0643  364 PHE A CD1 
2448  C CD2 . PHE A 364 ? 0.4783 0.4573 0.3424 0.2105  0.0063  0.0884  364 PHE A CD2 
2449  C CE1 . PHE A 364 ? 0.5174 0.4263 0.3308 0.2204  0.0071  0.0628  364 PHE A CE1 
2450  C CE2 . PHE A 364 ? 0.4750 0.4192 0.3330 0.1950  0.0046  0.0857  364 PHE A CE2 
2451  C CZ  . PHE A 364 ? 0.4935 0.4044 0.3276 0.1996  0.0055  0.0735  364 PHE A CZ  
2452  N N   . LEU A 365 ? 0.5269 0.6900 0.4213 0.2540  0.0287  0.1105  365 LEU A N   
2453  C CA  . LEU A 365 ? 0.5110 0.7328 0.4362 0.2551  0.0324  0.1272  365 LEU A CA  
2454  C C   . LEU A 365 ? 0.4887 0.7305 0.4481 0.2287  0.0292  0.1464  365 LEU A C   
2455  O O   . LEU A 365 ? 0.4748 0.7676 0.4643 0.2257  0.0318  0.1637  365 LEU A O   
2456  C CB  . LEU A 365 ? 0.5259 0.7900 0.4413 0.2746  0.0433  0.1292  365 LEU A CB  
2457  C CG  . LEU A 365 ? 0.5555 0.8074 0.4368 0.3046  0.0459  0.1110  365 LEU A CG  
2458  C CD1 . LEU A 365 ? 0.5714 0.8637 0.4403 0.3233  0.0562  0.1137  365 LEU A CD1 
2459  C CD2 . LEU A 365 ? 0.5584 0.8186 0.4487 0.3154  0.0434  0.1084  365 LEU A CD2 
2460  N N   . ARG A 366 ? 0.5039 0.7075 0.4605 0.2098  0.0231  0.1446  366 ARG A N   
2461  C CA  . ARG A 366 ? 0.4834 0.7013 0.4677 0.1855  0.0191  0.1613  366 ARG A CA  
2462  C C   . ARG A 366 ? 0.4595 0.6942 0.4776 0.1763  0.0100  0.1730  366 ARG A C   
2463  O O   . ARG A 366 ? 0.4575 0.6823 0.4749 0.1870  0.0056  0.1659  366 ARG A O   
2464  C CB  . ARG A 366 ? 0.4788 0.6487 0.4495 0.1701  0.0140  0.1546  366 ARG A CB  
2465  C CG  . ARG A 366 ? 0.4764 0.5951 0.4304 0.1736  0.0075  0.1401  366 ARG A CG  
2466  C CD  . ARG A 366 ? 0.4652 0.5443 0.4123 0.1567  0.0027  0.1378  366 ARG A CD  
2467  N NE  . ARG A 366 ? 0.4419 0.5374 0.4160 0.1363  -0.0032 0.1532  366 ARG A NE  
2468  C CZ  . ARG A 366 ? 0.4244 0.5228 0.4203 0.1288  -0.0130 0.1608  366 ARG A CZ  
2469  N NH1 . ARG A 366 ? 0.4308 0.5168 0.4252 0.1384  -0.0171 0.1528  366 ARG A NH1 
2470  N NH2 . ARG A 366 ? 0.4102 0.5206 0.4292 0.1088  -0.0194 0.1725  366 ARG A NH2 
2471  N N   . ASP A 367 ? 0.5011 0.7602 0.5491 0.1564  0.0059  0.1912  367 ASP A N   
2472  C CA  . ASP A 367 ? 0.4769 0.7494 0.5601 0.1440  -0.0063 0.2039  367 ASP A CA  
2473  C C   . ASP A 367 ? 0.4811 0.7922 0.5824 0.1568  -0.0043 0.2079  367 ASP A C   
2474  O O   . ASP A 367 ? 0.4849 0.7786 0.5882 0.1610  -0.0119 0.1990  367 ASP A O   
2475  C CB  . ASP A 367 ? 0.4722 0.6900 0.5459 0.1365  -0.0186 0.1912  367 ASP A CB  
2476  C CG  . ASP A 367 ? 0.4585 0.6774 0.5633 0.1162  -0.0328 0.1996  367 ASP A CG  
2477  O OD1 . ASP A 367 ? 0.4549 0.7122 0.5895 0.1136  -0.0354 0.2113  367 ASP A OD1 
2478  O OD2 . ASP A 367 ? 0.4675 0.6475 0.5659 0.1032  -0.0417 0.1935  367 ASP A OD2 
2479  N N   . ASN A 368 ? 0.4516 0.8153 0.5648 0.1629  0.0069  0.2208  368 ASN A N   
2480  C CA  . ASN A 368 ? 0.4509 0.8553 0.5806 0.1744  0.0116  0.2252  368 ASN A CA  
2481  C C   . ASN A 368 ? 0.4466 0.9088 0.6071 0.1639  0.0190  0.2493  368 ASN A C   
2482  O O   . ASN A 368 ? 0.4411 0.9078 0.6137 0.1455  0.0175  0.2622  368 ASN A O   
2483  C CB  . ASN A 368 ? 0.4746 0.8749 0.5695 0.2039  0.0221  0.2083  368 ASN A CB  
2484  C CG  . ASN A 368 ? 0.4811 0.8457 0.5633 0.2140  0.0145  0.1904  368 ASN A CG  
2485  O OD1 . ASN A 368 ? 0.4842 0.8678 0.5869 0.2149  0.0106  0.1934  368 ASN A OD1 
2486  N ND2 . ASN A 368 ? 0.4890 0.8001 0.5368 0.2208  0.0120  0.1721  368 ASN A ND2 
2487  N N   . GLN A 369 ? 0.4516 0.9568 0.6239 0.1752  0.0272  0.2559  369 GLN A N   
2488  C CA  . GLN A 369 ? 0.4524 1.0129 0.6515 0.1666  0.0359  0.2801  369 GLN A CA  
2489  C C   . GLN A 369 ? 0.4739 1.0696 0.6502 0.1918  0.0542  0.2798  369 GLN A C   
2490  O O   . GLN A 369 ? 0.4896 1.1313 0.6826 0.1929  0.0620  0.2965  369 GLN A O   
2491  C CB  . GLN A 369 ? 0.4516 1.0323 0.6902 0.1524  0.0268  0.2933  369 GLN A CB  
2492  C CG  . GLN A 369 ? 0.4408 0.9786 0.6937 0.1351  0.0063  0.2861  369 GLN A CG  
2493  C CD  . GLN A 369 ? 0.4501 1.0046 0.7455 0.1091  -0.0046 0.3066  369 GLN A CD  
2494  O OE1 . GLN A 369 ? 0.4381 0.9770 0.7435 0.0880  -0.0125 0.3148  369 GLN A OE1 
2495  N NE2 . GLN A 369 ? 0.4631 1.0470 0.7827 0.1108  -0.0060 0.3147  369 GLN A NE2 
2496  N N   . LEU A 370 ? 0.4501 1.0211 0.5857 0.2126  0.0600  0.2605  370 LEU A N   
2497  C CA  . LEU A 370 ? 0.4726 1.0693 0.5795 0.2382  0.0753  0.2569  370 LEU A CA  
2498  C C   . LEU A 370 ? 0.4740 1.1066 0.5855 0.2320  0.0853  0.2769  370 LEU A C   
2499  O O   . LEU A 370 ? 0.4564 1.0848 0.5856 0.2100  0.0808  0.2886  370 LEU A O   
2500  C CB  . LEU A 370 ? 0.4853 1.0378 0.5459 0.2607  0.0758  0.2297  370 LEU A CB  
2501  C CG  . LEU A 370 ? 0.4832 0.9837 0.5339 0.2623  0.0634  0.2096  370 LEU A CG  
2502  C CD1 . LEU A 370 ? 0.5016 0.9569 0.5045 0.2834  0.0641  0.1848  370 LEU A CD1 
2503  C CD2 . LEU A 370 ? 0.4906 1.0077 0.5550 0.2683  0.0618  0.2090  370 LEU A CD2 
2504  N N   . SER A 371 ? 0.4722 1.1374 0.5643 0.2526  0.0974  0.2804  371 SER A N   
2505  C CA  . SER A 371 ? 0.4804 1.1810 0.5748 0.2494  0.1053  0.3012  371 SER A CA  
2506  C C   . SER A 371 ? 0.5123 1.2221 0.5639 0.2814  0.1142  0.2912  371 SER A C   
2507  O O   . SER A 371 ? 0.5280 1.2161 0.5487 0.3041  0.1143  0.2687  371 SER A O   
2508  C CB  . SER A 371 ? 0.4798 1.2233 0.6154 0.2322  0.1048  0.3297  371 SER A CB  
2509  O OG  . SER A 371 ? 0.4955 1.2601 0.6337 0.2466  0.1076  0.3284  371 SER A OG  
2510  N N   . GLY A 372 ? 0.5496 1.2885 0.5997 0.2836  0.1190  0.3075  372 GLY A N   
2511  C CA  . GLY A 372 ? 0.5819 1.3308 0.5956 0.3139  0.1243  0.2996  372 GLY A CA  
2512  C C   . GLY A 372 ? 0.5862 1.2944 0.5650 0.3250  0.1218  0.2769  372 GLY A C   
2513  O O   . GLY A 372 ? 0.5629 1.2386 0.5464 0.3078  0.1177  0.2699  372 GLY A O   
2514  N N   . PRO A 373 ? 0.6150 1.3231 0.5591 0.3541  0.1235  0.2648  373 PRO A N   
2515  C CA  . PRO A 373 ? 0.6243 1.2905 0.5355 0.3653  0.1199  0.2413  373 PRO A CA  
2516  C C   . PRO A 373 ? 0.6274 1.2412 0.5104 0.3740  0.1136  0.2132  373 PRO A C   
2517  O O   . PRO A 373 ? 0.6285 1.2401 0.5114 0.3781  0.1124  0.2091  373 PRO A O   
2518  C CB  . PRO A 373 ? 0.6615 1.3494 0.5487 0.3944  0.1225  0.2403  373 PRO A CB  
2519  C CG  . PRO A 373 ? 0.6773 1.4015 0.5685 0.4073  0.1258  0.2511  373 PRO A CG  
2520  C CD  . PRO A 373 ? 0.6468 1.3916 0.5800 0.3785  0.1280  0.2714  373 PRO A CD  
2521  N N   . ILE A 374 ? 0.6592 1.2276 0.5179 0.3756  0.1092  0.1932  374 ILE A N   
2522  C CA  . ILE A 374 ? 0.6686 1.1802 0.4961 0.3847  0.1015  0.1656  374 ILE A CA  
2523  C C   . ILE A 374 ? 0.7110 1.2116 0.5007 0.4173  0.0964  0.1485  374 ILE A C   
2524  O O   . ILE A 374 ? 0.7311 1.2333 0.5053 0.4293  0.0959  0.1451  374 ILE A O   
2525  C CB  . ILE A 374 ? 0.6573 1.1208 0.4739 0.3684  0.0978  0.1530  374 ILE A CB  
2526  C CG1 . ILE A 374 ? 0.6304 1.0891 0.4749 0.3383  0.0990  0.1647  374 ILE A CG1 
2527  C CG2 . ILE A 374 ? 0.6814 1.0846 0.4575 0.3836  0.0878  0.1236  374 ILE A CG2 
2528  C CD1 . ILE A 374 ? 0.6340 1.0848 0.4866 0.3401  0.0970  0.1604  374 ILE A CD1 
2529  N N   . PRO A 375 ? 0.6917 1.1809 0.4657 0.4321  0.0917  0.1379  375 PRO A N   
2530  C CA  . PRO A 375 ? 0.7344 1.2076 0.4706 0.4625  0.0841  0.1208  375 PRO A CA  
2531  C C   . PRO A 375 ? 0.7503 1.1619 0.4554 0.4670  0.0733  0.0961  375 PRO A C   
2532  O O   . PRO A 375 ? 0.7324 1.1022 0.4380 0.4496  0.0696  0.0865  375 PRO A O   
2533  C CB  . PRO A 375 ? 0.7423 1.2110 0.4724 0.4698  0.0809  0.1150  375 PRO A CB  
2534  C CG  . PRO A 375 ? 0.7052 1.2036 0.4752 0.4456  0.0897  0.1339  375 PRO A CG  
2535  C CD  . PRO A 375 ? 0.6733 1.1627 0.4639 0.4212  0.0925  0.1406  375 PRO A CD  
2536  N N   . PRO A 376 ? 0.7957 1.1992 0.4730 0.4901  0.0673  0.0857  376 PRO A N   
2537  C CA  . PRO A 376 ? 0.8146 1.1574 0.4622 0.4935  0.0551  0.0625  376 PRO A CA  
2538  C C   . PRO A 376 ? 0.8249 1.1124 0.4523 0.4938  0.0425  0.0429  376 PRO A C   
2539  O O   . PRO A 376 ? 0.8317 1.0651 0.4420 0.4872  0.0325  0.0266  376 PRO A O   
2540  C CB  . PRO A 376 ? 0.8560 1.2087 0.4785 0.5228  0.0503  0.0573  376 PRO A CB  
2541  C CG  . PRO A 376 ? 0.8492 1.2721 0.4950 0.5278  0.0641  0.0821  376 PRO A CG  
2542  C CD  . PRO A 376 ? 0.8217 1.2718 0.4942 0.5137  0.0712  0.0963  376 PRO A CD  
2543  N N   . GLY A 377 ? 0.8355 1.1339 0.4643 0.4998  0.0422  0.0446  377 GLY A N   
2544  C CA  . GLY A 377 ? 0.8479 1.0948 0.4575 0.4998  0.0301  0.0270  377 GLY A CA  
2545  C C   . GLY A 377 ? 0.8157 1.0313 0.4405 0.4732  0.0314  0.0253  377 GLY A C   
2546  O O   . GLY A 377 ? 0.8269 0.9928 0.4354 0.4705  0.0206  0.0102  377 GLY A O   
2547  N N   . ILE A 378 ? 0.8229 1.0664 0.4789 0.4534  0.0437  0.0412  378 ILE A N   
2548  C CA  . ILE A 378 ? 0.7929 1.0086 0.4640 0.4299  0.0451  0.0407  378 ILE A CA  
2549  C C   . ILE A 378 ? 0.8049 0.9557 0.4531 0.4237  0.0337  0.0226  378 ILE A C   
2550  O O   . ILE A 378 ? 0.8044 0.9101 0.4473 0.4150  0.0266  0.0124  378 ILE A O   
2551  C CB  . ILE A 378 ? 0.7527 1.0121 0.4609 0.4104  0.0591  0.0625  378 ILE A CB  
2552  C CG1 . ILE A 378 ? 0.7389 1.0570 0.4754 0.4115  0.0682  0.0814  378 ILE A CG1 
2553  C CG2 . ILE A 378 ? 0.7424 0.9658 0.4639 0.3863  0.0578  0.0609  378 ILE A CG2 
2554  C CD1 . ILE A 378 ? 0.7052 1.0559 0.4855 0.3875  0.0778  0.1023  378 ILE A CD1 
2555  N N   . ALA A 379 ? 0.8367 0.9813 0.4724 0.4268  0.0313  0.0190  379 ALA A N   
2556  C CA  . ALA A 379 ? 0.8504 0.9358 0.4648 0.4200  0.0195  0.0028  379 ALA A CA  
2557  C C   . ALA A 379 ? 0.8960 0.9471 0.4772 0.4401  0.0029  -0.0147 379 ALA A C   
2558  O O   . ALA A 379 ? 0.9235 0.9358 0.4867 0.4387  -0.0079 -0.0264 379 ALA A O   
2559  C CB  . ALA A 379 ? 0.8366 0.9312 0.4565 0.4072  0.0250  0.0092  379 ALA A CB  
2560  N N   . ASN A 380 ? 0.9075 0.9724 0.4797 0.4583  -0.0003 -0.0164 380 ASN A N   
2561  C CA  . ASN A 380 ? 0.9528 0.9847 0.4925 0.4773  -0.0174 -0.0324 380 ASN A CA  
2562  C C   . ASN A 380 ? 0.9643 0.9299 0.4898 0.4639  -0.0322 -0.0471 380 ASN A C   
2563  O O   . ASN A 380 ? 0.9999 0.9288 0.5001 0.4729  -0.0486 -0.0607 380 ASN A O   
2564  C CB  . ASN A 380 ? 0.9710 1.0308 0.5042 0.4978  -0.0174 -0.0305 380 ASN A CB  
2565  C CG  . ASN A 380 ? 1.0079 1.0878 0.5207 0.5266  -0.0227 -0.0331 380 ASN A CG  
2566  O OD1 . ASN A 380 ? 1.0148 1.0985 0.5235 0.5313  -0.0230 -0.0334 380 ASN A OD1 
2567  N ND2 . ASN A 380 ? 1.0336 1.1257 0.5326 0.5470  -0.0272 -0.0353 380 ASN A ND2 
2568  N N   . SER A 381 ? 0.9054 0.8559 0.4486 0.4423  -0.0272 -0.0438 381 SER A N   
2569  C CA  . SER A 381 ? 0.9153 0.8074 0.4502 0.4280  -0.0398 -0.0549 381 SER A CA  
2570  C C   . SER A 381 ? 0.9209 0.7741 0.4497 0.4157  -0.0485 -0.0620 381 SER A C   
2571  O O   . SER A 381 ? 0.8953 0.7589 0.4388 0.4042  -0.0398 -0.0551 381 SER A O   
2572  C CB  . SER A 381 ? 0.8823 0.7718 0.4414 0.4085  -0.0311 -0.0476 381 SER A CB  
2573  O OG  . SER A 381 ? 0.8758 0.8032 0.4427 0.4187  -0.0232 -0.0407 381 SER A OG  
2574  N N   . THR A 382 ? 0.9363 0.7450 0.4440 0.4178  -0.0667 -0.0753 382 THR A N   
2575  C CA  . THR A 382 ? 0.9434 0.7111 0.4480 0.4032  -0.0775 -0.0822 382 THR A CA  
2576  C C   . THR A 382 ? 0.9165 0.6550 0.4439 0.3739  -0.0750 -0.0780 382 THR A C   
2577  O O   . THR A 382 ? 0.9114 0.6243 0.4455 0.3577  -0.0798 -0.0792 382 THR A O   
2578  C CB  . THR A 382 ? 0.9907 0.7225 0.4686 0.4143  -0.0991 -0.0965 382 THR A CB  
2579  O OG1 . THR A 382 ? 1.0020 0.7085 0.4783 0.4091  -0.1061 -0.1002 382 THR A OG1 
2580  C CG2 . THR A 382 ? 1.0197 0.7807 0.4755 0.4458  -0.1023 -0.0996 382 THR A CG2 
2581  N N   . GLU A 383 ? 0.9179 0.6609 0.4585 0.3669  -0.0680 -0.0724 383 GLU A N   
2582  C CA  . GLU A 383 ? 0.8920 0.6120 0.4561 0.3404  -0.0646 -0.0661 383 GLU A CA  
2583  C C   . GLU A 383 ? 0.8496 0.6005 0.4391 0.3315  -0.0476 -0.0522 383 GLU A C   
2584  O O   . GLU A 383 ? 0.8264 0.5641 0.4365 0.3112  -0.0438 -0.0449 383 GLU A O   
2585  C CB  . GLU A 383 ? 0.9034 0.6045 0.4658 0.3374  -0.0696 -0.0688 383 GLU A CB  
2586  C CG  . GLU A 383 ? 0.9249 0.5799 0.4844 0.3240  -0.0842 -0.0754 383 GLU A CG  
2587  C CD  . GLU A 383 ? 0.9703 0.6095 0.5010 0.3425  -0.1010 -0.0886 383 GLU A CD  
2588  O OE1 . GLU A 383 ? 0.9884 0.6486 0.5001 0.3660  -0.1017 -0.0926 383 GLU A OE1 
2589  O OE2 . GLU A 383 ? 0.9885 0.5957 0.5169 0.3337  -0.1143 -0.0943 383 GLU A OE2 
2590  N N   . LEU A 384 ? 0.7813 0.5753 0.3710 0.3462  -0.0375 -0.0470 384 LEU A N   
2591  C CA  . LEU A 384 ? 0.7417 0.5673 0.3583 0.3379  -0.0227 -0.0321 384 LEU A CA  
2592  C C   . LEU A 384 ? 0.7230 0.5244 0.3547 0.3166  -0.0241 -0.0267 384 LEU A C   
2593  O O   . LEU A 384 ? 0.7373 0.5218 0.3576 0.3164  -0.0311 -0.0330 384 LEU A O   
2594  C CB  . LEU A 384 ? 0.7368 0.6177 0.3528 0.3569  -0.0117 -0.0260 384 LEU A CB  
2595  C CG  . LEU A 384 ? 0.6946 0.6213 0.3449 0.3411  0.0018  -0.0058 384 LEU A CG  
2596  C CD1 . LEU A 384 ? 0.6760 0.6010 0.3453 0.3337  0.0044  0.0003  384 LEU A CD1 
2597  C CD2 . LEU A 384 ? 0.6940 0.6807 0.3448 0.3571  0.0123  0.0022  384 LEU A CD2 
2598  N N   . THR A 385 ? 0.7131 0.5141 0.3708 0.2968  -0.0187 -0.0144 385 THR A N   
2599  C CA  . THR A 385 ? 0.6927 0.4759 0.3679 0.2695  -0.0202 -0.0067 385 THR A CA  
2600  C C   . THR A 385 ? 0.6526 0.4739 0.3571 0.2510  -0.0100 0.0110  385 THR A C   
2601  O O   . THR A 385 ? 0.6355 0.4577 0.3527 0.2319  -0.0098 0.0180  385 THR A O   
2602  C CB  . THR A 385 ? 0.6958 0.4356 0.3755 0.2533  -0.0263 -0.0097 385 THR A CB  
2603  O OG1 . THR A 385 ? 0.6932 0.4398 0.3761 0.2557  -0.0228 -0.0095 385 THR A OG1 
2604  C CG2 . THR A 385 ? 0.7287 0.4336 0.3902 0.2540  -0.0393 -0.0237 385 THR A CG2 
2605  N N   . VAL A 386 ? 0.6324 0.4846 0.3482 0.2565  -0.0028 0.0183  386 VAL A N   
2606  C CA  . VAL A 386 ? 0.5972 0.4828 0.3420 0.2394  0.0042  0.0351  386 VAL A CA  
2607  C C   . VAL A 386 ? 0.5927 0.5310 0.3441 0.2530  0.0117  0.0416  386 VAL A C   
2608  O O   . VAL A 386 ? 0.6055 0.5500 0.3491 0.2714  0.0125  0.0364  386 VAL A O   
2609  C CB  . VAL A 386 ? 0.5819 0.4464 0.3410 0.2275  0.0032  0.0401  386 VAL A CB  
2610  C CG1 . VAL A 386 ? 0.5501 0.4498 0.3376 0.2135  0.0079  0.0561  386 VAL A CG1 
2611  C CG2 . VAL A 386 ? 0.5837 0.4026 0.3406 0.2124  -0.0023 0.0376  386 VAL A CG2 
2612  N N   . LEU A 387 ? 0.5724 0.5497 0.3394 0.2439  0.0171  0.0541  387 LEU A N   
2613  C CA  . LEU A 387 ? 0.5732 0.6060 0.3498 0.2551  0.0253  0.0638  387 LEU A CA  
2614  C C   . LEU A 387 ? 0.5411 0.6045 0.3519 0.2324  0.0286  0.0835  387 LEU A C   
2615  O O   . LEU A 387 ? 0.5375 0.6163 0.3553 0.2207  0.0306  0.0919  387 LEU A O   
2616  C CB  . LEU A 387 ? 0.6027 0.6535 0.3580 0.2717  0.0282  0.0589  387 LEU A CB  
2617  C CG  . LEU A 387 ? 0.6153 0.7135 0.3643 0.2971  0.0361  0.0613  387 LEU A CG  
2618  C CD1 . LEU A 387 ? 0.6444 0.7471 0.3646 0.3153  0.0366  0.0528  387 LEU A CD1 
2619  C CD2 . LEU A 387 ? 0.5887 0.7432 0.3715 0.2874  0.0450  0.0834  387 LEU A CD2 
2620  N N   . GLN A 388 ? 0.5372 0.6069 0.3684 0.2268  0.0276  0.0903  388 GLN A N   
2621  C CA  . GLN A 388 ? 0.5084 0.5998 0.3722 0.2054  0.0271  0.1077  388 GLN A CA  
2622  C C   . GLN A 388 ? 0.5011 0.6501 0.3868 0.2114  0.0329  0.1221  388 GLN A C   
2623  O O   . GLN A 388 ? 0.5068 0.6678 0.3951 0.2255  0.0335  0.1200  388 GLN A O   
2624  C CB  . GLN A 388 ? 0.4981 0.5565 0.3703 0.1952  0.0200  0.1061  388 GLN A CB  
2625  C CG  . GLN A 388 ? 0.5050 0.5093 0.3591 0.1889  0.0153  0.0948  388 GLN A CG  
2626  C CD  . GLN A 388 ? 0.4848 0.4780 0.3537 0.1651  0.0118  0.1035  388 GLN A CD  
2627  O OE1 . GLN A 388 ? 0.4657 0.4865 0.3586 0.1529  0.0109  0.1173  388 GLN A OE1 
2628  N NE2 . GLN A 388 ? 0.4902 0.4430 0.3457 0.1586  0.0090  0.0959  388 GLN A NE2 
2629  N N   . LEU A 389 ? 0.4982 0.6837 0.4013 0.2005  0.0369  0.1377  389 LEU A N   
2630  C CA  . LEU A 389 ? 0.4861 0.7308 0.4134 0.2047  0.0433  0.1549  389 LEU A CA  
2631  C C   . LEU A 389 ? 0.4568 0.7268 0.4205 0.1801  0.0405  0.1762  389 LEU A C   
2632  O O   . LEU A 389 ? 0.4533 0.7754 0.4405 0.1806  0.0459  0.1939  389 LEU A O   
2633  C CB  . LEU A 389 ? 0.5082 0.7855 0.4184 0.2233  0.0537  0.1555  389 LEU A CB  
2634  C CG  . LEU A 389 ? 0.5401 0.8025 0.4138 0.2522  0.0562  0.1360  389 LEU A CG  
2635  C CD1 . LEU A 389 ? 0.5576 0.8640 0.4198 0.2715  0.0667  0.1412  389 LEU A CD1 
2636  C CD2 . LEU A 389 ? 0.5388 0.7995 0.4146 0.2658  0.0542  0.1296  389 LEU A CD2 
2637  N N   . ASP A 390 ? 0.5123 0.7481 0.4818 0.1591  0.0318  0.1761  390 ASP A N   
2638  C CA  . ASP A 390 ? 0.4848 0.7415 0.4856 0.1363  0.0275  0.1956  390 ASP A CA  
2639  C C   . ASP A 390 ? 0.4679 0.7545 0.5030 0.1323  0.0226  0.2093  390 ASP A C   
2640  O O   . ASP A 390 ? 0.4760 0.7599 0.5097 0.1455  0.0213  0.2020  390 ASP A O   
2641  C CB  . ASP A 390 ? 0.4757 0.6873 0.4734 0.1173  0.0181  0.1911  390 ASP A CB  
2642  C CG  . ASP A 390 ? 0.4749 0.6481 0.4706 0.1170  0.0092  0.1809  390 ASP A CG  
2643  O OD1 . ASP A 390 ? 0.4905 0.6353 0.4616 0.1317  0.0112  0.1644  390 ASP A OD1 
2644  O OD2 . ASP A 390 ? 0.4538 0.6241 0.4718 0.1026  -0.0007 0.1897  390 ASP A OD2 
2645  N N   . THR A 391 ? 0.4478 0.7620 0.5144 0.1134  0.0186  0.2298  391 THR A N   
2646  C CA  . THR A 391 ? 0.4372 0.7802 0.5422 0.1053  0.0108  0.2456  391 THR A CA  
2647  C C   . THR A 391 ? 0.4452 0.8347 0.5597 0.1242  0.0198  0.2509  391 THR A C   
2648  O O   . THR A 391 ? 0.4474 0.8346 0.5677 0.1335  0.0152  0.2453  391 THR A O   
2649  C CB  . THR A 391 ? 0.4322 0.7325 0.5395 0.0990  -0.0041 0.2360  391 THR A CB  
2650  O OG1 . THR A 391 ? 0.4298 0.6826 0.5171 0.0888  -0.0089 0.2259  391 THR A OG1 
2651  C CG2 . THR A 391 ? 0.4225 0.7402 0.5697 0.0809  -0.0157 0.2498  391 THR A CG2 
2652  N N   . ASN A 392 ? 0.4531 0.8860 0.5681 0.1314  0.0329  0.2621  392 ASN A N   
2653  C CA  . ASN A 392 ? 0.4567 0.9396 0.5792 0.1516  0.0437  0.2688  392 ASN A CA  
2654  C C   . ASN A 392 ? 0.4574 0.9980 0.6006 0.1474  0.0542  0.2937  392 ASN A C   
2655  O O   . ASN A 392 ? 0.4590 0.9973 0.6098 0.1285  0.0520  0.3047  392 ASN A O   
2656  C CB  . ASN A 392 ? 0.4864 0.9500 0.5657 0.1795  0.0524  0.2457  392 ASN A CB  
2657  C CG  . ASN A 392 ? 0.4881 0.9268 0.5609 0.1914  0.0459  0.2299  392 ASN A CG  
2658  O OD1 . ASN A 392 ? 0.4782 0.9520 0.5724 0.2001  0.0466  0.2376  392 ASN A OD1 
2659  N ND2 . ASN A 392 ? 0.4952 0.8738 0.5392 0.1917  0.0394  0.2088  392 ASN A ND2 
2660  N N   . ASN A 393 ? 0.4733 1.0623 0.6221 0.1646  0.0663  0.3019  393 ASN A N   
2661  C CA  . ASN A 393 ? 0.4732 1.1104 0.6349 0.1599  0.0767  0.3257  393 ASN A CA  
2662  C C   . ASN A 393 ? 0.5006 1.1580 0.6265 0.1891  0.0914  0.3197  393 ASN A C   
2663  O O   . ASN A 393 ? 0.5139 1.2084 0.6423 0.1985  0.0976  0.3325  393 ASN A O   
2664  C CB  . ASN A 393 ? 0.4727 1.1379 0.6680 0.1487  0.0730  0.3435  393 ASN A CB  
2665  C CG  . ASN A 393 ? 0.4608 1.1037 0.6903 0.1190  0.0560  0.3503  393 ASN A CG  
2666  O OD1 . ASN A 393 ? 0.4492 1.0494 0.6744 0.1144  0.0447  0.3333  393 ASN A OD1 
2667  N ND2 . ASN A 393 ? 0.4615 1.1283 0.7219 0.1000  0.0518  0.3747  393 ASN A ND2 
2668  N N   . PHE A 394 ? 0.5038 1.1339 0.5951 0.2045  0.0953  0.2995  394 PHE A N   
2669  C CA  . PHE A 394 ? 0.5267 1.1636 0.5788 0.2332  0.1046  0.2886  394 PHE A CA  
2670  C C   . PHE A 394 ? 0.5235 1.1813 0.5776 0.2296  0.1067  0.3016  394 PHE A C   
2671  O O   . PHE A 394 ? 0.5071 1.1646 0.5851 0.2048  0.1018  0.3149  394 PHE A O   
2672  C CB  . PHE A 394 ? 0.5604 1.1478 0.5689 0.2493  0.1051  0.2588  394 PHE A CB  
2673  C CG  . PHE A 394 ? 0.5705 1.1292 0.5691 0.2615  0.0985  0.2394  394 PHE A CG  
2674  C CD1 . PHE A 394 ? 0.5510 1.0743 0.5674 0.2416  0.0852  0.2352  394 PHE A CD1 
2675  C CD2 . PHE A 394 ? 0.5864 1.1529 0.5563 0.2940  0.1049  0.2256  394 PHE A CD2 
2676  C CE1 . PHE A 394 ? 0.5456 1.0421 0.5516 0.2537  0.0794  0.2180  394 PHE A CE1 
2677  C CE2 . PHE A 394 ? 0.5865 1.1262 0.5469 0.3055  0.0986  0.2083  394 PHE A CE2 
2678  C CZ  . PHE A 394 ? 0.5611 1.0659 0.5397 0.2851  0.0862  0.2048  394 PHE A CZ  
2679  N N   . THR A 395 ? 0.5121 1.1859 0.5409 0.2562  0.1129  0.2958  395 THR A N   
2680  C CA  . THR A 395 ? 0.5256 1.2225 0.5550 0.2591  0.1162  0.3062  395 THR A CA  
2681  C C   . THR A 395 ? 0.5539 1.2331 0.5393 0.2885  0.1200  0.2832  395 THR A C   
2682  O O   . THR A 395 ? 0.5681 1.2259 0.5247 0.3092  0.1195  0.2630  395 THR A O   
2683  C CB  . THR A 395 ? 0.5377 1.2889 0.5915 0.2607  0.1195  0.3337  395 THR A CB  
2684  O OG1 . THR A 395 ? 0.5597 1.3260 0.5959 0.2860  0.1240  0.3282  395 THR A OG1 
2685  C CG2 . THR A 395 ? 0.5147 1.2786 0.6125 0.2292  0.1133  0.3572  395 THR A CG2 
2686  N N   . GLY A 396 ? 0.5626 1.2478 0.5423 0.2899  0.1223  0.2858  396 GLY A N   
2687  C CA  . GLY A 396 ? 0.5945 1.2690 0.5351 0.3189  0.1249  0.2678  396 GLY A CA  
2688  C C   . GLY A 396 ? 0.5960 1.2131 0.5051 0.3171  0.1204  0.2414  396 GLY A C   
2689  O O   . GLY A 396 ? 0.5721 1.1596 0.4898 0.2911  0.1163  0.2393  396 GLY A O   
2690  N N   . PHE A 397 ? 0.6511 1.2503 0.5215 0.3456  0.1196  0.2214  397 PHE A N   
2691  C CA  . PHE A 397 ? 0.6619 1.2068 0.4980 0.3476  0.1135  0.1965  397 PHE A CA  
2692  C C   . PHE A 397 ? 0.6627 1.1596 0.4766 0.3513  0.1062  0.1740  397 PHE A C   
2693  O O   . PHE A 397 ? 0.6622 1.1689 0.4805 0.3604  0.1065  0.1741  397 PHE A O   
2694  C CB  . PHE A 397 ? 0.7005 1.2471 0.5055 0.3770  0.1136  0.1862  397 PHE A CB  
2695  C CG  . PHE A 397 ? 0.7041 1.2870 0.5232 0.3740  0.1199  0.2047  397 PHE A CG  
2696  C CD1 . PHE A 397 ? 0.6779 1.2994 0.5384 0.3502  0.1253  0.2321  397 PHE A CD1 
2697  C CD2 . PHE A 397 ? 0.7365 1.3128 0.5266 0.3958  0.1192  0.1945  397 PHE A CD2 
2698  C CE1 . PHE A 397 ? 0.6840 1.3366 0.5565 0.3480  0.1303  0.2491  397 PHE A CE1 
2699  C CE2 . PHE A 397 ? 0.7421 1.3509 0.5431 0.3947  0.1253  0.2113  397 PHE A CE2 
2700  C CZ  . PHE A 397 ? 0.7157 1.3627 0.5580 0.3705  0.1312  0.2388  397 PHE A CZ  
2701  N N   . LEU A 398 ? 0.6993 1.1426 0.4887 0.3438  0.0986  0.1552  398 LEU A N   
2702  C CA  . LEU A 398 ? 0.7081 1.0998 0.4708 0.3500  0.0897  0.1322  398 LEU A CA  
2703  C C   . LEU A 398 ? 0.7499 1.1253 0.4765 0.3841  0.0839  0.1119  398 LEU A C   
2704  O O   . LEU A 398 ? 0.7723 1.1543 0.4848 0.3976  0.0837  0.1094  398 LEU A O   
2705  C CB  . LEU A 398 ? 0.6994 1.0393 0.4512 0.3273  0.0814  0.1226  398 LEU A CB  
2706  C CG  . LEU A 398 ? 0.6622 1.0009 0.4439 0.2934  0.0817  0.1383  398 LEU A CG  
2707  C CD1 . LEU A 398 ? 0.6691 0.9465 0.4322 0.2806  0.0700  0.1234  398 LEU A CD1 
2708  C CD2 . LEU A 398 ? 0.6474 1.0219 0.4586 0.2903  0.0876  0.1540  398 LEU A CD2 
2709  N N   . PRO A 399 ? 0.7592 1.1117 0.4700 0.3989  0.0779  0.0975  399 PRO A N   
2710  C CA  . PRO A 399 ? 0.8017 1.1359 0.4787 0.4310  0.0693  0.0789  399 PRO A CA  
2711  C C   . PRO A 399 ? 0.8224 1.0979 0.4678 0.4320  0.0566  0.0568  399 PRO A C   
2712  O O   . PRO A 399 ? 0.8056 1.0431 0.4502 0.4098  0.0520  0.0512  399 PRO A O   
2713  C CB  . PRO A 399 ? 0.8061 1.1302 0.4791 0.4410  0.0652  0.0720  399 PRO A CB  
2714  C CG  . PRO A 399 ? 0.7680 1.0873 0.4650 0.4137  0.0694  0.0802  399 PRO A CG  
2715  C CD  . PRO A 399 ? 0.7378 1.0785 0.4604 0.3870  0.0774  0.0981  399 PRO A CD  
2716  N N   . ASP A 400 ? 0.8734 1.1416 0.4923 0.4587  0.0494  0.0450  400 ASP A N   
2717  C CA  . ASP A 400 ? 0.8986 1.1121 0.4872 0.4625  0.0348  0.0241  400 ASP A CA  
2718  C C   . ASP A 400 ? 0.9118 1.0667 0.4807 0.4634  0.0195  0.0041  400 ASP A C   
2719  O O   . ASP A 400 ? 0.9299 1.0346 0.4772 0.4616  0.0055  -0.0124 400 ASP A O   
2720  C CB  . ASP A 400 ? 0.9454 1.1683 0.5112 0.4929  0.0300  0.0179  400 ASP A CB  
2721  C CG  . ASP A 400 ? 0.9339 1.2066 0.5157 0.4911  0.0434  0.0364  400 ASP A CG  
2722  O OD1 . ASP A 400 ? 0.9356 1.1925 0.5126 0.4795  0.0416  0.0340  400 ASP A OD1 
2723  O OD2 . ASP A 400 ? 0.9308 1.2582 0.5300 0.5010  0.0550  0.0541  400 ASP A OD2 
2724  N N   . THR A 401 ? 0.8704 1.0302 0.4466 0.4659  0.0209  0.0058  401 THR A N   
2725  C CA  . THR A 401 ? 0.8813 0.9872 0.4417 0.4646  0.0071  -0.0105 401 THR A CA  
2726  C C   . THR A 401 ? 0.8480 0.9270 0.4219 0.4344  0.0090  -0.0089 401 THR A C   
2727  O O   . THR A 401 ? 0.8512 0.8921 0.4183 0.4307  0.0008  -0.0183 401 THR A O   
2728  C CB  . THR A 401 ? 0.8910 1.0130 0.4511 0.4808  0.0069  -0.0091 401 THR A CB  
2729  O OG1 . THR A 401 ? 0.8546 1.0258 0.4469 0.4692  0.0236  0.0107  401 THR A OG1 
2730  C CG2 . THR A 401 ? 0.9301 1.0729 0.4712 0.5128  0.0022  -0.0119 401 THR A CG2 
2731  N N   . ILE A 402 ? 0.8591 0.9554 0.4501 0.4126  0.0184  0.0035  402 ILE A N   
2732  C CA  . ILE A 402 ? 0.8312 0.9190 0.4404 0.3840  0.0231  0.0128  402 ILE A CA  
2733  C C   . ILE A 402 ? 0.8606 0.8818 0.4506 0.3754  0.0087  -0.0039 402 ILE A C   
2734  O O   . ILE A 402 ? 0.8626 0.8669 0.4710 0.3606  0.0080  -0.0016 402 ILE A O   
2735  C CB  . ILE A 402 ? 0.8171 0.9332 0.4466 0.3616  0.0316  0.0308  402 ILE A CB  
2736  C CG1 . ILE A 402 ? 0.7907 0.8977 0.4472 0.3297  0.0329  0.0433  402 ILE A CG1 
2737  C CG2 . ILE A 402 ? 0.8343 0.9251 0.4444 0.3619  0.0227  0.0208  402 ILE A CG2 
2738  C CD1 . ILE A 402 ? 0.7730 0.9146 0.4570 0.3263  0.0422  0.0573  402 ILE A CD1 
2739  N N   . CYS A 403 ? 0.8389 0.8208 0.4060 0.3799  -0.0048 -0.0193 403 CYS A N   
2740  C CA  . CYS A 403 ? 0.8537 0.7718 0.4131 0.3686  -0.0207 -0.0338 403 CYS A CA  
2741  C C   . CYS A 403 ? 0.8937 0.7764 0.4216 0.3933  -0.0376 -0.0543 403 CYS A C   
2742  O O   . CYS A 403 ? 0.9145 0.7533 0.4284 0.3896  -0.0533 -0.0668 403 CYS A O   
2743  C CB  . CYS A 403 ? 0.8616 0.7611 0.4370 0.3397  -0.0251 -0.0287 403 CYS A CB  
2744  S SG  . CYS A 403 ? 0.8700 0.7011 0.4546 0.3169  -0.0406 -0.0380 403 CYS A SG  
2745  N N   . ARG A 404 ? 0.8313 0.7358 0.3548 0.4148  -0.0372 -0.0544 404 ARG A N   
2746  C CA  . ARG A 404 ? 0.8771 0.7568 0.3747 0.4364  -0.0552 -0.0685 404 ARG A CA  
2747  C C   . ARG A 404 ? 0.8965 0.7118 0.3824 0.4248  -0.0750 -0.0823 404 ARG A C   
2748  O O   . ARG A 404 ? 0.9293 0.7115 0.3963 0.4302  -0.0931 -0.0943 404 ARG A O   
2749  C CB  . ARG A 404 ? 0.8888 0.8008 0.3840 0.4580  -0.0513 -0.0648 404 ARG A CB  
2750  C CG  . ARG A 404 ? 0.9387 0.8327 0.4046 0.4836  -0.0691 -0.0775 404 ARG A CG  
2751  C CD  . ARG A 404 ? 0.9495 0.8847 0.4133 0.5070  -0.0629 -0.0717 404 ARG A CD  
2752  N NE  . ARG A 404 ? 0.9547 0.8698 0.4146 0.5046  -0.0688 -0.0756 404 ARG A NE  
2753  C CZ  . ARG A 404 ? 0.9722 0.9091 0.4241 0.5246  -0.0690 -0.0745 404 ARG A CZ  
2754  N NH1 . ARG A 404 ? 0.9870 0.9676 0.4344 0.5495  -0.0637 -0.0689 404 ARG A NH1 
2755  N NH2 . ARG A 404 ? 0.9760 0.8910 0.4245 0.5196  -0.0745 -0.0788 404 ARG A NH2 
2756  N N   . GLY A 405 ? 0.8569 0.6552 0.3568 0.4077  -0.0720 -0.0797 405 GLY A N   
2757  C CA  . GLY A 405 ? 0.8722 0.6149 0.3690 0.3927  -0.0886 -0.0894 405 GLY A CA  
2758  C C   . GLY A 405 ? 0.8603 0.5698 0.3689 0.3688  -0.0939 -0.0906 405 GLY A C   
2759  O O   . GLY A 405 ? 0.8744 0.5408 0.3847 0.3544  -0.1087 -0.0968 405 GLY A O   
2760  N N   . GLY A 406 ? 0.8877 0.6185 0.4066 0.3632  -0.0821 -0.0834 406 GLY A N   
2761  C CA  . GLY A 406 ? 0.8760 0.5765 0.4077 0.3411  -0.0874 -0.0833 406 GLY A CA  
2762  C C   . GLY A 406 ? 0.8470 0.5261 0.4080 0.3141  -0.0841 -0.0739 406 GLY A C   
2763  O O   . GLY A 406 ? 0.8427 0.4907 0.4172 0.2925  -0.0928 -0.0731 406 GLY A O   
2764  N N   . LYS A 407 ? 0.8466 0.5450 0.4199 0.3138  -0.0718 -0.0652 407 LYS A N   
2765  C CA  . LYS A 407 ? 0.8210 0.5027 0.4208 0.2891  -0.0685 -0.0553 407 LYS A CA  
2766  C C   . LYS A 407 ? 0.7768 0.4971 0.4033 0.2761  -0.0512 -0.0371 407 LYS A C   
2767  O O   . LYS A 407 ? 0.7557 0.4635 0.4024 0.2585  -0.0478 -0.0284 407 LYS A O   
2768  C CB  . LYS A 407 ? 0.8363 0.5054 0.4313 0.2907  -0.0731 -0.0601 407 LYS A CB  
2769  C CG  . LYS A 407 ? 0.8797 0.5240 0.4508 0.3016  -0.0910 -0.0750 407 LYS A CG  
2770  C CD  . LYS A 407 ? 0.8920 0.5164 0.4643 0.2967  -0.0966 -0.0771 407 LYS A CD  
2771  C CE  . LYS A 407 ? 0.9381 0.5450 0.4831 0.3141  -0.1141 -0.0910 407 LYS A CE  
2772  N NZ  . LYS A 407 ? 0.9518 0.5449 0.4947 0.3142  -0.1181 -0.0928 407 LYS A NZ  
2773  N N   . LEU A 408 ? 0.7291 0.4985 0.3575 0.2820  -0.0407 -0.0299 408 LEU A N   
2774  C CA  . LEU A 408 ? 0.6880 0.4975 0.3448 0.2663  -0.0264 -0.0115 408 LEU A CA  
2775  C C   . LEU A 408 ? 0.6603 0.4569 0.3412 0.2362  -0.0266 -0.0014 408 LEU A C   
2776  O O   . LEU A 408 ? 0.6636 0.4509 0.3424 0.2280  -0.0320 -0.0034 408 LEU A O   
2777  C CB  . LEU A 408 ? 0.6822 0.5457 0.3374 0.2773  -0.0165 -0.0043 408 LEU A CB  
2778  C CG  . LEU A 408 ? 0.6445 0.5534 0.3292 0.2645  -0.0031 0.0152  408 LEU A CG  
2779  C CD1 . LEU A 408 ? 0.6433 0.5627 0.3317 0.2758  0.0012  0.0161  408 LEU A CD1 
2780  C CD2 . LEU A 408 ? 0.6391 0.5980 0.3254 0.2700  0.0055  0.0250  408 LEU A CD2 
2781  N N   . GLU A 409 ? 0.6770 0.4734 0.3797 0.2212  -0.0212 0.0091  409 GLU A N   
2782  C CA  . GLU A 409 ? 0.6455 0.4310 0.3707 0.1948  -0.0206 0.0193  409 GLU A CA  
2783  C C   . GLU A 409 ? 0.6245 0.4516 0.3724 0.1820  -0.0109 0.0355  409 GLU A C   
2784  O O   . GLU A 409 ? 0.6189 0.4539 0.3772 0.1667  -0.0107 0.0422  409 GLU A O   
2785  C CB  . GLU A 409 ? 0.6297 0.3800 0.3615 0.1877  -0.0230 0.0196  409 GLU A CB  
2786  C CG  . GLU A 409 ? 0.6648 0.3725 0.3765 0.2000  -0.0331 0.0056  409 GLU A CG  
2787  C CD  . GLU A 409 ? 0.6560 0.3394 0.3849 0.1793  -0.0342 0.0081  409 GLU A CD  
2788  O OE1 . GLU A 409 ? 0.6276 0.3246 0.3769 0.1657  -0.0264 0.0191  409 GLU A OE1 
2789  O OE2 . GLU A 409 ? 0.6753 0.3337 0.4013 0.1745  -0.0428 -0.0003 409 GLU A OE2 
2790  N N   . ASN A 410 ? 0.5801 0.4331 0.3367 0.1878  -0.0042 0.0421  410 ASN A N   
2791  C CA  . ASN A 410 ? 0.5489 0.4362 0.3302 0.1743  0.0024  0.0582  410 ASN A CA  
2792  C C   . ASN A 410 ? 0.5490 0.4842 0.3315 0.1884  0.0093  0.0635  410 ASN A C   
2793  O O   . ASN A 410 ? 0.5601 0.5029 0.3359 0.2054  0.0112  0.0593  410 ASN A O   
2794  C CB  . ASN A 410 ? 0.5339 0.4064 0.3296 0.1657  0.0024  0.0634  410 ASN A CB  
2795  C CG  . ASN A 410 ? 0.5381 0.3634 0.3311 0.1552  -0.0030 0.0590  410 ASN A CG  
2796  O OD1 . ASN A 410 ? 0.5391 0.3501 0.3311 0.1450  -0.0064 0.0577  410 ASN A OD1 
2797  N ND2 . ASN A 410 ? 0.5411 0.3438 0.3337 0.1582  -0.0037 0.0577  410 ASN A ND2 
2798  N N   . LEU A 411 ? 0.5327 0.5011 0.3241 0.1817  0.0133  0.0736  411 LEU A N   
2799  C CA  . LEU A 411 ? 0.5317 0.5511 0.3279 0.1931  0.0212  0.0826  411 LEU A CA  
2800  C C   . LEU A 411 ? 0.5015 0.5527 0.3286 0.1734  0.0246  0.1022  411 LEU A C   
2801  O O   . LEU A 411 ? 0.4883 0.5319 0.3238 0.1551  0.0221  0.1078  411 LEU A O   
2802  C CB  . LEU A 411 ? 0.5529 0.5855 0.3277 0.2072  0.0229  0.0774  411 LEU A CB  
2803  C CG  . LEU A 411 ? 0.5512 0.6417 0.3326 0.2177  0.0329  0.0905  411 LEU A CG  
2804  C CD1 . LEU A 411 ? 0.5612 0.6732 0.3401 0.2387  0.0375  0.0889  411 LEU A CD1 
2805  C CD2 . LEU A 411 ? 0.5721 0.6725 0.3309 0.2302  0.0343  0.0862  411 LEU A CD2 
2806  N N   . THR A 412 ? 0.5487 0.6350 0.3932 0.1775  0.0292  0.1127  412 THR A N   
2807  C CA  . THR A 412 ? 0.5169 0.6278 0.3936 0.1585  0.0291  0.1309  412 THR A CA  
2808  C C   . THR A 412 ? 0.5139 0.6824 0.4065 0.1660  0.0369  0.1459  412 THR A C   
2809  O O   . THR A 412 ? 0.5203 0.7067 0.4112 0.1834  0.0404  0.1437  412 THR A O   
2810  C CB  . THR A 412 ? 0.4968 0.5841 0.3852 0.1518  0.0232  0.1295  412 THR A CB  
2811  O OG1 . THR A 412 ? 0.4985 0.5395 0.3791 0.1398  0.0171  0.1218  412 THR A OG1 
2812  C CG2 . THR A 412 ? 0.4691 0.5857 0.3901 0.1374  0.0213  0.1474  412 THR A CG2 
2813  N N   . LEU A 413 ? 0.4737 0.6723 0.3823 0.1533  0.0396  0.1620  413 LEU A N   
2814  C CA  . LEU A 413 ? 0.4727 0.7296 0.3977 0.1596  0.0482  0.1794  413 LEU A CA  
2815  C C   . LEU A 413 ? 0.4493 0.7326 0.4105 0.1361  0.0458  0.2020  413 LEU A C   
2816  O O   . LEU A 413 ? 0.4482 0.7775 0.4233 0.1358  0.0528  0.2196  413 LEU A O   
2817  C CB  . LEU A 413 ? 0.4924 0.7675 0.3938 0.1753  0.0564  0.1773  413 LEU A CB  
2818  C CG  . LEU A 413 ? 0.5211 0.7697 0.3835 0.2000  0.0567  0.1547  413 LEU A CG  
2819  C CD1 . LEU A 413 ? 0.5368 0.7810 0.3754 0.2052  0.0582  0.1500  413 LEU A CD1 
2820  C CD2 . LEU A 413 ? 0.5367 0.8182 0.3935 0.2260  0.0641  0.1540  413 LEU A CD2 
2821  N N   . ASP A 414 ? 0.4743 0.7293 0.4506 0.1171  0.0353  0.2026  414 ASP A N   
2822  C CA  . ASP A 414 ? 0.4541 0.7247 0.4606 0.0939  0.0297  0.2218  414 ASP A CA  
2823  C C   . ASP A 414 ? 0.4472 0.7696 0.4872 0.0925  0.0318  0.2426  414 ASP A C   
2824  O O   . ASP A 414 ? 0.4513 0.7882 0.4965 0.1058  0.0338  0.2406  414 ASP A O   
2825  C CB  . ASP A 414 ? 0.4415 0.6692 0.4545 0.0777  0.0169  0.2164  414 ASP A CB  
2826  C CG  . ASP A 414 ? 0.4468 0.6266 0.4321 0.0768  0.0149  0.1992  414 ASP A CG  
2827  O OD1 . ASP A 414 ? 0.4614 0.6381 0.4224 0.0892  0.0218  0.1895  414 ASP A OD1 
2828  O OD2 . ASP A 414 ? 0.4378 0.5828 0.4272 0.0634  0.0061  0.1926  414 ASP A OD2 
2829  N N   . ASP A 415 ? 0.4712 0.8198 0.5374 0.0749  0.0311  0.2594  415 ASP A N   
2830  C CA  . ASP A 415 ? 0.4639 0.8572 0.5708 0.0659  0.0292  0.2819  415 ASP A CA  
2831  C C   . ASP A 415 ? 0.4888 0.9323 0.5980 0.0877  0.0412  0.2925  415 ASP A C   
2832  O O   . ASP A 415 ? 0.4908 0.9472 0.6167 0.0932  0.0382  0.2945  415 ASP A O   
2833  C CB  . ASP A 415 ? 0.4472 0.8166 0.5751 0.0520  0.0136  0.2814  415 ASP A CB  
2834  C CG  . ASP A 415 ? 0.4400 0.7660 0.5679 0.0310  0.0022  0.2721  415 ASP A CG  
2835  O OD1 . ASP A 415 ? 0.4260 0.7646 0.5688 0.0162  0.0009  0.2806  415 ASP A OD1 
2836  O OD2 . ASP A 415 ? 0.4442 0.7245 0.5571 0.0308  -0.0056 0.2555  415 ASP A OD2 
2837  N N   . ASN A 416 ? 0.4711 0.9398 0.5652 0.1007  0.0547  0.2928  416 ASN A N   
2838  C CA  . ASN A 416 ? 0.4880 1.0046 0.5796 0.1246  0.0682  0.2996  416 ASN A CA  
2839  C C   . ASN A 416 ? 0.4774 1.0332 0.5828 0.1244  0.0747  0.3119  416 ASN A C   
2840  O O   . ASN A 416 ? 0.4757 1.0252 0.5973 0.1039  0.0677  0.3186  416 ASN A O   
2841  C CB  . ASN A 416 ? 0.5181 1.0079 0.5643 0.1517  0.0737  0.2743  416 ASN A CB  
2842  C CG  . ASN A 416 ? 0.5297 0.9967 0.5760 0.1591  0.0670  0.2599  416 ASN A CG  
2843  O OD1 . ASN A 416 ? 0.5373 1.0384 0.5935 0.1746  0.0724  0.2642  416 ASN A OD1 
2844  N ND2 . ASN A 416 ? 0.5244 0.9346 0.5592 0.1491  0.0557  0.2433  416 ASN A ND2 
2845  N N   . HIS A 417 ? 0.4773 1.0697 0.5736 0.1490  0.0854  0.3140  417 HIS A N   
2846  C CA  . HIS A 417 ? 0.4966 1.1224 0.5985 0.1540  0.0897  0.3258  417 HIS A CA  
2847  C C   . HIS A 417 ? 0.5177 1.1381 0.5780 0.1826  0.0994  0.3074  417 HIS A C   
2848  O O   . HIS A 417 ? 0.5502 1.2068 0.6067 0.2025  0.1063  0.3145  417 HIS A O   
2849  C CB  . HIS A 417 ? 0.5084 1.1848 0.6414 0.1546  0.0897  0.3519  417 HIS A CB  
2850  C CG  . HIS A 417 ? 0.4846 1.1614 0.6562 0.1265  0.0771  0.3702  417 HIS A CG  
2851  N ND1 . HIS A 417 ? 0.4708 1.1393 0.6645 0.1018  0.0665  0.3807  417 HIS A ND1 
2852  C CD2 . HIS A 417 ? 0.4709 1.1502 0.6601 0.1195  0.0722  0.3781  417 HIS A CD2 
2853  C CE1 . HIS A 417 ? 0.4599 1.1245 0.6823 0.0817  0.0541  0.3947  417 HIS A CE1 
2854  N NE2 . HIS A 417 ? 0.4611 1.1313 0.6812 0.0909  0.0580  0.3935  417 HIS A NE2 
2855  N N   . PHE A 418 ? 0.5051 1.0759 0.5316 0.1850  0.0979  0.2835  418 PHE A N   
2856  C CA  . PHE A 418 ? 0.5317 1.0878 0.5170 0.2096  0.1030  0.2643  418 PHE A CA  
2857  C C   . PHE A 418 ? 0.5392 1.1031 0.5242 0.2047  0.1043  0.2696  418 PHE A C   
2858  O O   . PHE A 418 ? 0.5222 1.0798 0.5280 0.1790  0.0990  0.2794  418 PHE A O   
2859  C CB  . PHE A 418 ? 0.5350 1.0310 0.4843 0.2116  0.0975  0.2385  418 PHE A CB  
2860  C CG  . PHE A 418 ? 0.5387 1.0233 0.4755 0.2261  0.0971  0.2281  418 PHE A CG  
2861  C CD1 . PHE A 418 ? 0.5625 1.0664 0.4816 0.2569  0.1030  0.2203  418 PHE A CD1 
2862  C CD2 . PHE A 418 ? 0.5211 0.9728 0.4625 0.2100  0.0891  0.2256  418 PHE A CD2 
2863  C CE1 . PHE A 418 ? 0.5674 1.0589 0.4740 0.2709  0.1020  0.2094  418 PHE A CE1 
2864  C CE2 . PHE A 418 ? 0.5265 0.9640 0.4564 0.2238  0.0870  0.2148  418 PHE A CE2 
2865  C CZ  . PHE A 418 ? 0.5495 1.0087 0.4597 0.2547  0.0948  0.2075  418 PHE A CZ  
2866  N N   . GLU A 419 ? 0.5796 1.1557 0.5394 0.2310  0.1105  0.2625  419 GLU A N   
2867  C CA  . GLU A 419 ? 0.5922 1.1766 0.5464 0.2318  0.1127  0.2664  419 GLU A CA  
2868  C C   . GLU A 419 ? 0.6237 1.1857 0.5322 0.2602  0.1144  0.2435  419 GLU A C   
2869  O O   . GLU A 419 ? 0.6354 1.1750 0.5189 0.2777  0.1127  0.2253  419 GLU A O   
2870  C CB  . GLU A 419 ? 0.5961 1.2391 0.5815 0.2333  0.1180  0.2939  419 GLU A CB  
2871  C CG  . GLU A 419 ? 0.6281 1.3051 0.5969 0.2673  0.1259  0.2951  419 GLU A CG  
2872  C CD  . GLU A 419 ? 0.6318 1.3668 0.6337 0.2668  0.1301  0.3254  419 GLU A CD  
2873  O OE1 . GLU A 419 ? 0.6089 1.3563 0.6480 0.2403  0.1256  0.3446  419 GLU A OE1 
2874  O OE2 . GLU A 419 ? 0.6649 1.4314 0.6546 0.2933  0.1368  0.3305  419 GLU A OE2 
2875  N N   . GLY A 420 ? 0.6267 1.1921 0.5237 0.2651  0.1163  0.2439  420 GLY A N   
2876  C CA  . GLY A 420 ? 0.6593 1.2025 0.5138 0.2917  0.1157  0.2228  420 GLY A CA  
2877  C C   . GLY A 420 ? 0.6576 1.1401 0.4848 0.2818  0.1063  0.2005  420 GLY A C   
2878  O O   . GLY A 420 ? 0.6307 1.0893 0.4717 0.2540  0.1011  0.2023  420 GLY A O   
2879  N N   . PRO A 421 ? 0.6743 1.1298 0.4621 0.3052  0.1024  0.1793  421 PRO A N   
2880  C CA  . PRO A 421 ? 0.6770 1.0754 0.4384 0.2963  0.0917  0.1593  421 PRO A CA  
2881  C C   . PRO A 421 ? 0.6756 1.0323 0.4210 0.2976  0.0835  0.1413  421 PRO A C   
2882  O O   . PRO A 421 ? 0.6737 1.0440 0.4259 0.3071  0.0865  0.1424  421 PRO A O   
2883  C CB  . PRO A 421 ? 0.7152 1.1069 0.4435 0.3227  0.0897  0.1462  421 PRO A CB  
2884  C CG  . PRO A 421 ? 0.7382 1.1654 0.4631 0.3536  0.0961  0.1485  421 PRO A CG  
2885  C CD  . PRO A 421 ? 0.7112 1.1874 0.4776 0.3411  0.1059  0.1738  421 PRO A CD  
2886  N N   . VAL A 422 ? 0.7060 1.0117 0.4304 0.2883  0.0724  0.1254  422 VAL A N   
2887  C CA  . VAL A 422 ? 0.7100 0.9702 0.4156 0.2906  0.0627  0.1074  422 VAL A CA  
2888  C C   . VAL A 422 ? 0.7516 0.9918 0.4209 0.3236  0.0563  0.0853  422 VAL A C   
2889  O O   . VAL A 422 ? 0.7802 1.0108 0.4291 0.3352  0.0518  0.0765  422 VAL A O   
2890  C CB  . VAL A 422 ? 0.6955 0.9105 0.3971 0.2663  0.0520  0.1019  422 VAL A CB  
2891  C CG1 . VAL A 422 ? 0.6896 0.8667 0.3849 0.2619  0.0441  0.0920  422 VAL A CG1 
2892  C CG2 . VAL A 422 ? 0.6620 0.8983 0.3971 0.2366  0.0568  0.1233  422 VAL A CG2 
2893  N N   . PRO A 423 ? 0.7699 1.0025 0.4306 0.3398  0.0545  0.0758  423 PRO A N   
2894  C CA  . PRO A 423 ? 0.8175 1.0294 0.4451 0.3719  0.0461  0.0549  423 PRO A CA  
2895  C C   . PRO A 423 ? 0.8393 0.9917 0.4376 0.3712  0.0293  0.0335  423 PRO A C   
2896  O O   . PRO A 423 ? 0.8194 0.9379 0.4199 0.3481  0.0225  0.0312  423 PRO A O   
2897  C CB  . PRO A 423 ? 0.8135 1.0233 0.4422 0.3823  0.0461  0.0505  423 PRO A CB  
2898  C CG  . PRO A 423 ? 0.7736 1.0231 0.4395 0.3618  0.0587  0.0734  423 PRO A CG  
2899  C CD  . PRO A 423 ? 0.7459 0.9895 0.4275 0.3307  0.0592  0.0843  423 PRO A CD  
2900  N N   . LYS A 424 ? 0.8612 1.0012 0.4326 0.3974  0.0213  0.0186  424 LYS A N   
2901  C CA  . LYS A 424 ? 0.8860 0.9696 0.4300 0.3991  0.0027  -0.0024 424 LYS A CA  
2902  C C   . LYS A 424 ? 0.8890 0.9219 0.4232 0.3936  -0.0105 -0.0171 424 LYS A C   
2903  O O   . LYS A 424 ? 0.8942 0.8798 0.4169 0.3814  -0.0250 -0.0287 424 LYS A O   
2904  C CB  . LYS A 424 ? 0.9327 1.0119 0.4500 0.4321  -0.0054 -0.0158 424 LYS A CB  
2905  C CG  . LYS A 424 ? 0.9377 1.0685 0.4612 0.4442  0.0078  -0.0016 424 LYS A CG  
2906  C CD  . LYS A 424 ? 0.9017 1.0580 0.4493 0.4155  0.0192  0.0176  424 LYS A CD  
2907  C CE  . LYS A 424 ? 0.9215 1.0967 0.4602 0.4274  0.0217  0.0208  424 LYS A CE  
2908  N NZ  . LYS A 424 ? 0.8881 1.0896 0.4515 0.3998  0.0325  0.0409  424 LYS A NZ  
2909  N N   . SER A 425 ? 0.9121 0.9540 0.4514 0.4026  -0.0064 -0.0164 425 SER A N   
2910  C CA  . SER A 425 ? 0.9164 0.9114 0.4476 0.3974  -0.0179 -0.0288 425 SER A CA  
2911  C C   . SER A 425 ? 0.8758 0.8573 0.4237 0.3646  -0.0156 -0.0194 425 SER A C   
2912  O O   . SER A 425 ? 0.8914 0.8226 0.4287 0.3555  -0.0289 -0.0308 425 SER A O   
2913  C CB  . SER A 425 ? 0.9184 0.9306 0.4527 0.4146  -0.0131 -0.0282 425 SER A CB  
2914  O OG  . SER A 425 ? 0.9628 0.9922 0.4823 0.4457  -0.0157 -0.0334 425 SER A OG  
2915  N N   . LEU A 426 ? 0.8344 0.8593 0.4096 0.3465  -0.0003 0.0026  426 LEU A N   
2916  C CA  . LEU A 426 ? 0.8097 0.8233 0.4087 0.3137  0.0003  0.0142  426 LEU A CA  
2917  C C   . LEU A 426 ? 0.8109 0.7962 0.4097 0.2962  -0.0096 0.0106  426 LEU A C   
2918  O O   . LEU A 426 ? 0.8052 0.7576 0.4230 0.2712  -0.0163 0.0100  426 LEU A O   
2919  C CB  . LEU A 426 ? 0.7731 0.8409 0.4041 0.3001  0.0173  0.0394  426 LEU A CB  
2920  C CG  . LEU A 426 ? 0.7444 0.8026 0.4123 0.2676  0.0182  0.0506  426 LEU A CG  
2921  C CD1 . LEU A 426 ? 0.7632 0.7722 0.4286 0.2647  0.0079  0.0359  426 LEU A CD1 
2922  C CD2 . LEU A 426 ? 0.7155 0.8245 0.4110 0.2627  0.0321  0.0716  426 LEU A CD2 
2923  N N   . ARG A 427 ? 0.8259 0.8251 0.4040 0.3098  -0.0102 0.0087  427 ARG A N   
2924  C CA  . ARG A 427 ? 0.8323 0.8042 0.4075 0.2958  -0.0209 0.0037  427 ARG A CA  
2925  C C   . ARG A 427 ? 0.8682 0.7784 0.4310 0.2952  -0.0410 -0.0180 427 ARG A C   
2926  O O   . ARG A 427 ? 0.8632 0.7437 0.4429 0.2705  -0.0491 -0.0185 427 ARG A O   
2927  C CB  . ARG A 427 ? 0.8381 0.8353 0.4002 0.3117  -0.0177 0.0033  427 ARG A CB  
2928  C CG  . ARG A 427 ? 0.8536 0.8170 0.4003 0.3068  -0.0326 -0.0076 427 ARG A CG  
2929  C CD  . ARG A 427 ? 0.8771 0.8642 0.4128 0.3256  -0.0294 -0.0096 427 ARG A CD  
2930  N NE  . ARG A 427 ? 0.9260 0.8825 0.4321 0.3536  -0.0442 -0.0322 427 ARG A NE  
2931  C CZ  . ARG A 427 ? 0.9579 0.9379 0.4522 0.3820  -0.0399 -0.0352 427 ARG A CZ  
2932  N NH1 . ARG A 427 ? 0.9451 0.9809 0.4543 0.3865  -0.0206 -0.0170 427 ARG A NH1 
2933  N NH2 . ARG A 427 ? 0.9960 0.9424 0.4640 0.4068  -0.0566 -0.0558 427 ARG A NH2 
2934  N N   . ASP A 428 ? 0.8775 0.7680 0.4116 0.3223  -0.0496 -0.0353 428 ASP A N   
2935  C CA  . ASP A 428 ? 0.9072 0.7380 0.4279 0.3241  -0.0709 -0.0559 428 ASP A CA  
2936  C C   . ASP A 428 ? 0.9105 0.7140 0.4511 0.3095  -0.0729 -0.0562 428 ASP A C   
2937  O O   . ASP A 428 ? 0.9409 0.6942 0.4763 0.3066  -0.0902 -0.0701 428 ASP A O   
2938  C CB  . ASP A 428 ? 0.9503 0.7692 0.4329 0.3606  -0.0819 -0.0749 428 ASP A CB  
2939  C CG  . ASP A 428 ? 0.9600 0.8162 0.4389 0.3752  -0.0748 -0.0704 428 ASP A CG  
2940  O OD1 . ASP A 428 ? 0.9411 0.8113 0.4287 0.3592  -0.0703 -0.0610 428 ASP A OD1 
2941  O OD2 . ASP A 428 ? 0.9879 0.8590 0.4550 0.4033  -0.0743 -0.0756 428 ASP A OD2 
2942  N N   . CYS A 429 ? 0.8681 0.7028 0.4315 0.3005  -0.0567 -0.0407 429 CYS A N   
2943  C CA  . CYS A 429 ? 0.8738 0.6851 0.4549 0.2881  -0.0573 -0.0398 429 CYS A CA  
2944  C C   . CYS A 429 ? 0.8636 0.6490 0.4729 0.2549  -0.0613 -0.0334 429 CYS A C   
2945  O O   . CYS A 429 ? 0.8309 0.6416 0.4663 0.2341  -0.0502 -0.0167 429 CYS A O   
2946  C CB  . CYS A 429 ? 0.8501 0.7045 0.4466 0.2897  -0.0397 -0.0253 429 CYS A CB  
2947  S SG  . CYS A 429 ? 0.8617 0.6912 0.4780 0.2770  -0.0393 -0.0234 429 CYS A SG  
2948  N N   . LYS A 430 ? 0.8941 0.6288 0.4986 0.2504  -0.0781 -0.0461 430 LYS A N   
2949  C CA  . LYS A 430 ? 0.8777 0.5874 0.5075 0.2213  -0.0830 -0.0405 430 LYS A CA  
2950  C C   . LYS A 430 ? 0.8403 0.5409 0.4956 0.2035  -0.0764 -0.0304 430 LYS A C   
2951  O O   . LYS A 430 ? 0.8121 0.4993 0.4906 0.1795  -0.0772 -0.0225 430 LYS A O   
2952  C CB  . LYS A 430 ? 0.8852 0.5458 0.5027 0.2231  -0.1047 -0.0566 430 LYS A CB  
2953  C CG  . LYS A 430 ? 0.9228 0.5832 0.5078 0.2469  -0.1154 -0.0711 430 LYS A CG  
2954  C CD  . LYS A 430 ? 0.9347 0.5434 0.5115 0.2458  -0.1397 -0.0867 430 LYS A CD  
2955  C CE  . LYS A 430 ? 0.9528 0.5652 0.5277 0.2401  -0.1463 -0.0883 430 LYS A CE  
2956  N NZ  . LYS A 430 ? 0.9700 0.5355 0.5273 0.2490  -0.1728 -0.1075 430 LYS A NZ  
2957  N N   . SER A 431 ? 0.8095 0.5173 0.4601 0.2159  -0.0701 -0.0303 431 SER A N   
2958  C CA  . SER A 431 ? 0.7734 0.4670 0.4431 0.2030  -0.0658 -0.0230 431 SER A CA  
2959  C C   . SER A 431 ? 0.7466 0.4779 0.4400 0.1895  -0.0495 -0.0052 431 SER A C   
2960  O O   . SER A 431 ? 0.7158 0.4412 0.4214 0.1839  -0.0447 0.0007  431 SER A O   
2961  C CB  . SER A 431 ? 0.7852 0.4615 0.4366 0.2239  -0.0696 -0.0333 431 SER A CB  
2962  O OG  . SER A 431 ? 0.7941 0.5088 0.4319 0.2450  -0.0605 -0.0336 431 SER A OG  
2963  N N   . LEU A 432 ? 0.6915 0.4597 0.3914 0.1847  -0.0421 0.0036  432 LEU A N   
2964  C CA  . LEU A 432 ? 0.6554 0.4589 0.3780 0.1724  -0.0292 0.0205  432 LEU A CA  
2965  C C   . LEU A 432 ? 0.6303 0.4158 0.3769 0.1474  -0.0292 0.0295  432 LEU A C   
2966  O O   . LEU A 432 ? 0.6332 0.3934 0.3831 0.1354  -0.0367 0.0268  432 LEU A O   
2967  C CB  . LEU A 432 ? 0.6450 0.4901 0.3687 0.1727  -0.0226 0.0287  432 LEU A CB  
2968  C CG  . LEU A 432 ? 0.6645 0.5408 0.3682 0.1985  -0.0179 0.0252  432 LEU A CG  
2969  C CD1 . LEU A 432 ? 0.6547 0.5718 0.3612 0.1970  -0.0109 0.0359  432 LEU A CD1 
2970  C CD2 . LEU A 432 ? 0.6579 0.5537 0.3675 0.2078  -0.0100 0.0298  432 LEU A CD2 
2971  N N   . ILE A 433 ? 0.6008 0.4001 0.3640 0.1407  -0.0213 0.0403  433 ILE A N   
2972  C CA  . ILE A 433 ? 0.5622 0.3481 0.3462 0.1202  -0.0203 0.0497  433 ILE A CA  
2973  C C   . ILE A 433 ? 0.5645 0.3861 0.3670 0.1095  -0.0129 0.0644  433 ILE A C   
2974  O O   . ILE A 433 ? 0.5419 0.3652 0.3571 0.0929  -0.0136 0.0717  433 ILE A O   
2975  C CB  . ILE A 433 ? 0.5771 0.3363 0.3621 0.1229  -0.0206 0.0480  433 ILE A CB  
2976  C CG1 . ILE A 433 ? 0.5985 0.3187 0.3673 0.1313  -0.0299 0.0347  433 ILE A CG1 
2977  C CG2 . ILE A 433 ? 0.5455 0.2955 0.3502 0.1048  -0.0182 0.0590  433 ILE A CG2 
2978  C CD1 . ILE A 433 ? 0.6009 0.2959 0.3746 0.1294  -0.0301 0.0339  433 ILE A CD1 
2979  N N   . ARG A 434 ? 0.5724 0.4218 0.3775 0.1187  -0.0070 0.0691  434 ARG A N   
2980  C CA  . ARG A 434 ? 0.5468 0.4319 0.3707 0.1095  -0.0018 0.0837  434 ARG A CA  
2981  C C   . ARG A 434 ? 0.5650 0.4900 0.3837 0.1225  0.0033  0.0862  434 ARG A C   
2982  O O   . ARG A 434 ? 0.5855 0.5187 0.3935 0.1407  0.0057  0.0806  434 ARG A O   
2983  C CB  . ARG A 434 ? 0.5200 0.4042 0.3574 0.1066  -0.0002 0.0900  434 ARG A CB  
2984  C CG  . ARG A 434 ? 0.4848 0.3492 0.3358 0.0889  -0.0031 0.0963  434 ARG A CG  
2985  C CD  . ARG A 434 ? 0.4658 0.3300 0.3276 0.0889  -0.0026 0.1019  434 ARG A CD  
2986  N NE  . ARG A 434 ? 0.4467 0.3441 0.3272 0.0812  -0.0026 0.1138  434 ARG A NE  
2987  C CZ  . ARG A 434 ? 0.4269 0.3272 0.3263 0.0623  -0.0075 0.1169  434 ARG A CZ  
2988  N NH1 . ARG A 434 ? 0.4200 0.2993 0.3240 0.0499  -0.0115 0.1103  434 ARG A NH1 
2989  N NH2 . ARG A 434 ? 0.4145 0.3414 0.3294 0.0561  -0.0094 0.1259  434 ARG A NH2 
2990  N N   . VAL A 435 ? 0.5172 0.4680 0.3432 0.1141  0.0053  0.0954  435 VAL A N   
2991  C CA  . VAL A 435 ? 0.5214 0.5153 0.3454 0.1248  0.0116  0.1020  435 VAL A CA  
2992  C C   . VAL A 435 ? 0.4956 0.5222 0.3464 0.1093  0.0148  0.1211  435 VAL A C   
2993  O O   . VAL A 435 ? 0.4801 0.4977 0.3425 0.0907  0.0110  0.1273  435 VAL A O   
2994  C CB  . VAL A 435 ? 0.5393 0.5339 0.3440 0.1316  0.0105  0.0957  435 VAL A CB  
2995  C CG1 . VAL A 435 ? 0.5514 0.5887 0.3476 0.1499  0.0183  0.1003  435 VAL A CG1 
2996  C CG2 . VAL A 435 ? 0.5637 0.5150 0.3460 0.1406  0.0025  0.0767  435 VAL A CG2 
2997  N N   . ARG A 436 ? 0.5248 0.5888 0.3862 0.1170  0.0206  0.1306  436 ARG A N   
2998  C CA  . ARG A 436 ? 0.4928 0.5878 0.3829 0.1022  0.0216  0.1498  436 ARG A CA  
2999  C C   . ARG A 436 ? 0.4975 0.6441 0.3929 0.1126  0.0302  0.1620  436 ARG A C   
3000  O O   . ARG A 436 ? 0.5032 0.6716 0.4010 0.1269  0.0347  0.1630  436 ARG A O   
3001  C CB  . ARG A 436 ? 0.4807 0.5660 0.3869 0.0975  0.0177  0.1518  436 ARG A CB  
3002  C CG  . ARG A 436 ? 0.4748 0.5140 0.3784 0.0866  0.0103  0.1438  436 ARG A CG  
3003  C CD  . ARG A 436 ? 0.4574 0.4958 0.3832 0.0753  0.0048  0.1529  436 ARG A CD  
3004  N NE  . ARG A 436 ? 0.4423 0.5108 0.3922 0.0603  0.0027  0.1677  436 ARG A NE  
3005  C CZ  . ARG A 436 ? 0.4286 0.4833 0.3936 0.0416  -0.0048 0.1667  436 ARG A CZ  
3006  N NH1 . ARG A 436 ? 0.4269 0.4426 0.3841 0.0364  -0.0098 0.1550  436 ARG A NH1 
3007  N NH2 . ARG A 436 ? 0.4182 0.4994 0.4058 0.0291  -0.0071 0.1769  436 ARG A NH2 
3008  N N   . PHE A 437 ? 0.4542 0.6212 0.3515 0.1060  0.0327  0.1719  437 PHE A N   
3009  C CA  . PHE A 437 ? 0.4586 0.6767 0.3636 0.1138  0.0418  0.1856  437 PHE A CA  
3010  C C   . PHE A 437 ? 0.4369 0.6838 0.3817 0.0928  0.0407  0.2039  437 PHE A C   
3011  O O   . PHE A 437 ? 0.4388 0.7277 0.3977 0.0948  0.0476  0.2162  437 PHE A O   
3012  C CB  . PHE A 437 ? 0.4754 0.6951 0.3590 0.1212  0.0450  0.1797  437 PHE A CB  
3013  C CG  . PHE A 437 ? 0.5044 0.7149 0.3511 0.1493  0.0478  0.1639  437 PHE A CG  
3014  C CD1 . PHE A 437 ? 0.5129 0.6871 0.3460 0.1579  0.0425  0.1462  437 PHE A CD1 
3015  C CD2 . PHE A 437 ? 0.5246 0.7572 0.3563 0.1651  0.0538  0.1615  437 PHE A CD2 
3016  C CE1 . PHE A 437 ? 0.5421 0.7030 0.3438 0.1827  0.0424  0.1286  437 PHE A CE1 
3017  C CE2 . PHE A 437 ? 0.5546 0.7753 0.3517 0.1920  0.0540  0.1444  437 PHE A CE2 
3018  C CZ  . PHE A 437 ? 0.5640 0.7483 0.3447 0.2011  0.0476  0.1282  437 PHE A CZ  
3019  N N   . LYS A 438 ? 0.4577 0.6815 0.4207 0.0738  0.0313  0.2051  438 LYS A N   
3020  C CA  . LYS A 438 ? 0.4354 0.6751 0.4326 0.0522  0.0261  0.2182  438 LYS A CA  
3021  C C   . LYS A 438 ? 0.4373 0.7286 0.4619 0.0549  0.0311  0.2367  438 LYS A C   
3022  O O   . LYS A 438 ? 0.4432 0.7506 0.4671 0.0692  0.0354  0.2393  438 LYS A O   
3023  C CB  . LYS A 438 ? 0.4213 0.6255 0.4294 0.0368  0.0143  0.2127  438 LYS A CB  
3024  C CG  . LYS A 438 ? 0.4063 0.6107 0.4401 0.0148  0.0055  0.2184  438 LYS A CG  
3025  C CD  . LYS A 438 ? 0.3959 0.5696 0.4393 0.0044  -0.0059 0.2117  438 LYS A CD  
3026  C CE  . LYS A 438 ? 0.3911 0.5463 0.4430 -0.0127 -0.0150 0.2067  438 LYS A CE  
3027  N NZ  . LYS A 438 ? 0.3874 0.5761 0.4684 -0.0242 -0.0190 0.2218  438 LYS A NZ  
3028  N N   . GLY A 439 ? 0.4312 0.7491 0.4809 0.0416  0.0300  0.2501  439 GLY A N   
3029  C CA  . GLY A 439 ? 0.4219 0.7894 0.5050 0.0399  0.0321  0.2709  439 GLY A CA  
3030  C C   . GLY A 439 ? 0.4361 0.8468 0.5125 0.0628  0.0462  0.2778  439 GLY A C   
3031  O O   . GLY A 439 ? 0.4358 0.8688 0.5205 0.0730  0.0497  0.2844  439 GLY A O   
3032  N N   . ASN A 440 ? 0.4460 0.8687 0.5066 0.0723  0.0538  0.2759  440 ASN A N   
3033  C CA  . ASN A 440 ? 0.4641 0.9265 0.5153 0.0969  0.0667  0.2800  440 ASN A CA  
3034  C C   . ASN A 440 ? 0.4738 0.9593 0.5284 0.0968  0.0704  0.2882  440 ASN A C   
3035  O O   . ASN A 440 ? 0.4642 0.9418 0.5350 0.0763  0.0628  0.2942  440 ASN A O   
3036  C CB  . ASN A 440 ? 0.4816 0.9182 0.4897 0.1205  0.0721  0.2586  440 ASN A CB  
3037  C CG  . ASN A 440 ? 0.4785 0.9085 0.4844 0.1288  0.0712  0.2546  440 ASN A CG  
3038  O OD1 . ASN A 440 ? 0.4836 0.9520 0.4992 0.1435  0.0782  0.2634  440 ASN A OD1 
3039  N ND2 . ASN A 440 ? 0.4716 0.8526 0.4646 0.1204  0.0622  0.2416  440 ASN A ND2 
3040  N N   . SER A 441 ? 0.4718 0.9848 0.5098 0.1213  0.0812  0.2879  441 SER A N   
3041  C CA  . SER A 441 ? 0.4864 1.0204 0.5216 0.1263  0.0859  0.2945  441 SER A CA  
3042  C C   . SER A 441 ? 0.5110 1.0269 0.5019 0.1501  0.0921  0.2748  441 SER A C   
3043  O O   . SER A 441 ? 0.5326 1.0770 0.5141 0.1696  0.0998  0.2786  441 SER A O   
3044  C CB  . SER A 441 ? 0.4934 1.0857 0.5566 0.1336  0.0912  0.3184  441 SER A CB  
3045  O OG  . SER A 441 ? 0.4751 1.0808 0.5791 0.1089  0.0820  0.3380  441 SER A OG  
3046  N N   . PHE A 442 ? 0.5018 0.9685 0.4644 0.1497  0.0871  0.2537  442 PHE A N   
3047  C CA  . PHE A 442 ? 0.5269 0.9689 0.4466 0.1706  0.0889  0.2335  442 PHE A CA  
3048  C C   . PHE A 442 ? 0.5366 0.9780 0.4488 0.1672  0.0889  0.2349  442 PHE A C   
3049  O O   . PHE A 442 ? 0.5201 0.9585 0.4531 0.1433  0.0843  0.2448  442 PHE A O   
3050  C CB  . PHE A 442 ? 0.5236 0.9104 0.4188 0.1665  0.0804  0.2132  442 PHE A CB  
3051  C CG  . PHE A 442 ? 0.5256 0.9072 0.4135 0.1799  0.0811  0.2058  442 PHE A CG  
3052  C CD1 . PHE A 442 ? 0.5510 0.9473 0.4174 0.2104  0.0870  0.1971  442 PHE A CD1 
3053  C CD2 . PHE A 442 ? 0.5043 0.8646 0.4059 0.1633  0.0747  0.2067  442 PHE A CD2 
3054  C CE1 . PHE A 442 ? 0.5545 0.9441 0.4129 0.2235  0.0869  0.1891  442 PHE A CE1 
3055  C CE2 . PHE A 442 ? 0.5078 0.8618 0.4011 0.1765  0.0750  0.1998  442 PHE A CE2 
3056  C CZ  . PHE A 442 ? 0.5326 0.9012 0.4041 0.2064  0.0812  0.1908  442 PHE A CZ  
3057  N N   . SER A 443 ? 0.5036 0.9460 0.3846 0.1924  0.0931  0.2240  443 SER A N   
3058  C CA  . SER A 443 ? 0.5180 0.9636 0.3888 0.1943  0.0943  0.2255  443 SER A CA  
3059  C C   . SER A 443 ? 0.5439 0.9513 0.3698 0.2125  0.0898  0.2014  443 SER A C   
3060  O O   . SER A 443 ? 0.5542 0.9375 0.3575 0.2268  0.0864  0.1844  443 SER A O   
3061  C CB  . SER A 443 ? 0.5329 1.0334 0.4177 0.2097  0.1044  0.2434  443 SER A CB  
3062  O OG  . SER A 443 ? 0.5516 1.0727 0.4250 0.2381  0.1102  0.2393  443 SER A OG  
3063  N N   . GLY A 444 ? 0.5968 0.9972 0.4098 0.2121  0.0884  0.1997  444 GLY A N   
3064  C CA  . GLY A 444 ? 0.6244 0.9904 0.3962 0.2294  0.0823  0.1780  444 GLY A CA  
3065  C C   . GLY A 444 ? 0.6145 0.9409 0.3790 0.2079  0.0722  0.1715  444 GLY A C   
3066  O O   . GLY A 444 ? 0.5856 0.9058 0.3749 0.1798  0.0692  0.1814  444 GLY A O   
3067  N N   . ASP A 445 ? 0.6805 0.9789 0.4099 0.2231  0.0654  0.1538  445 ASP A N   
3068  C CA  . ASP A 445 ? 0.6761 0.9362 0.3945 0.2066  0.0544  0.1457  445 ASP A CA  
3069  C C   . ASP A 445 ? 0.6621 0.8804 0.3759 0.1949  0.0438  0.1338  445 ASP A C   
3070  O O   . ASP A 445 ? 0.6797 0.8772 0.3715 0.2128  0.0389  0.1174  445 ASP A O   
3071  C CB  . ASP A 445 ? 0.7122 0.9572 0.3955 0.2284  0.0491  0.1306  445 ASP A CB  
3072  C CG  . ASP A 445 ? 0.7080 0.9253 0.3850 0.2111  0.0396  0.1275  445 ASP A CG  
3073  O OD1 . ASP A 445 ? 0.7024 0.8786 0.3694 0.2014  0.0270  0.1147  445 ASP A OD1 
3074  O OD2 . ASP A 445 ? 0.7112 0.9485 0.3937 0.2079  0.0444  0.1383  445 ASP A OD2 
3075  N N   . ILE A 446 ? 0.6762 0.8812 0.4113 0.1658  0.0395  0.1419  446 ILE A N   
3076  C CA  . ILE A 446 ? 0.6603 0.8302 0.3966 0.1536  0.0306  0.1345  446 ILE A CA  
3077  C C   . ILE A 446 ? 0.6837 0.8091 0.3853 0.1655  0.0174  0.1128  446 ILE A C   
3078  O O   . ILE A 446 ? 0.6859 0.7834 0.3781 0.1694  0.0108  0.1020  446 ILE A O   
3079  C CB  . ILE A 446 ? 0.6268 0.7910 0.3928 0.1217  0.0277  0.1472  446 ILE A CB  
3080  C CG1 . ILE A 446 ? 0.6083 0.7453 0.3825 0.1104  0.0217  0.1439  446 ILE A CG1 
3081  C CG2 . ILE A 446 ? 0.6297 0.7750 0.3870 0.1115  0.0201  0.1445  446 ILE A CG2 
3082  C CD1 . ILE A 446 ? 0.5954 0.7554 0.3903 0.1112  0.0293  0.1523  446 ILE A CD1 
3083  N N   . SER A 447 ? 0.7335 0.8501 0.4160 0.1720  0.0121  0.1055  447 SER A N   
3084  C CA  . SER A 447 ? 0.7574 0.8308 0.4080 0.1845  -0.0031 0.0835  447 SER A CA  
3085  C C   . SER A 447 ? 0.7958 0.8660 0.4196 0.2162  -0.0044 0.0671  447 SER A C   
3086  O O   . SER A 447 ? 0.8196 0.8488 0.4199 0.2267  -0.0190 0.0471  447 SER A O   
3087  C CB  . SER A 447 ? 0.7650 0.8286 0.4056 0.1803  -0.0101 0.0807  447 SER A CB  
3088  O OG  . SER A 447 ? 0.8036 0.8941 0.4330 0.1991  -0.0028 0.0814  447 SER A OG  
3089  N N   . GLU A 448 ? 0.7798 0.8909 0.4081 0.2316  0.0094  0.0753  448 GLU A N   
3090  C CA  . GLU A 448 ? 0.8121 0.9246 0.4175 0.2635  0.0093  0.0614  448 GLU A CA  
3091  C C   . GLU A 448 ? 0.8033 0.9213 0.4168 0.2682  0.0140  0.0619  448 GLU A C   
3092  O O   . GLU A 448 ? 0.8321 0.9405 0.4249 0.2937  0.0103  0.0471  448 GLU A O   
3093  C CB  . GLU A 448 ? 0.8287 0.9841 0.4334 0.2816  0.0214  0.0703  448 GLU A CB  
3094  C CG  . GLU A 448 ? 0.8780 1.0156 0.4497 0.3068  0.0122  0.0528  448 GLU A CG  
3095  C CD  . GLU A 448 ? 0.8928 1.0721 0.4664 0.3195  0.0243  0.0655  448 GLU A CD  
3096  O OE1 . GLU A 448 ? 0.8719 1.0973 0.4695 0.3176  0.0400  0.0854  448 GLU A OE1 
3097  O OE2 . GLU A 448 ? 0.9170 1.0830 0.4690 0.3316  0.0172  0.0559  448 GLU A OE2 
3098  N N   . ALA A 449 ? 0.7183 0.8501 0.3613 0.2450  0.0208  0.0781  449 ALA A N   
3099  C CA  . ALA A 449 ? 0.7083 0.8502 0.3622 0.2486  0.0264  0.0810  449 ALA A CA  
3100  C C   . ALA A 449 ? 0.7106 0.8042 0.3510 0.2463  0.0136  0.0658  449 ALA A C   
3101  O O   . ALA A 449 ? 0.7250 0.8119 0.3547 0.2635  0.0128  0.0562  449 ALA A O   
3102  C CB  . ALA A 449 ? 0.6701 0.8480 0.3636 0.2255  0.0380  0.1053  449 ALA A CB  
3103  N N   . PHE A 450 ? 0.7153 0.7748 0.3569 0.2261  0.0032  0.0640  450 PHE A N   
3104  C CA  . PHE A 450 ? 0.7208 0.7345 0.3673 0.2158  -0.0079 0.0515  450 PHE A CA  
3105  C C   . PHE A 450 ? 0.7497 0.7160 0.3751 0.2199  -0.0255 0.0305  450 PHE A C   
3106  O O   . PHE A 450 ? 0.7525 0.7160 0.3709 0.2163  -0.0303 0.0299  450 PHE A O   
3107  C CB  . PHE A 450 ? 0.6857 0.6963 0.3691 0.1830  -0.0057 0.0650  450 PHE A CB  
3108  C CG  . PHE A 450 ? 0.6570 0.7091 0.3646 0.1763  0.0081  0.0851  450 PHE A CG  
3109  C CD1 . PHE A 450 ? 0.6542 0.7057 0.3708 0.1797  0.0111  0.0843  450 PHE A CD1 
3110  C CD2 . PHE A 450 ? 0.6337 0.7245 0.3559 0.1664  0.0169  0.1053  450 PHE A CD2 
3111  C CE1 . PHE A 450 ? 0.6289 0.7180 0.3694 0.1735  0.0219  0.1025  450 PHE A CE1 
3112  C CE2 . PHE A 450 ? 0.6074 0.7349 0.3575 0.1581  0.0273  0.1234  450 PHE A CE2 
3113  C CZ  . PHE A 450 ? 0.6058 0.7333 0.3629 0.1628  0.0295  0.1228  450 PHE A CZ  
3114  N N   . GLY A 451 ? 0.7449 0.6733 0.3613 0.2272  -0.0361 0.0138  451 GLY A N   
3115  C CA  . GLY A 451 ? 0.7787 0.6580 0.3812 0.2277  -0.0552 -0.0052 451 GLY A CA  
3116  C C   . GLY A 451 ? 0.7673 0.6157 0.3989 0.1973  -0.0613 -0.0030 451 GLY A C   
3117  O O   . GLY A 451 ? 0.7387 0.6050 0.3964 0.1748  -0.0526 0.0130  451 GLY A O   
3118  N N   . VAL A 452 ? 0.7804 0.5826 0.4078 0.1970  -0.0768 -0.0184 452 VAL A N   
3119  C CA  . VAL A 452 ? 0.7597 0.5322 0.4144 0.1704  -0.0823 -0.0158 452 VAL A CA  
3120  C C   . VAL A 452 ? 0.7522 0.5138 0.4175 0.1687  -0.0784 -0.0144 452 VAL A C   
3121  O O   . VAL A 452 ? 0.7771 0.5326 0.4229 0.1899  -0.0806 -0.0241 452 VAL A O   
3122  C CB  . VAL A 452 ? 0.7858 0.5144 0.4337 0.1681  -0.1030 -0.0311 452 VAL A CB  
3123  C CG1 . VAL A 452 ? 0.7811 0.5192 0.4294 0.1602  -0.1059 -0.0285 452 VAL A CG1 
3124  C CG2 . VAL A 452 ? 0.8331 0.5384 0.4480 0.1962  -0.1167 -0.0507 452 VAL A CG2 
3125  N N   . TYR A 453 ? 0.7573 0.5160 0.4519 0.1449  -0.0728 -0.0026 453 TYR A N   
3126  C CA  . TYR A 453 ? 0.7452 0.4948 0.4513 0.1419  -0.0679 0.0007  453 TYR A CA  
3127  C C   . TYR A 453 ? 0.7184 0.4366 0.4474 0.1196  -0.0735 0.0037  453 TYR A C   
3128  O O   . TYR A 453 ? 0.6862 0.4164 0.4379 0.1005  -0.0660 0.0171  453 TYR A O   
3129  C CB  . TYR A 453 ? 0.7136 0.5039 0.4322 0.1395  -0.0511 0.0162  453 TYR A CB  
3130  C CG  . TYR A 453 ? 0.7177 0.5479 0.4202 0.1577  -0.0433 0.0185  453 TYR A CG  
3131  C CD1 . TYR A 453 ? 0.7415 0.5767 0.4211 0.1836  -0.0431 0.0092  453 TYR A CD1 
3132  C CD2 . TYR A 453 ? 0.6893 0.5530 0.3994 0.1499  -0.0361 0.0309  453 TYR A CD2 
3133  C CE1 . TYR A 453 ? 0.7338 0.6089 0.3992 0.2019  -0.0347 0.0129  453 TYR A CE1 
3134  C CE2 . TYR A 453 ? 0.6865 0.5892 0.3835 0.1666  -0.0279 0.0356  453 TYR A CE2 
3135  C CZ  . TYR A 453 ? 0.7075 0.6172 0.3825 0.1929  -0.0266 0.0269  453 TYR A CZ  
3136  O OH  . TYR A 453 ? 0.7061 0.6582 0.3685 0.2111  -0.0170 0.0332  453 TYR A OH  
3137  N N   . PRO A 454 ? 0.7722 0.4496 0.4959 0.1221  -0.0873 -0.0079 454 PRO A N   
3138  C CA  . PRO A 454 ? 0.7396 0.3891 0.4871 0.1009  -0.0924 -0.0031 454 PRO A CA  
3139  C C   . PRO A 454 ? 0.6956 0.3477 0.4620 0.0907  -0.0810 0.0092  454 PRO A C   
3140  O O   . PRO A 454 ? 0.6600 0.3028 0.4488 0.0719  -0.0799 0.0183  454 PRO A O   
3141  C CB  . PRO A 454 ? 0.7527 0.3593 0.4888 0.1089  -0.1108 -0.0182 454 PRO A CB  
3142  C CG  . PRO A 454 ? 0.8080 0.4196 0.5112 0.1350  -0.1170 -0.0327 454 PRO A CG  
3143  C CD  . PRO A 454 ? 0.8133 0.4683 0.5101 0.1448  -0.0993 -0.0249 454 PRO A CD  
3144  N N   . THR A 455 ? 0.6872 0.3523 0.4448 0.1037  -0.0727 0.0098  455 THR A N   
3145  C CA  . THR A 455 ? 0.6675 0.3335 0.4398 0.0970  -0.0631 0.0202  455 THR A CA  
3146  C C   . THR A 455 ? 0.6361 0.3420 0.4175 0.0934  -0.0493 0.0325  455 THR A C   
3147  O O   . THR A 455 ? 0.6220 0.3323 0.4120 0.0920  -0.0417 0.0398  455 THR A O   
3148  C CB  . THR A 455 ? 0.6909 0.3385 0.4489 0.1135  -0.0653 0.0121  455 THR A CB  
3149  O OG1 . THR A 455 ? 0.7068 0.3741 0.4419 0.1350  -0.0647 0.0034  455 THR A OG1 
3150  C CG2 . THR A 455 ? 0.7161 0.3281 0.4754 0.1100  -0.0786 0.0027  455 THR A CG2 
3151  N N   . LEU A 456 ? 0.6526 0.3863 0.4325 0.0920  -0.0469 0.0354  456 LEU A N   
3152  C CA  . LEU A 456 ? 0.6237 0.3953 0.4137 0.0880  -0.0358 0.0481  456 LEU A CA  
3153  C C   . LEU A 456 ? 0.5718 0.3410 0.3849 0.0681  -0.0324 0.0602  456 LEU A C   
3154  O O   . LEU A 456 ? 0.5581 0.3118 0.3800 0.0549  -0.0372 0.0613  456 LEU A O   
3155  C CB  . LEU A 456 ? 0.6427 0.4430 0.4257 0.0907  -0.0347 0.0495  456 LEU A CB  
3156  C CG  . LEU A 456 ? 0.6139 0.4565 0.4063 0.0892  -0.0241 0.0632  456 LEU A CG  
3157  C CD1 . LEU A 456 ? 0.6227 0.4803 0.4093 0.1053  -0.0180 0.0628  456 LEU A CD1 
3158  C CD2 . LEU A 456 ? 0.6257 0.4948 0.4108 0.0916  -0.0230 0.0660  456 LEU A CD2 
3159  N N   . ASN A 457 ? 0.5992 0.3838 0.4217 0.0672  -0.0249 0.0692  457 ASN A N   
3160  C CA  . ASN A 457 ? 0.5568 0.3387 0.3978 0.0523  -0.0222 0.0801  457 ASN A CA  
3161  C C   . ASN A 457 ? 0.5343 0.3494 0.3864 0.0457  -0.0177 0.0918  457 ASN A C   
3162  O O   . ASN A 457 ? 0.5097 0.3309 0.3774 0.0308  -0.0186 0.0978  457 ASN A O   
3163  C CB  . ASN A 457 ? 0.5479 0.3193 0.3961 0.0552  -0.0193 0.0784  457 ASN A CB  
3164  C CG  . ASN A 457 ? 0.5155 0.3095 0.3952 0.0404  -0.0153 0.0840  457 ASN A CG  
3165  O OD1 . ASN A 457 ? 0.5011 0.3140 0.3865 0.0412  -0.0129 0.0898  457 ASN A OD1 
3166  N ND2 . ASN A 457 ? 0.5015 0.2963 0.4030 0.0291  -0.0151 0.0823  457 ASN A ND2 
3167  N N   . PHE A 458 ? 0.5127 0.3546 0.3621 0.0555  -0.0133 0.0942  458 PHE A N   
3168  C CA  . PHE A 458 ? 0.4916 0.3655 0.3547 0.0489  -0.0103 0.1070  458 PHE A CA  
3169  C C   . PHE A 458 ? 0.5180 0.4251 0.3742 0.0597  -0.0064 0.1081  458 PHE A C   
3170  O O   . PHE A 458 ? 0.5443 0.4547 0.3884 0.0761  -0.0040 0.1011  458 PHE A O   
3171  C CB  . PHE A 458 ? 0.4696 0.3442 0.3435 0.0489  -0.0087 0.1129  458 PHE A CB  
3172  C CG  . PHE A 458 ? 0.4447 0.3475 0.3387 0.0369  -0.0102 0.1222  458 PHE A CG  
3173  C CD1 . PHE A 458 ? 0.4476 0.3850 0.3452 0.0423  -0.0064 0.1316  458 PHE A CD1 
3174  C CD2 . PHE A 458 ? 0.4302 0.3215 0.3344 0.0221  -0.0153 0.1170  458 PHE A CD2 
3175  C CE1 . PHE A 458 ? 0.4306 0.3895 0.3483 0.0302  -0.0088 0.1372  458 PHE A CE1 
3176  C CE2 . PHE A 458 ? 0.4164 0.3262 0.3335 0.0160  -0.0150 0.1195  458 PHE A CE2 
3177  C CZ  . PHE A 458 ? 0.4195 0.3621 0.3465 0.0176  -0.0137 0.1306  458 PHE A CZ  
3178  N N   . ILE A 459 ? 0.4788 0.4108 0.3420 0.0515  -0.0057 0.1175  459 ILE A N   
3179  C CA  . ILE A 459 ? 0.4853 0.4538 0.3439 0.0612  -0.0005 0.1223  459 ILE A CA  
3180  C C   . ILE A 459 ? 0.4655 0.4643 0.3444 0.0477  0.0007  0.1399  459 ILE A C   
3181  O O   . ILE A 459 ? 0.4528 0.4418 0.3413 0.0315  -0.0040 0.1440  459 ILE A O   
3182  C CB  . ILE A 459 ? 0.5056 0.4698 0.3435 0.0698  -0.0019 0.1127  459 ILE A CB  
3183  C CG1 . ILE A 459 ? 0.5184 0.5197 0.3463 0.0865  0.0050  0.1160  459 ILE A CG1 
3184  C CG2 . ILE A 459 ? 0.4975 0.4550 0.3395 0.0543  -0.0063 0.1161  459 ILE A CG2 
3185  C CD1 . ILE A 459 ? 0.5454 0.5391 0.3468 0.1016  0.0027  0.1033  459 ILE A CD1 
3186  N N   . ASP A 460 ? 0.5138 0.5489 0.4009 0.0542  0.0063  0.1500  460 ASP A N   
3187  C CA  . ASP A 460 ? 0.4800 0.5436 0.3930 0.0397  0.0062  0.1623  460 ASP A CA  
3188  C C   . ASP A 460 ? 0.4879 0.5950 0.4012 0.0509  0.0146  0.1712  460 ASP A C   
3189  O O   . ASP A 460 ? 0.4973 0.6260 0.4129 0.0633  0.0196  0.1754  460 ASP A O   
3190  C CB  . ASP A 460 ? 0.4619 0.5223 0.3965 0.0316  0.0023  0.1645  460 ASP A CB  
3191  C CG  . ASP A 460 ? 0.4454 0.5249 0.4074 0.0153  -0.0015 0.1724  460 ASP A CG  
3192  O OD1 . ASP A 460 ? 0.4455 0.5402 0.4109 0.0095  -0.0003 0.1766  460 ASP A OD1 
3193  O OD2 . ASP A 460 ? 0.4350 0.5129 0.4143 0.0094  -0.0064 0.1738  460 ASP A OD2 
3194  N N   . LEU A 461 ? 0.4465 0.5668 0.3572 0.0474  0.0162  0.1739  461 LEU A N   
3195  C CA  . LEU A 461 ? 0.4566 0.6186 0.3678 0.0582  0.0249  0.1822  461 LEU A CA  
3196  C C   . LEU A 461 ? 0.4420 0.6334 0.3854 0.0424  0.0248  0.1966  461 LEU A C   
3197  O O   . LEU A 461 ? 0.4498 0.6719 0.3957 0.0469  0.0308  0.2043  461 LEU A O   
3198  C CB  . LEU A 461 ? 0.4769 0.6334 0.3595 0.0698  0.0268  0.1744  461 LEU A CB  
3199  C CG  . LEU A 461 ? 0.4984 0.6180 0.3480 0.0836  0.0227  0.1586  461 LEU A CG  
3200  C CD1 . LEU A 461 ? 0.5174 0.6263 0.3429 0.0895  0.0202  0.1509  461 LEU A CD1 
3201  C CD2 . LEU A 461 ? 0.5270 0.6534 0.3617 0.1070  0.0275  0.1516  461 LEU A CD2 
3202  N N   . SER A 462 ? 0.4389 0.6206 0.4065 0.0256  0.0173  0.1995  462 SER A N   
3203  C CA  . SER A 462 ? 0.4267 0.6285 0.4237 0.0097  0.0133  0.2107  462 SER A CA  
3204  C C   . SER A 462 ? 0.4281 0.6792 0.4465 0.0151  0.0197  0.2279  462 SER A C   
3205  O O   . SER A 462 ? 0.4337 0.7015 0.4489 0.0292  0.0260  0.2307  462 SER A O   
3206  C CB  . SER A 462 ? 0.4100 0.5872 0.4243 -0.0060 0.0020  0.2067  462 SER A CB  
3207  O OG  . SER A 462 ? 0.4090 0.5432 0.4047 -0.0088 -0.0026 0.1911  462 SER A OG  
3208  N N   . ASN A 463 ? 0.4233 0.6985 0.4642 0.0045  0.0175  0.2399  463 ASN A N   
3209  C CA  . ASN A 463 ? 0.4240 0.7485 0.4917 0.0065  0.0215  0.2595  463 ASN A CA  
3210  C C   . ASN A 463 ? 0.4416 0.7971 0.4932 0.0293  0.0358  0.2628  463 ASN A C   
3211  O O   . ASN A 463 ? 0.4438 0.8243 0.5017 0.0409  0.0415  0.2692  463 ASN A O   
3212  C CB  . ASN A 463 ? 0.4112 0.7427 0.5055 -0.0006 0.0146  0.2671  463 ASN A CB  
3213  C CG  . ASN A 463 ? 0.3972 0.6964 0.5041 -0.0197 -0.0006 0.2610  463 ASN A CG  
3214  O OD1 . ASN A 463 ? 0.3950 0.6852 0.5057 -0.0307 -0.0071 0.2597  463 ASN A OD1 
3215  N ND2 . ASN A 463 ? 0.3896 0.6705 0.5008 -0.0217 -0.0064 0.2563  463 ASN A ND2 
3216  N N   . ASN A 464 ? 0.4640 0.8174 0.4934 0.0371  0.0412  0.2575  464 ASN A N   
3217  C CA  . ASN A 464 ? 0.4851 0.8643 0.4945 0.0614  0.0536  0.2575  464 ASN A CA  
3218  C C   . ASN A 464 ? 0.4969 0.8916 0.5032 0.0621  0.0568  0.2632  464 ASN A C   
3219  O O   . ASN A 464 ? 0.4877 0.8765 0.5101 0.0435  0.0497  0.2688  464 ASN A O   
3220  C CB  . ASN A 464 ? 0.4974 0.8437 0.4680 0.0777  0.0556  0.2373  464 ASN A CB  
3221  C CG  . ASN A 464 ? 0.4955 0.8440 0.4657 0.0881  0.0576  0.2350  464 ASN A CG  
3222  O OD1 . ASN A 464 ? 0.5053 0.8898 0.4781 0.1057  0.0662  0.2414  464 ASN A OD1 
3223  N ND2 . ASN A 464 ? 0.4839 0.7941 0.4509 0.0785  0.0495  0.2258  464 ASN A ND2 
3224  N N   . ASN A 465 ? 0.5353 0.9487 0.5192 0.0852  0.0669  0.2608  465 ASN A N   
3225  C CA  . ASN A 465 ? 0.5508 0.9821 0.5293 0.0902  0.0713  0.2667  465 ASN A CA  
3226  C C   . ASN A 465 ? 0.5722 0.9762 0.5078 0.1066  0.0731  0.2479  465 ASN A C   
3227  O O   . ASN A 465 ? 0.5976 1.0224 0.5170 0.1265  0.0806  0.2485  465 ASN A O   
3228  C CB  . ASN A 465 ? 0.5628 1.0497 0.5583 0.1048  0.0810  0.2852  465 ASN A CB  
3229  C CG  . ASN A 465 ? 0.5775 1.0878 0.5842 0.1003  0.0827  0.2995  465 ASN A CG  
3230  O OD1 . ASN A 465 ? 0.5640 1.0594 0.5852 0.0781  0.0744  0.3036  465 ASN A OD1 
3231  N ND2 . ASN A 465 ? 0.6080 1.1544 0.6069 0.1227  0.0930  0.3071  465 ASN A ND2 
3232  N N   . PHE A 466 ? 0.5578 0.9145 0.4746 0.0990  0.0650  0.2312  466 PHE A N   
3233  C CA  . PHE A 466 ? 0.5781 0.9047 0.4558 0.1118  0.0629  0.2136  466 PHE A CA  
3234  C C   . PHE A 466 ? 0.5814 0.9020 0.4569 0.1015  0.0600  0.2163  466 PHE A C   
3235  O O   . PHE A 466 ? 0.5624 0.8709 0.4579 0.0778  0.0533  0.2217  466 PHE A O   
3236  C CB  . PHE A 466 ? 0.5723 0.8516 0.4335 0.1065  0.0538  0.1971  466 PHE A CB  
3237  C CG  . PHE A 466 ? 0.5765 0.8544 0.4286 0.1223  0.0562  0.1899  466 PHE A CG  
3238  C CD1 . PHE A 466 ? 0.6043 0.8864 0.4270 0.1510  0.0604  0.1785  466 PHE A CD1 
3239  C CD2 . PHE A 466 ? 0.5550 0.8251 0.4265 0.1099  0.0531  0.1931  466 PHE A CD2 
3240  C CE1 . PHE A 466 ? 0.6109 0.8892 0.4237 0.1667  0.0616  0.1704  466 PHE A CE1 
3241  C CE2 . PHE A 466 ? 0.5605 0.8280 0.4222 0.1252  0.0551  0.1863  466 PHE A CE2 
3242  C CZ  . PHE A 466 ? 0.5886 0.8600 0.4207 0.1535  0.0594  0.1748  466 PHE A CZ  
3243  N N   . HIS A 467 ? 0.5787 0.9068 0.4291 0.1207  0.0643  0.2117  467 HIS A N   
3244  C CA  . HIS A 467 ? 0.5867 0.9069 0.4287 0.1147  0.0615  0.2124  467 HIS A CA  
3245  C C   . HIS A 467 ? 0.6032 0.8816 0.4071 0.1233  0.0534  0.1915  467 HIS A C   
3246  O O   . HIS A 467 ? 0.6098 0.8662 0.3946 0.1343  0.0497  0.1770  467 HIS A O   
3247  C CB  . HIS A 467 ? 0.6064 0.9696 0.4512 0.1299  0.0718  0.2253  467 HIS A CB  
3248  C CG  . HIS A 467 ? 0.6387 1.0106 0.4521 0.1627  0.0776  0.2148  467 HIS A CG  
3249  N ND1 . HIS A 467 ? 0.6465 1.0483 0.4641 0.1819  0.0856  0.2183  467 HIS A ND1 
3250  C CD2 . HIS A 467 ? 0.6672 1.0214 0.4446 0.1812  0.0751  0.2002  467 HIS A CD2 
3251  C CE1 . HIS A 467 ? 0.6790 1.0798 0.4639 0.2114  0.0878  0.2056  467 HIS A CE1 
3252  N NE2 . HIS A 467 ? 0.6925 1.0641 0.4527 0.2116  0.0811  0.1941  467 HIS A NE2 
3253  N N   . GLY A 468 ? 0.6221 0.8888 0.4157 0.1181  0.0493  0.1902  468 GLY A N   
3254  C CA  . GLY A 468 ? 0.6399 0.8695 0.3990 0.1262  0.0399  0.1716  468 GLY A CA  
3255  C C   . GLY A 468 ? 0.6191 0.8106 0.3829 0.1025  0.0279  0.1667  468 GLY A C   
3256  O O   . GLY A 468 ? 0.5917 0.7833 0.3844 0.0801  0.0268  0.1764  468 GLY A O   
3257  N N   . GLN A 469 ? 0.7059 0.8639 0.4411 0.1094  0.0175  0.1503  469 GLN A N   
3258  C CA  . GLN A 469 ? 0.6885 0.8103 0.4250 0.0906  0.0051  0.1447  469 GLN A CA  
3259  C C   . GLN A 469 ? 0.6880 0.7820 0.4142 0.0956  -0.0021 0.1320  469 GLN A C   
3260  O O   . GLN A 469 ? 0.7092 0.8027 0.4158 0.1178  -0.0010 0.1216  469 GLN A O   
3261  C CB  . GLN A 469 ? 0.7126 0.8164 0.4275 0.0931  -0.0037 0.1367  469 GLN A CB  
3262  C CG  . GLN A 469 ? 0.7488 0.8391 0.4278 0.1202  -0.0094 0.1184  469 GLN A CG  
3263  C CD  . GLN A 469 ? 0.7608 0.8170 0.4210 0.1186  -0.0249 0.1051  469 GLN A CD  
3264  O OE1 . GLN A 469 ? 0.7737 0.8341 0.4242 0.1216  -0.0263 0.1052  469 GLN A OE1 
3265  N NE2 . GLN A 469 ? 0.7563 0.7777 0.4120 0.1144  -0.0374 0.0936  469 GLN A NE2 
3266  N N   . LEU A 470 ? 0.6502 0.7195 0.3895 0.0759  -0.0099 0.1326  470 LEU A N   
3267  C CA  . LEU A 470 ? 0.6576 0.6999 0.3910 0.0789  -0.0162 0.1234  470 LEU A CA  
3268  C C   . LEU A 470 ? 0.6974 0.7043 0.4044 0.0925  -0.0287 0.1009  470 LEU A C   
3269  O O   . LEU A 470 ? 0.7046 0.6945 0.4057 0.0868  -0.0378 0.0952  470 LEU A O   
3270  C CB  . LEU A 470 ? 0.6278 0.6534 0.3885 0.0531  -0.0205 0.1296  470 LEU A CB  
3271  C CG  . LEU A 470 ? 0.5912 0.6381 0.3841 0.0383  -0.0121 0.1433  470 LEU A CG  
3272  C CD1 . LEU A 470 ? 0.5664 0.5904 0.3818 0.0165  -0.0181 0.1443  470 LEU A CD1 
3273  C CD2 . LEU A 470 ? 0.5958 0.6566 0.3884 0.0518  -0.0049 0.1434  470 LEU A CD2 
3274  N N   . SER A 471 ? 0.6741 0.6686 0.3675 0.1099  -0.0304 0.0871  471 SER A N   
3275  C CA  . SER A 471 ? 0.7121 0.6684 0.3846 0.1215  -0.0449 0.0642  471 SER A CA  
3276  C C   . SER A 471 ? 0.7035 0.6216 0.3965 0.1002  -0.0557 0.0569  471 SER A C   
3277  O O   . SER A 471 ? 0.6865 0.6038 0.4044 0.0840  -0.0511 0.0651  471 SER A O   
3278  C CB  . SER A 471 ? 0.7306 0.6833 0.3827 0.1465  -0.0448 0.0521  471 SER A CB  
3279  O OG  . SER A 471 ? 0.7646 0.6741 0.4011 0.1546  -0.0616 0.0299  471 SER A OG  
3280  N N   . ALA A 472 ? 0.6950 0.5819 0.3775 0.1013  -0.0706 0.0419  472 ALA A N   
3281  C CA  . ALA A 472 ? 0.6840 0.5355 0.3863 0.0831  -0.0812 0.0351  472 ALA A CA  
3282  C C   . ALA A 472 ? 0.6947 0.5206 0.3974 0.0892  -0.0858 0.0240  472 ALA A C   
3283  O O   . ALA A 472 ? 0.6889 0.4851 0.4083 0.0756  -0.0944 0.0191  472 ALA A O   
3284  C CB  . ALA A 472 ? 0.7011 0.5288 0.3954 0.0814  -0.0969 0.0235  472 ALA A CB  
3285  N N   . ASN A 473 ? 0.7298 0.5675 0.4150 0.1097  -0.0802 0.0209  473 ASN A N   
3286  C CA  . ASN A 473 ? 0.7519 0.5661 0.4362 0.1167  -0.0842 0.0110  473 ASN A CA  
3287  C C   . ASN A 473 ? 0.7273 0.5397 0.4413 0.0971  -0.0766 0.0218  473 ASN A C   
3288  O O   . ASN A 473 ? 0.7461 0.5300 0.4655 0.0957  -0.0826 0.0144  473 ASN A O   
3289  C CB  . ASN A 473 ? 0.7647 0.5976 0.4239 0.1438  -0.0779 0.0072  473 ASN A CB  
3290  C CG  . ASN A 473 ? 0.7959 0.6180 0.4201 0.1688  -0.0896 -0.0092 473 ASN A CG  
3291  O OD1 . ASN A 473 ? 0.8107 0.6055 0.4300 0.1655  -0.1048 -0.0199 473 ASN A OD1 
3292  N ND2 . ASN A 473 ? 0.8111 0.6548 0.4105 0.1953  -0.0832 -0.0115 473 ASN A ND2 
3293  N N   . TRP A 474 ? 0.7237 0.5646 0.4560 0.0829  -0.0646 0.0393  474 TRP A N   
3294  C CA  . TRP A 474 ? 0.6975 0.5375 0.4552 0.0670  -0.0580 0.0494  474 TRP A CA  
3295  C C   . TRP A 474 ? 0.6916 0.4976 0.4662 0.0504  -0.0670 0.0455  474 TRP A C   
3296  O O   . TRP A 474 ? 0.6694 0.4642 0.4591 0.0429  -0.0641 0.0489  474 TRP A O   
3297  C CB  . TRP A 474 ? 0.6539 0.5278 0.4272 0.0548  -0.0472 0.0681  474 TRP A CB  
3298  C CG  . TRP A 474 ? 0.6540 0.5657 0.4179 0.0686  -0.0365 0.0763  474 TRP A CG  
3299  C CD1 . TRP A 474 ? 0.6571 0.5983 0.4127 0.0731  -0.0320 0.0845  474 TRP A CD1 
3300  C CD2 . TRP A 474 ? 0.6582 0.5840 0.4213 0.0803  -0.0287 0.0783  474 TRP A CD2 
3301  N NE1 . TRP A 474 ? 0.6506 0.6256 0.4020 0.0865  -0.0212 0.0927  474 TRP A NE1 
3302  C CE2 . TRP A 474 ? 0.6550 0.6213 0.4110 0.0911  -0.0193 0.0885  474 TRP A CE2 
3303  C CE3 . TRP A 474 ? 0.6636 0.5724 0.4314 0.0829  -0.0286 0.0731  474 TRP A CE3 
3304  C CZ2 . TRP A 474 ? 0.6550 0.6466 0.4102 0.1043  -0.0101 0.0936  474 TRP A CZ2 
3305  C CZ3 . TRP A 474 ? 0.6658 0.5974 0.4308 0.0962  -0.0201 0.0768  474 TRP A CZ3 
3306  C CH2 . TRP A 474 ? 0.6600 0.6334 0.4195 0.1067  -0.0110 0.0869  474 TRP A CH2 
3307  N N   . GLU A 475 ? 0.7422 0.5326 0.5149 0.0451  -0.0777 0.0391  475 GLU A N   
3308  C CA  . GLU A 475 ? 0.7298 0.4911 0.5213 0.0293  -0.0862 0.0369  475 GLU A CA  
3309  C C   . GLU A 475 ? 0.7543 0.4846 0.5451 0.0349  -0.0931 0.0270  475 GLU A C   
3310  O O   . GLU A 475 ? 0.7252 0.4380 0.5363 0.0219  -0.0939 0.0309  475 GLU A O   
3311  C CB  . GLU A 475 ? 0.7458 0.4971 0.5344 0.0249  -0.0980 0.0307  475 GLU A CB  
3312  C CG  . GLU A 475 ? 0.7206 0.4470 0.5322 0.0075  -0.1064 0.0306  475 GLU A CG  
3313  C CD  . GLU A 475 ? 0.7650 0.4652 0.5698 0.0110  -0.1244 0.0162  475 GLU A CD  
3314  O OE1 . GLU A 475 ? 0.8088 0.5121 0.5889 0.0263  -0.1304 0.0065  475 GLU A OE1 
3315  O OE2 . GLU A 475 ? 0.7477 0.4244 0.5721 -0.0009 -0.1329 0.0150  475 GLU A OE2 
3316  N N   . GLN A 476 ? 0.7424 0.4659 0.5095 0.0552  -0.0980 0.0147  476 GLN A N   
3317  C CA  . GLN A 476 ? 0.7516 0.4432 0.5160 0.0616  -0.1064 0.0047  476 GLN A CA  
3318  C C   . GLN A 476 ? 0.7221 0.4182 0.4962 0.0604  -0.0948 0.0128  476 GLN A C   
3319  O O   . GLN A 476 ? 0.7217 0.3903 0.4995 0.0610  -0.1003 0.0081  476 GLN A O   
3320  C CB  . GLN A 476 ? 0.8025 0.4844 0.5355 0.0861  -0.1164 -0.0117 476 GLN A CB  
3321  C CG  . GLN A 476 ? 0.8310 0.5015 0.5515 0.0901  -0.1313 -0.0225 476 GLN A CG  
3322  C CD  . GLN A 476 ? 0.8806 0.5379 0.5669 0.1172  -0.1431 -0.0401 476 GLN A CD  
3323  O OE1 . GLN A 476 ? 0.9000 0.5416 0.5764 0.1297  -0.1462 -0.0475 476 GLN A OE1 
3324  N NE2 . GLN A 476 ? 0.8847 0.5478 0.5511 0.1280  -0.1502 -0.0473 476 GLN A NE2 
3325  N N   . SER A 477 ? 0.7314 0.4607 0.5101 0.0587  -0.0799 0.0251  477 SER A N   
3326  C CA  . SER A 477 ? 0.7073 0.4414 0.4974 0.0559  -0.0696 0.0336  477 SER A CA  
3327  C C   . SER A 477 ? 0.6555 0.3790 0.4716 0.0350  -0.0681 0.0435  477 SER A C   
3328  O O   . SER A 477 ? 0.6181 0.3613 0.4476 0.0250  -0.0591 0.0560  477 SER A O   
3329  C CB  . SER A 477 ? 0.7009 0.4740 0.4880 0.0619  -0.0567 0.0430  477 SER A CB  
3330  O OG  . SER A 477 ? 0.7414 0.5257 0.5048 0.0837  -0.0564 0.0349  477 SER A OG  
3331  N N   . GLN A 478 ? 0.7096 0.4010 0.5330 0.0291  -0.0780 0.0381  478 GLN A N   
3332  C CA  . GLN A 478 ? 0.6772 0.3624 0.5267 0.0104  -0.0766 0.0469  478 GLN A CA  
3333  C C   . GLN A 478 ? 0.6510 0.3587 0.5212 0.0062  -0.0613 0.0544  478 GLN A C   
3334  O O   . GLN A 478 ? 0.6183 0.3489 0.5163 -0.0052 -0.0523 0.0594  478 GLN A O   
3335  C CB  . GLN A 478 ? 0.6847 0.3559 0.5484 0.0054  -0.0854 0.0375  478 GLN A CB  
3336  C CG  . GLN A 478 ? 0.7000 0.3599 0.5579 0.0027  -0.0992 0.0312  478 GLN A CG  
3337  C CD  . GLN A 478 ? 0.6764 0.3616 0.5579 -0.0132 -0.0930 0.0393  478 GLN A CD  
3338  O OE1 . GLN A 478 ? 0.6628 0.3639 0.5730 -0.0230 -0.0861 0.0421  478 GLN A OE1 
3339  N NE2 . GLN A 478 ? 0.6688 0.3585 0.5359 -0.0133 -0.0945 0.0436  478 GLN A NE2 
3340  N N   . LYS A 479 ? 0.6545 0.3566 0.5101 0.0184  -0.0583 0.0542  479 LYS A N   
3341  C CA  . LYS A 479 ? 0.6240 0.3458 0.4974 0.0162  -0.0456 0.0604  479 LYS A CA  
3342  C C   . LYS A 479 ? 0.6113 0.3556 0.4810 0.0175  -0.0386 0.0697  479 LYS A C   
3343  O O   . LYS A 479 ? 0.5883 0.3487 0.4713 0.0175  -0.0302 0.0738  479 LYS A O   
3344  C CB  . LYS A 479 ? 0.6431 0.3479 0.5066 0.0279  -0.0466 0.0543  479 LYS A CB  
3345  C CG  . LYS A 479 ? 0.6638 0.3507 0.5359 0.0252  -0.0532 0.0466  479 LYS A CG  
3346  C CD  . LYS A 479 ? 0.6391 0.3437 0.5452 0.0103  -0.0456 0.0524  479 LYS A CD  
3347  C CE  . LYS A 479 ? 0.6557 0.3451 0.5718 0.0081  -0.0496 0.0480  479 LYS A CE  
3348  N NZ  . LYS A 479 ? 0.6584 0.3422 0.5751 0.0148  -0.0452 0.0481  479 LYS A NZ  
3349  N N   . LEU A 480 ? 0.5895 0.3376 0.4427 0.0185  -0.0423 0.0736  480 LEU A N   
3350  C CA  . LEU A 480 ? 0.5621 0.3403 0.4174 0.0178  -0.0353 0.0834  480 LEU A CA  
3351  C C   . LEU A 480 ? 0.5251 0.3282 0.4131 0.0036  -0.0287 0.0881  480 LEU A C   
3352  O O   . LEU A 480 ? 0.5161 0.3212 0.4165 -0.0052 -0.0297 0.0854  480 LEU A O   
3353  C CB  . LEU A 480 ? 0.5791 0.3807 0.4243 0.0218  -0.0363 0.0819  480 LEU A CB  
3354  C CG  . LEU A 480 ? 0.5712 0.4084 0.4189 0.0237  -0.0289 0.0921  480 LEU A CG  
3355  C CD1 . LEU A 480 ? 0.5897 0.4360 0.4307 0.0384  -0.0237 0.0903  480 LEU A CD1 
3356  C CD2 . LEU A 480 ? 0.5897 0.4491 0.4290 0.0256  -0.0295 0.0933  480 LEU A CD2 
3357  N N   . VAL A 481 ? 0.5444 0.3674 0.4450 0.0047  -0.0215 0.0931  481 VAL A N   
3358  C CA  . VAL A 481 ? 0.5181 0.3620 0.4416 -0.0012 -0.0138 0.0936  481 VAL A CA  
3359  C C   . VAL A 481 ? 0.5096 0.3726 0.4312 -0.0018 -0.0118 0.0990  481 VAL A C   
3360  O O   . VAL A 481 ? 0.4921 0.3643 0.4225 -0.0067 -0.0095 0.0953  481 VAL A O   
3361  C CB  . VAL A 481 ? 0.5020 0.3475 0.4401 0.0026  -0.0069 0.0912  481 VAL A CB  
3362  C CG1 . VAL A 481 ? 0.5092 0.3394 0.4527 0.0018  -0.0076 0.0861  481 VAL A CG1 
3363  C CG2 . VAL A 481 ? 0.5055 0.3541 0.4402 0.0092  -0.0079 0.0958  481 VAL A CG2 
3364  N N   . ALA A 482 ? 0.4878 0.3566 0.3962 0.0034  -0.0138 0.1066  482 ALA A N   
3365  C CA  . ALA A 482 ? 0.4819 0.3698 0.3896 0.0008  -0.0134 0.1111  482 ALA A CA  
3366  C C   . ALA A 482 ? 0.5035 0.4048 0.3969 0.0034  -0.0164 0.1201  482 ALA A C   
3367  O O   . ALA A 482 ? 0.5112 0.4169 0.3924 0.0143  -0.0163 0.1257  482 ALA A O   
3368  C CB  . ALA A 482 ? 0.4758 0.3670 0.3857 0.0044  -0.0121 0.1114  482 ALA A CB  
3369  N N   . PHE A 483 ? 0.4791 0.3928 0.3755 -0.0035 -0.0177 0.1216  483 PHE A N   
3370  C CA  . PHE A 483 ? 0.4851 0.4213 0.3706 0.0002  -0.0177 0.1301  483 PHE A CA  
3371  C C   . PHE A 483 ? 0.4747 0.4383 0.3786 -0.0069 -0.0153 0.1347  483 PHE A C   
3372  O O   . PHE A 483 ? 0.4648 0.4284 0.3809 -0.0167 -0.0174 0.1314  483 PHE A O   
3373  C CB  . PHE A 483 ? 0.4967 0.4232 0.3696 -0.0017 -0.0225 0.1284  483 PHE A CB  
3374  C CG  . PHE A 483 ? 0.5298 0.4773 0.3858 0.0100  -0.0202 0.1293  483 PHE A CG  
3375  C CD1 . PHE A 483 ? 0.5542 0.5236 0.4042 0.0246  -0.0134 0.1305  483 PHE A CD1 
3376  C CD2 . PHE A 483 ? 0.5483 0.4942 0.3943 0.0085  -0.0240 0.1262  483 PHE A CD2 
3377  C CE1 . PHE A 483 ? 0.5789 0.5694 0.4124 0.0387  -0.0097 0.1293  483 PHE A CE1 
3378  C CE2 . PHE A 483 ? 0.5824 0.5474 0.4110 0.0224  -0.0210 0.1244  483 PHE A CE2 
3379  C CZ  . PHE A 483 ? 0.5899 0.5778 0.4117 0.0381  -0.0135 0.1263  483 PHE A CZ  
3380  N N   . ILE A 484 ? 0.4414 0.4304 0.3495 -0.0011 -0.0114 0.1426  484 ILE A N   
3381  C CA  . ILE A 484 ? 0.4287 0.4440 0.3591 -0.0084 -0.0108 0.1493  484 ILE A CA  
3382  C C   . ILE A 484 ? 0.4351 0.4858 0.3631 -0.0008 -0.0047 0.1601  484 ILE A C   
3383  O O   . ILE A 484 ? 0.4438 0.5098 0.3658 0.0121  0.0006  0.1641  484 ILE A O   
3384  C CB  . ILE A 484 ? 0.4135 0.4282 0.3584 -0.0093 -0.0122 0.1494  484 ILE A CB  
3385  C CG1 . ILE A 484 ? 0.4114 0.3923 0.3541 -0.0121 -0.0158 0.1370  484 ILE A CG1 
3386  C CG2 . ILE A 484 ? 0.4058 0.4456 0.3758 -0.0182 -0.0149 0.1571  484 ILE A CG2 
3387  C CD1 . ILE A 484 ? 0.4014 0.3799 0.3560 -0.0123 -0.0181 0.1353  484 ILE A CD1 
3388  N N   . LEU A 485 ? 0.4316 0.4971 0.3640 -0.0066 -0.0046 0.1643  485 LEU A N   
3389  C CA  . LEU A 485 ? 0.4421 0.5422 0.3712 0.0020  0.0024  0.1738  485 LEU A CA  
3390  C C   . LEU A 485 ? 0.4324 0.5570 0.3866 -0.0096 0.0013  0.1838  485 LEU A C   
3391  O O   . LEU A 485 ? 0.4411 0.5793 0.3919 -0.0095 0.0035  0.1879  485 LEU A O   
3392  C CB  . LEU A 485 ? 0.4609 0.5523 0.3613 0.0117  0.0038  0.1684  485 LEU A CB  
3393  C CG  . LEU A 485 ? 0.4822 0.6011 0.3650 0.0321  0.0124  0.1713  485 LEU A CG  
3394  C CD1 . LEU A 485 ? 0.5031 0.6032 0.3526 0.0444  0.0099  0.1609  485 LEU A CD1 
3395  C CD2 . LEU A 485 ? 0.4850 0.6452 0.3842 0.0321  0.0192  0.1843  485 LEU A CD2 
3396  N N   . SER A 486 ? 0.4340 0.5628 0.4133 -0.0193 -0.0036 0.1874  486 SER A N   
3397  C CA  . SER A 486 ? 0.4308 0.5791 0.4346 -0.0310 -0.0081 0.1963  486 SER A CA  
3398  C C   . SER A 486 ? 0.4364 0.6297 0.4549 -0.0262 -0.0016 0.2135  486 SER A C   
3399  O O   . SER A 486 ? 0.4380 0.6492 0.4526 -0.0140 0.0060  0.2181  486 SER A O   
3400  C CB  . SER A 486 ? 0.4123 0.5481 0.4361 -0.0418 -0.0182 0.1932  486 SER A CB  
3401  O OG  . SER A 486 ? 0.4102 0.5575 0.4450 -0.0382 -0.0174 0.1987  486 SER A OG  
3402  N N   . ASN A 487 ? 0.4812 0.6939 0.5168 -0.0346 -0.0047 0.2232  487 ASN A N   
3403  C CA  . ASN A 487 ? 0.4823 0.7402 0.5384 -0.0325 -0.0003 0.2421  487 ASN A CA  
3404  C C   . ASN A 487 ? 0.5013 0.7829 0.5390 -0.0142 0.0137  0.2460  487 ASN A C   
3405  O O   . ASN A 487 ? 0.5036 0.8148 0.5488 -0.0039 0.0207  0.2551  487 ASN A O   
3406  C CB  . ASN A 487 ? 0.4719 0.7465 0.5555 -0.0369 -0.0053 0.2516  487 ASN A CB  
3407  C CG  . ASN A 487 ? 0.4740 0.7920 0.5876 -0.0411 -0.0068 0.2730  487 ASN A CG  
3408  O OD1 . ASN A 487 ? 0.4781 0.8039 0.5981 -0.0476 -0.0100 0.2791  487 ASN A OD1 
3409  N ND2 . ASN A 487 ? 0.4725 0.8191 0.6048 -0.0368 -0.0048 0.2854  487 ASN A ND2 
3410  N N   . ASN A 488 ? 0.4723 0.7409 0.4847 -0.0087 0.0173  0.2384  488 ASN A N   
3411  C CA  . ASN A 488 ? 0.4929 0.7834 0.4848 0.0108  0.0291  0.2406  488 ASN A CA  
3412  C C   . ASN A 488 ? 0.5046 0.8060 0.4921 0.0101  0.0310  0.2460  488 ASN A C   
3413  O O   . ASN A 488 ? 0.4957 0.7913 0.4994 -0.0059 0.0233  0.2499  488 ASN A O   
3414  C CB  . ASN A 488 ? 0.5052 0.7664 0.4621 0.0242  0.0313  0.2237  488 ASN A CB  
3415  C CG  . ASN A 488 ? 0.5037 0.7733 0.4588 0.0367  0.0359  0.2225  488 ASN A CG  
3416  O OD1 . ASN A 488 ? 0.5199 0.8152 0.4638 0.0565  0.0453  0.2247  488 ASN A OD1 
3417  N ND2 . ASN A 488 ? 0.4875 0.7353 0.4528 0.0267  0.0292  0.2183  488 ASN A ND2 
3418  N N   . SER A 489 ? 0.5052 0.8218 0.4698 0.0290  0.0405  0.2454  489 SER A N   
3419  C CA  . SER A 489 ? 0.5204 0.8489 0.4775 0.0318  0.0435  0.2508  489 SER A CA  
3420  C C   . SER A 489 ? 0.5350 0.8302 0.4545 0.0396  0.0418  0.2342  489 SER A C   
3421  O O   . SER A 489 ? 0.5573 0.8640 0.4569 0.0543  0.0475  0.2342  489 SER A O   
3422  C CB  . SER A 489 ? 0.5378 0.9145 0.4996 0.0494  0.0552  0.2650  489 SER A CB  
3423  O OG  . SER A 489 ? 0.5257 0.9341 0.5215 0.0443  0.0561  0.2805  489 SER A OG  
3424  N N   . ILE A 490 ? 0.5279 0.7821 0.4377 0.0306  0.0330  0.2202  490 ILE A N   
3425  C CA  . ILE A 490 ? 0.5418 0.7634 0.4174 0.0375  0.0289  0.2049  490 ILE A CA  
3426  C C   . ILE A 490 ? 0.5417 0.7502 0.4166 0.0255  0.0233  0.2054  490 ILE A C   
3427  O O   . ILE A 490 ? 0.5226 0.7224 0.4201 0.0067  0.0171  0.2087  490 ILE A O   
3428  C CB  . ILE A 490 ? 0.5321 0.7174 0.3986 0.0342  0.0217  0.1916  490 ILE A CB  
3429  C CG1 . ILE A 490 ? 0.5480 0.7398 0.3966 0.0553  0.0271  0.1856  490 ILE A CG1 
3430  C CG2 . ILE A 490 ? 0.5364 0.6843 0.3820 0.0297  0.0124  0.1795  490 ILE A CG2 
3431  C CD1 . ILE A 490 ? 0.5358 0.7044 0.3870 0.0513  0.0226  0.1788  490 ILE A CD1 
3432  N N   . THR A 491 ? 0.5232 0.7299 0.3709 0.0384  0.0248  0.2010  491 THR A N   
3433  C CA  . THR A 491 ? 0.5289 0.7233 0.3692 0.0314  0.0200  0.2004  491 THR A CA  
3434  C C   . THR A 491 ? 0.5365 0.6914 0.3481 0.0338  0.0103  0.1838  491 THR A C   
3435  O O   . THR A 491 ? 0.5360 0.6728 0.3362 0.0391  0.0067  0.1736  491 THR A O   
3436  C CB  . THR A 491 ? 0.5525 0.7779 0.3842 0.0453  0.0285  0.2095  491 THR A CB  
3437  O OG1 . THR A 491 ? 0.5792 0.8013 0.3766 0.0690  0.0306  0.1982  491 THR A OG1 
3438  C CG2 . THR A 491 ? 0.5478 0.8168 0.4077 0.0468  0.0383  0.2268  491 THR A CG2 
3439  N N   . GLY A 492 ? 0.5117 0.6536 0.3124 0.0299  0.0051  0.1817  492 GLY A N   
3440  C CA  . GLY A 492 ? 0.5206 0.6280 0.2958 0.0322  -0.0058 0.1674  492 GLY A CA  
3441  C C   . GLY A 492 ? 0.4959 0.5743 0.2859 0.0140  -0.0148 0.1627  492 GLY A C   
3442  O O   . GLY A 492 ? 0.4722 0.5553 0.2918 -0.0004 -0.0131 0.1688  492 GLY A O   
3443  N N   . ALA A 493 ? 0.5064 0.5558 0.2765 0.0163  -0.0253 0.1509  493 ALA A N   
3444  C CA  . ALA A 493 ? 0.4850 0.5087 0.2694 0.0019  -0.0334 0.1459  493 ALA A CA  
3445  C C   . ALA A 493 ? 0.4787 0.4875 0.2627 0.0031  -0.0368 0.1400  493 ALA A C   
3446  O O   . ALA A 493 ? 0.4944 0.5086 0.2610 0.0175  -0.0351 0.1375  493 ALA A O   
3447  C CB  . ALA A 493 ? 0.4948 0.4992 0.2637 0.0018  -0.0439 0.1387  493 ALA A CB  
3448  N N   . ILE A 494 ? 0.5123 0.5041 0.3180 -0.0111 -0.0411 0.1369  494 ILE A N   
3449  C CA  . ILE A 494 ? 0.5055 0.4794 0.3146 -0.0131 -0.0449 0.1319  494 ILE A CA  
3450  C C   . ILE A 494 ? 0.5261 0.4714 0.3113 -0.0096 -0.0589 0.1211  494 ILE A C   
3451  O O   . ILE A 494 ? 0.5249 0.4559 0.3124 -0.0174 -0.0670 0.1162  494 ILE A O   
3452  C CB  . ILE A 494 ? 0.4751 0.4410 0.3174 -0.0288 -0.0440 0.1301  494 ILE A CB  
3453  C CG1 . ILE A 494 ? 0.4594 0.4478 0.3235 -0.0331 -0.0356 0.1371  494 ILE A CG1 
3454  C CG2 . ILE A 494 ? 0.4710 0.4174 0.3161 -0.0296 -0.0466 0.1250  494 ILE A CG2 
3455  C CD1 . ILE A 494 ? 0.4341 0.4167 0.3247 -0.0425 -0.0357 0.1330  494 ILE A CD1 
3456  N N   . PRO A 495 ? 0.5735 0.5088 0.3464 0.0058  -0.0592 0.1080  495 PRO A N   
3457  C CA  . PRO A 495 ? 0.5982 0.5020 0.3597 0.0120  -0.0712 0.0885  495 PRO A CA  
3458  C C   . PRO A 495 ? 0.5790 0.4568 0.3620 -0.0061 -0.0789 0.0853  495 PRO A C   
3459  O O   . PRO A 495 ? 0.5599 0.4356 0.3621 -0.0163 -0.0744 0.0915  495 PRO A O   
3460  C CB  . PRO A 495 ? 0.6347 0.5319 0.3846 0.0291  -0.0696 0.0780  495 PRO A CB  
3461  C CG  . PRO A 495 ? 0.6278 0.5606 0.3745 0.0376  -0.0558 0.0914  495 PRO A CG  
3462  C CD  . PRO A 495 ? 0.5833 0.5343 0.3532 0.0181  -0.0498 0.1103  495 PRO A CD  
3463  N N   . PRO A 496 ? 0.5911 0.4498 0.3715 -0.0097 -0.0905 0.0761  496 PRO A N   
3464  C CA  . PRO A 496 ? 0.5752 0.4125 0.3780 -0.0263 -0.0971 0.0744  496 PRO A CA  
3465  C C   . PRO A 496 ? 0.5756 0.3920 0.3891 -0.0263 -0.0984 0.0674  496 PRO A C   
3466  O O   . PRO A 496 ? 0.5573 0.3637 0.3923 -0.0398 -0.0984 0.0716  496 PRO A O   
3467  C CB  . PRO A 496 ? 0.5916 0.4140 0.3866 -0.0260 -0.1104 0.0640  496 PRO A CB  
3468  C CG  . PRO A 496 ? 0.6091 0.4504 0.3788 -0.0126 -0.1086 0.0651  496 PRO A CG  
3469  C CD  . PRO A 496 ? 0.6172 0.4739 0.3746 0.0022  -0.0985 0.0671  496 PRO A CD  
3470  N N   . GLU A 497 ? 0.6339 0.4437 0.4319 -0.0105 -0.0993 0.0574  497 GLU A N   
3471  C CA  . GLU A 497 ? 0.6466 0.4350 0.4530 -0.0096 -0.1011 0.0510  497 GLU A CA  
3472  C C   . GLU A 497 ? 0.6130 0.4126 0.4341 -0.0156 -0.0887 0.0628  497 GLU A C   
3473  O O   . GLU A 497 ? 0.6106 0.3923 0.4439 -0.0192 -0.0892 0.0609  497 GLU A O   
3474  C CB  . GLU A 497 ? 0.6966 0.4754 0.4794 0.0110  -0.1062 0.0371  497 GLU A CB  
3475  C CG  . GLU A 497 ? 0.7298 0.4908 0.4963 0.0194  -0.1220 0.0224  497 GLU A CG  
3476  C CD  . GLU A 497 ? 0.7283 0.5120 0.4733 0.0292  -0.1199 0.0244  497 GLU A CD  
3477  O OE1 . GLU A 497 ? 0.7084 0.5228 0.4499 0.0314  -0.1058 0.0372  497 GLU A OE1 
3478  O OE2 . GLU A 497 ? 0.7493 0.5202 0.4815 0.0347  -0.1328 0.0137  497 GLU A OE2 
3479  N N   . ILE A 498 ? 0.5799 0.4079 0.4005 -0.0166 -0.0785 0.0755  498 ILE A N   
3480  C CA  . ILE A 498 ? 0.5588 0.3968 0.3934 -0.0220 -0.0688 0.0864  498 ILE A CA  
3481  C C   . ILE A 498 ? 0.5391 0.3629 0.3956 -0.0380 -0.0706 0.0912  498 ILE A C   
3482  O O   . ILE A 498 ? 0.5255 0.3495 0.3976 -0.0388 -0.0639 0.0908  498 ILE A O   
3483  C CB  . ILE A 498 ? 0.5477 0.4189 0.3807 -0.0219 -0.0603 0.1002  498 ILE A CB  
3484  C CG1 . ILE A 498 ? 0.5685 0.4574 0.3801 -0.0036 -0.0564 0.0970  498 ILE A CG1 
3485  C CG2 . ILE A 498 ? 0.5262 0.4069 0.3763 -0.0278 -0.0525 0.1104  498 ILE A CG2 
3486  C CD1 . ILE A 498 ? 0.5770 0.4643 0.3835 0.0092  -0.0517 0.0920  498 ILE A CD1 
3487  N N   . TRP A 499 ? 0.3615 0.3580 0.5879 -0.0235 -0.0022 -0.0908 499 TRP A N   
3488  C CA  . TRP A 499 ? 0.3807 0.3827 0.6195 -0.0219 0.0081  -0.0785 499 TRP A CA  
3489  C C   . TRP A 499 ? 0.3677 0.3829 0.6812 -0.0294 0.0224  -0.0773 499 TRP A C   
3490  O O   . TRP A 499 ? 0.3868 0.4041 0.7116 -0.0295 0.0405  -0.0575 499 TRP A O   
3491  C CB  . TRP A 499 ? 0.3946 0.4054 0.6135 -0.0104 -0.0065 -0.0926 499 TRP A CB  
3492  C CG  . TRP A 499 ? 0.3974 0.3940 0.5521 -0.0033 -0.0217 -0.0967 499 TRP A CG  
3493  C CD1 . TRP A 499 ? 0.3932 0.3954 0.5324 0.0064  -0.0408 -0.1178 499 TRP A CD1 
3494  C CD2 . TRP A 499 ? 0.4114 0.3856 0.5110 -0.0051 -0.0185 -0.0779 499 TRP A CD2 
3495  N NE1 . TRP A 499 ? 0.4069 0.3898 0.4831 0.0106  -0.0457 -0.1095 499 TRP A NE1 
3496  C CE2 . TRP A 499 ? 0.4168 0.3831 0.4731 0.0019  -0.0325 -0.0860 499 TRP A CE2 
3497  C CE3 . TRP A 499 ? 0.4279 0.3883 0.5118 -0.0113 -0.0062 -0.0553 499 TRP A CE3 
3498  C CZ2 . TRP A 499 ? 0.4342 0.3796 0.4407 -0.0001 -0.0321 -0.0710 499 TRP A CZ2 
3499  C CZ3 . TRP A 499 ? 0.4408 0.3822 0.4758 -0.0128 -0.0105 -0.0447 499 TRP A CZ3 
3500  C CH2 . TRP A 499 ? 0.4422 0.3763 0.4431 -0.0088 -0.0221 -0.0520 499 TRP A CH2 
3501  N N   . ASN A 500 ? 0.4570 0.4796 0.8216 -0.0353 0.0158  -0.0975 500 ASN A N   
3502  C CA  . ASN A 500 ? 0.4373 0.4665 0.8754 -0.0438 0.0306  -0.0934 500 ASN A CA  
3503  C C   . ASN A 500 ? 0.4434 0.4531 0.8739 -0.0467 0.0501  -0.0642 500 ASN A C   
3504  O O   . ASN A 500 ? 0.4574 0.4649 0.9263 -0.0468 0.0619  -0.0556 500 ASN A O   
3505  C CB  . ASN A 500 ? 0.4493 0.4869 0.9205 -0.0392 0.0142  -0.1227 500 ASN A CB  
3506  C CG  . ASN A 500 ? 0.4559 0.5145 0.9680 -0.0356 0.0055  -0.1412 500 ASN A CG  
3507  O OD1 . ASN A 500 ? 0.4509 0.5197 0.9757 -0.0373 0.0166  -0.1287 500 ASN A OD1 
3508  N ND2 . ASN A 500 ? 0.4703 0.5377 1.0040 -0.0290 -0.0142 -0.1709 500 ASN A ND2 
3509  N N   . MET A 501 ? 0.3834 0.3779 0.7651 -0.0478 0.0516  -0.0494 501 MET A N   
3510  C CA  . MET A 501 ? 0.3901 0.3688 0.7583 -0.0473 0.0670  -0.0204 501 MET A CA  
3511  C C   . MET A 501 ? 0.4182 0.3940 0.7682 -0.0448 0.0854  0.0075  501 MET A C   
3512  O O   . MET A 501 ? 0.4516 0.4182 0.7390 -0.0377 0.0822  0.0197  501 MET A O   
3513  C CB  . MET A 501 ? 0.3943 0.3602 0.7208 -0.0474 0.0576  -0.0195 501 MET A CB  
3514  C CG  . MET A 501 ? 0.3866 0.3575 0.7171 -0.0465 0.0408  -0.0485 501 MET A CG  
3515  S SD  . MET A 501 ? 0.3966 0.3577 0.6828 -0.0448 0.0354  -0.0433 501 MET A SD  
3516  C CE  . MET A 501 ? 0.4024 0.3504 0.6853 -0.0455 0.0506  -0.0066 501 MET A CE  
3517  N N   . THR A 502 ? 0.3902 0.3751 0.7812 -0.0440 0.1016  0.0159  502 THR A N   
3518  C CA  . THR A 502 ? 0.4127 0.4004 0.7907 -0.0391 0.1234  0.0406  502 THR A CA  
3519  C C   . THR A 502 ? 0.4379 0.4056 0.7669 -0.0319 0.1355  0.0723  502 THR A C   
3520  O O   . THR A 502 ? 0.4721 0.4376 0.7531 -0.0206 0.1436  0.0872  502 THR A O   
3521  C CB  . THR A 502 ? 0.4070 0.4070 0.8375 -0.0379 0.1386  0.0440  502 THR A CB  
3522  O OG1 . THR A 502 ? 0.4286 0.4152 0.8786 -0.0369 0.1469  0.0578  502 THR A OG1 
3523  C CG2 . THR A 502 ? 0.3939 0.4124 0.8722 -0.0429 0.1215  0.0104  502 THR A CG2 
3524  N N   . GLN A 503 ? 0.4366 0.3921 0.7633 -0.0314 0.1300  0.0775  503 GLN A N   
3525  C CA  . GLN A 503 ? 0.4547 0.3951 0.7401 -0.0221 0.1380  0.1058  503 GLN A CA  
3526  C C   . GLN A 503 ? 0.4794 0.4065 0.7060 -0.0200 0.1233  0.1085  503 GLN A C   
3527  O O   . GLN A 503 ? 0.4911 0.4065 0.6791 -0.0104 0.1240  0.1289  503 GLN A O   
3528  C CB  . GLN A 503 ? 0.4553 0.3904 0.7698 -0.0214 0.1390  0.1111  503 GLN A CB  
3529  C CG  . GLN A 503 ? 0.4788 0.4178 0.8398 -0.0195 0.1587  0.1218  503 GLN A CG  
3530  C CD  . GLN A 503 ? 0.5074 0.4468 0.8434 -0.0097 0.1809  0.1477  503 GLN A CD  
3531  O OE1 . GLN A 503 ? 0.5181 0.4680 0.8879 -0.0106 0.1956  0.1483  503 GLN A OE1 
3532  N NE2 . GLN A 503 ? 0.5274 0.4558 0.8027 0.0016  0.1826  0.1682  503 GLN A NE2 
3533  N N   . LEU A 504 ? 0.4440 0.3777 0.6533 -0.0237 0.1026  0.0824  504 LEU A N   
3534  C CA  . LEU A 504 ? 0.4597 0.3856 0.6112 -0.0201 0.0829  0.0788  504 LEU A CA  
3535  C C   . LEU A 504 ? 0.4942 0.4126 0.5883 -0.0077 0.0840  0.0910  504 LEU A C   
3536  O O   . LEU A 504 ? 0.5161 0.4404 0.6043 -0.0025 0.0916  0.0875  504 LEU A O   
3537  C CB  . LEU A 504 ? 0.4538 0.3867 0.6013 -0.0263 0.0645  0.0512  504 LEU A CB  
3538  C CG  . LEU A 504 ? 0.4425 0.3712 0.5699 -0.0302 0.0481  0.0448  504 LEU A CG  
3539  C CD1 . LEU A 504 ? 0.4195 0.3489 0.5861 -0.0341 0.0523  0.0483  504 LEU A CD1 
3540  C CD2 . LEU A 504 ? 0.4381 0.3724 0.5557 -0.0336 0.0350  0.0218  504 LEU A CD2 
3541  N N   . SER A 505 ? 0.4657 0.3723 0.5189 -0.0013 0.0750  0.1033  505 SER A N   
3542  C CA  . SER A 505 ? 0.5075 0.4041 0.4993 0.0120  0.0693  0.1090  505 SER A CA  
3543  C C   . SER A 505 ? 0.5192 0.4082 0.4742 0.0088  0.0421  0.0942  505 SER A C   
3544  O O   . SER A 505 ? 0.5393 0.4189 0.4495 0.0169  0.0333  0.0885  505 SER A O   
3545  C CB  . SER A 505 ? 0.5182 0.4057 0.4862 0.0260  0.0792  0.1359  505 SER A CB  
3546  O OG  . SER A 505 ? 0.5488 0.4279 0.4577 0.0430  0.0791  0.1403  505 SER A OG  
3547  N N   . GLN A 506 ? 0.4702 0.3627 0.4462 -0.0025 0.0297  0.0878  506 GLN A N   
3548  C CA  . GLN A 506 ? 0.4728 0.3606 0.4266 -0.0089 0.0073  0.0755  506 GLN A CA  
3549  C C   . GLN A 506 ? 0.4472 0.3453 0.4351 -0.0224 0.0057  0.0616  506 GLN A C   
3550  O O   . GLN A 506 ? 0.4232 0.3309 0.4486 -0.0267 0.0119  0.0636  506 GLN A O   
3551  C CB  . GLN A 506 ? 0.4862 0.3706 0.4258 -0.0057 -0.0071 0.0851  506 GLN A CB  
3552  C CG  . GLN A 506 ? 0.4863 0.3716 0.4256 -0.0171 -0.0277 0.0736  506 GLN A CG  
3553  C CD  . GLN A 506 ? 0.5107 0.3921 0.4295 -0.0119 -0.0481 0.0787  506 GLN A CD  
3554  O OE1 . GLN A 506 ? 0.5206 0.4013 0.4295 0.0013  -0.0469 0.0928  506 GLN A OE1 
3555  N NE2 . GLN A 506 ? 0.5194 0.3979 0.4332 -0.0215 -0.0677 0.0678  506 GLN A NE2 
3556  N N   . LEU A 507 ? 0.4499 0.3441 0.4215 -0.0267 -0.0024 0.0479  507 LEU A N   
3557  C CA  . LEU A 507 ? 0.4304 0.3324 0.4212 -0.0361 -0.0043 0.0358  507 LEU A CA  
3558  C C   . LEU A 507 ? 0.4392 0.3316 0.4047 -0.0425 -0.0187 0.0331  507 LEU A C   
3559  O O   . LEU A 507 ? 0.4568 0.3333 0.3894 -0.0394 -0.0271 0.0308  507 LEU A O   
3560  C CB  . LEU A 507 ? 0.4222 0.3290 0.4216 -0.0335 0.0019  0.0232  507 LEU A CB  
3561  C CG  . LEU A 507 ? 0.4121 0.3254 0.4192 -0.0379 -0.0013 0.0090  507 LEU A CG  
3562  C CD1 . LEU A 507 ? 0.4001 0.3252 0.4378 -0.0432 0.0029  0.0080  507 LEU A CD1 
3563  C CD2 . LEU A 507 ? 0.4080 0.3291 0.4282 -0.0321 0.0014  -0.0047 507 LEU A CD2 
3564  N N   . ASP A 508 ? 0.4527 0.3543 0.4373 -0.0511 -0.0204 0.0335  508 ASP A N   
3565  C CA  . ASP A 508 ? 0.4555 0.3507 0.4283 -0.0601 -0.0313 0.0342  508 ASP A CA  
3566  C C   . ASP A 508 ? 0.4502 0.3581 0.4418 -0.0667 -0.0228 0.0304  508 ASP A C   
3567  O O   . ASP A 508 ? 0.4495 0.3747 0.4714 -0.0692 -0.0173 0.0327  508 ASP A O   
3568  C CB  . ASP A 508 ? 0.4673 0.3643 0.4464 -0.0628 -0.0431 0.0422  508 ASP A CB  
3569  C CG  . ASP A 508 ? 0.4744 0.3634 0.4486 -0.0742 -0.0566 0.0417  508 ASP A CG  
3570  O OD1 . ASP A 508 ? 0.4702 0.3491 0.4334 -0.0799 -0.0538 0.0385  508 ASP A OD1 
3571  O OD2 . ASP A 508 ? 0.4878 0.3801 0.4715 -0.0771 -0.0707 0.0449  508 ASP A OD2 
3572  N N   . LEU A 509 ? 0.4486 0.3475 0.4194 -0.0667 -0.0213 0.0252  509 LEU A N   
3573  C CA  . LEU A 509 ? 0.4499 0.3576 0.4253 -0.0698 -0.0123 0.0234  509 LEU A CA  
3574  C C   . LEU A 509 ? 0.4716 0.3643 0.4294 -0.0788 -0.0158 0.0318  509 LEU A C   
3575  O O   . LEU A 509 ? 0.4849 0.3755 0.4291 -0.0782 -0.0076 0.0332  509 LEU A O   
3576  C CB  . LEU A 509 ? 0.4527 0.3629 0.4176 -0.0593 -0.0072 0.0110  509 LEU A CB  
3577  C CG  . LEU A 509 ? 0.4315 0.3538 0.4217 -0.0524 -0.0041 0.0013  509 LEU A CG  
3578  C CD1 . LEU A 509 ? 0.4348 0.3612 0.4193 -0.0428 -0.0040 -0.0148 509 LEU A CD1 
3579  C CD2 . LEU A 509 ? 0.4323 0.3714 0.4585 -0.0550 0.0032  0.0025  509 LEU A CD2 
3580  N N   . SER A 510 ? 0.5011 0.3819 0.4589 -0.0866 -0.0282 0.0376  510 SER A N   
3581  C CA  . SER A 510 ? 0.5193 0.3794 0.4650 -0.0966 -0.0343 0.0443  510 SER A CA  
3582  C C   . SER A 510 ? 0.5181 0.3929 0.4916 -0.1091 -0.0228 0.0546  510 SER A C   
3583  O O   . SER A 510 ? 0.5109 0.4135 0.5161 -0.1102 -0.0142 0.0554  510 SER A O   
3584  C CB  . SER A 510 ? 0.5177 0.3612 0.4594 -0.1006 -0.0542 0.0429  510 SER A CB  
3585  O OG  . SER A 510 ? 0.5042 0.3681 0.4769 -0.1046 -0.0601 0.0444  510 SER A OG  
3586  N N   . SER A 511 ? 0.5301 0.3851 0.4930 -0.1177 -0.0209 0.0637  511 SER A N   
3587  C CA  . SER A 511 ? 0.5356 0.4022 0.5273 -0.1316 -0.0069 0.0776  511 SER A CA  
3588  C C   . SER A 511 ? 0.5492 0.4419 0.5428 -0.1230 0.0169  0.0796  511 SER A C   
3589  O O   . SER A 511 ? 0.5394 0.4614 0.5707 -0.1279 0.0285  0.0835  511 SER A O   
3590  C CB  . SER A 511 ? 0.5140 0.3972 0.5545 -0.1462 -0.0176 0.0791  511 SER A CB  
3591  O OG  . SER A 511 ? 0.5149 0.3756 0.5509 -0.1492 -0.0386 0.0730  511 SER A OG  
3592  N N   . ASN A 512 ? 0.5489 0.4315 0.5013 -0.1078 0.0225  0.0748  512 ASN A N   
3593  C CA  . ASN A 512 ? 0.5663 0.4696 0.5099 -0.0951 0.0410  0.0714  512 ASN A CA  
3594  C C   . ASN A 512 ? 0.6048 0.4869 0.5001 -0.0853 0.0487  0.0788  512 ASN A C   
3595  O O   . ASN A 512 ? 0.6118 0.4639 0.4889 -0.0912 0.0428  0.0901  512 ASN A O   
3596  C CB  . ASN A 512 ? 0.5651 0.4831 0.5120 -0.0818 0.0344  0.0511  512 ASN A CB  
3597  C CG  . ASN A 512 ? 0.5419 0.4865 0.5354 -0.0863 0.0365  0.0479  512 ASN A CG  
3598  O OD1 . ASN A 512 ? 0.5516 0.5193 0.5620 -0.0817 0.0519  0.0459  512 ASN A OD1 
3599  N ND2 . ASN A 512 ? 0.5069 0.4477 0.5186 -0.0926 0.0207  0.0472  512 ASN A ND2 
3600  N N   . ARG A 513 ? 0.6436 0.5396 0.5163 -0.0684 0.0606  0.0716  513 ARG A N   
3601  C CA  . ARG A 513 ? 0.6712 0.5500 0.4908 -0.0532 0.0664  0.0771  513 ARG A CA  
3602  C C   . ARG A 513 ? 0.6679 0.5496 0.4611 -0.0322 0.0522  0.0528  513 ARG A C   
3603  O O   . ARG A 513 ? 0.6798 0.5674 0.4386 -0.0134 0.0583  0.0464  513 ARG A O   
3604  C CB  . ARG A 513 ? 0.6876 0.5802 0.4968 -0.0488 0.0945  0.0920  513 ARG A CB  
3605  C CG  . ARG A 513 ? 0.6802 0.5692 0.5197 -0.0707 0.1109  0.1195  513 ARG A CG  
3606  C CD  . ARG A 513 ? 0.6964 0.5444 0.5196 -0.0805 0.1006  0.1355  513 ARG A CD  
3607  N NE  . ARG A 513 ? 0.7288 0.5632 0.5448 -0.0877 0.1252  0.1664  513 ARG A NE  
3608  C CZ  . ARG A 513 ? 0.7453 0.5390 0.5401 -0.0929 0.1223  0.1850  513 ARG A CZ  
3609  N NH1 . ARG A 513 ? 0.7425 0.5061 0.5191 -0.0900 0.0952  0.1739  513 ARG A NH1 
3610  N NH2 . ARG A 513 ? 0.7621 0.5594 0.5675 -0.0982 0.1395  0.2096  513 ARG A NH2 
3611  N N   . ILE A 514 ? 0.5673 0.4461 0.3777 -0.0345 0.0330  0.0387  514 ILE A N   
3612  C CA  . ILE A 514 ? 0.5588 0.4432 0.3586 -0.0180 0.0191  0.0155  514 ILE A CA  
3613  C C   . ILE A 514 ? 0.5914 0.4518 0.3459 -0.0048 0.0085  0.0179  514 ILE A C   
3614  O O   . ILE A 514 ? 0.6014 0.4360 0.3463 -0.0118 0.0033  0.0316  514 ILE A O   
3615  C CB  . ILE A 514 ? 0.5170 0.4084 0.3554 -0.0253 0.0074  0.0038  514 ILE A CB  
3616  C CG1 . ILE A 514 ? 0.4900 0.4032 0.3716 -0.0352 0.0166  0.0028  514 ILE A CG1 
3617  C CG2 . ILE A 514 ? 0.5098 0.4084 0.3476 -0.0107 -0.0055 -0.0187 514 ILE A CG2 
3618  C CD1 . ILE A 514 ? 0.4640 0.3740 0.3749 -0.0485 0.0099  0.0088  514 ILE A CD1 
3619  N N   . THR A 515 ? 0.5626 0.4306 0.2894 0.0162  0.0030  0.0028  515 THR A N   
3620  C CA  . THR A 515 ? 0.5772 0.4262 0.2587 0.0342  -0.0092 0.0032  515 THR A CA  
3621  C C   . THR A 515 ? 0.5561 0.4169 0.2533 0.0453  -0.0308 -0.0233 515 THR A C   
3622  O O   . THR A 515 ? 0.5177 0.3976 0.2609 0.0368  -0.0336 -0.0385 515 THR A O   
3623  C CB  . THR A 515 ? 0.6279 0.4772 0.2596 0.0534  -0.0001 0.0078  515 THR A CB  
3624  O OG1 . THR A 515 ? 0.6194 0.4983 0.2631 0.0619  0.0020  -0.0153 515 THR A OG1 
3625  C CG2 . THR A 515 ? 0.6560 0.4900 0.2732 0.0420  0.0246  0.0404  515 THR A CG2 
3626  N N   . GLY A 516 ? 0.6083 0.4577 0.2700 0.0647  -0.0455 -0.0271 516 GLY A N   
3627  C CA  . GLY A 516 ? 0.5932 0.4566 0.2746 0.0762  -0.0664 -0.0517 516 GLY A CA  
3628  C C   . GLY A 516 ? 0.5769 0.4251 0.2729 0.0700  -0.0728 -0.0450 516 GLY A C   
3629  O O   . GLY A 516 ? 0.5831 0.4052 0.2676 0.0586  -0.0648 -0.0233 516 GLY A O   
3630  N N   . GLU A 517 ? 0.5814 0.4472 0.3063 0.0780  -0.0874 -0.0655 517 GLU A N   
3631  C CA  . GLU A 517 ? 0.5686 0.4249 0.3083 0.0764  -0.0919 -0.0624 517 GLU A CA  
3632  C C   . GLU A 517 ? 0.5242 0.4078 0.3232 0.0669  -0.0895 -0.0769 517 GLU A C   
3633  O O   . GLU A 517 ? 0.5090 0.4199 0.3411 0.0675  -0.0926 -0.0957 517 GLU A O   
3634  C CB  . GLU A 517 ? 0.6020 0.4499 0.3151 0.1005  -0.1101 -0.0677 517 GLU A CB  
3635  C CG  . GLU A 517 ? 0.6104 0.4883 0.3379 0.1181  -0.1242 -0.0891 517 GLU A CG  
3636  C CD  . GLU A 517 ? 0.6466 0.5154 0.3532 0.1409  -0.1376 -0.0870 517 GLU A CD  
3637  O OE1 . GLU A 517 ? 0.6375 0.5139 0.3673 0.1492  -0.1482 -0.0967 517 GLU A OE1 
3638  O OE2 . GLU A 517 ? 0.6880 0.5419 0.3541 0.1519  -0.1369 -0.0757 517 GLU A OE2 
3639  N N   . LEU A 518 ? 0.5015 0.3754 0.3128 0.0589  -0.0836 -0.0678 518 LEU A N   
3640  C CA  . LEU A 518 ? 0.4665 0.3624 0.3288 0.0506  -0.0763 -0.0748 518 LEU A CA  
3641  C C   . LEU A 518 ? 0.4637 0.3838 0.3574 0.0650  -0.0867 -0.0935 518 LEU A C   
3642  O O   . LEU A 518 ? 0.4845 0.3957 0.3585 0.0804  -0.0964 -0.0944 518 LEU A O   
3643  C CB  . LEU A 518 ? 0.4617 0.3388 0.3174 0.0422  -0.0671 -0.0593 518 LEU A CB  
3644  C CG  . LEU A 518 ? 0.4438 0.3178 0.3088 0.0236  -0.0545 -0.0472 518 LEU A CG  
3645  C CD1 . LEU A 518 ? 0.4552 0.3169 0.2964 0.0156  -0.0535 -0.0384 518 LEU A CD1 
3646  C CD2 . LEU A 518 ? 0.4489 0.3042 0.3010 0.0209  -0.0511 -0.0364 518 LEU A CD2 
3647  N N   . PRO A 519 ? 0.4205 0.3710 0.3678 0.0605  -0.0852 -0.1089 519 PRO A N   
3648  C CA  . PRO A 519 ? 0.4182 0.3966 0.4076 0.0723  -0.0960 -0.1283 519 PRO A CA  
3649  C C   . PRO A 519 ? 0.4044 0.3907 0.4246 0.0712  -0.0828 -0.1211 519 PRO A C   
3650  O O   . PRO A 519 ? 0.3951 0.3677 0.4077 0.0607  -0.0654 -0.1034 519 PRO A O   
3651  C CB  . PRO A 519 ? 0.4018 0.4060 0.4425 0.0640  -0.0978 -0.1469 519 PRO A CB  
3652  C CG  . PRO A 519 ? 0.3828 0.3754 0.4266 0.0450  -0.0780 -0.1305 519 PRO A CG  
3653  C CD  . PRO A 519 ? 0.3981 0.3587 0.3761 0.0444  -0.0742 -0.1097 519 PRO A CD  
3654  N N   . GLU A 520 ? 0.3861 0.3969 0.4410 0.0845  -0.0918 -0.1358 520 GLU A N   
3655  C CA  . GLU A 520 ? 0.3865 0.4132 0.4811 0.0850  -0.0753 -0.1305 520 GLU A CA  
3656  C C   . GLU A 520 ? 0.3677 0.4145 0.5233 0.0668  -0.0553 -0.1273 520 GLU A C   
3657  O O   . GLU A 520 ? 0.3681 0.4244 0.5502 0.0654  -0.0344 -0.1160 520 GLU A O   
3658  C CB  . GLU A 520 ? 0.3967 0.4505 0.5235 0.1041  -0.0891 -0.1477 520 GLU A CB  
3659  C CG  . GLU A 520 ? 0.4228 0.4534 0.4895 0.1258  -0.1073 -0.1475 520 GLU A CG  
3660  C CD  . GLU A 520 ? 0.4364 0.4372 0.4606 0.1310  -0.0935 -0.1289 520 GLU A CD  
3661  O OE1 . GLU A 520 ? 0.4277 0.4262 0.4611 0.1190  -0.0706 -0.1160 520 GLU A OE1 
3662  O OE2 . GLU A 520 ? 0.4606 0.4381 0.4399 0.1489  -0.1070 -0.1278 520 GLU A OE2 
3663  N N   . SER A 521 ? 0.3633 0.4146 0.5392 0.0546  -0.0599 -0.1360 521 SER A N   
3664  C CA  . SER A 521 ? 0.3504 0.4111 0.5780 0.0367  -0.0410 -0.1299 521 SER A CA  
3665  C C   . SER A 521 ? 0.3642 0.3988 0.5546 0.0275  -0.0210 -0.1028 521 SER A C   
3666  O O   . SER A 521 ? 0.3621 0.4005 0.5887 0.0151  -0.0031 -0.0922 521 SER A O   
3667  C CB  . SER A 521 ? 0.3244 0.3920 0.5776 0.0293  -0.0546 -0.1497 521 SER A CB  
3668  O OG  . SER A 521 ? 0.3149 0.3879 0.6224 0.0126  -0.0371 -0.1440 521 SER A OG  
3669  N N   . ILE A 522 ? 0.4001 0.4075 0.5214 0.0337  -0.0253 -0.0918 522 ILE A N   
3670  C CA  . ILE A 522 ? 0.4176 0.4012 0.5026 0.0271  -0.0116 -0.0694 522 ILE A CA  
3671  C C   . ILE A 522 ? 0.4390 0.4318 0.5498 0.0273  0.0114  -0.0550 522 ILE A C   
3672  O O   . ILE A 522 ? 0.4474 0.4276 0.5443 0.0209  0.0244  -0.0372 522 ILE A O   
3673  C CB  . ILE A 522 ? 0.4323 0.3867 0.4492 0.0355  -0.0226 -0.0640 522 ILE A CB  
3674  C CG1 . ILE A 522 ? 0.4327 0.3627 0.4143 0.0259  -0.0167 -0.0466 522 ILE A CG1 
3675  C CG2 . ILE A 522 ? 0.4554 0.4102 0.4626 0.0516  -0.0214 -0.0651 522 ILE A CG2 
3676  C CD1 . ILE A 522 ? 0.4142 0.3469 0.4111 0.0118  -0.0149 -0.0443 522 ILE A CD1 
3677  N N   . SER A 523 ? 0.4228 0.4391 0.5711 0.0362  0.0174  -0.0616 523 SER A N   
3678  C CA  . SER A 523 ? 0.4265 0.4546 0.5999 0.0389  0.0441  -0.0459 523 SER A CA  
3679  C C   . SER A 523 ? 0.4105 0.4486 0.6364 0.0237  0.0631  -0.0343 523 SER A C   
3680  O O   . SER A 523 ? 0.4153 0.4554 0.6488 0.0253  0.0889  -0.0135 523 SER A O   
3681  C CB  . SER A 523 ? 0.4098 0.4670 0.6236 0.0515  0.0471  -0.0570 523 SER A CB  
3682  O OG  . SER A 523 ? 0.4158 0.4853 0.6486 0.0569  0.0771  -0.0397 523 SER A OG  
3683  N N   . ASN A 524 ? 0.4131 0.4554 0.6725 0.0111  0.0517  -0.0467 524 ASN A N   
3684  C CA  . ASN A 524 ? 0.3821 0.4327 0.7028 -0.0032 0.0674  -0.0395 524 ASN A CA  
3685  C C   . ASN A 524 ? 0.3922 0.4195 0.6827 -0.0081 0.0826  -0.0133 524 ASN A C   
3686  O O   . ASN A 524 ? 0.3572 0.3867 0.6951 -0.0178 0.0990  -0.0017 524 ASN A O   
3687  C CB  . ASN A 524 ? 0.3462 0.4037 0.7036 -0.0121 0.0468  -0.0650 524 ASN A CB  
3688  C CG  . ASN A 524 ? 0.3123 0.4012 0.7367 -0.0109 0.0373  -0.0894 524 ASN A CG  
3689  O OD1 . ASN A 524 ? 0.3196 0.4265 0.7560 -0.0015 0.0425  -0.0891 524 ASN A OD1 
3690  N ND2 . ASN A 524 ? 0.2914 0.3884 0.7618 -0.0191 0.0218  -0.1128 524 ASN A ND2 
3691  N N   . ILE A 525 ? 0.4185 0.4231 0.6352 -0.0012 0.0763  -0.0040 525 ILE A N   
3692  C CA  . ILE A 525 ? 0.4264 0.4105 0.6126 -0.0044 0.0833  0.0169  525 ILE A CA  
3693  C C   . ILE A 525 ? 0.4528 0.4272 0.5929 0.0086  0.0975  0.0372  525 ILE A C   
3694  O O   . ILE A 525 ? 0.4662 0.4202 0.5542 0.0119  0.0919  0.0478  525 ILE A O   
3695  C CB  . ILE A 525 ? 0.4192 0.3862 0.5639 -0.0087 0.0613  0.0089  525 ILE A CB  
3696  C CG1 . ILE A 525 ? 0.4248 0.3838 0.5207 -0.0009 0.0433  -0.0036 525 ILE A CG1 
3697  C CG2 . ILE A 525 ? 0.4012 0.3757 0.5885 -0.0194 0.0531  -0.0066 525 ILE A CG2 
3698  C CD1 . ILE A 525 ? 0.4214 0.3652 0.4825 -0.0063 0.0255  -0.0089 525 ILE A CD1 
3699  N N   . ASN A 526 ? 0.4620 0.4526 0.6222 0.0175  0.1155  0.0410  526 ASN A N   
3700  C CA  . ASN A 526 ? 0.5010 0.4842 0.6109 0.0350  0.1286  0.0550  526 ASN A CA  
3701  C C   . ASN A 526 ? 0.5052 0.4702 0.5775 0.0394  0.1406  0.0808  526 ASN A C   
3702  O O   . ASN A 526 ? 0.5298 0.4823 0.5425 0.0561  0.1438  0.0887  526 ASN A O   
3703  C CB  . ASN A 526 ? 0.4778 0.4880 0.6321 0.0431  0.1538  0.0588  526 ASN A CB  
3704  C CG  . ASN A 526 ? 0.4339 0.4595 0.6569 0.0329  0.1825  0.0781  526 ASN A CG  
3705  O OD1 . ASN A 526 ? 0.4109 0.4290 0.6611 0.0181  0.1784  0.0816  526 ASN A OD1 
3706  N ND2 . ASN A 526 ? 0.4265 0.4732 0.6808 0.0414  0.2132  0.0916  526 ASN A ND2 
3707  N N   . ARG A 527 ? 0.5273 0.4894 0.6307 0.0274  0.1455  0.0927  527 ARG A N   
3708  C CA  . ARG A 527 ? 0.5327 0.4763 0.5975 0.0335  0.1516  0.1167  527 ARG A CA  
3709  C C   . ARG A 527 ? 0.5505 0.4739 0.5556 0.0348  0.1220  0.1078  527 ARG A C   
3710  O O   . ARG A 527 ? 0.5515 0.4606 0.5184 0.0426  0.1209  0.1242  527 ARG A O   
3711  C CB  . ARG A 527 ? 0.4948 0.4393 0.6151 0.0212  0.1643  0.1319  527 ARG A CB  
3712  C CG  . ARG A 527 ? 0.4798 0.4364 0.6511 0.0223  0.2007  0.1545  527 ARG A CG  
3713  C CD  . ARG A 527 ? 0.4711 0.4211 0.6848 0.0137  0.2031  0.1646  527 ARG A CD  
3714  N NE  . ARG A 527 ? 0.4800 0.4436 0.7594 0.0098  0.2203  0.1669  527 ARG A NE  
3715  C CZ  . ARG A 527 ? 0.5214 0.4839 0.7998 0.0210  0.2437  0.1912  527 ARG A CZ  
3716  N NH1 . ARG A 527 ? 0.5586 0.5095 0.7707 0.0388  0.2518  0.2131  527 ARG A NH1 
3717  N NH2 . ARG A 527 ? 0.5314 0.5036 0.8754 0.0150  0.2579  0.1925  527 ARG A NH2 
3718  N N   . ILE A 528 ? 0.5330 0.4551 0.5314 0.0277  0.0982  0.0833  528 ILE A N   
3719  C CA  . ILE A 528 ? 0.5306 0.4350 0.4852 0.0252  0.0720  0.0758  528 ILE A CA  
3720  C C   . ILE A 528 ? 0.5545 0.4420 0.4425 0.0418  0.0655  0.0785  528 ILE A C   
3721  O O   . ILE A 528 ? 0.5764 0.4656 0.4462 0.0560  0.0769  0.0778  528 ILE A O   
3722  C CB  . ILE A 528 ? 0.5279 0.4339 0.4921 0.0147  0.0529  0.0527  528 ILE A CB  
3723  C CG1 . ILE A 528 ? 0.5143 0.4055 0.4505 0.0074  0.0307  0.0486  528 ILE A CG1 
3724  C CG2 . ILE A 528 ? 0.5627 0.4682 0.5075 0.0245  0.0501  0.0399  528 ILE A CG2 
3725  C CD1 . ILE A 528 ? 0.4878 0.3866 0.4552 -0.0067 0.0226  0.0373  528 ILE A CD1 
3726  N N   . SER A 529 ? 0.5591 0.4312 0.4129 0.0413  0.0461  0.0798  529 SER A N   
3727  C CA  . SER A 529 ? 0.5983 0.4512 0.3891 0.0555  0.0311  0.0753  529 SER A CA  
3728  C C   . SER A 529 ? 0.5936 0.4317 0.3684 0.0447  0.0004  0.0598  529 SER A C   
3729  O O   . SER A 529 ? 0.6243 0.4435 0.3545 0.0536  -0.0157 0.0488  529 SER A O   
3730  C CB  . SER A 529 ? 0.6381 0.4859 0.3959 0.0713  0.0373  0.0949  529 SER A CB  
3731  O OG  . SER A 529 ? 0.6247 0.4760 0.4062 0.0616  0.0312  0.1057  529 SER A OG  
3732  N N   . LYS A 530 ? 0.5728 0.4183 0.3842 0.0265  -0.0071 0.0583  530 LYS A N   
3733  C CA  . LYS A 530 ? 0.5632 0.3985 0.3701 0.0138  -0.0308 0.0464  530 LYS A CA  
3734  C C   . LYS A 530 ? 0.5437 0.3888 0.3874 -0.0006 -0.0267 0.0390  530 LYS A C   
3735  O O   . LYS A 530 ? 0.5269 0.3889 0.4096 -0.0081 -0.0164 0.0437  530 LYS A O   
3736  C CB  . LYS A 530 ? 0.5610 0.3984 0.3730 0.0086  -0.0445 0.0533  530 LYS A CB  
3737  C CG  . LYS A 530 ? 0.5787 0.3977 0.3494 0.0147  -0.0699 0.0460  530 LYS A CG  
3738  C CD  . LYS A 530 ? 0.5877 0.4144 0.3719 0.0101  -0.0861 0.0516  530 LYS A CD  
3739  C CE  . LYS A 530 ? 0.6079 0.4175 0.3550 0.0165  -0.1161 0.0403  530 LYS A CE  
3740  N NZ  . LYS A 530 ? 0.6073 0.4283 0.3813 0.0071  -0.1370 0.0409  530 LYS A NZ  
3741  N N   . LEU A 531 ? 0.5397 0.3720 0.3680 -0.0023 -0.0354 0.0269  531 LEU A N   
3742  C CA  . LEU A 531 ? 0.5186 0.3571 0.3694 -0.0119 -0.0337 0.0200  531 LEU A CA  
3743  C C   . LEU A 531 ? 0.5121 0.3334 0.3498 -0.0227 -0.0501 0.0165  531 LEU A C   
3744  O O   . LEU A 531 ? 0.5370 0.3350 0.3450 -0.0187 -0.0612 0.0106  531 LEU A O   
3745  C CB  . LEU A 531 ? 0.5164 0.3561 0.3637 -0.0015 -0.0269 0.0119  531 LEU A CB  
3746  C CG  . LEU A 531 ? 0.4873 0.3369 0.3556 -0.0060 -0.0259 0.0036  531 LEU A CG  
3747  C CD1 . LEU A 531 ? 0.4669 0.3357 0.3719 -0.0168 -0.0195 0.0059  531 LEU A CD1 
3748  C CD2 . LEU A 531 ? 0.4903 0.3512 0.3692 0.0062  -0.0183 -0.0040 531 LEU A CD2 
3749  N N   . GLN A 532 ? 0.5183 0.3506 0.3814 -0.0360 -0.0503 0.0206  532 GLN A N   
3750  C CA  . GLN A 532 ? 0.5146 0.3352 0.3763 -0.0488 -0.0611 0.0211  532 GLN A CA  
3751  C C   . GLN A 532 ? 0.5038 0.3341 0.3806 -0.0547 -0.0512 0.0209  532 GLN A C   
3752  O O   . GLN A 532 ? 0.4919 0.3426 0.3967 -0.0608 -0.0431 0.0240  532 GLN A O   
3753  C CB  . GLN A 532 ? 0.5228 0.3512 0.4020 -0.0575 -0.0697 0.0268  532 GLN A CB  
3754  C CG  . GLN A 532 ? 0.5503 0.3714 0.4086 -0.0471 -0.0808 0.0266  532 GLN A CG  
3755  C CD  . GLN A 532 ? 0.5634 0.3996 0.4434 -0.0512 -0.0888 0.0329  532 GLN A CD  
3756  O OE1 . GLN A 532 ? 0.5844 0.4325 0.4678 -0.0414 -0.0826 0.0400  532 GLN A OE1 
3757  N NE2 . GLN A 532 ? 0.5577 0.3936 0.4558 -0.0652 -0.1025 0.0315  532 GLN A NE2 
3758  N N   . LEU A 533 ? 0.5064 0.3209 0.3612 -0.0500 -0.0524 0.0169  533 LEU A N   
3759  C CA  . LEU A 533 ? 0.5073 0.3267 0.3634 -0.0511 -0.0451 0.0170  533 LEU A CA  
3760  C C   . LEU A 533 ? 0.5327 0.3281 0.3721 -0.0592 -0.0494 0.0248  533 LEU A C   
3761  O O   . LEU A 533 ? 0.5586 0.3507 0.3857 -0.0561 -0.0435 0.0276  533 LEU A O   
3762  C CB  . LEU A 533 ? 0.5003 0.3233 0.3463 -0.0362 -0.0431 0.0072  533 LEU A CB  
3763  C CG  . LEU A 533 ? 0.4795 0.3270 0.3520 -0.0301 -0.0359 0.0001  533 LEU A CG  
3764  C CD1 . LEU A 533 ? 0.4773 0.3311 0.3483 -0.0167 -0.0365 -0.0113 533 LEU A CD1 
3765  C CD2 . LEU A 533 ? 0.4788 0.3485 0.3831 -0.0374 -0.0273 0.0006  533 LEU A CD2 
3766  N N   . ASN A 534 ? 0.5415 0.3192 0.3806 -0.0688 -0.0601 0.0286  534 ASN A N   
3767  C CA  . ASN A 534 ? 0.5738 0.3228 0.4029 -0.0782 -0.0653 0.0363  534 ASN A CA  
3768  C C   . ASN A 534 ? 0.5727 0.3348 0.4253 -0.0922 -0.0522 0.0494  534 ASN A C   
3769  O O   . ASN A 534 ? 0.5467 0.3402 0.4262 -0.0958 -0.0428 0.0503  534 ASN A O   
3770  C CB  . ASN A 534 ? 0.5943 0.3216 0.4233 -0.0850 -0.0838 0.0322  534 ASN A CB  
3771  C CG  . ASN A 534 ? 0.5758 0.3271 0.4345 -0.0932 -0.0886 0.0313  534 ASN A CG  
3772  O OD1 . ASN A 534 ? 0.5514 0.3257 0.4141 -0.0843 -0.0842 0.0280  534 ASN A OD1 
3773  N ND2 . ASN A 534 ? 0.5899 0.3367 0.4734 -0.1097 -0.0980 0.0350  534 ASN A ND2 
3774  N N   . GLY A 535 ? 0.6009 0.3375 0.4439 -0.0992 -0.0499 0.0608  535 GLY A N   
3775  C CA  . GLY A 535 ? 0.6058 0.3530 0.4702 -0.1123 -0.0332 0.0770  535 GLY A CA  
3776  C C   . GLY A 535 ? 0.6147 0.3867 0.4686 -0.1007 -0.0141 0.0791  535 GLY A C   
3777  O O   . GLY A 535 ? 0.6070 0.4092 0.4883 -0.1062 -0.0006 0.0826  535 GLY A O   
3778  N N   . ASN A 536 ? 0.5924 0.3527 0.4074 -0.0828 -0.0147 0.0749  536 ASN A N   
3779  C CA  . ASN A 536 ? 0.6083 0.3901 0.4079 -0.0683 -0.0020 0.0717  536 ASN A CA  
3780  C C   . ASN A 536 ? 0.6409 0.3963 0.3941 -0.0540 -0.0010 0.0798  536 ASN A C   
3781  O O   . ASN A 536 ? 0.6626 0.3823 0.4008 -0.0574 -0.0071 0.0907  536 ASN A O   
3782  C CB  . ASN A 536 ? 0.5912 0.3972 0.4001 -0.0571 -0.0093 0.0503  536 ASN A CB  
3783  C CG  . ASN A 536 ? 0.5725 0.4098 0.4222 -0.0659 -0.0025 0.0462  536 ASN A CG  
3784  O OD1 . ASN A 536 ? 0.5845 0.4428 0.4424 -0.0639 0.0115  0.0468  536 ASN A OD1 
3785  N ND2 . ASN A 536 ? 0.5420 0.3812 0.4144 -0.0730 -0.0125 0.0423  536 ASN A ND2 
3786  N N   . ARG A 537 ? 0.6704 0.4416 0.3997 -0.0359 0.0048  0.0734  537 ARG A N   
3787  C CA  . ARG A 537 ? 0.6940 0.4439 0.3740 -0.0167 0.0029  0.0794  537 ARG A CA  
3788  C C   . ARG A 537 ? 0.6777 0.4351 0.3445 0.0037  -0.0157 0.0562  537 ARG A C   
3789  O O   . ARG A 537 ? 0.6858 0.4458 0.3184 0.0249  -0.0189 0.0513  537 ARG A O   
3790  C CB  . ARG A 537 ? 0.7230 0.4836 0.3780 -0.0079 0.0230  0.0914  537 ARG A CB  
3791  C CG  . ARG A 537 ? 0.7268 0.4946 0.4095 -0.0283 0.0461  0.1117  537 ARG A CG  
3792  C CD  . ARG A 537 ? 0.7595 0.5113 0.4038 -0.0213 0.0682  0.1393  537 ARG A CD  
3793  N NE  . ARG A 537 ? 0.7747 0.5516 0.3869 0.0006  0.0804  0.1324  537 ARG A NE  
3794  C CZ  . ARG A 537 ? 0.8195 0.5881 0.3836 0.0188  0.0935  0.1484  537 ARG A CZ  
3795  N NH1 . ARG A 537 ? 0.8564 0.6013 0.4159 0.0156  0.0947  0.1708  537 ARG A NH1 
3796  N NH2 . ARG A 537 ? 0.8358 0.6306 0.3718 0.0404  0.1011  0.1360  537 ARG A NH2 
3797  N N   . LEU A 538 ? 0.6206 0.3835 0.3153 -0.0014 -0.0278 0.0419  538 LEU A N   
3798  C CA  . LEU A 538 ? 0.6095 0.3811 0.3018 0.0158  -0.0431 0.0218  538 LEU A CA  
3799  C C   . LEU A 538 ? 0.6501 0.3900 0.3046 0.0314  -0.0542 0.0277  538 LEU A C   
3800  O O   . LEU A 538 ? 0.6720 0.3780 0.3164 0.0241  -0.0551 0.0422  538 LEU A O   
3801  C CB  . LEU A 538 ? 0.5689 0.3521 0.2982 0.0069  -0.0481 0.0104  538 LEU A CB  
3802  C CG  . LEU A 538 ? 0.5312 0.3436 0.2994 -0.0061 -0.0387 0.0055  538 LEU A CG  
3803  C CD1 . LEU A 538 ? 0.5042 0.3193 0.2989 -0.0144 -0.0418 0.0023  538 LEU A CD1 
3804  C CD2 . LEU A 538 ? 0.5187 0.3604 0.2988 0.0050  -0.0386 -0.0123 538 LEU A CD2 
3805  N N   . SER A 539 ? 0.6291 0.3795 0.2656 0.0541  -0.0650 0.0147  539 SER A N   
3806  C CA  . SER A 539 ? 0.6742 0.3970 0.2712 0.0744  -0.0767 0.0206  539 SER A CA  
3807  C C   . SER A 539 ? 0.6568 0.3977 0.2727 0.0906  -0.0937 -0.0023 539 SER A C   
3808  O O   . SER A 539 ? 0.6139 0.3809 0.2692 0.0834  -0.0945 -0.0183 539 SER A O   
3809  C CB  . SER A 539 ? 0.7126 0.4395 0.2810 0.0882  -0.0707 0.0284  539 SER A CB  
3810  O OG  . SER A 539 ? 0.6963 0.4584 0.2715 0.0926  -0.0693 0.0124  539 SER A OG  
3811  N N   . GLY A 540 ? 0.6886 0.4196 0.2894 0.1106  -0.1032 -0.0027 540 GLY A N   
3812  C CA  . GLY A 540 ? 0.6770 0.4261 0.2986 0.1276  -0.1187 -0.0229 540 GLY A CA  
3813  C C   . GLY A 540 ? 0.6648 0.3968 0.2969 0.1230  -0.1208 -0.0235 540 GLY A C   
3814  O O   . GLY A 540 ? 0.6682 0.3714 0.2908 0.1067  -0.1130 -0.0097 540 GLY A O   
3815  N N   . LYS A 541 ? 0.6412 0.3926 0.2944 0.1389  -0.1323 -0.0412 541 LYS A N   
3816  C CA  . LYS A 541 ? 0.6331 0.3737 0.2974 0.1388  -0.1317 -0.0441 541 LYS A CA  
3817  C C   . LYS A 541 ? 0.5847 0.3515 0.2900 0.1179  -0.1171 -0.0495 541 LYS A C   
3818  O O   . LYS A 541 ? 0.5543 0.3543 0.2885 0.1090  -0.1124 -0.0571 541 LYS A O   
3819  C CB  . LYS A 541 ? 0.6419 0.3981 0.3200 0.1650  -0.1450 -0.0597 541 LYS A CB  
3820  C CG  . LYS A 541 ? 0.5980 0.4072 0.3352 0.1644  -0.1418 -0.0797 541 LYS A CG  
3821  C CD  . LYS A 541 ? 0.6095 0.4388 0.3672 0.1912  -0.1552 -0.0949 541 LYS A CD  
3822  C CE  . LYS A 541 ? 0.6307 0.4759 0.3815 0.2100  -0.1771 -0.1051 541 LYS A CE  
3823  N NZ  . LYS A 541 ? 0.6440 0.5116 0.4194 0.2379  -0.1934 -0.1208 541 LYS A NZ  
3824  N N   . ILE A 542 ? 0.6134 0.3620 0.3180 0.1118  -0.1108 -0.0457 542 ILE A N   
3825  C CA  . ILE A 542 ? 0.5769 0.3476 0.3137 0.0975  -0.0974 -0.0489 542 ILE A CA  
3826  C C   . ILE A 542 ? 0.5554 0.3664 0.3336 0.1099  -0.0947 -0.0641 542 ILE A C   
3827  O O   . ILE A 542 ? 0.5734 0.3828 0.3498 0.1297  -0.1001 -0.0711 542 ILE A O   
3828  C CB  . ILE A 542 ? 0.5926 0.3312 0.3091 0.0921  -0.0945 -0.0426 542 ILE A CB  
3829  C CG1 . ILE A 542 ? 0.6068 0.3137 0.3006 0.0734  -0.0958 -0.0281 542 ILE A CG1 
3830  C CG2 . ILE A 542 ? 0.5649 0.3280 0.3081 0.0864  -0.0813 -0.0462 542 ILE A CG2 
3831  C CD1 . ILE A 542 ? 0.6300 0.3018 0.3050 0.0682  -0.0992 -0.0257 542 ILE A CD1 
3832  N N   . PRO A 543 ? 0.5217 0.3693 0.3424 0.0992  -0.0859 -0.0695 543 PRO A N   
3833  C CA  . PRO A 543 ? 0.5216 0.4094 0.3928 0.1085  -0.0826 -0.0834 543 PRO A CA  
3834  C C   . PRO A 543 ? 0.5281 0.4182 0.4079 0.1157  -0.0691 -0.0812 543 PRO A C   
3835  O O   . PRO A 543 ? 0.5314 0.4038 0.3923 0.1069  -0.0580 -0.0705 543 PRO A O   
3836  C CB  . PRO A 543 ? 0.5015 0.4175 0.4149 0.0908  -0.0740 -0.0862 543 PRO A CB  
3837  C CG  . PRO A 543 ? 0.4874 0.3790 0.3733 0.0731  -0.0661 -0.0708 543 PRO A CG  
3838  C CD  . PRO A 543 ? 0.4977 0.3507 0.3280 0.0777  -0.0773 -0.0628 543 PRO A CD  
3839  N N   . SER A 544 ? 0.5227 0.4368 0.4311 0.1340  -0.0704 -0.0925 544 SER A N   
3840  C CA  . SER A 544 ? 0.5324 0.4556 0.4531 0.1440  -0.0532 -0.0910 544 SER A CA  
3841  C C   . SER A 544 ? 0.5307 0.4828 0.4954 0.1296  -0.0291 -0.0844 544 SER A C   
3842  O O   . SER A 544 ? 0.5458 0.5028 0.5121 0.1369  -0.0097 -0.0782 544 SER A O   
3843  C CB  . SER A 544 ? 0.5302 0.4773 0.4784 0.1682  -0.0592 -0.1045 544 SER A CB  
3844  O OG  . SER A 544 ? 0.5251 0.5215 0.5439 0.1647  -0.0572 -0.1152 544 SER A OG  
3845  N N   . GLY A 545 ? 0.4886 0.4577 0.4865 0.1113  -0.0291 -0.0848 545 GLY A N   
3846  C CA  . GLY A 545 ? 0.4927 0.4826 0.5322 0.0967  -0.0066 -0.0757 545 GLY A CA  
3847  C C   . GLY A 545 ? 0.5074 0.4704 0.5058 0.0885  0.0059  -0.0578 545 GLY A C   
3848  O O   . GLY A 545 ? 0.5196 0.4961 0.5450 0.0805  0.0267  -0.0462 545 GLY A O   
3849  N N   . ILE A 546 ? 0.5578 0.4828 0.4944 0.0907  -0.0072 -0.0549 546 ILE A N   
3850  C CA  . ILE A 546 ? 0.5745 0.4749 0.4716 0.0864  -0.0002 -0.0418 546 ILE A CA  
3851  C C   . ILE A 546 ? 0.5974 0.5024 0.4855 0.1033  0.0179  -0.0375 546 ILE A C   
3852  O O   . ILE A 546 ? 0.6083 0.5046 0.4748 0.1022  0.0294  -0.0256 546 ILE A O   
3853  C CB  . ILE A 546 ? 0.5622 0.4214 0.4043 0.0844  -0.0207 -0.0425 546 ILE A CB  
3854  C CG1 . ILE A 546 ? 0.5401 0.3974 0.3890 0.0711  -0.0342 -0.0448 546 ILE A CG1 
3855  C CG2 . ILE A 546 ? 0.5679 0.4048 0.3768 0.0776  -0.0189 -0.0324 546 ILE A CG2 
3856  C CD1 . ILE A 546 ? 0.5266 0.3956 0.3977 0.0520  -0.0275 -0.0372 546 ILE A CD1 
3857  N N   . ARG A 547 ? 0.5936 0.5137 0.4968 0.1214  0.0212  -0.0470 547 ARG A N   
3858  C CA  . ARG A 547 ? 0.6086 0.5380 0.5061 0.1405  0.0428  -0.0433 547 ARG A CA  
3859  C C   . ARG A 547 ? 0.6126 0.5687 0.5455 0.1333  0.0722  -0.0265 547 ARG A C   
3860  O O   . ARG A 547 ? 0.6320 0.5814 0.5335 0.1443  0.0903  -0.0152 547 ARG A O   
3861  C CB  . ARG A 547 ? 0.6017 0.5542 0.5291 0.1598  0.0436  -0.0564 547 ARG A CB  
3862  C CG  . ARG A 547 ? 0.6150 0.6009 0.5740 0.1748  0.0760  -0.0502 547 ARG A CG  
3863  C CD  . ARG A 547 ? 0.5999 0.6200 0.6098 0.1905  0.0762  -0.0639 547 ARG A CD  
3864  N NE  . ARG A 547 ? 0.5903 0.6186 0.6320 0.1802  0.0491  -0.0771 547 ARG A NE  
3865  C CZ  . ARG A 547 ? 0.5620 0.6305 0.6788 0.1680  0.0511  -0.0814 547 ARG A CZ  
3866  N NH1 . ARG A 547 ? 0.5441 0.6490 0.7214 0.1618  0.0809  -0.0716 547 ARG A NH1 
3867  N NH2 . ARG A 547 ? 0.5392 0.6104 0.6706 0.1626  0.0225  -0.0961 547 ARG A NH2 
3868  N N   . LEU A 548 ? 0.5138 0.4973 0.5093 0.1161  0.0768  -0.0246 548 LEU A N   
3869  C CA  . LEU A 548 ? 0.5060 0.5160 0.5498 0.1090  0.1068  -0.0078 548 LEU A CA  
3870  C C   . LEU A 548 ? 0.5045 0.4958 0.5269 0.0948  0.1109  0.0095  548 LEU A C   
3871  O O   . LEU A 548 ? 0.5017 0.5091 0.5621 0.0882  0.1355  0.0268  548 LEU A O   
3872  C CB  . LEU A 548 ? 0.4740 0.5215 0.6047 0.0972  0.1081  -0.0168 548 LEU A CB  
3873  C CG  . LEU A 548 ? 0.4767 0.5538 0.6456 0.1128  0.1079  -0.0321 548 LEU A CG  
3874  C CD1 . LEU A 548 ? 0.4471 0.5608 0.7037 0.1000  0.1011  -0.0459 548 LEU A CD1 
3875  C CD2 . LEU A 548 ? 0.5036 0.5977 0.6775 0.1304  0.1422  -0.0184 548 LEU A CD2 
3876  N N   . LEU A 549 ? 0.5515 0.5096 0.5186 0.0902  0.0879  0.0064  549 LEU A N   
3877  C CA  . LEU A 549 ? 0.5666 0.5080 0.5104 0.0803  0.0892  0.0219  549 LEU A CA  
3878  C C   . LEU A 549 ? 0.5925 0.5150 0.4737 0.0988  0.0971  0.0316  549 LEU A C   
3879  O O   . LEU A 549 ? 0.6032 0.4963 0.4281 0.1025  0.0763  0.0253  549 LEU A O   
3880  C CB  . LEU A 549 ? 0.5605 0.4815 0.4864 0.0654  0.0613  0.0132  549 LEU A CB  
3881  C CG  . LEU A 549 ? 0.5400 0.4736 0.5055 0.0543  0.0476  -0.0023 549 LEU A CG  
3882  C CD1 . LEU A 549 ? 0.5212 0.4314 0.4548 0.0444  0.0238  -0.0082 549 LEU A CD1 
3883  C CD2 . LEU A 549 ? 0.5199 0.4797 0.5522 0.0416  0.0608  0.0012  549 LEU A CD2 
3884  N N   . THR A 550 ? 0.5713 0.5115 0.4642 0.1114  0.1282  0.0470  550 THR A N   
3885  C CA  . THR A 550 ? 0.6226 0.5484 0.4514 0.1355  0.1385  0.0539  550 THR A CA  
3886  C C   . THR A 550 ? 0.6463 0.5498 0.4270 0.1356  0.1330  0.0683  550 THR A C   
3887  O O   . THR A 550 ? 0.6906 0.5715 0.4027 0.1539  0.1242  0.0645  550 THR A O   
3888  C CB  . THR A 550 ? 0.6429 0.5974 0.4986 0.1512  0.1783  0.0686  550 THR A CB  
3889  O OG1 . THR A 550 ? 0.6305 0.6024 0.5362 0.1380  0.2030  0.0930  550 THR A OG1 
3890  C CG2 . THR A 550 ? 0.6223 0.6028 0.5292 0.1537  0.1809  0.0520  550 THR A CG2 
3891  N N   . ASN A 551 ? 0.6843 0.5933 0.4999 0.1174  0.1360  0.0828  551 ASN A N   
3892  C CA  . ASN A 551 ? 0.6941 0.5844 0.4696 0.1184  0.1280  0.0965  551 ASN A CA  
3893  C C   . ASN A 551 ? 0.6900 0.5569 0.4357 0.1083  0.0892  0.0789  551 ASN A C   
3894  O O   . ASN A 551 ? 0.6837 0.5373 0.4006 0.1084  0.0766  0.0865  551 ASN A O   
3895  C CB  . ASN A 551 ? 0.6721 0.5755 0.5001 0.1043  0.1459  0.1191  551 ASN A CB  
3896  C CG  . ASN A 551 ? 0.6769 0.5912 0.5074 0.1195  0.1851  0.1480  551 ASN A CG  
3897  O OD1 . ASN A 551 ? 0.6593 0.5971 0.5432 0.1176  0.2125  0.1538  551 ASN A OD1 
3898  N ND2 . ASN A 551 ? 0.6962 0.5945 0.4700 0.1356  0.1883  0.1670  551 ASN A ND2 
3899  N N   . LEU A 552 ? 0.6582 0.5208 0.4133 0.1000  0.0707  0.0571  552 LEU A N   
3900  C CA  . LEU A 552 ? 0.6499 0.4912 0.3861 0.0879  0.0380  0.0427  552 LEU A CA  
3901  C C   . LEU A 552 ? 0.6985 0.5124 0.3678 0.1025  0.0194  0.0363  552 LEU A C   
3902  O O   . LEU A 552 ? 0.7367 0.5412 0.3667 0.1236  0.0233  0.0290  552 LEU A O   
3903  C CB  . LEU A 552 ? 0.6275 0.4675 0.3817 0.0811  0.0270  0.0245  552 LEU A CB  
3904  C CG  . LEU A 552 ? 0.6181 0.4375 0.3630 0.0671  -0.0010 0.0118  552 LEU A CG  
3905  C CD1 . LEU A 552 ? 0.5853 0.4139 0.3630 0.0462  -0.0053 0.0189  552 LEU A CD1 
3906  C CD2 . LEU A 552 ? 0.6073 0.4274 0.3654 0.0685  -0.0045 -0.0013 552 LEU A CD2 
3907  N N   . GLU A 553 ? 0.7730 0.5756 0.4320 0.0922  -0.0020 0.0370  553 GLU A N   
3908  C CA  . GLU A 553 ? 0.7846 0.5615 0.3883 0.1025  -0.0275 0.0265  553 GLU A CA  
3909  C C   . GLU A 553 ? 0.7738 0.5304 0.3808 0.0858  -0.0579 0.0084  553 GLU A C   
3910  O O   . GLU A 553 ? 0.7808 0.5166 0.3606 0.0929  -0.0760 -0.0084 553 GLU A O   
3911  C CB  . GLU A 553 ? 0.7903 0.5707 0.3806 0.1060  -0.0322 0.0411  553 GLU A CB  
3912  C CG  . GLU A 553 ? 0.8142 0.6092 0.3927 0.1253  -0.0033 0.0618  553 GLU A CG  
3913  C CD  . GLU A 553 ? 0.8210 0.6228 0.4004 0.1256  -0.0097 0.0760  553 GLU A CD  
3914  O OE1 . GLU A 553 ? 0.8112 0.6051 0.3835 0.1190  -0.0408 0.0637  553 GLU A OE1 
3915  O OE2 . GLU A 553 ? 0.8283 0.6435 0.4196 0.1322  0.0163  0.0998  553 GLU A OE2 
3916  N N   . TYR A 554 ? 0.7198 0.4869 0.3743 0.0620  -0.0602 0.0115  554 TYR A N   
3917  C CA  . TYR A 554 ? 0.7054 0.4563 0.3686 0.0439  -0.0849 0.0010  554 TYR A CA  
3918  C C   . TYR A 554 ? 0.6838 0.4428 0.3847 0.0289  -0.0762 0.0011  554 TYR A C   
3919  O O   . TYR A 554 ? 0.6733 0.4565 0.4120 0.0197  -0.0618 0.0110  554 TYR A O   
3920  C CB  . TYR A 554 ? 0.7030 0.4619 0.3818 0.0323  -0.0985 0.0076  554 TYR A CB  
3921  C CG  . TYR A 554 ? 0.7029 0.4500 0.4000 0.0120  -0.1218 -0.0008 554 TYR A CG  
3922  C CD1 . TYR A 554 ? 0.6870 0.4448 0.4262 -0.0080 -0.1146 0.0039  554 TYR A CD1 
3923  C CD2 . TYR A 554 ? 0.7145 0.4409 0.3888 0.0132  -0.1504 -0.0135 554 TYR A CD2 
3924  C CE1 . TYR A 554 ? 0.6786 0.4274 0.4378 -0.0268 -0.1307 0.0002  554 TYR A CE1 
3925  C CE2 . TYR A 554 ? 0.7105 0.4278 0.4120 -0.0078 -0.1699 -0.0197 554 TYR A CE2 
3926  C CZ  . TYR A 554 ? 0.6950 0.4242 0.4399 -0.0282 -0.1576 -0.0108 554 TYR A CZ  
3927  O OH  . TYR A 554 ? 0.6863 0.4079 0.4613 -0.0493 -0.1720 -0.0133 554 TYR A OH  
3928  N N   . LEU A 555 ? 0.6638 0.4004 0.3519 0.0286  -0.0861 -0.0104 555 LEU A N   
3929  C CA  . LEU A 555 ? 0.6382 0.3779 0.3507 0.0188  -0.0808 -0.0104 555 LEU A CA  
3930  C C   . LEU A 555 ? 0.6473 0.3647 0.3626 0.0019  -0.0982 -0.0126 555 LEU A C   
3931  O O   . LEU A 555 ? 0.6845 0.3709 0.3750 0.0039  -0.1159 -0.0217 555 LEU A O   
3932  C CB  . LEU A 555 ? 0.6504 0.3833 0.3479 0.0358  -0.0744 -0.0184 555 LEU A CB  
3933  C CG  . LEU A 555 ? 0.6220 0.3874 0.3470 0.0432  -0.0524 -0.0144 555 LEU A CG  
3934  C CD1 . LEU A 555 ? 0.6367 0.3969 0.3515 0.0605  -0.0499 -0.0240 555 LEU A CD1 
3935  C CD2 . LEU A 555 ? 0.5938 0.3807 0.3590 0.0269  -0.0471 -0.0089 555 LEU A CD2 
3936  N N   . ASP A 556 ? 0.6205 0.3528 0.3672 -0.0142 -0.0922 -0.0044 556 ASP A N   
3937  C CA  . ASP A 556 ? 0.6267 0.3414 0.3816 -0.0309 -0.1019 -0.0017 556 ASP A CA  
3938  C C   . ASP A 556 ? 0.6122 0.3360 0.3789 -0.0336 -0.0891 0.0039  556 ASP A C   
3939  O O   . ASP A 556 ? 0.5893 0.3407 0.3818 -0.0401 -0.0775 0.0097  556 ASP A O   
3940  C CB  . ASP A 556 ? 0.6218 0.3484 0.4027 -0.0475 -0.1083 0.0039  556 ASP A CB  
3941  C CG  . ASP A 556 ? 0.6437 0.3448 0.4309 -0.0633 -0.1238 0.0036  556 ASP A CG  
3942  O OD1 . ASP A 556 ? 0.6640 0.3388 0.4390 -0.0642 -0.1245 0.0039  556 ASP A OD1 
3943  O OD2 . ASP A 556 ? 0.6474 0.3546 0.4551 -0.0747 -0.1359 0.0035  556 ASP A OD2 
3944  N N   . LEU A 557 ? 0.6190 0.3181 0.3641 -0.0260 -0.0927 0.0011  557 LEU A N   
3945  C CA  . LEU A 557 ? 0.6244 0.3269 0.3702 -0.0243 -0.0845 0.0062  557 LEU A CA  
3946  C C   . LEU A 557 ? 0.6577 0.3283 0.3941 -0.0345 -0.0894 0.0158  557 LEU A C   
3947  O O   . LEU A 557 ? 0.6815 0.3434 0.4042 -0.0279 -0.0853 0.0213  557 LEU A O   
3948  C CB  . LEU A 557 ? 0.6174 0.3215 0.3479 -0.0030 -0.0832 -0.0028 557 LEU A CB  
3949  C CG  . LEU A 557 ? 0.5873 0.3231 0.3336 0.0070  -0.0745 -0.0101 557 LEU A CG  
3950  C CD1 . LEU A 557 ? 0.5891 0.3259 0.3262 0.0278  -0.0744 -0.0193 557 LEU A CD1 
3951  C CD2 . LEU A 557 ? 0.5665 0.3371 0.3454 -0.0012 -0.0630 -0.0072 557 LEU A CD2 
3952  N N   . SER A 558 ? 0.7055 0.3585 0.4508 -0.0499 -0.0986 0.0186  558 SER A N   
3953  C CA  . SER A 558 ? 0.7282 0.3549 0.4747 -0.0598 -0.1020 0.0274  558 SER A CA  
3954  C C   . SER A 558 ? 0.7241 0.3664 0.4913 -0.0734 -0.0856 0.0446  558 SER A C   
3955  O O   . SER A 558 ? 0.7117 0.3809 0.4907 -0.0769 -0.0749 0.0482  558 SER A O   
3956  C CB  . SER A 558 ? 0.7208 0.3401 0.4833 -0.0692 -0.1170 0.0206  558 SER A CB  
3957  O OG  . SER A 558 ? 0.6998 0.3466 0.4954 -0.0841 -0.1162 0.0231  558 SER A OG  
3958  N N   . SER A 559 ? 0.7240 0.3489 0.4964 -0.0800 -0.0820 0.0558  559 SER A N   
3959  C CA  . SER A 559 ? 0.7335 0.3690 0.5218 -0.0903 -0.0627 0.0754  559 SER A CA  
3960  C C   . SER A 559 ? 0.7470 0.3950 0.5087 -0.0780 -0.0501 0.0804  559 SER A C   
3961  O O   . SER A 559 ? 0.7372 0.4118 0.5123 -0.0845 -0.0377 0.0853  559 SER A O   
3962  C CB  . SER A 559 ? 0.7089 0.3713 0.5452 -0.1103 -0.0579 0.0790  559 SER A CB  
3963  O OG  . SER A 559 ? 0.7181 0.3666 0.5806 -0.1214 -0.0690 0.0760  559 SER A OG  
3964  N N   . ASN A 560 ? 0.7095 0.3384 0.4329 -0.0582 -0.0548 0.0774  560 ASN A N   
3965  C CA  . ASN A 560 ? 0.7145 0.3594 0.4121 -0.0406 -0.0484 0.0759  560 ASN A CA  
3966  C C   . ASN A 560 ? 0.7449 0.3639 0.4065 -0.0231 -0.0493 0.0841  560 ASN A C   
3967  O O   . ASN A 560 ? 0.7605 0.3549 0.4253 -0.0279 -0.0491 0.0942  560 ASN A O   
3968  C CB  . ASN A 560 ? 0.6926 0.3652 0.3984 -0.0290 -0.0571 0.0529  560 ASN A CB  
3969  C CG  . ASN A 560 ? 0.6689 0.3822 0.4088 -0.0389 -0.0489 0.0469  560 ASN A CG  
3970  O OD1 . ASN A 560 ? 0.6669 0.4057 0.4101 -0.0351 -0.0383 0.0465  560 ASN A OD1 
3971  N ND2 . ASN A 560 ? 0.6501 0.3676 0.4128 -0.0494 -0.0550 0.0416  560 ASN A ND2 
3972  N N   . ARG A 561 ? 0.7189 0.3498 0.3526 -0.0013 -0.0513 0.0778  561 ARG A N   
3973  C CA  . ARG A 561 ? 0.7466 0.3639 0.3508 0.0194  -0.0536 0.0823  561 ARG A CA  
3974  C C   . ARG A 561 ? 0.7390 0.3614 0.3321 0.0425  -0.0710 0.0618  561 ARG A C   
3975  O O   . ARG A 561 ? 0.7588 0.3882 0.3318 0.0638  -0.0749 0.0586  561 ARG A O   
3976  C CB  . ARG A 561 ? 0.7660 0.4001 0.3500 0.0277  -0.0392 0.0939  561 ARG A CB  
3977  C CG  . ARG A 561 ? 0.7706 0.4091 0.3706 0.0065  -0.0176 0.1142  561 ARG A CG  
3978  C CD  . ARG A 561 ? 0.8068 0.4562 0.3787 0.0196  -0.0013 0.1289  561 ARG A CD  
3979  N NE  . ARG A 561 ? 0.7906 0.4714 0.3443 0.0366  -0.0039 0.1107  561 ARG A NE  
3980  C CZ  . ARG A 561 ? 0.8084 0.5101 0.3447 0.0443  0.0122  0.1161  561 ARG A CZ  
3981  N NH1 . ARG A 561 ? 0.8433 0.5399 0.3772 0.0366  0.0348  0.1427  561 ARG A NH1 
3982  N NH2 . ARG A 561 ? 0.7930 0.5240 0.3185 0.0604  0.0052  0.0926  561 ARG A NH2 
3983  N N   . PHE A 562 ? 0.7388 0.3612 0.3478 0.0397  -0.0811 0.0475  562 PHE A N   
3984  C CA  . PHE A 562 ? 0.7366 0.3631 0.3413 0.0617  -0.0949 0.0301  562 PHE A CA  
3985  C C   . PHE A 562 ? 0.7830 0.3769 0.3675 0.0748  -0.1004 0.0352  562 PHE A C   
3986  O O   . PHE A 562 ? 0.8094 0.3715 0.3920 0.0626  -0.0980 0.0464  562 PHE A O   
3987  C CB  . PHE A 562 ? 0.7057 0.3405 0.3350 0.0555  -0.0983 0.0159  562 PHE A CB  
3988  C CG  . PHE A 562 ? 0.6547 0.3327 0.3190 0.0425  -0.0891 0.0076  562 PHE A CG  
3989  C CD1 . PHE A 562 ? 0.6280 0.3454 0.3095 0.0519  -0.0878 -0.0050 562 PHE A CD1 
3990  C CD2 . PHE A 562 ? 0.6475 0.3251 0.3299 0.0217  -0.0838 0.0115  562 PHE A CD2 
3991  C CE1 . PHE A 562 ? 0.5862 0.3379 0.3024 0.0401  -0.0791 -0.0116 562 PHE A CE1 
3992  C CE2 . PHE A 562 ? 0.6074 0.3215 0.3208 0.0121  -0.0756 0.0059  562 PHE A CE2 
3993  C CZ  . PHE A 562 ? 0.5766 0.3257 0.3070 0.0210  -0.0721 -0.0047 562 PHE A CZ  
3994  N N   . SER A 563 ? 0.7461 0.3504 0.3201 0.0997  -0.1091 0.0258  563 SER A N   
3995  C CA  . SER A 563 ? 0.7966 0.3745 0.3468 0.1141  -0.1123 0.0348  563 SER A CA  
3996  C C   . SER A 563 ? 0.8129 0.3809 0.3591 0.1366  -0.1266 0.0207  563 SER A C   
3997  O O   . SER A 563 ? 0.8590 0.3960 0.3865 0.1451  -0.1296 0.0291  563 SER A O   
3998  C CB  . SER A 563 ? 0.8139 0.4107 0.3475 0.1266  -0.1091 0.0409  563 SER A CB  
3999  O OG  . SER A 563 ? 0.8207 0.4157 0.3487 0.1091  -0.0927 0.0604  563 SER A OG  
4000  N N   . PHE A 564 ? 0.7633 0.3579 0.3284 0.1474  -0.1343 0.0009  564 PHE A N   
4001  C CA  . PHE A 564 ? 0.7801 0.3713 0.3446 0.1717  -0.1463 -0.0128 564 PHE A CA  
4002  C C   . PHE A 564 ? 0.7679 0.3488 0.3420 0.1686  -0.1469 -0.0222 564 PHE A C   
4003  O O   . PHE A 564 ? 0.7500 0.3232 0.3293 0.1475  -0.1399 -0.0180 564 PHE A O   
4004  C CB  . PHE A 564 ? 0.7621 0.3979 0.3445 0.1928  -0.1554 -0.0286 564 PHE A CB  
4005  C CG  . PHE A 564 ? 0.7914 0.4317 0.3563 0.2037  -0.1589 -0.0228 564 PHE A CG  
4006  C CD1 . PHE A 564 ? 0.8400 0.4606 0.3837 0.2246  -0.1678 -0.0208 564 PHE A CD1 
4007  C CD2 . PHE A 564 ? 0.7760 0.4394 0.3425 0.1944  -0.1530 -0.0191 564 PHE A CD2 
4008  C CE1 . PHE A 564 ? 0.8743 0.4978 0.3968 0.2370  -0.1712 -0.0141 564 PHE A CE1 
4009  C CE2 . PHE A 564 ? 0.8104 0.4773 0.3552 0.2074  -0.1559 -0.0141 564 PHE A CE2 
4010  C CZ  . PHE A 564 ? 0.8606 0.5072 0.3821 0.2289  -0.1651 -0.0109 564 PHE A CZ  
4011  N N   . GLU A 565 ? 0.8391 0.4225 0.4157 0.1916  -0.1550 -0.0356 565 GLU A N   
4012  C CA  . GLU A 565 ? 0.8435 0.4140 0.4217 0.1931  -0.1542 -0.0442 565 GLU A CA  
4013  C C   . GLU A 565 ? 0.7985 0.3970 0.4014 0.1859  -0.1452 -0.0521 565 GLU A C   
4014  O O   . GLU A 565 ? 0.7596 0.4011 0.3906 0.1853  -0.1405 -0.0569 565 GLU A O   
4015  C CB  . GLU A 565 ? 0.8677 0.4445 0.4477 0.2208  -0.1620 -0.0562 565 GLU A CB  
4016  C CG  . GLU A 565 ? 0.8470 0.4709 0.4533 0.2414  -0.1670 -0.0671 565 GLU A CG  
4017  C CD  . GLU A 565 ? 0.8792 0.4961 0.4690 0.2532  -0.1776 -0.0621 565 GLU A CD  
4018  O OE1 . GLU A 565 ? 0.9073 0.4882 0.4686 0.2408  -0.1756 -0.0457 565 GLU A OE1 
4019  O OE2 . GLU A 565 ? 0.8816 0.5323 0.4908 0.2744  -0.1869 -0.0741 565 GLU A OE2 
4020  N N   . ILE A 566 ? 0.8355 0.4189 0.4335 0.1761  -0.1407 -0.0544 566 ILE A N   
4021  C CA  . ILE A 566 ? 0.8002 0.4114 0.4187 0.1682  -0.1281 -0.0613 566 ILE A CA  
4022  C C   . ILE A 566 ? 0.7850 0.4406 0.4324 0.1893  -0.1200 -0.0747 566 ILE A C   
4023  O O   . ILE A 566 ? 0.8148 0.4714 0.4611 0.2107  -0.1253 -0.0807 566 ILE A O   
4024  C CB  . ILE A 566 ? 0.8207 0.4088 0.4242 0.1597  -0.1286 -0.0614 566 ILE A CB  
4025  C CG1 . ILE A 566 ? 0.8333 0.3873 0.4233 0.1344  -0.1353 -0.0497 566 ILE A CG1 
4026  C CG2 . ILE A 566 ? 0.7945 0.4129 0.4128 0.1582  -0.1146 -0.0678 566 ILE A CG2 
4027  C CD1 . ILE A 566 ? 0.8526 0.3887 0.4351 0.1253  -0.1398 -0.0528 566 ILE A CD1 
4028  N N   . PRO A 567 ? 0.7554 0.4536 0.4355 0.1818  -0.1060 -0.0782 567 PRO A N   
4029  C CA  . PRO A 567 ? 0.7412 0.4857 0.4595 0.1990  -0.0946 -0.0889 567 PRO A CA  
4030  C C   . PRO A 567 ? 0.7649 0.5010 0.4693 0.2163  -0.0867 -0.0952 567 PRO A C   
4031  O O   . PRO A 567 ? 0.7713 0.4946 0.4563 0.2080  -0.0785 -0.0922 567 PRO A O   
4032  C CB  . PRO A 567 ? 0.7065 0.4924 0.4627 0.1781  -0.0778 -0.0844 567 PRO A CB  
4033  C CG  . PRO A 567 ? 0.6948 0.4648 0.4382 0.1545  -0.0857 -0.0743 567 PRO A CG  
4034  C CD  . PRO A 567 ? 0.7224 0.4361 0.4161 0.1539  -0.0983 -0.0689 567 PRO A CD  
4035  N N   . PRO A 568 ? 0.7733 0.5224 0.4891 0.2390  -0.0895 -0.1026 568 PRO A N   
4036  C CA  . PRO A 568 ? 0.8006 0.5507 0.5077 0.2547  -0.0789 -0.1079 568 PRO A CA  
4037  C C   . PRO A 568 ? 0.7804 0.5729 0.5176 0.2592  -0.0514 -0.1103 568 PRO A C   
4038  O O   . PRO A 568 ? 0.8088 0.6030 0.5336 0.2725  -0.0385 -0.1131 568 PRO A O   
4039  C CB  . PRO A 568 ? 0.8249 0.5810 0.5419 0.2770  -0.0895 -0.1149 568 PRO A CB  
4040  C CG  . PRO A 568 ? 0.8035 0.5770 0.5452 0.2753  -0.1027 -0.1146 568 PRO A CG  
4041  C CD  . PRO A 568 ? 0.7664 0.5417 0.5124 0.2526  -0.0998 -0.1084 568 PRO A CD  
4042  N N   . THR A 569 ? 0.7651 0.5912 0.5415 0.2496  -0.0410 -0.1086 569 THR A N   
4043  C CA  . THR A 569 ? 0.7482 0.6186 0.5625 0.2487  -0.0115 -0.1046 569 THR A CA  
4044  C C   . THR A 569 ? 0.7549 0.6116 0.5430 0.2291  -0.0004 -0.0921 569 THR A C   
4045  O O   . THR A 569 ? 0.7536 0.6442 0.5715 0.2239  0.0250  -0.0828 569 THR A O   
4046  C CB  . THR A 569 ? 0.7239 0.6473 0.6113 0.2383  -0.0079 -0.1048 569 THR A CB  
4047  O OG1 . THR A 569 ? 0.7284 0.6895 0.6565 0.2282  0.0219  -0.0949 569 THR A OG1 
4048  C CG2 . THR A 569 ? 0.7087 0.6193 0.5932 0.2155  -0.0295 -0.1021 569 THR A CG2 
4049  N N   . LEU A 570 ? 0.7935 0.6020 0.5302 0.2183  -0.0188 -0.0906 570 LEU A N   
4050  C CA  . LEU A 570 ? 0.7970 0.5924 0.5088 0.2015  -0.0134 -0.0805 570 LEU A CA  
4051  C C   . LEU A 570 ? 0.8338 0.6091 0.4983 0.2227  -0.0054 -0.0860 570 LEU A C   
4052  O O   . LEU A 570 ? 0.8600 0.5985 0.4867 0.2188  -0.0249 -0.0880 570 LEU A O   
4053  C CB  . LEU A 570 ? 0.7842 0.5429 0.4724 0.1794  -0.0371 -0.0774 570 LEU A CB  
4054  C CG  . LEU A 570 ? 0.7647 0.5441 0.4891 0.1542  -0.0392 -0.0681 570 LEU A CG  
4055  C CD1 . LEU A 570 ? 0.7491 0.4907 0.4462 0.1358  -0.0588 -0.0639 570 LEU A CD1 
4056  C CD2 . LEU A 570 ? 0.7603 0.5736 0.5145 0.1423  -0.0183 -0.0575 570 LEU A CD2 
4057  N N   . ASN A 571 ? 0.8171 0.6282 0.4994 0.2382  0.0235  -0.0820 571 ASN A N   
4058  C CA  . ASN A 571 ? 0.8584 0.6617 0.5017 0.2556  0.0331  -0.0821 571 ASN A CA  
4059  C C   . ASN A 571 ? 0.8645 0.6975 0.5117 0.2601  0.0669  -0.0671 571 ASN A C   
4060  O O   . ASN A 571 ? 0.8996 0.7411 0.5282 0.2783  0.0831  -0.0641 571 ASN A O   
4061  C CB  . ASN A 571 ? 0.8855 0.6976 0.5367 0.2780  0.0353  -0.0920 571 ASN A CB  
4062  C CG  . ASN A 571 ? 0.8585 0.7182 0.5749 0.2845  0.0530  -0.0924 571 ASN A CG  
4063  O OD1 . ASN A 571 ? 0.8225 0.7192 0.5813 0.2785  0.0766  -0.0822 571 ASN A OD1 
4064  N ND2 . ASN A 571 ? 0.8731 0.7336 0.6038 0.2966  0.0406  -0.1034 571 ASN A ND2 
4065  N N   . ASN A 572 ? 0.8434 0.6953 0.5228 0.2381  0.0756  -0.0522 572 ASN A N   
4066  C CA  . ASN A 572 ? 0.8423 0.7255 0.5391 0.2382  0.1095  -0.0313 572 ASN A CA  
4067  C C   . ASN A 572 ? 0.8400 0.7111 0.5252 0.2153  0.1021  -0.0169 572 ASN A C   
4068  O O   . ASN A 572 ? 0.8281 0.7265 0.5602 0.1994  0.1202  0.0011  572 ASN A O   
4069  C CB  . ASN A 572 ? 0.8238 0.7586 0.6047 0.2328  0.1346  -0.0230 572 ASN A CB  
4070  C CG  . ASN A 572 ? 0.8268 0.7928 0.6267 0.2398  0.1770  0.0000  572 ASN A CG  
4071  O OD1 . ASN A 572 ? 0.8501 0.8163 0.6121 0.2658  0.1975  0.0031  572 ASN A OD1 
4072  N ND2 . ASN A 572 ? 0.8020 0.7925 0.6610 0.2161  0.1903  0.0173  572 ASN A ND2 
4073  N N   . LEU A 573 ? 0.8285 0.6584 0.4567 0.2130  0.0742  -0.0256 573 LEU A N   
4074  C CA  . LEU A 573 ? 0.8239 0.6439 0.4407 0.1943  0.0651  -0.0134 573 LEU A CA  
4075  C C   . LEU A 573 ? 0.8625 0.6632 0.4103 0.2149  0.0667  -0.0111 573 LEU A C   
4076  O O   . LEU A 573 ? 0.8835 0.6547 0.4037 0.2113  0.0347  -0.0238 573 LEU A O   
4077  C CB  . LEU A 573 ? 0.8001 0.5936 0.4171 0.1715  0.0300  -0.0240 573 LEU A CB  
4078  C CG  . LEU A 573 ? 0.7739 0.5820 0.4462 0.1538  0.0246  -0.0271 573 LEU A CG  
4079  C CD1 . LEU A 573 ? 0.7537 0.5360 0.4203 0.1322  -0.0042 -0.0318 573 LEU A CD1 
4080  C CD2 . LEU A 573 ? 0.7697 0.6190 0.5034 0.1421  0.0483  -0.0118 573 LEU A CD2 
4081  N N   . PRO A 574 ? 0.8547 0.6795 0.4036 0.2284  0.0988  0.0085  574 PRO A N   
4082  C CA  . PRO A 574 ? 0.9069 0.7210 0.4117 0.2456  0.0951  0.0110  574 PRO A CA  
4083  C C   . PRO A 574 ? 0.9139 0.7107 0.3964 0.2345  0.0717  0.0144  574 PRO A C   
4084  O O   . PRO A 574 ? 0.9627 0.7484 0.4074 0.2497  0.0629  0.0109  574 PRO A O   
4085  C CB  . PRO A 574 ? 0.9213 0.7685 0.4436 0.2598  0.1392  0.0355  574 PRO A CB  
4086  C CG  . PRO A 574 ? 0.8660 0.7383 0.4468 0.2398  0.1613  0.0526  574 PRO A CG  
4087  C CD  . PRO A 574 ? 0.8345 0.6996 0.4427 0.2230  0.1368  0.0308  574 PRO A CD  
4088  N N   . ARG A 575 ? 0.9236 0.7195 0.4298 0.2099  0.0610  0.0200  575 ARG A N   
4089  C CA  . ARG A 575 ? 0.9290 0.7140 0.4239 0.1986  0.0385  0.0229  575 ARG A CA  
4090  C C   . ARG A 575 ? 0.9057 0.6697 0.4097 0.1763  0.0020  0.0050  575 ARG A C   
4091  O O   . ARG A 575 ? 0.9003 0.6583 0.4024 0.1655  -0.0183 0.0052  575 ARG A O   
4092  C CB  . ARG A 575 ? 0.9044 0.7100 0.4256 0.1892  0.0603  0.0515  575 ARG A CB  
4093  C CG  . ARG A 575 ? 0.9328 0.7581 0.4521 0.2084  0.0973  0.0741  575 ARG A CG  
4094  C CD  . ARG A 575 ? 0.9142 0.7561 0.4713 0.1959  0.1180  0.1035  575 ARG A CD  
4095  N NE  . ARG A 575 ? 0.9415 0.8047 0.5180 0.2086  0.1593  0.1273  575 ARG A NE  
4096  C CZ  . ARG A 575 ? 0.9157 0.8013 0.5433 0.2034  0.1903  0.1367  575 ARG A CZ  
4097  N NH1 . ARG A 575 ? 0.8832 0.7736 0.5431 0.1883  0.1860  0.1237  575 ARG A NH1 
4098  N NH2 . ARG A 575 ? 0.9324 0.8374 0.5844 0.2130  0.2258  0.1586  575 ARG A NH2 
4099  N N   . LEU A 576 ? 0.8939 0.6481 0.4112 0.1696  -0.0059 -0.0092 576 LEU A N   
4100  C CA  . LEU A 576 ? 0.8706 0.6047 0.4023 0.1474  -0.0365 -0.0222 576 LEU A CA  
4101  C C   . LEU A 576 ? 0.9108 0.6205 0.4203 0.1517  -0.0633 -0.0391 576 LEU A C   
4102  O O   . LEU A 576 ? 0.9435 0.6409 0.4316 0.1700  -0.0647 -0.0511 576 LEU A O   
4103  C CB  . LEU A 576 ? 0.8418 0.5709 0.3923 0.1421  -0.0360 -0.0307 576 LEU A CB  
4104  C CG  . LEU A 576 ? 0.8143 0.5275 0.3876 0.1165  -0.0595 -0.0362 576 LEU A CG  
4105  C CD1 . LEU A 576 ? 0.7854 0.5227 0.4000 0.0957  -0.0502 -0.0211 576 LEU A CD1 
4106  C CD2 . LEU A 576 ? 0.8214 0.5192 0.4014 0.1188  -0.0657 -0.0478 576 LEU A CD2 
4107  N N   . TYR A 577 ? 0.8814 0.5850 0.3976 0.1358  -0.0848 -0.0401 577 TYR A N   
4108  C CA  . TYR A 577 ? 0.9187 0.5986 0.4219 0.1361  -0.1131 -0.0572 577 TYR A CA  
4109  C C   . TYR A 577 ? 0.8966 0.5599 0.4299 0.1101  -0.1351 -0.0631 577 TYR A C   
4110  O O   . TYR A 577 ? 0.9276 0.5699 0.4577 0.1072  -0.1592 -0.0764 577 TYR A O   
4111  C CB  . TYR A 577 ? 0.9496 0.6366 0.4328 0.1441  -0.1220 -0.0553 577 TYR A CB  
4112  C CG  . TYR A 577 ? 0.9171 0.6194 0.4249 0.1249  -0.1285 -0.0430 577 TYR A CG  
4113  C CD1 . TYR A 577 ? 0.9106 0.6029 0.4411 0.1048  -0.1561 -0.0516 577 TYR A CD1 
4114  C CD2 . TYR A 577 ? 0.8967 0.6236 0.4081 0.1277  -0.1063 -0.0213 577 TYR A CD2 
4115  C CE1 . TYR A 577 ? 0.8830 0.5915 0.4382 0.0891  -0.1627 -0.0405 577 TYR A CE1 
4116  C CE2 . TYR A 577 ? 0.8701 0.6103 0.4050 0.1125  -0.1131 -0.0092 577 TYR A CE2 
4117  C CZ  . TYR A 577 ? 0.8628 0.5948 0.4186 0.0940  -0.1420 -0.0196 577 TYR A CZ  
4118  O OH  . TYR A 577 ? 0.8382 0.5852 0.4197 0.0807  -0.1494 -0.0077 577 TYR A OH  
4119  N N   . TYR A 578 ? 0.8473 0.5191 0.4098 0.0918  -0.1269 -0.0531 578 TYR A N   
4120  C CA  . TYR A 578 ? 0.8285 0.4865 0.4194 0.0672  -0.1429 -0.0544 578 TYR A CA  
4121  C C   . TYR A 578 ? 0.7989 0.4574 0.4047 0.0611  -0.1293 -0.0492 578 TYR A C   
4122  O O   . TYR A 578 ? 0.7727 0.4528 0.3824 0.0650  -0.1095 -0.0404 578 TYR A O   
4123  C CB  . TYR A 578 ? 0.8053 0.4777 0.4186 0.0479  -0.1514 -0.0458 578 TYR A CB  
4124  C CG  . TYR A 578 ? 0.7931 0.4534 0.4380 0.0220  -0.1674 -0.0461 578 TYR A CG  
4125  C CD1 . TYR A 578 ? 0.7574 0.4217 0.4245 0.0056  -0.1572 -0.0368 578 TYR A CD1 
4126  C CD2 . TYR A 578 ? 0.8211 0.4684 0.4759 0.0140  -0.1914 -0.0552 578 TYR A CD2 
4127  C CE1 . TYR A 578 ? 0.7504 0.4061 0.4477 -0.0176 -0.1666 -0.0338 578 TYR A CE1 
4128  C CE2 . TYR A 578 ? 0.8116 0.4524 0.5027 -0.0106 -0.2015 -0.0523 578 TYR A CE2 
4129  C CZ  . TYR A 578 ? 0.7762 0.4218 0.4880 -0.0262 -0.1870 -0.0400 578 TYR A CZ  
4130  O OH  . TYR A 578 ? 0.7696 0.4134 0.5197 -0.0493 -0.1906 -0.0336 578 TYR A OH  
4131  N N   . MET A 579 ? 0.8200 0.4548 0.4343 0.0525  -0.1404 -0.0536 579 MET A N   
4132  C CA  . MET A 579 ? 0.7974 0.4307 0.4237 0.0476  -0.1308 -0.0483 579 MET A CA  
4133  C C   . MET A 579 ? 0.8116 0.4195 0.4509 0.0298  -0.1458 -0.0467 579 MET A C   
4134  O O   . MET A 579 ? 0.8567 0.4393 0.4858 0.0353  -0.1587 -0.0542 579 MET A O   
4135  C CB  . MET A 579 ? 0.8140 0.4458 0.4237 0.0714  -0.1202 -0.0544 579 MET A CB  
4136  C CG  . MET A 579 ? 0.7974 0.4249 0.4174 0.0699  -0.1157 -0.0513 579 MET A CG  
4137  S SD  . MET A 579 ? 0.8183 0.4471 0.4240 0.0997  -0.1067 -0.0600 579 MET A SD  
4138  C CE  . MET A 579 ? 0.7843 0.4555 0.4016 0.1077  -0.0820 -0.0573 579 MET A CE  
4139  N N   . ASN A 580 ? 0.7991 0.4146 0.4617 0.0088  -0.1429 -0.0363 580 ASN A N   
4140  C CA  . ASN A 580 ? 0.8087 0.4061 0.4883 -0.0095 -0.1503 -0.0298 580 ASN A CA  
4141  C C   . ASN A 580 ? 0.7981 0.3947 0.4787 -0.0101 -0.1371 -0.0209 580 ASN A C   
4142  O O   . ASN A 580 ? 0.7709 0.3888 0.4637 -0.0158 -0.1249 -0.0146 580 ASN A O   
4143  C CB  . ASN A 580 ? 0.7946 0.4057 0.5061 -0.0327 -0.1556 -0.0234 580 ASN A CB  
4144  C CG  . ASN A 580 ? 0.8170 0.4138 0.5531 -0.0501 -0.1621 -0.0177 580 ASN A CG  
4145  O OD1 . ASN A 580 ? 0.8473 0.4220 0.5748 -0.0471 -0.1604 -0.0154 580 ASN A OD1 
4146  N ND2 . ASN A 580 ? 0.8090 0.4198 0.5791 -0.0678 -0.1688 -0.0151 580 ASN A ND2 
4147  N N   . LEU A 581 ? 0.7848 0.3565 0.4523 -0.0024 -0.1406 -0.0210 581 LEU A N   
4148  C CA  . LEU A 581 ? 0.7822 0.3487 0.4443 0.0016  -0.1315 -0.0128 581 LEU A CA  
4149  C C   . LEU A 581 ? 0.8083 0.3537 0.4789 -0.0117 -0.1331 -0.0010 581 LEU A C   
4150  O O   . LEU A 581 ? 0.8264 0.3569 0.4833 -0.0028 -0.1296 0.0050  581 LEU A O   
4151  C CB  . LEU A 581 ? 0.7954 0.3555 0.4336 0.0285  -0.1314 -0.0224 581 LEU A CB  
4152  C CG  . LEU A 581 ? 0.7774 0.3630 0.4125 0.0454  -0.1251 -0.0337 581 LEU A CG  
4153  C CD1 . LEU A 581 ? 0.7898 0.3758 0.4128 0.0712  -0.1224 -0.0409 581 LEU A CD1 
4154  C CD2 . LEU A 581 ? 0.7327 0.3550 0.3877 0.0369  -0.1121 -0.0302 581 LEU A CD2 
4155  N N   . SER A 582 ? 0.8414 0.3870 0.5377 -0.0319 -0.1376 0.0029  582 SER A N   
4156  C CA  . SER A 582 ? 0.8732 0.3976 0.5856 -0.0449 -0.1377 0.0134  582 SER A CA  
4157  C C   . SER A 582 ? 0.8625 0.3976 0.5867 -0.0546 -0.1187 0.0341  582 SER A C   
4158  O O   . SER A 582 ? 0.8272 0.3899 0.5542 -0.0560 -0.1079 0.0386  582 SER A O   
4159  C CB  . SER A 582 ? 0.8840 0.4087 0.6280 -0.0624 -0.1489 0.0087  582 SER A CB  
4160  O OG  . SER A 582 ? 0.8970 0.4192 0.6757 -0.0824 -0.1392 0.0247  582 SER A OG  
4161  N N   . ARG A 583 ? 0.8943 0.4058 0.6247 -0.0598 -0.1135 0.0475  583 ARG A N   
4162  C CA  . ARG A 583 ? 0.8977 0.4159 0.6368 -0.0669 -0.0930 0.0708  583 ARG A CA  
4163  C C   . ARG A 583 ? 0.8774 0.4076 0.5825 -0.0485 -0.0848 0.0740  583 ARG A C   
4164  O O   . ARG A 583 ? 0.8483 0.4066 0.5574 -0.0518 -0.0728 0.0800  583 ARG A O   
4165  C CB  . ARG A 583 ? 0.8711 0.4179 0.6527 -0.0893 -0.0825 0.0791  583 ARG A CB  
4166  C CG  . ARG A 583 ? 0.8912 0.4264 0.7128 -0.1073 -0.0900 0.0769  583 ARG A CG  
4167  C CD  . ARG A 583 ? 0.8602 0.4300 0.7254 -0.1258 -0.0860 0.0768  583 ARG A CD  
4168  N NE  . ARG A 583 ? 0.8948 0.4548 0.8020 -0.1431 -0.0936 0.0732  583 ARG A NE  
4169  C CZ  . ARG A 583 ? 0.9068 0.4490 0.8134 -0.1418 -0.1182 0.0532  583 ARG A CZ  
4170  N NH1 . ARG A 583 ? 0.9018 0.4351 0.7675 -0.1231 -0.1355 0.0362  583 ARG A NH1 
4171  N NH2 . ARG A 583 ? 0.9366 0.4702 0.8844 -0.1588 -0.1248 0.0495  583 ARG A NH2 
4172  N N   . ASN A 584 ? 0.8720 0.3809 0.5450 -0.0274 -0.0926 0.0681  584 ASN A N   
4173  C CA  . ASN A 584 ? 0.8649 0.3846 0.5078 -0.0058 -0.0897 0.0669  584 ASN A CA  
4174  C C   . ASN A 584 ? 0.9155 0.4061 0.5337 0.0122  -0.0932 0.0726  584 ASN A C   
4175  O O   . ASN A 584 ? 0.9604 0.4217 0.5863 0.0050  -0.0937 0.0822  584 ASN A O   
4176  C CB  . ASN A 584 ? 0.8424 0.3798 0.4793 0.0060  -0.0993 0.0456  584 ASN A CB  
4177  C CG  . ASN A 584 ? 0.8145 0.3843 0.4707 -0.0066 -0.0922 0.0447  584 ASN A CG  
4178  O OD1 . ASN A 584 ? 0.8130 0.4050 0.4639 -0.0011 -0.0840 0.0487  584 ASN A OD1 
4179  N ND2 . ASN A 584 ? 0.7945 0.3688 0.4729 -0.0219 -0.0968 0.0384  584 ASN A ND2 
4180  N N   . ASP A 585 ? 0.9254 0.4250 0.5180 0.0363  -0.0965 0.0663  585 ASP A N   
4181  C CA  . ASP A 585 ? 0.9721 0.4495 0.5406 0.0565  -0.1001 0.0723  585 ASP A CA  
4182  C C   . ASP A 585 ? 0.9742 0.4505 0.5296 0.0809  -0.1154 0.0509  585 ASP A C   
4183  O O   . ASP A 585 ? 1.0046 0.4800 0.5410 0.1034  -0.1196 0.0509  585 ASP A O   
4184  C CB  . ASP A 585 ? 0.9838 0.4770 0.5343 0.0667  -0.0895 0.0874  585 ASP A CB  
4185  C CG  . ASP A 585 ? 1.0287 0.5070 0.5830 0.0521  -0.0729 0.1163  585 ASP A CG  
4186  O OD1 . ASP A 585 ? 1.0298 0.4979 0.6129 0.0280  -0.0673 0.1234  585 ASP A OD1 
4187  O OD2 . ASP A 585 ? 1.0720 0.5509 0.6027 0.0656  -0.0654 0.1320  585 ASP A OD2 
4188  N N   . LEU A 586 ? 0.9477 0.4261 0.5136 0.0785  -0.1234 0.0330  586 LEU A N   
4189  C CA  . LEU A 586 ? 0.9491 0.4304 0.5061 0.1032  -0.1345 0.0139  586 LEU A CA  
4190  C C   . LEU A 586 ? 1.0027 0.4478 0.5447 0.1154  -0.1424 0.0154  586 LEU A C   
4191  O O   . LEU A 586 ? 1.0313 0.4459 0.5776 0.1011  -0.1435 0.0222  586 LEU A O   
4192  C CB  . LEU A 586 ? 0.9193 0.4125 0.4882 0.0995  -0.1376 -0.0025 586 LEU A CB  
4193  C CG  . LEU A 586 ? 0.8803 0.4033 0.4668 0.0839  -0.1292 -0.0008 586 LEU A CG  
4194  C CD1 . LEU A 586 ? 0.8714 0.3849 0.4717 0.0562  -0.1269 0.0055  586 LEU A CD1 
4195  C CD2 . LEU A 586 ? 0.8475 0.3976 0.4429 0.0979  -0.1294 -0.0163 586 LEU A CD2 
4196  N N   . ASP A 587 ? 1.0253 0.4754 0.5546 0.1426  -0.1488 0.0083  587 ASP A N   
4197  C CA  . ASP A 587 ? 1.0810 0.4997 0.5934 0.1560  -0.1536 0.0176  587 ASP A CA  
4198  C C   . ASP A 587 ? 1.1045 0.5141 0.6107 0.1804  -0.1655 0.0007  587 ASP A C   
4199  O O   . ASP A 587 ? 1.1586 0.5528 0.6511 0.1993  -0.1710 0.0053  587 ASP A O   
4200  C CB  . ASP A 587 ? 1.0965 0.5291 0.5959 0.1682  -0.1502 0.0299  587 ASP A CB  
4201  C CG  . ASP A 587 ? 1.0601 0.5369 0.5659 0.1877  -0.1557 0.0123  587 ASP A CG  
4202  O OD1 . ASP A 587 ? 1.0169 0.5157 0.5406 0.1877  -0.1576 -0.0049 587 ASP A OD1 
4203  O OD2 . ASP A 587 ? 1.0776 0.5685 0.5728 0.2037  -0.1584 0.0159  587 ASP A OD2 
4204  N N   . GLN A 588 ? 1.0851 0.5053 0.6005 0.1822  -0.1687 -0.0175 588 GLN A N   
4205  C CA  . GLN A 588 ? 1.1102 0.5269 0.6214 0.2071  -0.1773 -0.0328 588 GLN A CA  
4206  C C   . GLN A 588 ? 1.1162 0.5250 0.6315 0.2005  -0.1789 -0.0452 588 GLN A C   
4207  O O   . GLN A 588 ? 1.1070 0.5052 0.6272 0.1763  -0.1767 -0.0410 588 GLN A O   
4208  C CB  . GLN A 588 ? 1.0830 0.5447 0.6046 0.2311  -0.1783 -0.0449 588 GLN A CB  
4209  C CG  . GLN A 588 ? 1.1203 0.5773 0.6325 0.2552  -0.1866 -0.0428 588 GLN A CG  
4210  C CD  . GLN A 588 ? 1.0929 0.6008 0.6242 0.2752  -0.1896 -0.0543 588 GLN A CD  
4211  O OE1 . GLN A 588 ? 1.0781 0.6042 0.6105 0.2740  -0.1900 -0.0486 588 GLN A OE1 
4212  N NE2 . GLN A 588 ? 1.0844 0.6189 0.6351 0.2937  -0.1912 -0.0708 588 GLN A NE2 
4213  N N   . THR A 589 ? 1.0845 0.5010 0.5990 0.2235  -0.1828 -0.0608 589 THR A N   
4214  C CA  . THR A 589 ? 1.0967 0.5046 0.6097 0.2233  -0.1847 -0.0734 589 THR A CA  
4215  C C   . THR A 589 ? 1.0464 0.4928 0.5720 0.2161  -0.1748 -0.0790 589 THR A C   
4216  O O   . THR A 589 ? 1.0046 0.4912 0.5453 0.2215  -0.1658 -0.0790 589 THR A O   
4217  C CB  . THR A 589 ? 1.1324 0.5381 0.6404 0.2528  -0.1891 -0.0874 589 THR A CB  
4218  O OG1 . THR A 589 ? 1.0974 0.5536 0.6216 0.2713  -0.1801 -0.0956 589 THR A OG1 
4219  C CG2 . THR A 589 ? 1.1806 0.5533 0.6784 0.2641  -0.1980 -0.0803 589 THR A CG2 
4220  N N   . ILE A 590 ? 1.0510 0.4845 0.5728 0.2043  -0.1770 -0.0840 590 ILE A N   
4221  C CA  . ILE A 590 ? 1.0136 0.4791 0.5439 0.1993  -0.1673 -0.0884 590 ILE A CA  
4222  C C   . ILE A 590 ? 1.0059 0.5066 0.5419 0.2260  -0.1562 -0.0995 590 ILE A C   
4223  O O   . ILE A 590 ? 1.0458 0.5350 0.5710 0.2462  -0.1599 -0.1104 590 ILE A O   
4224  C CB  . ILE A 590 ? 1.0363 0.4793 0.5587 0.1867  -0.1754 -0.0941 590 ILE A CB  
4225  C CG1 . ILE A 590 ? 1.0505 0.4596 0.5770 0.1600  -0.1857 -0.0838 590 ILE A CG1 
4226  C CG2 . ILE A 590 ? 1.0004 0.4755 0.5293 0.1814  -0.1651 -0.0958 590 ILE A CG2 
4227  C CD1 . ILE A 590 ? 1.0845 0.4677 0.6097 0.1492  -0.1986 -0.0927 590 ILE A CD1 
4228  N N   . PRO A 591 ? 1.0086 0.5527 0.5649 0.2268  -0.1412 -0.0976 591 PRO A N   
4229  C CA  . PRO A 591 ? 1.0022 0.5843 0.5725 0.2506  -0.1268 -0.1073 591 PRO A CA  
4230  C C   . PRO A 591 ? 1.0237 0.6079 0.5795 0.2594  -0.1188 -0.1162 591 PRO A C   
4231  O O   . PRO A 591 ? 1.0226 0.5958 0.5663 0.2449  -0.1203 -0.1142 591 PRO A O   
4232  C CB  . PRO A 591 ? 0.9471 0.5722 0.5479 0.2432  -0.1128 -0.1023 591 PRO A CB  
4233  C CG  . PRO A 591 ? 0.9260 0.5361 0.5209 0.2155  -0.1164 -0.0921 591 PRO A CG  
4234  C CD  . PRO A 591 ? 0.9618 0.5230 0.5331 0.2055  -0.1353 -0.0871 591 PRO A CD  
4235  N N   . GLU A 592 ? 1.2457 0.6333 0.6521 0.2151  -0.0644 -0.2104 592 GLU A N   
4236  C CA  . GLU A 592 ? 1.2703 0.6557 0.6627 0.2213  -0.0602 -0.2193 592 GLU A CA  
4237  C C   . GLU A 592 ? 1.2385 0.6594 0.6380 0.2181  -0.0446 -0.2161 592 GLU A C   
4238  O O   . GLU A 592 ? 1.2594 0.6754 0.6419 0.2185  -0.0444 -0.2215 592 GLU A O   
4239  C CB  . GLU A 592 ? 1.2916 0.6749 0.6887 0.2383  -0.0530 -0.2284 592 GLU A CB  
4240  C CG  . GLU A 592 ? 1.3312 0.7008 0.7082 0.2449  -0.0532 -0.2401 592 GLU A CG  
4241  C CD  . GLU A 592 ? 1.3295 0.7226 0.7194 0.2585  -0.0342 -0.2476 592 GLU A CD  
4242  O OE1 . GLU A 592 ? 1.2923 0.7169 0.7093 0.2611  -0.0198 -0.2428 592 GLU A OE1 
4243  O OE2 . GLU A 592 ? 1.3660 0.7467 0.7401 0.2657  -0.0338 -0.2590 592 GLU A OE2 
4244  N N   . GLY A 593 ? 1.1430 0.5985 0.5669 0.2148  -0.0323 -0.2074 593 GLY A N   
4245  C CA  . GLY A 593 ? 1.1128 0.6015 0.5452 0.2111  -0.0183 -0.2034 593 GLY A CA  
4246  C C   . GLY A 593 ? 1.1143 0.5965 0.5313 0.1980  -0.0286 -0.2008 593 GLY A C   
4247  O O   . GLY A 593 ? 1.1023 0.6038 0.5190 0.1961  -0.0200 -0.1993 593 GLY A O   
4248  N N   . LEU A 594 ? 1.1190 0.5740 0.5239 0.1880  -0.0473 -0.2005 594 LEU A N   
4249  C CA  . LEU A 594 ? 1.1225 0.5718 0.5152 0.1743  -0.0588 -0.1994 594 LEU A CA  
4250  C C   . LEU A 594 ? 1.1613 0.5933 0.5298 0.1785  -0.0628 -0.2073 594 LEU A C   
4251  O O   . LEU A 594 ? 1.1571 0.5982 0.5194 0.1723  -0.0638 -0.2063 594 LEU A O   
4252  C CB  . LEU A 594 ? 1.1333 0.5576 0.5209 0.1606  -0.0782 -0.1978 594 LEU A CB  
4253  C CG  . LEU A 594 ? 1.0919 0.5386 0.4977 0.1462  -0.0786 -0.1897 594 LEU A CG  
4254  C CD1 . LEU A 594 ? 1.0507 0.5294 0.4814 0.1540  -0.0611 -0.1841 594 LEU A CD1 
4255  C CD2 . LEU A 594 ? 1.1085 0.5279 0.5082 0.1310  -0.0977 -0.1886 594 LEU A CD2 
4256  N N   . THR A 595 ? 1.2162 0.6233 0.5707 0.1891  -0.0659 -0.2156 595 THR A N   
4257  C CA  . THR A 595 ? 1.2565 0.6465 0.5868 0.1941  -0.0696 -0.2245 595 THR A CA  
4258  C C   . THR A 595 ? 1.2467 0.6628 0.5772 0.2015  -0.0512 -0.2251 595 THR A C   
4259  O O   . THR A 595 ? 1.2774 0.6827 0.5862 0.2040  -0.0536 -0.2313 595 THR A O   
4260  C CB  . THR A 595 ? 1.3002 0.6595 0.6181 0.2045  -0.0766 -0.2343 595 THR A CB  
4261  O OG1 . THR A 595 ? 1.2935 0.6694 0.6236 0.2187  -0.0593 -0.2372 595 THR A OG1 
4262  C CG2 . THR A 595 ? 1.3083 0.6422 0.6287 0.1976  -0.0931 -0.2319 595 THR A CG2 
4263  N N   . LYS A 596 ? 1.2044 0.6538 0.5587 0.2045  -0.0334 -0.2188 596 LYS A N   
4264  C CA  . LYS A 596 ? 1.1955 0.6696 0.5515 0.2096  -0.0157 -0.2184 596 LYS A CA  
4265  C C   . LYS A 596 ? 1.1733 0.6639 0.5287 0.1996  -0.0155 -0.2109 596 LYS A C   
4266  O O   . LYS A 596 ? 1.1719 0.6783 0.5237 0.2024  -0.0032 -0.2101 596 LYS A O   
4267  C CB  . LYS A 596 ? 1.1636 0.6673 0.5482 0.2163  0.0032  -0.2155 596 LYS A CB  
4268  C CG  . LYS A 596 ? 1.1807 0.6716 0.5711 0.2265  0.0029  -0.2224 596 LYS A CG  
4269  C CD  . LYS A 596 ? 1.1466 0.6705 0.5689 0.2319  0.0213  -0.2196 596 LYS A CD  
4270  C CE  . LYS A 596 ? 1.1548 0.6672 0.5883 0.2399  0.0174  -0.2238 596 LYS A CE  
4271  N NZ  . LYS A 596 ? 1.1185 0.6647 0.5865 0.2438  0.0337  -0.2206 596 LYS A NZ  
4272  N N   . LEU A 597 ? 1.1543 0.6413 0.5132 0.1876  -0.0291 -0.2059 597 LEU A N   
4273  C CA  . LEU A 597 ? 1.1391 0.6381 0.4961 0.1778  -0.0327 -0.2006 597 LEU A CA  
4274  C C   . LEU A 597 ? 1.1837 0.6551 0.5103 0.1763  -0.0471 -0.2076 597 LEU A C   
4275  O O   . LEU A 597 ? 1.2004 0.6500 0.5193 0.1686  -0.0653 -0.2105 597 LEU A O   
4276  C CB  . LEU A 597 ? 1.1040 0.6137 0.4803 0.1648  -0.0413 -0.1940 597 LEU A CB  
4277  C CG  . LEU A 597 ? 1.0655 0.5947 0.4699 0.1647  -0.0330 -0.1884 597 LEU A CG  
4278  C CD1 . LEU A 597 ? 1.0377 0.5756 0.4557 0.1498  -0.0435 -0.1835 597 LEU A CD1 
4279  C CD2 . LEU A 597 ? 1.0340 0.5967 0.4579 0.1713  -0.0120 -0.1834 597 LEU A CD2 
4280  N N   . SER A 598 ? 1.2007 0.6730 0.5099 0.1832  -0.0391 -0.2104 598 SER A N   
4281  C CA  . SER A 598 ? 1.2490 0.6938 0.5269 0.1846  -0.0513 -0.2186 598 SER A CA  
4282  C C   . SER A 598 ? 1.2496 0.6885 0.5214 0.1723  -0.0689 -0.2164 598 SER A C   
4283  O O   . SER A 598 ? 1.2874 0.7003 0.5386 0.1708  -0.0845 -0.2234 598 SER A O   
4284  C CB  . SER A 598 ? 1.2716 0.7206 0.5315 0.1943  -0.0372 -0.2218 598 SER A CB  
4285  O OG  . SER A 598 ? 1.2417 0.7174 0.5112 0.1914  -0.0258 -0.2128 598 SER A OG  
4286  N N   . GLN A 599 ? 1.2240 0.6871 0.5147 0.1637  -0.0673 -0.2076 599 GLN A N   
4287  C CA  . GLN A 599 ? 1.2248 0.6877 0.5103 0.1536  -0.0815 -0.2060 599 GLN A CA  
4288  C C   . GLN A 599 ? 1.2101 0.6703 0.5113 0.1393  -0.0991 -0.2056 599 GLN A C   
4289  O O   . GLN A 599 ? 1.2030 0.6695 0.5075 0.1295  -0.1104 -0.2041 599 GLN A O   
4290  C CB  . GLN A 599 ? 1.1943 0.6849 0.4896 0.1525  -0.0707 -0.1976 599 GLN A CB  
4291  C CG  . GLN A 599 ? 1.2250 0.7097 0.4933 0.1603  -0.0647 -0.1988 599 GLN A CG  
4292  C CD  . GLN A 599 ? 1.2460 0.7264 0.5027 0.1732  -0.0479 -0.2027 599 GLN A CD  
4293  O OE1 . GLN A 599 ? 1.2186 0.7191 0.4946 0.1772  -0.0308 -0.1988 599 GLN A OE1 
4294  N NE2 . GLN A 599 ? 1.2953 0.7509 0.5217 0.1795  -0.0528 -0.2114 599 GLN A NE2 
4295  N N   . LEU A 600 ? 1.1890 0.6405 0.5005 0.1370  -0.1020 -0.2070 600 LEU A N   
4296  C CA  . LEU A 600 ? 1.1791 0.6273 0.5041 0.1214  -0.1188 -0.2068 600 LEU A CA  
4297  C C   . LEU A 600 ? 1.2174 0.6418 0.5251 0.1153  -0.1384 -0.2137 600 LEU A C   
4298  O O   . LEU A 600 ? 1.2600 0.6590 0.5435 0.1240  -0.1418 -0.2208 600 LEU A O   
4299  C CB  . LEU A 600 ? 1.1761 0.6136 0.5107 0.1196  -0.1199 -0.2069 600 LEU A CB  
4300  C CG  . LEU A 600 ? 1.1351 0.5951 0.4927 0.1211  -0.1057 -0.2001 600 LEU A CG  
4301  C CD1 . LEU A 600 ? 1.1447 0.6008 0.4964 0.1380  -0.0904 -0.2015 600 LEU A CD1 
4302  C CD2 . LEU A 600 ? 1.1260 0.5793 0.4968 0.1080  -0.1166 -0.1985 600 LEU A CD2 
4303  N N   . GLN A 601 ? 1.1888 0.6237 0.5111 0.1001  -0.1514 -0.2123 601 GLN A N   
4304  C CA  . GLN A 601 ? 1.2188 0.6348 0.5338 0.0906  -0.1718 -0.2187 601 GLN A CA  
4305  C C   . GLN A 601 ? 1.2134 0.6232 0.5456 0.0751  -0.1836 -0.2191 601 GLN A C   
4306  O O   . GLN A 601 ? 1.2491 0.6321 0.5708 0.0711  -0.1975 -0.2253 601 GLN A O   
4307  C CB  . GLN A 601 ? 1.2090 0.6421 0.5293 0.0839  -0.1794 -0.2179 601 GLN A CB  
4308  C CG  . GLN A 601 ? 1.2159 0.6460 0.5483 0.0673  -0.1997 -0.2221 601 GLN A CG  
4309  C CD  . GLN A 601 ? 1.2210 0.6601 0.5515 0.0649  -0.2092 -0.2238 601 GLN A CD  
4310  O OE1 . GLN A 601 ? 1.2162 0.6646 0.5369 0.0744  -0.2008 -0.2205 601 GLN A OE1 
4311  N NE2 . GLN A 601 ? 1.2322 0.6681 0.5725 0.0519  -0.2270 -0.2290 601 GLN A NE2 
4312  N N   . MET A 602 ? 1.1948 0.6284 0.5528 0.0661  -0.1780 -0.2127 602 MET A N   
4313  C CA  . MET A 602 ? 1.1879 0.6182 0.5629 0.0497  -0.1876 -0.2118 602 MET A CA  
4314  C C   . MET A 602 ? 1.1639 0.6004 0.5478 0.0529  -0.1748 -0.2060 602 MET A C   
4315  O O   . MET A 602 ? 1.1298 0.5921 0.5236 0.0598  -0.1598 -0.2009 602 MET A O   
4316  C CB  . MET A 602 ? 1.1595 0.6175 0.5612 0.0308  -0.1967 -0.2106 602 MET A CB  
4317  C CG  . MET A 602 ? 1.1860 0.6360 0.5822 0.0253  -0.2124 -0.2172 602 MET A CG  
4318  S SD  . MET A 602 ? 1.1484 0.6395 0.5747 0.0120  -0.2176 -0.2161 602 MET A SD  
4319  C CE  . MET A 602 ? 1.1336 0.6359 0.5915 -0.0137 -0.2280 -0.2164 602 MET A CE  
4320  N N   . LEU A 603 ? 1.1266 0.5383 0.5069 0.0480  -0.1814 -0.2065 603 LEU A N   
4321  C CA  . LEU A 603 ? 1.1111 0.5228 0.4969 0.0519  -0.1714 -0.2014 603 LEU A CA  
4322  C C   . LEU A 603 ? 1.1224 0.5166 0.5145 0.0338  -0.1847 -0.1997 603 LEU A C   
4323  O O   . LEU A 603 ? 1.1642 0.5230 0.5406 0.0335  -0.1959 -0.2035 603 LEU A O   
4324  C CB  . LEU A 603 ? 1.1358 0.5268 0.5012 0.0737  -0.1616 -0.2041 603 LEU A CB  
4325  C CG  . LEU A 603 ? 1.1296 0.5135 0.4985 0.0797  -0.1539 -0.2003 603 LEU A CG  
4326  C CD1 . LEU A 603 ? 1.0796 0.5006 0.4688 0.0826  -0.1371 -0.1936 603 LEU A CD1 
4327  C CD2 . LEU A 603 ? 1.1640 0.5231 0.5134 0.0995  -0.1491 -0.2055 603 LEU A CD2 
4328  N N   . ASP A 604 ? 1.0810 0.5002 0.4962 0.0181  -0.1838 -0.1939 604 ASP A N   
4329  C CA  . ASP A 604 ? 1.0887 0.4962 0.5124 -0.0030 -0.1955 -0.1907 604 ASP A CA  
4330  C C   . ASP A 604 ? 1.0752 0.4805 0.5004 -0.0006 -0.1869 -0.1841 604 ASP A C   
4331  O O   . ASP A 604 ? 1.0334 0.4716 0.4746 0.0003  -0.1751 -0.1800 604 ASP A O   
4332  C CB  . ASP A 604 ? 1.0604 0.5007 0.5114 -0.0257 -0.2019 -0.1895 604 ASP A CB  
4333  C CG  . ASP A 604 ? 1.0758 0.5035 0.5357 -0.0504 -0.2151 -0.1867 604 ASP A CG  
4334  O OD1 . ASP A 604 ? 1.1063 0.4987 0.5504 -0.0505 -0.2193 -0.1840 604 ASP A OD1 
4335  O OD2 . ASP A 604 ? 1.0582 0.5122 0.5423 -0.0699 -0.2210 -0.1871 604 ASP A OD2 
4336  N N   . LEU A 605 ? 1.1119 0.4780 0.5208 0.0010  -0.1936 -0.1832 605 LEU A N   
4337  C CA  . LEU A 605 ? 1.1070 0.4643 0.5151 0.0021  -0.1888 -0.1768 605 LEU A CA  
4338  C C   . LEU A 605 ? 1.1285 0.4631 0.5376 -0.0224 -0.2035 -0.1709 605 LEU A C   
4339  O O   . LEU A 605 ? 1.1450 0.4546 0.5449 -0.0210 -0.2049 -0.1659 605 LEU A O   
4340  C CB  . LEU A 605 ? 1.1315 0.4629 0.5206 0.0282  -0.1822 -0.1798 605 LEU A CB  
4341  C CG  . LEU A 605 ? 1.1154 0.4676 0.5029 0.0522  -0.1659 -0.1845 605 LEU A CG  
4342  C CD1 . LEU A 605 ? 1.1405 0.4696 0.5139 0.0751  -0.1599 -0.1875 605 LEU A CD1 
4343  C CD2 . LEU A 605 ? 1.0617 0.4587 0.4699 0.0531  -0.1503 -0.1802 605 LEU A CD2 
4344  N N   . SER A 606 ? 1.1385 0.4825 0.5603 -0.0453 -0.2143 -0.1709 606 SER A N   
4345  C CA  . SER A 606 ? 1.1653 0.4866 0.5884 -0.0701 -0.2284 -0.1652 606 SER A CA  
4346  C C   . SER A 606 ? 1.1394 0.4787 0.5769 -0.0893 -0.2247 -0.1547 606 SER A C   
4347  O O   . SER A 606 ? 1.0960 0.4715 0.5466 -0.0857 -0.2122 -0.1532 606 SER A O   
4348  C CB  . SER A 606 ? 1.1721 0.5034 0.6084 -0.0880 -0.2392 -0.1693 606 SER A CB  
4349  O OG  . SER A 606 ? 1.1250 0.5069 0.5886 -0.0975 -0.2327 -0.1699 606 SER A OG  
4350  N N   . TYR A 607 ? 1.2243 0.5378 0.6588 -0.1107 -0.2357 -0.1469 607 TYR A N   
4351  C CA  . TYR A 607 ? 1.2066 0.5366 0.6551 -0.1360 -0.2342 -0.1353 607 TYR A CA  
4352  C C   . TYR A 607 ? 1.1812 0.5228 0.6286 -0.1208 -0.2206 -0.1291 607 TYR A C   
4353  O O   . TYR A 607 ? 1.1294 0.5246 0.6041 -0.1236 -0.2064 -0.1237 607 TYR A O   
4354  C CB  . TYR A 607 ? 1.1662 0.5498 0.6482 -0.1582 -0.2312 -0.1355 607 TYR A CB  
4355  C CG  . TYR A 607 ? 1.1899 0.5688 0.6824 -0.1782 -0.2430 -0.1371 607 TYR A CG  
4356  C CD1 . TYR A 607 ? 1.2138 0.5752 0.6975 -0.1651 -0.2504 -0.1477 607 TYR A CD1 
4357  C CD2 . TYR A 607 ? 1.1896 0.5830 0.7012 -0.2102 -0.2459 -0.1281 607 TYR A CD2 
4358  C CE1 . TYR A 607 ? 1.2363 0.5935 0.7302 -0.1825 -0.2613 -0.1503 607 TYR A CE1 
4359  C CE2 . TYR A 607 ? 1.2116 0.6024 0.7348 -0.2276 -0.2554 -0.1304 607 TYR A CE2 
4360  C CZ  . TYR A 607 ? 1.2348 0.6068 0.7492 -0.2134 -0.2637 -0.1420 607 TYR A CZ  
4361  O OH  . TYR A 607 ? 1.2574 0.6270 0.7840 -0.2301 -0.2735 -0.1455 607 TYR A OH  
4362  N N   . ASN A 608 ? 1.2115 0.5114 0.6357 -0.1016 -0.2224 -0.1279 608 ASN A N   
4363  C CA  . ASN A 608 ? 1.1869 0.5025 0.6159 -0.0793 -0.2071 -0.1220 608 ASN A CA  
4364  C C   . ASN A 608 ? 1.2276 0.4993 0.6402 -0.0780 -0.2148 -0.1124 608 ASN A C   
4365  O O   . ASN A 608 ? 1.2694 0.5045 0.6704 -0.0981 -0.2305 -0.1077 608 ASN A O   
4366  C CB  . ASN A 608 ? 1.1804 0.4950 0.5977 -0.0468 -0.1986 -0.1362 608 ASN A CB  
4367  C CG  . ASN A 608 ? 1.1237 0.4959 0.5647 -0.0429 -0.1834 -0.1388 608 ASN A CG  
4368  O OD1 . ASN A 608 ? 1.0855 0.5012 0.5544 -0.0624 -0.1785 -0.1308 608 ASN A OD1 
4369  N ND2 . ASN A 608 ? 1.1202 0.4922 0.5499 -0.0183 -0.1762 -0.1507 608 ASN A ND2 
4370  N N   . GLN A 609 ? 1.2261 0.5008 0.6385 -0.0542 -0.2045 -0.1097 609 GLN A N   
4371  C CA  . GLN A 609 ? 1.2657 0.4968 0.6614 -0.0462 -0.2123 -0.1027 609 GLN A CA  
4372  C C   . GLN A 609 ? 1.2884 0.4886 0.6647 -0.0112 -0.2115 -0.1167 609 GLN A C   
4373  O O   . GLN A 609 ? 1.2989 0.4839 0.6712 0.0063  -0.2100 -0.1134 609 GLN A O   
4374  C CB  . GLN A 609 ? 1.2360 0.4978 0.6503 -0.0505 -0.2024 -0.0862 609 GLN A CB  
4375  C CG  . GLN A 609 ? 1.2321 0.5094 0.6581 -0.0867 -0.2064 -0.0705 609 GLN A CG  
4376  C CD  . GLN A 609 ? 1.1977 0.5236 0.6472 -0.0905 -0.1921 -0.0573 609 GLN A CD  
4377  O OE1 . GLN A 609 ? 1.2004 0.5238 0.6488 -0.0700 -0.1870 -0.0536 609 GLN A OE1 
4378  N NE2 . GLN A 609 ? 1.1718 0.5430 0.6438 -0.1164 -0.1861 -0.0512 609 GLN A NE2 
4379  N N   . LEU A 610 ? 1.2618 0.4534 0.6260 -0.0008 -0.2128 -0.1331 610 LEU A N   
4380  C CA  . LEU A 610 ? 1.2777 0.4531 0.6292 0.0320  -0.2082 -0.1460 610 LEU A CA  
4381  C C   . LEU A 610 ? 1.3338 0.4597 0.6692 0.0375  -0.2237 -0.1452 610 LEU A C   
4382  O O   . LEU A 610 ? 1.3670 0.4671 0.6946 0.0185  -0.2394 -0.1426 610 LEU A O   
4383  C CB  . LEU A 610 ? 1.2627 0.4635 0.6179 0.0389  -0.2013 -0.1564 610 LEU A CB  
4384  C CG  . LEU A 610 ? 1.2077 0.4603 0.5803 0.0375  -0.1856 -0.1580 610 LEU A CG  
4385  C CD1 . LEU A 610 ? 1.2019 0.4722 0.5750 0.0490  -0.1795 -0.1674 610 LEU A CD1 
4386  C CD2 . LEU A 610 ? 1.1734 0.4502 0.5565 0.0543  -0.1690 -0.1562 610 LEU A CD2 
4387  N N   . ASP A 611 ? 1.3869 0.5030 0.7202 0.0634  -0.2194 -0.1478 611 ASP A N   
4388  C CA  . ASP A 611 ? 1.4385 0.5121 0.7590 0.0724  -0.2335 -0.1486 611 ASP A CA  
4389  C C   . ASP A 611 ? 1.4413 0.5250 0.7628 0.1029  -0.2240 -0.1624 611 ASP A C   
4390  O O   . ASP A 611 ? 1.4060 0.5272 0.7366 0.1140  -0.2070 -0.1695 611 ASP A O   
4391  C CB  . ASP A 611 ? 1.4545 0.5040 0.7730 0.0716  -0.2408 -0.1369 611 ASP A CB  
4392  C CG  . ASP A 611 ? 1.4241 0.4986 0.7553 0.0972  -0.2251 -0.1391 611 ASP A CG  
4393  O OD1 . ASP A 611 ? 1.3776 0.4948 0.7220 0.1051  -0.2067 -0.1444 611 ASP A OD1 
4394  O OD2 . ASP A 611 ? 1.4466 0.5003 0.7764 0.1094  -0.2314 -0.1353 611 ASP A OD2 
4395  N N   . GLY A 612 ? 1.4953 0.5464 0.8080 0.1150  -0.2349 -0.1657 612 GLY A N   
4396  C CA  . GLY A 612 ? 1.5034 0.5626 0.8171 0.1411  -0.2271 -0.1794 612 GLY A CA  
4397  C C   . GLY A 612 ? 1.5293 0.5776 0.8313 0.1383  -0.2337 -0.1891 612 GLY A C   
4398  O O   . GLY A 612 ? 1.5434 0.5762 0.8375 0.1166  -0.2458 -0.1857 612 GLY A O   
4399  N N   . GLU A 613 ? 1.5965 0.6548 0.8985 0.1603  -0.2251 -0.2018 613 GLU A N   
4400  C CA  . GLU A 613 ? 1.6283 0.6748 0.9178 0.1620  -0.2309 -0.2128 613 GLU A CA  
4401  C C   . GLU A 613 ? 1.5911 0.6752 0.8837 0.1627  -0.2150 -0.2175 613 GLU A C   
4402  O O   . GLU A 613 ? 1.5504 0.6715 0.8561 0.1728  -0.1955 -0.2170 613 GLU A O   
4403  C CB  . GLU A 613 ? 1.6603 0.6921 0.9461 0.1845  -0.2324 -0.2246 613 GLU A CB  
4404  C CG  . GLU A 613 ? 1.7020 0.6929 0.9835 0.1847  -0.2511 -0.2212 613 GLU A CG  
4405  C CD  . GLU A 613 ? 1.7480 0.7197 1.0236 0.2035  -0.2569 -0.2352 613 GLU A CD  
4406  O OE1 . GLU A 613 ? 1.7391 0.7362 1.0235 0.2238  -0.2410 -0.2449 613 GLU A OE1 
4407  O OE2 . GLU A 613 ? 1.7996 0.7316 1.0630 0.1972  -0.2770 -0.2368 613 GLU A OE2 
4408  N N   . ILE A 614 ? 1.5727 0.6474 0.8543 0.1516  -0.2238 -0.2215 614 ILE A N   
4409  C CA  . ILE A 614 ? 1.5472 0.6534 0.8293 0.1521  -0.2115 -0.2260 614 ILE A CA  
4410  C C   . ILE A 614 ? 1.5542 0.6729 0.8336 0.1758  -0.1982 -0.2376 614 ILE A C   
4411  O O   . ILE A 614 ? 1.5969 0.6911 0.8635 0.1842  -0.2068 -0.2477 614 ILE A O   
4412  C CB  . ILE A 614 ? 1.5684 0.6597 0.8400 0.1350  -0.2262 -0.2282 614 ILE A CB  
4413  C CG1 . ILE A 614 ? 1.5765 0.6462 0.8506 0.1104  -0.2428 -0.2180 614 ILE A CG1 
4414  C CG2 . ILE A 614 ? 1.5348 0.6615 0.8100 0.1317  -0.2147 -0.2293 614 ILE A CG2 
4415  C CD1 . ILE A 614 ? 1.5930 0.6534 0.8624 0.0913  -0.2565 -0.2197 614 ILE A CD1 
4416  N N   . SER A 615 ? 1.5462 0.7035 0.8386 0.1858  -0.1770 -0.2363 615 SER A N   
4417  C CA  . SER A 615 ? 1.5500 0.7238 0.8425 0.2059  -0.1619 -0.2464 615 SER A CA  
4418  C C   . SER A 615 ? 1.5765 0.7438 0.8511 0.2065  -0.1651 -0.2560 615 SER A C   
4419  O O   . SER A 615 ? 1.5652 0.7402 0.8349 0.1938  -0.1676 -0.2529 615 SER A O   
4420  C CB  . SER A 615 ? 1.4984 0.7179 0.8098 0.2117  -0.1386 -0.2415 615 SER A CB  
4421  O OG  . SER A 615 ? 1.5020 0.7398 0.8137 0.2273  -0.1230 -0.2508 615 SER A OG  
4422  N N   . SER A 616 ? 1.5938 0.7472 0.8589 0.2215  -0.1653 -0.2683 616 SER A N   
4423  C CA  . SER A 616 ? 1.6239 0.7703 0.8702 0.2242  -0.1678 -0.2788 616 SER A CA  
4424  C C   . SER A 616 ? 1.5951 0.7782 0.8422 0.2277  -0.1480 -0.2790 616 SER A C   
4425  O O   . SER A 616 ? 1.6152 0.7948 0.8454 0.2271  -0.1502 -0.2854 616 SER A O   
4426  C CB  . SER A 616 ? 1.6703 0.7938 0.9075 0.2400  -0.1722 -0.2929 616 SER A CB  
4427  O OG  . SER A 616 ? 1.7148 0.8140 0.9310 0.2377  -0.1857 -0.3021 616 SER A OG  
4428  N N   . GLN A 617 ? 1.5848 0.8022 0.8511 0.2311  -0.1294 -0.2720 617 GLN A N   
4429  C CA  . GLN A 617 ? 1.5579 0.8103 0.8267 0.2335  -0.1102 -0.2708 617 GLN A CA  
4430  C C   . GLN A 617 ? 1.5405 0.8019 0.8046 0.2182  -0.1145 -0.2632 617 GLN A C   
4431  O O   . GLN A 617 ? 1.5200 0.8070 0.7835 0.2190  -0.1012 -0.2617 617 GLN A O   
4432  C CB  . GLN A 617 ? 1.5153 0.8021 0.8096 0.2399  -0.0902 -0.2649 617 GLN A CB  
4433  C CG  . GLN A 617 ? 1.5349 0.8210 0.8375 0.2563  -0.0822 -0.2740 617 GLN A CG  
4434  C CD  . GLN A 617 ? 1.5706 0.8553 0.8584 0.2673  -0.0748 -0.2880 617 GLN A CD  
4435  O OE1 . GLN A 617 ? 1.5804 0.8660 0.8504 0.2637  -0.0741 -0.2903 617 GLN A OE1 
4436  N NE2 . GLN A 617 ? 1.5943 0.8765 0.8894 0.2810  -0.0696 -0.2980 617 GLN A NE2 
4437  N N   . PHE A 618 ? 1.5296 0.7713 0.7916 0.2036  -0.1329 -0.2584 618 PHE A N   
4438  C CA  . PHE A 618 ? 1.5124 0.7619 0.7712 0.1887  -0.1390 -0.2533 618 PHE A CA  
4439  C C   . PHE A 618 ? 1.5439 0.7843 0.7805 0.1913  -0.1434 -0.2622 618 PHE A C   
4440  O O   . PHE A 618 ? 1.5319 0.7839 0.7656 0.1820  -0.1456 -0.2589 618 PHE A O   
4441  C CB  . PHE A 618 ? 1.5137 0.7428 0.7760 0.1712  -0.1585 -0.2481 618 PHE A CB  
4442  C CG  . PHE A 618 ? 1.4686 0.7177 0.7523 0.1617  -0.1534 -0.2364 618 PHE A CG  
4443  C CD1 . PHE A 618 ? 1.4593 0.7081 0.7545 0.1686  -0.1477 -0.2331 618 PHE A CD1 
4444  C CD2 . PHE A 618 ? 1.4370 0.7062 0.7301 0.1461  -0.1547 -0.2295 618 PHE A CD2 
4445  C CE1 . PHE A 618 ? 1.4238 0.6907 0.7374 0.1601  -0.1432 -0.2229 618 PHE A CE1 
4446  C CE2 . PHE A 618 ? 1.3964 0.6852 0.7093 0.1372  -0.1499 -0.2199 618 PHE A CE2 
4447  C CZ  . PHE A 618 ? 1.3878 0.6748 0.7098 0.1442  -0.1440 -0.2165 618 PHE A CZ  
4448  N N   . ARG A 619 ? 1.6043 0.8240 0.8253 0.2039  -0.1455 -0.2739 619 ARG A N   
4449  C CA  . ARG A 619 ? 1.6385 0.8507 0.8368 0.2086  -0.1475 -0.2834 619 ARG A CA  
4450  C C   . ARG A 619 ? 1.6107 0.8548 0.8075 0.2131  -0.1284 -0.2809 619 ARG A C   
4451  O O   . ARG A 619 ? 1.6308 0.8725 0.8089 0.2127  -0.1310 -0.2851 619 ARG A O   
4452  C CB  . ARG A 619 ? 1.6862 0.8739 0.8712 0.2228  -0.1505 -0.2972 619 ARG A CB  
4453  C CG  . ARG A 619 ? 1.7286 0.9014 0.8874 0.2276  -0.1563 -0.3091 619 ARG A CG  
4454  C CD  . ARG A 619 ? 1.7617 0.9258 0.9117 0.2450  -0.1490 -0.3229 619 ARG A CD  
4455  N NE  . ARG A 619 ? 1.8131 0.9605 0.9366 0.2499  -0.1556 -0.3357 619 ARG A NE  
4456  C CZ  . ARG A 619 ? 1.8319 0.9858 0.9425 0.2632  -0.1423 -0.3467 619 ARG A CZ  
4457  N NH1 . ARG A 619 ? 1.8146 0.9925 0.9379 0.2725  -0.1212 -0.3469 619 ARG A NH1 
4458  N NH2 . ARG A 619 ? 1.8744 1.0112 0.9594 0.2667  -0.1502 -0.3584 619 ARG A NH2 
4459  N N   . SER A 620 ? 1.5624 0.8356 0.7786 0.2168  -0.1098 -0.2738 620 SER A N   
4460  C CA  . SER A 620 ? 1.5401 0.8440 0.7572 0.2198  -0.0912 -0.2702 620 SER A CA  
4461  C C   . SER A 620 ? 1.5160 0.8329 0.7341 0.2065  -0.0959 -0.2610 620 SER A C   
4462  O O   . SER A 620 ? 1.5132 0.8460 0.7230 0.2080  -0.0862 -0.2596 620 SER A O   
4463  C CB  . SER A 620 ? 1.5025 0.8350 0.7444 0.2259  -0.0712 -0.2648 620 SER A CB  
4464  O OG  . SER A 620 ? 1.5277 0.8507 0.7715 0.2385  -0.0669 -0.2740 620 SER A OG  
4465  N N   . LEU A 621 ? 1.4649 0.7752 0.6931 0.1932  -0.1106 -0.2551 621 LEU A N   
4466  C CA  . LEU A 621 ? 1.4393 0.7642 0.6729 0.1798  -0.1158 -0.2474 621 LEU A CA  
4467  C C   . LEU A 621 ? 1.4776 0.7837 0.6871 0.1772  -0.1300 -0.2542 621 LEU A C   
4468  O O   . LEU A 621 ? 1.4958 0.7814 0.7019 0.1677  -0.1493 -0.2571 621 LEU A O   
4469  C CB  . LEU A 621 ? 1.4120 0.7377 0.6659 0.1656  -0.1263 -0.2403 621 LEU A CB  
4470  C CG  . LEU A 621 ? 1.3770 0.7180 0.6537 0.1674  -0.1151 -0.2337 621 LEU A CG  
4471  C CD1 . LEU A 621 ? 1.3550 0.6951 0.6478 0.1511  -0.1271 -0.2271 621 LEU A CD1 
4472  C CD2 . LEU A 621 ? 1.3389 0.7160 0.6291 0.1732  -0.0937 -0.2274 621 LEU A CD2 
4473  N N   . GLN A 622 ? 1.5064 0.8200 0.6992 0.1854  -0.1202 -0.2570 622 GLN A N   
4474  C CA  . GLN A 622 ? 1.5486 0.8433 0.7149 0.1858  -0.1322 -0.2647 622 GLN A CA  
4475  C C   . GLN A 622 ? 1.5363 0.8361 0.7056 0.1721  -0.1459 -0.2597 622 GLN A C   
4476  O O   . GLN A 622 ? 1.5709 0.8517 0.7226 0.1697  -0.1613 -0.2663 622 GLN A O   
4477  C CB  . GLN A 622 ? 1.5691 0.8702 0.7149 0.1983  -0.1168 -0.2689 622 GLN A CB  
4478  C CG  . GLN A 622 ? 1.5940 0.8865 0.7332 0.2122  -0.1063 -0.2783 622 GLN A CG  
4479  C CD  . GLN A 622 ? 1.6178 0.9181 0.7368 0.2227  -0.0904 -0.2833 622 GLN A CD  
4480  O OE1 . GLN A 622 ? 1.6258 0.9293 0.7279 0.2204  -0.0912 -0.2813 622 GLN A OE1 
4481  N NE2 . GLN A 622 ? 1.6264 0.9300 0.7472 0.2341  -0.0760 -0.2901 622 GLN A NE2 
4482  N N   . ASN A 623 ? 1.4504 0.7763 0.6428 0.1634  -0.1409 -0.2490 623 ASN A N   
4483  C CA  . ASN A 623 ? 1.4354 0.7701 0.6350 0.1503  -0.1534 -0.2447 623 ASN A CA  
4484  C C   . ASN A 623 ? 1.4142 0.7489 0.6374 0.1350  -0.1668 -0.2420 623 ASN A C   
4485  O O   . ASN A 623 ? 1.3976 0.7435 0.6326 0.1225  -0.1771 -0.2390 623 ASN A O   
4486  C CB  . ASN A 623 ? 1.3990 0.7643 0.6081 0.1502  -0.1397 -0.2354 623 ASN A CB  
4487  C CG  . ASN A 623 ? 1.4170 0.7849 0.6052 0.1642  -0.1231 -0.2365 623 ASN A CG  
4488  O OD1 . ASN A 623 ? 1.4186 0.7879 0.6067 0.1740  -0.1083 -0.2382 623 ASN A OD1 
4489  N ND2 . ASN A 623 ? 1.4323 0.8009 0.6030 0.1647  -0.1258 -0.2359 623 ASN A ND2 
4490  N N   . LEU A 624 ? 1.3986 0.7210 0.6290 0.1352  -0.1672 -0.2433 624 LEU A N   
4491  C CA  . LEU A 624 ? 1.3799 0.7017 0.6318 0.1197  -0.1785 -0.2399 624 LEU A CA  
4492  C C   . LEU A 624 ? 1.4077 0.7112 0.6551 0.1078  -0.2005 -0.2457 624 LEU A C   
4493  O O   . LEU A 624 ? 1.4528 0.7283 0.6799 0.1133  -0.2097 -0.2545 624 LEU A O   
4494  C CB  . LEU A 624 ? 1.3848 0.6917 0.6403 0.1240  -0.1752 -0.2403 624 LEU A CB  
4495  C CG  . LEU A 624 ? 1.3625 0.6703 0.6398 0.1084  -0.1829 -0.2347 624 LEU A CG  
4496  C CD1 . LEU A 624 ? 1.3088 0.6533 0.6102 0.1005  -0.1734 -0.2254 624 LEU A CD1 
4497  C CD2 . LEU A 624 ? 1.3743 0.6632 0.6504 0.1154  -0.1801 -0.2352 624 LEU A CD2 
4498  N N   . GLU A 625 ? 1.3396 0.6606 0.6079 0.0913  -0.2088 -0.2414 625 GLU A N   
4499  C CA  . GLU A 625 ? 1.3604 0.6698 0.6312 0.0777  -0.2292 -0.2466 625 GLU A CA  
4500  C C   . GLU A 625 ? 1.3512 0.6565 0.6431 0.0601  -0.2390 -0.2445 625 GLU A C   
4501  O O   . GLU A 625 ? 1.3810 0.6662 0.6711 0.0510  -0.2554 -0.2502 625 GLU A O   
4502  C CB  . GLU A 625 ? 1.3420 0.6755 0.6219 0.0710  -0.2333 -0.2451 625 GLU A CB  
4503  C CG  . GLU A 625 ? 1.3748 0.6984 0.6277 0.0830  -0.2355 -0.2507 625 GLU A CG  
4504  C CD  . GLU A 625 ? 1.3516 0.7011 0.6126 0.0800  -0.2354 -0.2467 625 GLU A CD  
4505  O OE1 . GLU A 625 ? 1.3373 0.6999 0.6195 0.0652  -0.2478 -0.2469 625 GLU A OE1 
4506  O OE2 . GLU A 625 ? 1.3489 0.7059 0.5956 0.0921  -0.2230 -0.2436 625 GLU A OE2 
4507  N N   . ARG A 626 ? 1.3640 0.6876 0.6758 0.0545  -0.2295 -0.2364 626 ARG A N   
4508  C CA  . ARG A 626 ? 1.3546 0.6760 0.6861 0.0362  -0.2378 -0.2331 626 ARG A CA  
4509  C C   . ARG A 626 ? 1.3465 0.6597 0.6778 0.0417  -0.2278 -0.2279 626 ARG A C   
4510  O O   . ARG A 626 ? 1.3220 0.6512 0.6532 0.0542  -0.2112 -0.2239 626 ARG A O   
4511  C CB  . ARG A 626 ? 1.3116 0.6693 0.6732 0.0186  -0.2390 -0.2283 626 ARG A CB  
4512  C CG  . ARG A 626 ? 1.3205 0.6862 0.6875 0.0104  -0.2518 -0.2339 626 ARG A CG  
4513  C CD  . ARG A 626 ? 1.2885 0.6830 0.6898 -0.0121 -0.2577 -0.2314 626 ARG A CD  
4514  N NE  . ARG A 626 ? 1.3124 0.7012 0.7196 -0.0241 -0.2745 -0.2385 626 ARG A NE  
4515  C CZ  . ARG A 626 ? 1.2896 0.7084 0.7240 -0.0385 -0.2802 -0.2399 626 ARG A CZ  
4516  N NH1 . ARG A 626 ? 1.2422 0.6992 0.7007 -0.0431 -0.2712 -0.2346 626 ARG A NH1 
4517  N NH2 . ARG A 626 ? 1.3153 0.7269 0.7543 -0.0480 -0.2953 -0.2474 626 ARG A NH2 
4518  N N   . LEU A 627 ? 1.3238 0.6114 0.6554 0.0319  -0.2383 -0.2278 627 LEU A N   
4519  C CA  . LEU A 627 ? 1.3214 0.5966 0.6525 0.0353  -0.2322 -0.2227 627 LEU A CA  
4520  C C   . LEU A 627 ? 1.3237 0.5897 0.6693 0.0122  -0.2444 -0.2179 627 LEU A C   
4521  O O   . LEU A 627 ? 1.3562 0.6008 0.6990 0.0010  -0.2600 -0.2218 627 LEU A O   
4522  C CB  . LEU A 627 ? 1.3636 0.6047 0.6701 0.0541  -0.2322 -0.2286 627 LEU A CB  
4523  C CG  . LEU A 627 ? 1.3498 0.5989 0.6507 0.0752  -0.2136 -0.2272 627 LEU A CG  
4524  C CD1 . LEU A 627 ? 1.3926 0.6070 0.6753 0.0897  -0.2165 -0.2331 627 LEU A CD1 
4525  C CD2 . LEU A 627 ? 1.3070 0.5779 0.6273 0.0696  -0.2034 -0.2175 627 LEU A CD2 
4526  N N   . ASP A 628 ? 1.2514 0.5337 0.6123 0.0043  -0.2369 -0.2093 628 ASP A N   
4527  C CA  . ASP A 628 ? 1.2529 0.5279 0.6269 -0.0191 -0.2465 -0.2030 628 ASP A CA  
4528  C C   . ASP A 628 ? 1.2480 0.5117 0.6180 -0.0139 -0.2392 -0.1958 628 ASP A C   
4529  O O   . ASP A 628 ? 1.2079 0.4997 0.5890 -0.0107 -0.2258 -0.1909 628 ASP A O   
4530  C CB  . ASP A 628 ? 1.2131 0.5281 0.6157 -0.0402 -0.2465 -0.1996 628 ASP A CB  
4531  C CG  . ASP A 628 ? 1.2216 0.5301 0.6387 -0.0678 -0.2577 -0.1943 628 ASP A CG  
4532  O OD1 . ASP A 628 ? 1.2573 0.5284 0.6609 -0.0708 -0.2652 -0.1913 628 ASP A OD1 
4533  O OD2 . ASP A 628 ? 1.1933 0.5353 0.6365 -0.0868 -0.2588 -0.1928 628 ASP A OD2 
4534  N N   . LEU A 629 ? 1.2898 0.5124 0.6448 -0.0127 -0.2486 -0.1953 629 LEU A N   
4535  C CA  . LEU A 629 ? 1.2933 0.4988 0.6430 -0.0076 -0.2447 -0.1885 629 LEU A CA  
4536  C C   . LEU A 629 ? 1.3138 0.4966 0.6673 -0.0325 -0.2582 -0.1799 629 LEU A C   
4537  O O   . LEU A 629 ? 1.3361 0.4898 0.6795 -0.0291 -0.2613 -0.1747 629 LEU A O   
4538  C CB  . LEU A 629 ? 1.3265 0.5030 0.6553 0.0185  -0.2431 -0.1947 629 LEU A CB  
4539  C CG  . LEU A 629 ? 1.3146 0.5091 0.6369 0.0443  -0.2285 -0.2026 629 LEU A CG  
4540  C CD1 . LEU A 629 ? 1.3324 0.5085 0.6436 0.0671  -0.2221 -0.2049 629 LEU A CD1 
4541  C CD2 . LEU A 629 ? 1.2604 0.5009 0.5991 0.0447  -0.2125 -0.1993 629 LEU A CD2 
4542  N N   . SER A 630 ? 1.3391 0.5362 0.7084 -0.0578 -0.2660 -0.1779 630 SER A N   
4543  C CA  . SER A 630 ? 1.3631 0.5396 0.7369 -0.0840 -0.2787 -0.1696 630 SER A CA  
4544  C C   . SER A 630 ? 1.3391 0.5264 0.7216 -0.0973 -0.2724 -0.1570 630 SER A C   
4545  O O   . SER A 630 ? 1.2966 0.5157 0.6875 -0.0901 -0.2587 -0.1558 630 SER A O   
4546  C CB  . SER A 630 ? 1.3603 0.5555 0.7528 -0.1071 -0.2867 -0.1720 630 SER A CB  
4547  O OG  . SER A 630 ? 1.3085 0.5540 0.7256 -0.1170 -0.2768 -0.1706 630 SER A OG  
4548  N N   . HIS A 631 ? 1.4162 0.5762 0.7962 -0.1175 -0.2828 -0.1471 631 HIS A N   
4549  C CA  . HIS A 631 ? 1.4020 0.5678 0.7883 -0.1350 -0.2792 -0.1332 631 HIS A CA  
4550  C C   . HIS A 631 ? 1.3898 0.5496 0.7638 -0.1112 -0.2692 -0.1318 631 HIS A C   
4551  O O   . HIS A 631 ? 1.3467 0.5402 0.7316 -0.1108 -0.2568 -0.1293 631 HIS A O   
4552  C CB  . HIS A 631 ? 1.3555 0.5735 0.7705 -0.1590 -0.2721 -0.1299 631 HIS A CB  
4553  C CG  . HIS A 631 ? 1.3671 0.5939 0.7988 -0.1841 -0.2810 -0.1305 631 HIS A CG  
4554  N ND1 . HIS A 631 ? 1.3872 0.6051 0.8169 -0.1765 -0.2889 -0.1421 631 HIS A ND1 
4555  C CD2 . HIS A 631 ? 1.3618 0.6076 0.8138 -0.2165 -0.2825 -0.1213 631 HIS A CD2 
4556  C CE1 . HIS A 631 ? 1.3936 0.6235 0.8423 -0.2022 -0.2954 -0.1408 631 HIS A CE1 
4557  N NE2 . HIS A 631 ? 1.3781 0.6261 0.8414 -0.2267 -0.2910 -0.1284 631 HIS A NE2 
4558  N N   . ASN A 632 ? 1.4055 0.5235 0.7585 -0.0903 -0.2748 -0.1342 632 ASN A N   
4559  C CA  . ASN A 632 ? 1.3998 0.5098 0.7427 -0.0642 -0.2661 -0.1345 632 ASN A CA  
4560  C C   . ASN A 632 ? 1.4515 0.5105 0.7771 -0.0595 -0.2787 -0.1286 632 ASN A C   
4561  O O   . ASN A 632 ? 1.4895 0.5208 0.8108 -0.0783 -0.2934 -0.1231 632 ASN A O   
4562  C CB  . ASN A 632 ? 1.3832 0.5103 0.7236 -0.0331 -0.2547 -0.1485 632 ASN A CB  
4563  C CG  . ASN A 632 ? 1.3276 0.5064 0.6850 -0.0334 -0.2397 -0.1516 632 ASN A CG  
4564  O OD1 . ASN A 632 ? 1.2937 0.4948 0.6587 -0.0294 -0.2280 -0.1477 632 ASN A OD1 
4565  N ND2 . ASN A 632 ? 1.3188 0.5172 0.6833 -0.0378 -0.2406 -0.1587 632 ASN A ND2 
4566  N N   . ASN A 633 ? 1.4581 0.5068 0.7760 -0.0336 -0.2727 -0.1299 633 ASN A N   
4567  C CA  . ASN A 633 ? 1.5051 0.5091 0.8088 -0.0235 -0.2842 -0.1258 633 ASN A CA  
4568  C C   . ASN A 633 ? 1.5174 0.5152 0.8142 0.0113  -0.2804 -0.1401 633 ASN A C   
4569  O O   . ASN A 633 ? 1.5338 0.5142 0.8256 0.0309  -0.2811 -0.1399 633 ASN A O   
4570  C CB  . ASN A 633 ? 1.5000 0.4969 0.8036 -0.0262 -0.2826 -0.1123 633 ASN A CB  
4571  C CG  . ASN A 633 ? 1.5540 0.5028 0.8444 -0.0290 -0.2994 -0.1024 633 ASN A CG  
4572  O OD1 . ASN A 633 ? 1.5947 0.5161 0.8775 -0.0385 -0.3136 -0.1029 633 ASN A OD1 
4573  N ND2 . ASN A 633 ? 1.5555 0.4946 0.8437 -0.0202 -0.2984 -0.0933 633 ASN A ND2 
4574  N N   . LEU A 634 ? 1.5167 0.5314 0.8145 0.0185  -0.2761 -0.1526 634 LEU A N   
4575  C CA  . LEU A 634 ? 1.5299 0.5418 0.8211 0.0483  -0.2716 -0.1663 634 LEU A CA  
4576  C C   . LEU A 634 ? 1.5887 0.5551 0.8665 0.0513  -0.2896 -0.1688 634 LEU A C   
4577  O O   . LEU A 634 ? 1.6178 0.5622 0.8911 0.0307  -0.3046 -0.1659 634 LEU A O   
4578  C CB  . LEU A 634 ? 1.5094 0.5501 0.8033 0.0525  -0.2630 -0.1773 634 LEU A CB  
4579  C CG  . LEU A 634 ? 1.4528 0.5402 0.7612 0.0470  -0.2470 -0.1754 634 LEU A CG  
4580  C CD1 . LEU A 634 ? 1.4455 0.5490 0.7571 0.0330  -0.2500 -0.1800 634 LEU A CD1 
4581  C CD2 . LEU A 634 ? 1.4228 0.5388 0.7361 0.0744  -0.2272 -0.1814 634 LEU A CD2 
4582  N N   . SER A 635 ? 1.6221 0.5766 0.8958 0.0766  -0.2881 -0.1746 635 SER A N   
4583  C CA  . SER A 635 ? 1.6778 0.5906 0.9403 0.0828  -0.3050 -0.1782 635 SER A CA  
4584  C C   . SER A 635 ? 1.6899 0.6079 0.9482 0.1082  -0.2996 -0.1958 635 SER A C   
4585  O O   . SER A 635 ? 1.6572 0.6096 0.9200 0.1184  -0.2834 -0.2037 635 SER A O   
4586  C CB  . SER A 635 ? 1.6942 0.5855 0.9567 0.0889  -0.3108 -0.1692 635 SER A CB  
4587  O OG  . SER A 635 ? 1.6631 0.5816 0.9352 0.1133  -0.2942 -0.1736 635 SER A OG  
4588  N N   . GLY A 636 ? 1.7314 0.6148 0.9809 0.1176  -0.3136 -0.2018 636 GLY A N   
4589  C CA  . GLY A 636 ? 1.7507 0.6347 0.9947 0.1388  -0.3108 -0.2190 636 GLY A CA  
4590  C C   . GLY A 636 ? 1.7687 0.6458 1.0039 0.1276  -0.3186 -0.2259 636 GLY A C   
4591  O O   . GLY A 636 ? 1.7691 0.6394 1.0041 0.1031  -0.3274 -0.2179 636 GLY A O   
4592  N N   . GLN A 637 ? 1.8188 0.6985 1.0475 0.1458  -0.3151 -0.2417 637 GLN A N   
4593  C CA  . GLN A 637 ? 1.8374 0.7122 1.0568 0.1392  -0.3216 -0.2504 637 GLN A CA  
4594  C C   . GLN A 637 ? 1.7950 0.7115 1.0168 0.1419  -0.3034 -0.2541 637 GLN A C   
4595  O O   . GLN A 637 ? 1.7635 0.7098 0.9912 0.1578  -0.2845 -0.2563 637 GLN A O   
4596  C CB  . GLN A 637 ? 1.8876 0.7368 1.0958 0.1561  -0.3308 -0.2659 637 GLN A CB  
4597  C CG  . GLN A 637 ? 1.9303 0.7401 1.1372 0.1584  -0.3476 -0.2636 637 GLN A CG  
4598  C CD  . GLN A 637 ? 1.9856 0.7651 1.1815 0.1687  -0.3617 -0.2785 637 GLN A CD  
4599  O OE1 . GLN A 637 ? 1.9921 0.7810 1.1804 0.1759  -0.3576 -0.2915 637 GLN A OE1 
4600  N NE2 . GLN A 637 ? 2.0276 0.7698 1.2220 0.1693  -0.3788 -0.2766 637 GLN A NE2 
4601  N N   . ILE A 638 ? 1.8175 0.7366 1.0363 0.1256  -0.3095 -0.2545 638 ILE A N   
4602  C CA  . ILE A 638 ? 1.7788 0.7337 0.9982 0.1276  -0.2955 -0.2586 638 ILE A CA  
4603  C C   . ILE A 638 ? 1.7981 0.7573 1.0065 0.1519  -0.2870 -0.2736 638 ILE A C   
4604  O O   . ILE A 638 ? 1.8467 0.7781 1.0433 0.1576  -0.2994 -0.2841 638 ILE A O   
4605  C CB  . ILE A 638 ? 1.7834 0.7367 1.0020 0.1065  -0.3068 -0.2579 638 ILE A CB  
4606  C CG1 . ILE A 638 ? 1.7651 0.7180 0.9969 0.0804  -0.3135 -0.2433 638 ILE A CG1 
4607  C CG2 . ILE A 638 ? 1.7542 0.7424 0.9720 0.1105  -0.2938 -0.2627 638 ILE A CG2 
4608  C CD1 . ILE A 638 ? 1.7688 0.7231 1.0048 0.0579  -0.3246 -0.2428 638 ILE A CD1 
4609  N N   . PRO A 639 ? 1.7896 0.7833 1.0021 0.1659  -0.2658 -0.2751 639 PRO A N   
4610  C CA  . PRO A 639 ? 1.8070 0.8063 1.0104 0.1882  -0.2557 -0.2889 639 PRO A CA  
4611  C C   . PRO A 639 ? 1.8374 0.8277 1.0243 0.1877  -0.2633 -0.2998 639 PRO A C   
4612  O O   . PRO A 639 ? 1.8182 0.8257 1.0034 0.1773  -0.2613 -0.2971 639 PRO A O   
4613  C CB  . PRO A 639 ? 1.7570 0.7999 0.9707 0.1964  -0.2311 -0.2850 639 PRO A CB  
4614  C CG  . PRO A 639 ? 1.7162 0.7769 0.9404 0.1771  -0.2303 -0.2715 639 PRO A CG  
4615  C CD  . PRO A 639 ? 1.7335 0.7635 0.9604 0.1609  -0.2497 -0.2642 639 PRO A CD  
4616  N N   . PRO A 640 ? 1.8570 0.8204 1.0316 0.1991  -0.2726 -0.3129 640 PRO A N   
4617  C CA  . PRO A 640 ? 1.8903 0.8430 1.0479 0.1991  -0.2811 -0.3243 640 PRO A CA  
4618  C C   . PRO A 640 ? 1.8730 0.8568 1.0223 0.2080  -0.2635 -0.3296 640 PRO A C   
4619  O O   . PRO A 640 ? 1.8954 0.8739 1.0301 0.2061  -0.2700 -0.3371 640 PRO A O   
4620  C CB  . PRO A 640 ? 1.9439 0.8640 1.0924 0.2127  -0.2920 -0.3378 640 PRO A CB  
4621  C CG  . PRO A 640 ? 1.9429 0.8475 1.1046 0.2118  -0.2975 -0.3298 640 PRO A CG  
4622  C CD  . PRO A 640 ? 1.8869 0.8260 1.0635 0.2111  -0.2786 -0.3177 640 PRO A CD  
4623  N N   . SER A 641 ? 1.8701 0.8856 1.0281 0.2173  -0.2418 -0.3256 641 SER A N   
4624  C CA  . SER A 641 ? 1.8522 0.8980 1.0031 0.2235  -0.2244 -0.3282 641 SER A CA  
4625  C C   . SER A 641 ? 1.8217 0.8856 0.9749 0.2072  -0.2251 -0.3182 641 SER A C   
4626  O O   . SER A 641 ? 1.8043 0.8932 0.9519 0.2107  -0.2117 -0.3183 641 SER A O   
4627  C CB  . SER A 641 ? 1.8210 0.8964 0.9840 0.2365  -0.2009 -0.3262 641 SER A CB  
4628  O OG  . SER A 641 ? 1.7747 0.8671 0.9580 0.2277  -0.1956 -0.3115 641 SER A OG  
4629  N N   . PHE A 642 ? 1.8618 0.9141 1.0238 0.1892  -0.2403 -0.3097 642 PHE A N   
4630  C CA  . PHE A 642 ? 1.8353 0.9050 1.0022 0.1728  -0.2426 -0.3018 642 PHE A CA  
4631  C C   . PHE A 642 ? 1.8645 0.9221 1.0151 0.1689  -0.2555 -0.3104 642 PHE A C   
4632  O O   . PHE A 642 ? 1.8411 0.9159 0.9946 0.1581  -0.2566 -0.3058 642 PHE A O   
4633  C CB  . PHE A 642 ? 1.8114 0.8758 0.9960 0.1535  -0.2532 -0.2902 642 PHE A CB  
4634  C CG  . PHE A 642 ? 1.7596 0.8490 0.9622 0.1526  -0.2383 -0.2785 642 PHE A CG  
4635  C CD1 . PHE A 642 ? 1.7437 0.8538 0.9482 0.1698  -0.2183 -0.2794 642 PHE A CD1 
4636  C CD2 . PHE A 642 ? 1.7322 0.8257 0.9511 0.1338  -0.2441 -0.2671 642 PHE A CD2 
4637  C CE1 . PHE A 642 ? 1.7010 0.8349 0.9234 0.1693  -0.2049 -0.2692 642 PHE A CE1 
4638  C CE2 . PHE A 642 ? 1.6893 0.8056 0.9241 0.1332  -0.2308 -0.2571 642 PHE A CE2 
4639  C CZ  . PHE A 642 ? 1.6711 0.8075 0.9079 0.1515  -0.2115 -0.2582 642 PHE A CZ  
4640  N N   . LYS A 643 ? 1.8618 0.8908 0.9963 0.1778  -0.2659 -0.3232 643 LYS A N   
4641  C CA  . LYS A 643 ? 1.8984 0.9157 1.0159 0.1760  -0.2778 -0.3328 643 LYS A CA  
4642  C C   . LYS A 643 ? 1.8868 0.9282 0.9905 0.1854  -0.2635 -0.3360 643 LYS A C   
4643  O O   . LYS A 643 ? 1.9027 0.9422 0.9948 0.1809  -0.2722 -0.3402 643 LYS A O   
4644  C CB  . LYS A 643 ? 1.9512 0.9330 1.0548 0.1852  -0.2910 -0.3468 643 LYS A CB  
4645  C CG  . LYS A 643 ? 1.9696 0.9527 1.0613 0.2073  -0.2770 -0.3572 643 LYS A CG  
4646  C CD  . LYS A 643 ? 2.0259 0.9734 1.1066 0.2158  -0.2915 -0.3715 643 LYS A CD  
4647  C CE  . LYS A 643 ? 2.0453 0.9969 1.1153 0.2375  -0.2769 -0.3838 643 LYS A CE  
4648  N NZ  . LYS A 643 ? 2.0451 1.0184 1.0979 0.2447  -0.2631 -0.3892 643 LYS A NZ  
4649  N N   . ASP A 644 ? 1.8849 0.9483 0.9896 0.1979  -0.2421 -0.3340 644 ASP A N   
4650  C CA  . ASP A 644 ? 1.8806 0.9659 0.9713 0.2068  -0.2269 -0.3364 644 ASP A CA  
4651  C C   . ASP A 644 ? 1.8339 0.9505 0.9361 0.1969  -0.2180 -0.3231 644 ASP A C   
4652  O O   . ASP A 644 ? 1.8232 0.9601 0.9161 0.2035  -0.2035 -0.3225 644 ASP A O   
4653  C CB  . ASP A 644 ? 1.8845 0.9789 0.9718 0.2247  -0.2074 -0.3420 644 ASP A CB  
4654  C CG  . ASP A 644 ? 1.9339 0.9992 1.0106 0.2360  -0.2155 -0.3568 644 ASP A CG  
4655  O OD1 . ASP A 644 ? 1.9733 1.0124 1.0369 0.2328  -0.2342 -0.3651 644 ASP A OD1 
4656  O OD2 . ASP A 644 ? 1.9339 1.0031 1.0170 0.2481  -0.2035 -0.3606 644 ASP A OD2 
4657  N N   . MET A 645 ? 1.8175 0.9386 0.9399 0.1809  -0.2261 -0.3127 645 MET A N   
4658  C CA  . MET A 645 ? 1.7716 0.9229 0.9078 0.1707  -0.2193 -0.3009 645 MET A CA  
4659  C C   . MET A 645 ? 1.7792 0.9260 0.9096 0.1592  -0.2357 -0.3028 645 MET A C   
4660  O O   . MET A 645 ? 1.7769 0.9152 0.9201 0.1439  -0.2515 -0.3005 645 MET A O   
4661  C CB  . MET A 645 ? 1.7309 0.8932 0.8938 0.1602  -0.2171 -0.2895 645 MET A CB  
4662  C CG  . MET A 645 ? 1.7030 0.8786 0.8741 0.1723  -0.1979 -0.2861 645 MET A CG  
4663  S SD  . MET A 645 ? 1.6621 0.8451 0.8612 0.1619  -0.1968 -0.2740 645 MET A SD  
4664  C CE  . MET A 645 ? 1.6532 0.8332 0.8625 0.1375  -0.2163 -0.2688 645 MET A CE  
4665  N N   . LEU A 646 ? 1.7420 0.8949 0.8529 0.1664  -0.2319 -0.3071 646 LEU A N   
4666  C CA  . LEU A 646 ? 1.7614 0.9079 0.8638 0.1582  -0.2483 -0.3108 646 LEU A CA  
4667  C C   . LEU A 646 ? 1.7182 0.8896 0.8418 0.1430  -0.2507 -0.3000 646 LEU A C   
4668  O O   . LEU A 646 ? 1.7260 0.8926 0.8550 0.1308  -0.2678 -0.3018 646 LEU A O   
4669  C CB  . LEU A 646 ? 1.7947 0.9384 0.8672 0.1711  -0.2438 -0.3186 646 LEU A CB  
4670  C CG  . LEU A 646 ? 1.8416 0.9639 0.8902 0.1873  -0.2404 -0.3316 646 LEU A CG  
4671  C CD1 . LEU A 646 ? 1.8251 0.9626 0.8746 0.1998  -0.2167 -0.3294 646 LEU A CD1 
4672  C CD2 . LEU A 646 ? 1.8846 0.9968 0.9033 0.1936  -0.2465 -0.3412 646 LEU A CD2 
4673  N N   . ALA A 647 ? 1.6514 0.8506 0.7890 0.1433  -0.2339 -0.2895 647 ALA A N   
4674  C CA  . ALA A 647 ? 1.6096 0.8348 0.7684 0.1298  -0.2354 -0.2801 647 ALA A CA  
4675  C C   . ALA A 647 ? 1.5876 0.8138 0.7738 0.1124  -0.2460 -0.2759 647 ALA A C   
4676  O O   . ALA A 647 ? 1.5648 0.8074 0.7686 0.0984  -0.2538 -0.2720 647 ALA A O   
4677  C CB  . ALA A 647 ? 1.5690 0.8234 0.7352 0.1356  -0.2142 -0.2706 647 ALA A CB  
4678  N N   . LEU A 648 ? 1.6124 0.8218 0.8026 0.1128  -0.2465 -0.2768 648 LEU A N   
4679  C CA  . LEU A 648 ? 1.5945 0.8029 0.8086 0.0956  -0.2556 -0.2719 648 LEU A CA  
4680  C C   . LEU A 648 ? 1.6161 0.8131 0.8348 0.0806  -0.2766 -0.2770 648 LEU A C   
4681  O O   . LEU A 648 ? 1.6611 0.8333 0.8612 0.0855  -0.2879 -0.2868 648 LEU A O   
4682  C CB  . LEU A 648 ? 1.6101 0.7956 0.8218 0.1008  -0.2541 -0.2728 648 LEU A CB  
4683  C CG  . LEU A 648 ? 1.5930 0.7750 0.8262 0.0848  -0.2602 -0.2659 648 LEU A CG  
4684  C CD1 . LEU A 648 ? 1.5391 0.7530 0.7926 0.0809  -0.2454 -0.2549 648 LEU A CD1 
4685  C CD2 . LEU A 648 ? 1.6265 0.7756 0.8501 0.0918  -0.2643 -0.2696 648 LEU A CD2 
4686  N N   . THR A 649 ? 1.5720 0.7890 0.8172 0.0619  -0.2817 -0.2709 649 THR A N   
4687  C CA  . THR A 649 ? 1.5873 0.7988 0.8435 0.0452  -0.3005 -0.2754 649 THR A CA  
4688  C C   . THR A 649 ? 1.5749 0.7849 0.8555 0.0252  -0.3072 -0.2706 649 THR A C   
4689  O O   . THR A 649 ? 1.6052 0.7948 0.8881 0.0144  -0.3227 -0.2758 649 THR A O   
4690  C CB  . THR A 649 ? 1.5647 0.8052 0.8323 0.0391  -0.3028 -0.2747 649 THR A CB  
4691  O OG1 . THR A 649 ? 1.5160 0.7875 0.8153 0.0236  -0.2983 -0.2662 649 THR A OG1 
4692  C CG2 . THR A 649 ? 1.5621 0.8121 0.8095 0.0572  -0.2908 -0.2743 649 THR A CG2 
4693  N N   . HIS A 650 ? 1.5692 0.8000 0.8677 0.0194  -0.2958 -0.2608 650 HIS A N   
4694  C CA  . HIS A 650 ? 1.5555 0.7880 0.8772 -0.0012 -0.3009 -0.2550 650 HIS A CA  
4695  C C   . HIS A 650 ? 1.5548 0.7732 0.8711 0.0048  -0.2919 -0.2487 650 HIS A C   
4696  O O   . HIS A 650 ? 1.5282 0.7600 0.8400 0.0187  -0.2762 -0.2446 650 HIS A O   
4697  C CB  . HIS A 650 ? 1.5045 0.7787 0.8568 -0.0170 -0.2971 -0.2491 650 HIS A CB  
4698  C CG  . HIS A 650 ? 1.5071 0.7964 0.8710 -0.0263 -0.3081 -0.2553 650 HIS A CG  
4699  N ND1 . HIS A 650 ? 1.5349 0.8144 0.8787 -0.0134 -0.3135 -0.2634 650 HIS A ND1 
4700  C CD2 . HIS A 650 ? 1.4876 0.8020 0.8817 -0.0470 -0.3146 -0.2551 650 HIS A CD2 
4701  C CE1 . HIS A 650 ? 1.5313 0.8276 0.8919 -0.0252 -0.3238 -0.2677 650 HIS A CE1 
4702  N NE2 . HIS A 650 ? 1.5037 0.8227 0.8962 -0.0456 -0.3241 -0.2632 650 HIS A NE2 
4703  N N   . VAL A 651 ? 1.5501 0.7410 0.8674 -0.0058 -0.3022 -0.2477 651 VAL A N   
4704  C CA  . VAL A 651 ? 1.5512 0.7254 0.8645 -0.0024 -0.2967 -0.2411 651 VAL A CA  
4705  C C   . VAL A 651 ? 1.5474 0.7183 0.8801 -0.0279 -0.3051 -0.2335 651 VAL A C   
4706  O O   . VAL A 651 ? 1.5647 0.7305 0.9071 -0.0453 -0.3185 -0.2363 651 VAL A O   
4707  C CB  . VAL A 651 ? 1.5998 0.7339 0.8872 0.0150  -0.3012 -0.2478 651 VAL A CB  
4708  C CG1 . VAL A 651 ? 1.5974 0.7182 0.8813 0.0225  -0.2938 -0.2414 651 VAL A CG1 
4709  C CG2 . VAL A 651 ? 1.6109 0.7480 0.8789 0.0370  -0.2948 -0.2567 651 VAL A CG2 
4710  N N   . ASP A 652 ? 1.4634 0.6381 0.8022 -0.0309 -0.2967 -0.2239 652 ASP A N   
4711  C CA  . ASP A 652 ? 1.4668 0.6322 0.8189 -0.0544 -0.3040 -0.2151 652 ASP A CA  
4712  C C   . ASP A 652 ? 1.4739 0.6171 0.8143 -0.0453 -0.2989 -0.2081 652 ASP A C   
4713  O O   . ASP A 652 ? 1.4391 0.6028 0.7824 -0.0361 -0.2845 -0.2036 652 ASP A O   
4714  C CB  . ASP A 652 ? 1.4203 0.6280 0.8016 -0.0754 -0.2991 -0.2089 652 ASP A CB  
4715  C CG  . ASP A 652 ? 1.4307 0.6319 0.8281 -0.1045 -0.3088 -0.2018 652 ASP A CG  
4716  O OD1 . ASP A 652 ? 1.4667 0.6300 0.8515 -0.1077 -0.3162 -0.1974 652 ASP A OD1 
4717  O OD2 . ASP A 652 ? 1.4037 0.6386 0.8275 -0.1242 -0.3087 -0.2006 652 ASP A OD2 
4718  N N   . VAL A 653 ? 1.4590 0.5605 0.7871 -0.0472 -0.3110 -0.2076 653 VAL A N   
4719  C CA  . VAL A 653 ? 1.4731 0.5488 0.7896 -0.0378 -0.3090 -0.2015 653 VAL A CA  
4720  C C   . VAL A 653 ? 1.4911 0.5459 0.8141 -0.0629 -0.3197 -0.1899 653 VAL A C   
4721  O O   . VAL A 653 ? 1.5162 0.5402 0.8282 -0.0582 -0.3235 -0.1845 653 VAL A O   
4722  C CB  . VAL A 653 ? 1.5148 0.5581 0.8087 -0.0129 -0.3129 -0.2113 653 VAL A CB  
4723  C CG1 . VAL A 653 ? 1.5200 0.5468 0.8048 0.0033  -0.3069 -0.2071 653 VAL A CG1 
4724  C CG2 . VAL A 653 ? 1.5047 0.5679 0.7917 0.0063  -0.3045 -0.2227 653 VAL A CG2 
4725  N N   . SER A 654 ? 1.5319 0.6051 0.8741 -0.0900 -0.3242 -0.1859 654 SER A N   
4726  C CA  . SER A 654 ? 1.5533 0.6081 0.9025 -0.1169 -0.3342 -0.1747 654 SER A CA  
4727  C C   . SER A 654 ? 1.5355 0.5915 0.8854 -0.1224 -0.3267 -0.1608 654 SER A C   
4728  O O   . SER A 654 ? 1.4953 0.5777 0.8481 -0.1108 -0.3127 -0.1599 654 SER A O   
4729  C CB  . SER A 654 ? 1.5377 0.6214 0.9119 -0.1446 -0.3373 -0.1743 654 SER A CB  
4730  O OG  . SER A 654 ? 1.4817 0.6145 0.8754 -0.1494 -0.3238 -0.1723 654 SER A OG  
4731  N N   . HIS A 655 ? 1.5953 0.6217 0.9422 -0.1406 -0.3365 -0.1495 655 HIS A N   
4732  C CA  . HIS A 655 ? 1.5855 0.6097 0.9325 -0.1512 -0.3319 -0.1341 655 HIS A CA  
4733  C C   . HIS A 655 ? 1.5785 0.5924 0.9098 -0.1216 -0.3240 -0.1352 655 HIS A C   
4734  O O   . HIS A 655 ? 1.5363 0.5789 0.8741 -0.1167 -0.3105 -0.1323 655 HIS A O   
4735  C CB  . HIS A 655 ? 1.5366 0.6090 0.9080 -0.1747 -0.3214 -0.1272 655 HIS A CB  
4736  C CG  . HIS A 655 ? 1.5430 0.6291 0.9341 -0.2053 -0.3278 -0.1251 655 HIS A CG  
4737  N ND1 . HIS A 655 ? 1.5433 0.6428 0.9447 -0.2047 -0.3320 -0.1381 655 HIS A ND1 
4738  C CD2 . HIS A 655 ? 1.5503 0.6404 0.9536 -0.2371 -0.3300 -0.1117 655 HIS A CD2 
4739  C CE1 . HIS A 655 ? 1.5493 0.6610 0.9703 -0.2340 -0.3365 -0.1339 655 HIS A CE1 
4740  N NE2 . HIS A 655 ? 1.5534 0.6608 0.9762 -0.2544 -0.3347 -0.1178 655 HIS A NE2 
4741  N N   . ASN A 656 ? 1.6030 0.5776 0.9156 -0.1013 -0.3324 -0.1405 656 ASN A N   
4742  C CA  . ASN A 656 ? 1.6008 0.5662 0.9010 -0.0709 -0.3253 -0.1438 656 ASN A CA  
4743  C C   . ASN A 656 ? 1.6557 0.5715 0.9401 -0.0642 -0.3395 -0.1403 656 ASN A C   
4744  O O   . ASN A 656 ? 1.6917 0.5812 0.9746 -0.0858 -0.3535 -0.1322 656 ASN A O   
4745  C CB  . ASN A 656 ? 1.5833 0.5686 0.8810 -0.0438 -0.3157 -0.1602 656 ASN A CB  
4746  C CG  . ASN A 656 ? 1.5258 0.5560 0.8345 -0.0361 -0.2968 -0.1609 656 ASN A CG  
4747  O OD1 . ASN A 656 ? 1.5097 0.5443 0.8162 -0.0194 -0.2867 -0.1588 656 ASN A OD1 
4748  N ND2 . ASN A 656 ? 1.4948 0.5597 0.8170 -0.0476 -0.2921 -0.1643 656 ASN A ND2 
4749  N N   . ASN A 657 ? 1.6994 0.6045 0.9741 -0.0343 -0.3354 -0.1464 657 ASN A N   
4750  C CA  . ASN A 657 ? 1.7477 0.6099 1.0097 -0.0239 -0.3480 -0.1439 657 ASN A CA  
4751  C C   . ASN A 657 ? 1.7688 0.6211 1.0221 0.0063  -0.3487 -0.1612 657 ASN A C   
4752  O O   . ASN A 657 ? 1.7860 0.6224 1.0335 0.0281  -0.3495 -0.1639 657 ASN A O   
4753  C CB  . ASN A 657 ? 1.7368 0.5964 0.9986 -0.0182 -0.3432 -0.1323 657 ASN A CB  
4754  C CG  . ASN A 657 ? 1.7894 0.6034 1.0404 -0.0184 -0.3598 -0.1240 657 ASN A CG  
4755  O OD1 . ASN A 657 ? 1.8230 0.6120 1.0705 -0.0431 -0.3738 -0.1140 657 ASN A OD1 
4756  N ND2 . ASN A 657 ? 1.7972 0.6022 1.0443 0.0090  -0.3582 -0.1281 657 ASN A ND2 
4757  N N   . LEU A 658 ? 1.7691 0.6324 1.0223 0.0078  -0.3483 -0.1734 658 LEU A N   
4758  C CA  . LEU A 658 ? 1.7890 0.6463 1.0333 0.0340  -0.3479 -0.1902 658 LEU A CA  
4759  C C   . LEU A 658 ? 1.8477 0.6640 1.0825 0.0293  -0.3681 -0.1949 658 LEU A C   
4760  O O   . LEU A 658 ? 1.8707 0.6664 1.1070 0.0043  -0.3817 -0.1854 658 LEU A O   
4761  C CB  . LEU A 658 ? 1.7546 0.6491 1.0026 0.0403  -0.3347 -0.2007 658 LEU A CB  
4762  C CG  . LEU A 658 ? 1.6972 0.6335 0.9553 0.0473  -0.3140 -0.1972 658 LEU A CG  
4763  C CD1 . LEU A 658 ? 1.6608 0.6299 0.9293 0.0295  -0.3082 -0.1957 658 LEU A CD1 
4764  C CD2 . LEU A 658 ? 1.6871 0.6396 0.9415 0.0783  -0.2996 -0.2091 658 LEU A CD2 
4765  N N   . GLN A 659 ? 1.8458 0.6519 1.0716 0.0533  -0.3695 -0.2100 659 GLN A N   
4766  C CA  . GLN A 659 ? 1.9036 0.6703 1.1201 0.0534  -0.3885 -0.2168 659 GLN A CA  
4767  C C   . GLN A 659 ? 1.9155 0.6879 1.1240 0.0758  -0.3849 -0.2363 659 GLN A C   
4768  O O   . GLN A 659 ? 1.8828 0.6866 1.0921 0.0936  -0.3674 -0.2433 659 GLN A O   
4769  C CB  . GLN A 659 ? 1.9400 0.6715 1.1522 0.0601  -0.3996 -0.2111 659 GLN A CB  
4770  C CG  . GLN A 659 ? 1.9330 0.6729 1.1442 0.0911  -0.3892 -0.2195 659 GLN A CG  
4771  C CD  . GLN A 659 ? 1.9584 0.6705 1.1692 0.0952  -0.3987 -0.2105 659 GLN A CD  
4772  O OE1 . GLN A 659 ? 1.9797 0.6664 1.1893 0.0737  -0.4123 -0.1960 659 GLN A OE1 
4773  N NE2 . GLN A 659 ? 1.9574 0.6753 1.1700 0.1223  -0.3917 -0.2189 659 GLN A NE2 
4774  N N   . GLY A 660 ? 1.9720 0.7141 1.1728 0.0739  -0.4016 -0.2447 660 GLY A N   
4775  C CA  . GLY A 660 ? 1.9931 0.7344 1.1841 0.0947  -0.4008 -0.2635 660 GLY A CA  
4776  C C   . GLY A 660 ? 1.9881 0.7436 1.1774 0.0852  -0.4015 -0.2707 660 GLY A C   
4777  O O   . GLY A 660 ? 1.9572 0.7328 1.1556 0.0651  -0.3983 -0.2620 660 GLY A O   
4778  N N   . PRO A 661 ? 1.9973 0.7434 1.1755 0.0998  -0.4059 -0.2873 661 PRO A N   
4779  C CA  . PRO A 661 ? 1.9954 0.7548 1.1705 0.0930  -0.4071 -0.2952 661 PRO A CA  
4780  C C   . PRO A 661 ? 1.9447 0.7484 1.1211 0.1006  -0.3861 -0.2960 661 PRO A C   
4781  O O   . PRO A 661 ? 1.9274 0.7477 1.1006 0.1209  -0.3706 -0.2995 661 PRO A O   
4782  C CB  . PRO A 661 ? 2.0471 0.7815 1.2080 0.1097  -0.4173 -0.3131 661 PRO A CB  
4783  C CG  . PRO A 661 ? 2.0565 0.7836 1.2137 0.1326  -0.4111 -0.3172 661 PRO A CG  
4784  C CD  . PRO A 661 ? 2.0395 0.7611 1.2079 0.1224  -0.4114 -0.3001 661 PRO A CD  
4785  N N   . ILE A 662 ? 1.9458 0.7695 1.1286 0.0836  -0.3858 -0.2927 662 ILE A N   
4786  C CA  . ILE A 662 ? 1.8975 0.7633 1.0831 0.0878  -0.3676 -0.2918 662 ILE A CA  
4787  C C   . ILE A 662 ? 1.9131 0.7854 1.0824 0.1085  -0.3619 -0.3073 662 ILE A C   
4788  O O   . ILE A 662 ? 1.9577 0.8061 1.1162 0.1112  -0.3755 -0.3188 662 ILE A O   
4789  C CB  . ILE A 662 ? 1.8708 0.7561 1.0699 0.0631  -0.3706 -0.2844 662 ILE A CB  
4790  C CG1 . ILE A 662 ? 1.9090 0.7762 1.1046 0.0532  -0.3882 -0.2934 662 ILE A CG1 
4791  C CG2 . ILE A 662 ? 1.8520 0.7357 1.0673 0.0420  -0.3730 -0.2685 662 ILE A CG2 
4792  C CD1 . ILE A 662 ? 1.8835 0.7738 1.0949 0.0302  -0.3910 -0.2886 662 ILE A CD1 
4793  N N   . PRO A 663 ? 1.9499 0.8532 1.1166 0.1231  -0.3420 -0.3083 663 PRO A N   
4794  C CA  . PRO A 663 ? 1.9639 0.8767 1.1146 0.1391  -0.3358 -0.3216 663 PRO A CA  
4795  C C   . PRO A 663 ? 1.9647 0.8854 1.1136 0.1260  -0.3438 -0.3238 663 PRO A C   
4796  O O   . PRO A 663 ? 1.9363 0.8699 1.1001 0.1063  -0.3470 -0.3140 663 PRO A O   
4797  C CB  . PRO A 663 ? 1.9203 0.8682 1.0733 0.1524  -0.3116 -0.3178 663 PRO A CB  
4798  C CG  . PRO A 663 ? 1.8804 0.8423 1.0528 0.1391  -0.3066 -0.3019 663 PRO A CG  
4799  C CD  . PRO A 663 ? 1.9071 0.8343 1.0841 0.1284  -0.3244 -0.2983 663 PRO A CD  
4800  N N   . ASP A 664 ? 1.9540 0.8677 1.0850 0.1372  -0.3471 -0.3375 664 ASP A N   
4801  C CA  . ASP A 664 ? 1.9650 0.8808 1.0921 0.1270  -0.3579 -0.3422 664 ASP A CA  
4802  C C   . ASP A 664 ? 1.9345 0.8846 1.0556 0.1332  -0.3426 -0.3415 664 ASP A C   
4803  O O   . ASP A 664 ? 1.9483 0.9025 1.0514 0.1515  -0.3328 -0.3501 664 ASP A O   
4804  C CB  . ASP A 664 ? 2.0245 0.9086 1.1346 0.1346  -0.3734 -0.3579 664 ASP A CB  
4805  C CG  . ASP A 664 ? 2.0381 0.9276 1.1394 0.1303  -0.3815 -0.3653 664 ASP A CG  
4806  O OD1 . ASP A 664 ? 2.0131 0.9179 1.1287 0.1124  -0.3859 -0.3579 664 ASP A OD1 
4807  O OD2 . ASP A 664 ? 2.0750 0.9538 1.1554 0.1449  -0.3836 -0.3791 664 ASP A OD2 
4808  N N   . ASN A 665 ? 1.9548 0.9296 1.0916 0.1173  -0.3409 -0.3314 665 ASN A N   
4809  C CA  . ASN A 665 ? 1.9296 0.9345 1.0622 0.1200  -0.3308 -0.3303 665 ASN A CA  
4810  C C   . ASN A 665 ? 1.9175 0.9322 1.0647 0.0995  -0.3433 -0.3269 665 ASN A C   
4811  O O   . ASN A 665 ? 1.9266 0.9268 1.0880 0.0830  -0.3576 -0.3251 665 ASN A O   
4812  C CB  . ASN A 665 ? 1.8811 0.9164 1.0210 0.1264  -0.3086 -0.3202 665 ASN A CB  
4813  C CG  . ASN A 665 ? 1.8415 0.8875 1.0067 0.1112  -0.3067 -0.3068 665 ASN A CG  
4814  O OD1 . ASN A 665 ? 1.8329 0.8798 1.0137 0.0916  -0.3184 -0.3022 665 ASN A OD1 
4815  N ND2 . ASN A 665 ? 1.8174 0.8731 0.9873 0.1201  -0.2913 -0.3008 665 ASN A ND2 
4816  N N   . ALA A 666 ? 1.8949 0.9348 1.0396 0.1002  -0.3378 -0.3261 666 ALA A N   
4817  C CA  . ALA A 666 ? 1.8838 0.9362 1.0437 0.0824  -0.3496 -0.3245 666 ALA A CA  
4818  C C   . ALA A 666 ? 1.8429 0.9117 1.0334 0.0622  -0.3492 -0.3127 666 ALA A C   
4819  O O   . ALA A 666 ? 1.8449 0.9138 1.0525 0.0437  -0.3629 -0.3129 666 ALA A O   
4820  C CB  . ALA A 666 ? 1.8688 0.9460 1.0202 0.0886  -0.3427 -0.3247 666 ALA A CB  
4821  N N   . ALA A 667 ? 1.8126 0.8963 1.0112 0.0651  -0.3335 -0.3028 667 ALA A N   
4822  C CA  . ALA A 667 ? 1.7720 0.8742 0.9987 0.0461  -0.3318 -0.2915 667 ALA A CA  
4823  C C   . ALA A 667 ? 1.7936 0.8690 1.0290 0.0326  -0.3440 -0.2900 667 ALA A C   
4824  O O   . ALA A 667 ? 1.7813 0.8643 1.0388 0.0107  -0.3520 -0.2855 667 ALA A O   
4825  C CB  . ALA A 667 ? 1.7288 0.8542 0.9603 0.0541  -0.3117 -0.2820 667 ALA A CB  
4826  N N   . PHE A 668 ? 1.8406 0.8851 1.0599 0.0447  -0.3454 -0.2937 668 PHE A N   
4827  C CA  . PHE A 668 ? 1.8632 0.8791 1.0893 0.0326  -0.3573 -0.2910 668 PHE A CA  
4828  C C   . PHE A 668 ? 1.9002 0.8969 1.1293 0.0187  -0.3773 -0.2983 668 PHE A C   
4829  O O   . PHE A 668 ? 1.9069 0.8923 1.1514 -0.0012 -0.3872 -0.2931 668 PHE A O   
4830  C CB  . PHE A 668 ? 1.8960 0.8840 1.1047 0.0510  -0.3546 -0.2941 668 PHE A CB  
4831  C CG  . PHE A 668 ? 1.8627 0.8641 1.0764 0.0580  -0.3382 -0.2844 668 PHE A CG  
4832  C CD1 . PHE A 668 ? 1.8383 0.8429 1.0700 0.0411  -0.3384 -0.2720 668 PHE A CD1 
4833  C CD2 . PHE A 668 ? 1.8527 0.8643 1.0536 0.0809  -0.3223 -0.2878 668 PHE A CD2 
4834  C CE1 . PHE A 668 ? 1.8053 0.8219 1.0412 0.0480  -0.3240 -0.2635 668 PHE A CE1 
4835  C CE2 . PHE A 668 ? 1.8170 0.8424 1.0245 0.0877  -0.3072 -0.2795 668 PHE A CE2 
4836  C CZ  . PHE A 668 ? 1.7965 0.8238 1.0212 0.0717  -0.3085 -0.2676 668 PHE A CZ  
4837  N N   . ARG A 669 ? 1.8414 0.8340 1.0558 0.0283  -0.3832 -0.3101 669 ARG A N   
4838  C CA  . ARG A 669 ? 1.8797 0.8533 1.0962 0.0169  -0.4026 -0.3186 669 ARG A CA  
4839  C C   . ARG A 669 ? 1.8532 0.8507 1.0978 -0.0081 -0.4078 -0.3135 669 ARG A C   
4840  O O   . ARG A 669 ? 1.8696 0.8534 1.1292 -0.0274 -0.4199 -0.3122 669 ARG A O   
4841  C CB  . ARG A 669 ? 1.9108 0.8781 1.1046 0.0336  -0.4068 -0.3324 669 ARG A CB  
4842  C CG  . ARG A 669 ? 1.9482 0.8882 1.1158 0.0562  -0.4049 -0.3408 669 ARG A CG  
4843  C CD  . ARG A 669 ? 1.9876 0.9172 1.1333 0.0688  -0.4127 -0.3556 669 ARG A CD  
4844  N NE  . ARG A 669 ? 1.9890 0.9247 1.1114 0.0923  -0.3980 -0.3600 669 ARG A NE  
4845  C CZ  . ARG A 669 ? 1.9827 0.9373 1.0921 0.1009  -0.3916 -0.3633 669 ARG A CZ  
4846  N NH1 . ARG A 669 ? 1.9741 0.9435 1.0914 0.0894  -0.3995 -0.3633 669 ARG A NH1 
4847  N NH2 . ARG A 669 ? 1.9865 0.9456 1.0750 0.1210  -0.3769 -0.3668 669 ARG A NH2 
4848  N N   . ASN A 670 ? 1.8619 0.8962 1.1152 -0.0086 -0.3985 -0.3107 670 ASN A N   
4849  C CA  . ASN A 670 ? 1.8343 0.8966 1.1165 -0.0308 -0.4024 -0.3075 670 ASN A CA  
4850  C C   . ASN A 670 ? 1.7958 0.8752 1.1026 -0.0485 -0.3948 -0.2943 670 ASN A C   
4851  O O   . ASN A 670 ? 1.7691 0.8775 1.1029 -0.0672 -0.3952 -0.2912 670 ASN A O   
4852  C CB  . ASN A 670 ? 1.8076 0.9025 1.0900 -0.0237 -0.3963 -0.3098 670 ASN A CB  
4853  C CG  . ASN A 670 ? 1.8450 0.9237 1.0985 -0.0042 -0.4015 -0.3214 670 ASN A CG  
4854  O OD1 . ASN A 670 ? 1.8706 0.9260 1.0988 0.0139  -0.3979 -0.3249 670 ASN A OD1 
4855  N ND2 . ASN A 670 ? 1.8493 0.9413 1.1069 -0.0076 -0.4100 -0.3280 670 ASN A ND2 
4856  N N   . ALA A 671 ? 1.7501 0.8134 1.0488 -0.0429 -0.3877 -0.2869 671 ALA A N   
4857  C CA  . ALA A 671 ? 1.7174 0.7941 1.0366 -0.0596 -0.3810 -0.2740 671 ALA A CA  
4858  C C   . ALA A 671 ? 1.7366 0.8019 1.0750 -0.0860 -0.3942 -0.2720 671 ALA A C   
4859  O O   . ALA A 671 ? 1.7843 0.8132 1.1120 -0.0866 -0.4072 -0.2770 671 ALA A O   
4860  C CB  . ALA A 671 ? 1.7189 0.7768 1.0228 -0.0461 -0.3722 -0.2673 671 ALA A CB  
4861  N N   . PRO A 672 ? 1.7240 0.8204 1.0915 -0.1083 -0.3910 -0.2652 672 PRO A N   
4862  C CA  . PRO A 672 ? 1.7417 0.8302 1.1294 -0.1354 -0.4015 -0.2626 672 PRO A CA  
4863  C C   . PRO A 672 ? 1.7593 0.8177 1.1403 -0.1421 -0.4020 -0.2514 672 PRO A C   
4864  O O   . PRO A 672 ? 1.7509 0.8001 1.1152 -0.1262 -0.3933 -0.2457 672 PRO A O   
4865  C CB  . PRO A 672 ? 1.6929 0.8307 1.1143 -0.1546 -0.3941 -0.2588 672 PRO A CB  
4866  C CG  . PRO A 672 ? 1.6474 0.8140 1.0653 -0.1385 -0.3788 -0.2554 672 PRO A CG  
4867  C CD  . PRO A 672 ? 1.6668 0.8074 1.0505 -0.1096 -0.3763 -0.2590 672 PRO A CD  
4868  N N   . PRO A 673 ? 1.7666 0.8088 1.1603 -0.1655 -0.4121 -0.2477 673 PRO A N   
4869  C CA  . PRO A 673 ? 1.7871 0.7983 1.1731 -0.1732 -0.4136 -0.2353 673 PRO A CA  
4870  C C   . PRO A 673 ? 1.7438 0.7779 1.1376 -0.1788 -0.3991 -0.2212 673 PRO A C   
4871  O O   . PRO A 673 ? 1.7577 0.7654 1.1381 -0.1767 -0.3984 -0.2112 673 PRO A O   
4872  C CB  . PRO A 673 ? 1.8181 0.8173 1.2216 -0.2013 -0.4257 -0.2339 673 PRO A CB  
4873  C CG  . PRO A 673 ? 1.8337 0.8383 1.2421 -0.1985 -0.4349 -0.2499 673 PRO A CG  
4874  C CD  . PRO A 673 ? 1.7881 0.8330 1.1998 -0.1837 -0.4241 -0.2558 673 PRO A CD  
4875  N N   . ASP A 674 ? 1.7606 0.8428 1.1760 -0.1856 -0.3882 -0.2204 674 ASP A N   
4876  C CA  . ASP A 674 ? 1.7197 0.8261 1.1432 -0.1904 -0.3742 -0.2080 674 ASP A CA  
4877  C C   . ASP A 674 ? 1.7102 0.8086 1.1100 -0.1621 -0.3648 -0.2071 674 ASP A C   
4878  O O   . ASP A 674 ? 1.6900 0.7916 1.0886 -0.1634 -0.3560 -0.1959 674 ASP A O   
4879  C CB  . ASP A 674 ? 1.6664 0.8288 1.1211 -0.2030 -0.3652 -0.2093 674 ASP A CB  
4880  C CG  . ASP A 674 ? 1.6793 0.8557 1.1605 -0.2276 -0.3734 -0.2141 674 ASP A CG  
4881  O OD1 . ASP A 674 ? 1.7223 0.8747 1.2062 -0.2469 -0.3810 -0.2082 674 ASP A OD1 
4882  O OD2 . ASP A 674 ? 1.6570 0.8686 1.1569 -0.2277 -0.3721 -0.2238 674 ASP A OD2 
4883  N N   . ALA A 675 ? 1.6416 0.7311 1.0231 -0.1370 -0.3659 -0.2187 675 ALA A N   
4884  C CA  . ALA A 675 ? 1.6285 0.7157 0.9900 -0.1095 -0.3549 -0.2193 675 ALA A CA  
4885  C C   . ALA A 675 ? 1.6638 0.7079 1.0031 -0.0978 -0.3582 -0.2154 675 ALA A C   
4886  O O   . ALA A 675 ? 1.6569 0.6979 0.9804 -0.0737 -0.3490 -0.2172 675 ALA A O   
4887  C CB  . ALA A 675 ? 1.6321 0.7257 0.9813 -0.0879 -0.3541 -0.2327 675 ALA A CB  
4888  N N   . PHE A 676 ? 1.6077 0.6194 0.9465 -0.1137 -0.3709 -0.2103 676 PHE A N   
4889  C CA  . PHE A 676 ? 1.6430 0.6132 0.9623 -0.1028 -0.3756 -0.2061 676 PHE A CA  
4890  C C   . PHE A 676 ? 1.6565 0.6096 0.9829 -0.1273 -0.3812 -0.1909 676 PHE A C   
4891  O O   . PHE A 676 ? 1.6952 0.6086 1.0067 -0.1221 -0.3892 -0.1869 676 PHE A O   
4892  C CB  . PHE A 676 ? 1.6957 0.6295 0.9975 -0.0890 -0.3890 -0.2183 676 PHE A CB  
4893  C CG  . PHE A 676 ? 1.6895 0.6373 0.9816 -0.0663 -0.3843 -0.2329 676 PHE A CG  
4894  C CD1 . PHE A 676 ? 1.6832 0.6307 0.9586 -0.0382 -0.3738 -0.2374 676 PHE A CD1 
4895  C CD2 . PHE A 676 ? 1.6913 0.6536 0.9913 -0.0735 -0.3901 -0.2420 676 PHE A CD2 
4896  C CE1 . PHE A 676 ? 1.6799 0.6408 0.9451 -0.0189 -0.3686 -0.2496 676 PHE A CE1 
4897  C CE2 . PHE A 676 ? 1.6888 0.6625 0.9776 -0.0535 -0.3863 -0.2541 676 PHE A CE2 
4898  C CZ  . PHE A 676 ? 1.6837 0.6564 0.9543 -0.0267 -0.3753 -0.2575 676 PHE A CZ  
4899  N N   . GLU A 677 ? 1.6858 0.6682 1.0347 -0.1538 -0.3771 -0.1823 677 GLU A N   
4900  C CA  . GLU A 677 ? 1.7009 0.6696 1.0568 -0.1803 -0.3817 -0.1670 677 GLU A CA  
4901  C C   . GLU A 677 ? 1.6959 0.6509 1.0389 -0.1724 -0.3755 -0.1548 677 GLU A C   
4902  O O   . GLU A 677 ? 1.6633 0.6352 1.0011 -0.1521 -0.3636 -0.1570 677 GLU A O   
4903  C CB  . GLU A 677 ? 1.6651 0.6770 1.0504 -0.2092 -0.3756 -0.1616 677 GLU A CB  
4904  C CG  . GLU A 677 ? 1.6865 0.7009 1.0880 -0.2280 -0.3859 -0.1685 677 GLU A CG  
4905  C CD  . GLU A 677 ? 1.6732 0.7129 1.1013 -0.2630 -0.3829 -0.1577 677 GLU A CD  
4906  O OE1 . GLU A 677 ? 1.6259 0.7054 1.0693 -0.2707 -0.3696 -0.1513 677 GLU A OE1 
4907  O OE2 . GLU A 677 ? 1.7103 0.7318 1.1450 -0.2829 -0.3931 -0.1559 677 GLU A OE2 
4908  N N   . GLY A 678 ? 1.7248 0.6488 1.0630 -0.1887 -0.3839 -0.1417 678 GLY A N   
4909  C CA  . GLY A 678 ? 1.7211 0.6337 1.0498 -0.1868 -0.3792 -0.1276 678 GLY A CA  
4910  C C   . GLY A 678 ? 1.7255 0.6194 1.0344 -0.1520 -0.3765 -0.1334 678 GLY A C   
4911  O O   . GLY A 678 ? 1.6938 0.6029 1.0015 -0.1428 -0.3649 -0.1281 678 GLY A O   
4912  N N   . ASN A 679 ? 1.7591 0.6227 1.0539 -0.1323 -0.3864 -0.1451 679 ASN A N   
4913  C CA  . ASN A 679 ? 1.7710 0.6148 1.0486 -0.1000 -0.3849 -0.1510 679 ASN A CA  
4914  C C   . ASN A 679 ? 1.8282 0.6222 1.0928 -0.1004 -0.4009 -0.1447 679 ASN A C   
4915  O O   . ASN A 679 ? 1.8579 0.6327 1.1256 -0.1261 -0.4122 -0.1347 679 ASN A O   
4916  C CB  . ASN A 679 ? 1.7685 0.6213 1.0405 -0.0745 -0.3819 -0.1704 679 ASN A CB  
4917  C CG  . ASN A 679 ? 1.7137 0.6086 0.9907 -0.0587 -0.3627 -0.1753 679 ASN A CG  
4918  O OD1 . ASN A 679 ? 1.7003 0.5977 0.9712 -0.0377 -0.3533 -0.1753 679 ASN A OD1 
4919  N ND2 . ASN A 679 ? 1.6819 0.6116 0.9718 -0.0688 -0.3570 -0.1796 679 ASN A ND2 
4920  N N   . LYS A 680 ? 1.8780 0.6527 1.1294 -0.0716 -0.4014 -0.1504 680 LYS A N   
4921  C CA  . LYS A 680 ? 1.9306 0.6597 1.1708 -0.0702 -0.4167 -0.1439 680 LYS A CA  
4922  C C   . LYS A 680 ? 1.9813 0.6787 1.2132 -0.0607 -0.4319 -0.1571 680 LYS A C   
4923  O O   . LYS A 680 ? 2.0237 0.6916 1.2544 -0.0799 -0.4473 -0.1512 680 LYS A O   
4924  C CB  . LYS A 680 ? 1.9227 0.6481 1.1562 -0.0452 -0.4103 -0.1421 680 LYS A CB  
4925  C CG  . LYS A 680 ? 1.9423 0.6442 1.1722 -0.0583 -0.4174 -0.1228 680 LYS A CG  
4926  C CD  . LYS A 680 ? 1.9532 0.6406 1.1756 -0.0289 -0.4175 -0.1254 680 LYS A CD  
4927  C CE  . LYS A 680 ? 1.9651 0.6354 1.1842 -0.0406 -0.4225 -0.1053 680 LYS A CE  
4928  N NZ  . LYS A 680 ? 1.9685 0.6318 1.1841 -0.0109 -0.4211 -0.1085 680 LYS A NZ  
4929  N N   . ASP A 681 ? 1.9578 0.6615 1.1839 -0.0319 -0.4274 -0.1749 681 ASP A N   
4930  C CA  . ASP A 681 ? 2.0081 0.6808 1.2250 -0.0197 -0.4416 -0.1886 681 ASP A CA  
4931  C C   . ASP A 681 ? 1.9944 0.6893 1.2100 -0.0046 -0.4348 -0.2073 681 ASP A C   
4932  O O   . ASP A 681 ? 2.0162 0.7006 1.2225 0.0203  -0.4364 -0.2219 681 ASP A O   
4933  C CB  . ASP A 681 ? 2.0394 0.6840 1.2465 0.0040  -0.4474 -0.1911 681 ASP A CB  
4934  C CG  . ASP A 681 ? 2.1046 0.7030 1.3043 0.0013  -0.4693 -0.1942 681 ASP A CG  
4935  O OD1 . ASP A 681 ? 2.1288 0.7073 1.3310 -0.0261 -0.4812 -0.1823 681 ASP A OD1 
4936  O OD2 . ASP A 681 ? 2.1325 0.7154 1.3248 0.0261  -0.4741 -0.2089 681 ASP A OD2 
4937  N N   . LEU A 682 ? 1.9553 0.6821 1.1805 -0.0193 -0.4270 -0.2073 682 LEU A N   
4938  C CA  . LEU A 682 ? 1.9418 0.6911 1.1648 -0.0053 -0.4204 -0.2237 682 LEU A CA  
4939  C C   . LEU A 682 ? 1.9917 0.7133 1.2088 -0.0076 -0.4374 -0.2351 682 LEU A C   
4940  O O   . LEU A 682 ? 2.0059 0.7201 1.2313 -0.0324 -0.4480 -0.2308 682 LEU A O   
4941  C CB  . LEU A 682 ? 1.8903 0.6823 1.1266 -0.0201 -0.4083 -0.2202 682 LEU A CB  
4942  C CG  . LEU A 682 ? 1.8353 0.6634 1.0762 -0.0102 -0.3881 -0.2153 682 LEU A CG  
4943  C CD1 . LEU A 682 ? 1.7894 0.6586 1.0448 -0.0257 -0.3788 -0.2133 682 LEU A CD1 
4944  C CD2 . LEU A 682 ? 1.8318 0.6667 1.0614 0.0229  -0.3776 -0.2278 682 LEU A CD2 
4945  N N   . CYS A 683 ? 2.0129 0.7210 1.2171 0.0180  -0.4396 -0.2503 683 CYS A N   
4946  C CA  . CYS A 683 ? 2.0611 0.7438 1.2584 0.0194  -0.4553 -0.2634 683 CYS A CA  
4947  C C   . CYS A 683 ? 2.0441 0.7527 1.2441 0.0145  -0.4520 -0.2727 683 CYS A C   
4948  O O   . CYS A 683 ? 2.0452 0.7560 1.2561 -0.0097 -0.4596 -0.2685 683 CYS A O   
4949  C CB  . CYS A 683 ? 2.0940 0.7573 1.2771 0.0490  -0.4575 -0.2777 683 CYS A CB  
4950  S SG  . CYS A 683 ? 2.1483 0.7876 1.3207 0.0563  -0.4734 -0.2979 683 CYS A SG  
4951  N N   . ASN B 26  ? 0.6473 0.6608 0.4962 0.1248  -0.2022 0.0640  26  ASN B N   
4952  C CA  . ASN B 26  ? 0.6904 0.6688 0.5299 0.1205  -0.2351 0.0560  26  ASN B CA  
4953  C C   . ASN B 26  ? 0.7505 0.6369 0.5206 0.1347  -0.2387 0.0538  26  ASN B C   
4954  O O   . ASN B 26  ? 0.7582 0.6154 0.4906 0.1472  -0.2131 0.0546  26  ASN B O   
4955  C CB  . ASN B 26  ? 0.6840 0.6973 0.5675 0.0915  -0.2432 0.0667  26  ASN B CB  
4956  C CG  . ASN B 26  ? 0.6949 0.6786 0.5575 0.0837  -0.2280 0.0858  26  ASN B CG  
4957  O OD1 . ASN B 26  ? 0.6881 0.6526 0.5219 0.0998  -0.2051 0.0892  26  ASN B OD1 
4958  N ND2 . ASN B 26  ? 0.7172 0.6961 0.5956 0.0585  -0.2433 0.0969  26  ASN B ND2 
4959  N N   . ALA B 27  ? 0.7307 0.5779 0.4908 0.1293  -0.2664 0.0488  27  ALA B N   
4960  C CA  . ALA B 27  ? 0.7915 0.5567 0.4899 0.1427  -0.2667 0.0411  27  ALA B CA  
4961  C C   . ALA B 27  ? 0.7959 0.5402 0.4667 0.1482  -0.2417 0.0517  27  ALA B C   
4962  O O   . ALA B 27  ? 0.8208 0.5289 0.4442 0.1647  -0.2204 0.0460  27  ALA B O   
4963  C CB  . ALA B 27  ? 0.8374 0.5677 0.5375 0.1359  -0.3054 0.0324  27  ALA B CB  
4964  N N   . GLU B 28  ? 0.8497 0.6156 0.5479 0.1346  -0.2459 0.0664  28  GLU B N   
4965  C CA  . GLU B 28  ? 0.8571 0.6040 0.5339 0.1429  -0.2266 0.0721  28  GLU B CA  
4966  C C   . GLU B 28  ? 0.8178 0.5980 0.4946 0.1549  -0.1902 0.0743  28  GLU B C   
4967  O O   . GLU B 28  ? 0.8374 0.5926 0.4804 0.1725  -0.1708 0.0687  28  GLU B O   
4968  C CB  . GLU B 28  ? 0.8541 0.6120 0.5583 0.1231  -0.2421 0.0888  28  GLU B CB  
4969  C CG  . GLU B 28  ? 0.9072 0.6186 0.6061 0.1095  -0.2803 0.0877  28  GLU B CG  
4970  C CD  . GLU B 28  ? 0.9148 0.6308 0.6376 0.0820  -0.2946 0.1083  28  GLU B CD  
4971  O OE1 . GLU B 28  ? 0.8903 0.6292 0.6195 0.0815  -0.2724 0.1190  28  GLU B OE1 
4972  O OE2 . GLU B 28  ? 0.9501 0.6456 0.6863 0.0584  -0.3270 0.1129  28  GLU B OE2 
4973  N N   . GLY B 29  ? 0.7913 0.6318 0.5092 0.1460  -0.1808 0.0796  29  GLY B N   
4974  C CA  . GLY B 29  ? 0.7541 0.6277 0.4806 0.1542  -0.1479 0.0798  29  GLY B CA  
4975  C C   . GLY B 29  ? 0.7843 0.6205 0.4632 0.1700  -0.1357 0.0708  29  GLY B C   
4976  O O   . GLY B 29  ? 0.7827 0.6198 0.4490 0.1782  -0.1067 0.0696  29  GLY B O   
4977  N N   . ASP B 30  ? 0.7806 0.5869 0.4394 0.1694  -0.1547 0.0623  30  ASP B N   
4978  C CA  . ASP B 30  ? 0.8259 0.5839 0.4297 0.1797  -0.1434 0.0550  30  ASP B CA  
4979  C C   . ASP B 30  ? 0.8821 0.5869 0.4284 0.1931  -0.1319 0.0512  30  ASP B C   
4980  O O   . ASP B 30  ? 0.9135 0.5952 0.4136 0.2023  -0.1058 0.0516  30  ASP B O   
4981  C CB  . ASP B 30  ? 0.8540 0.5862 0.4485 0.1778  -0.1700 0.0434  30  ASP B CB  
4982  C CG  . ASP B 30  ? 0.8080 0.5919 0.4515 0.1714  -0.1796 0.0415  30  ASP B CG  
4983  O OD1 . ASP B 30  ? 0.7787 0.5896 0.4329 0.1719  -0.1606 0.0471  30  ASP B OD1 
4984  O OD2 . ASP B 30  ? 0.8047 0.6038 0.4771 0.1674  -0.2075 0.0321  30  ASP B OD2 
4985  N N   . ALA B 31  ? 0.8768 0.5613 0.4224 0.1945  -0.1515 0.0471  31  ALA B N   
4986  C CA  . ALA B 31  ? 0.9339 0.5698 0.4252 0.2129  -0.1453 0.0391  31  ALA B CA  
4987  C C   . ALA B 31  ? 0.9180 0.5795 0.4072 0.2251  -0.1138 0.0434  31  ALA B C   
4988  O O   . ALA B 31  ? 0.9563 0.6002 0.4020 0.2386  -0.0864 0.0354  31  ALA B O   
4989  C CB  . ALA B 31  ? 0.9574 0.5676 0.4565 0.2108  -0.1781 0.0330  31  ALA B CB  
4990  N N   . LEU B 32  ? 0.8868 0.6019 0.4397 0.2141  -0.1114 0.0505  32  LEU B N   
4991  C CA  . LEU B 32  ? 0.8599 0.6137 0.4374 0.2203  -0.0802 0.0468  32  LEU B CA  
4992  C C   . LEU B 32  ? 0.8383 0.6234 0.4225 0.2158  -0.0442 0.0476  32  LEU B C   
4993  O O   . LEU B 32  ? 0.8398 0.6457 0.4274 0.2237  -0.0131 0.0388  32  LEU B O   
4994  C CB  . LEU B 32  ? 0.8092 0.6049 0.4449 0.2100  -0.0905 0.0554  32  LEU B CB  
4995  C CG  . LEU B 32  ? 0.8426 0.6033 0.4688 0.2151  -0.1200 0.0542  32  LEU B CG  
4996  C CD1 . LEU B 32  ? 0.8046 0.5971 0.4773 0.1959  -0.1339 0.0701  32  LEU B CD1 
4997  C CD2 . LEU B 32  ? 0.8754 0.6214 0.4800 0.2415  -0.1084 0.0361  32  LEU B CD2 
4998  N N   . SER B 33  ? 0.8370 0.6262 0.4256 0.2030  -0.0501 0.0560  33  SER B N   
4999  C CA  . SER B 33  ? 0.8308 0.6347 0.4174 0.1965  -0.0221 0.0583  33  SER B CA  
5000  C C   . SER B 33  ? 0.9038 0.6583 0.4187 0.2027  -0.0004 0.0538  33  SER B C   
5001  O O   . SER B 33  ? 0.9093 0.6804 0.4230 0.1958  0.0345  0.0542  33  SER B O   
5002  C CB  . SER B 33  ? 0.8092 0.6189 0.4099 0.1860  -0.0421 0.0652  33  SER B CB  
5003  O OG  . SER B 33  ? 0.7432 0.6103 0.4105 0.1796  -0.0542 0.0686  33  SER B OG  
5004  N N   . ALA B 34  ? 0.9393 0.6331 0.3926 0.2142  -0.0203 0.0494  34  ALA B N   
5005  C CA  . ALA B 34  ? 1.0198 0.6651 0.3946 0.2230  0.0020  0.0442  34  ALA B CA  
5006  C C   . ALA B 34  ? 1.0222 0.7024 0.4084 0.2325  0.0385  0.0319  34  ALA B C   
5007  O O   . ALA B 34  ? 1.0588 0.7430 0.4157 0.2281  0.0787  0.0300  34  ALA B O   
5008  C CB  . ALA B 34  ? 1.0855 0.6606 0.3980 0.2380  -0.0321 0.0377  34  ALA B CB  
5009  N N   . LEU B 35  ? 0.9829 0.6882 0.4107 0.2450  0.0239  0.0222  35  LEU B N   
5010  C CA  . LEU B 35  ? 0.9872 0.7318 0.4363 0.2591  0.0515  0.0050  35  LEU B CA  
5011  C C   . LEU B 35  ? 0.9494 0.7610 0.4561 0.2436  0.0888  0.0068  35  LEU B C   
5012  O O   . LEU B 35  ? 0.9655 0.8065 0.4709 0.2468  0.1281  -0.0062 35  LEU B O   
5013  C CB  . LEU B 35  ? 0.9833 0.7327 0.4666 0.2741  0.0187  -0.0032 35  LEU B CB  
5014  C CG  . LEU B 35  ? 1.0379 0.7976 0.5210 0.3023  0.0240  -0.0286 35  LEU B CG  
5015  C CD1 . LEU B 35  ? 1.0420 0.7805 0.5444 0.3115  -0.0220 -0.0293 35  LEU B CD1 
5016  C CD2 . LEU B 35  ? 1.0086 0.8409 0.5456 0.3032  0.0630  -0.0411 35  LEU B CD2 
5017  N N   . LYS B 36  ? 0.8913 0.7313 0.4514 0.2267  0.0766  0.0208  36  LYS B N   
5018  C CA  . LYS B 36  ? 0.8411 0.7433 0.4628 0.2141  0.1036  0.0207  36  LYS B CA  
5019  C C   . LYS B 36  ? 0.8789 0.7782 0.4727 0.1967  0.1420  0.0248  36  LYS B C   
5020  O O   . LYS B 36  ? 0.8623 0.8135 0.4988 0.1890  0.1750  0.0169  36  LYS B O   
5021  C CB  . LYS B 36  ? 0.7767 0.7008 0.4474 0.2022  0.0788  0.0345  36  LYS B CB  
5022  C CG  . LYS B 36  ? 0.7296 0.7081 0.4586 0.1895  0.0989  0.0353  36  LYS B CG  
5023  C CD  . LYS B 36  ? 0.6823 0.6722 0.4411 0.1803  0.0728  0.0480  36  LYS B CD  
5024  C CE  . LYS B 36  ? 0.6419 0.6793 0.4550 0.1705  0.0872  0.0469  36  LYS B CE  
5025  N NZ  . LYS B 36  ? 0.5959 0.6870 0.4695 0.1821  0.0887  0.0354  36  LYS B NZ  
5026  N N   . ASN B 37  ? 0.9776 0.8138 0.4982 0.1892  0.1369  0.0368  37  ASN B N   
5027  C CA  . ASN B 37  ? 1.0213 0.8393 0.5014 0.1679  0.1702  0.0462  37  ASN B CA  
5028  C C   . ASN B 37  ? 1.0812 0.8906 0.5064 0.1727  0.2100  0.0355  37  ASN B C   
5029  O O   . ASN B 37  ? 1.1124 0.9297 0.5209 0.1501  0.2506  0.0413  37  ASN B O   
5030  C CB  . ASN B 37  ? 1.0397 0.7850 0.4574 0.1588  0.1425  0.0640  37  ASN B CB  
5031  C CG  . ASN B 37  ? 0.9823 0.7454 0.4552 0.1535  0.1081  0.0714  37  ASN B CG  
5032  O OD1 . ASN B 37  ? 0.9898 0.7562 0.4766 0.1354  0.1123  0.0808  37  ASN B OD1 
5033  N ND2 . ASN B 37  ? 0.9373 0.7120 0.4406 0.1685  0.0735  0.0666  37  ASN B ND2 
5034  N N   . SER B 38  ? 1.0758 0.8694 0.4711 0.2006  0.1995  0.0196  38  SER B N   
5035  C CA  . SER B 38  ? 1.1435 0.9395 0.5006 0.2068  0.2310  0.0043  38  SER B CA  
5036  C C   . SER B 38  ? 1.1098 0.9898 0.5377 0.2177  0.2580  -0.0220 38  SER B C   
5037  O O   . SER B 38  ? 1.1595 1.0608 0.5751 0.2199  0.2839  -0.0395 38  SER B O   
5038  C CB  . SER B 38  ? 1.1992 0.9306 0.4902 0.2323  0.1982  -0.0026 38  SER B CB  
5039  O OG  . SER B 38  ? 1.2427 0.9974 0.5249 0.2489  0.2186  -0.0261 38  SER B OG  
5040  N N   . LEU B 39  ? 1.0325 0.9628 0.5360 0.2257  0.2496  -0.0277 39  LEU B N   
5041  C CA  . LEU B 39  ? 0.9980 1.0082 0.5804 0.2359  0.2661  -0.0553 39  LEU B CA  
5042  C C   . LEU B 39  ? 0.9525 1.0267 0.6077 0.2071  0.2955  -0.0518 39  LEU B C   
5043  O O   . LEU B 39  ? 0.9097 0.9754 0.5841 0.1917  0.2824  -0.0306 39  LEU B O   
5044  C CB  . LEU B 39  ? 0.9511 0.9671 0.5699 0.2688  0.2251  -0.0686 39  LEU B CB  
5045  C CG  . LEU B 39  ? 0.9983 0.9656 0.5647 0.3030  0.1945  -0.0836 39  LEU B CG  
5046  C CD1 . LEU B 39  ? 0.9587 0.9458 0.5792 0.3280  0.1593  -0.1006 39  LEU B CD1 
5047  C CD2 . LEU B 39  ? 1.0682 1.0423 0.6041 0.3066  0.2201  -0.1029 39  LEU B CD2 
5048  N N   . ALA B 40  ? 0.9531 1.0927 0.6554 0.1970  0.3296  -0.0755 40  ALA B N   
5049  C CA  . ALA B 40  ? 0.9073 1.1168 0.6955 0.1734  0.3517  -0.0811 40  ALA B CA  
5050  C C   . ALA B 40  ? 0.8385 1.0892 0.7085 0.1987  0.3216  -0.1020 40  ALA B C   
5051  O O   . ALA B 40  ? 0.8487 1.1075 0.7294 0.2265  0.3071  -0.1273 40  ALA B O   
5052  C CB  . ALA B 40  ? 0.9555 1.2213 0.7626 0.1483  0.4005  -0.1014 40  ALA B CB  
5053  N N   . ASP B 41  ? 0.7992 1.0691 0.7222 0.1899  0.3081  -0.0905 41  ASP B N   
5054  C CA  . ASP B 41  ? 0.7399 1.0324 0.7269 0.2113  0.2710  -0.1032 41  ASP B CA  
5055  C C   . ASP B 41  ? 0.7070 1.0587 0.7837 0.1925  0.2856  -0.1158 41  ASP B C   
5056  O O   . ASP B 41  ? 0.6657 1.0251 0.7706 0.1786  0.2773  -0.1004 41  ASP B O   
5057  C CB  . ASP B 41  ? 0.7064 0.9579 0.6676 0.2221  0.2338  -0.0772 41  ASP B CB  
5058  C CG  . ASP B 41  ? 0.6600 0.9200 0.6640 0.2441  0.1922  -0.0874 41  ASP B CG  
5059  O OD1 . ASP B 41  ? 0.6476 0.9462 0.7137 0.2456  0.1901  -0.1098 41  ASP B OD1 
5060  O OD2 . ASP B 41  ? 0.6662 0.8876 0.6368 0.2583  0.1614  -0.0713 41  ASP B OD2 
5061  N N   . PRO B 42  ? 0.7790 0.9288 0.7188 0.2419  0.3064  0.2685  42  PRO B N   
5062  C CA  . PRO B 42  ? 0.7356 0.9408 0.7828 0.2433  0.3163  0.2728  42  PRO B CA  
5063  C C   . PRO B 42  ? 0.6922 0.9072 0.7641 0.2474  0.2976  0.2396  42  PRO B C   
5064  O O   . PRO B 42  ? 0.6456 0.9045 0.8182 0.2386  0.2872  0.2316  42  PRO B O   
5065  C CB  . PRO B 42  ? 0.7794 0.9956 0.8172 0.2634  0.3366  0.2818  42  PRO B CB  
5066  C CG  . PRO B 42  ? 0.8336 0.9968 0.7562 0.2794  0.3323  0.2636  42  PRO B CG  
5067  C CD  . PRO B 42  ? 0.8406 0.9649 0.7069 0.2627  0.3145  0.2601  42  PRO B CD  
5068  N N   . ASN B 43  ? 0.7329 0.9053 0.7188 0.2588  0.2858  0.2171  43  ASN B N   
5069  C CA  . ASN B 43  ? 0.7047 0.8845 0.7033 0.2664  0.2654  0.1883  43  ASN B CA  
5070  C C   . ASN B 43  ? 0.6998 0.8621 0.6969 0.2447  0.2325  0.1725  43  ASN B C   
5071  O O   . ASN B 43  ? 0.6782 0.8440 0.6725 0.2511  0.2134  0.1504  43  ASN B O   
5072  C CB  . ASN B 43  ? 0.7481 0.8849 0.6643 0.2860  0.2634  0.1753  43  ASN B CB  
5073  C CG  . ASN B 43  ? 0.7658 0.9275 0.7092 0.3024  0.2756  0.1774  43  ASN B CG  
5074  O OD1 . ASN B 43  ? 0.8121 0.9606 0.7251 0.3119  0.2947  0.1901  43  ASN B OD1 
5075  N ND2 . ASN B 43  ? 0.7346 0.9349 0.7348 0.3054  0.2622  0.1632  43  ASN B ND2 
5076  N N   . LYS B 44  ? 0.6715 0.8190 0.6707 0.2215  0.2265  0.1859  44  LYS B N   
5077  C CA  . LYS B 44  ? 0.6706 0.8052 0.6754 0.2007  0.1972  0.1734  44  LYS B CA  
5078  C C   . LYS B 44  ? 0.6835 0.7745 0.6044 0.2060  0.1827  0.1579  44  LYS B C   
5079  O O   . LYS B 44  ? 0.6718 0.7678 0.6050 0.1994  0.1600  0.1413  44  LYS B O   
5080  C CB  . LYS B 44  ? 0.6061 0.7908 0.7112 0.1939  0.1793  0.1541  44  LYS B CB  
5081  C CG  . LYS B 44  ? 0.5728 0.7965 0.7797 0.1822  0.1891  0.1690  44  LYS B CG  
5082  C CD  . LYS B 44  ? 0.6219 0.8212 0.8096 0.1687  0.2045  0.2046  44  LYS B CD  
5083  C CE  . LYS B 44  ? 0.5916 0.8300 0.8816 0.1608  0.2220  0.2296  44  LYS B CE  
5084  N NZ  . LYS B 44  ? 0.5777 0.8163 0.9328 0.1365  0.2088  0.2397  44  LYS B NZ  
5085  N N   . VAL B 45  ? 0.6973 0.7463 0.5355 0.2188  0.1965  0.1633  45  VAL B N   
5086  C CA  . VAL B 45  ? 0.7215 0.7239 0.4883 0.2231  0.1842  0.1507  45  VAL B CA  
5087  C C   . VAL B 45  ? 0.7178 0.6914 0.4605 0.1980  0.1629  0.1523  45  VAL B C   
5088  O O   . VAL B 45  ? 0.7049 0.6668 0.4380 0.1928  0.1443  0.1421  45  VAL B O   
5089  C CB  . VAL B 45  ? 0.7818 0.7434 0.4826 0.2406  0.1988  0.1487  45  VAL B CB  
5090  C CG1 . VAL B 45  ? 0.8136 0.7161 0.4555 0.2300  0.1790  0.1355  45  VAL B CG1 
5091  C CG2 . VAL B 45  ? 0.7841 0.7662 0.5032 0.2679  0.2111  0.1426  45  VAL B CG2 
5092  N N   . LEU B 46  ? 0.7280 0.6945 0.4632 0.1833  0.1660  0.1681  46  LEU B N   
5093  C CA  . LEU B 46  ? 0.7285 0.6708 0.4434 0.1596  0.1451  0.1711  46  LEU B CA  
5094  C C   . LEU B 46  ? 0.6986 0.6750 0.4873 0.1425  0.1296  0.1728  46  LEU B C   
5095  O O   . LEU B 46  ? 0.6882 0.6540 0.4743 0.1236  0.1160  0.1819  46  LEU B O   
5096  C CB  . LEU B 46  ? 0.7657 0.6946 0.4547 0.1493  0.1471  0.1794  46  LEU B CB  
5097  C CG  . LEU B 46  ? 0.8241 0.7168 0.4475 0.1583  0.1496  0.1639  46  LEU B CG  
5098  C CD1 . LEU B 46  ? 0.8611 0.7394 0.4474 0.1429  0.1392  0.1676  46  LEU B CD1 
5099  C CD2 . LEU B 46  ? 0.8337 0.6903 0.4261 0.1621  0.1377  0.1430  46  LEU B CD2 
5100  N N   . GLN B 47  ? 0.6411 0.6600 0.4986 0.1496  0.1293  0.1610  47  GLN B N   
5101  C CA  . GLN B 47  ? 0.6538 0.7077 0.5907 0.1355  0.1143  0.1554  47  GLN B CA  
5102  C C   . GLN B 47  ? 0.6367 0.6762 0.5555 0.1233  0.0915  0.1467  47  GLN B C   
5103  O O   . GLN B 47  ? 0.6333 0.6797 0.5888 0.1065  0.0801  0.1516  47  GLN B O   
5104  C CB  . GLN B 47  ? 0.6334 0.7363 0.6404 0.1483  0.1143  0.1359  47  GLN B CB  
5105  C CG  . GLN B 47  ? 0.5824 0.7189 0.6551 0.1402  0.0925  0.1147  47  GLN B CG  
5106  C CD  . GLN B 47  ? 0.5211 0.7061 0.6961 0.1404  0.0929  0.1033  47  GLN B CD  
5107  O OE1 . GLN B 47  ? 0.4983 0.7070 0.6958 0.1541  0.1046  0.1002  47  GLN B OE1 
5108  N NE2 . GLN B 47  ? 0.4936 0.6937 0.7375 0.1251  0.0797  0.0962  47  GLN B NE2 
5109  N N   . SER B 48  ? 0.5689 0.5893 0.4357 0.1321  0.0861  0.1369  48  SER B N   
5110  C CA  . SER B 48  ? 0.5574 0.5711 0.4130 0.1223  0.0674  0.1318  48  SER B CA  
5111  C C   . SER B 48  ? 0.5786 0.5554 0.3989 0.1015  0.0589  0.1473  48  SER B C   
5112  O O   . SER B 48  ? 0.5657 0.5424 0.3898 0.0902  0.0433  0.1463  48  SER B O   
5113  C CB  . SER B 48  ? 0.5736 0.5747 0.3851 0.1374  0.0671  0.1256  48  SER B CB  
5114  O OG  . SER B 48  ? 0.6202 0.5783 0.3724 0.1459  0.0801  0.1325  48  SER B OG  
5115  N N   . TRP B 49  ? 0.6149 0.5658 0.4013 0.0978  0.0683  0.1617  49  TRP B N   
5116  C CA  . TRP B 49  ? 0.6359 0.5542 0.3806 0.0801  0.0573  0.1734  49  TRP B CA  
5117  C C   . TRP B 49  ? 0.6080 0.5506 0.4075 0.0646  0.0477  0.1864  49  TRP B C   
5118  O O   . TRP B 49  ? 0.6133 0.5647 0.4307 0.0615  0.0556  0.2042  49  TRP B O   
5119  C CB  . TRP B 49  ? 0.6824 0.5783 0.3838 0.0808  0.0661  0.1723  49  TRP B CB  
5120  C CG  . TRP B 49  ? 0.7155 0.5828 0.3712 0.0926  0.0709  0.1548  49  TRP B CG  
5121  C CD1 . TRP B 49  ? 0.7048 0.5715 0.3635 0.1073  0.0750  0.1446  49  TRP B CD1 
5122  C CD2 . TRP B 49  ? 0.7704 0.6056 0.3713 0.0942  0.0724  0.1473  49  TRP B CD2 
5123  N NE1 . TRP B 49  ? 0.7490 0.5804 0.3626 0.1170  0.0799  0.1334  49  TRP B NE1 
5124  C CE2 . TRP B 49  ? 0.7916 0.6010 0.3671 0.1102  0.0787  0.1331  49  TRP B CE2 
5125  C CE3 . TRP B 49  ? 0.8092 0.6366 0.3776 0.0867  0.0693  0.1519  49  TRP B CE3 
5126  C CZ2 . TRP B 49  ? 0.8533 0.6214 0.3710 0.1198  0.0829  0.1216  49  TRP B CZ2 
5127  C CZ3 . TRP B 49  ? 0.8699 0.6632 0.3780 0.0968  0.0725  0.1382  49  TRP B CZ3 
5128  C CH2 . TRP B 49  ? 0.8930 0.6529 0.3756 0.1134  0.0795  0.1221  49  TRP B CH2 
5129  N N   . ASP B 50  ? 0.5450 0.5006 0.3750 0.0558  0.0314  0.1788  50  ASP B N   
5130  C CA  . ASP B 50  ? 0.5227 0.5025 0.4141 0.0430  0.0209  0.1861  50  ASP B CA  
5131  C C   . ASP B 50  ? 0.5398 0.4951 0.3956 0.0257  0.0064  0.2033  50  ASP B C   
5132  O O   . ASP B 50  ? 0.5474 0.4869 0.3734 0.0186  -0.0066 0.1982  50  ASP B O   
5133  C CB  . ASP B 50  ? 0.5356 0.5483 0.4785 0.0467  0.0119  0.1656  50  ASP B CB  
5134  C CG  . ASP B 50  ? 0.5305 0.5682 0.5451 0.0369  0.0020  0.1679  50  ASP B CG  
5135  O OD1 . ASP B 50  ? 0.5261 0.5571 0.5588 0.0274  0.0036  0.1893  50  ASP B OD1 
5136  O OD2 . ASP B 50  ? 0.5198 0.5857 0.5733 0.0409  -0.0065 0.1490  50  ASP B OD2 
5137  N N   . ALA B 51  ? 0.5517 0.5071 0.4162 0.0189  0.0080  0.2224  51  ALA B N   
5138  C CA  . ALA B 51  ? 0.5834 0.5162 0.4126 0.0051  -0.0065 0.2232  51  ALA B CA  
5139  C C   . ALA B 51  ? 0.5556 0.5029 0.4237 -0.0067 -0.0243 0.2240  51  ALA B C   
5140  O O   . ALA B 51  ? 0.5781 0.5098 0.4161 -0.0152 -0.0370 0.2206  51  ALA B O   
5141  C CB  . ALA B 51  ? 0.6070 0.5454 0.4413 0.0049  0.0012  0.2411  51  ALA B CB  
5142  N N   . THR B 52  ? 0.5209 0.5012 0.4602 -0.0054 -0.0256 0.2301  52  THR B N   
5143  C CA  . THR B 52  ? 0.4959 0.4942 0.4794 -0.0148 -0.0417 0.2330  52  THR B CA  
5144  C C   . THR B 52  ? 0.4879 0.4856 0.4505 -0.0163 -0.0506 0.2195  52  THR B C   
5145  O O   . THR B 52  ? 0.4821 0.5022 0.4861 -0.0203 -0.0604 0.2175  52  THR B O   
5146  C CB  . THR B 52  ? 0.4876 0.5191 0.5632 -0.0089 -0.0379 0.2284  52  THR B CB  
5147  O OG1 . THR B 52  ? 0.5172 0.5666 0.6107 0.0049  -0.0306 0.1978  52  THR B OG1 
5148  C CG2 . THR B 52  ? 0.4819 0.5143 0.5894 -0.0078 -0.0262 0.2495  52  THR B CG2 
5149  N N   . LEU B 53  ? 0.5172 0.4907 0.4217 -0.0114 -0.0446 0.2065  53  LEU B N   
5150  C CA  . LEU B 53  ? 0.5169 0.4872 0.4035 -0.0125 -0.0495 0.1972  53  LEU B CA  
5151  C C   . LEU B 53  ? 0.5506 0.4918 0.4028 -0.0264 -0.0593 0.1950  53  LEU B C   
5152  O O   . LEU B 53  ? 0.5829 0.5020 0.4035 -0.0293 -0.0602 0.1960  53  LEU B O   
5153  C CB  . LEU B 53  ? 0.5247 0.4861 0.3784 0.0029  -0.0370 0.1878  53  LEU B CB  
5154  C CG  . LEU B 53  ? 0.4876 0.4908 0.3823 0.0217  -0.0281 0.1710  53  LEU B CG  
5155  C CD1 . LEU B 53  ? 0.4544 0.4916 0.4164 0.0250  -0.0277 0.1629  53  LEU B CD1 
5156  C CD2 . LEU B 53  ? 0.5008 0.4945 0.3635 0.0392  -0.0140 0.1613  53  LEU B CD2 
5157  N N   . VAL B 54  ? 0.5357 0.4847 0.3993 -0.0339 -0.0672 0.1956  54  VAL B N   
5158  C CA  . VAL B 54  ? 0.5649 0.4947 0.4114 -0.0505 -0.0808 0.1982  54  VAL B CA  
5159  C C   . VAL B 54  ? 0.6112 0.4987 0.4007 -0.0495 -0.0790 0.1913  54  VAL B C   
5160  O O   . VAL B 54  ? 0.6464 0.5151 0.4074 -0.0584 -0.0900 0.1918  54  VAL B O   
5161  C CB  . VAL B 54  ? 0.5514 0.4993 0.4256 -0.0585 -0.0868 0.2047  54  VAL B CB  
5162  C CG1 . VAL B 54  ? 0.5903 0.5105 0.4436 -0.0774 -0.1016 0.2090  54  VAL B CG1 
5163  C CG2 . VAL B 54  ? 0.5162 0.5065 0.4464 -0.0630 -0.0942 0.2147  54  VAL B CG2 
5164  N N   . THR B 55  ? 0.6585 0.5326 0.4297 -0.0377 -0.0667 0.1861  55  THR B N   
5165  C CA  . THR B 55  ? 0.7032 0.5372 0.4250 -0.0348 -0.0641 0.1802  55  THR B CA  
5166  C C   . THR B 55  ? 0.6927 0.5321 0.4041 -0.0124 -0.0438 0.1750  55  THR B C   
5167  O O   . THR B 55  ? 0.6553 0.5239 0.3939 0.0001  -0.0339 0.1763  55  THR B O   
5168  C CB  . THR B 55  ? 0.7304 0.5370 0.4433 -0.0447 -0.0709 0.1841  55  THR B CB  
5169  O OG1 . THR B 55  ? 0.7035 0.5321 0.4390 -0.0287 -0.0544 0.1887  55  THR B OG1 
5170  C CG2 . THR B 55  ? 0.7377 0.5468 0.4724 -0.0698 -0.0928 0.1935  55  THR B CG2 
5171  N N   . PRO B 56  ? 0.7274 0.5367 0.3954 -0.0079 -0.0399 0.1677  56  PRO B N   
5172  C CA  . PRO B 56  ? 0.7208 0.5356 0.3820 0.0104  -0.0222 0.1619  56  PRO B CA  
5173  C C   . PRO B 56  ? 0.7274 0.5287 0.3835 0.0204  -0.0149 0.1590  56  PRO B C   
5174  O O   . PRO B 56  ? 0.7361 0.5306 0.3775 0.0377  -0.0008 0.1508  56  PRO B O   
5175  C CB  . PRO B 56  ? 0.7714 0.5541 0.3818 0.0135  -0.0198 0.1534  56  PRO B CB  
5176  C CG  . PRO B 56  ? 0.8224 0.5624 0.3948 -0.0025 -0.0393 0.1503  56  PRO B CG  
5177  C CD  . PRO B 56  ? 0.7871 0.5542 0.4043 -0.0193 -0.0537 0.1616  56  PRO B CD  
5178  N N   . CYS B 57  ? 0.7266 0.5257 0.3974 0.0122  -0.0223 0.1682  57  CYS B N   
5179  C CA  . CYS B 57  ? 0.7415 0.5265 0.4088 0.0214  -0.0150 0.1726  57  CYS B CA  
5180  C C   . CYS B 57  ? 0.7021 0.5309 0.3946 0.0394  -0.0031 0.1710  57  CYS B C   
5181  O O   . CYS B 57  ? 0.7179 0.5377 0.4026 0.0548  0.0071  0.1714  57  CYS B O   
5182  C CB  . CYS B 57  ? 0.7523 0.5282 0.4358 0.0066  -0.0246 0.1886  57  CYS B CB  
5183  S SG  . CYS B 57  ? 0.8494 0.5548 0.4930 -0.0208 -0.0478 0.1841  57  CYS B SG  
5184  N N   . THR B 58  ? 0.6238 0.4937 0.3428 0.0409  -0.0042 0.1673  58  THR B N   
5185  C CA  . THR B 58  ? 0.5936 0.5047 0.3327 0.0647  0.0073  0.1596  58  THR B CA  
5186  C C   . THR B 58  ? 0.5916 0.5058 0.3238 0.0814  0.0188  0.1486  58  THR B C   
5187  O O   . THR B 58  ? 0.5671 0.5217 0.3187 0.1035  0.0267  0.1430  58  THR B O   
5188  C CB  . THR B 58  ? 0.5532 0.5127 0.3289 0.0663  0.0023  0.1610  58  THR B CB  
5189  O OG1 . THR B 58  ? 0.5406 0.5013 0.3269 0.0574  -0.0033 0.1613  58  THR B OG1 
5190  C CG2 . THR B 58  ? 0.5568 0.5171 0.3417 0.0524  -0.0058 0.1731  58  THR B CG2 
5191  N N   . TRP B 59  ? 0.6260 0.5042 0.3313 0.0738  0.0200  0.1464  59  TRP B N   
5192  C CA  . TRP B 59  ? 0.6309 0.5109 0.3285 0.0903  0.0341  0.1396  59  TRP B CA  
5193  C C   . TRP B 59  ? 0.6551 0.5210 0.3332 0.1114  0.0468  0.1346  59  TRP B C   
5194  O O   . TRP B 59  ? 0.6818 0.5200 0.3424 0.1101  0.0445  0.1378  59  TRP B O   
5195  C CB  . TRP B 59  ? 0.6586 0.5112 0.3313 0.0780  0.0331  0.1403  59  TRP B CB  
5196  C CG  . TRP B 59  ? 0.6412 0.5065 0.3328 0.0586  0.0208  0.1495  59  TRP B CG  
5197  C CD1 . TRP B 59  ? 0.6044 0.4982 0.3331 0.0530  0.0121  0.1560  59  TRP B CD1 
5198  C CD2 . TRP B 59  ? 0.6646 0.5172 0.3384 0.0463  0.0166  0.1550  59  TRP B CD2 
5199  N NE1 . TRP B 59  ? 0.6030 0.4972 0.3413 0.0367  0.0025  0.1664  59  TRP B NE1 
5200  C CE2 . TRP B 59  ? 0.6390 0.5111 0.3440 0.0315  0.0044  0.1671  59  TRP B CE2 
5201  C CE3 . TRP B 59  ? 0.7098 0.5385 0.3416 0.0496  0.0225  0.1512  59  TRP B CE3 
5202  C CZ2 . TRP B 59  ? 0.6543 0.5261 0.3539 0.0185  -0.0030 0.1786  59  TRP B CZ2 
5203  C CZ3 . TRP B 59  ? 0.7264 0.5589 0.3486 0.0381  0.0157  0.1607  59  TRP B CZ3 
5204  C CH2 . TRP B 59  ? 0.6968 0.5532 0.3553 0.0224  0.0029  0.1760  59  TRP B CH2 
5205  N N   . PHE B 60  ? 0.6513 0.5366 0.3351 0.1328  0.0611  0.1304  60  PHE B N   
5206  C CA  . PHE B 60  ? 0.6778 0.5501 0.3432 0.1561  0.0745  0.1273  60  PHE B CA  
5207  C C   . PHE B 60  ? 0.7295 0.5505 0.3504 0.1558  0.0821  0.1236  60  PHE B C   
5208  O O   . PHE B 60  ? 0.7382 0.5500 0.3480 0.1425  0.0801  0.1227  60  PHE B O   
5209  C CB  . PHE B 60  ? 0.6526 0.5732 0.3437 0.1820  0.0865  0.1258  60  PHE B CB  
5210  C CG  . PHE B 60  ? 0.6099 0.5873 0.3370 0.1892  0.0780  0.1255  60  PHE B CG  
5211  C CD1 . PHE B 60  ? 0.6051 0.5891 0.3365 0.1861  0.0685  0.1273  60  PHE B CD1 
5212  C CD2 . PHE B 60  ? 0.5711 0.6014 0.3510 0.1925  0.0768  0.1136  60  PHE B CD2 
5213  C CE1 . PHE B 60  ? 0.5710 0.6141 0.3315 0.1964  0.0608  0.1240  60  PHE B CE1 
5214  C CE2 . PHE B 60  ? 0.5490 0.6353 0.3721 0.1974  0.0647  0.1012  60  PHE B CE2 
5215  C CZ  . PHE B 60  ? 0.5357 0.6304 0.3415 0.2022  0.0572  0.1067  60  PHE B CZ  
5216  N N   . HIS B 61  ? 0.7727 0.5605 0.3652 0.1738  0.0912  0.1225  61  HIS B N   
5217  C CA  . HIS B 61  ? 0.8376 0.5676 0.3757 0.1819  0.1000  0.1164  61  HIS B CA  
5218  C C   . HIS B 61  ? 0.8770 0.5558 0.3772 0.1589  0.0844  0.1143  61  HIS B C   
5219  O O   . HIS B 61  ? 0.9436 0.5665 0.3853 0.1657  0.0886  0.1055  61  HIS B O   
5220  C CB  . HIS B 61  ? 0.8440 0.5880 0.3758 0.1921  0.1146  0.1111  61  HIS B CB  
5221  C CG  . HIS B 61  ? 0.8008 0.6017 0.3777 0.2097  0.1269  0.1155  61  HIS B CG  
5222  N ND1 . HIS B 61  ? 0.8046 0.6162 0.3883 0.2376  0.1384  0.1172  61  HIS B ND1 
5223  C CD2 . HIS B 61  ? 0.7584 0.6081 0.3750 0.2052  0.1297  0.1206  61  HIS B CD2 
5224  C CE1 . HIS B 61  ? 0.7649 0.6337 0.3905 0.2488  0.1458  0.1204  61  HIS B CE1 
5225  N NE2 . HIS B 61  ? 0.7381 0.6283 0.3837 0.2297  0.1421  0.1228  61  HIS B NE2 
5226  N N   . VAL B 62  ? 0.7964 0.6662 0.3235 0.1597  -0.0826 -0.0199 62  VAL B N   
5227  C CA  . VAL B 62  ? 0.8224 0.6570 0.3359 0.1525  -0.1076 -0.0248 62  VAL B CA  
5228  C C   . VAL B 62  ? 0.8222 0.6399 0.3657 0.1397  -0.1185 -0.0284 62  VAL B C   
5229  O O   . VAL B 62  ? 0.7965 0.6329 0.3821 0.1280  -0.1094 -0.0196 62  VAL B O   
5230  C CB  . VAL B 62  ? 0.8168 0.6640 0.3415 0.1418  -0.1122 -0.0117 62  VAL B CB  
5231  C CG1 . VAL B 62  ? 0.8383 0.6648 0.3649 0.1305  -0.1415 -0.0130 62  VAL B CG1 
5232  C CG2 . VAL B 62  ? 0.8428 0.6964 0.3284 0.1567  -0.1014 -0.0090 62  VAL B CG2 
5233  N N   . THR B 63  ? 0.8788 0.6562 0.3967 0.1404  -0.1355 -0.0420 63  THR B N   
5234  C CA  . THR B 63  ? 0.8955 0.6503 0.4389 0.1274  -0.1445 -0.0463 63  THR B CA  
5235  C C   . THR B 63  ? 0.9336 0.6668 0.4740 0.1095  -0.1720 -0.0516 63  THR B C   
5236  O O   . THR B 63  ? 0.9587 0.6731 0.4527 0.1120  -0.1858 -0.0616 63  THR B O   
5237  C CB  . THR B 63  ? 0.9306 0.6536 0.4478 0.1432  -0.1345 -0.0584 63  THR B CB  
5238  O OG1 . THR B 63  ? 0.9949 0.6691 0.4592 0.1462  -0.1459 -0.0752 63  THR B OG1 
5239  C CG2 . THR B 63  ? 0.9054 0.6576 0.4126 0.1667  -0.1112 -0.0530 63  THR B CG2 
5240  N N   . CYS B 64  ? 0.9159 0.6540 0.5055 0.0907  -0.1797 -0.0441 64  CYS B N   
5241  C CA  . CYS B 64  ? 0.9419 0.6728 0.5443 0.0701  -0.2067 -0.0457 64  CYS B CA  
5242  C C   . CYS B 64  ? 0.9888 0.6821 0.6011 0.0575  -0.2106 -0.0582 64  CYS B C   
5243  O O   . CYS B 64  ? 1.0043 0.6793 0.6202 0.0666  -0.1907 -0.0610 64  CYS B O   
5244  C CB  . CYS B 64  ? 0.9114 0.6831 0.5701 0.0594  -0.2098 -0.0218 64  CYS B CB  
5245  S SG  . CYS B 64  ? 0.8823 0.6914 0.5290 0.0722  -0.2037 -0.0044 64  CYS B SG  
5246  N N   . ASN B 65  ? 0.9741 0.6576 0.5900 0.0354  -0.2368 -0.0650 65  ASN B N   
5247  C CA  . ASN B 65  ? 1.0261 0.6766 0.6608 0.0166  -0.2407 -0.0751 65  ASN B CA  
5248  C C   . ASN B 65  ? 0.9976 0.6830 0.7108 0.0010  -0.2427 -0.0537 65  ASN B C   
5249  O O   . ASN B 65  ? 0.9516 0.6798 0.6984 0.0074  -0.2372 -0.0315 65  ASN B O   
5250  C CB  . ASN B 65  ? 1.0706 0.6869 0.6606 -0.0033 -0.2662 -0.0978 65  ASN B CB  
5251  C CG  . ASN B 65  ? 1.0507 0.7090 0.6463 -0.0188 -0.2992 -0.0907 65  ASN B CG  
5252  O OD1 . ASN B 65  ? 1.0083 0.7214 0.6584 -0.0187 -0.3036 -0.0657 65  ASN B OD1 
5253  N ND2 . ASN B 65  ? 1.0902 0.7202 0.6248 -0.0315 -0.3213 -0.1119 65  ASN B ND2 
5254  N N   . SER B 66  ? 0.9776 0.6402 0.7190 -0.0193 -0.2465 -0.0594 66  SER B N   
5255  C CA  . SER B 66  ? 0.9603 0.6511 0.7778 -0.0320 -0.2431 -0.0377 66  SER B CA  
5256  C C   . SER B 66  ? 0.9272 0.6760 0.7844 -0.0435 -0.2672 -0.0180 66  SER B C   
5257  O O   . SER B 66  ? 0.9048 0.6851 0.8258 -0.0460 -0.2589 0.0073  66  SER B O   
5258  C CB  . SER B 66  ? 0.9958 0.6485 0.8334 -0.0530 -0.2419 -0.0489 66  SER B CB  
5259  O OG  . SER B 66  ? 1.0309 0.6560 0.8277 -0.0731 -0.2652 -0.0737 66  SER B OG  
5260  N N   . ASP B 67  ? 0.9698 0.7324 0.7883 -0.0481 -0.2949 -0.0269 67  ASP B N   
5261  C CA  . ASP B 67  ? 0.9352 0.7576 0.7847 -0.0548 -0.3200 -0.0061 67  ASP B CA  
5262  C C   . ASP B 67  ? 0.8959 0.7472 0.7334 -0.0280 -0.3074 0.0132  67  ASP B C   
5263  O O   . ASP B 67  ? 0.8786 0.7776 0.7331 -0.0268 -0.3250 0.0332  67  ASP B O   
5264  C CB  . ASP B 67  ? 0.9597 0.7822 0.7686 -0.0768 -0.3597 -0.0259 67  ASP B CB  
5265  C CG  . ASP B 67  ? 0.9940 0.7965 0.8245 -0.1117 -0.3749 -0.0423 67  ASP B CG  
5266  O OD1 . ASP B 67  ? 0.9945 0.7996 0.8883 -0.1182 -0.3582 -0.0304 67  ASP B OD1 
5267  O OD2 . ASP B 67  ? 1.0369 0.8167 0.8174 -0.1342 -0.4013 -0.0679 67  ASP B OD2 
5268  N N   . ASN B 68  ? 0.9183 0.7438 0.7265 -0.0070 -0.2772 0.0086  68  ASN B N   
5269  C CA  . ASN B 68  ? 0.8872 0.7331 0.6795 0.0152  -0.2603 0.0234  68  ASN B CA  
5270  C C   . ASN B 68  ? 0.8872 0.7401 0.6218 0.0223  -0.2809 0.0155  68  ASN B C   
5271  O O   . ASN B 68  ? 0.8730 0.7540 0.6034 0.0363  -0.2761 0.0338  68  ASN B O   
5272  C CB  . ASN B 68  ? 0.8565 0.7411 0.7087 0.0187  -0.2471 0.0576  68  ASN B CB  
5273  C CG  . ASN B 68  ? 0.8583 0.7287 0.7596 0.0136  -0.2216 0.0662  68  ASN B CG  
5274  O OD1 . ASN B 68  ? 0.8727 0.7434 0.8159 -0.0024 -0.2312 0.0682  68  ASN B OD1 
5275  N ND2 . ASN B 68  ? 0.8477 0.7048 0.7419 0.0252  -0.1884 0.0708  68  ASN B ND2 
5276  N N   . SER B 69  ? 0.9576 0.7785 0.6422 0.0131  -0.3011 -0.0115 69  SER B N   
5277  C CA  . SER B 69  ? 0.9728 0.7848 0.5872 0.0210  -0.3163 -0.0235 69  SER B CA  
5278  C C   . SER B 69  ? 0.9824 0.7538 0.5423 0.0414  -0.2898 -0.0406 69  SER B C   
5279  O O   . SER B 69  ? 1.0055 0.7410 0.5609 0.0404  -0.2764 -0.0556 69  SER B O   
5280  C CB  . SER B 69  ? 1.0155 0.8125 0.5995 -0.0042 -0.3540 -0.0433 69  SER B CB  
5281  O OG  . SER B 69  ? 1.0687 0.8540 0.5782 0.0034  -0.3688 -0.0538 69  SER B OG  
5282  N N   . VAL B 70  ? 1.0111 0.7904 0.5316 0.0617  -0.2805 -0.0357 70  VAL B N   
5283  C CA  . VAL B 70  ? 1.0125 0.7649 0.4892 0.0831  -0.2535 -0.0472 70  VAL B CA  
5284  C C   . VAL B 70  ? 1.0695 0.7666 0.4803 0.0816  -0.2622 -0.0751 70  VAL B C   
5285  O O   . VAL B 70  ? 1.1240 0.8042 0.4872 0.0725  -0.2872 -0.0860 70  VAL B O   
5286  C CB  . VAL B 70  ? 0.9968 0.7703 0.4482 0.1031  -0.2401 -0.0346 70  VAL B CB  
5287  C CG1 . VAL B 70  ? 1.0119 0.7596 0.4130 0.1247  -0.2157 -0.0472 70  VAL B CG1 
5288  C CG2 . VAL B 70  ? 0.9517 0.7663 0.4618 0.1052  -0.2205 -0.0090 70  VAL B CG2 
5289  N N   . THR B 71  ? 1.0769 0.7430 0.4804 0.0909  -0.2400 -0.0861 71  THR B N   
5290  C CA  . THR B 71  ? 1.1496 0.7531 0.4875 0.0938  -0.2385 -0.1108 71  THR B CA  
5291  C C   . THR B 71  ? 1.1650 0.7499 0.4594 0.1266  -0.2068 -0.1136 71  THR B C   
5292  O O   . THR B 71  ? 1.2358 0.7646 0.4667 0.1347  -0.1995 -0.1312 71  THR B O   
5293  C CB  . THR B 71  ? 1.1523 0.7241 0.5136 0.0778  -0.2383 -0.1214 71  THR B CB  
5294  O OG1 . THR B 71  ? 1.0974 0.6849 0.5002 0.0940  -0.2109 -0.1100 71  THR B OG1 
5295  C CG2 . THR B 71  ? 1.1361 0.7320 0.5495 0.0446  -0.2676 -0.1166 71  THR B CG2 
5296  N N   . ARG B 72  ? 1.0910 0.7219 0.4198 0.1442  -0.1853 -0.0957 72  ARG B N   
5297  C CA  . ARG B 72  ? 1.0931 0.7204 0.3930 0.1746  -0.1551 -0.0948 72  ARG B CA  
5298  C C   . ARG B 72  ? 1.0442 0.7269 0.3687 0.1846  -0.1413 -0.0766 72  ARG B C   
5299  O O   . ARG B 72  ? 0.9901 0.7147 0.3701 0.1707  -0.1446 -0.0626 72  ARG B O   
5300  C CB  . ARG B 72  ? 1.0943 0.7171 0.4192 0.1848  -0.1359 -0.0943 72  ARG B CB  
5301  C CG  . ARG B 72  ? 1.1081 0.7267 0.4016 0.2191  -0.1058 -0.0922 72  ARG B CG  
5302  C CD  . ARG B 72  ? 1.1219 0.7299 0.4319 0.2311  -0.0902 -0.0911 72  ARG B CD  
5303  N NE  . ARG B 72  ? 1.1706 0.7436 0.4276 0.2651  -0.0646 -0.0942 72  ARG B NE  
5304  C CZ  . ARG B 72  ? 1.2393 0.7401 0.4485 0.2724  -0.0571 -0.1078 72  ARG B CZ  
5305  N NH1 . ARG B 72  ? 1.2707 0.7291 0.4812 0.2449  -0.0750 -0.1215 72  ARG B NH1 
5306  N NH2 . ARG B 72  ? 1.2752 0.7487 0.4446 0.3056  -0.0281 -0.1042 72  ARG B NH2 
5307  N N   . VAL B 73  ? 1.0480 0.7301 0.3409 0.2059  -0.1203 -0.0753 73  VAL B N   
5308  C CA  . VAL B 73  ? 1.0109 0.7424 0.3263 0.2156  -0.1002 -0.0594 73  VAL B CA  
5309  C C   . VAL B 73  ? 1.0217 0.7603 0.3270 0.2426  -0.0700 -0.0572 73  VAL B C   
5310  O O   . VAL B 73  ? 1.0775 0.7858 0.3413 0.2586  -0.0587 -0.0617 73  VAL B O   
5311  C CB  . VAL B 73  ? 1.0359 0.7684 0.3323 0.2115  -0.1055 -0.0551 73  VAL B CB  
5312  C CG1 . VAL B 73  ? 1.0051 0.7808 0.3203 0.2214  -0.0798 -0.0398 73  VAL B CG1 
5313  C CG2 . VAL B 73  ? 1.0263 0.7622 0.3371 0.1886  -0.1359 -0.0525 73  VAL B CG2 
5314  N N   . ASP B 74  ? 1.0335 0.8142 0.3760 0.2483  -0.0566 -0.0485 74  ASP B N   
5315  C CA  . ASP B 74  ? 1.0407 0.8414 0.3822 0.2756  -0.0301 -0.0426 74  ASP B CA  
5316  C C   . ASP B 74  ? 1.0067 0.8678 0.3749 0.2784  -0.0101 -0.0285 74  ASP B C   
5317  O O   . ASP B 74  ? 0.9719 0.8889 0.3848 0.2692  -0.0040 -0.0193 74  ASP B O   
5318  C CB  . ASP B 74  ? 1.0343 0.8497 0.4048 0.2787  -0.0291 -0.0406 74  ASP B CB  
5319  C CG  . ASP B 74  ? 1.0694 0.8237 0.4210 0.2701  -0.0469 -0.0544 74  ASP B CG  
5320  O OD1 . ASP B 74  ? 1.1264 0.8245 0.4244 0.2890  -0.0401 -0.0643 74  ASP B OD1 
5321  O OD2 . ASP B 74  ? 1.0417 0.8010 0.4308 0.2436  -0.0646 -0.0552 74  ASP B OD2 
5322  N N   . LEU B 75  ? 1.0513 0.8990 0.3923 0.2881  0.0011  -0.0273 75  LEU B N   
5323  C CA  . LEU B 75  ? 1.0328 0.9295 0.3934 0.2904  0.0231  -0.0148 75  LEU B CA  
5324  C C   . LEU B 75  ? 1.0669 0.9742 0.4150 0.3215  0.0508  -0.0078 75  LEU B C   
5325  O O   . LEU B 75  ? 1.0784 1.0035 0.4254 0.3274  0.0700  0.0001  75  LEU B O   
5326  C CB  . LEU B 75  ? 1.0482 0.9251 0.3912 0.2773  0.0172  -0.0149 75  LEU B CB  
5327  C CG  . LEU B 75  ? 1.0015 0.8981 0.3736 0.2502  0.0044  -0.0108 75  LEU B CG  
5328  C CD1 . LEU B 75  ? 1.0261 0.9020 0.3761 0.2442  0.0005  -0.0073 75  LEU B CD1 
5329  C CD2 . LEU B 75  ? 0.9501 0.9087 0.3661 0.2411  0.0243  -0.0005 75  LEU B CD2 
5330  N N   . GLY B 76  ? 1.1028 0.9972 0.4412 0.3435  0.0556  -0.0086 76  GLY B N   
5331  C CA  . GLY B 76  ? 1.1378 1.0446 0.4677 0.3777  0.0843  0.0026  76  GLY B CA  
5332  C C   . GLY B 76  ? 1.0880 1.0899 0.4738 0.3812  0.1033  0.0203  76  GLY B C   
5333  O O   . GLY B 76  ? 1.0390 1.0936 0.4661 0.3648  0.0943  0.0231  76  GLY B O   
5334  N N   . ASN B 77  ? 1.0999 1.1248 0.4869 0.4008  0.1300  0.0326  77  ASN B N   
5335  C CA  . ASN B 77  ? 1.0639 1.1862 0.5066 0.4049  0.1509  0.0511  77  ASN B CA  
5336  C C   . ASN B 77  ? 1.0114 1.1891 0.4959 0.3644  0.1430  0.0494  77  ASN B C   
5337  O O   . ASN B 77  ? 0.9782 1.2327 0.5104 0.3522  0.1423  0.0567  77  ASN B O   
5338  C CB  . ASN B 77  ? 1.0561 1.2246 0.5243 0.4303  0.1561  0.0638  77  ASN B CB  
5339  C CG  . ASN B 77  ? 1.0627 1.3049 0.5663 0.4570  0.1855  0.0876  77  ASN B CG  
5340  O OD1 . ASN B 77  ? 1.1150 1.3192 0.5896 0.4894  0.2054  0.0958  77  ASN B OD1 
5341  N ND2 . ASN B 77  ? 1.0150 1.3645 0.5827 0.4411  0.1879  0.0996  77  ASN B ND2 
5342  N N   . ALA B 78  ? 1.0486 1.1853 0.5121 0.3432  0.1380  0.0407  78  ALA B N   
5343  C CA  . ALA B 78  ? 1.0134 1.1820 0.5059 0.3053  0.1342  0.0391  78  ALA B CA  
5344  C C   . ALA B 78  ? 1.0120 1.2112 0.5199 0.2957  0.1613  0.0475  78  ALA B C   
5345  O O   . ALA B 78  ? 0.9899 1.2078 0.5177 0.2634  0.1647  0.0467  78  ALA B O   
5346  C CB  . ALA B 78  ? 1.0159 1.1171 0.4781 0.2873  0.1087  0.0262  78  ALA B CB  
5347  N N   . ASN B 79  ? 1.0361 1.2353 0.5340 0.3224  0.1834  0.0561  79  ASN B N   
5348  C CA  . ASN B 79  ? 1.0432 1.2640 0.5538 0.3151  0.2115  0.0643  79  ASN B CA  
5349  C C   . ASN B 79  ? 1.0598 1.2216 0.5379 0.2968  0.2082  0.0570  79  ASN B C   
5350  O O   . ASN B 79  ? 1.0504 1.2332 0.5477 0.2750  0.2280  0.0612  79  ASN B O   
5351  C CB  . ASN B 79  ? 0.9993 1.3189 0.5767 0.2894  0.2276  0.0733  79  ASN B CB  
5352  C CG  . ASN B 79  ? 0.9924 1.3857 0.6084 0.3129  0.2374  0.0877  79  ASN B CG  
5353  O OD1 . ASN B 79  ? 1.0299 1.3968 0.6222 0.3522  0.2455  0.0948  79  ASN B OD1 
5354  N ND2 . ASN B 79  ? 0.9482 1.4352 0.6236 0.2885  0.2367  0.0932  79  ASN B ND2 
5355  N N   . LEU B 80  ? 1.2483 1.1463 0.5312 0.2984  0.0384  -0.0697 80  LEU B N   
5356  C CA  . LEU B 80  ? 1.2629 1.1136 0.5351 0.2787  0.0361  -0.0671 80  LEU B CA  
5357  C C   . LEU B 80  ? 1.2829 1.1343 0.5221 0.2960  0.0422  -0.0699 80  LEU B C   
5358  O O   . LEU B 80  ? 1.3086 1.1419 0.5210 0.3284  0.0337  -0.0769 80  LEU B O   
5359  C CB  . LEU B 80  ? 1.2696 1.0503 0.5375 0.2795  0.0140  -0.0682 80  LEU B CB  
5360  C CG  . LEU B 80  ? 1.2573 1.0292 0.5572 0.2601  0.0071  -0.0635 80  LEU B CG  
5361  C CD1 . LEU B 80  ? 1.2728 0.9829 0.5642 0.2664  -0.0157 -0.0661 80  LEU B CD1 
5362  C CD2 . LEU B 80  ? 1.2510 1.0293 0.5686 0.2255  0.0196  -0.0543 80  LEU B CD2 
5363  N N   . SER B 81  ? 1.2800 1.1475 0.5175 0.2746  0.0587  -0.0643 81  SER B N   
5364  C CA  . SER B 81  ? 1.3035 1.1684 0.5115 0.2874  0.0654  -0.0648 81  SER B CA  
5365  C C   . SER B 81  ? 1.3157 1.1265 0.5088 0.2756  0.0612  -0.0592 81  SER B C   
5366  O O   . SER B 81  ? 1.3043 1.0972 0.5134 0.2497  0.0646  -0.0513 81  SER B O   
5367  C CB  . SER B 81  ? 1.2997 1.2311 0.5178 0.2725  0.0904  -0.0607 81  SER B CB  
5368  O OG  . SER B 81  ? 1.3247 1.2551 0.5267 0.2822  0.0957  -0.0594 81  SER B OG  
5369  N N   . GLY B 82  ? 1.3357 1.1250 0.5068 0.2938  0.0538  -0.0618 82  GLY B N   
5370  C CA  . GLY B 82  ? 1.3488 1.0975 0.5031 0.2886  0.0493  -0.0557 82  GLY B CA  
5371  C C   . GLY B 82  ? 1.3761 1.0953 0.5119 0.3102  0.0282  -0.0641 82  GLY B C   
5372  O O   . GLY B 82  ? 1.3934 1.1217 0.5238 0.3301  0.0240  -0.0732 82  GLY B O   
5373  N N   . GLN B 83  ? 1.3641 1.0495 0.4883 0.3055  0.0161  -0.0603 83  GLN B N   
5374  C CA  . GLN B 83  ? 1.3933 1.0531 0.4975 0.3185  -0.0039 -0.0689 83  GLN B CA  
5375  C C   . GLN B 83  ? 1.3899 1.0162 0.4926 0.3089  -0.0262 -0.0714 83  GLN B C   
5376  O O   . GLN B 83  ? 1.3674 0.9903 0.4816 0.2942  -0.0248 -0.0605 83  GLN B O   
5377  C CB  . GLN B 83  ? 1.4122 1.0783 0.5015 0.3222  0.0026  -0.0615 83  GLN B CB  
5378  C CG  . GLN B 83  ? 1.4099 1.1081 0.5033 0.3215  0.0298  -0.0523 83  GLN B CG  
5379  C CD  . GLN B 83  ? 1.4389 1.1441 0.5142 0.3349  0.0334  -0.0508 83  GLN B CD  
5380  O OE1 . GLN B 83  ? 1.4563 1.1451 0.5168 0.3404  0.0188  -0.0516 83  GLN B OE1 
5381  N NE2 . GLN B 83  ? 1.4463 1.1811 0.5228 0.3392  0.0526  -0.0487 83  GLN B NE2 
5382  N N   . LEU B 84  ? 1.3715 0.9716 0.4576 0.3160  -0.0457 -0.0855 84  LEU B N   
5383  C CA  . LEU B 84  ? 1.3760 0.9461 0.4576 0.3031  -0.0681 -0.0898 84  LEU B CA  
5384  C C   . LEU B 84  ? 1.3724 0.9525 0.4519 0.2926  -0.0739 -0.0781 84  LEU B C   
5385  O O   . LEU B 84  ? 1.3746 0.9766 0.4505 0.2988  -0.0609 -0.0682 84  LEU B O   
5386  C CB  . LEU B 84  ? 1.4202 0.9558 0.4767 0.3089  -0.0838 -0.1085 84  LEU B CB  
5387  C CG  . LEU B 84  ? 1.4263 0.9290 0.4828 0.3090  -0.0906 -0.1178 84  LEU B CG  
5388  C CD1 . LEU B 84  ? 1.4038 0.9292 0.4780 0.3248  -0.0720 -0.1135 84  LEU B CD1 
5389  C CD2 . LEU B 84  ? 1.4845 0.9417 0.5065 0.3134  -0.1019 -0.1354 84  LEU B CD2 
5390  N N   . VAL B 85  ? 1.3297 0.8960 0.4111 0.2777  -0.0930 -0.0779 85  VAL B N   
5391  C CA  . VAL B 85  ? 1.3209 0.9058 0.4058 0.2690  -0.0987 -0.0626 85  VAL B CA  
5392  C C   . VAL B 85  ? 1.3462 0.9237 0.4178 0.2555  -0.1255 -0.0736 85  VAL B C   
5393  O O   . VAL B 85  ? 1.3560 0.9040 0.4245 0.2442  -0.1397 -0.0870 85  VAL B O   
5394  C CB  . VAL B 85  ? 1.2785 0.8702 0.3968 0.2586  -0.0901 -0.0442 85  VAL B CB  
5395  C CG1 . VAL B 85  ? 1.2726 0.8821 0.3961 0.2513  -0.0998 -0.0282 85  VAL B CG1 
5396  C CG2 . VAL B 85  ? 1.2623 0.8651 0.3894 0.2653  -0.0606 -0.0320 85  VAL B CG2 
5397  N N   . MET B 86  ? 1.3702 0.9762 0.4324 0.2551  -0.1311 -0.0679 86  MET B N   
5398  C CA  . MET B 86  ? 1.3984 1.0086 0.4460 0.2372  -0.1561 -0.0793 86  MET B CA  
5399  C C   . MET B 86  ? 1.3777 0.9954 0.4428 0.2175  -0.1715 -0.0709 86  MET B C   
5400  O O   . MET B 86  ? 1.4023 1.0171 0.4561 0.1954  -0.1931 -0.0836 86  MET B O   
5401  C CB  . MET B 86  ? 1.4181 1.0695 0.4528 0.2427  -0.1572 -0.0741 86  MET B CB  
5402  C CG  . MET B 86  ? 1.3915 1.0899 0.4445 0.2512  -0.1478 -0.0453 86  MET B CG  
5403  S SD  . MET B 86  ? 1.3735 1.1105 0.4456 0.2323  -0.1666 -0.0301 86  MET B SD  
5404  C CE  . MET B 86  ? 1.4188 1.1638 0.4651 0.2036  -0.1977 -0.0570 86  MET B CE  
5405  N N   . GLN B 87  ? 1.3213 0.9477 0.4121 0.2227  -0.1600 -0.0498 87  GLN B N   
5406  C CA  . GLN B 87  ? 1.2963 0.9315 0.4138 0.2046  -0.1720 -0.0400 87  GLN B CA  
5407  C C   . GLN B 87  ? 1.2989 0.8932 0.4243 0.1867  -0.1831 -0.0577 87  GLN B C   
5408  O O   . GLN B 87  ? 1.2810 0.8811 0.4295 0.1687  -0.1942 -0.0516 87  GLN B O   
5409  C CB  . GLN B 87  ? 1.2531 0.9021 0.4030 0.2138  -0.1516 -0.0135 87  GLN B CB  
5410  C CG  . GLN B 87  ? 1.2542 0.9419 0.3962 0.2307  -0.1403 0.0111  87  GLN B CG  
5411  C CD  . GLN B 87  ? 1.2702 0.9584 0.3959 0.2498  -0.1191 0.0116  87  GLN B CD  
5412  O OE1 . GLN B 87  ? 1.2945 0.9715 0.4007 0.2514  -0.1239 -0.0084 87  GLN B OE1 
5413  N NE2 . GLN B 87  ? 1.2605 0.9584 0.3937 0.2642  -0.0936 0.0349  87  GLN B NE2 
5414  N N   . LEU B 88  ? 1.4015 0.9550 0.5060 0.1940  -0.1787 -0.0778 88  LEU B N   
5415  C CA  . LEU B 88  ? 1.4146 0.9232 0.5183 0.1823  -0.1863 -0.0935 88  LEU B CA  
5416  C C   . LEU B 88  ? 1.4566 0.9491 0.5360 0.1551  -0.2102 -0.1084 88  LEU B C   
5417  O O   . LEU B 88  ? 1.4762 0.9292 0.5553 0.1410  -0.2164 -0.1181 88  LEU B O   
5418  C CB  . LEU B 88  ? 1.4414 0.9127 0.5202 0.2028  -0.1738 -0.1095 88  LEU B CB  
5419  C CG  . LEU B 88  ? 1.4006 0.8858 0.5082 0.2220  -0.1508 -0.0979 88  LEU B CG  
5420  C CD1 . LEU B 88  ? 1.4319 0.8975 0.5110 0.2459  -0.1384 -0.1116 88  LEU B CD1 
5421  C CD2 . LEU B 88  ? 1.3750 0.8528 0.5194 0.2122  -0.1503 -0.0911 88  LEU B CD2 
5422  N N   . GLY B 89  ? 1.4210 0.9441 0.4781 0.1459  -0.2228 -0.1105 89  GLY B N   
5423  C CA  . GLY B 89  ? 1.4616 0.9818 0.4982 0.1127  -0.2450 -0.1246 89  GLY B CA  
5424  C C   . GLY B 89  ? 1.4306 0.9967 0.4986 0.0903  -0.2588 -0.1077 89  GLY B C   
5425  O O   . GLY B 89  ? 1.4640 1.0397 0.5150 0.0579  -0.2787 -0.1181 89  GLY B O   
5426  N N   . GLN B 90  ? 1.3843 0.9813 0.4978 0.1050  -0.2472 -0.0815 90  GLN B N   
5427  C CA  . GLN B 90  ? 1.3508 0.9941 0.4986 0.0899  -0.2563 -0.0612 90  GLN B CA  
5428  C C   . GLN B 90  ? 1.3360 0.9448 0.5077 0.0721  -0.2598 -0.0632 90  GLN B C   
5429  O O   . GLN B 90  ? 1.3007 0.9443 0.5065 0.0641  -0.2637 -0.0439 90  GLN B O   
5430  C CB  . GLN B 90  ? 1.3028 0.9897 0.4796 0.1172  -0.2390 -0.0307 90  GLN B CB  
5431  C CG  . GLN B 90  ? 1.3171 1.0303 0.4698 0.1411  -0.2293 -0.0256 90  GLN B CG  
5432  C CD  . GLN B 90  ? 1.3265 1.1110 0.4720 0.1383  -0.2420 -0.0114 90  GLN B CD  
5433  O OE1 . GLN B 90  ? 1.2966 1.1252 0.4663 0.1528  -0.2322 0.0172  90  GLN B OE1 
5434  N NE2 . GLN B 90  ? 1.3681 1.1696 0.4873 0.1181  -0.2598 -0.0308 90  GLN B NE2 
5435  N N   . LEU B 91  ? 1.3740 0.9156 0.5265 0.0693  -0.2570 -0.0845 91  LEU B N   
5436  C CA  . LEU B 91  ? 1.3643 0.8688 0.5360 0.0568  -0.2577 -0.0858 91  LEU B CA  
5437  C C   . LEU B 91  ? 1.4281 0.8903 0.5624 0.0228  -0.2741 -0.1089 91  LEU B C   
5438  O O   . LEU B 91  ? 1.4762 0.8692 0.5740 0.0263  -0.2686 -0.1297 91  LEU B O   
5439  C CB  . LEU B 91  ? 1.3501 0.8108 0.5282 0.0837  -0.2378 -0.0887 91  LEU B CB  
5440  C CG  . LEU B 91  ? 1.2942 0.7854 0.5125 0.1084  -0.2191 -0.0674 91  LEU B CG  
5441  C CD1 . LEU B 91  ? 1.2603 0.7818 0.5221 0.0976  -0.2220 -0.0462 91  LEU B CD1 
5442  C CD2 . LEU B 91  ? 1.2809 0.8080 0.4916 0.1270  -0.2094 -0.0593 91  LEU B CD2 
5443  N N   . PRO B 92  ? 1.3896 0.8910 0.5282 -0.0107 -0.2928 -0.1055 92  PRO B N   
5444  C CA  . PRO B 92  ? 1.4624 0.9239 0.5567 -0.0508 -0.3078 -0.1304 92  PRO B CA  
5445  C C   . PRO B 92  ? 1.4940 0.8703 0.5744 -0.0592 -0.3015 -0.1431 92  PRO B C   
5446  O O   . PRO B 92  ? 1.5720 0.8769 0.5960 -0.0743 -0.3018 -0.1691 92  PRO B O   
5447  C CB  . PRO B 92  ? 1.4472 0.9864 0.5636 -0.0841 -0.3271 -0.1173 92  PRO B CB  
5448  C CG  . PRO B 92  ? 1.3658 0.9575 0.5425 -0.0594 -0.3191 -0.0847 92  PRO B CG  
5449  C CD  . PRO B 92  ? 1.3356 0.9167 0.5187 -0.0143 -0.2990 -0.0779 92  PRO B CD  
5450  N N   . ASN B 93  ? 1.4403 0.8185 0.5660 -0.0483 -0.2941 -0.1251 93  ASN B N   
5451  C CA  . ASN B 93  ? 1.4680 0.7723 0.5835 -0.0544 -0.2877 -0.1332 93  ASN B CA  
5452  C C   . ASN B 93  ? 1.4662 0.7185 0.5743 -0.0123 -0.2664 -0.1366 93  ASN B C   
5453  O O   . ASN B 93  ? 1.4914 0.6824 0.5881 -0.0089 -0.2580 -0.1415 93  ASN B O   
5454  C CB  . ASN B 93  ? 1.4156 0.7540 0.5830 -0.0672 -0.2922 -0.1119 93  ASN B CB  
5455  C CG  . ASN B 93  ? 1.4331 0.8137 0.6005 -0.1142 -0.3130 -0.1110 93  ASN B CG  
5456  O OD1 . ASN B 93  ? 1.5045 0.8370 0.6292 -0.1512 -0.3206 -0.1311 93  ASN B OD1 
5457  N ND2 . ASN B 93  ? 1.3734 0.8446 0.5851 -0.1132 -0.3208 -0.0873 93  ASN B ND2 
5458  N N   . LEU B 94  ? 1.4623 0.7418 0.5759 0.0201  -0.2566 -0.1328 94  LEU B N   
5459  C CA  . LEU B 94  ? 1.4578 0.7047 0.5668 0.0596  -0.2365 -0.1346 94  LEU B CA  
5460  C C   . LEU B 94  ? 1.5452 0.7034 0.5899 0.0640  -0.2300 -0.1585 94  LEU B C   
5461  O O   . LEU B 94  ? 1.6051 0.7374 0.5992 0.0580  -0.2337 -0.1768 94  LEU B O   
5462  C CB  . LEU B 94  ? 1.4249 0.7182 0.5433 0.0864  -0.2281 -0.1285 94  LEU B CB  
5463  C CG  . LEU B 94  ? 1.4346 0.7037 0.5362 0.1245  -0.2086 -0.1345 94  LEU B CG  
5464  C CD1 . LEU B 94  ? 1.3796 0.6653 0.5254 0.1445  -0.1944 -0.1192 94  LEU B CD1 
5465  C CD2 . LEU B 94  ? 1.4249 0.7333 0.5200 0.1397  -0.2044 -0.1335 94  LEU B CD2 
5466  N N   . GLN B 95  ? 1.5334 0.6425 0.5756 0.0771  -0.2187 -0.1578 95  GLN B N   
5467  C CA  . GLN B 95  ? 1.6244 0.6408 0.6025 0.0844  -0.2083 -0.1764 95  GLN B CA  
5468  C C   . GLN B 95  ? 1.6312 0.6361 0.5974 0.1341  -0.1863 -0.1756 95  GLN B C   
5469  O O   . GLN B 95  ? 1.6971 0.6603 0.6216 0.1438  -0.1756 -0.1853 95  GLN B O   
5470  C CB  . GLN B 95  ? 1.6434 0.6135 0.6243 0.0707  -0.2055 -0.1722 95  GLN B CB  
5471  C CG  . GLN B 95  ? 1.6373 0.6234 0.6327 0.0198  -0.2265 -0.1711 95  GLN B CG  
5472  C CD  . GLN B 95  ? 1.6445 0.5928 0.6503 0.0094  -0.2226 -0.1636 95  GLN B CD  
5473  O OE1 . GLN B 95  ? 1.6691 0.5714 0.6636 0.0385  -0.2024 -0.1601 95  GLN B OE1 
5474  N NE2 . GLN B 95  ? 1.6158 0.6019 0.6547 -0.0300 -0.2388 -0.1548 95  GLN B NE2 
5475  N N   . TYR B 96  ? 1.5490 0.6803 0.5064 0.4216  -0.1365 -0.1192 96  TYR B N   
5476  C CA  . TYR B 96  ? 1.5479 0.7032 0.5054 0.4307  -0.1189 -0.1203 96  TYR B CA  
5477  C C   . TYR B 96  ? 1.5507 0.7176 0.5014 0.4328  -0.0853 -0.1141 96  TYR B C   
5478  O O   . TYR B 96  ? 1.5334 0.6998 0.5000 0.4146  -0.0685 -0.1111 96  TYR B O   
5479  C CB  . TYR B 96  ? 1.5203 0.6925 0.5024 0.4136  -0.1183 -0.1263 96  TYR B CB  
5480  C CG  . TYR B 96  ? 1.5264 0.6820 0.5084 0.4111  -0.1531 -0.1312 96  TYR B CG  
5481  C CD1 . TYR B 96  ? 1.5199 0.6568 0.5084 0.3917  -0.1745 -0.1317 96  TYR B CD1 
5482  C CD2 . TYR B 96  ? 1.5440 0.7021 0.5164 0.4285  -0.1659 -0.1352 96  TYR B CD2 
5483  C CE1 . TYR B 96  ? 1.5326 0.6498 0.5159 0.3854  -0.2082 -0.1342 96  TYR B CE1 
5484  C CE2 . TYR B 96  ? 1.5591 0.6922 0.5261 0.4260  -0.1999 -0.1385 96  TYR B CE2 
5485  C CZ  . TYR B 96  ? 1.5540 0.6649 0.5259 0.4023  -0.2211 -0.1371 96  TYR B CZ  
5486  O OH  . TYR B 96  ? 1.5748 0.6571 0.5384 0.3958  -0.2562 -0.1384 96  TYR B OH  
5487  N N   . LEU B 97  ? 1.5748 0.7536 0.5032 0.4536  -0.0768 -0.1109 97  LEU B N   
5488  C CA  . LEU B 97  ? 1.5875 0.7773 0.4994 0.4551  -0.0471 -0.1027 97  LEU B CA  
5489  C C   . LEU B 97  ? 1.5853 0.8188 0.4974 0.4596  -0.0306 -0.1032 97  LEU B C   
5490  O O   . LEU B 97  ? 1.6021 0.8550 0.5038 0.4821  -0.0385 -0.1054 97  LEU B O   
5491  C CB  . LEU B 97  ? 1.6214 0.7941 0.5033 0.4742  -0.0514 -0.0961 97  LEU B CB  
5492  C CG  . LEU B 97  ? 1.6360 0.8071 0.5063 0.4675  -0.0272 -0.0813 97  LEU B CG  
5493  C CD1 . LEU B 97  ? 1.6630 0.8050 0.5115 0.4816  -0.0390 -0.0755 97  LEU B CD1 
5494  C CD2 . LEU B 97  ? 1.6504 0.8593 0.5036 0.4725  -0.0062 -0.0754 97  LEU B CD2 
5495  N N   . GLU B 98  ? 1.5648 0.8185 0.4918 0.4378  -0.0082 -0.1006 98  GLU B N   
5496  C CA  . GLU B 98  ? 1.5597 0.8620 0.4874 0.4385  0.0084  -0.1012 98  GLU B CA  
5497  C C   . GLU B 98  ? 1.5672 0.8961 0.4915 0.4214  0.0379  -0.0839 98  GLU B C   
5498  O O   . GLU B 98  ? 1.5482 0.8815 0.4964 0.3899  0.0544  -0.0753 98  GLU B O   
5499  C CB  . GLU B 98  ? 1.5245 0.8401 0.4851 0.4196  0.0075  -0.1079 98  GLU B CB  
5500  C CG  . GLU B 98  ? 1.5141 0.7988 0.4875 0.4228  -0.0236 -0.1188 98  GLU B CG  
5501  C CD  . GLU B 98  ? 1.5341 0.8191 0.4981 0.4514  -0.0491 -0.1241 98  GLU B CD  
5502  O OE1 . GLU B 98  ? 1.5427 0.8655 0.5022 0.4685  -0.0428 -0.1259 98  GLU B OE1 
5503  O OE2 . GLU B 98  ? 1.5444 0.7932 0.5042 0.4567  -0.0760 -0.1263 98  GLU B OE2 
5504  N N   . LEU B 99  ? 1.5991 0.9448 0.4909 0.4408  0.0431  -0.0783 99  LEU B N   
5505  C CA  . LEU B 99  ? 1.6134 0.9910 0.4955 0.4235  0.0689  -0.0597 99  LEU B CA  
5506  C C   . LEU B 99  ? 1.6198 1.0674 0.4896 0.4353  0.0809  -0.0603 99  LEU B C   
5507  O O   . LEU B 99  ? 1.6398 1.1234 0.4921 0.4259  0.0991  -0.0445 99  LEU B O   
5508  C CB  . LEU B 99  ? 1.6471 0.9966 0.5022 0.4304  0.0676  -0.0478 99  LEU B CB  
5509  C CG  . LEU B 99  ? 1.6491 0.9462 0.5150 0.4080  0.0688  -0.0367 99  LEU B CG  
5510  C CD1 . LEU B 99  ? 1.6794 0.9414 0.5195 0.4278  0.0562  -0.0323 99  LEU B CD1 
5511  C CD2 . LEU B 99  ? 1.6577 0.9655 0.5259 0.3728  0.0927  -0.0176 99  LEU B CD2 
5512  N N   . TYR B 100 ? 1.5990 1.0740 0.4931 0.4510  0.0682  -0.0751 100 TYR B N   
5513  C CA  . TYR B 100 ? 1.5997 1.1500 0.5015 0.4651  0.0741  -0.0766 100 TYR B CA  
5514  C C   . TYR B 100 ? 1.5886 1.1957 0.4962 0.4346  0.1025  -0.0635 100 TYR B C   
5515  O O   . TYR B 100 ? 1.5766 1.1596 0.4857 0.4038  0.1151  -0.0568 100 TYR B O   
5516  C CB  . TYR B 100 ? 1.5868 1.1410 0.5088 0.4901  0.0512  -0.0952 100 TYR B CB  
5517  C CG  . TYR B 100 ? 1.5556 1.0938 0.4997 0.4715  0.0492  -0.1013 100 TYR B CG  
5518  C CD1 . TYR B 100 ? 1.5357 1.1306 0.4964 0.4576  0.0661  -0.0993 100 TYR B CD1 
5519  C CD2 . TYR B 100 ? 1.5462 1.0181 0.4956 0.4660  0.0299  -0.1083 100 TYR B CD2 
5520  C CE1 . TYR B 100 ? 1.5078 1.0899 0.4880 0.4401  0.0645  -0.1048 100 TYR B CE1 
5521  C CE2 . TYR B 100 ? 1.5181 0.9797 0.4884 0.4473  0.0277  -0.1138 100 TYR B CE2 
5522  C CZ  . TYR B 100 ? 1.4994 1.0140 0.4840 0.4352  0.0453  -0.1124 100 TYR B CZ  
5523  O OH  . TYR B 100 ? 1.4721 0.9778 0.4766 0.4161  0.0432  -0.1179 100 TYR B OH  
5524  N N   . SER B 101 ? 1.5954 1.2813 0.5060 0.4428  0.1119  -0.0597 101 SER B N   
5525  C CA  . SER B 101 ? 1.5847 1.3427 0.5053 0.4145  0.1362  -0.0473 101 SER B CA  
5526  C C   . SER B 101 ? 1.5988 1.3393 0.4980 0.3720  0.1581  -0.0240 101 SER B C   
5527  O O   . SER B 101 ? 1.5853 1.3144 0.4895 0.3402  0.1710  -0.0175 101 SER B O   
5528  C CB  . SER B 101 ? 1.5513 1.3228 0.5002 0.4101  0.1343  -0.0582 101 SER B CB  
5529  O OG  . SER B 101 ? 1.5398 1.3682 0.4971 0.3737  0.1588  -0.0438 101 SER B OG  
5530  N N   . ASN B 102 ? 1.6315 1.3660 0.5037 0.3716  0.1611  -0.0106 102 ASN B N   
5531  C CA  . ASN B 102 ? 1.6585 1.3750 0.5028 0.3323  0.1796  0.0153  102 ASN B CA  
5532  C C   . ASN B 102 ? 1.6893 1.4616 0.5155 0.3310  0.1857  0.0313  102 ASN B C   
5533  O O   . ASN B 102 ? 1.6876 1.5134 0.5246 0.3616  0.1771  0.0201  102 ASN B O   
5534  C CB  . ASN B 102 ? 1.6654 1.2807 0.5083 0.3233  0.1693  0.0167  102 ASN B CB  
5535  C CG  . ASN B 102 ? 1.6303 1.2050 0.5097 0.3053  0.1657  0.0066  102 ASN B CG  
5536  O OD1 . ASN B 102 ? 1.6218 1.2093 0.5155 0.2669  0.1802  0.0167  102 ASN B OD1 
5537  N ND2 . ASN B 102 ? 1.6120 1.1396 0.5049 0.3310  0.1456  -0.0128 102 ASN B ND2 
5538  N N   . ASN B 103 ? 1.7228 1.4792 0.5191 0.2940  0.1996  0.0582  103 ASN B N   
5539  C CA  . ASN B 103 ? 1.7574 1.5629 0.5323 0.2836  0.2055  0.0781  103 ASN B CA  
5540  C C   . ASN B 103 ? 1.7937 1.5214 0.5345 0.2933  0.1960  0.0867  103 ASN B C   
5541  O O   . ASN B 103 ? 1.8345 1.5610 0.5448 0.2671  0.2030  0.1128  103 ASN B O   
5542  C CB  . ASN B 103 ? 1.7765 1.6278 0.5400 0.2291  0.2257  0.1065  103 ASN B CB  
5543  C CG  . ASN B 103 ? 1.8065 1.7373 0.5561 0.2150  0.2310  0.1253  103 ASN B CG  
5544  O OD1 . ASN B 103 ? 1.7958 1.7970 0.5633 0.2442  0.2257  0.1112  103 ASN B OD1 
5545  N ND2 . ASN B 103 ? 1.8503 1.7645 0.5656 0.1688  0.2403  0.1576  103 ASN B ND2 
5546  N N   . ILE B 104 ? 1.7815 1.4434 0.5268 0.3292  0.1782  0.0659  104 ILE B N   
5547  C CA  . ILE B 104 ? 1.8110 1.3993 0.5320 0.3388  0.1668  0.0721  104 ILE B CA  
5548  C C   . ILE B 104 ? 1.8319 1.4689 0.5397 0.3608  0.1618  0.0748  104 ILE B C   
5549  O O   . ILE B 104 ? 1.8120 1.5095 0.5426 0.3898  0.1551  0.0560  104 ILE B O   
5550  C CB  . ILE B 104 ? 1.7853 1.3012 0.5284 0.3641  0.1471  0.0489  104 ILE B CB  
5551  C CG1 . ILE B 104 ? 1.7519 1.2410 0.5310 0.3391  0.1501  0.0427  104 ILE B CG1 
5552  C CG2 . ILE B 104 ? 1.8123 1.2560 0.5398 0.3687  0.1351  0.0568  104 ILE B CG2 
5553  C CD1 . ILE B 104 ? 1.7194 1.1650 0.5235 0.3640  0.1314  0.0176  104 ILE B CD1 
5554  N N   . THR B 105 ? 1.8749 1.4843 0.5486 0.3458  0.1637  0.0983  105 THR B N   
5555  C CA  . THR B 105 ? 1.8980 1.5514 0.5596 0.3603  0.1593  0.1040  105 THR B CA  
5556  C C   . THR B 105 ? 1.9164 1.4911 0.5598 0.3854  0.1423  0.1006  105 THR B C   
5557  O O   . THR B 105 ? 1.9094 1.4022 0.5518 0.3928  0.1332  0.0926  105 THR B O   
5558  C CB  . THR B 105 ? 1.9365 1.6351 0.5732 0.3177  0.1743  0.1375  105 THR B CB  
5559  O OG1 . THR B 105 ? 1.9813 1.5952 0.5806 0.2997  0.1711  0.1612  105 THR B OG1 
5560  C CG2 . THR B 105 ? 1.9255 1.6653 0.5724 0.2783  0.1912  0.1479  105 THR B CG2 
5561  N N   . GLY B 106 ? 1.9404 1.5459 0.5701 0.3977  0.1376  0.1066  106 GLY B N   
5562  C CA  . GLY B 106 ? 1.9606 1.5022 0.5726 0.4194  0.1219  0.1059  106 GLY B CA  
5563  C C   . GLY B 106 ? 1.9366 1.4806 0.5688 0.4645  0.1039  0.0747  106 GLY B C   
5564  O O   . GLY B 106 ? 1.9104 1.5083 0.5682 0.4826  0.1023  0.0539  106 GLY B O   
5565  N N   . THR B 107 ? 1.9506 1.4312 0.5697 0.4821  0.0883  0.0727  107 THR B N   
5566  C CA  . THR B 107 ? 1.9379 1.4085 0.5694 0.5206  0.0682  0.0468  107 THR B CA  
5567  C C   . THR B 107 ? 1.9113 1.3153 0.5581 0.5296  0.0544  0.0296  107 THR B C   
5568  O O   . THR B 107 ? 1.9047 1.2661 0.5504 0.5088  0.0604  0.0376  107 THR B O   
5569  C CB  . THR B 107 ? 1.9703 1.4223 0.5789 0.5328  0.0583  0.0553  107 THR B CB  
5570  O OG1 . THR B 107 ? 1.9621 1.4101 0.5812 0.5681  0.0387  0.0301  107 THR B OG1 
5571  C CG2 . THR B 107 ? 1.9883 1.3583 0.5780 0.5200  0.0540  0.0721  107 THR B CG2 
5572  N N   . ILE B 108 ? 1.8999 1.2950 0.5596 0.5596  0.0344  0.0063  108 ILE B N   
5573  C CA  . ILE B 108 ? 1.8791 1.2142 0.5519 0.5674  0.0165  -0.0091 108 ILE B CA  
5574  C C   . ILE B 108 ? 1.9001 1.1805 0.5545 0.5740  0.0027  -0.0027 108 ILE B C   
5575  O O   . ILE B 108 ? 1.9188 1.2089 0.5639 0.5932  -0.0079 -0.0066 108 ILE B O   
5576  C CB  . ILE B 108 ? 1.8616 1.2121 0.5561 0.5922  -0.0011 -0.0349 108 ILE B CB  
5577  C CG1 . ILE B 108 ? 1.8412 1.2483 0.5558 0.5877  0.0118  -0.0407 108 ILE B CG1 
5578  C CG2 . ILE B 108 ? 1.8446 1.1342 0.5506 0.5950  -0.0224 -0.0472 108 ILE B CG2 
5579  C CD1 . ILE B 108 ? 1.8333 1.2557 0.5653 0.6149  -0.0065 -0.0637 108 ILE B CD1 
5580  N N   . PRO B 109 ? 1.9106 1.1363 0.5594 0.5598  0.0021  0.0067  109 PRO B N   
5581  C CA  . PRO B 109 ? 1.9310 1.1110 0.5648 0.5674  -0.0115 0.0140  109 PRO B CA  
5582  C C   . PRO B 109 ? 1.9168 1.0771 0.5644 0.5867  -0.0370 -0.0072 109 PRO B C   
5583  O O   . PRO B 109 ? 1.8898 1.0356 0.5569 0.5842  -0.0460 -0.0212 109 PRO B O   
5584  C CB  . PRO B 109 ? 1.9318 1.0662 0.5650 0.5464  -0.0045 0.0291  109 PRO B CB  
5585  C CG  . PRO B 109 ? 1.8963 1.0446 0.5597 0.5300  0.0050  0.0190  109 PRO B CG  
5586  C CD  . PRO B 109 ? 1.8942 1.1006 0.5498 0.5368  0.0143  0.0117  109 PRO B CD  
5587  N N   . GLU B 110 ? 1.9545 1.1146 0.5910 0.6030  -0.0495 -0.0083 110 GLU B N   
5588  C CA  . GLU B 110 ? 1.9493 1.0908 0.5943 0.6184  -0.0750 -0.0266 110 GLU B CA  
5589  C C   . GLU B 110 ? 1.9322 1.0308 0.5885 0.6096  -0.0886 -0.0289 110 GLU B C   
5590  O O   . GLU B 110 ? 1.9241 1.0088 0.5906 0.6151  -0.1106 -0.0439 110 GLU B O   
5591  C CB  . GLU B 110 ? 1.9791 1.1251 0.6068 0.6332  -0.0837 -0.0241 110 GLU B CB  
5592  C CG  . GLU B 110 ? 1.9955 1.1147 0.6114 0.6270  -0.0835 -0.0058 110 GLU B CG  
5593  C CD  . GLU B 110 ? 2.0252 1.1565 0.6242 0.6397  -0.0894 -0.0019 110 GLU B CD  
5594  O OE1 . GLU B 110 ? 2.0299 1.1659 0.6293 0.6543  -0.1058 -0.0192 110 GLU B OE1 
5595  O OE2 . GLU B 110 ? 2.0474 1.1811 0.6314 0.6340  -0.0785 0.0191  110 GLU B OE2 
5596  N N   . GLN B 111 ? 1.9378 1.0160 0.5918 0.5952  -0.0774 -0.0134 111 GLN B N   
5597  C CA  . GLN B 111 ? 1.9224 0.9688 0.5892 0.5885  -0.0898 -0.0143 111 GLN B CA  
5598  C C   . GLN B 111 ? 1.8896 0.9349 0.5772 0.5796  -0.0961 -0.0301 111 GLN B C   
5599  O O   . GLN B 111 ? 1.8732 0.9017 0.5769 0.5729  -0.1093 -0.0330 111 GLN B O   
5600  C CB  . GLN B 111 ? 1.9319 0.9580 0.5986 0.5775  -0.0758 0.0068  111 GLN B CB  
5601  C CG  . GLN B 111 ? 1.9677 0.9851 0.6129 0.5866  -0.0761 0.0238  111 GLN B CG  
5602  C CD  . GLN B 111 ? 1.9692 0.9924 0.6193 0.5993  -0.0969 0.0128  111 GLN B CD  
5603  O OE1 . GLN B 111 ? 1.9857 1.0276 0.6225 0.6093  -0.0992 0.0094  111 GLN B OE1 
5604  N NE2 . GLN B 111 ? 1.9530 0.9643 0.6229 0.5975  -0.1120 0.0072  111 GLN B NE2 
5605  N N   . LEU B 112 ? 1.8974 0.9670 0.5926 0.5778  -0.0872 -0.0395 112 LEU B N   
5606  C CA  . LEU B 112 ? 1.8673 0.9371 0.5874 0.5693  -0.0968 -0.0548 112 LEU B CA  
5607  C C   . LEU B 112 ? 1.8634 0.9224 0.5915 0.5768  -0.1269 -0.0678 112 LEU B C   
5608  O O   . LEU B 112 ? 1.8414 0.8950 0.5891 0.5665  -0.1402 -0.0771 112 LEU B O   
5609  C CB  . LEU B 112 ? 1.8510 0.9544 0.5833 0.5663  -0.0819 -0.0602 112 LEU B CB  
5610  C CG  . LEU B 112 ? 1.8534 0.9720 0.5820 0.5510  -0.0522 -0.0491 112 LEU B CG  
5611  C CD1 . LEU B 112 ? 1.8696 1.0265 0.5828 0.5577  -0.0356 -0.0402 112 LEU B CD1 
5612  C CD2 . LEU B 112 ? 1.8262 0.9572 0.5827 0.5356  -0.0464 -0.0587 112 LEU B CD2 
5613  N N   . GLY B 113 ? 1.8971 0.9524 0.6097 0.5917  -0.1381 -0.0680 113 GLY B N   
5614  C CA  . GLY B 113 ? 1.9038 0.9418 0.6193 0.5944  -0.1670 -0.0793 113 GLY B CA  
5615  C C   . GLY B 113 ? 1.8922 0.9128 0.6172 0.5793  -0.1806 -0.0773 113 GLY B C   
5616  O O   . GLY B 113 ? 1.8952 0.9043 0.6255 0.5736  -0.2051 -0.0863 113 GLY B O   
5617  N N   . ASN B 114 ? 1.9081 0.9288 0.6357 0.5720  -0.1662 -0.0648 114 ASN B N   
5618  C CA  . ASN B 114 ? 1.8964 0.9126 0.6391 0.5596  -0.1777 -0.0610 114 ASN B CA  
5619  C C   . ASN B 114 ? 1.8711 0.8882 0.6346 0.5421  -0.1854 -0.0677 114 ASN B C   
5620  O O   . ASN B 114 ? 1.8605 0.8830 0.6410 0.5304  -0.1971 -0.0651 114 ASN B O   
5621  C CB  . ASN B 114 ? 1.9099 0.9243 0.6509 0.5629  -0.1605 -0.0429 114 ASN B CB  
5622  C CG  . ASN B 114 ? 1.9406 0.9564 0.6670 0.5752  -0.1602 -0.0351 114 ASN B CG  
5623  O OD1 . ASN B 114 ? 1.9490 0.9686 0.6674 0.5804  -0.1744 -0.0435 114 ASN B OD1 
5624  N ND2 . ASN B 114 ? 1.9516 0.9617 0.6749 0.5793  -0.1448 -0.0183 114 ASN B ND2 
5625  N N   . LEU B 115 ? 1.6923 1.1605 0.6021 0.3413  -0.3141 -0.2180 115 LEU B N   
5626  C CA  . LEU B 115 ? 1.6675 1.1435 0.5982 0.3420  -0.3073 -0.2248 115 LEU B CA  
5627  C C   . LEU B 115 ? 1.6631 1.1458 0.5989 0.3345  -0.3028 -0.2328 115 LEU B C   
5628  O O   . LEU B 115 ? 1.6649 1.1419 0.5942 0.3309  -0.2921 -0.2338 115 LEU B O   
5629  C CB  . LEU B 115 ? 1.6604 1.1297 0.5884 0.3441  -0.2945 -0.2203 115 LEU B CB  
5630  C CG  . LEU B 115 ? 1.6671 1.1285 0.5871 0.3500  -0.2982 -0.2111 115 LEU B CG  
5631  C CD1 . LEU B 115 ? 1.6628 1.1188 0.5770 0.3506  -0.2834 -0.2068 115 LEU B CD1 
5632  C CD2 . LEU B 115 ? 1.6557 1.1227 0.5936 0.3565  -0.3102 -0.2138 115 LEU B CD2 
5633  N N   . THR B 116 ? 1.6591 1.1540 0.6068 0.3323  -0.3126 -0.2392 116 THR B N   
5634  C CA  . THR B 116 ? 1.6587 1.1600 0.6089 0.3237  -0.3108 -0.2459 116 THR B CA  
5635  C C   . THR B 116 ? 1.6453 1.1471 0.6030 0.3185  -0.3009 -0.2486 116 THR B C   
5636  O O   . THR B 116 ? 1.6539 1.1464 0.6018 0.3140  -0.2949 -0.2498 116 THR B O   
5637  C CB  . THR B 116 ? 1.6537 1.1723 0.6186 0.3219  -0.3227 -0.2531 116 THR B CB  
5638  O OG1 . THR B 116 ? 1.6708 1.1858 0.6264 0.3265  -0.3343 -0.2503 116 THR B OG1 
5639  C CG2 . THR B 116 ? 1.6532 1.1795 0.6203 0.3111  -0.3208 -0.2595 116 THR B CG2 
5640  N N   . GLU B 117 ? 1.6261 1.1387 0.6009 0.3190  -0.3004 -0.2503 117 GLU B N   
5641  C CA  . GLU B 117 ? 1.6153 1.1270 0.5950 0.3140  -0.2924 -0.2506 117 GLU B CA  
5642  C C   . GLU B 117 ? 1.6151 1.1128 0.5877 0.3214  -0.2840 -0.2439 117 GLU B C   
5643  O O   . GLU B 117 ? 1.6109 1.1098 0.5862 0.3288  -0.2854 -0.2404 117 GLU B O   
5644  C CB  . GLU B 117 ? 1.5953 1.1297 0.5961 0.3083  -0.2956 -0.2560 117 GLU B CB  
5645  C CG  . GLU B 117 ? 1.5907 1.1295 0.5942 0.2957  -0.2931 -0.2581 117 GLU B CG  
5646  C CD  . GLU B 117 ? 1.5913 1.1128 0.5873 0.2967  -0.2853 -0.2525 117 GLU B CD  
5647  O OE1 . GLU B 117 ? 1.5893 1.1016 0.5825 0.3066  -0.2798 -0.2478 117 GLU B OE1 
5648  O OE2 . GLU B 117 ? 1.5957 1.1121 0.5877 0.2874  -0.2861 -0.2529 117 GLU B OE2 
5649  N N   . LEU B 118 ? 1.6213 1.1054 0.5847 0.3198  -0.2765 -0.2429 118 LEU B N   
5650  C CA  . LEU B 118 ? 1.6238 1.0956 0.5792 0.3268  -0.2678 -0.2378 118 LEU B CA  
5651  C C   . LEU B 118 ? 1.6289 1.0883 0.5797 0.3245  -0.2625 -0.2403 118 LEU B C   
5652  O O   . LEU B 118 ? 1.6417 1.0945 0.5861 0.3201  -0.2653 -0.2454 118 LEU B O   
5653  C CB  . LEU B 118 ? 1.6410 1.1058 0.5801 0.3317  -0.2669 -0.2345 118 LEU B CB  
5654  C CG  . LEU B 118 ? 1.6451 1.1019 0.5746 0.3377  -0.2583 -0.2290 118 LEU B CG  
5655  C CD1 . LEU B 118 ? 1.6558 1.1029 0.5764 0.3376  -0.2498 -0.2335 118 LEU B CD1 
5656  C CD2 . LEU B 118 ? 1.6263 1.0869 0.5686 0.3412  -0.2561 -0.2252 118 LEU B CD2 
5657  N N   . VAL B 119 ? 1.6208 1.0757 0.5745 0.3280  -0.2562 -0.2372 119 VAL B N   
5658  C CA  . VAL B 119 ? 1.6278 1.0682 0.5772 0.3278  -0.2534 -0.2400 119 VAL B CA  
5659  C C   . VAL B 119 ? 1.6343 1.0652 0.5758 0.3367  -0.2440 -0.2391 119 VAL B C   
5660  O O   . VAL B 119 ? 1.6510 1.0703 0.5833 0.3393  -0.2419 -0.2454 119 VAL B O   
5661  C CB  . VAL B 119 ? 1.6141 1.0587 0.5742 0.3216  -0.2563 -0.2384 119 VAL B CB  
5662  C CG1 . VAL B 119 ? 1.6229 1.0491 0.5770 0.3243  -0.2545 -0.2396 119 VAL B CG1 
5663  C CG2 . VAL B 119 ? 1.6138 1.0672 0.5785 0.3099  -0.2659 -0.2416 119 VAL B CG2 
5664  N N   . SER B 120 ? 1.6222 1.0592 0.5676 0.3412  -0.2384 -0.2326 120 SER B N   
5665  C CA  . SER B 120 ? 1.6258 1.0568 0.5655 0.3482  -0.2289 -0.2313 120 SER B CA  
5666  C C   . SER B 120 ? 1.6272 1.0648 0.5602 0.3515  -0.2250 -0.2251 120 SER B C   
5667  O O   . SER B 120 ? 1.6165 1.0617 0.5554 0.3513  -0.2291 -0.2194 120 SER B O   
5668  C CB  . SER B 120 ? 1.6119 1.0413 0.5607 0.3495  -0.2259 -0.2285 120 SER B CB  
5669  O OG  . SER B 120 ? 1.6186 1.0402 0.5623 0.3562  -0.2176 -0.2304 120 SER B OG  
5670  N N   . LEU B 121 ? 1.6424 1.0776 0.5625 0.3542  -0.2184 -0.2272 121 LEU B N   
5671  C CA  . LEU B 121 ? 1.6479 1.0884 0.5574 0.3556  -0.2142 -0.2202 121 LEU B CA  
5672  C C   . LEU B 121 ? 1.6489 1.0891 0.5562 0.3598  -0.2028 -0.2217 121 LEU B C   
5673  O O   . LEU B 121 ? 1.6626 1.1029 0.5634 0.3607  -0.1973 -0.2305 121 LEU B O   
5674  C CB  . LEU B 121 ? 1.6680 1.1118 0.5616 0.3516  -0.2170 -0.2214 121 LEU B CB  
5675  C CG  . LEU B 121 ? 1.6714 1.1176 0.5612 0.3484  -0.2284 -0.2151 121 LEU B CG  
5676  C CD1 . LEU B 121 ? 1.6739 1.1211 0.5559 0.3494  -0.2304 -0.2039 121 LEU B CD1 
5677  C CD2 . LEU B 121 ? 1.6553 1.1017 0.5621 0.3484  -0.2365 -0.2166 121 LEU B CD2 
5678  N N   . ASP B 122 ? 1.6594 1.1009 0.5731 0.3625  -0.1994 -0.2145 122 ASP B N   
5679  C CA  . ASP B 122 ? 1.6584 1.1013 0.5715 0.3665  -0.1885 -0.2152 122 ASP B CA  
5680  C C   . ASP B 122 ? 1.6625 1.1121 0.5644 0.3651  -0.1852 -0.2053 122 ASP B C   
5681  O O   . ASP B 122 ? 1.6505 1.0998 0.5575 0.3662  -0.1869 -0.1967 122 ASP B O   
5682  C CB  . ASP B 122 ? 1.6403 1.0791 0.5687 0.3698  -0.1873 -0.2146 122 ASP B CB  
5683  C CG  . ASP B 122 ? 1.6425 1.0719 0.5773 0.3701  -0.1917 -0.2238 122 ASP B CG  
5684  O OD1 . ASP B 122 ? 1.6431 1.0703 0.5798 0.3656  -0.2007 -0.2252 122 ASP B OD1 
5685  O OD2 . ASP B 122 ? 1.6445 1.0690 0.5844 0.3742  -0.1872 -0.2292 122 ASP B OD2 
5686  N N   . LEU B 123 ? 1.6791 1.1352 0.5647 0.3617  -0.1813 -0.2072 123 LEU B N   
5687  C CA  . LEU B 123 ? 1.6890 1.1519 0.5592 0.3575  -0.1791 -0.1972 123 LEU B CA  
5688  C C   . LEU B 123 ? 1.6948 1.1687 0.5598 0.3575  -0.1656 -0.2017 123 LEU B C   
5689  O O   . LEU B 123 ? 1.7072 1.1901 0.5563 0.3514  -0.1627 -0.1944 123 LEU B O   
5690  C CB  . LEU B 123 ? 1.7096 1.1752 0.5617 0.3500  -0.1870 -0.1936 123 LEU B CB  
5691  C CG  . LEU B 123 ? 1.7092 1.1662 0.5613 0.3491  -0.2024 -0.1850 123 LEU B CG  
5692  C CD1 . LEU B 123 ? 1.7052 1.1572 0.5561 0.3503  -0.2077 -0.1719 123 LEU B CD1 
5693  C CD2 . LEU B 123 ? 1.6930 1.1440 0.5642 0.3535  -0.2079 -0.1920 123 LEU B CD2 
5694  N N   . TYR B 124 ? 1.6913 1.1652 0.5691 0.3637  -0.1585 -0.2137 124 TYR B N   
5695  C CA  . TYR B 124 ? 1.6978 1.1846 0.5737 0.3649  -0.1461 -0.2220 124 TYR B CA  
5696  C C   . TYR B 124 ? 1.6892 1.1810 0.5641 0.3646  -0.1398 -0.2112 124 TYR B C   
5697  O O   . TYR B 124 ? 1.6762 1.1590 0.5551 0.3653  -0.1451 -0.1989 124 TYR B O   
5698  C CB  . TYR B 124 ? 1.6935 1.1750 0.5858 0.3736  -0.1435 -0.2376 124 TYR B CB  
5699  C CG  . TYR B 124 ? 1.6737 1.1399 0.5824 0.3797  -0.1479 -0.2333 124 TYR B CG  
5700  C CD1 . TYR B 124 ? 1.6681 1.1208 0.5829 0.3795  -0.1587 -0.2323 124 TYR B CD1 
5701  C CD2 . TYR B 124 ? 1.6617 1.1292 0.5787 0.3843  -0.1412 -0.2305 124 TYR B CD2 
5702  C CE1 . TYR B 124 ? 1.6511 1.0942 0.5803 0.3820  -0.1628 -0.2282 124 TYR B CE1 
5703  C CE2 . TYR B 124 ? 1.6419 1.1004 0.5790 0.3863  -0.1448 -0.2247 124 TYR B CE2 
5704  C CZ  . TYR B 124 ? 1.6367 1.0841 0.5802 0.3843  -0.1555 -0.2234 124 TYR B CZ  
5705  O OH  . TYR B 124 ? 1.6177 1.0608 0.5812 0.3832  -0.1590 -0.2172 124 TYR B OH  
5706  N N   . LEU B 125 ? 1.7243 1.2327 0.5944 0.3632  -0.1284 -0.2174 125 LEU B N   
5707  C CA  . LEU B 125 ? 1.7181 1.2343 0.5867 0.3622  -0.1207 -0.2089 125 LEU B CA  
5708  C C   . LEU B 125 ? 1.7232 1.2365 0.5756 0.3536  -0.1273 -0.1898 125 LEU B C   
5709  O O   . LEU B 125 ? 1.7094 1.2125 0.5683 0.3559  -0.1309 -0.1783 125 LEU B O   
5710  C CB  . LEU B 125 ? 1.6960 1.2020 0.5853 0.3720  -0.1187 -0.2093 125 LEU B CB  
5711  C CG  . LEU B 125 ? 1.6942 1.2023 0.5988 0.3810  -0.1128 -0.2268 125 LEU B CG  
5712  C CD1 . LEU B 125 ? 1.6717 1.1670 0.6005 0.3872  -0.1154 -0.2227 125 LEU B CD1 
5713  C CD2 . LEU B 125 ? 1.7020 1.2323 0.6040 0.3801  -0.0998 -0.2346 125 LEU B CD2 
5714  N N   . ASN B 126 ? 1.7412 1.2639 0.5727 0.3430  -0.1300 -0.1868 126 ASN B N   
5715  C CA  . ASN B 126 ? 1.7530 1.2711 0.5661 0.3337  -0.1395 -0.1681 126 ASN B CA  
5716  C C   . ASN B 126 ? 1.7789 1.3187 0.5677 0.3192  -0.1349 -0.1663 126 ASN B C   
5717  O O   . ASN B 126 ? 1.7842 1.3454 0.5730 0.3173  -0.1223 -0.1808 126 ASN B O   
5718  C CB  . ASN B 126 ? 1.7543 1.2547 0.5672 0.3349  -0.1556 -0.1627 126 ASN B CB  
5719  C CG  . ASN B 126 ? 1.7340 1.2175 0.5647 0.3419  -0.1638 -0.1538 126 ASN B CG  
5720  O OD1 . ASN B 126 ? 1.7338 1.2143 0.5656 0.3374  -0.1684 -0.1390 126 ASN B OD1 
5721  N ND2 . ASN B 126 ? 1.7158 1.1910 0.5661 0.3508  -0.1656 -0.1625 126 ASN B ND2 
5722  N N   . ASN B 127 ? 1.7842 1.3193 0.5525 0.3080  -0.1464 -0.1487 127 ASN B N   
5723  C CA  . ASN B 127 ? 1.8123 1.3682 0.5540 0.2901  -0.1450 -0.1429 127 ASN B CA  
5724  C C   . ASN B 127 ? 1.8326 1.3833 0.5585 0.2818  -0.1594 -0.1368 127 ASN B C   
5725  O O   . ASN B 127 ? 1.8581 1.4148 0.5598 0.2655  -0.1674 -0.1219 127 ASN B O   
5726  C CB  . ASN B 127 ? 1.8202 1.3764 0.5491 0.2809  -0.1469 -0.1241 127 ASN B CB  
5727  C CG  . ASN B 127 ? 1.8489 1.4327 0.5506 0.2596  -0.1427 -0.1185 127 ASN B CG  
5728  O OD1 . ASN B 127 ? 1.8742 1.4573 0.5540 0.2450  -0.1555 -0.1048 127 ASN B OD1 
5729  N ND2 . ASN B 127 ? 1.8459 1.4561 0.5493 0.2567  -0.1252 -0.1294 127 ASN B ND2 
5730  N N   . LEU B 128 ? 1.8597 1.3991 0.5991 0.2918  -0.1636 -0.1474 128 LEU B N   
5731  C CA  . LEU B 128 ? 1.8770 1.4117 0.6040 0.2852  -0.1770 -0.1432 128 LEU B CA  
5732  C C   . LEU B 128 ? 1.9014 1.4643 0.6080 0.2700  -0.1700 -0.1506 128 LEU B C   
5733  O O   . LEU B 128 ? 1.8994 1.4848 0.6097 0.2698  -0.1538 -0.1675 128 LEU B O   
5734  C CB  . LEU B 128 ? 1.8595 1.3791 0.6069 0.2988  -0.1813 -0.1547 128 LEU B CB  
5735  C CG  . LEU B 128 ? 1.8455 1.3391 0.6062 0.3084  -0.1963 -0.1454 128 LEU B CG  
5736  C CD1 . LEU B 128 ? 1.8296 1.3141 0.6005 0.3148  -0.1948 -0.1374 128 LEU B CD1 
5737  C CD2 . LEU B 128 ? 1.8277 1.3137 0.6089 0.3193  -0.1966 -0.1597 128 LEU B CD2 
5738  N N   . SER B 129 ? 1.8783 1.4416 0.5643 0.2568  -0.1833 -0.1386 129 SER B N   
5739  C CA  . SER B 129 ? 1.9038 1.4963 0.5682 0.2397  -0.1783 -0.1446 129 SER B CA  
5740  C C   . SER B 129 ? 1.9158 1.5018 0.5739 0.2367  -0.1910 -0.1441 129 SER B C   
5741  O O   . SER B 129 ? 1.9021 1.4623 0.5750 0.2493  -0.2020 -0.1419 129 SER B O   
5742  C CB  . SER B 129 ? 1.9295 1.5385 0.5670 0.2183  -0.1808 -0.1262 129 SER B CB  
5743  O OG  . SER B 129 ? 1.9450 1.5320 0.5705 0.2112  -0.2029 -0.1008 129 SER B OG  
5744  N N   . GLY B 130 ? 1.9627 1.5748 0.5990 0.2191  -0.1893 -0.1469 130 GLY B N   
5745  C CA  . GLY B 130 ? 1.9760 1.5857 0.6046 0.2145  -0.2004 -0.1470 130 GLY B CA  
5746  C C   . GLY B 130 ? 1.9609 1.5724 0.6082 0.2274  -0.1912 -0.1726 130 GLY B C   
5747  O O   . GLY B 130 ? 1.9428 1.5590 0.6086 0.2389  -0.1765 -0.1910 130 GLY B O   
5748  N N   . PRO B 131 ? 1.9372 1.5439 0.5809 0.2255  -0.2012 -0.1737 131 PRO B N   
5749  C CA  . PRO B 131 ? 1.9274 1.5362 0.5866 0.2350  -0.1941 -0.1972 131 PRO B CA  
5750  C C   . PRO B 131 ? 1.8983 1.4767 0.5857 0.2557  -0.1983 -0.2002 131 PRO B C   
5751  O O   . PRO B 131 ? 1.8847 1.4424 0.5805 0.2632  -0.2057 -0.1862 131 PRO B O   
5752  C CB  . PRO B 131 ? 1.9508 1.5678 0.5914 0.2217  -0.2047 -0.1934 131 PRO B CB  
5753  C CG  . PRO B 131 ? 1.9605 1.5598 0.5894 0.2158  -0.2239 -0.1654 131 PRO B CG  
5754  C CD  . PRO B 131 ? 1.9595 1.5595 0.5838 0.2128  -0.2206 -0.1528 131 PRO B CD  
5755  N N   . ILE B 132 ? 1.8760 1.4534 0.5779 0.2637  -0.1938 -0.2195 132 ILE B N   
5756  C CA  . ILE B 132 ? 1.8521 1.4043 0.5787 0.2797  -0.1987 -0.2232 132 ILE B CA  
5757  C C   . ILE B 132 ? 1.8597 1.4038 0.5817 0.2765  -0.2128 -0.2183 132 ILE B C   
5758  O O   . ILE B 132 ? 1.8740 1.4310 0.5885 0.2700  -0.2110 -0.2298 132 ILE B O   
5759  C CB  . ILE B 132 ? 1.8404 1.3944 0.5868 0.2899  -0.1870 -0.2461 132 ILE B CB  
5760  C CG1 . ILE B 132 ? 1.8259 1.3801 0.5842 0.2977  -0.1763 -0.2486 132 ILE B CG1 
5761  C CG2 . ILE B 132 ? 1.8247 1.3573 0.5902 0.3003  -0.1947 -0.2503 132 ILE B CG2 
5762  C CD1 . ILE B 132 ? 1.8414 1.4236 0.5855 0.2881  -0.1642 -0.2542 132 ILE B CD1 
5763  N N   . PRO B 133 ? 1.8522 1.3772 0.5784 0.2803  -0.2271 -0.2027 133 PRO B N   
5764  C CA  . PRO B 133 ? 1.8615 1.3811 0.5829 0.2767  -0.2417 -0.1978 133 PRO B CA  
5765  C C   . PRO B 133 ? 1.8547 1.3736 0.5888 0.2814  -0.2387 -0.2153 133 PRO B C   
5766  O O   . PRO B 133 ? 1.8345 1.3446 0.5894 0.2922  -0.2327 -0.2257 133 PRO B O   
5767  C CB  . PRO B 133 ? 1.8481 1.3467 0.5811 0.2849  -0.2559 -0.1836 133 PRO B CB  
5768  C CG  . PRO B 133 ? 1.8367 1.3312 0.5745 0.2897  -0.2494 -0.1777 133 PRO B CG  
5769  C CD  . PRO B 133 ? 1.8427 1.3556 0.5721 0.2844  -0.2319 -0.1870 133 PRO B CD  
5770  N N   . SER B 134 ? 1.7540 1.2033 0.8423 0.3267  -0.3785 -0.3314 134 SER B N   
5771  C CA  . SER B 134 ? 1.7324 1.1997 0.8456 0.3358  -0.3810 -0.3358 134 SER B CA  
5772  C C   . SER B 134 ? 1.7269 1.1867 0.8483 0.3441  -0.3838 -0.3353 134 SER B C   
5773  O O   . SER B 134 ? 1.7115 1.1849 0.8517 0.3479  -0.3847 -0.3400 134 SER B O   
5774  C CB  . SER B 134 ? 1.7386 1.2145 0.8474 0.3397  -0.3835 -0.3370 134 SER B CB  
5775  O OG  . SER B 134 ? 1.7620 1.2178 0.8487 0.3463  -0.3883 -0.3316 134 SER B OG  
5776  N N   . THR B 135 ? 1.7004 1.1391 0.8065 0.3457  -0.3847 -0.3313 135 THR B N   
5777  C CA  . THR B 135 ? 1.6971 1.1327 0.8111 0.3535  -0.3868 -0.3336 135 THR B CA  
5778  C C   . THR B 135 ? 1.6800 1.1217 0.8098 0.3475  -0.3829 -0.3358 135 THR B C   
5779  O O   . THR B 135 ? 1.6752 1.1205 0.8140 0.3508  -0.3830 -0.3398 135 THR B O   
5780  C CB  . THR B 135 ? 1.7232 1.1321 0.8143 0.3588  -0.3899 -0.3302 135 THR B CB  
5781  O OG1 . THR B 135 ? 1.7376 1.1283 0.8093 0.3476  -0.3863 -0.3250 135 THR B OG1 
5782  C CG2 . THR B 135 ? 1.7452 1.1453 0.8201 0.3707  -0.3974 -0.3292 135 THR B CG2 
5783  N N   . LEU B 136 ? 1.6922 1.1366 0.8243 0.3388  -0.3800 -0.3344 136 LEU B N   
5784  C CA  . LEU B 136 ? 1.6816 1.1282 0.8243 0.3344  -0.3785 -0.3357 136 LEU B CA  
5785  C C   . LEU B 136 ? 1.6710 1.1282 0.8282 0.3359  -0.3797 -0.3401 136 LEU B C   
5786  O O   . LEU B 136 ? 1.6693 1.1225 0.8294 0.3318  -0.3792 -0.3408 136 LEU B O   
5787  C CB  . LEU B 136 ? 1.6801 1.1296 0.8220 0.3276  -0.3774 -0.3350 136 LEU B CB  
5788  C CG  . LEU B 136 ? 1.6931 1.1369 0.8191 0.3215  -0.3751 -0.3330 136 LEU B CG  
5789  C CD1 . LEU B 136 ? 1.6882 1.1483 0.8200 0.3156  -0.3743 -0.3371 136 LEU B CD1 
5790  C CD2 . LEU B 136 ? 1.7054 1.1299 0.8180 0.3183  -0.3733 -0.3299 136 LEU B CD2 
5791  N N   . GLY B 137 ? 1.6605 1.1285 0.8232 0.3402  -0.3812 -0.3432 137 GLY B N   
5792  C CA  . GLY B 137 ? 1.6550 1.1306 0.8285 0.3396  -0.3818 -0.3486 137 GLY B CA  
5793  C C   . GLY B 137 ? 1.6562 1.1340 0.8325 0.3387  -0.3803 -0.3531 137 GLY B C   
5794  O O   . GLY B 137 ? 1.6561 1.1374 0.8375 0.3336  -0.3793 -0.3585 137 GLY B O   
5795  N N   . ARG B 138 ? 1.6410 1.1166 0.8126 0.3430  -0.3801 -0.3527 138 ARG B N   
5796  C CA  . ARG B 138 ? 1.6425 1.1256 0.8189 0.3425  -0.3783 -0.3601 138 ARG B CA  
5797  C C   . ARG B 138 ? 1.6448 1.1182 0.8174 0.3322  -0.3742 -0.3596 138 ARG B C   
5798  O O   . ARG B 138 ? 1.6470 1.1290 0.8231 0.3268  -0.3709 -0.3676 138 ARG B O   
5799  C CB  . ARG B 138 ? 1.6507 1.1345 0.8231 0.3543  -0.3814 -0.3619 138 ARG B CB  
5800  C CG  . ARG B 138 ? 1.6575 1.1392 0.8227 0.3645  -0.3869 -0.3582 138 ARG B CG  
5801  C CD  . ARG B 138 ? 1.6663 1.1595 0.8338 0.3786  -0.3927 -0.3659 138 ARG B CD  
5802  N NE  . ARG B 138 ? 1.6816 1.1610 0.8394 0.3875  -0.3954 -0.3668 138 ARG B NE  
5803  C CZ  . ARG B 138 ? 1.6826 1.1768 0.8509 0.3934  -0.3958 -0.3783 138 ARG B CZ  
5804  N NH1 . ARG B 138 ? 1.6695 1.1944 0.8575 0.3889  -0.3926 -0.3902 138 ARG B NH1 
5805  N NH2 . ARG B 138 ? 1.6995 1.1781 0.8578 0.4030  -0.3990 -0.3795 138 ARG B NH2 
5806  N N   . LEU B 139 ? 1.6576 1.1159 0.8225 0.3286  -0.3744 -0.3516 139 LEU B N   
5807  C CA  . LEU B 139 ? 1.6628 1.1101 0.8210 0.3193  -0.3719 -0.3500 139 LEU B CA  
5808  C C   . LEU B 139 ? 1.6680 1.1089 0.8234 0.3114  -0.3728 -0.3507 139 LEU B C   
5809  O O   . LEU B 139 ? 1.6723 1.1010 0.8218 0.3104  -0.3764 -0.3456 139 LEU B O   
5810  C CB  . LEU B 139 ? 1.6643 1.1004 0.8151 0.3193  -0.3729 -0.3427 139 LEU B CB  
5811  C CG  . LEU B 139 ? 1.6661 1.1003 0.8131 0.3261  -0.3734 -0.3403 139 LEU B CG  
5812  C CD1 . LEU B 139 ? 1.6688 1.0953 0.8083 0.3220  -0.3735 -0.3351 139 LEU B CD1 
5813  C CD2 . LEU B 139 ? 1.6732 1.1052 0.8175 0.3299  -0.3717 -0.3444 139 LEU B CD2 
5814  N N   . LYS B 140 ? 1.6812 1.1300 0.8392 0.3058  -0.3702 -0.3587 140 LYS B N   
5815  C CA  . LYS B 140 ? 1.6941 1.1304 0.8437 0.2966  -0.3711 -0.3601 140 LYS B CA  
5816  C C   . LYS B 140 ? 1.7126 1.1254 0.8432 0.2858  -0.3712 -0.3560 140 LYS B C   
5817  O O   . LYS B 140 ? 1.7313 1.1227 0.8478 0.2802  -0.3748 -0.3544 140 LYS B O   
5818  C CB  . LYS B 140 ? 1.6972 1.1486 0.8516 0.2892  -0.3668 -0.3716 140 LYS B CB  
5819  C CG  . LYS B 140 ? 1.6819 1.1588 0.8538 0.3003  -0.3678 -0.3770 140 LYS B CG  
5820  C CD  . LYS B 140 ? 1.6774 1.1503 0.8526 0.3078  -0.3728 -0.3724 140 LYS B CD  
5821  C CE  . LYS B 140 ? 1.6673 1.1647 0.8560 0.3159  -0.3737 -0.3787 140 LYS B CE  
5822  N NZ  . LYS B 140 ? 1.6721 1.1862 0.8658 0.3069  -0.3699 -0.3917 140 LYS B NZ  
5823  N N   . LYS B 141 ? 1.6388 1.0521 0.7659 0.2832  -0.3682 -0.3544 141 LYS B N   
5824  C CA  . LYS B 141 ? 1.6583 1.0495 0.7651 0.2730  -0.3689 -0.3499 141 LYS B CA  
5825  C C   . LYS B 141 ? 1.6584 1.0369 0.7612 0.2814  -0.3763 -0.3404 141 LYS B C   
5826  O O   . LYS B 141 ? 1.6769 1.0360 0.7616 0.2754  -0.3794 -0.3358 141 LYS B O   
5827  C CB  . LYS B 141 ? 1.6598 1.0598 0.7641 0.2646  -0.3616 -0.3547 141 LYS B CB  
5828  C CG  . LYS B 141 ? 1.6557 1.0804 0.7703 0.2595  -0.3539 -0.3683 141 LYS B CG  
5829  C CD  . LYS B 141 ? 1.6669 1.0930 0.7775 0.2490  -0.3519 -0.3759 141 LYS B CD  
5830  C CE  . LYS B 141 ? 1.6480 1.0980 0.7809 0.2613  -0.3532 -0.3817 141 LYS B CE  
5831  N NZ  . LYS B 141 ? 1.6581 1.1174 0.7899 0.2492  -0.3494 -0.3931 141 LYS B NZ  
5832  N N   . LEU B 142 ? 1.6647 1.0557 0.7828 0.2940  -0.3792 -0.3385 142 LEU B N   
5833  C CA  . LEU B 142 ? 1.6630 1.0511 0.7809 0.3008  -0.3850 -0.3333 142 LEU B CA  
5834  C C   . LEU B 142 ? 1.6828 1.0509 0.7879 0.3030  -0.3943 -0.3308 142 LEU B C   
5835  O O   . LEU B 142 ? 1.6910 1.0509 0.7944 0.3052  -0.3977 -0.3331 142 LEU B O   
5836  C CB  . LEU B 142 ? 1.6449 1.0512 0.7787 0.3105  -0.3851 -0.3342 142 LEU B CB  
5837  C CG  . LEU B 142 ? 1.6428 1.0545 0.7807 0.3176  -0.3912 -0.3334 142 LEU B CG  
5838  C CD1 . LEU B 142 ? 1.6461 1.0569 0.7783 0.3148  -0.3919 -0.3310 142 LEU B CD1 
5839  C CD2 . LEU B 142 ? 1.6290 1.0590 0.7788 0.3227  -0.3890 -0.3360 142 LEU B CD2 
5840  N N   . ARG B 143 ? 1.7004 1.0592 0.7952 0.3034  -0.3994 -0.3269 143 ARG B N   
5841  C CA  . ARG B 143 ? 1.7240 1.0621 0.8047 0.3098  -0.4116 -0.3248 143 ARG B CA  
5842  C C   . ARG B 143 ? 1.7154 1.0701 0.8086 0.3230  -0.4190 -0.3267 143 ARG B C   
5843  O O   . ARG B 143 ? 1.7264 1.0758 0.8198 0.3349  -0.4293 -0.3296 143 ARG B O   
5844  C CB  . ARG B 143 ? 1.7529 1.0641 0.8060 0.3002  -0.4144 -0.3196 143 ARG B CB  
5845  C CG  . ARG B 143 ? 1.7675 1.0636 0.8042 0.2831  -0.4062 -0.3200 143 ARG B CG  
5846  C CD  . ARG B 143 ? 1.8097 1.0683 0.8098 0.2740  -0.4128 -0.3143 143 ARG B CD  
5847  N NE  . ARG B 143 ? 1.8236 1.0746 0.8066 0.2527  -0.4021 -0.3159 143 ARG B NE  
5848  C CZ  . ARG B 143 ? 1.8658 1.0818 0.8112 0.2382  -0.4046 -0.3116 143 ARG B CZ  
5849  N NH1 . ARG B 143 ? 1.9018 1.0816 0.8200 0.2451  -0.4194 -0.3039 143 ARG B NH1 
5850  N NH2 . ARG B 143 ? 1.8759 1.0929 0.8087 0.2164  -0.3925 -0.3160 143 ARG B NH2 
5851  N N   . PHE B 144 ? 1.6856 1.0610 0.7888 0.3209  -0.4142 -0.3270 144 PHE B N   
5852  C CA  . PHE B 144 ? 1.6801 1.0754 0.7937 0.3294  -0.4201 -0.3310 144 PHE B CA  
5853  C C   . PHE B 144 ? 1.6559 1.0784 0.7863 0.3258  -0.4105 -0.3345 144 PHE B C   
5854  O O   . PHE B 144 ? 1.6495 1.0718 0.7773 0.3162  -0.4017 -0.3319 144 PHE B O   
5855  C CB  . PHE B 144 ? 1.6942 1.0835 0.7953 0.3269  -0.4251 -0.3283 144 PHE B CB  
5856  C CG  . PHE B 144 ? 1.7240 1.0784 0.7987 0.3237  -0.4311 -0.3219 144 PHE B CG  
5857  C CD1 . PHE B 144 ? 1.7511 1.0819 0.8119 0.3345  -0.4446 -0.3215 144 PHE B CD1 
5858  C CD2 . PHE B 144 ? 1.7299 1.0726 0.7904 0.3091  -0.4235 -0.3171 144 PHE B CD2 
5859  C CE1 . PHE B 144 ? 1.7873 1.0787 0.8159 0.3288  -0.4504 -0.3148 144 PHE B CE1 
5860  C CE2 . PHE B 144 ? 1.7620 1.0720 0.7937 0.3023  -0.4279 -0.3117 144 PHE B CE2 
5861  C CZ  . PHE B 144 ? 1.7927 1.0745 0.8061 0.3112  -0.4413 -0.3096 144 PHE B CZ  
5862  N N   . LEU B 145 ? 1.6799 1.1235 0.8245 0.3331  -0.4127 -0.3413 145 LEU B N   
5863  C CA  . LEU B 145 ? 1.6646 1.1307 0.8189 0.3276  -0.4042 -0.3451 145 LEU B CA  
5864  C C   . LEU B 145 ? 1.6631 1.1578 0.8283 0.3318  -0.4086 -0.3550 145 LEU B C   
5865  O O   . LEU B 145 ? 1.6636 1.1707 0.8391 0.3425  -0.4151 -0.3622 145 LEU B O   
5866  C CB  . LEU B 145 ? 1.6563 1.1234 0.8158 0.3287  -0.3995 -0.3452 145 LEU B CB  
5867  C CG  . LEU B 145 ? 1.6486 1.1301 0.8098 0.3220  -0.3912 -0.3471 145 LEU B CG  
5868  C CD1 . LEU B 145 ? 1.6462 1.1151 0.8031 0.3207  -0.3861 -0.3421 145 LEU B CD1 
5869  C CD2 . LEU B 145 ? 1.6447 1.1522 0.8171 0.3255  -0.3928 -0.3566 145 LEU B CD2 
5870  N N   . ARG B 146 ? 1.6512 1.1586 0.8147 0.3229  -0.4049 -0.3574 146 ARG B N   
5871  C CA  . ARG B 146 ? 1.6504 1.1917 0.8251 0.3238  -0.4080 -0.3697 146 ARG B CA  
5872  C C   . ARG B 146 ? 1.6468 1.2030 0.8185 0.3072  -0.3961 -0.3736 146 ARG B C   
5873  O O   . ARG B 146 ? 1.6515 1.1951 0.8107 0.2953  -0.3899 -0.3689 146 ARG B O   
5874  C CB  . ARG B 146 ? 1.6602 1.2039 0.8325 0.3275  -0.4166 -0.3711 146 ARG B CB  
5875  C CG  . ARG B 146 ? 1.6744 1.1943 0.8404 0.3428  -0.4299 -0.3661 146 ARG B CG  
5876  C CD  . ARG B 146 ? 1.6887 1.2012 0.8440 0.3430  -0.4370 -0.3634 146 ARG B CD  
5877  N NE  . ARG B 146 ? 1.7101 1.1859 0.8476 0.3518  -0.4473 -0.3546 146 ARG B NE  
5878  C CZ  . ARG B 146 ? 1.7172 1.1612 0.8363 0.3419  -0.4422 -0.3432 146 ARG B CZ  
5879  N NH1 . ARG B 146 ? 1.7032 1.1478 0.8219 0.3266  -0.4281 -0.3395 146 ARG B NH1 
5880  N NH2 . ARG B 146 ? 1.7431 1.1530 0.8416 0.3473  -0.4517 -0.3364 146 ARG B NH2 
5881  N N   . LEU B 147 ? 1.9966 1.1459 0.6689 0.3496  -0.1201 -0.2558 147 LEU B N   
5882  C CA  . LEU B 147 ? 1.9717 1.1793 0.6444 0.3450  -0.1040 -0.2443 147 LEU B CA  
5883  C C   . LEU B 147 ? 1.9761 1.2096 0.6598 0.3632  -0.0919 -0.2690 147 LEU B C   
5884  O O   . LEU B 147 ? 1.9680 1.2519 0.6466 0.3590  -0.0781 -0.2692 147 LEU B O   
5885  C CB  . LEU B 147 ? 1.9846 1.2245 0.6324 0.3246  -0.1025 -0.2429 147 LEU B CB  
5886  C CG  . LEU B 147 ? 1.9915 1.2058 0.6255 0.3061  -0.1160 -0.2276 147 LEU B CG  
5887  C CD1 . LEU B 147 ? 2.0056 1.2592 0.6158 0.2867  -0.1140 -0.2276 147 LEU B CD1 
5888  C CD2 . LEU B 147 ? 1.9527 1.1545 0.6027 0.2994  -0.1181 -0.1894 147 LEU B CD2 
5889  N N   . ASN B 148 ? 2.0213 1.2221 0.7209 0.3829  -0.0970 -0.2892 148 ASN B N   
5890  C CA  . ASN B 148 ? 2.0315 1.2543 0.7432 0.4006  -0.0866 -0.3181 148 ASN B CA  
5891  C C   . ASN B 148 ? 1.9925 1.2521 0.7212 0.4069  -0.0721 -0.3007 148 ASN B C   
5892  O O   . ASN B 148 ? 1.9576 1.2210 0.6919 0.3992  -0.0708 -0.2668 148 ASN B O   
5893  C CB  . ASN B 148 ? 2.0562 1.2327 0.7862 0.4201  -0.0976 -0.3420 148 ASN B CB  
5894  C CG  . ASN B 148 ? 2.0365 1.1723 0.7819 0.4267  -0.1088 -0.3177 148 ASN B CG  
5895  O OD1 . ASN B 148 ? 2.0335 1.1388 0.7694 0.4141  -0.1200 -0.2969 148 ASN B OD1 
5896  N ND2 . ASN B 148 ? 2.0235 1.1603 0.7935 0.4451  -0.1056 -0.3204 148 ASN B ND2 
5897  N N   . ASN B 149 ? 1.9892 1.2792 0.7336 0.4191  -0.0602 -0.3244 149 ASN B N   
5898  C CA  . ASN B 149 ? 1.9562 1.2850 0.7188 0.4263  -0.0448 -0.3142 149 ASN B CA  
5899  C C   . ASN B 149 ? 1.9286 1.2958 0.6757 0.4085  -0.0347 -0.2834 149 ASN B C   
5900  O O   . ASN B 149 ? 1.8930 1.2629 0.6513 0.4074  -0.0315 -0.2539 149 ASN B O   
5901  C CB  . ASN B 149 ? 1.9381 1.2343 0.7209 0.4442  -0.0504 -0.3046 149 ASN B CB  
5902  C CG  . ASN B 149 ? 1.9560 1.2401 0.7682 0.4644  -0.0534 -0.3343 149 ASN B CG  
5903  O OD1 . ASN B 149 ? 1.9904 1.2537 0.8044 0.4667  -0.0619 -0.3594 149 ASN B OD1 
5904  N ND2 . ASN B 149 ? 1.9328 1.2309 0.7710 0.4785  -0.0463 -0.3315 149 ASN B ND2 
5905  N N   . ASN B 150 ? 1.9714 1.3730 0.7014 0.3917  -0.0295 -0.2890 150 ASN B N   
5906  C CA  . ASN B 150 ? 1.9504 1.3916 0.6673 0.3729  -0.0215 -0.2599 150 ASN B CA  
5907  C C   . ASN B 150 ? 1.9643 1.4611 0.6768 0.3625  -0.0082 -0.2766 150 ASN B C   
5908  O O   . ASN B 150 ? 1.9859 1.4912 0.7084 0.3706  -0.0031 -0.3106 150 ASN B O   
5909  C CB  . ASN B 150 ? 1.9557 1.3720 0.6497 0.3562  -0.0353 -0.2389 150 ASN B CB  
5910  C CG  . ASN B 150 ? 1.9188 1.3121 0.6315 0.3542  -0.0401 -0.2038 150 ASN B CG  
5911  O OD1 . ASN B 150 ? 1.8877 1.3093 0.6078 0.3439  -0.0323 -0.1735 150 ASN B OD1 
5912  N ND2 . ASN B 150 ? 1.9234 1.2653 0.6450 0.3633  -0.0527 -0.2078 150 ASN B ND2 
5913  N N   . SER B 151 ? 1.9519 1.4876 0.6508 0.3431  -0.0024 -0.2520 151 SER B N   
5914  C CA  . SER B 151 ? 1.9668 1.5574 0.6560 0.3280  0.0091  -0.2627 151 SER B CA  
5915  C C   . SER B 151 ? 1.9925 1.5902 0.6515 0.3053  0.0000  -0.2592 151 SER B C   
5916  O O   . SER B 151 ? 1.9950 1.6401 0.6412 0.2861  0.0067  -0.2478 151 SER B O   
5917  C CB  . SER B 151 ? 1.9344 1.5719 0.6349 0.3228  0.0243  -0.2366 151 SER B CB  
5918  O OG  . SER B 151 ? 1.9510 1.6408 0.6441 0.3098  0.0369  -0.2507 151 SER B OG  
5919  N N   . LEU B 152 ? 2.0178 1.5694 0.6658 0.3064  -0.0158 -0.2683 152 LEU B N   
5920  C CA  . LEU B 152 ? 2.0409 1.5958 0.6619 0.2849  -0.0259 -0.2642 152 LEU B CA  
5921  C C   . LEU B 152 ? 2.0785 1.6670 0.6858 0.2735  -0.0195 -0.2984 152 LEU B C   
5922  O O   . LEU B 152 ? 2.0956 1.6815 0.7154 0.2857  -0.0126 -0.3340 152 LEU B O   
5923  C CB  . LEU B 152 ? 2.0520 1.5458 0.6673 0.2894  -0.0439 -0.2661 152 LEU B CB  
5924  C CG  . LEU B 152 ? 2.0253 1.4933 0.6394 0.2842  -0.0542 -0.2265 152 LEU B CG  
5925  C CD1 . LEU B 152 ? 1.9830 1.4654 0.6179 0.2920  -0.0441 -0.1982 152 LEU B CD1 
5926  C CD2 . LEU B 152 ? 2.0360 1.4382 0.6500 0.2939  -0.0694 -0.2344 152 LEU B CD2 
5927  N N   . SER B 153 ? 2.0611 1.6824 0.6442 0.2486  -0.0218 -0.2874 153 SER B N   
5928  C CA  . SER B 153 ? 2.0979 1.7573 0.6639 0.2324  -0.0150 -0.3169 153 SER B CA  
5929  C C   . SER B 153 ? 2.1209 1.7837 0.6587 0.2091  -0.0278 -0.3099 153 SER B C   
5930  O O   . SER B 153 ? 2.1027 1.7711 0.6330 0.1974  -0.0361 -0.2716 153 SER B O   
5931  C CB  . SER B 153 ? 2.0903 1.8114 0.6561 0.2218  0.0021  -0.3100 153 SER B CB  
5932  O OG  . SER B 153 ? 2.0623 1.8059 0.6246 0.2102  -0.0001 -0.2639 153 SER B OG  
5933  N N   . GLY B 154 ? 2.1812 1.8419 0.7067 0.2018  -0.0289 -0.3469 154 GLY B N   
5934  C CA  . GLY B 154 ? 2.2070 1.8708 0.7063 0.1796  -0.0407 -0.3461 154 GLY B CA  
5935  C C   . GLY B 154 ? 2.2417 1.8681 0.7410 0.1850  -0.0458 -0.3877 154 GLY B C   
5936  O O   . GLY B 154 ? 2.2571 1.8788 0.7716 0.1973  -0.0356 -0.4241 154 GLY B O   
5937  N N   . GLU B 155 ? 2.2166 1.8172 0.7017 0.1750  -0.0614 -0.3811 155 GLU B N   
5938  C CA  . GLU B 155 ? 2.2495 1.8116 0.7350 0.1781  -0.0679 -0.4167 155 GLU B CA  
5939  C C   . GLU B 155 ? 2.2379 1.7428 0.7250 0.1841  -0.0862 -0.3956 155 GLU B C   
5940  O O   . GLU B 155 ? 2.2136 1.7207 0.6932 0.1760  -0.0945 -0.3559 155 GLU B O   
5941  C CB  . GLU B 155 ? 2.2897 1.8902 0.7504 0.1512  -0.0656 -0.4410 155 GLU B CB  
5942  C CG  . GLU B 155 ? 2.3269 1.8934 0.7915 0.1532  -0.0688 -0.4833 155 GLU B CG  
5943  C CD  . GLU B 155 ? 2.3675 1.9775 0.8083 0.1252  -0.0634 -0.5104 155 GLU B CD  
5944  O OE1 . GLU B 155 ? 2.3684 2.0143 0.7833 0.1014  -0.0694 -0.4867 155 GLU B OE1 
5945  O OE2 . GLU B 155 ? 2.3994 2.0081 0.8488 0.1261  -0.0531 -0.5553 155 GLU B OE2 
5946  N N   . ILE B 156 ? 2.2498 1.7034 0.7488 0.1974  -0.0922 -0.4223 156 ILE B N   
5947  C CA  . ILE B 156 ? 2.2427 1.6368 0.7444 0.2034  -0.1089 -0.4062 156 ILE B CA  
5948  C C   . ILE B 156 ? 2.2602 1.6602 0.7378 0.1787  -0.1200 -0.3989 156 ILE B C   
5949  O O   . ILE B 156 ? 2.2959 1.7104 0.7633 0.1660  -0.1183 -0.4300 156 ILE B O   
5950  C CB  . ILE B 156 ? 2.2604 1.5994 0.7838 0.2239  -0.1123 -0.4367 156 ILE B CB  
5951  C CG1 . ILE B 156 ? 2.2403 1.5714 0.7900 0.2492  -0.1037 -0.4396 156 ILE B CG1 
5952  C CG2 . ILE B 156 ? 2.2587 1.5378 0.7811 0.2256  -0.1299 -0.4211 156 ILE B CG2 
5953  C CD1 . ILE B 156 ? 2.2595 1.6254 0.8220 0.2536  -0.0875 -0.4770 156 ILE B CD1 
5954  N N   . PRO B 157 ? 2.2340 1.6251 0.7042 0.1705  -0.1309 -0.3594 157 PRO B N   
5955  C CA  . PRO B 157 ? 2.2496 1.6474 0.6995 0.1468  -0.1423 -0.3509 157 PRO B CA  
5956  C C   . PRO B 157 ? 2.2796 1.6284 0.7300 0.1478  -0.1517 -0.3784 157 PRO B C   
5957  O O   . PRO B 157 ? 2.2776 1.5718 0.7450 0.1669  -0.1555 -0.3864 157 PRO B O   
5958  C CB  . PRO B 157 ? 2.2131 1.6012 0.6650 0.1431  -0.1515 -0.3028 157 PRO B CB  
5959  C CG  . PRO B 157 ? 2.1787 1.5705 0.6481 0.1607  -0.1421 -0.2851 157 PRO B CG  
5960  C CD  . PRO B 157 ? 2.1911 1.5768 0.6726 0.1802  -0.1307 -0.3205 157 PRO B CD  
5961  N N   . ARG B 158 ? 2.3088 1.6792 0.7408 0.1260  -0.1556 -0.3922 158 ARG B N   
5962  C CA  . ARG B 158 ? 2.3366 1.6634 0.7685 0.1232  -0.1652 -0.4144 158 ARG B CA  
5963  C C   . ARG B 158 ? 2.3170 1.5922 0.7526 0.1253  -0.1804 -0.3843 158 ARG B C   
5964  O O   . ARG B 158 ? 2.3319 1.5540 0.7758 0.1319  -0.1878 -0.3987 158 ARG B O   
5965  C CB  . ARG B 158 ? 2.3694 1.7370 0.7798 0.0969  -0.1659 -0.4323 158 ARG B CB  
5966  C CG  . ARG B 158 ? 2.3971 1.7258 0.8056 0.0893  -0.1764 -0.4510 158 ARG B CG  
5967  C CD  . ARG B 158 ? 2.3859 1.7119 0.7810 0.0716  -0.1915 -0.4174 158 ARG B CD  
5968  N NE  . ARG B 158 ? 2.4004 1.6701 0.8009 0.0718  -0.2027 -0.4264 158 ARG B NE  
5969  C CZ  . ARG B 158 ? 2.3896 1.6391 0.7848 0.0609  -0.2163 -0.3994 158 ARG B CZ  
5970  N NH1 . ARG B 158 ? 2.3636 1.6433 0.7505 0.0495  -0.2213 -0.3609 158 ARG B NH1 
5971  N NH2 . ARG B 158 ? 2.4054 1.6036 0.8066 0.0612  -0.2249 -0.4112 158 ARG B NH2 
5972  N N   . SER B 159 ? 2.2841 1.5747 0.7159 0.1191  -0.1845 -0.3424 159 SER B N   
5973  C CA  . SER B 159 ? 2.2650 1.5116 0.7008 0.1177  -0.1977 -0.3134 159 SER B CA  
5974  C C   . SER B 159 ? 2.2546 1.4394 0.7090 0.1408  -0.1993 -0.3160 159 SER B C   
5975  O O   . SER B 159 ? 2.2561 1.3913 0.7133 0.1398  -0.2104 -0.3095 159 SER B O   
5976  C CB  . SER B 159 ? 2.2297 1.5086 0.6646 0.1081  -0.1992 -0.2689 159 SER B CB  
5977  O OG  . SER B 159 ? 2.2022 1.4970 0.6496 0.1235  -0.1880 -0.2568 159 SER B OG  
5978  N N   . LEU B 160 ? 2.2887 1.4763 0.7564 0.1607  -0.1887 -0.3250 160 LEU B N   
5979  C CA  . LEU B 160 ? 2.2797 1.4123 0.7657 0.1827  -0.1909 -0.3265 160 LEU B CA  
5980  C C   . LEU B 160 ? 2.3137 1.3981 0.8066 0.1887  -0.1973 -0.3578 160 LEU B C   
5981  O O   . LEU B 160 ? 2.3098 1.3427 0.8171 0.2036  -0.2029 -0.3556 160 LEU B O   
5982  C CB  . LEU B 160 ? 2.2642 1.4162 0.7642 0.2022  -0.1779 -0.3317 160 LEU B CB  
5983  C CG  . LEU B 160 ? 2.2256 1.4166 0.7260 0.2009  -0.1706 -0.2979 160 LEU B CG  
5984  C CD1 . LEU B 160 ? 2.2156 1.4288 0.7302 0.2194  -0.1566 -0.3095 160 LEU B CD1 
5985  C CD2 . LEU B 160 ? 2.1949 1.3513 0.7019 0.2016  -0.1786 -0.2624 160 LEU B CD2 
5986  N N   . THR B 161 ? 2.3176 1.4186 0.8021 0.1767  -0.1966 -0.3862 161 THR B N   
5987  C CA  . THR B 161 ? 2.3508 1.4083 0.8452 0.1805  -0.2021 -0.4157 161 THR B CA  
5988  C C   . THR B 161 ? 2.3569 1.3765 0.8435 0.1667  -0.2162 -0.4027 161 THR B C   
5989  O O   . THR B 161 ? 2.3810 1.3567 0.8786 0.1705  -0.2221 -0.4212 161 THR B O   
5990  C CB  . THR B 161 ? 2.3859 1.4789 0.8777 0.1731  -0.1930 -0.4556 161 THR B CB  
5991  O OG1 . THR B 161 ? 2.3950 1.5258 0.8628 0.1473  -0.1952 -0.4513 161 THR B OG1 
5992  C CG2 . THR B 161 ? 2.3798 1.5160 0.8783 0.1837  -0.1777 -0.4685 161 THR B CG2 
5993  N N   . ALA B 162 ? 2.3221 1.3584 0.7932 0.1504  -0.2215 -0.3712 162 ALA B N   
5994  C CA  . ALA B 162 ? 2.3271 1.3329 0.7913 0.1350  -0.2343 -0.3588 162 ALA B CA  
5995  C C   . ALA B 162 ? 2.3022 1.2581 0.7750 0.1416  -0.2422 -0.3301 162 ALA B C   
5996  O O   . ALA B 162 ? 2.3031 1.2327 0.7716 0.1283  -0.2523 -0.3172 162 ALA B O   
5997  C CB  . ALA B 162 ? 2.3218 1.3760 0.7666 0.1110  -0.2366 -0.3419 162 ALA B CB  
5998  N N   . VAL B 163 ? 2.2957 1.2395 0.7807 0.1606  -0.2376 -0.3204 163 VAL B N   
5999  C CA  . VAL B 163 ? 2.2716 1.1727 0.7635 0.1647  -0.2440 -0.2928 163 VAL B CA  
6000  C C   . VAL B 163 ? 2.2939 1.1321 0.7954 0.1686  -0.2535 -0.3042 163 VAL B C   
6001  O O   . VAL B 163 ? 2.2857 1.0885 0.7864 0.1598  -0.2620 -0.2846 163 VAL B O   
6002  C CB  . VAL B 163 ? 2.2432 1.1532 0.7454 0.1830  -0.2357 -0.2803 163 VAL B CB  
6003  C CG1 . VAL B 163 ? 2.2612 1.1732 0.7759 0.2030  -0.2287 -0.3109 163 VAL B CG1 
6004  C CG2 . VAL B 163 ? 2.2172 1.0867 0.7369 0.1865  -0.2403 -0.2538 163 VAL B CG2 
6005  N N   . LEU B 164 ? 2.3278 1.1541 0.8408 0.1808  -0.2516 -0.3358 164 LEU B N   
6006  C CA  . LEU B 164 ? 2.3543 1.1251 0.8827 0.1869  -0.2597 -0.3504 164 LEU B CA  
6007  C C   . LEU B 164 ? 2.3388 1.0634 0.8807 0.2001  -0.2652 -0.3308 164 LEU B C   
6008  O O   . LEU B 164 ? 2.3604 1.0428 0.9191 0.2082  -0.2715 -0.3413 164 LEU B O   
6009  C CB  . LEU B 164 ? 2.3741 1.1284 0.8944 0.1666  -0.2678 -0.3535 164 LEU B CB  
6010  C CG  . LEU B 164 ? 2.3623 1.0718 0.8822 0.1573  -0.2780 -0.3265 164 LEU B CG  
6011  C CD1 . LEU B 164 ? 2.3789 1.0330 0.9191 0.1689  -0.2846 -0.3313 164 LEU B CD1 
6012  C CD2 . LEU B 164 ? 2.3717 1.0859 0.8785 0.1336  -0.2834 -0.3244 164 LEU B CD2 
6013  N N   . THR B 165 ? 2.2840 1.0178 0.8203 0.2014  -0.2627 -0.3032 165 THR B N   
6014  C CA  . THR B 165 ? 2.2690 0.9638 0.8163 0.2119  -0.2670 -0.2849 165 THR B CA  
6015  C C   . THR B 165 ? 2.2546 0.9657 0.8131 0.2335  -0.2592 -0.2874 165 THR B C   
6016  O O   . THR B 165 ? 2.2453 0.9254 0.8148 0.2439  -0.2630 -0.2750 165 THR B O   
6017  C CB  . THR B 165 ? 2.2402 0.9270 0.7772 0.1964  -0.2697 -0.2517 165 THR B CB  
6018  O OG1 . THR B 165 ? 2.1992 0.9366 0.7448 0.1979  -0.2582 -0.2316 165 THR B OG1 
6019  C CG2 . THR B 165 ? 2.2497 0.9376 0.7736 0.1735  -0.2748 -0.2494 165 THR B CG2 
6020  N N   . LEU B 166 ? 2.2524 1.0130 0.8087 0.2392  -0.2484 -0.3023 166 LEU B N   
6021  C CA  . LEU B 166 ? 2.2392 1.0193 0.8080 0.2595  -0.2398 -0.3069 166 LEU B CA  
6022  C C   . LEU B 166 ? 2.2625 1.0063 0.8554 0.2782  -0.2450 -0.3257 166 LEU B C   
6023  O O   . LEU B 166 ? 2.2939 1.0342 0.8963 0.2802  -0.2460 -0.3533 166 LEU B O   
6024  C CB  . LEU B 166 ? 2.2388 1.0799 0.8017 0.2590  -0.2270 -0.3231 166 LEU B CB  
6025  C CG  . LEU B 166 ? 2.2309 1.1010 0.8085 0.2789  -0.2158 -0.3359 166 LEU B CG  
6026  C CD1 . LEU B 166 ? 2.1951 1.0599 0.7841 0.2891  -0.2138 -0.3090 166 LEU B CD1 
6027  C CD2 . LEU B 166 ? 2.2273 1.1620 0.7943 0.2715  -0.2028 -0.3453 166 LEU B CD2 
6028  N N   . GLN B 167 ? 2.2475 0.9659 0.8523 0.2909  -0.2484 -0.3102 167 GLN B N   
6029  C CA  . GLN B 167 ? 2.2668 0.9521 0.8978 0.3090  -0.2551 -0.3222 167 GLN B CA  
6030  C C   . GLN B 167 ? 2.2582 0.9724 0.9067 0.3303  -0.2457 -0.3349 167 GLN B C   
6031  O O   . GLN B 167 ? 2.2820 0.9955 0.9531 0.3434  -0.2455 -0.3609 167 GLN B O   
6032  C CB  . GLN B 167 ? 2.2596 0.8965 0.8946 0.3075  -0.2670 -0.2957 167 GLN B CB  
6033  C CG  . GLN B 167 ? 2.2726 0.8751 0.8971 0.2875  -0.2772 -0.2852 167 GLN B CG  
6034  C CD  . GLN B 167 ? 2.3059 0.8670 0.9513 0.2921  -0.2892 -0.2949 167 GLN B CD  
6035  O OE1 . GLN B 167 ? 2.3331 0.8996 0.9916 0.2984  -0.2883 -0.3225 167 GLN B OE1 
6036  N NE2 . GLN B 167 ? 2.3041 0.8264 0.9542 0.2877  -0.2998 -0.2719 167 GLN B NE2 
6037  N N   . VAL B 168 ? 2.2244 0.9653 0.8655 0.3336  -0.2373 -0.3176 168 VAL B N   
6038  C CA  . VAL B 168 ? 2.2119 0.9814 0.8703 0.3533  -0.2278 -0.3266 168 VAL B CA  
6039  C C   . VAL B 168 ? 2.1908 1.0224 0.8367 0.3472  -0.2115 -0.3278 168 VAL B C   
6040  O O   . VAL B 168 ? 2.1597 1.0153 0.7960 0.3317  -0.2070 -0.3004 168 VAL B O   
6041  C CB  . VAL B 168 ? 2.1858 0.9385 0.8577 0.3624  -0.2311 -0.3012 168 VAL B CB  
6042  C CG1 . VAL B 168 ? 2.1751 0.9566 0.8676 0.3837  -0.2218 -0.3126 168 VAL B CG1 
6043  C CG2 . VAL B 168 ? 2.2090 0.8990 0.8882 0.3648  -0.2488 -0.2959 168 VAL B CG2 
6044  N N   . LEU B 169 ? 2.2028 1.0681 0.8597 0.3574  -0.2016 -0.3557 169 LEU B N   
6045  C CA  . LEU B 169 ? 2.1892 1.1158 0.8345 0.3508  -0.1860 -0.3602 169 LEU B CA  
6046  C C   . LEU B 169 ? 2.1813 1.1381 0.8496 0.3700  -0.1744 -0.3755 169 LEU B C   
6047  O O   . LEU B 169 ? 2.2008 1.1383 0.8955 0.3859  -0.1777 -0.3968 169 LEU B O   
6048  C CB  . LEU B 169 ? 2.2175 1.1633 0.8511 0.3356  -0.1841 -0.3830 169 LEU B CB  
6049  C CG  . LEU B 169 ? 2.2106 1.2179 0.8249 0.3202  -0.1714 -0.3847 169 LEU B CG  
6050  C CD1 . LEU B 169 ? 2.2109 1.2648 0.8396 0.3308  -0.1558 -0.4074 169 LEU B CD1 
6051  C CD2 . LEU B 169 ? 2.1751 1.1992 0.7711 0.3085  -0.1703 -0.3468 169 LEU B CD2 
6052  N N   . ASP B 170 ? 2.1588 1.1641 0.8202 0.3681  -0.1608 -0.3637 170 ASP B N   
6053  C CA  . ASP B 170 ? 2.1479 1.1860 0.8314 0.3850  -0.1482 -0.3765 170 ASP B CA  
6054  C C   . ASP B 170 ? 2.1252 1.2259 0.7956 0.3747  -0.1319 -0.3679 170 ASP B C   
6055  O O   . ASP B 170 ? 2.0941 1.2070 0.7536 0.3657  -0.1299 -0.3357 170 ASP B O   
6056  C CB  . ASP B 170 ? 2.1270 1.1376 0.8281 0.4022  -0.1529 -0.3599 170 ASP B CB  
6057  C CG  . ASP B 170 ? 2.1207 1.1583 0.8509 0.4216  -0.1424 -0.3769 170 ASP B CG  
6058  O OD1 . ASP B 170 ? 2.1398 1.2060 0.8810 0.4235  -0.1338 -0.4065 170 ASP B OD1 
6059  O OD2 . ASP B 170 ? 2.0972 1.1283 0.8401 0.4340  -0.1424 -0.3614 170 ASP B OD2 
6060  N N   . LEU B 171 ? 2.1334 1.2765 0.8100 0.3742  -0.1196 -0.3952 171 LEU B N   
6061  C CA  . LEU B 171 ? 2.1153 1.3214 0.7827 0.3647  -0.1033 -0.3894 171 LEU B CA  
6062  C C   . LEU B 171 ? 2.1136 1.3522 0.8068 0.3795  -0.0890 -0.4122 171 LEU B C   
6063  O O   . LEU B 171 ? 2.1170 1.4077 0.8058 0.3703  -0.0747 -0.4245 171 LEU B O   
6064  C CB  . LEU B 171 ? 2.1364 1.3725 0.7792 0.3416  -0.1010 -0.3982 171 LEU B CB  
6065  C CG  . LEU B 171 ? 2.1262 1.3635 0.7409 0.3204  -0.1083 -0.3674 171 LEU B CG  
6066  C CD1 . LEU B 171 ? 2.0867 1.3607 0.6979 0.3159  -0.0996 -0.3332 171 LEU B CD1 
6067  C CD2 . LEU B 171 ? 2.1301 1.3055 0.7407 0.3207  -0.1259 -0.3545 171 LEU B CD2 
6068  N N   . SER B 172 ? 2.1371 1.3466 0.8581 0.4012  -0.0928 -0.4176 172 SER B N   
6069  C CA  . SER B 172 ? 2.1369 1.3734 0.8880 0.4163  -0.0807 -0.4409 172 SER B CA  
6070  C C   . SER B 172 ? 2.1022 1.3901 0.8529 0.4147  -0.0645 -0.4240 172 SER B C   
6071  O O   . SER B 172 ? 2.0747 1.3701 0.8073 0.4060  -0.0641 -0.3909 172 SER B O   
6072  C CB  . SER B 172 ? 2.1390 1.3310 0.9215 0.4393  -0.0913 -0.4457 172 SER B CB  
6073  O OG  . SER B 172 ? 2.1374 1.3569 0.9526 0.4538  -0.0799 -0.4673 172 SER B OG  
6074  N N   . ASN B 173 ? 2.1441 1.4686 0.9175 0.4221  -0.0501 -0.4477 173 ASN B N   
6075  C CA  . ASN B 173 ? 2.1125 1.4849 0.8931 0.4232  -0.0338 -0.4353 173 ASN B CA  
6076  C C   . ASN B 173 ? 2.0991 1.5122 0.8486 0.4005  -0.0258 -0.4127 173 ASN B C   
6077  O O   . ASN B 173 ? 2.0648 1.4954 0.8117 0.3988  -0.0205 -0.3823 173 ASN B O   
6078  C CB  . ASN B 173 ? 2.0798 1.4303 0.8781 0.4403  -0.0380 -0.4116 173 ASN B CB  
6079  C CG  . ASN B 173 ? 2.0677 1.4448 0.9009 0.4560  -0.0259 -0.4261 173 ASN B CG  
6080  O OD1 . ASN B 173 ? 2.0675 1.4945 0.9054 0.4495  -0.0091 -0.4399 173 ASN B OD1 
6081  N ND2 . ASN B 173 ? 2.0582 1.4028 0.9162 0.4755  -0.0348 -0.4223 173 ASN B ND2 
6082  N N   . ASN B 174 ? 2.1167 1.5461 0.8444 0.3821  -0.0250 -0.4270 174 ASN B N   
6083  C CA  . ASN B 174 ? 2.1090 1.5760 0.8069 0.3587  -0.0205 -0.4047 174 ASN B CA  
6084  C C   . ASN B 174 ? 2.1408 1.6502 0.8260 0.3410  -0.0103 -0.4329 174 ASN B C   
6085  O O   . ASN B 174 ? 2.1758 1.6670 0.8612 0.3399  -0.0148 -0.4641 174 ASN B O   
6086  C CB  . ASN B 174 ? 2.1081 1.5388 0.7827 0.3489  -0.0373 -0.3794 174 ASN B CB  
6087  C CG  . ASN B 174 ? 2.0702 1.4790 0.7494 0.3563  -0.0422 -0.3418 174 ASN B CG  
6088  O OD1 . ASN B 174 ? 2.0431 1.4836 0.7160 0.3462  -0.0354 -0.3125 174 ASN B OD1 
6089  N ND2 . ASN B 174 ? 2.0690 1.4243 0.7608 0.3727  -0.0539 -0.3422 174 ASN B ND2 
6090  N N   . PRO B 175 ? 2.1022 1.6678 0.7765 0.3257  0.0036  -0.4227 175 PRO B N   
6091  C CA  . PRO B 175 ? 2.1345 1.7443 0.7929 0.3051  0.0143  -0.4485 175 PRO B CA  
6092  C C   . PRO B 175 ? 2.1549 1.7702 0.7783 0.2807  0.0049  -0.4398 175 PRO B C   
6093  O O   . PRO B 175 ? 2.1489 1.8041 0.7500 0.2600  0.0079  -0.4164 175 PRO B O   
6094  C CB  . PRO B 175 ? 2.1136 1.7785 0.7749 0.2984  0.0318  -0.4354 175 PRO B CB  
6095  C CG  . PRO B 175 ? 2.0710 1.7256 0.7349 0.3048  0.0262  -0.3905 175 PRO B CG  
6096  C CD  . PRO B 175 ? 2.0622 1.6544 0.7427 0.3274  0.0120  -0.3897 175 PRO B CD  
6097  N N   . LEU B 176 ? 2.1813 1.7556 0.8010 0.2824  -0.0076 -0.4584 176 LEU B N   
6098  C CA  . LEU B 176 ? 2.2065 1.7870 0.7956 0.2588  -0.0158 -0.4582 176 LEU B CA  
6099  C C   . LEU B 176 ? 2.2491 1.8590 0.8317 0.2444  -0.0048 -0.5015 176 LEU B C   
6100  O O   . LEU B 176 ? 2.2594 1.8808 0.8633 0.2534  0.0090  -0.5320 176 LEU B O   
6101  C CB  . LEU B 176 ? 2.2117 1.7315 0.7985 0.2652  -0.0353 -0.4526 176 LEU B CB  
6102  C CG  . LEU B 176 ? 2.1781 1.6614 0.7642 0.2725  -0.0489 -0.4107 176 LEU B CG  
6103  C CD1 . LEU B 176 ? 2.1547 1.6771 0.7221 0.2541  -0.0477 -0.3712 176 LEU B CD1 
6104  C CD2 . LEU B 176 ? 2.1516 1.6057 0.7665 0.2991  -0.0477 -0.4050 176 LEU B CD2 
6105  N N   . THR B 177 ? 2.2747 1.8973 0.8286 0.2205  -0.0104 -0.5046 177 THR B N   
6106  C CA  . THR B 177 ? 2.3186 1.9689 0.8615 0.2021  -0.0001 -0.5450 177 THR B CA  
6107  C C   . THR B 177 ? 2.3462 1.9702 0.8731 0.1906  -0.0140 -0.5556 177 THR B C   
6108  O O   . THR B 177 ? 2.3309 1.9279 0.8476 0.1904  -0.0307 -0.5257 177 THR B O   
6109  C CB  . THR B 177 ? 2.3262 2.0431 0.8426 0.1748  0.0129  -0.5371 177 THR B CB  
6110  O OG1 . THR B 177 ? 2.3010 2.0330 0.7966 0.1631  0.0022  -0.4893 177 THR B OG1 
6111  C CG2 . THR B 177 ? 2.3139 2.0580 0.8492 0.1838  0.0318  -0.5442 177 THR B CG2 
6112  N N   . GLY B 178 ? 2.4072 2.0385 0.9330 0.1799  -0.0057 -0.5992 178 GLY B N   
6113  C CA  . GLY B 178 ? 2.4378 2.0469 0.9509 0.1678  -0.0162 -0.6158 178 GLY B CA  
6114  C C   . GLY B 178 ? 2.4502 2.0005 0.9959 0.1906  -0.0214 -0.6437 178 GLY B C   
6115  O O   . GLY B 178 ? 2.4343 1.9590 1.0126 0.2166  -0.0190 -0.6479 178 GLY B O   
6116  N N   . ASP B 179 ? 2.4453 1.9743 0.9829 0.1798  -0.0294 -0.6618 179 ASP B N   
6117  C CA  . ASP B 179 ? 2.4630 1.9361 1.0311 0.1977  -0.0350 -0.6888 179 ASP B CA  
6118  C C   . ASP B 179 ? 2.4389 1.8545 1.0113 0.2133  -0.0566 -0.6562 179 ASP B C   
6119  O O   . ASP B 179 ? 2.4189 1.8378 0.9656 0.2033  -0.0676 -0.6194 179 ASP B O   
6120  C CB  . ASP B 179 ? 2.5108 1.9883 1.0704 0.1771  -0.0307 -0.7279 179 ASP B CB  
6121  C CG  . ASP B 179 ? 2.5414 2.0717 1.0910 0.1571  -0.0078 -0.7605 179 ASP B CG  
6122  O OD1 . ASP B 179 ? 2.5530 2.0791 1.1320 0.1701  0.0065  -0.7893 179 ASP B OD1 
6123  O OD2 . ASP B 179 ? 2.5566 2.1299 1.0674 0.1273  -0.0043 -0.7558 179 ASP B OD2 
6124  N N   . ILE B 180 ? 2.4403 1.8025 1.0466 0.2368  -0.0623 -0.6693 180 ILE B N   
6125  C CA  . ILE B 180 ? 2.4221 1.7243 1.0340 0.2513  -0.0820 -0.6409 180 ILE B CA  
6126  C C   . ILE B 180 ? 2.4436 1.7271 1.0346 0.2329  -0.0937 -0.6412 180 ILE B C   
6127  O O   . ILE B 180 ? 2.4796 1.7500 1.0820 0.2282  -0.0918 -0.6765 180 ILE B O   
6128  C CB  . ILE B 180 ? 2.4261 1.6782 1.0805 0.2790  -0.0856 -0.6560 180 ILE B CB  
6129  C CG1 . ILE B 180 ? 2.3963 1.6610 1.0707 0.2991  -0.0781 -0.6453 180 ILE B CG1 
6130  C CG2 . ILE B 180 ? 2.4207 1.6082 1.0779 0.2876  -0.1063 -0.6336 180 ILE B CG2 
6131  C CD1 . ILE B 180 ? 2.4112 1.7206 1.1033 0.2990  -0.0572 -0.6806 180 ILE B CD1 
6132  N N   . PRO B 181 ? 2.4305 1.7129 0.9937 0.2213  -0.1053 -0.6036 181 PRO B N   
6133  C CA  . PRO B 181 ? 2.4505 1.7179 0.9945 0.2025  -0.1164 -0.6036 181 PRO B CA  
6134  C C   . PRO B 181 ? 2.4564 1.6524 1.0192 0.2163  -0.1312 -0.6021 181 PRO B C   
6135  O O   . PRO B 181 ? 2.4293 1.5889 0.9927 0.2265  -0.1430 -0.5682 181 PRO B O   
6136  C CB  . PRO B 181 ? 2.4225 1.7158 0.9355 0.1871  -0.1230 -0.5603 181 PRO B CB  
6137  C CG  . PRO B 181 ? 2.3826 1.6682 0.9068 0.2065  -0.1223 -0.5303 181 PRO B CG  
6138  C CD  . PRO B 181 ? 2.3882 1.6825 0.9393 0.2247  -0.1083 -0.5594 181 PRO B CD  
6139  N N   . VAL B 182 ? 2.4762 1.6526 1.0554 0.2153  -0.1299 -0.6390 182 VAL B N   
6140  C CA  . VAL B 182 ? 2.4888 1.6019 1.0819 0.2215  -0.1444 -0.6386 182 VAL B CA  
6141  C C   . VAL B 182 ? 2.5062 1.6277 1.0723 0.1953  -0.1503 -0.6388 182 VAL B C   
6142  O O   . VAL B 182 ? 2.5414 1.6756 1.1094 0.1825  -0.1441 -0.6741 182 VAL B O   
6143  C CB  . VAL B 182 ? 2.5179 1.6022 1.1506 0.2369  -0.1398 -0.6764 182 VAL B CB  
6144  C CG1 . VAL B 182 ? 2.5324 1.5527 1.1793 0.2411  -0.1552 -0.6733 182 VAL B CG1 
6145  C CG2 . VAL B 182 ? 2.4993 1.5800 1.1597 0.2623  -0.1345 -0.6745 182 VAL B CG2 
6146  N N   . ASN B 183 ? 2.4816 1.5975 1.0238 0.1864  -0.1620 -0.5996 183 ASN B N   
6147  C CA  . ASN B 183 ? 2.4942 1.6157 1.0125 0.1623  -0.1699 -0.5945 183 ASN B CA  
6148  C C   . ASN B 183 ? 2.4991 1.5560 1.0264 0.1653  -0.1852 -0.5844 183 ASN B C   
6149  O O   . ASN B 183 ? 2.5098 1.5650 1.0207 0.1462  -0.1927 -0.5804 183 ASN B O   
6150  C CB  . ASN B 183 ? 2.4660 1.6283 0.9539 0.1470  -0.1726 -0.5576 183 ASN B CB  
6151  C CG  . ASN B 183 ? 2.4852 1.6819 0.9474 0.1182  -0.1753 -0.5619 183 ASN B CG  
6152  O OD1 . ASN B 183 ? 2.4721 1.6610 0.9191 0.1062  -0.1874 -0.5324 183 ASN B OD1 
6153  N ND2 . ASN B 183 ? 2.5170 1.7537 0.9752 0.1061  -0.1639 -0.5994 183 ASN B ND2 
6154  N N   . GLY B 184 ? 2.4982 1.5039 1.0515 0.1879  -0.1902 -0.5797 184 GLY B N   
6155  C CA  . GLY B 184 ? 2.5009 1.4446 1.0635 0.1910  -0.2048 -0.5660 184 GLY B CA  
6156  C C   . GLY B 184 ? 2.4630 1.3810 1.0203 0.1993  -0.2141 -0.5225 184 GLY B C   
6157  O O   . GLY B 184 ? 2.4425 1.3745 0.9760 0.1849  -0.2188 -0.4942 184 GLY B O   
6158  N N   . SER B 185 ? 2.5374 1.4172 1.1192 0.2217  -0.2170 -0.5180 185 SER B N   
6159  C CA  . SER B 185 ? 2.5034 1.3590 1.0870 0.2341  -0.2231 -0.4828 185 SER B CA  
6160  C C   . SER B 185 ? 2.4947 1.3634 1.0989 0.2564  -0.2143 -0.4926 185 SER B C   
6161  O O   . SER B 185 ? 2.4867 1.3182 1.1107 0.2740  -0.2202 -0.4823 185 SER B O   
6162  C CB  . SER B 185 ? 2.4703 1.3515 1.0260 0.2206  -0.2241 -0.4482 185 SER B CB  
6163  O OG  . SER B 185 ? 2.4710 1.3243 1.0142 0.2044  -0.2355 -0.4304 185 SER B OG  
6164  N N   . PHE B 186 ? 2.3538 1.5954 1.0103 0.2856  -0.1913 -0.5344 186 PHE B N   
6165  C CA  . PHE B 186 ? 2.3523 1.5810 1.0087 0.3133  -0.1684 -0.5257 186 PHE B CA  
6166  C C   . PHE B 186 ? 2.3760 1.5624 1.0252 0.3164  -0.1981 -0.5356 186 PHE B C   
6167  O O   . PHE B 186 ? 2.3765 1.5499 1.0272 0.3372  -0.1833 -0.5305 186 PHE B O   
6168  C CB  . PHE B 186 ? 2.3532 1.6150 1.0009 0.3667  -0.1358 -0.5163 186 PHE B CB  
6169  C CG  . PHE B 186 ? 2.3320 1.6384 1.0137 0.3655  -0.0946 -0.4947 186 PHE B CG  
6170  C CD1 . PHE B 186 ? 2.3213 1.6549 1.0226 0.3364  -0.0979 -0.4938 186 PHE B CD1 
6171  C CD2 . PHE B 186 ? 2.3245 1.6491 1.0299 0.3921  -0.0521 -0.4744 186 PHE B CD2 
6172  C CE1 . PHE B 186 ? 2.3056 1.6823 1.0510 0.3350  -0.0607 -0.4744 186 PHE B CE1 
6173  C CE2 . PHE B 186 ? 2.3094 1.6754 1.0616 0.3897  -0.0144 -0.4533 186 PHE B CE2 
6174  C CZ  . PHE B 186 ? 2.3010 1.6924 1.0740 0.3617  -0.0192 -0.4541 186 PHE B CZ  
6175  N N   . SER B 187 ? 2.3469 1.5112 0.9922 0.2970  -0.2394 -0.5507 187 SER B N   
6176  C CA  . SER B 187 ? 2.3876 1.5069 1.0305 0.3004  -0.2707 -0.5629 187 SER B CA  
6177  C C   . SER B 187 ? 2.3813 1.4618 1.0302 0.2708  -0.2764 -0.5541 187 SER B C   
6178  O O   . SER B 187 ? 2.4076 1.4525 1.0555 0.2841  -0.2900 -0.5591 187 SER B O   
6179  C CB  . SER B 187 ? 2.4265 1.5299 1.0707 0.2839  -0.3133 -0.5823 187 SER B CB  
6180  O OG  . SER B 187 ? 2.4113 1.5178 1.0632 0.2364  -0.3242 -0.5779 187 SER B OG  
6181  N N   . LEU B 188 ? 2.3545 1.4446 1.0099 0.2313  -0.2673 -0.5422 188 LEU B N   
6182  C CA  . LEU B 188 ? 2.3395 1.4149 1.0184 0.1953  -0.2710 -0.5251 188 LEU B CA  
6183  C C   . LEU B 188 ? 2.3028 1.3964 0.9975 0.2126  -0.2327 -0.5120 188 LEU B C   
6184  O O   . LEU B 188 ? 2.2926 1.3772 1.0050 0.1892  -0.2353 -0.4996 188 LEU B O   
6185  C CB  . LEU B 188 ? 2.3094 1.4133 1.0126 0.1390  -0.2740 -0.5109 188 LEU B CB  
6186  C CG  . LEU B 188 ? 2.3385 1.4314 1.0365 0.1098  -0.3099 -0.5197 188 LEU B CG  
6187  C CD1 . LEU B 188 ? 2.3289 1.4563 1.0176 0.1262  -0.2991 -0.5329 188 LEU B CD1 
6188  C CD2 . LEU B 188 ? 2.3196 1.4288 1.0435 0.0496  -0.3187 -0.4998 188 LEU B CD2 
6189  N N   . PHE B 189 ? 2.2961 1.4174 0.9876 0.2525  -0.1977 -0.5130 189 PHE B N   
6190  C CA  . PHE B 189 ? 2.2561 1.4012 0.9732 0.2651  -0.1573 -0.4998 189 PHE B CA  
6191  C C   . PHE B 189 ? 2.2846 1.3988 0.9861 0.3052  -0.1570 -0.5066 189 PHE B C   
6192  O O   . PHE B 189 ? 2.3324 1.4176 1.0029 0.3341  -0.1803 -0.5231 189 PHE B O   
6193  C CB  . PHE B 189 ? 2.2220 1.4166 0.9561 0.2835  -0.1158 -0.4919 189 PHE B CB  
6194  C CG  . PHE B 189 ? 2.1945 1.4263 0.9557 0.2434  -0.1101 -0.4859 189 PHE B CG  
6195  C CD1 . PHE B 189 ? 2.2057 1.4416 0.9489 0.2345  -0.1311 -0.4938 189 PHE B CD1 
6196  C CD2 . PHE B 189 ? 2.1575 1.4240 0.9650 0.2143  -0.0849 -0.4761 189 PHE B CD2 
6197  C CE1 . PHE B 189 ? 2.1804 1.4535 0.9507 0.1977  -0.1258 -0.4901 189 PHE B CE1 
6198  C CE2 . PHE B 189 ? 2.1322 1.4381 0.9673 0.1778  -0.0800 -0.4747 189 PHE B CE2 
6199  C CZ  . PHE B 189 ? 2.1438 1.4523 0.9599 0.1694  -0.1001 -0.4808 189 PHE B CZ  
6200  N N   . THR B 190 ? 2.3374 1.4639 1.0667 0.3063  -0.1298 -0.4958 190 THR B N   
6201  C CA  . THR B 190 ? 2.3492 1.4527 1.0771 0.3335  -0.1259 -0.4990 190 THR B CA  
6202  C C   . THR B 190 ? 2.3274 1.4616 1.0663 0.3755  -0.0799 -0.4940 190 THR B C   
6203  O O   . THR B 190 ? 2.2988 1.4754 1.0661 0.3708  -0.0456 -0.4816 190 THR B O   
6204  C CB  . THR B 190 ? 2.3474 1.4496 1.1049 0.2977  -0.1294 -0.4889 190 THR B CB  
6205  O OG1 . THR B 190 ? 2.3766 1.4504 1.1241 0.2598  -0.1726 -0.4878 190 THR B OG1 
6206  C CG2 . THR B 190 ? 2.3589 1.4410 1.1204 0.3247  -0.1244 -0.4922 190 THR B CG2 
6207  N N   . PRO B 191 ? 2.3029 1.4212 1.0276 0.4161  -0.0775 -0.5014 191 PRO B N   
6208  C CA  . PRO B 191 ? 2.2825 1.4375 1.0259 0.4538  -0.0320 -0.4900 191 PRO B CA  
6209  C C   . PRO B 191 ? 2.2466 1.4279 1.0355 0.4426  0.0086  -0.4776 191 PRO B C   
6210  O O   . PRO B 191 ? 2.2316 1.4426 1.0409 0.4716  0.0495  -0.4662 191 PRO B O   
6211  C CB  . PRO B 191 ? 2.3016 1.4424 1.0402 0.4849  -0.0433 -0.4970 191 PRO B CB  
6212  C CG  . PRO B 191 ? 2.3323 1.4236 1.0553 0.4620  -0.0936 -0.5127 191 PRO B CG  
6213  C CD  . PRO B 191 ? 2.3377 1.4205 1.0448 0.4282  -0.1161 -0.5148 191 PRO B CD  
6214  N N   . ILE B 192 ? 2.2249 1.4062 1.0422 0.3992  -0.0006 -0.4760 192 ILE B N   
6215  C CA  . ILE B 192 ? 2.1900 1.4113 1.0659 0.3839  0.0376  -0.4662 192 ILE B CA  
6216  C C   . ILE B 192 ? 2.1665 1.4288 1.0706 0.3753  0.0649  -0.4558 192 ILE B C   
6217  O O   . ILE B 192 ? 2.1396 1.4376 1.0963 0.3807  0.1062  -0.4473 192 ILE B O   
6218  C CB  . ILE B 192 ? 2.1882 1.4083 1.0841 0.3404  0.0185  -0.4693 192 ILE B CB  
6219  C CG1 . ILE B 192 ? 2.2195 1.3966 1.0907 0.3515  -0.0102 -0.4768 192 ILE B CG1 
6220  C CG2 . ILE B 192 ? 2.1510 1.4191 1.1115 0.3258  0.0567  -0.4663 192 ILE B CG2 
6221  C CD1 . ILE B 192 ? 2.2250 1.4062 1.1168 0.3138  -0.0270 -0.4750 192 ILE B CD1 
6222  N N   . SER B 193 ? 2.1479 1.4059 1.0230 0.3629  0.0423  -0.4571 193 SER B N   
6223  C CA  . SER B 193 ? 2.1275 1.4232 1.0275 0.3582  0.0652  -0.4477 193 SER B CA  
6224  C C   . SER B 193 ? 2.1338 1.4457 1.0354 0.4060  0.0988  -0.4339 193 SER B C   
6225  O O   . SER B 193 ? 2.1135 1.4617 1.0573 0.4070  0.1303  -0.4203 193 SER B O   
6226  C CB  . SER B 193 ? 2.1428 1.4294 1.0082 0.3357  0.0301  -0.4539 193 SER B CB  
6227  O OG  . SER B 193 ? 2.1393 1.4163 1.0065 0.2893  0.0011  -0.4612 193 SER B OG  
6228  N N   . PHE B 194 ? 2.1721 1.4613 1.0316 0.4461  0.0927  -0.4363 194 PHE B N   
6229  C CA  . PHE B 194 ? 2.1858 1.4957 1.0372 0.4940  0.1219  -0.4208 194 PHE B CA  
6230  C C   . PHE B 194 ? 2.1854 1.4952 1.0506 0.5254  0.1487  -0.4158 194 PHE B C   
6231  O O   . PHE B 194 ? 2.2072 1.5286 1.0494 0.5696  0.1646  -0.4062 194 PHE B O   
6232  C CB  . PHE B 194 ? 2.2258 1.5229 1.0095 0.5195  0.0917  -0.4303 194 PHE B CB  
6233  C CG  . PHE B 194 ? 2.2279 1.5274 0.9979 0.4920  0.0657  -0.4360 194 PHE B CG  
6234  C CD1 . PHE B 194 ? 2.2325 1.4995 0.9839 0.4550  0.0225  -0.4560 194 PHE B CD1 
6235  C CD2 . PHE B 194 ? 2.2283 1.5640 1.0065 0.5035  0.0841  -0.4195 194 PHE B CD2 
6236  C CE1 . PHE B 194 ? 2.2337 1.5052 0.9754 0.4287  -0.0005 -0.4613 194 PHE B CE1 
6237  C CE2 . PHE B 194 ? 2.2300 1.5702 0.9973 0.4787  0.0599  -0.4266 194 PHE B CE2 
6238  C CZ  . PHE B 194 ? 2.2309 1.5395 0.9799 0.4408  0.0180  -0.4486 194 PHE B CZ  
6239  N N   . ALA B 195 ? 2.1865 1.4886 1.0889 0.5042  0.1540  -0.4223 195 ALA B N   
6240  C CA  . ALA B 195 ? 2.1805 1.4834 1.1004 0.5319  0.1785  -0.4200 195 ALA B CA  
6241  C C   . ALA B 195 ? 2.1607 1.5050 1.1388 0.5510  0.2331  -0.3945 195 ALA B C   
6242  O O   . ALA B 195 ? 2.1418 1.5122 1.1693 0.5302  0.2529  -0.3830 195 ALA B O   
6243  C CB  . ALA B 195 ? 2.1654 1.4524 1.1112 0.5027  0.1667  -0.4349 195 ALA B CB  
6244  N N   . ASN B 196 ? 2.1161 1.4673 1.0921 0.5913  0.2575  -0.3856 196 ASN B N   
6245  C CA  . ASN B 196 ? 2.0988 1.4876 1.1347 0.6126  0.3114  -0.3575 196 ASN B CA  
6246  C C   . ASN B 196 ? 2.1062 1.5237 1.1498 0.6221  0.3293  -0.3303 196 ASN B C   
6247  O O   . ASN B 196 ? 2.0822 1.5289 1.1976 0.6193  0.3689  -0.3073 196 ASN B O   
6248  C CB  . ASN B 196 ? 2.0534 1.4547 1.1744 0.5834  0.3362  -0.3608 196 ASN B CB  
6249  C CG  . ASN B 196 ? 2.0385 1.4677 1.2207 0.6104  0.3879  -0.3390 196 ASN B CG  
6250  O OD1 . ASN B 196 ? 2.0577 1.4947 1.2186 0.6431  0.3955  -0.3261 196 ASN B OD1 
6251  N ND2 . ASN B 196 ? 1.9987 1.4527 1.2712 0.5893  0.4198  -0.3328 196 ASN B ND2 
6252  N N   . THR B 197 ? 2.1341 1.5444 1.1085 0.6338  0.2996  -0.3337 197 THR B N   
6253  C CA  . THR B 197 ? 2.1456 1.5829 1.1207 0.6413  0.3092  -0.3105 197 THR B CA  
6254  C C   . THR B 197 ? 2.1841 1.6498 1.1220 0.6940  0.3276  -0.2849 197 THR B C   
6255  O O   . THR B 197 ? 2.1962 1.6925 1.1443 0.7063  0.3441  -0.2568 197 THR B O   
6256  C CB  . THR B 197 ? 2.1555 1.5735 1.0848 0.6140  0.2626  -0.3324 197 THR B CB  
6257  O OG1 . THR B 197 ? 2.1274 1.5193 1.0764 0.5680  0.2403  -0.3575 197 THR B OG1 
6258  C CG2 . THR B 197 ? 2.1538 1.6006 1.1084 0.6071  0.2740  -0.3120 197 THR B CG2 
6259  N N   . LYS B 198 ? 2.1850 1.6462 1.0823 0.7261  0.3257  -0.2931 198 LYS B N   
6260  C CA  . LYS B 198 ? 2.2302 1.7281 1.0889 0.7766  0.3414  -0.2707 198 LYS B CA  
6261  C C   . LYS B 198 ? 2.2673 1.7767 1.0601 0.7900  0.3110  -0.2757 198 LYS B C   
6262  O O   . LYS B 198 ? 2.2956 1.8486 1.0680 0.8275  0.3309  -0.2469 198 LYS B O   
6263  C CB  . LYS B 198 ? 2.2148 1.7546 1.1360 0.7980  0.4004  -0.2221 198 LYS B CB  
6264  C CG  . LYS B 198 ? 2.1722 1.7039 1.1741 0.7806  0.4328  -0.2182 198 LYS B CG  
6265  C CD  . LYS B 198 ? 2.1502 1.7199 1.2344 0.7906  0.4878  -0.1692 198 LYS B CD  
6266  C CE  . LYS B 198 ? 2.1020 1.6633 1.2785 0.7663  0.5166  -0.1725 198 LYS B CE  
6267  N NZ  . LYS B 198 ? 2.0809 1.6761 1.3509 0.7739  0.5698  -0.1261 198 LYS B NZ  
6268  N N   . LEU B 199 ? 2.2939 1.7680 1.0565 0.7584  0.2622  -0.3108 199 LEU B N   
6269  C CA  . LEU B 199 ? 2.3220 1.8063 1.0300 0.7654  0.2282  -0.3208 199 LEU B CA  
6270  C C   . LEU B 199 ? 2.3561 1.8607 1.0203 0.7939  0.2021  -0.3324 199 LEU B C   
6271  O O   . LEU B 199 ? 2.3894 1.9406 1.0236 0.8302  0.2093  -0.3153 199 LEU B O   
6272  C CB  . LEU B 199 ? 2.3068 1.7482 1.0073 0.7188  0.1857  -0.3530 199 LEU B CB  
6273  C CG  . LEU B 199 ? 2.2796 1.7238 1.0310 0.6826  0.1992  -0.3385 199 LEU B CG  
6274  C CD1 . LEU B 199 ? 2.2697 1.6799 1.0056 0.6383  0.1536  -0.3695 199 LEU B CD1 
6275  C CD2 . LEU B 199 ? 2.2975 1.7891 1.0557 0.7067  0.2230  -0.3044 199 LEU B CD2 
6276  N N   . THR B 200 ? 2.3606 1.8347 1.0239 0.7793  0.1722  -0.3614 200 THR B N   
6277  C CA  . THR B 200 ? 2.4060 1.8977 1.0367 0.8046  0.1459  -0.3791 200 THR B CA  
6278  C C   . THR B 200 ? 2.4045 1.8886 1.0576 0.8112  0.1559  -0.3837 200 THR B C   
6279  O O   . THR B 200 ? 2.3730 1.8560 1.0655 0.8083  0.1941  -0.3630 200 THR B O   
6280  C CB  . THR B 200 ? 2.4264 1.8880 1.0325 0.7817  0.0880  -0.4181 200 THR B CB  
6281  O OG1 . THR B 200 ? 2.4264 1.8971 1.0149 0.7731  0.0777  -0.4153 200 THR B OG1 
6282  C CG2 . THR B 200 ? 2.4754 1.9609 1.0556 0.8109  0.0628  -0.4397 200 THR B CG2 
6283  N N   . GLU C 1   ? 0.7539 0.3549 0.8766 0.0389  0.2313  0.0078  1   GLU C N   
6284  C CA  . GLU C 1   ? 0.7914 0.3327 0.8953 0.0292  0.2220  -0.0111 1   GLU C CA  
6285  C C   . GLU C 1   ? 0.7855 0.3183 0.8605 0.0605  0.2193  -0.0183 1   GLU C C   
6286  O O   . GLU C 1   ? 0.7531 0.3313 0.8254 0.0854  0.2232  -0.0052 1   GLU C O   
6287  C CB  . GLU C 1   ? 0.7669 0.3324 0.8990 -0.0026 0.2020  -0.0312 1   GLU C CB  
6288  C CG  . GLU C 1   ? 0.7480 0.3623 0.9214 -0.0256 0.2042  -0.0187 1   GLU C CG  
6289  C CD  . GLU C 1   ? 0.8006 0.3809 0.9712 -0.0405 0.2200  0.0034  1   GLU C CD  
6290  O OE1 . GLU C 1   ? 0.8595 0.3857 1.0177 -0.0720 0.2161  0.0010  1   GLU C OE1 
6291  O OE2 . GLU C 1   ? 0.7898 0.3947 0.9654 -0.0242 0.2361  0.0236  1   GLU C OE2 
6292  N N   . SER C 2   ? 0.8216 0.3001 0.8723 0.0562  0.2124  -0.0373 2   SER C N   
6293  C CA  . SER C 2   ? 0.8194 0.2923 0.8432 0.0870  0.2111  -0.0431 2   SER C CA  
6294  C C   . SER C 2   ? 0.8367 0.2824 0.8441 0.0679  0.1909  -0.0709 2   SER C C   
6295  O O   . SER C 2   ? 0.8866 0.2850 0.8826 0.0360  0.1856  -0.0809 2   SER C O   
6296  C CB  . SER C 2   ? 0.8768 0.3112 0.8629 0.1220  0.2330  -0.0188 2   SER C CB  
6297  O OG  . SER C 2   ? 0.8472 0.3333 0.8478 0.1466  0.2468  0.0110  2   SER C OG  
6298  N N   . SER C 3   ? 0.7980 0.2803 0.8018 0.0841  0.1776  -0.0806 3   SER C N   
6299  C CA  . SER C 3   ? 0.8110 0.2789 0.7961 0.0719  0.1570  -0.1033 3   SER C CA  
6300  C C   . SER C 3   ? 0.7722 0.2826 0.7509 0.1012  0.1504  -0.1030 3   SER C C   
6301  O O   . SER C 3   ? 0.7253 0.2842 0.7214 0.1195  0.1567  -0.0899 3   SER C O   
6302  C CB  . SER C 3   ? 0.7835 0.2691 0.8008 0.0336  0.1396  -0.1224 3   SER C CB  
6303  O OG  . SER C 3   ? 0.7112 0.2610 0.7732 0.0368  0.1389  -0.1199 3   SER C OG  
6304  N N   . SER C 4   ? 0.7981 0.2886 0.7501 0.1028  0.1388  -0.1169 4   SER C N   
6305  C CA  . SER C 4   ? 0.7646 0.2956 0.7126 0.1273  0.1328  -0.1165 4   SER C CA  
6306  C C   . SER C 4   ? 0.7005 0.2791 0.6764 0.1104  0.1112  -0.1325 4   SER C C   
6307  O O   . SER C 4   ? 0.6857 0.2669 0.6840 0.0820  0.1023  -0.1429 4   SER C O   
6308  C CB  . SER C 4   ? 0.8224 0.3137 0.7314 0.1385  0.1339  -0.1235 4   SER C CB  
6309  O OG  . SER C 4   ? 0.8504 0.3073 0.7492 0.1063  0.1165  -0.1485 4   SER C OG  
6310  N N   . SER C 5   ? 0.6667 0.2848 0.6417 0.1287  0.1060  -0.1312 5   SER C N   
6311  C CA  . SER C 5   ? 0.6165 0.2732 0.6091 0.1160  0.0871  -0.1447 5   SER C CA  
6312  C C   . SER C 5   ? 0.6358 0.2778 0.6077 0.1144  0.0721  -0.1605 5   SER C C   
6313  O O   . SER C 5   ? 0.6677 0.2952 0.6195 0.1331  0.0804  -0.1582 5   SER C O   
6314  C CB  . SER C 5   ? 0.5729 0.2787 0.5746 0.1320  0.0925  -0.1336 5   SER C CB  
6315  O OG  . SER C 5   ? 0.5922 0.3048 0.5702 0.1636  0.1048  -0.1164 5   SER C OG  
6316  N N   . HIS C 6   ? 0.6228 0.2714 0.6014 0.0906  0.0568  -0.1726 6   HIS C N   
6317  C CA  . HIS C 6   ? 0.6471 0.2779 0.5999 0.0833  0.0453  -0.1861 6   HIS C CA  
6318  C C   . HIS C 6   ? 0.5950 0.2774 0.5620 0.0879  0.0403  -0.1841 6   HIS C C   
6319  O O   . HIS C 6   ? 0.5472 0.2719 0.5511 0.0757  0.0296  -0.1846 6   HIS C O   
6320  C CB  . HIS C 6   ? 0.6669 0.2812 0.6318 0.0457  0.0344  -0.2007 6   HIS C CB  
6321  C CG  . HIS C 6   ? 0.7088 0.2961 0.6391 0.0327  0.0227  -0.2166 6   HIS C CG  
6322  N ND1 . HIS C 6   ? 0.6736 0.3018 0.6138 0.0324  0.0129  -0.2216 6   HIS C ND1 
6323  C CD2 . HIS C 6   ? 0.7830 0.3131 0.6769 0.0192  0.0148  -0.2309 6   HIS C CD2 
6324  C CE1 . HIS C 6   ? 0.7277 0.3200 0.6284 0.0168  0.0060  -0.2365 6   HIS C CE1 
6325  N NE2 . HIS C 6   ? 0.7976 0.3286 0.6669 0.0101  0.0025  -0.2426 6   HIS C NE2 
6326  N N   . SER C 7   ? 0.6027 0.2852 0.5485 0.1062  0.0496  -0.1823 7   SER C N   
6327  C CA  . SER C 7   ? 0.5594 0.2922 0.5185 0.1094  0.0346  -0.1834 7   SER C CA  
6328  C C   . SER C 7   ? 0.5559 0.2932 0.5217 0.0860  0.0147  -0.1978 7   SER C C   
6329  O O   . SER C 7   ? 0.6012 0.3044 0.5396 0.0779  0.0140  -0.2098 7   SER C O   
6330  C CB  . SER C 7   ? 0.5761 0.3153 0.5144 0.1364  0.0433  -0.1788 7   SER C CB  
6331  O OG  . SER C 7   ? 0.5383 0.3254 0.4815 0.1425  0.0268  -0.1774 7   SER C OG  
6332  N N   . GLU C 8   ? 0.5323 0.3098 0.5335 0.0753  0.0006  -0.1976 8   GLU C N   
6333  C CA  . GLU C 8   ? 0.5305 0.3230 0.5510 0.0576  -0.0176 -0.2103 8   GLU C CA  
6334  C C   . GLU C 8   ? 0.5246 0.3366 0.5317 0.0647  -0.0291 -0.2144 8   GLU C C   
6335  O O   . GLU C 8   ? 0.5046 0.3371 0.5054 0.0809  -0.0270 -0.2057 8   GLU C O   
6336  C CB  . GLU C 8   ? 0.5016 0.3253 0.5662 0.0519  -0.0220 -0.2076 8   GLU C CB  
6337  C CG  . GLU C 8   ? 0.5092 0.3196 0.5921 0.0461  -0.0097 -0.2037 8   GLU C CG  
6338  C CD  . GLU C 8   ? 0.5540 0.3393 0.6446 0.0238  -0.0138 -0.2168 8   GLU C CD  
6339  O OE1 . GLU C 8   ? 0.5899 0.3325 0.6392 0.0203  -0.0093 -0.2196 8   GLU C OE1 
6340  O OE2 . GLU C 8   ? 0.5666 0.3820 0.6936 0.0071  -0.0189 -0.2103 8   GLU C OE2 
6341  N N   . ARG C 9   ? 0.5280 0.3353 0.5294 0.0498  -0.0432 -0.2294 9   ARG C N   
6342  C CA  . ARG C 9   ? 0.5290 0.3534 0.5143 0.0549  -0.0553 -0.2352 9   ARG C CA  
6343  C C   . ARG C 9   ? 0.4783 0.3493 0.4913 0.0652  -0.0647 -0.2278 9   ARG C C   
6344  O O   . ARG C 9   ? 0.4563 0.3419 0.5013 0.0635  -0.0641 -0.2225 9   ARG C O   
6345  C CB  . ARG C 9   ? 0.5626 0.3822 0.5408 0.0290  -0.0733 -0.2528 9   ARG C CB  
6346  C CG  . ARG C 9   ? 0.6294 0.4016 0.5466 0.0259  -0.0664 -0.2626 9   ARG C CG  
6347  C CD  . ARG C 9   ? 0.6868 0.4323 0.5830 -0.0137 -0.0792 -0.2790 9   ARG C CD  
6348  N NE  . ARG C 9   ? 0.7252 0.4218 0.6111 -0.0296 -0.0668 -0.2802 9   ARG C NE  
6349  C CZ  . ARG C 9   ? 0.7673 0.4497 0.6489 -0.0721 -0.0808 -0.2901 9   ARG C CZ  
6350  N NH1 . ARG C 9   ? 0.7744 0.4963 0.6641 -0.1051 -0.1084 -0.2975 9   ARG C NH1 
6351  N NH2 . ARG C 9   ? 0.8056 0.4388 0.6746 -0.0850 -0.0689 -0.2892 9   ARG C NH2 
6352  N N   . ALA C 10  ? 0.5025 0.3905 0.4977 0.0764  -0.0716 -0.2281 10  ALA C N   
6353  C CA  . ALA C 10  ? 0.4794 0.4033 0.4899 0.0826  -0.0797 -0.2191 10  ALA C CA  
6354  C C   . ALA C 10  ? 0.4834 0.4336 0.5229 0.0693  -0.0936 -0.2166 10  ALA C C   
6355  O O   . ALA C 10  ? 0.4968 0.4470 0.5500 0.0540  -0.0993 -0.2225 10  ALA C O   
6356  C CB  . ALA C 10  ? 0.4944 0.4353 0.4772 0.0968  -0.0821 -0.2148 10  ALA C CB  
6357  N N   . GLY C 11  ? 0.4363 0.4118 0.4844 0.0740  -0.0988 -0.2039 11  GLY C N   
6358  C CA  . GLY C 11  ? 0.4444 0.4459 0.5235 0.0696  -0.1058 -0.1936 11  GLY C CA  
6359  C C   . GLY C 11  ? 0.4432 0.4761 0.5223 0.0613  -0.1243 -0.1961 11  GLY C C   
6360  O O   . GLY C 11  ? 0.4555 0.4794 0.5178 0.0487  -0.1307 -0.2115 11  GLY C O   
6361  N N   . GLY C 12  ? 0.4300 0.4946 0.5218 0.0664  -0.1319 -0.1809 12  GLY C N   
6362  C CA  . GLY C 12  ? 0.4365 0.5401 0.5293 0.0575  -0.1508 -0.1795 12  GLY C CA  
6363  C C   . GLY C 12  ? 0.4244 0.5663 0.5453 0.0670  -0.1542 -0.1539 12  GLY C C   
6364  O O   . GLY C 12  ? 0.4254 0.5606 0.5687 0.0798  -0.1399 -0.1378 12  GLY C O   
6365  N N   . ARG C 13  ? 0.4462 0.6247 0.5610 0.0634  -0.1707 -0.1490 13  ARG C N   
6366  C CA  . ARG C 13  ? 0.4399 0.6537 0.5766 0.0765  -0.1728 -0.1212 13  ARG C CA  
6367  C C   . ARG C 13  ? 0.4432 0.7218 0.6170 0.0675  -0.1859 -0.1031 13  ARG C C   
6368  O O   . ARG C 13  ? 0.4392 0.7441 0.6498 0.0838  -0.1765 -0.0743 13  ARG C O   
6369  C CB  . ARG C 13  ? 0.4422 0.6632 0.5504 0.0798  -0.1821 -0.1204 13  ARG C CB  
6370  C CG  . ARG C 13  ? 0.4427 0.6823 0.5647 0.0958  -0.1797 -0.0906 13  ARG C CG  
6371  C CD  . ARG C 13  ? 0.4703 0.6526 0.5809 0.1090  -0.1578 -0.0834 13  ARG C CD  
6372  N NE  . ARG C 13  ? 0.4976 0.6762 0.6000 0.1209  -0.1543 -0.0592 13  ARG C NE  
6373  C CZ  . ARG C 13  ? 0.4983 0.6686 0.5693 0.1145  -0.1605 -0.0591 13  ARG C CZ  
6374  N NH1 . ARG C 13  ? 0.4668 0.6381 0.5141 0.1013  -0.1684 -0.0793 13  ARG C NH1 
6375  N NH2 . ARG C 13  ? 0.5340 0.6965 0.5966 0.1234  -0.1566 -0.0347 13  ARG C NH2 
6376  N N   . THR D 47  ? 0.3572 0.2926 0.6318 0.0076  -0.1813 -0.0794 47  THR D N   
6377  C CA  . THR D 47  ? 0.3723 0.3159 0.6573 -0.0013 -0.1939 -0.0742 47  THR D CA  
6378  C C   . THR D 47  ? 0.3514 0.3318 0.6757 -0.0042 -0.1856 -0.0673 47  THR D C   
6379  O O   . THR D 47  ? 0.3252 0.3237 0.6652 0.0031  -0.1699 -0.0668 47  THR D O   
6380  C CB  . THR D 47  ? 0.3875 0.3164 0.6495 0.0074  -0.2068 -0.0781 47  THR D CB  
6381  O OG1 . THR D 47  ? 0.3666 0.3155 0.6442 0.0176  -0.2020 -0.0778 47  THR D OG1 
6382  C CG2 . THR D 47  ? 0.4008 0.2987 0.6217 0.0169  -0.2069 -0.0855 47  THR D CG2 
6383  N N   . VAL D 48  ? 0.3566 0.3472 0.6936 -0.0143 -0.1944 -0.0619 48  VAL D N   
6384  C CA  . VAL D 48  ? 0.3422 0.3658 0.7115 -0.0160 -0.1860 -0.0556 48  VAL D CA  
6385  C C   . VAL D 48  ? 0.3315 0.3621 0.6998 -0.0022 -0.1842 -0.0565 48  VAL D C   
6386  O O   . VAL D 48  ? 0.3127 0.3651 0.6978 0.0026  -0.1694 -0.0534 48  VAL D O   
6387  C CB  . VAL D 48  ? 0.3628 0.3947 0.7448 -0.0307 -0.1966 -0.0506 48  VAL D CB  
6388  C CG1 . VAL D 48  ? 0.3492 0.4158 0.7644 -0.0335 -0.1853 -0.0450 48  VAL D CG1 
6389  C CG2 . VAL D 48  ? 0.3808 0.3972 0.7531 -0.0450 -0.2002 -0.0503 48  VAL D CG2 
6390  N N   . GLU D 49  ? 0.3907 0.4005 0.7347 0.0039  -0.1982 -0.0606 49  GLU D N   
6391  C CA  . GLU D 49  ? 0.3845 0.3977 0.7226 0.0157  -0.1967 -0.0612 49  GLU D CA  
6392  C C   . GLU D 49  ? 0.3619 0.3749 0.6914 0.0276  -0.1795 -0.0647 49  GLU D C   
6393  O O   . GLU D 49  ? 0.3498 0.3754 0.6820 0.0340  -0.1684 -0.0624 49  GLU D O   
6394  C CB  . GLU D 49  ? 0.4097 0.3989 0.7202 0.0182  -0.2155 -0.0648 49  GLU D CB  
6395  C CG  . GLU D 49  ? 0.4361 0.4215 0.7489 0.0058  -0.2322 -0.0616 49  GLU D CG  
6396  C CD  . GLU D 49  ? 0.4546 0.4175 0.7492 -0.0027 -0.2393 -0.0646 49  GLU D CD  
6397  O OE1 . GLU D 49  ? 0.4574 0.3973 0.7245 0.0040  -0.2381 -0.0710 49  GLU D OE1 
6398  O OE2 . GLU D 49  ? 0.4682 0.4358 0.7743 -0.0161 -0.2451 -0.0606 49  GLU D OE2 
6399  N N   . GLU D 50  ? 0.3476 0.3452 0.6636 0.0299  -0.1767 -0.0703 50  GLU D N   
6400  C CA  . GLU D 50  ? 0.3292 0.3273 0.6357 0.0397  -0.1582 -0.0735 50  GLU D CA  
6401  C C   . GLU D 50  ? 0.3068 0.3296 0.6351 0.0364  -0.1380 -0.0674 50  GLU D C   
6402  O O   . GLU D 50  ? 0.2938 0.3257 0.6144 0.0416  -0.1221 -0.0653 50  GLU D O   
6403  C CB  . GLU D 50  ? 0.3396 0.3162 0.6285 0.0427  -0.1609 -0.0810 50  GLU D CB  
6404  C CG  . GLU D 50  ? 0.3528 0.3021 0.6083 0.0506  -0.1745 -0.0891 50  GLU D CG  
6405  C CD  . GLU D 50  ? 0.3611 0.2847 0.5914 0.0510  -0.1753 -0.0949 50  GLU D CD  
6406  O OE1 . GLU D 50  ? 0.3599 0.2835 0.6006 0.0422  -0.1707 -0.0926 50  GLU D OE1 
6407  O OE2 . GLU D 50  ? 0.3732 0.2845 0.5650 0.0568  -0.1740 -0.0972 50  GLU D OE2 
6408  N N   . ALA D 51  ? 0.3123 0.3451 0.6630 0.0262  -0.1380 -0.0639 51  ALA D N   
6409  C CA  . ALA D 51  ? 0.2952 0.3494 0.6633 0.0230  -0.1188 -0.0588 51  ALA D CA  
6410  C C   . ALA D 51  ? 0.2924 0.3665 0.6706 0.0241  -0.1130 -0.0533 51  ALA D C   
6411  O O   . ALA D 51  ? 0.2795 0.3640 0.6542 0.0277  -0.0957 -0.0508 51  ALA D O   
6412  C CB  . ALA D 51  ? 0.3005 0.3612 0.6881 0.0097  -0.1210 -0.0560 51  ALA D CB  
6413  N N   . ASN D 52  ? 0.2655 0.3436 0.6533 0.0205  -0.1284 -0.0513 52  ASN D N   
6414  C CA  . ASN D 52  ? 0.2649 0.3609 0.6629 0.0225  -0.1253 -0.0467 52  ASN D CA  
6415  C C   . ASN D 52  ? 0.2580 0.3478 0.6341 0.0335  -0.1184 -0.0478 52  ASN D C   
6416  O O   . ASN D 52  ? 0.2510 0.3546 0.6296 0.0365  -0.1075 -0.0440 52  ASN D O   
6417  C CB  . ASN D 52  ? 0.2842 0.3831 0.6939 0.0168  -0.1449 -0.0449 52  ASN D CB  
6418  C CG  . ASN D 52  ? 0.2905 0.4065 0.7257 0.0041  -0.1466 -0.0413 52  ASN D CG  
6419  O OD1 . ASN D 52  ? 0.2828 0.4209 0.7355 0.0022  -0.1344 -0.0381 52  ASN D OD1 
6420  N ND2 . ASN D 52  ? 0.3070 0.4122 0.7413 -0.0055 -0.1618 -0.0422 52  ASN D ND2 
6421  N N   . ALA D 53  ? 0.2663 0.3349 0.6186 0.0390  -0.1247 -0.0528 53  ALA D N   
6422  C CA  . ALA D 53  ? 0.2614 0.3243 0.5901 0.0476  -0.1176 -0.0534 53  ALA D CA  
6423  C C   . ALA D 53  ? 0.2436 0.3110 0.5595 0.0498  -0.0955 -0.0518 53  ALA D C   
6424  O O   . ALA D 53  ? 0.2376 0.3118 0.5437 0.0538  -0.0855 -0.0479 53  ALA D O   
6425  C CB  . ALA D 53  ? 0.2723 0.3121 0.5768 0.0522  -0.1295 -0.0598 53  ALA D CB  
6426  N N   . LEU D 54  ? 0.2516 0.3142 0.5656 0.0470  -0.0887 -0.0543 54  LEU D N   
6427  C CA  . LEU D 54  ? 0.2373 0.3043 0.5378 0.0475  -0.0689 -0.0515 54  LEU D CA  
6428  C C   . LEU D 54  ? 0.2326 0.3192 0.5502 0.0448  -0.0601 -0.0457 54  LEU D C   
6429  O O   . LEU D 54  ? 0.2255 0.3171 0.5292 0.0477  -0.0479 -0.0420 54  LEU D O   
6430  C CB  . LEU D 54  ? 0.2336 0.2913 0.5306 0.0446  -0.0654 -0.0553 54  LEU D CB  
6431  C CG  . LEU D 54  ? 0.2332 0.2735 0.4998 0.0485  -0.0641 -0.0597 54  LEU D CG  
6432  C CD1 . LEU D 54  ? 0.2234 0.2655 0.4601 0.0520  -0.0483 -0.0542 54  LEU D CD1 
6433  C CD2 . LEU D 54  ? 0.2470 0.2741 0.5082 0.0518  -0.0814 -0.0654 54  LEU D CD2 
6434  N N   . LEU D 55  ? 0.2240 0.3219 0.5712 0.0389  -0.0672 -0.0449 55  LEU D N   
6435  C CA  . LEU D 55  ? 0.2217 0.3400 0.5856 0.0360  -0.0591 -0.0403 55  LEU D CA  
6436  C C   . LEU D 55  ? 0.2234 0.3505 0.5843 0.0413  -0.0588 -0.0370 55  LEU D C   
6437  O O   . LEU D 55  ? 0.2209 0.3584 0.5869 0.0423  -0.0491 -0.0350 55  LEU D O   
6438  C CB  . LEU D 55  ? 0.2302 0.3605 0.6252 0.0274  -0.0681 -0.0397 55  LEU D CB  
6439  C CG  . LEU D 55  ? 0.2272 0.3750 0.6380 0.0210  -0.0568 -0.0370 55  LEU D CG  
6440  C CD1 . LEU D 55  ? 0.2176 0.3558 0.6122 0.0212  -0.0435 -0.0382 55  LEU D CD1 
6441  C CD2 . LEU D 55  ? 0.2377 0.3961 0.6757 0.0102  -0.0669 -0.0363 55  LEU D CD2 
6442  N N   . LYS D 56  ? 0.2258 0.3464 0.5841 0.0448  -0.0714 -0.0379 56  LYS D N   
6443  C CA  . LYS D 56  ? 0.2283 0.3552 0.5829 0.0503  -0.0718 -0.0348 56  LYS D CA  
6444  C C   . LYS D 56  ? 0.2228 0.3397 0.5580 0.0554  -0.0609 -0.0360 56  LYS D C   
6445  O O   . LYS D 56  ? 0.2240 0.3478 0.5661 0.0580  -0.0561 -0.0348 56  LYS D O   
6446  C CB  . LYS D 56  ? 0.2413 0.3609 0.5984 0.0522  -0.0897 -0.0361 56  LYS D CB  
6447  C CG  . LYS D 56  ? 0.2495 0.3820 0.6201 0.0546  -0.0959 -0.0326 56  LYS D CG  
6448  C CD  . LYS D 56  ? 0.2631 0.3840 0.6271 0.0578  -0.1126 -0.0335 56  LYS D CD  
6449  C CE  . LYS D 56  ? 0.2606 0.3755 0.6029 0.0654  -0.1068 -0.0318 56  LYS D CE  
6450  N NZ  . LYS D 56  ? 0.2769 0.3858 0.6186 0.0685  -0.1236 -0.0312 56  LYS D NZ  
6451  N N   . TRP D 57  ? 0.2311 0.3323 0.5428 0.0565  -0.0577 -0.0387 57  TRP D N   
6452  C CA  . TRP D 57  ? 0.2267 0.3196 0.5197 0.0596  -0.0479 -0.0398 57  TRP D CA  
6453  C C   . TRP D 57  ? 0.2210 0.3199 0.5200 0.0569  -0.0353 -0.0393 57  TRP D C   
6454  O O   . TRP D 57  ? 0.2207 0.3206 0.5160 0.0591  -0.0291 -0.0386 57  TRP D O   
6455  C CB  . TRP D 57  ? 0.2239 0.3008 0.4920 0.0604  -0.0475 -0.0431 57  TRP D CB  
6456  C CG  . TRP D 57  ? 0.2197 0.2898 0.4684 0.0622  -0.0379 -0.0439 57  TRP D CG  
6457  C CD1 . TRP D 57  ? 0.2216 0.2926 0.4650 0.0659  -0.0357 -0.0424 57  TRP D CD1 
6458  C CD2 . TRP D 57  ? 0.2136 0.2760 0.4464 0.0600  -0.0299 -0.0459 57  TRP D CD2 
6459  N NE1 . TRP D 57  ? 0.2168 0.2816 0.4421 0.0657  -0.0269 -0.0431 57  TRP D NE1 
6460  C CE2 . TRP D 57  ? 0.2120 0.2719 0.4306 0.0620  -0.0235 -0.0451 57  TRP D CE2 
6461  C CE3 . TRP D 57  ? 0.2100 0.2677 0.4396 0.0564  -0.0283 -0.0478 57  TRP D CE3 
6462  C CZ2 . TRP D 57  ? 0.2073 0.2610 0.4092 0.0603  -0.0161 -0.0460 57  TRP D CZ2 
6463  C CZ3 . TRP D 57  ? 0.2056 0.2567 0.4181 0.0551  -0.0208 -0.0489 57  TRP D CZ3 
6464  C CH2 . TRP D 57  ? 0.2043 0.2540 0.4035 0.0569  -0.0151 -0.0478 57  TRP D CH2 
6465  N N   . LYS D 58  ? 0.2120 0.3144 0.5196 0.0520  -0.0319 -0.0396 58  LYS D N   
6466  C CA  . LYS D 58  ? 0.2082 0.3151 0.5201 0.0492  -0.0203 -0.0391 58  LYS D CA  
6467  C C   . LYS D 58  ? 0.2128 0.3340 0.5439 0.0504  -0.0181 -0.0372 58  LYS D C   
6468  O O   . LYS D 58  ? 0.2119 0.3336 0.5407 0.0507  -0.0092 -0.0372 58  LYS D O   
6469  C CB  . LYS D 58  ? 0.2054 0.3146 0.5248 0.0437  -0.0182 -0.0393 58  LYS D CB  
6470  C CG  . LYS D 58  ? 0.2028 0.3154 0.5249 0.0406  -0.0064 -0.0389 58  LYS D CG  
6471  C CD  . LYS D 58  ? 0.2072 0.3387 0.5558 0.0378  -0.0049 -0.0371 58  LYS D CD  
6472  C CE  . LYS D 58  ? 0.2058 0.3404 0.5566 0.0339  0.0063  -0.0370 58  LYS D CE  
6473  N NZ  . LYS D 58  ? 0.2030 0.3367 0.5545 0.0285  0.0064  -0.0368 58  LYS D NZ  
6474  N N   . SER D 59  ? 0.2063 0.3393 0.5569 0.0509  -0.0270 -0.0358 59  SER D N   
6475  C CA  . SER D 59  ? 0.2121 0.3600 0.5831 0.0525  -0.0259 -0.0344 59  SER D CA  
6476  C C   . SER D 59  ? 0.2136 0.3568 0.5752 0.0579  -0.0232 -0.0343 59  SER D C   
6477  O O   . SER D 59  ? 0.2171 0.3698 0.5916 0.0593  -0.0187 -0.0339 59  SER D O   
6478  C CB  . SER D 59  ? 0.2196 0.3804 0.6116 0.0521  -0.0380 -0.0328 59  SER D CB  
6479  O OG  . SER D 59  ? 0.2238 0.3775 0.6070 0.0569  -0.0479 -0.0322 59  SER D OG  
6480  N N   . THR D 60  ? 0.2169 0.3464 0.5569 0.0610  -0.0259 -0.0348 60  THR D N   
6481  C CA  . THR D 60  ? 0.2184 0.3436 0.5482 0.0656  -0.0237 -0.0342 60  THR D CA  
6482  C C   . THR D 60  ? 0.2133 0.3325 0.5299 0.0642  -0.0120 -0.0350 60  THR D C   
6483  O O   . THR D 60  ? 0.2149 0.3325 0.5259 0.0675  -0.0093 -0.0343 60  THR D O   
6484  C CB  . THR D 60  ? 0.2194 0.3333 0.5306 0.0691  -0.0307 -0.0343 60  THR D CB  
6485  O OG1 . THR D 60  ? 0.2126 0.3137 0.5005 0.0673  -0.0253 -0.0361 60  THR D OG1 
6486  C CG2 . THR D 60  ? 0.2246 0.3408 0.5444 0.0691  -0.0431 -0.0339 60  THR D CG2 
6487  N N   . PHE D 61  ? 0.2362 0.3520 0.5479 0.0595  -0.0057 -0.0361 61  PHE D N   
6488  C CA  . PHE D 61  ? 0.2321 0.3409 0.5294 0.0578  0.0039  -0.0366 61  PHE D CA  
6489  C C   . PHE D 61  ? 0.2361 0.3532 0.5457 0.0588  0.0095  -0.0360 61  PHE D C   
6490  O O   . PHE D 61  ? 0.2408 0.3707 0.5728 0.0589  0.0090  -0.0358 61  PHE D O   
6491  C CB  . PHE D 61  ? 0.2272 0.3315 0.5194 0.0526  0.0084  -0.0377 61  PHE D CB  
6492  C CG  . PHE D 61  ? 0.2233 0.3176 0.5004 0.0518  0.0038  -0.0389 61  PHE D CG  
6493  C CD1 . PHE D 61  ? 0.2238 0.3116 0.4873 0.0554  -0.0017 -0.0392 61  PHE D CD1 
6494  C CD2 . PHE D 61  ? 0.2201 0.3116 0.4968 0.0477  0.0049  -0.0399 61  PHE D CD2 
6495  C CE1 . PHE D 61  ? 0.2217 0.3005 0.4714 0.0552  -0.0059 -0.0409 61  PHE D CE1 
6496  C CE2 . PHE D 61  ? 0.2175 0.2997 0.4810 0.0475  0.0002  -0.0415 61  PHE D CE2 
6497  C CZ  . PHE D 61  ? 0.2186 0.2946 0.4685 0.0514  -0.0052 -0.0423 61  PHE D CZ  
6498  N N   . THR D 62  ? 0.3081 0.4184 0.6036 0.0596  0.0148  -0.0357 62  THR D N   
6499  C CA  . THR D 62  ? 0.3123 0.4285 0.6169 0.0611  0.0199  -0.0354 62  THR D CA  
6500  C C   . THR D 62  ? 0.3102 0.4235 0.6103 0.0569  0.0286  -0.0361 62  THR D C   
6501  O O   . THR D 62  ? 0.3048 0.4084 0.5887 0.0535  0.0307  -0.0363 62  THR D O   
6502  C CB  . THR D 62  ? 0.3135 0.4245 0.6065 0.0652  0.0189  -0.0344 62  THR D CB  
6503  O OG1 . THR D 62  ? 0.3141 0.4231 0.6025 0.0685  0.0109  -0.0336 62  THR D OG1 
6504  C CG2 . THR D 62  ? 0.3203 0.4404 0.6294 0.0686  0.0207  -0.0342 62  THR D CG2 
6505  N N   . ASN D 63  ? 0.3871 0.5091 0.7022 0.0575  0.0334  -0.0366 63  ASN D N   
6506  C CA  . ASN D 63  ? 0.3871 0.5072 0.6993 0.0543  0.0418  -0.0374 63  ASN D CA  
6507  C C   . ASN D 63  ? 0.3833 0.5002 0.6916 0.0493  0.0439  -0.0378 63  ASN D C   
6508  O O   . ASN D 63  ? 0.3804 0.4882 0.6744 0.0462  0.0485  -0.0378 63  ASN D O   
6509  C CB  . ASN D 63  ? 0.3848 0.4937 0.6774 0.0543  0.0446  -0.0367 63  ASN D CB  
6510  C CG  . ASN D 63  ? 0.3896 0.5022 0.6875 0.0590  0.0441  -0.0364 63  ASN D CG  
6511  O OD1 . ASN D 63  ? 0.3959 0.5201 0.7139 0.0621  0.0433  -0.0371 63  ASN D OD1 
6512  N ND2 . ASN D 63  ? 0.3892 0.4924 0.6697 0.0595  0.0444  -0.0353 63  ASN D ND2 
6513  N N   . GLN D 64  ? 0.3118 0.4365 0.6334 0.0486  0.0402  -0.0380 64  GLN D N   
6514  C CA  . GLN D 64  ? 0.3083 0.4303 0.6271 0.0442  0.0413  -0.0382 64  GLN D CA  
6515  C C   . GLN D 64  ? 0.3128 0.4456 0.6471 0.0415  0.0484  -0.0390 64  GLN D C   
6516  O O   . GLN D 64  ? 0.3188 0.4670 0.6745 0.0429  0.0489  -0.0395 64  GLN D O   
6517  C CB  . GLN D 64  ? 0.3065 0.4314 0.6314 0.0443  0.0332  -0.0379 64  GLN D CB  
6518  C CG  . GLN D 64  ? 0.3017 0.4139 0.6090 0.0418  0.0309  -0.0382 64  GLN D CG  
6519  C CD  . GLN D 64  ? 0.2961 0.3941 0.5790 0.0424  0.0322  -0.0382 64  GLN D CD  
6520  O OE1 . GLN D 64  ? 0.2966 0.3926 0.5733 0.0458  0.0297  -0.0377 64  GLN D OE1 
6521  N NE2 . GLN D 64  ? 0.2925 0.3816 0.5623 0.0390  0.0361  -0.0384 64  GLN D NE2 
6522  N N   . THR D 65  ? 0.2939 0.4196 0.6177 0.0376  0.0537  -0.0392 65  THR D N   
6523  C CA  . THR D 65  ? 0.2987 0.4339 0.6341 0.0346  0.0613  -0.0399 65  THR D CA  
6524  C C   . THR D 65  ? 0.2976 0.4396 0.6423 0.0306  0.0602  -0.0395 65  THR D C   
6525  O O   . THR D 65  ? 0.2919 0.4255 0.6275 0.0297  0.0547  -0.0389 65  THR D O   
6526  C CB  . THR D 65  ? 0.2983 0.4225 0.6173 0.0326  0.0680  -0.0402 65  THR D CB  
6527  O OG1 . THR D 65  ? 0.3045 0.4395 0.6354 0.0300  0.0760  -0.0413 65  THR D OG1 
6528  C CG2 . THR D 65  ? 0.2914 0.4003 0.5905 0.0301  0.0659  -0.0394 65  THR D CG2 
6529  N N   . SER D 66  ? 0.2812 0.4399 0.6448 0.0279  0.0656  -0.0400 66  SER D N   
6530  C CA  . SER D 66  ? 0.2812 0.4498 0.6555 0.0226  0.0655  -0.0391 66  SER D CA  
6531  C C   . SER D 66  ? 0.2770 0.4322 0.6336 0.0188  0.0685  -0.0386 66  SER D C   
6532  O O   . SER D 66  ? 0.2756 0.4355 0.6373 0.0141  0.0670  -0.0374 66  SER D O   
6533  C CB  . SER D 66  ? 0.2900 0.4817 0.6880 0.0193  0.0720  -0.0396 66  SER D CB  
6534  O OG  . SER D 66  ? 0.2909 0.4963 0.7026 0.0128  0.0706  -0.0380 66  SER D OG  
6535  N N   . SER D 67  ? 0.2932 0.4328 0.6301 0.0203  0.0723  -0.0392 67  SER D N   
6536  C CA  . SER D 67  ? 0.2902 0.4170 0.6104 0.0172  0.0753  -0.0389 67  SER D CA  
6537  C C   . SER D 67  ? 0.2820 0.3917 0.5845 0.0186  0.0681  -0.0385 67  SER D C   
6538  O O   . SER D 67  ? 0.2819 0.3805 0.5708 0.0165  0.0695  -0.0383 67  SER D O   
6539  C CB  . SER D 67  ? 0.2984 0.4181 0.6073 0.0176  0.0824  -0.0397 67  SER D CB  
6540  O OG  . SER D 67  ? 0.2885 0.3915 0.5781 0.0206  0.0786  -0.0394 67  SER D OG  
6541  N N   . SER D 68  ? 0.2477 0.3557 0.5502 0.0220  0.0605  -0.0385 68  SER D N   
6542  C CA  . SER D 68  ? 0.2410 0.3344 0.5263 0.0233  0.0540  -0.0387 68  SER D CA  
6543  C C   . SER D 68  ? 0.2380 0.3306 0.5258 0.0205  0.0507  -0.0386 68  SER D C   
6544  O O   . SER D 68  ? 0.2404 0.3466 0.5464 0.0177  0.0507  -0.0379 68  SER D O   
6545  C CB  . SER D 68  ? 0.2398 0.3336 0.5253 0.0274  0.0470  -0.0389 68  SER D CB  
6546  O OG  . SER D 68  ? 0.2401 0.3430 0.5406 0.0276  0.0408  -0.0388 68  SER D OG  
6547  N N   . LYS D 69  ? 0.2377 0.3158 0.5077 0.0208  0.0477  -0.0392 69  LYS D N   
6548  C CA  . LYS D 69  ? 0.2347 0.3100 0.5054 0.0188  0.0438  -0.0396 69  LYS D CA  
6549  C C   . LYS D 69  ? 0.2339 0.3159 0.5167 0.0199  0.0350  -0.0398 69  LYS D C   
6550  O O   . LYS D 69  ? 0.2323 0.3158 0.5214 0.0175  0.0310  -0.0397 69  LYS D O   
6551  C CB  . LYS D 69  ? 0.2306 0.2899 0.4794 0.0197  0.0419  -0.0407 69  LYS D CB  
6552  C CG  . LYS D 69  ? 0.2314 0.2845 0.4708 0.0173  0.0493  -0.0399 69  LYS D CG  
6553  C CD  . LYS D 69  ? 0.2294 0.2720 0.4480 0.0190  0.0486  -0.0400 69  LYS D CD  
6554  C CE  . LYS D 69  ? 0.2302 0.2663 0.4392 0.0167  0.0541  -0.0390 69  LYS D CE  
6555  N NZ  . LYS D 69  ? 0.2281 0.2566 0.4182 0.0183  0.0522  -0.0385 69  LYS D NZ  
6556  N N   . LEU D 70  ? 0.1993 0.2857 0.4862 0.0233  0.0313  -0.0400 70  LEU D N   
6557  C CA  . LEU D 70  ? 0.1999 0.2934 0.4990 0.0244  0.0222  -0.0399 70  LEU D CA  
6558  C C   . LEU D 70  ? 0.2040 0.3172 0.5290 0.0203  0.0223  -0.0378 70  LEU D C   
6559  O O   . LEU D 70  ? 0.2058 0.3277 0.5437 0.0202  0.0139  -0.0372 70  LEU D O   
6560  C CB  . LEU D 70  ? 0.2010 0.2928 0.4950 0.0294  0.0180  -0.0405 70  LEU D CB  
6561  C CG  . LEU D 70  ? 0.1980 0.2750 0.4675 0.0323  0.0166  -0.0421 70  LEU D CG  
6562  C CD1 . LEU D 70  ? 0.1997 0.2773 0.4673 0.0367  0.0097  -0.0425 70  LEU D CD1 
6563  C CD2 . LEU D 70  ? 0.1949 0.2612 0.4523 0.0312  0.0138  -0.0438 70  LEU D CD2 
6564  N N   . SER D 71  ? 0.2046 0.3264 0.5371 0.0162  0.0312  -0.0367 71  SER D N   
6565  C CA  . SER D 71  ? 0.2096 0.3531 0.5662 0.0097  0.0318  -0.0346 71  SER D CA  
6566  C C   . SER D 71  ? 0.2097 0.3558 0.5763 0.0027  0.0247  -0.0337 71  SER D C   
6567  O O   . SER D 71  ? 0.2168 0.3796 0.6084 -0.0044 0.0208  -0.0325 71  SER D O   
6568  C CB  . SER D 71  ? 0.2140 0.3651 0.5740 0.0056  0.0436  -0.0339 71  SER D CB  
6569  O OG  . SER D 71  ? 0.2154 0.3606 0.5670 0.0112  0.0495  -0.0355 71  SER D OG  
6570  N N   . SER D 72  ? 0.2325 0.3592 0.5909 0.0033  0.0226  -0.0365 72  SER D N   
6571  C CA  . SER D 72  ? 0.2377 0.3605 0.6166 -0.0042 0.0146  -0.0383 72  SER D CA  
6572  C C   . SER D 72  ? 0.2406 0.3634 0.6310 -0.0028 -0.0003 -0.0396 72  SER D C   
6573  O O   . SER D 72  ? 0.2481 0.3692 0.6551 -0.0109 -0.0109 -0.0402 72  SER D O   
6574  C CB  . SER D 72  ? 0.2340 0.3355 0.6008 -0.0023 0.0157  -0.0418 72  SER D CB  
6575  O OG  . SER D 72  ? 0.2270 0.3134 0.5677 0.0084  0.0137  -0.0443 72  SER D OG  
6576  N N   . TRP D 73  ? 0.2125 0.3359 0.5916 0.0058  -0.0028 -0.0395 73  TRP D N   
6577  C CA  . TRP D 73  ? 0.2168 0.3400 0.6050 0.0076  -0.0171 -0.0406 73  TRP D CA  
6578  C C   . TRP D 73  ? 0.2246 0.3708 0.6371 0.0010  -0.0202 -0.0372 73  TRP D C   
6579  O O   . TRP D 73  ? 0.2241 0.3818 0.6358 0.0055  -0.0181 -0.0353 73  TRP D O   
6580  C CB  . TRP D 73  ? 0.2117 0.3260 0.5752 0.0181  -0.0175 -0.0414 73  TRP D CB  
6581  C CG  . TRP D 73  ? 0.2062 0.2997 0.5423 0.0233  -0.0157 -0.0446 73  TRP D CG  
6582  C CD1 . TRP D 73  ? 0.2036 0.2862 0.5331 0.0214  -0.0108 -0.0468 73  TRP D CD1 
6583  C CD2 . TRP D 73  ? 0.2039 0.2869 0.5139 0.0304  -0.0183 -0.0454 73  TRP D CD2 
6584  N NE1 . TRP D 73  ? 0.2000 0.2670 0.4996 0.0270  -0.0109 -0.0489 73  TRP D NE1 
6585  C CE2 . TRP D 73  ? 0.2002 0.2679 0.4865 0.0321  -0.0149 -0.0477 73  TRP D CE2 
6586  C CE3 . TRP D 73  ? 0.2057 0.2919 0.5095 0.0351  -0.0231 -0.0439 73  TRP D CE3 
6587  C CZ2 . TRP D 73  ? 0.1989 0.2563 0.4566 0.0374  -0.0157 -0.0482 73  TRP D CZ2 
6588  C CZ3 . TRP D 73  ? 0.2049 0.2787 0.4841 0.0403  -0.0239 -0.0456 73  TRP D CZ3 
6589  C CH2 . TRP D 73  ? 0.2020 0.2623 0.4600 0.0408  -0.0201 -0.0481 73  TRP D CH2 
6590  N N   . VAL D 74  ? 0.2599 0.4129 0.6929 -0.0109 -0.0259 -0.0361 74  VAL D N   
6591  C CA  . VAL D 74  ? 0.2694 0.4459 0.7247 -0.0200 -0.0278 -0.0328 74  VAL D CA  
6592  C C   . VAL D 74  ? 0.2809 0.4574 0.7500 -0.0255 -0.0464 -0.0328 74  VAL D C   
6593  O O   . VAL D 74  ? 0.2843 0.4719 0.7621 -0.0224 -0.0525 -0.0320 74  VAL D O   
6594  C CB  . VAL D 74  ? 0.2750 0.4626 0.7390 -0.0331 -0.0182 -0.0305 74  VAL D CB  
6595  C CG1 . VAL D 74  ? 0.2859 0.4996 0.7722 -0.0429 -0.0195 -0.0277 74  VAL D CG1 
6596  C CG2 . VAL D 74  ? 0.2658 0.4524 0.7137 -0.0273 -0.0013 -0.0305 74  VAL D CG2 
6597  N N   . ASN D 75  ? 0.3223 0.4843 0.7909 -0.0342 -0.0568 -0.0337 75  ASN D N   
6598  C CA  . ASN D 75  ? 0.3377 0.4979 0.8149 -0.0413 -0.0757 -0.0333 75  ASN D CA  
6599  C C   . ASN D 75  ? 0.3394 0.4737 0.7999 -0.0339 -0.0904 -0.0373 75  ASN D C   
6600  O O   . ASN D 75  ? 0.3358 0.4506 0.7815 -0.0319 -0.0896 -0.0403 75  ASN D O   
6601  C CB  . ASN D 75  ? 0.3552 0.5184 0.8412 -0.0609 -0.0798 -0.0306 75  ASN D CB  
6602  C CG  . ASN D 75  ? 0.3626 0.4989 0.8312 -0.0674 -0.0846 -0.0320 75  ASN D CG  
6603  O OD1 . ASN D 75  ? 0.3505 0.4749 0.8066 -0.0599 -0.0759 -0.0342 75  ASN D OD1 
6604  N ND2 . ASN D 75  ? 0.3853 0.5098 0.8502 -0.0816 -0.0989 -0.0310 75  ASN D ND2 
6605  N N   . PRO D 76  ? 0.3398 0.4729 0.8009 -0.0295 -0.1041 -0.0379 76  PRO D N   
6606  C CA  . PRO D 76  ? 0.3436 0.4518 0.7851 -0.0217 -0.1182 -0.0424 76  PRO D CA  
6607  C C   . PRO D 76  ? 0.3634 0.4496 0.7937 -0.0324 -0.1342 -0.0441 76  PRO D C   
6608  O O   . PRO D 76  ? 0.3688 0.4306 0.7775 -0.0259 -0.1450 -0.0491 76  PRO D O   
6609  C CB  . PRO D 76  ? 0.3489 0.4639 0.7940 -0.0159 -0.1277 -0.0416 76  PRO D CB  
6610  C CG  . PRO D 76  ? 0.3415 0.4845 0.8059 -0.0163 -0.1145 -0.0375 76  PRO D CG  
6611  C CD  . PRO D 76  ? 0.3437 0.4982 0.8213 -0.0294 -0.1063 -0.0351 76  PRO D CD  
6612  N N   . ASN D 77  ? 0.3892 0.4811 0.8289 -0.0487 -0.1357 -0.0405 77  ASN D N   
6613  C CA  . ASN D 77  ? 0.4135 0.4798 0.8352 -0.0602 -0.1499 -0.0415 77  ASN D CA  
6614  C C   . ASN D 77  ? 0.4191 0.4605 0.8185 -0.0574 -0.1456 -0.0453 77  ASN D C   
6615  O O   . ASN D 77  ? 0.4062 0.4561 0.8117 -0.0541 -0.1291 -0.0450 77  ASN D O   
6616  C CB  . ASN D 77  ? 0.4301 0.5080 0.8649 -0.0793 -0.1495 -0.0365 77  ASN D CB  
6617  C CG  . ASN D 77  ? 0.4452 0.5344 0.8921 -0.0848 -0.1627 -0.0347 77  ASN D CG  
6618  O OD1 . ASN D 77  ? 0.4500 0.5299 0.8884 -0.0764 -0.1759 -0.0370 77  ASN D OD1 
6619  N ND2 . ASN D 77  ? 0.4544 0.5636 0.9203 -0.0994 -0.1592 -0.0308 77  ASN D ND2 
6620  N N   . THR D 78  ? 0.5054 0.5140 0.8756 -0.0582 -0.1603 -0.0491 78  THR D N   
6621  C CA  . THR D 78  ? 0.5076 0.4882 0.8511 -0.0556 -0.1572 -0.0530 78  THR D CA  
6622  C C   . THR D 78  ? 0.5115 0.4911 0.8565 -0.0713 -0.1486 -0.0480 78  THR D C   
6623  O O   . THR D 78  ? 0.5174 0.5182 0.8836 -0.0845 -0.1454 -0.0423 78  THR D O   
6624  C CB  . THR D 78  ? 0.5237 0.4683 0.8300 -0.0519 -0.1734 -0.0579 78  THR D CB  
6625  O OG1 . THR D 78  ? 0.5288 0.4778 0.8363 -0.0426 -0.1836 -0.0605 78  THR D OG1 
6626  C CG2 . THR D 78  ? 0.5237 0.4420 0.7996 -0.0404 -0.1682 -0.0637 78  THR D CG2 
6627  N N   . SER D 79  ? 0.5092 0.4638 0.8296 -0.0691 -0.1437 -0.0504 79  SER D N   
6628  C CA  . SER D 79  ? 0.5286 0.4753 0.8424 -0.0826 -0.1354 -0.0460 79  SER D CA  
6629  C C   . SER D 79  ? 0.5032 0.4807 0.8456 -0.0844 -0.1160 -0.0424 79  SER D C   
6630  O O   . SER D 79  ? 0.5149 0.4885 0.8527 -0.0947 -0.1062 -0.0386 79  SER D O   
6631  C CB  . SER D 79  ? 0.5472 0.4894 0.8587 -0.1013 -0.1446 -0.0411 79  SER D CB  
6632  O OG  . SER D 79  ? 0.5287 0.5069 0.8752 -0.1100 -0.1407 -0.0366 79  SER D OG  
6633  N N   . SER D 80  ? 0.4068 0.4142 0.7758 -0.0739 -0.1096 -0.0433 80  SER D N   
6634  C CA  . SER D 80  ? 0.3840 0.4172 0.7728 -0.0689 -0.0893 -0.0418 80  SER D CA  
6635  C C   . SER D 80  ? 0.3653 0.4026 0.7562 -0.0483 -0.0862 -0.0476 80  SER D C   
6636  O O   . SER D 80  ? 0.3542 0.3987 0.7481 -0.0398 -0.0708 -0.0490 80  SER D O   
6637  C CB  . SER D 80  ? 0.3681 0.4364 0.7842 -0.0768 -0.0809 -0.0360 80  SER D CB  
6638  O OG  . SER D 80  ? 0.3489 0.4378 0.7755 -0.0724 -0.0603 -0.0344 80  SER D OG  
6639  N N   . PHE D 81  ? 0.3404 0.3725 0.7276 -0.0406 -0.1007 -0.0510 81  PHE D N   
6640  C CA  . PHE D 81  ? 0.3330 0.3634 0.7155 -0.0218 -0.1003 -0.0573 81  PHE D CA  
6641  C C   . PHE D 81  ? 0.3429 0.3421 0.6946 -0.0144 -0.0993 -0.0635 81  PHE D C   
6642  O O   . PHE D 81  ? 0.3315 0.3347 0.6786 -0.0010 -0.0851 -0.0657 81  PHE D O   
6643  C CB  . PHE D 81  ? 0.3403 0.3667 0.7182 -0.0170 -0.1171 -0.0591 81  PHE D CB  
6644  C CG  . PHE D 81  ? 0.3337 0.3537 0.6999 0.0013  -0.1184 -0.0657 81  PHE D CG  
6645  C CD1 . PHE D 81  ? 0.3195 0.3561 0.6897 0.0133  -0.1010 -0.0643 81  PHE D CD1 
6646  C CD2 . PHE D 81  ? 0.3483 0.3384 0.6843 0.0063  -0.1333 -0.0722 81  PHE D CD2 
6647  C CE1 . PHE D 81  ? 0.3154 0.3413 0.6614 0.0269  -0.0984 -0.0687 81  PHE D CE1 
6648  C CE2 . PHE D 81  ? 0.3406 0.3239 0.6590 0.0237  -0.1314 -0.0773 81  PHE D CE2 
6649  C CZ  . PHE D 81  ? 0.3247 0.3275 0.6505 0.0331  -0.1142 -0.0755 81  PHE D CZ  
6650  N N   . CYS D 82  ? 0.4074 0.3730 0.7308 -0.0212 -0.1123 -0.0655 82  CYS D N   
6651  C CA  . CYS D 82  ? 0.4080 0.3405 0.6924 -0.0112 -0.1111 -0.0705 82  CYS D CA  
6652  C C   . CYS D 82  ? 0.4112 0.3353 0.6865 -0.0171 -0.0991 -0.0671 82  CYS D C   
6653  O O   . CYS D 82  ? 0.4167 0.3178 0.6560 -0.0092 -0.0971 -0.0686 82  CYS D O   
6654  C CB  . CYS D 82  ? 0.4243 0.3292 0.6744 -0.0120 -0.1273 -0.0715 82  CYS D CB  
6655  S SG  . CYS D 82  ? 0.4274 0.3341 0.6740 -0.0007 -0.1403 -0.0766 82  CYS D SG  
6656  N N   . THR D 83  ? 0.3850 0.3312 0.6895 -0.0308 -0.0901 -0.0613 83  THR D N   
6657  C CA  . THR D 83  ? 0.3900 0.3276 0.6853 -0.0376 -0.0785 -0.0578 83  THR D CA  
6658  C C   . THR D 83  ? 0.3710 0.3408 0.6915 -0.0350 -0.0577 -0.0549 83  THR D C   
6659  O O   . THR D 83  ? 0.3691 0.3299 0.6755 -0.0307 -0.0461 -0.0551 83  THR D O   
6660  C CB  . THR D 83  ? 0.4121 0.3418 0.7022 -0.0584 -0.0846 -0.0507 83  THR D CB  
6661  O OG1 . THR D 83  ? 0.4062 0.3659 0.7281 -0.0688 -0.0868 -0.0464 83  THR D OG1 
6662  C CG2 . THR D 83  ? 0.4391 0.3328 0.6908 -0.0582 -0.1007 -0.0524 83  THR D CG2 
6663  N N   . SER D 84  ? 0.3145 0.3212 0.6713 -0.0368 -0.0531 -0.0526 84  SER D N   
6664  C CA  . SER D 84  ? 0.2919 0.3303 0.6736 -0.0370 -0.0332 -0.0492 84  SER D CA  
6665  C C   . SER D 84  ? 0.2690 0.3278 0.6586 -0.0178 -0.0240 -0.0515 84  SER D C   
6666  O O   . SER D 84  ? 0.2581 0.3287 0.6441 -0.0135 -0.0067 -0.0490 84  SER D O   
6667  C CB  . SER D 84  ? 0.2962 0.3555 0.6918 -0.0520 -0.0301 -0.0415 84  SER D CB  
6668  O OG  . SER D 84  ? 0.2829 0.3663 0.6946 -0.0452 -0.0308 -0.0405 84  SER D OG  
6669  N N   . TRP D 85  ? 0.2442 0.2991 0.6309 -0.0070 -0.0354 -0.0556 85  TRP D N   
6670  C CA  . TRP D 85  ? 0.2344 0.2944 0.6055 0.0070  -0.0266 -0.0557 85  TRP D CA  
6671  C C   . TRP D 85  ? 0.2363 0.2808 0.5754 0.0156  -0.0171 -0.0586 85  TRP D C   
6672  O O   . TRP D 85  ? 0.2416 0.2680 0.5641 0.0205  -0.0248 -0.0634 85  TRP D O   
6673  C CB  . TRP D 85  ? 0.2381 0.2950 0.6067 0.0120  -0.0413 -0.0578 85  TRP D CB  
6674  C CG  . TRP D 85  ? 0.2457 0.3199 0.6348 0.0043  -0.0483 -0.0531 85  TRP D CG  
6675  C CD1 . TRP D 85  ? 0.2554 0.3416 0.6636 -0.0104 -0.0501 -0.0485 85  TRP D CD1 
6676  C CD2 . TRP D 85  ? 0.2477 0.3282 0.6351 0.0091  -0.0541 -0.0520 85  TRP D CD2 
6677  N NE1 . TRP D 85  ? 0.2624 0.3632 0.6825 -0.0136 -0.0569 -0.0452 85  TRP D NE1 
6678  C CE2 . TRP D 85  ? 0.2572 0.3548 0.6669 -0.0012 -0.0599 -0.0474 85  TRP D CE2 
6679  C CE3 . TRP D 85  ? 0.2444 0.3179 0.6108 0.0195  -0.0546 -0.0540 85  TRP D CE3 
6680  C CZ2 . TRP D 85  ? 0.2620 0.3697 0.6778 0.0007  -0.0672 -0.0455 85  TRP D CZ2 
6681  C CZ3 . TRP D 85  ? 0.2494 0.3323 0.6218 0.0207  -0.0617 -0.0516 85  TRP D CZ3 
6682  C CH2 . TRP D 85  ? 0.2577 0.3573 0.6560 0.0122  -0.0683 -0.0477 85  TRP D CH2 
6683  N N   . TYR D 86  ? 0.2563 0.3079 0.5779 0.0162  -0.0022 -0.0540 86  TYR D N   
6684  C CA  . TYR D 86  ? 0.2450 0.2865 0.5298 0.0205  0.0051  -0.0530 86  TYR D CA  
6685  C C   . TYR D 86  ? 0.2198 0.2540 0.4732 0.0274  -0.0010 -0.0531 86  TYR D C   
6686  O O   . TYR D 86  ? 0.2176 0.2580 0.4690 0.0299  -0.0038 -0.0515 86  TYR D O   
6687  C CB  . TYR D 86  ? 0.2172 0.2681 0.4883 0.0201  0.0174  -0.0471 86  TYR D CB  
6688  C CG  . TYR D 86  ? 0.2107 0.2531 0.4480 0.0232  0.0222  -0.0451 86  TYR D CG  
6689  C CD1 . TYR D 86  ? 0.2108 0.2509 0.4351 0.0262  0.0208  -0.0457 86  TYR D CD1 
6690  C CD2 . TYR D 86  ? 0.2106 0.2473 0.4408 0.0211  0.0280  -0.0445 86  TYR D CD2 
6691  C CE1 . TYR D 86  ? 0.2101 0.2443 0.4165 0.0268  0.0245  -0.0453 86  TYR D CE1 
6692  C CE2 . TYR D 86  ? 0.2106 0.2404 0.4221 0.0221  0.0313  -0.0443 86  TYR D CE2 
6693  C CZ  . TYR D 86  ? 0.2100 0.2395 0.4104 0.0247  0.0294  -0.0445 86  TYR D CZ  
6694  O OH  . TYR D 86  ? 0.2096 0.2346 0.3936 0.0254  0.0320  -0.0436 86  TYR D OH  
6695  N N   . GLY D 87  ? 0.2384 0.2601 0.4650 0.0309  -0.0024 -0.0539 87  GLY D N   
6696  C CA  . GLY D 87  ? 0.2396 0.2556 0.4369 0.0364  -0.0050 -0.0532 87  GLY D CA  
6697  C C   . GLY D 87  ? 0.2476 0.2554 0.4407 0.0400  -0.0164 -0.0565 87  GLY D C   
6698  O O   . GLY D 87  ? 0.2502 0.2550 0.4269 0.0435  -0.0186 -0.0577 87  GLY D O   
6699  N N   . VAL D 88  ? 0.2310 0.2354 0.4546 0.0371  -0.0277 -0.0628 88  VAL D N   
6700  C CA  . VAL D 88  ? 0.2438 0.2371 0.4657 0.0399  -0.0430 -0.0679 88  VAL D CA  
6701  C C   . VAL D 88  ? 0.2607 0.2332 0.4721 0.0398  -0.0509 -0.0708 88  VAL D C   
6702  O O   . VAL D 88  ? 0.2639 0.2320 0.4890 0.0352  -0.0491 -0.0706 88  VAL D O   
6703  C CB  . VAL D 88  ? 0.2457 0.2468 0.5056 0.0371  -0.0548 -0.0708 88  VAL D CB  
6704  C CG1 . VAL D 88  ? 0.2345 0.2528 0.4968 0.0373  -0.0453 -0.0658 88  VAL D CG1 
6705  C CG2 . VAL D 88  ? 0.2680 0.2703 0.5687 0.0306  -0.0607 -0.0718 88  VAL D CG2 
6706  N N   . ALA D 89  ? 0.2677 0.2251 0.4502 0.0440  -0.0582 -0.0726 89  ALA D N   
6707  C CA  . ALA D 89  ? 0.2904 0.2237 0.4536 0.0431  -0.0664 -0.0743 89  ALA D CA  
6708  C C   . ALA D 89  ? 0.3075 0.2288 0.4616 0.0449  -0.0815 -0.0783 89  ALA D C   
6709  O O   . ALA D 89  ? 0.3014 0.2299 0.4456 0.0499  -0.0803 -0.0789 89  ALA D O   
6710  C CB  . ALA D 89  ? 0.2904 0.2170 0.4190 0.0465  -0.0545 -0.0705 89  ALA D CB  
6711  N N   . CYS D 90  ? 0.3169 0.2182 0.4713 0.0392  -0.0956 -0.0800 90  CYS D N   
6712  C CA  . CYS D 90  ? 0.3367 0.2250 0.4823 0.0391  -0.1115 -0.0831 90  CYS D CA  
6713  C C   . CYS D 90  ? 0.3595 0.2260 0.4698 0.0402  -0.1141 -0.0836 90  CYS D C   
6714  O O   . CYS D 90  ? 0.3620 0.2217 0.4575 0.0399  -0.1055 -0.0815 90  CYS D O   
6715  C CB  . CYS D 90  ? 0.3500 0.2329 0.5216 0.0279  -0.1267 -0.0828 90  CYS D CB  
6716  S SG  . CYS D 90  ? 0.3240 0.2346 0.5479 0.0240  -0.1245 -0.0819 90  CYS D SG  
6717  N N   . SER D 91  ? 0.3560 0.2119 0.4542 0.0417  -0.1262 -0.0866 91  SER D N   
6718  C CA  . SER D 91  ? 0.3818 0.2163 0.4523 0.0415  -0.1320 -0.0877 91  SER D CA  
6719  C C   . SER D 91  ? 0.4052 0.2268 0.4763 0.0366  -0.1502 -0.0897 91  SER D C   
6720  O O   . SER D 91  ? 0.4005 0.2298 0.4785 0.0402  -0.1559 -0.0917 91  SER D O   
6721  C CB  . SER D 91  ? 0.3755 0.2142 0.4239 0.0508  -0.1223 -0.0891 91  SER D CB  
6722  O OG  . SER D 91  ? 0.3998 0.2196 0.4262 0.0510  -0.1278 -0.0908 91  SER D OG  
6723  N N   . LEU D 92  ? 0.3890 0.1910 0.4522 0.0276  -0.1594 -0.0884 92  LEU D N   
6724  C CA  . LEU D 92  ? 0.4138 0.2034 0.4769 0.0198  -0.1764 -0.0887 92  LEU D CA  
6725  C C   . LEU D 92  ? 0.4026 0.2076 0.4967 0.0136  -0.1830 -0.0871 92  LEU D C   
6726  O O   . LEU D 92  ? 0.4126 0.2165 0.5085 0.0125  -0.1949 -0.0883 92  LEU D O   
6727  C CB  . LEU D 92  ? 0.4287 0.2083 0.4678 0.0280  -0.1818 -0.0930 92  LEU D CB  
6728  C CG  . LEU D 92  ? 0.4385 0.2067 0.4514 0.0342  -0.1751 -0.0947 92  LEU D CG  
6729  C CD1 . LEU D 92  ? 0.4511 0.2128 0.4445 0.0418  -0.1791 -0.0990 92  LEU D CD1 
6730  C CD2 . LEU D 92  ? 0.4631 0.2118 0.4681 0.0249  -0.1808 -0.0927 92  LEU D CD2 
6731  N N   . GLY D 93  ? 0.4136 0.2344 0.5336 0.0092  -0.1749 -0.0842 93  GLY D N   
6732  C CA  . GLY D 93  ? 0.4006 0.2410 0.5566 0.0015  -0.1794 -0.0819 93  GLY D CA  
6733  C C   . GLY D 93  ? 0.3765 0.2357 0.5484 0.0125  -0.1772 -0.0849 93  GLY D C   
6734  O O   . GLY D 93  ? 0.3655 0.2437 0.5697 0.0066  -0.1816 -0.0829 93  GLY D O   
6735  N N   . SER D 94  ? 0.4031 0.2612 0.5541 0.0272  -0.1696 -0.0889 94  SER D N   
6736  C CA  . SER D 94  ? 0.3816 0.2572 0.5435 0.0376  -0.1662 -0.0915 94  SER D CA  
6737  C C   . SER D 94  ? 0.3554 0.2462 0.5143 0.0454  -0.1458 -0.0910 94  SER D C   
6738  O O   . SER D 94  ? 0.3590 0.2419 0.4923 0.0475  -0.1363 -0.0902 94  SER D O   
6739  C CB  . SER D 94  ? 0.3971 0.2619 0.5326 0.0448  -0.1743 -0.0948 94  SER D CB  
6740  O OG  . SER D 94  ? 0.3771 0.2581 0.5154 0.0545  -0.1675 -0.0967 94  SER D OG  
6741  N N   . ILE D 95  ? 0.3395 0.2533 0.5237 0.0485  -0.1385 -0.0906 95  ILE D N   
6742  C CA  . ILE D 95  ? 0.3159 0.2461 0.4938 0.0520  -0.1168 -0.0878 95  ILE D CA  
6743  C C   . ILE D 95  ? 0.3174 0.2436 0.4579 0.0582  -0.1081 -0.0877 95  ILE D C   
6744  O O   . ILE D 95  ? 0.3225 0.2477 0.4536 0.0622  -0.1137 -0.0900 95  ILE D O   
6745  C CB  . ILE D 95  ? 0.2926 0.2473 0.4993 0.0515  -0.1085 -0.0856 95  ILE D CB  
6746  C CG1 . ILE D 95  ? 0.2733 0.2403 0.4631 0.0528  -0.0851 -0.0803 95  ILE D CG1 
6747  C CG2 . ILE D 95  ? 0.2956 0.2536 0.5047 0.0548  -0.1174 -0.0874 95  ILE D CG2 
6748  C CD1 . ILE D 95  ? 0.2550 0.2424 0.4641 0.0506  -0.0735 -0.0755 95  ILE D CD1 
6749  N N   . ILE D 96  ? 0.3070 0.2303 0.4276 0.0583  -0.0948 -0.0846 96  ILE D N   
6750  C CA  . ILE D 96  ? 0.3044 0.2271 0.3964 0.0622  -0.0838 -0.0824 96  ILE D CA  
6751  C C   . ILE D 96  ? 0.2843 0.2217 0.3753 0.0622  -0.0670 -0.0776 96  ILE D C   
6752  O O   . ILE D 96  ? 0.2839 0.2246 0.3621 0.0657  -0.0639 -0.0788 96  ILE D O   
6753  C CB  . ILE D 96  ? 0.3234 0.2278 0.3935 0.0626  -0.0868 -0.0837 96  ILE D CB  
6754  C CG1 . ILE D 96  ? 0.3243 0.2234 0.3969 0.0588  -0.0823 -0.0813 96  ILE D CG1 
6755  C CG2 . ILE D 96  ? 0.3493 0.2367 0.4159 0.0631  -0.1060 -0.0890 96  ILE D CG2 
6756  C CD1 . ILE D 96  ? 0.3396 0.2256 0.3923 0.0606  -0.0831 -0.0825 96  ILE D CD1 
6757  N N   . ARG D 97  ? 0.3385 0.2851 0.4455 0.0586  -0.0599 -0.0740 97  ARG D N   
6758  C CA  . ARG D 97  ? 0.3255 0.2834 0.4329 0.0583  -0.0484 -0.0713 97  ARG D CA  
6759  C C   . ARG D 97  ? 0.3101 0.2826 0.4381 0.0551  -0.0420 -0.0678 97  ARG D C   
6760  O O   . ARG D 97  ? 0.3084 0.2812 0.4522 0.0519  -0.0432 -0.0663 97  ARG D O   
6761  C CB  . ARG D 97  ? 0.3312 0.2804 0.4312 0.0574  -0.0458 -0.0707 97  ARG D CB  
6762  C CG  . ARG D 97  ? 0.3196 0.2783 0.4195 0.0567  -0.0351 -0.0677 97  ARG D CG  
6763  C CD  . ARG D 97  ? 0.3289 0.2762 0.4182 0.0569  -0.0345 -0.0676 97  ARG D CD  
6764  N NE  . ARG D 97  ? 0.3447 0.2801 0.4175 0.0605  -0.0420 -0.0713 97  ARG D NE  
6765  C CZ  . ARG D 97  ? 0.3571 0.2804 0.4188 0.0615  -0.0439 -0.0720 97  ARG D CZ  
6766  N NH1 . ARG D 97  ? 0.3564 0.2762 0.4200 0.0592  -0.0389 -0.0693 97  ARG D NH1 
6767  N NH2 . ARG D 97  ? 0.3719 0.2860 0.4199 0.0652  -0.0514 -0.0757 97  ARG D NH2 
6768  N N   . LEU D 98  ? 0.2596 0.2434 0.3875 0.0556  -0.0355 -0.0663 98  LEU D N   
6769  C CA  . LEU D 98  ? 0.2479 0.2448 0.3926 0.0527  -0.0290 -0.0629 98  LEU D CA  
6770  C C   . LEU D 98  ? 0.2410 0.2429 0.3787 0.0515  -0.0191 -0.0603 98  LEU D C   
6771  O O   . LEU D 98  ? 0.2408 0.2435 0.3665 0.0536  -0.0170 -0.0602 98  LEU D O   
6772  C CB  . LEU D 98  ? 0.2474 0.2497 0.3975 0.0544  -0.0322 -0.0629 98  LEU D CB  
6773  C CG  . LEU D 98  ? 0.2389 0.2538 0.4052 0.0521  -0.0261 -0.0593 98  LEU D CG  
6774  C CD1 . LEU D 98  ? 0.2363 0.2568 0.4251 0.0486  -0.0272 -0.0577 98  LEU D CD1 
6775  C CD2 . LEU D 98  ? 0.2411 0.2590 0.4070 0.0552  -0.0292 -0.0592 98  LEU D CD2 
6776  N N   . ASN D 99  ? 0.2869 0.2913 0.4321 0.0482  -0.0135 -0.0582 99  ASN D N   
6777  C CA  . ASN D 99  ? 0.2823 0.2889 0.4202 0.0468  -0.0055 -0.0557 99  ASN D CA  
6778  C C   . ASN D 99  ? 0.2748 0.2909 0.4273 0.0429  0.0012  -0.0527 99  ASN D C   
6779  O O   . ASN D 99  ? 0.2727 0.2909 0.4377 0.0395  0.0040  -0.0517 99  ASN D O   
6780  C CB  . ASN D 99  ? 0.2864 0.2851 0.4173 0.0468  -0.0050 -0.0560 99  ASN D CB  
6781  C CG  . ASN D 99  ? 0.2840 0.2830 0.4037 0.0467  0.0010  -0.0538 99  ASN D CG  
6782  O OD1 . ASN D 99  ? 0.2798 0.2837 0.3954 0.0467  0.0042  -0.0523 99  ASN D OD1 
6783  N ND2 . ASN D 99  ? 0.2880 0.2803 0.4024 0.0469  0.0020  -0.0535 99  ASN D ND2 
6784  N N   . LEU D 100 ? 0.2254 0.2464 0.3759 0.0434  0.0039  -0.0512 100 LEU D N   
6785  C CA  . LEU D 100 ? 0.2216 0.2499 0.3841 0.0405  0.0096  -0.0486 100 LEU D CA  
6786  C C   . LEU D 100 ? 0.2194 0.2477 0.3714 0.0400  0.0153  -0.0463 100 LEU D C   
6787  O O   . LEU D 100 ? 0.2185 0.2510 0.3747 0.0397  0.0182  -0.0445 100 LEU D O   
6788  C CB  . LEU D 100 ? 0.2228 0.2565 0.3959 0.0422  0.0065  -0.0487 100 LEU D CB  
6789  C CG  . LEU D 100 ? 0.2248 0.2604 0.4132 0.0420  0.0006  -0.0502 100 LEU D CG  
6790  C CD1 . LEU D 100 ? 0.2271 0.2684 0.4252 0.0444  -0.0035 -0.0498 100 LEU D CD1 
6791  C CD2 . LEU D 100 ? 0.2228 0.2623 0.4268 0.0377  0.0047  -0.0489 100 LEU D CD2 
6792  N N   . THR D 101 ? 0.2296 0.2528 0.3684 0.0403  0.0161  -0.0462 101 THR D N   
6793  C CA  . THR D 101 ? 0.2278 0.2507 0.3576 0.0398  0.0205  -0.0438 101 THR D CA  
6794  C C   . THR D 101 ? 0.2257 0.2515 0.3655 0.0357  0.0264  -0.0418 101 THR D C   
6795  O O   . THR D 101 ? 0.2257 0.2513 0.3737 0.0331  0.0284  -0.0419 101 THR D O   
6796  C CB  . THR D 101 ? 0.2293 0.2466 0.3452 0.0412  0.0197  -0.0441 101 THR D CB  
6797  O OG1 . THR D 101 ? 0.2356 0.2490 0.3435 0.0450  0.0143  -0.0466 101 THR D OG1 
6798  C CG2 . THR D 101 ? 0.2278 0.2450 0.3341 0.0414  0.0227  -0.0419 101 THR D CG2 
6799  N N   . ASN D 102 ? 0.2331 0.2611 0.3721 0.0355  0.0294  -0.0399 102 ASN D N   
6800  C CA  . ASN D 102 ? 0.2330 0.2620 0.3783 0.0323  0.0352  -0.0380 102 ASN D CA  
6801  C C   . ASN D 102 ? 0.2345 0.2675 0.3971 0.0302  0.0375  -0.0384 102 ASN D C   
6802  O O   . ASN D 102 ? 0.2373 0.2697 0.4050 0.0274  0.0422  -0.0377 102 ASN D O   
6803  C CB  . ASN D 102 ? 0.2323 0.2569 0.3689 0.0307  0.0375  -0.0371 102 ASN D CB  
6804  C CG  . ASN D 102 ? 0.2328 0.2571 0.3698 0.0287  0.0425  -0.0350 102 ASN D CG  
6805  O OD1 . ASN D 102 ? 0.2347 0.2622 0.3809 0.0282  0.0451  -0.0345 102 ASN D OD1 
6806  N ND2 . ASN D 102 ? 0.2415 0.2620 0.3687 0.0282  0.0435  -0.0340 102 ASN D ND2 
6807  N N   . THR D 103 ? 0.2139 0.2513 0.3858 0.0319  0.0342  -0.0396 103 THR D N   
6808  C CA  . THR D 103 ? 0.2160 0.2591 0.4064 0.0306  0.0357  -0.0399 103 THR D CA  
6809  C C   . THR D 103 ? 0.2190 0.2682 0.4192 0.0314  0.0389  -0.0388 103 THR D C   
6810  O O   . THR D 103 ? 0.2219 0.2782 0.4389 0.0310  0.0405  -0.0389 103 THR D O   
6811  C CB  . THR D 103 ? 0.2162 0.2614 0.4133 0.0323  0.0294  -0.0417 103 THR D CB  
6812  O OG1 . THR D 103 ? 0.2146 0.2533 0.3995 0.0330  0.0254  -0.0432 103 THR D OG1 
6813  C CG2 . THR D 103 ? 0.2179 0.2690 0.4343 0.0302  0.0305  -0.0419 103 THR D CG2 
6814  N N   . GLY D 104 ? 0.2247 0.2722 0.4158 0.0328  0.0399  -0.0377 104 GLY D N   
6815  C CA  . GLY D 104 ? 0.2282 0.2811 0.4281 0.0342  0.0425  -0.0368 104 GLY D CA  
6816  C C   . GLY D 104 ? 0.2302 0.2901 0.4413 0.0375  0.0385  -0.0374 104 GLY D C   
6817  O O   . GLY D 104 ? 0.2342 0.3013 0.4589 0.0388  0.0405  -0.0370 104 GLY D O   
6818  N N   . ILE D 105 ? 0.2285 0.2868 0.4345 0.0394  0.0325  -0.0383 105 ILE D N   
6819  C CA  . ILE D 105 ? 0.2310 0.2953 0.4470 0.0429  0.0276  -0.0386 105 ILE D CA  
6820  C C   . ILE D 105 ? 0.2326 0.2976 0.4435 0.0463  0.0275  -0.0374 105 ILE D C   
6821  O O   . ILE D 105 ? 0.2306 0.2896 0.4252 0.0466  0.0285  -0.0368 105 ILE D O   
6822  C CB  . ILE D 105 ? 0.2296 0.2907 0.4404 0.0441  0.0209  -0.0402 105 ILE D CB  
6823  C CG1 . ILE D 105 ? 0.2277 0.2867 0.4415 0.0406  0.0210  -0.0413 105 ILE D CG1 
6824  C CG2 . ILE D 105 ? 0.2330 0.3006 0.4564 0.0475  0.0149  -0.0404 105 ILE D CG2 
6825  C CD1 . ILE D 105 ? 0.2276 0.2839 0.4397 0.0420  0.0137  -0.0433 105 ILE D CD1 
6826  N N   . GLU D 106 ? 0.2741 0.3470 0.4999 0.0490  0.0263  -0.0370 106 GLU D N   
6827  C CA  . GLU D 106 ? 0.2766 0.3507 0.4998 0.0530  0.0253  -0.0359 106 GLU D CA  
6828  C C   . GLU D 106 ? 0.2799 0.3590 0.5123 0.0569  0.0183  -0.0360 106 GLU D C   
6829  O O   . GLU D 106 ? 0.2830 0.3706 0.5346 0.0572  0.0163  -0.0362 106 GLU D O   
6830  C CB  . GLU D 106 ? 0.2801 0.3591 0.5133 0.0531  0.0304  -0.0351 106 GLU D CB  
6831  C CG  . GLU D 106 ? 0.2829 0.3623 0.5126 0.0571  0.0299  -0.0339 106 GLU D CG  
6832  C CD  . GLU D 106 ? 0.2874 0.3725 0.5297 0.0579  0.0343  -0.0337 106 GLU D CD  
6833  O OE1 . GLU D 106 ? 0.2868 0.3691 0.5258 0.0548  0.0399  -0.0338 106 GLU D OE1 
6834  O OE2 . GLU D 106 ? 0.2941 0.3866 0.5499 0.0620  0.0319  -0.0335 106 GLU D OE2 
6835  N N   . GLY D 107 ? 0.2416 0.3162 0.4611 0.0602  0.0144  -0.0357 107 GLY D N   
6836  C CA  . GLY D 107 ? 0.2456 0.3235 0.4722 0.0642  0.0069  -0.0357 107 GLY D CA  
6837  C C   . GLY D 107 ? 0.2459 0.3165 0.4542 0.0675  0.0038  -0.0355 107 GLY D C   
6838  O O   . GLY D 107 ? 0.2441 0.3099 0.4374 0.0679  0.0079  -0.0346 107 GLY D O   
6839  N N   . THR D 108 ? 0.2383 0.3085 0.4487 0.0700  -0.0037 -0.0362 108 THR D N   
6840  C CA  . THR D 108 ? 0.2409 0.3044 0.4359 0.0739  -0.0074 -0.0360 108 THR D CA  
6841  C C   . THR D 108 ? 0.2421 0.3013 0.4345 0.0737  -0.0142 -0.0385 108 THR D C   
6842  O O   . THR D 108 ? 0.2424 0.3056 0.4489 0.0716  -0.0181 -0.0396 108 THR D O   
6843  C CB  . THR D 108 ? 0.2476 0.3147 0.4493 0.0792  -0.0113 -0.0337 108 THR D CB  
6844  O OG1 . THR D 108 ? 0.2470 0.3174 0.4508 0.0796  -0.0051 -0.0319 108 THR D OG1 
6845  C CG2 . THR D 108 ? 0.2515 0.3108 0.4371 0.0835  -0.0147 -0.0332 108 THR D CG2 
6846  N N   . PHE D 109 ? 0.2513 0.3019 0.4256 0.0758  -0.0158 -0.0396 109 PHE D N   
6847  C CA  . PHE D 109 ? 0.2550 0.2996 0.4244 0.0766  -0.0235 -0.0426 109 PHE D CA  
6848  C C   . PHE D 109 ? 0.2638 0.3080 0.4381 0.0812  -0.0331 -0.0419 109 PHE D C   
6849  O O   . PHE D 109 ? 0.2695 0.3057 0.4340 0.0831  -0.0401 -0.0444 109 PHE D O   
6850  C CB  . PHE D 109 ? 0.2542 0.2894 0.4016 0.0765  -0.0207 -0.0449 109 PHE D CB  
6851  C CG  . PHE D 109 ? 0.2470 0.2821 0.3885 0.0722  -0.0127 -0.0449 109 PHE D CG  
6852  C CD1 . PHE D 109 ? 0.2428 0.2811 0.3945 0.0682  -0.0118 -0.0457 109 PHE D CD1 
6853  C CD2 . PHE D 109 ? 0.2451 0.2768 0.3716 0.0722  -0.0066 -0.0437 109 PHE D CD2 
6854  C CE1 . PHE D 109 ? 0.2375 0.2747 0.3832 0.0645  -0.0053 -0.0454 109 PHE D CE1 
6855  C CE2 . PHE D 109 ? 0.2397 0.2709 0.3610 0.0685  -0.0007 -0.0432 109 PHE D CE2 
6856  C CZ  . PHE D 109 ? 0.2361 0.2698 0.3666 0.0648  -0.0003 -0.0441 109 PHE D CZ  
6857  N N   . GLU D 110 ? 0.3196 0.3717 0.5082 0.0833  -0.0345 -0.0385 110 GLU D N   
6858  C CA  . GLU D 110 ? 0.3295 0.3814 0.5235 0.0877  -0.0450 -0.0369 110 GLU D CA  
6859  C C   . GLU D 110 ? 0.3338 0.3880 0.5410 0.0862  -0.0557 -0.0380 110 GLU D C   
6860  O O   . GLU D 110 ? 0.3446 0.3928 0.5473 0.0888  -0.0665 -0.0382 110 GLU D O   
6861  C CB  . GLU D 110 ? 0.3354 0.3958 0.5424 0.0905  -0.0442 -0.0330 110 GLU D CB  
6862  C CG  . GLU D 110 ? 0.3503 0.4108 0.5635 0.0952  -0.0561 -0.0305 110 GLU D CG  
6863  C CD  . GLU D 110 ? 0.3642 0.4164 0.5607 0.1001  -0.0556 -0.0286 110 GLU D CD  
6864  O OE1 . GLU D 110 ? 0.3601 0.4110 0.5473 0.1001  -0.0450 -0.0281 110 GLU D OE1 
6865  O OE2 . GLU D 110 ? 0.3666 0.4131 0.5589 0.1036  -0.0663 -0.0273 110 GLU D OE2 
6866  N N   . ASP D 111 ? 0.2837 0.3459 0.5069 0.0818  -0.0533 -0.0384 111 ASP D N   
6867  C CA  . ASP D 111 ? 0.2871 0.3527 0.5246 0.0794  -0.0627 -0.0389 111 ASP D CA  
6868  C C   . ASP D 111 ? 0.2820 0.3408 0.5114 0.0757  -0.0610 -0.0425 111 ASP D C   
6869  O O   . ASP D 111 ? 0.2811 0.3450 0.5252 0.0720  -0.0645 -0.0426 111 ASP D O   
6870  C CB  . ASP D 111 ? 0.2866 0.3674 0.5508 0.0772  -0.0623 -0.0364 111 ASP D CB  
6871  C CG  . ASP D 111 ? 0.2954 0.3832 0.5711 0.0813  -0.0687 -0.0331 111 ASP D CG  
6872  O OD1 . ASP D 111 ? 0.3053 0.3907 0.5813 0.0834  -0.0815 -0.0319 111 ASP D OD1 
6873  O OD2 . ASP D 111 ? 0.2938 0.3887 0.5776 0.0824  -0.0619 -0.0316 111 ASP D OD2 
6874  N N   . PHE D 112 ? 0.2694 0.3173 0.4763 0.0765  -0.0560 -0.0454 112 PHE D N   
6875  C CA  . PHE D 112 ? 0.2669 0.3069 0.4645 0.0738  -0.0558 -0.0492 112 PHE D CA  
6876  C C   . PHE D 112 ? 0.2767 0.3087 0.4715 0.0752  -0.0695 -0.0512 112 PHE D C   
6877  O O   . PHE D 112 ? 0.2855 0.3108 0.4694 0.0794  -0.0762 -0.0515 112 PHE D O   
6878  C CB  . PHE D 112 ? 0.2633 0.2953 0.4380 0.0744  -0.0475 -0.0515 112 PHE D CB  
6879  C CG  . PHE D 112 ? 0.2600 0.2862 0.4270 0.0712  -0.0454 -0.0549 112 PHE D CG  
6880  C CD1 . PHE D 112 ? 0.2522 0.2840 0.4287 0.0667  -0.0386 -0.0539 112 PHE D CD1 
6881  C CD2 . PHE D 112 ? 0.2664 0.2810 0.4161 0.0730  -0.0507 -0.0592 112 PHE D CD2 
6882  C CE1 . PHE D 112 ? 0.2503 0.2763 0.4198 0.0642  -0.0373 -0.0565 112 PHE D CE1 
6883  C CE2 . PHE D 112 ? 0.2650 0.2742 0.4078 0.0705  -0.0494 -0.0621 112 PHE D CE2 
6884  C CZ  . PHE D 112 ? 0.2567 0.2717 0.4097 0.0662  -0.0429 -0.0605 112 PHE D CZ  
6885  N N   . PRO D 113 ? 0.2865 0.3180 0.4914 0.0718  -0.0753 -0.0529 113 PRO D N   
6886  C CA  . PRO D 113 ? 0.3043 0.3248 0.5159 0.0727  -0.0965 -0.0600 113 PRO D CA  
6887  C C   . PRO D 113 ? 0.3126 0.3149 0.4979 0.0758  -0.1009 -0.0673 113 PRO D C   
6888  O O   . PRO D 113 ? 0.3174 0.3101 0.5000 0.0743  -0.1068 -0.0732 113 PRO D O   
6889  C CB  . PRO D 113 ? 0.3043 0.3301 0.5416 0.0670  -0.1023 -0.0611 113 PRO D CB  
6890  C CG  . PRO D 113 ? 0.2881 0.3190 0.5204 0.0643  -0.0844 -0.0590 113 PRO D CG  
6891  C CD  . PRO D 113 ? 0.2770 0.3149 0.4927 0.0669  -0.0677 -0.0521 113 PRO D CD  
6892  N N   . PHE D 114 ? 0.3149 0.3121 0.4795 0.0804  -0.0980 -0.0668 114 PHE D N   
6893  C CA  . PHE D 114 ? 0.3251 0.3062 0.4629 0.0839  -0.1019 -0.0737 114 PHE D CA  
6894  C C   . PHE D 114 ? 0.3487 0.3130 0.4855 0.0857  -0.1259 -0.0825 114 PHE D C   
6895  O O   . PHE D 114 ? 0.3566 0.3086 0.4786 0.0861  -0.1304 -0.0888 114 PHE D O   
6896  C CB  . PHE D 114 ? 0.3271 0.3058 0.4462 0.0883  -0.0966 -0.0716 114 PHE D CB  
6897  C CG  . PHE D 114 ? 0.3082 0.2990 0.4260 0.0863  -0.0759 -0.0632 114 PHE D CG  
6898  C CD1 . PHE D 114 ? 0.3013 0.2919 0.4074 0.0846  -0.0657 -0.0653 114 PHE D CD1 
6899  C CD2 . PHE D 114 ? 0.3051 0.3059 0.4364 0.0872  -0.0739 -0.0578 114 PHE D CD2 
6900  C CE1 . PHE D 114 ? 0.2915 0.2905 0.3989 0.0835  -0.0540 -0.0620 114 PHE D CE1 
6901  C CE2 . PHE D 114 ? 0.2957 0.3040 0.4276 0.0866  -0.0616 -0.0552 114 PHE D CE2 
6902  C CZ  . PHE D 114 ? 0.2889 0.2958 0.4085 0.0845  -0.0519 -0.0572 114 PHE D CZ  
6903  N N   . SER D 115 ? 0.3219 0.2849 0.4727 0.0862  -0.1417 -0.0813 115 SER D N   
6904  C CA  . SER D 115 ? 0.3482 0.2921 0.4946 0.0868  -0.1662 -0.0872 115 SER D CA  
6905  C C   . SER D 115 ? 0.3501 0.2908 0.5122 0.0813  -0.1740 -0.0895 115 SER D C   
6906  O O   . SER D 115 ? 0.3731 0.2929 0.5242 0.0814  -0.1928 -0.0950 115 SER D O   
6907  C CB  . SER D 115 ? 0.3614 0.3083 0.5197 0.0861  -0.1797 -0.0815 115 SER D CB  
6908  O OG  . SER D 115 ? 0.3632 0.3098 0.5060 0.0916  -0.1751 -0.0795 115 SER D OG  
6909  N N   . SER D 116 ? 0.3211 0.2799 0.5065 0.0764  -0.1603 -0.0850 116 SER D N   
6910  C CA  . SER D 116 ? 0.3230 0.2813 0.5290 0.0702  -0.1681 -0.0854 116 SER D CA  
6911  C C   . SER D 116 ? 0.3174 0.2673 0.5119 0.0701  -0.1613 -0.0908 116 SER D C   
6912  O O   . SER D 116 ? 0.3226 0.2671 0.5314 0.0654  -0.1704 -0.0920 116 SER D O   
6913  C CB  . SER D 116 ? 0.3069 0.2907 0.5469 0.0642  -0.1589 -0.0766 116 SER D CB  
6914  O OG  . SER D 116 ? 0.3075 0.3030 0.5538 0.0655  -0.1587 -0.0707 116 SER D OG  
6915  N N   . LEU D 117 ? 0.3310 0.2813 0.4996 0.0739  -0.1454 -0.0921 117 LEU D N   
6916  C CA  . LEU D 117 ? 0.3238 0.2722 0.4795 0.0727  -0.1344 -0.0930 117 LEU D CA  
6917  C C   . LEU D 117 ? 0.3359 0.2708 0.4555 0.0777  -0.1341 -0.0963 117 LEU D C   
6918  O O   . LEU D 117 ? 0.3236 0.2647 0.4257 0.0786  -0.1156 -0.0924 117 LEU D O   
6919  C CB  . LEU D 117 ? 0.2984 0.2654 0.4581 0.0702  -0.1098 -0.0855 117 LEU D CB  
6920  C CG  . LEU D 117 ? 0.2861 0.2700 0.4769 0.0662  -0.1051 -0.0799 117 LEU D CG  
6921  C CD1 . LEU D 117 ? 0.2657 0.2629 0.4506 0.0643  -0.0819 -0.0723 117 LEU D CD1 
6922  C CD2 . LEU D 117 ? 0.2922 0.2745 0.5114 0.0612  -0.1181 -0.0821 117 LEU D CD2 
6923  N N   . PRO D 118 ? 0.3623 0.2780 0.4698 0.0802  -0.1538 -0.1016 118 PRO D N   
6924  C CA  . PRO D 118 ? 0.3757 0.2795 0.4486 0.0851  -0.1508 -0.1029 118 PRO D CA  
6925  C C   . PRO D 118 ? 0.3689 0.2730 0.4288 0.0832  -0.1351 -0.1002 118 PRO D C   
6926  O O   . PRO D 118 ? 0.3671 0.2713 0.4060 0.0855  -0.1229 -0.0985 118 PRO D O   
6927  C CB  . PRO D 118 ? 0.4074 0.2886 0.4714 0.0866  -0.1743 -0.1067 118 PRO D CB  
6928  C CG  . PRO D 118 ? 0.4089 0.2888 0.5013 0.0802  -0.1866 -0.1060 118 PRO D CG  
6929  C CD  . PRO D 118 ? 0.3814 0.2843 0.5058 0.0774  -0.1783 -0.1042 118 PRO D CD  
6930  N N   . ASN D 119 ? 0.4032 0.3067 0.4764 0.0785  -0.1355 -0.0991 119 ASN D N   
6931  C CA  . ASN D 119 ? 0.4037 0.3021 0.4630 0.0768  -0.1252 -0.0971 119 ASN D CA  
6932  C C   . ASN D 119 ? 0.3775 0.2922 0.4412 0.0742  -0.1040 -0.0913 119 ASN D C   
6933  O O   . ASN D 119 ? 0.3765 0.2876 0.4349 0.0718  -0.0970 -0.0891 119 ASN D O   
6934  C CB  . ASN D 119 ? 0.4206 0.3044 0.4869 0.0724  -0.1379 -0.0984 119 ASN D CB  
6935  C CG  . ASN D 119 ? 0.4516 0.3140 0.5041 0.0729  -0.1561 -0.1019 119 ASN D CG  
6936  O OD1 . ASN D 119 ? 0.4634 0.3183 0.4928 0.0774  -0.1555 -0.1037 119 ASN D OD1 
6937  N ND2 . ASN D 119 ? 0.4662 0.3184 0.5327 0.0666  -0.1714 -0.1020 119 ASN D ND2 
6938  N N   . LEU D 120 ? 0.3336 0.2638 0.4049 0.0741  -0.0937 -0.0878 120 LEU D N   
6939  C CA  . LEU D 120 ? 0.3145 0.2575 0.3885 0.0719  -0.0773 -0.0827 120 LEU D CA  
6940  C C   . LEU D 120 ? 0.3193 0.2605 0.3748 0.0753  -0.0732 -0.0843 120 LEU D C   
6941  O O   . LEU D 120 ? 0.3263 0.2654 0.3687 0.0792  -0.0749 -0.0863 120 LEU D O   
6942  C CB  . LEU D 120 ? 0.2997 0.2573 0.3852 0.0716  -0.0707 -0.0797 120 LEU D CB  
6943  C CG  . LEU D 120 ? 0.2891 0.2554 0.3986 0.0678  -0.0695 -0.0762 120 LEU D CG  
6944  C CD1 . LEU D 120 ? 0.2780 0.2576 0.3951 0.0682  -0.0622 -0.0730 120 LEU D CD1 
6945  C CD2 . LEU D 120 ? 0.2826 0.2511 0.4008 0.0640  -0.0639 -0.0742 120 LEU D CD2 
6946  N N   . THR D 121 ? 0.3078 0.2495 0.3627 0.0738  -0.0681 -0.0832 121 THR D N   
6947  C CA  . THR D 121 ? 0.3112 0.2527 0.3522 0.0767  -0.0643 -0.0841 121 THR D CA  
6948  C C   . THR D 121 ? 0.2958 0.2491 0.3420 0.0745  -0.0535 -0.0805 121 THR D C   
6949  O O   . THR D 121 ? 0.2953 0.2520 0.3327 0.0766  -0.0498 -0.0804 121 THR D O   
6950  C CB  . THR D 121 ? 0.3271 0.2550 0.3587 0.0779  -0.0701 -0.0865 121 THR D CB  
6951  O OG1 . THR D 121 ? 0.3216 0.2493 0.3621 0.0741  -0.0667 -0.0841 121 THR D OG1 
6952  C CG2 . THR D 121 ? 0.3449 0.2581 0.3713 0.0786  -0.0814 -0.0895 121 THR D CG2 
6953  N N   . PHE D 122 ? 0.3056 0.2646 0.3660 0.0703  -0.0487 -0.0773 122 PHE D N   
6954  C CA  . PHE D 122 ? 0.2928 0.2612 0.3575 0.0678  -0.0388 -0.0736 122 PHE D CA  
6955  C C   . PHE D 122 ? 0.2803 0.2586 0.3593 0.0648  -0.0339 -0.0703 122 PHE D C   
6956  O O   . PHE D 122 ? 0.2780 0.2569 0.3704 0.0625  -0.0356 -0.0697 122 PHE D O   
6957  C CB  . PHE D 122 ? 0.2941 0.2578 0.3601 0.0661  -0.0371 -0.0726 122 PHE D CB  
6958  C CG  . PHE D 122 ? 0.2826 0.2542 0.3522 0.0635  -0.0277 -0.0686 122 PHE D CG  
6959  C CD1 . PHE D 122 ? 0.2714 0.2507 0.3546 0.0598  -0.0219 -0.0652 122 PHE D CD1 
6960  C CD2 . PHE D 122 ? 0.2843 0.2552 0.3439 0.0650  -0.0252 -0.0684 122 PHE D CD2 
6961  C CE1 . PHE D 122 ? 0.2631 0.2479 0.3476 0.0576  -0.0140 -0.0616 122 PHE D CE1 
6962  C CE2 . PHE D 122 ? 0.2753 0.2518 0.3372 0.0626  -0.0176 -0.0648 122 PHE D CE2 
6963  C CZ  . PHE D 122 ? 0.2652 0.2480 0.3385 0.0589  -0.0120 -0.0613 122 PHE D CZ  
6964  N N   . VAL D 123 ? 0.2470 0.2328 0.3239 0.0648  -0.0280 -0.0681 123 VAL D N   
6965  C CA  . VAL D 123 ? 0.2373 0.2318 0.3261 0.0624  -0.0231 -0.0647 123 VAL D CA  
6966  C C   . VAL D 123 ? 0.2296 0.2293 0.3161 0.0605  -0.0143 -0.0609 123 VAL D C   
6967  O O   . VAL D 123 ? 0.2308 0.2302 0.3065 0.0620  -0.0125 -0.0607 123 VAL D O   
6968  C CB  . VAL D 123 ? 0.2398 0.2355 0.3276 0.0650  -0.0263 -0.0656 123 VAL D CB  
6969  C CG1 . VAL D 123 ? 0.2314 0.2357 0.3295 0.0633  -0.0204 -0.0616 123 VAL D CG1 
6970  C CG2 . VAL D 123 ? 0.2476 0.2378 0.3398 0.0665  -0.0359 -0.0689 123 VAL D CG2 
6971  N N   . ASP D 124 ? 0.2386 0.2425 0.3352 0.0571  -0.0093 -0.0580 124 ASP D N   
6972  C CA  . ASP D 124 ? 0.2323 0.2403 0.3274 0.0550  -0.0019 -0.0542 124 ASP D CA  
6973  C C   . ASP D 124 ? 0.2266 0.2414 0.3356 0.0525  0.0016  -0.0517 124 ASP D C   
6974  O O   . ASP D 124 ? 0.2242 0.2410 0.3447 0.0497  0.0026  -0.0514 124 ASP D O   
6975  C CB  . ASP D 124 ? 0.2321 0.2370 0.3233 0.0537  0.0005  -0.0536 124 ASP D CB  
6976  C CG  . ASP D 124 ? 0.2277 0.2349 0.3139 0.0524  0.0065  -0.0502 124 ASP D CG  
6977  O OD1 . ASP D 124 ? 0.2230 0.2352 0.3143 0.0509  0.0101  -0.0476 124 ASP D OD1 
6978  O OD2 . ASP D 124 ? 0.2298 0.2336 0.3075 0.0532  0.0069  -0.0502 124 ASP D OD2 
6979  N N   . LEU D 125 ? 0.2193 0.2375 0.3278 0.0535  0.0035  -0.0499 125 LEU D N   
6980  C CA  . LEU D 125 ? 0.2158 0.2403 0.3366 0.0518  0.0066  -0.0476 125 LEU D CA  
6981  C C   . LEU D 125 ? 0.2129 0.2388 0.3284 0.0509  0.0124  -0.0443 125 LEU D C   
6982  O O   . LEU D 125 ? 0.2124 0.2419 0.3318 0.0515  0.0143  -0.0425 125 LEU D O   
6983  C CB  . LEU D 125 ? 0.2187 0.2455 0.3451 0.0547  0.0027  -0.0482 125 LEU D CB  
6984  C CG  . LEU D 125 ? 0.2228 0.2473 0.3543 0.0560  -0.0047 -0.0516 125 LEU D CG  
6985  C CD1 . LEU D 125 ? 0.2271 0.2523 0.3601 0.0597  -0.0095 -0.0522 125 LEU D CD1 
6986  C CD2 . LEU D 125 ? 0.2207 0.2488 0.3694 0.0528  -0.0052 -0.0517 125 LEU D CD2 
6987  N N   . SER D 126 ? 0.2426 0.2655 0.3494 0.0496  0.0147  -0.0437 126 SER D N   
6988  C CA  . SER D 126 ? 0.2397 0.2628 0.3402 0.0490  0.0189  -0.0409 126 SER D CA  
6989  C C   . SER D 126 ? 0.2367 0.2627 0.3464 0.0453  0.0230  -0.0393 126 SER D C   
6990  O O   . SER D 126 ? 0.2389 0.2660 0.3586 0.0428  0.0235  -0.0401 126 SER D O   
6991  C CB  . SER D 126 ? 0.2407 0.2593 0.3285 0.0497  0.0189  -0.0410 126 SER D CB  
6992  O OG  . SER D 126 ? 0.2408 0.2573 0.3299 0.0483  0.0183  -0.0422 126 SER D OG  
6993  N N   . MET D 127 ? 0.2599 0.2867 0.3667 0.0448  0.0261  -0.0372 127 MET D N   
6994  C CA  . MET D 127 ? 0.2584 0.2866 0.3726 0.0413  0.0304  -0.0357 127 MET D CA  
6995  C C   . MET D 127 ? 0.2596 0.2922 0.3894 0.0404  0.0315  -0.0360 127 MET D C   
6996  O O   . MET D 127 ? 0.2604 0.2939 0.3997 0.0375  0.0339  -0.0362 127 MET D O   
6997  C CB  . MET D 127 ? 0.2585 0.2838 0.3708 0.0386  0.0320  -0.0357 127 MET D CB  
6998  C CG  . MET D 127 ? 0.2613 0.2836 0.3611 0.0392  0.0320  -0.0348 127 MET D CG  
6999  S SD  . MET D 127 ? 0.2621 0.2817 0.3618 0.0360  0.0349  -0.0341 127 MET D SD  
7000  C CE  . MET D 127 ? 0.2741 0.2914 0.3717 0.0374  0.0318  -0.0362 127 MET D CE  
7001  N N   . ASN D 128 ? 0.2324 0.2679 0.3651 0.0433  0.0298  -0.0359 128 ASN D N   
7002  C CA  . ASN D 128 ? 0.2344 0.2753 0.3828 0.0435  0.0302  -0.0361 128 ASN D CA  
7003  C C   . ASN D 128 ? 0.2365 0.2797 0.3851 0.0463  0.0308  -0.0347 128 ASN D C   
7004  O O   . ASN D 128 ? 0.2377 0.2782 0.3751 0.0471  0.0317  -0.0335 128 ASN D O   
7005  C CB  . ASN D 128 ? 0.2355 0.2782 0.3906 0.0449  0.0256  -0.0381 128 ASN D CB  
7006  C CG  . ASN D 128 ? 0.2341 0.2749 0.3922 0.0419  0.0255  -0.0395 128 ASN D CG  
7007  O OD1 . ASN D 128 ? 0.2341 0.2769 0.4026 0.0389  0.0290  -0.0391 128 ASN D OD1 
7008  N ND2 . ASN D 128 ? 0.2337 0.2706 0.3828 0.0431  0.0215  -0.0411 128 ASN D ND2 
7009  N N   . ARG D 129 ? 0.2557 0.3045 0.4180 0.0480  0.0300  -0.0349 129 ARG D N   
7010  C CA  . ARG D 129 ? 0.2586 0.3104 0.4235 0.0513  0.0302  -0.0336 129 ARG D CA  
7011  C C   . ARG D 129 ? 0.2611 0.3153 0.4282 0.0557  0.0250  -0.0341 129 ARG D C   
7012  O O   . ARG D 129 ? 0.2654 0.3250 0.4442 0.0585  0.0239  -0.0336 129 ARG D O   
7013  C CB  . ARG D 129 ? 0.2616 0.3185 0.4419 0.0504  0.0339  -0.0332 129 ARG D CB  
7014  C CG  . ARG D 129 ? 0.2625 0.3170 0.4432 0.0460  0.0389  -0.0331 129 ARG D CG  
7015  C CD  . ARG D 129 ? 0.2655 0.3237 0.4564 0.0463  0.0432  -0.0325 129 ARG D CD  
7016  N NE  . ARG D 129 ? 0.2754 0.3313 0.4580 0.0481  0.0437  -0.0313 129 ARG D NE  
7017  C CZ  . ARG D 129 ? 0.2863 0.3465 0.4758 0.0519  0.0431  -0.0309 129 ARG D CZ  
7018  N NH1 . ARG D 129 ? 0.2893 0.3570 0.4948 0.0545  0.0416  -0.0316 129 ARG D NH1 
7019  N NH2 . ARG D 129 ? 0.2838 0.3411 0.4649 0.0532  0.0439  -0.0297 129 ARG D NH2 
7020  N N   . PHE D 130 ? 0.2248 0.2750 0.3813 0.0567  0.0216  -0.0350 130 PHE D N   
7021  C CA  . PHE D 130 ? 0.2281 0.2789 0.3846 0.0611  0.0165  -0.0354 130 PHE D CA  
7022  C C   . PHE D 130 ? 0.2304 0.2796 0.3774 0.0650  0.0173  -0.0334 130 PHE D C   
7023  O O   . PHE D 130 ? 0.2287 0.2734 0.3614 0.0646  0.0201  -0.0325 130 PHE D O   
7024  C CB  . PHE D 130 ? 0.2275 0.2733 0.3751 0.0611  0.0128  -0.0375 130 PHE D CB  
7025  C CG  . PHE D 130 ? 0.2265 0.2741 0.3855 0.0584  0.0104  -0.0396 130 PHE D CG  
7026  C CD1 . PHE D 130 ? 0.2294 0.2826 0.4051 0.0596  0.0062  -0.0400 130 PHE D CD1 
7027  C CD2 . PHE D 130 ? 0.2234 0.2673 0.3771 0.0549  0.0119  -0.0408 130 PHE D CD2 
7028  C CE1 . PHE D 130 ? 0.2288 0.2838 0.4159 0.0570  0.0040  -0.0416 130 PHE D CE1 
7029  C CE2 . PHE D 130 ? 0.2228 0.2679 0.3871 0.0526  0.0098  -0.0425 130 PHE D CE2 
7030  C CZ  . PHE D 130 ? 0.2253 0.2760 0.4065 0.0534  0.0060  -0.0429 130 PHE D CZ  
7031  N N   . SER D 131 ? 0.2268 0.2800 0.3826 0.0690  0.0146  -0.0326 131 SER D N   
7032  C CA  . SER D 131 ? 0.2301 0.2819 0.3787 0.0734  0.0152  -0.0304 131 SER D CA  
7033  C C   . SER D 131 ? 0.2351 0.2855 0.3830 0.0780  0.0096  -0.0302 131 SER D C   
7034  O O   . SER D 131 ? 0.2367 0.2894 0.3945 0.0782  0.0042  -0.0318 131 SER D O   
7035  C CB  . SER D 131 ? 0.2324 0.2898 0.3929 0.0744  0.0172  -0.0292 131 SER D CB  
7036  O OG  . SER D 131 ? 0.2358 0.3001 0.4156 0.0755  0.0136  -0.0297 131 SER D OG  
7037  N N   . GLY D 132 ? 0.2383 0.2843 0.3747 0.0817  0.0106  -0.0282 132 GLY D N   
7038  C CA  . GLY D 132 ? 0.2442 0.2869 0.3785 0.0860  0.0055  -0.0278 132 GLY D CA  
7039  C C   . GLY D 132 ? 0.2443 0.2781 0.3612 0.0857  0.0073  -0.0284 132 GLY D C   
7040  O O   . GLY D 132 ? 0.2410 0.2717 0.3476 0.0837  0.0134  -0.0272 132 GLY D O   
7041  N N   . THR D 133 ? 0.2472 0.2770 0.3619 0.0875  0.0011  -0.0307 133 THR D N   
7042  C CA  . THR D 133 ? 0.2493 0.2710 0.3487 0.0873  0.0011  -0.0331 133 THR D CA  
7043  C C   . THR D 133 ? 0.2492 0.2685 0.3447 0.0854  -0.0038 -0.0380 133 THR D C   
7044  O O   . THR D 133 ? 0.2480 0.2711 0.3540 0.0844  -0.0078 -0.0392 133 THR D O   
7045  C CB  . THR D 133 ? 0.2580 0.2749 0.3536 0.0922  -0.0034 -0.0329 133 THR D CB  
7046  O OG1 . THR D 133 ? 0.2637 0.2830 0.3704 0.0955  -0.0124 -0.0328 133 THR D OG1 
7047  C CG2 . THR D 133 ? 0.2583 0.2756 0.3553 0.0937  0.0024  -0.0283 133 THR D CG2 
7048  N N   . ILE D 134 ? 0.2526 0.2658 0.3331 0.0849  -0.0037 -0.0412 134 ILE D N   
7049  C CA  . ILE D 134 ? 0.2547 0.2645 0.3287 0.0840  -0.0088 -0.0461 134 ILE D CA  
7050  C C   . ILE D 134 ? 0.2654 0.2692 0.3334 0.0887  -0.0177 -0.0493 134 ILE D C   
7051  O O   . ILE D 134 ? 0.2722 0.2703 0.3265 0.0914  -0.0182 -0.0505 134 ILE D O   
7052  C CB  . ILE D 134 ? 0.2529 0.2601 0.3139 0.0815  -0.0046 -0.0477 134 ILE D CB  
7053  C CG1 . ILE D 134 ? 0.2481 0.2595 0.3146 0.0772  0.0029  -0.0441 134 ILE D CG1 
7054  C CG2 . ILE D 134 ? 0.2612 0.2647 0.3153 0.0817  -0.0105 -0.0527 134 ILE D CG2 
7055  C CD1 . ILE D 134 ? 0.2465 0.2559 0.3028 0.0749  0.0065  -0.0448 134 ILE D CD1 
7056  N N   . SER D 135 ? 0.2865 0.2909 0.3645 0.0897  -0.0253 -0.0505 135 SER D N   
7057  C CA  . SER D 135 ? 0.2983 0.2956 0.3717 0.0942  -0.0357 -0.0528 135 SER D CA  
7058  C C   . SER D 135 ? 0.3065 0.2942 0.3596 0.0955  -0.0392 -0.0584 135 SER D C   
7059  O O   . SER D 135 ? 0.3027 0.2909 0.3514 0.0926  -0.0366 -0.0608 135 SER D O   
7060  C CB  . SER D 135 ? 0.3000 0.3002 0.3901 0.0939  -0.0440 -0.0526 135 SER D CB  
7061  O OG  . SER D 135 ? 0.3127 0.3046 0.3979 0.0980  -0.0559 -0.0541 135 SER D OG  
7062  N N   . PRO D 136 ? 0.3146 0.2928 0.3542 0.1003  -0.0455 -0.0601 136 PRO D N   
7063  C CA  . PRO D 136 ? 0.3258 0.2936 0.3451 0.1023  -0.0499 -0.0655 136 PRO D CA  
7064  C C   . PRO D 136 ? 0.3288 0.2931 0.3512 0.1011  -0.0578 -0.0693 136 PRO D C   
7065  O O   . PRO D 136 ? 0.3354 0.2935 0.3439 0.1015  -0.0592 -0.0734 136 PRO D O   
7066  C CB  . PRO D 136 ? 0.3416 0.2979 0.3473 0.1078  -0.0566 -0.0658 136 PRO D CB  
7067  C CG  . PRO D 136 ? 0.3359 0.2985 0.3519 0.1084  -0.0517 -0.0602 136 PRO D CG  
7068  C CD  . PRO D 136 ? 0.3214 0.2970 0.3620 0.1043  -0.0486 -0.0566 136 PRO D CD  
7069  N N   . GLU D 137 ? 0.3769 0.3453 0.4184 0.0996  -0.0630 -0.0674 137 GLU D N   
7070  C CA  . GLU D 137 ? 0.3803 0.3447 0.4266 0.0981  -0.0714 -0.0705 137 GLU D CA  
7071  C C   . GLU D 137 ? 0.3756 0.3434 0.4212 0.0943  -0.0655 -0.0727 137 GLU D C   
7072  O O   . GLU D 137 ? 0.3821 0.3435 0.4256 0.0935  -0.0722 -0.0762 137 GLU D O   
7073  C CB  . GLU D 137 ? 0.3761 0.3477 0.4469 0.0965  -0.0766 -0.0664 137 GLU D CB  
7074  C CG  . GLU D 137 ? 0.3878 0.3577 0.4632 0.1012  -0.0869 -0.0647 137 GLU D CG  
7075  C CD  . GLU D 137 ? 0.4234 0.3765 0.4899 0.1068  -0.1113 -0.0734 137 GLU D CD  
7076  O OE1 . GLU D 137 ? 0.4423 0.3798 0.4817 0.1116  -0.1172 -0.0800 137 GLU D OE1 
7077  O OE2 . GLU D 137 ? 0.4413 0.3960 0.5265 0.1057  -0.1247 -0.0725 137 GLU D OE2 
7078  N N   . TRP D 138 ? 0.3059 0.2826 0.3530 0.0917  -0.0539 -0.0702 138 TRP D N   
7079  C CA  . TRP D 138 ? 0.3000 0.2791 0.3457 0.0884  -0.0491 -0.0713 138 TRP D CA  
7080  C C   . TRP D 138 ? 0.3117 0.2817 0.3384 0.0910  -0.0528 -0.0757 138 TRP D C   
7081  O O   . TRP D 138 ? 0.3121 0.2806 0.3379 0.0894  -0.0536 -0.0776 138 TRP D O   
7082  C CB  . TRP D 138 ? 0.2881 0.2760 0.3367 0.0855  -0.0375 -0.0672 138 TRP D CB  
7083  C CG  . TRP D 138 ? 0.2771 0.2738 0.3445 0.0822  -0.0329 -0.0629 138 TRP D CG  
7084  C CD1 . TRP D 138 ? 0.2734 0.2751 0.3483 0.0827  -0.0288 -0.0587 138 TRP D CD1 
7085  C CD2 . TRP D 138 ? 0.2702 0.2710 0.3506 0.0783  -0.0318 -0.0623 138 TRP D CD2 
7086  N NE1 . TRP D 138 ? 0.2652 0.2744 0.3566 0.0796  -0.0253 -0.0555 138 TRP D NE1 
7087  C CE2 . TRP D 138 ? 0.2628 0.2717 0.3579 0.0767  -0.0269 -0.0577 138 TRP D CE2 
7088  C CE3 . TRP D 138 ? 0.2706 0.2686 0.3514 0.0763  -0.0346 -0.0650 138 TRP D CE3 
7089  C CZ2 . TRP D 138 ? 0.2560 0.2705 0.3656 0.0730  -0.0244 -0.0561 138 TRP D CZ2 
7090  C CZ3 . TRP D 138 ? 0.2632 0.2662 0.3587 0.0725  -0.0320 -0.0632 138 TRP D CZ3 
7091  C CH2 . TRP D 138 ? 0.2559 0.2674 0.3656 0.0708  -0.0268 -0.0588 138 TRP D CH2 
7092  N N   . GLY D 139 ? 0.3371 0.3003 0.3484 0.0953  -0.0548 -0.0770 139 GLY D N   
7093  C CA  . GLY D 139 ? 0.3513 0.3051 0.3445 0.0984  -0.0579 -0.0808 139 GLY D CA  
7094  C C   . GLY D 139 ? 0.3654 0.3072 0.3538 0.1000  -0.0695 -0.0850 139 GLY D C   
7095  O O   . GLY D 139 ? 0.3794 0.3120 0.3531 0.1024  -0.0719 -0.0881 139 GLY D O   
7096  N N   . ARG D 140 ? 0.3904 0.3310 0.3914 0.0985  -0.0768 -0.0847 140 ARG D N   
7097  C CA  . ARG D 140 ? 0.4071 0.3347 0.4045 0.1003  -0.0915 -0.0896 140 ARG D CA  
7098  C C   . ARG D 140 ? 0.4031 0.3305 0.4067 0.0962  -0.0907 -0.0899 140 ARG D C   
7099  O O   . ARG D 140 ? 0.4316 0.3457 0.4287 0.0991  -0.1057 -0.0957 140 ARG D O   
7100  C CB  . ARG D 140 ? 0.4169 0.3426 0.4279 0.1031  -0.1080 -0.0928 140 ARG D CB  
7101  C CG  . ARG D 140 ? 0.4392 0.3599 0.4407 0.1086  -0.1135 -0.0934 140 ARG D CG  
7102  C CD  . ARG D 140 ? 0.4701 0.3775 0.4754 0.1127  -0.1382 -0.0987 140 ARG D CD  
7103  N NE  . ARG D 140 ? 0.4525 0.3730 0.4905 0.1078  -0.1382 -0.0943 140 ARG D NE  
7104  C CZ  . ARG D 140 ? 0.4598 0.3752 0.5143 0.1056  -0.1548 -0.0964 140 ARG D CZ  
7105  N NH1 . ARG D 140 ? 0.4949 0.3887 0.5347 0.1077  -0.1751 -0.1038 140 ARG D NH1 
7106  N NH2 . ARG D 140 ? 0.4372 0.3694 0.5234 0.1006  -0.1507 -0.0895 140 ARG D NH2 
7107  N N   . PHE D 141 ? 0.3302 0.2696 0.3442 0.0929  -0.0806 -0.0872 141 PHE D N   
7108  C CA  . PHE D 141 ? 0.3285 0.2670 0.3479 0.0900  -0.0811 -0.0881 141 PHE D CA  
7109  C C   . PHE D 141 ? 0.3412 0.2721 0.3427 0.0930  -0.0807 -0.0908 141 PHE D C   
7110  O O   . PHE D 141 ? 0.3346 0.2724 0.3341 0.0929  -0.0724 -0.0895 141 PHE D O   
7111  C CB  . PHE D 141 ? 0.3092 0.2615 0.3446 0.0857  -0.0713 -0.0843 141 PHE D CB  
7112  C CG  . PHE D 141 ? 0.2986 0.2585 0.3539 0.0829  -0.0710 -0.0812 141 PHE D CG  
7113  C CD1 . PHE D 141 ? 0.3019 0.2574 0.3695 0.0811  -0.0797 -0.0817 141 PHE D CD1 
7114  C CD2 . PHE D 141 ? 0.2869 0.2578 0.3493 0.0821  -0.0624 -0.0773 141 PHE D CD2 
7115  C CE1 . PHE D 141 ? 0.2936 0.2580 0.3828 0.0792  -0.0803 -0.0787 141 PHE D CE1 
7116  C CE2 . PHE D 141 ? 0.2792 0.2576 0.3608 0.0803  -0.0619 -0.0739 141 PHE D CE2 
7117  C CZ  . PHE D 141 ? 0.2819 0.2581 0.3774 0.0788  -0.0702 -0.0741 141 PHE D CZ  
7118  N N   . SER D 142 ? 0.3554 0.2711 0.3443 0.0954  -0.0901 -0.0944 142 SER D N   
7119  C CA  . SER D 142 ? 0.3713 0.2784 0.3429 0.0990  -0.0897 -0.0973 142 SER D CA  
7120  C C   . SER D 142 ? 0.3679 0.2771 0.3433 0.0975  -0.0866 -0.0973 142 SER D C   
7121  O O   . SER D 142 ? 0.3714 0.2817 0.3389 0.1001  -0.0816 -0.0981 142 SER D O   
7122  C CB  . SER D 142 ? 0.3965 0.2847 0.3536 0.1008  -0.1006 -0.1013 142 SER D CB  
7123  O OG  . SER D 142 ? 0.4011 0.2815 0.3655 0.0971  -0.1092 -0.1019 142 SER D OG  
7124  N N   . LYS D 143 ? 0.3565 0.2654 0.3443 0.0935  -0.0898 -0.0963 143 LYS D N   
7125  C CA  . LYS D 143 ? 0.3557 0.2639 0.3459 0.0920  -0.0878 -0.0962 143 LYS D CA  
7126  C C   . LYS D 143 ? 0.3354 0.2590 0.3355 0.0899  -0.0771 -0.0927 143 LYS D C   
7127  O O   . LYS D 143 ? 0.3348 0.2579 0.3358 0.0890  -0.0750 -0.0923 143 LYS D O   
7128  C CB  . LYS D 143 ? 0.3599 0.2596 0.3586 0.0879  -0.0951 -0.0962 143 LYS D CB  
7129  C CG  . LYS D 143 ? 0.3841 0.2651 0.3712 0.0886  -0.1069 -0.0997 143 LYS D CG  
7130  C CD  . LYS D 143 ? 0.3897 0.2613 0.3853 0.0831  -0.1138 -0.0991 143 LYS D CD  
7131  C CE  . LYS D 143 ? 0.4207 0.2709 0.4025 0.0840  -0.1289 -0.1036 143 LYS D CE  
7132  N NZ  . LYS D 143 ? 0.4334 0.2719 0.4230 0.0792  -0.1405 -0.1041 143 LYS D NZ  
7133  N N   . LEU D 144 ? 0.3179 0.2533 0.3243 0.0889  -0.0708 -0.0899 144 LEU D N   
7134  C CA  . LEU D 144 ? 0.3001 0.2484 0.3159 0.0857  -0.0610 -0.0862 144 LEU D CA  
7135  C C   . LEU D 144 ? 0.3023 0.2521 0.3092 0.0877  -0.0563 -0.0864 144 LEU D C   
7136  O O   . LEU D 144 ? 0.3109 0.2587 0.3066 0.0916  -0.0563 -0.0880 144 LEU D O   
7137  C CB  . LEU D 144 ? 0.2882 0.2463 0.3105 0.0845  -0.0558 -0.0833 144 LEU D CB  
7138  C CG  . LEU D 144 ? 0.2710 0.2404 0.3052 0.0800  -0.0465 -0.0788 144 LEU D CG  
7139  C CD1 . LEU D 144 ? 0.2650 0.2352 0.3138 0.0762  -0.0474 -0.0777 144 LEU D CD1 
7140  C CD2 . LEU D 144 ? 0.2631 0.2399 0.3001 0.0796  -0.0413 -0.0759 144 LEU D CD2 
7141  N N   . GLU D 145 ? 0.2945 0.2477 0.3071 0.0851  -0.0525 -0.0846 145 GLU D N   
7142  C CA  . GLU D 145 ? 0.2957 0.2508 0.3025 0.0866  -0.0487 -0.0847 145 GLU D CA  
7143  C C   . GLU D 145 ? 0.2796 0.2454 0.2941 0.0828  -0.0400 -0.0804 145 GLU D C   
7144  O O   . GLU D 145 ? 0.2791 0.2484 0.2891 0.0840  -0.0363 -0.0800 145 GLU D O   
7145  C CB  . GLU D 145 ? 0.3065 0.2524 0.3099 0.0879  -0.0536 -0.0870 145 GLU D CB  
7146  C CG  . GLU D 145 ? 0.3230 0.2556 0.3206 0.0901  -0.0629 -0.0906 145 GLU D CG  
7147  C CD  . GLU D 145 ? 0.3365 0.2580 0.3291 0.0915  -0.0680 -0.0927 145 GLU D CD  
7148  O OE1 . GLU D 145 ? 0.3299 0.2542 0.3273 0.0895  -0.0645 -0.0908 145 GLU D OE1 
7149  O OE2 . GLU D 145 ? 0.3553 0.2638 0.3384 0.0946  -0.0757 -0.0964 145 GLU D OE2 
7150  N N   . TYR D 146 ? 0.2590 0.2294 0.2850 0.0783  -0.0367 -0.0773 146 TYR D N   
7151  C CA  . TYR D 146 ? 0.2456 0.2242 0.2783 0.0745  -0.0285 -0.0730 146 TYR D CA  
7152  C C   . TYR D 146 ? 0.2363 0.2209 0.2774 0.0720  -0.0250 -0.0702 146 TYR D C   
7153  O O   . TYR D 146 ? 0.2351 0.2189 0.2844 0.0708  -0.0276 -0.0704 146 TYR D O   
7154  C CB  . TYR D 146 ? 0.2423 0.2196 0.2809 0.0718  -0.0269 -0.0717 146 TYR D CB  
7155  C CG  . TYR D 146 ? 0.2315 0.2150 0.2742 0.0685  -0.0191 -0.0675 146 TYR D CG  
7156  C CD1 . TYR D 146 ? 0.2331 0.2169 0.2697 0.0696  -0.0175 -0.0675 146 TYR D CD1 
7157  C CD2 . TYR D 146 ? 0.2210 0.2098 0.2737 0.0647  -0.0137 -0.0637 146 TYR D CD2 
7158  C CE1 . TYR D 146 ? 0.2244 0.2127 0.2642 0.0666  -0.0112 -0.0638 146 TYR D CE1 
7159  C CE2 . TYR D 146 ? 0.2131 0.2061 0.2681 0.0620  -0.0070 -0.0599 146 TYR D CE2 
7160  C CZ  . TYR D 146 ? 0.2148 0.2071 0.2630 0.0628  -0.0059 -0.0599 146 TYR D CZ  
7161  O OH  . TYR D 146 ? 0.2080 0.2034 0.2580 0.0603  -0.0001 -0.0562 146 TYR D OH  
7162  N N   . PHE D 147 ? 0.2354 0.2254 0.2750 0.0714  -0.0197 -0.0676 147 PHE D N   
7163  C CA  . PHE D 147 ? 0.2289 0.2235 0.2748 0.0700  -0.0166 -0.0649 147 PHE D CA  
7164  C C   . PHE D 147 ? 0.2195 0.2193 0.2691 0.0668  -0.0086 -0.0603 147 PHE D C   
7165  O O   . PHE D 147 ? 0.2198 0.2203 0.2628 0.0673  -0.0059 -0.0594 147 PHE D O   
7166  C CB  . PHE D 147 ? 0.2355 0.2285 0.2734 0.0736  -0.0192 -0.0665 147 PHE D CB  
7167  C CG  . PHE D 147 ? 0.2319 0.2278 0.2763 0.0733  -0.0182 -0.0646 147 PHE D CG  
7168  C CD1 . PHE D 147 ? 0.2269 0.2252 0.2842 0.0712  -0.0188 -0.0635 147 PHE D CD1 
7169  C CD2 . PHE D 147 ? 0.2344 0.2307 0.2727 0.0756  -0.0169 -0.0639 147 PHE D CD2 
7170  C CE1 . PHE D 147 ? 0.2248 0.2261 0.2894 0.0716  -0.0185 -0.0617 147 PHE D CE1 
7171  C CE2 . PHE D 147 ? 0.2324 0.2307 0.2767 0.0760  -0.0166 -0.0621 147 PHE D CE2 
7172  C CZ  . PHE D 147 ? 0.2277 0.2288 0.2856 0.0742  -0.0176 -0.0610 147 PHE D CZ  
7173  N N   . ASP D 148 ? 0.2372 0.2402 0.2972 0.0637  -0.0053 -0.0573 148 ASP D N   
7174  C CA  . ASP D 148 ? 0.2299 0.2364 0.2927 0.0609  0.0016  -0.0529 148 ASP D CA  
7175  C C   . ASP D 148 ? 0.2253 0.2361 0.2976 0.0598  0.0043  -0.0500 148 ASP D C   
7176  O O   . ASP D 148 ? 0.2231 0.2358 0.3054 0.0582  0.0038  -0.0500 148 ASP D O   
7177  C CB  . ASP D 148 ? 0.2277 0.2332 0.2924 0.0587  0.0031  -0.0523 148 ASP D CB  
7178  C CG  . ASP D 148 ? 0.2229 0.2301 0.2860 0.0567  0.0089  -0.0486 148 ASP D CG  
7179  O OD1 . ASP D 148 ? 0.2199 0.2297 0.2837 0.0563  0.0123  -0.0458 148 ASP D OD1 
7180  O OD2 . ASP D 148 ? 0.2230 0.2284 0.2838 0.0560  0.0095  -0.0486 148 ASP D OD2 
7181  N N   . LEU D 149 ? 0.1983 0.2105 0.2680 0.0607  0.0071  -0.0478 149 LEU D N   
7182  C CA  . LEU D 149 ? 0.1952 0.2115 0.2729 0.0604  0.0099  -0.0447 149 LEU D CA  
7183  C C   . LEU D 149 ? 0.1914 0.2092 0.2672 0.0589  0.0156  -0.0407 149 LEU D C   
7184  O O   . LEU D 149 ? 0.1908 0.2110 0.2695 0.0598  0.0179  -0.0383 149 LEU D O   
7185  C CB  . LEU D 149 ? 0.1993 0.2154 0.2762 0.0637  0.0074  -0.0454 149 LEU D CB  
7186  C CG  . LEU D 149 ? 0.2037 0.2188 0.2848 0.0656  0.0005  -0.0491 149 LEU D CG  
7187  C CD1 . LEU D 149 ? 0.2080 0.2230 0.2887 0.0692  -0.0017 -0.0490 149 LEU D CD1 
7188  C CD2 . LEU D 149 ? 0.2006 0.2193 0.2957 0.0635  -0.0006 -0.0491 149 LEU D CD2 
7189  N N   . SER D 150 ? 0.2350 0.2510 0.3058 0.0571  0.0174  -0.0403 150 SER D N   
7190  C CA  . SER D 150 ? 0.2325 0.2489 0.3000 0.0561  0.0216  -0.0371 150 SER D CA  
7191  C C   . SER D 150 ? 0.2289 0.2494 0.3046 0.0542  0.0237  -0.0354 150 SER D C   
7192  O O   . SER D 150 ? 0.2279 0.2508 0.3131 0.0527  0.0227  -0.0366 150 SER D O   
7193  C CB  . SER D 150 ? 0.2322 0.2460 0.2938 0.0549  0.0220  -0.0376 150 SER D CB  
7194  O OG  . SER D 150 ? 0.2364 0.2474 0.2928 0.0563  0.0189  -0.0409 150 SER D OG  
7195  N N   . ILE D 151 ? 0.2291 0.2504 0.3024 0.0538  0.0265  -0.0331 151 ILE D N   
7196  C CA  . ILE D 151 ? 0.2263 0.2508 0.3076 0.0510  0.0286  -0.0323 151 ILE D CA  
7197  C C   . ILE D 151 ? 0.2270 0.2553 0.3200 0.0513  0.0282  -0.0328 151 ILE D C   
7198  O O   . ILE D 151 ? 0.2446 0.2745 0.3472 0.0489  0.0283  -0.0338 151 ILE D O   
7199  C CB  . ILE D 151 ? 0.2238 0.2474 0.3071 0.0474  0.0295  -0.0328 151 ILE D CB  
7200  C CG1 . ILE D 151 ? 0.2241 0.2443 0.2965 0.0482  0.0289  -0.0327 151 ILE D CG1 
7201  C CG2 . ILE D 151 ? 0.2222 0.2473 0.3128 0.0442  0.0328  -0.0317 151 ILE D CG2 
7202  C CD1 . ILE D 151 ? 0.2227 0.2415 0.2956 0.0458  0.0293  -0.0332 151 ILE D CD1 
7203  N N   . ASN D 152 ? 0.2386 0.2682 0.3313 0.0544  0.0280  -0.0318 152 ASN D N   
7204  C CA  . ASN D 152 ? 0.2406 0.2742 0.3446 0.0558  0.0272  -0.0321 152 ASN D CA  
7205  C C   . ASN D 152 ? 0.2425 0.2774 0.3451 0.0584  0.0286  -0.0302 152 ASN D C   
7206  O O   . ASN D 152 ? 0.2440 0.2769 0.3390 0.0579  0.0305  -0.0291 152 ASN D O   
7207  C CB  . ASN D 152 ? 0.2428 0.2762 0.3481 0.0583  0.0233  -0.0336 152 ASN D CB  
7208  C CG  . ASN D 152 ? 0.2442 0.2785 0.3578 0.0555  0.0216  -0.0359 152 ASN D CG  
7209  O OD1 . ASN D 152 ? 0.2412 0.2793 0.3677 0.0533  0.0228  -0.0360 152 ASN D OD1 
7210  N ND2 . ASN D 152 ? 0.2435 0.2740 0.3504 0.0557  0.0189  -0.0377 152 ASN D ND2 
7211  N N   . GLN D 153 ? 0.2479 0.2862 0.3588 0.0614  0.0273  -0.0301 153 GLN D N   
7212  C CA  . GLN D 153 ? 0.2509 0.2902 0.3606 0.0649  0.0280  -0.0284 153 GLN D CA  
7213  C C   . GLN D 153 ? 0.2552 0.2935 0.3616 0.0701  0.0253  -0.0277 153 GLN D C   
7214  O O   . GLN D 153 ? 0.2618 0.3030 0.3750 0.0736  0.0242  -0.0268 153 GLN D O   
7215  C CB  . GLN D 153 ? 0.2522 0.2964 0.3766 0.0642  0.0295  -0.0283 153 GLN D CB  
7216  C CG  . GLN D 153 ? 0.2493 0.2932 0.3778 0.0589  0.0331  -0.0285 153 GLN D CG  
7217  C CD  . GLN D 153 ? 0.2552 0.3029 0.3988 0.0566  0.0336  -0.0296 153 GLN D CD  
7218  O OE1 . GLN D 153 ? 0.2668 0.3190 0.4214 0.0590  0.0313  -0.0301 153 GLN D OE1 
7219  N NE2 . GLN D 153 ? 0.2578 0.3036 0.4024 0.0521  0.0365  -0.0299 153 GLN D NE2 
7220  N N   . LEU D 154 ? 0.2238 0.2573 0.3208 0.0704  0.0244  -0.0281 154 LEU D N   
7221  C CA  . LEU D 154 ? 0.2284 0.2586 0.3222 0.0741  0.0225  -0.0277 154 LEU D CA  
7222  C C   . LEU D 154 ? 0.2312 0.2571 0.3159 0.0766  0.0262  -0.0246 154 LEU D C   
7223  O O   . LEU D 154 ? 0.2294 0.2532 0.3056 0.0745  0.0294  -0.0234 154 LEU D O   
7224  C CB  . LEU D 154 ? 0.2283 0.2541 0.3170 0.0725  0.0199  -0.0306 154 LEU D CB  
7225  C CG  . LEU D 154 ? 0.2258 0.2541 0.3218 0.0698  0.0166  -0.0335 154 LEU D CG  
7226  C CD1 . LEU D 154 ? 0.2275 0.2512 0.3168 0.0694  0.0130  -0.0370 154 LEU D CD1 
7227  C CD2 . LEU D 154 ? 0.2273 0.2613 0.3385 0.0712  0.0131  -0.0340 154 LEU D CD2 
7228  N N   . VAL D 155 ? 0.2508 0.2753 0.3383 0.0802  0.0249  -0.0237 155 VAL D N   
7229  C CA  . VAL D 155 ? 0.2540 0.2736 0.3366 0.0807  0.0281  -0.0213 155 VAL D CA  
7230  C C   . VAL D 155 ? 0.2578 0.2731 0.3401 0.0823  0.0244  -0.0248 155 VAL D C   
7231  O O   . VAL D 155 ? 0.2595 0.2755 0.3421 0.0831  0.0184  -0.0280 155 VAL D O   
7232  C CB  . VAL D 155 ? 0.2217 0.2452 0.3081 0.0844  0.0282  -0.0182 155 VAL D CB  
7233  C CG1 . VAL D 155 ? 0.2186 0.2470 0.3008 0.0833  0.0289  -0.0191 155 VAL D CG1 
7234  C CG2 . VAL D 155 ? 0.2242 0.2541 0.3243 0.0893  0.0231  -0.0191 155 VAL D CG2 
7235  N N   . GLY D 156 ? 0.2637 0.2749 0.3429 0.0824  0.0258  -0.0255 156 GLY D N   
7236  C CA  . GLY D 156 ? 0.2707 0.2780 0.3413 0.0852  0.0199  -0.0296 156 GLY D CA  
7237  C C   . GLY D 156 ? 0.2715 0.2758 0.3275 0.0831  0.0198  -0.0337 156 GLY D C   
7238  O O   . GLY D 156 ? 0.2847 0.2899 0.3395 0.0788  0.0242  -0.0336 156 GLY D O   
7239  N N   . GLU D 157 ? 0.3451 0.3452 0.3895 0.0868  0.0143  -0.0371 157 GLU D N   
7240  C CA  . GLU D 157 ? 0.3491 0.3461 0.3785 0.0864  0.0141  -0.0404 157 GLU D CA  
7241  C C   . GLU D 157 ? 0.3490 0.3464 0.3766 0.0860  0.0096  -0.0435 157 GLU D C   
7242  O O   . GLU D 157 ? 0.3474 0.3469 0.3841 0.0861  0.0062  -0.0435 157 GLU D O   
7243  C CB  . GLU D 157 ? 0.3643 0.3545 0.3789 0.0913  0.0117  -0.0420 157 GLU D CB  
7244  C CG  . GLU D 157 ? 0.3660 0.3548 0.3813 0.0925  0.0151  -0.0392 157 GLU D CG  
7245  C CD  . GLU D 157 ? 0.3904 0.3713 0.3872 0.0962  0.0153  -0.0405 157 GLU D CD  
7246  O OE1 . GLU D 157 ? 0.4009 0.3784 0.3856 0.0970  0.0142  -0.0436 157 GLU D OE1 
7247  O OE2 . GLU D 157 ? 0.3947 0.3721 0.3890 0.0984  0.0169  -0.0384 157 GLU D OE2 
7248  N N   . ILE D 158 ? 0.2801 0.2754 0.2967 0.0856  0.0097  -0.0462 158 ILE D N   
7249  C CA  . ILE D 158 ? 0.2822 0.2767 0.2953 0.0859  0.0050  -0.0497 158 ILE D CA  
7250  C C   . ILE D 158 ? 0.2953 0.2829 0.2962 0.0912  -0.0013 -0.0533 158 ILE D C   
7251  O O   . ILE D 158 ? 0.3043 0.2871 0.2930 0.0937  0.0003  -0.0540 158 ILE D O   
7252  C CB  . ILE D 158 ? 0.2805 0.2760 0.2897 0.0833  0.0081  -0.0507 158 ILE D CB  
7253  C CG1 . ILE D 158 ? 0.2689 0.2693 0.2891 0.0782  0.0128  -0.0476 158 ILE D CG1 
7254  C CG2 . ILE D 158 ? 0.2863 0.2794 0.2896 0.0850  0.0027  -0.0549 158 ILE D CG2 
7255  C CD1 . ILE D 158 ? 0.2676 0.2685 0.2848 0.0759  0.0165  -0.0477 158 ILE D CD1 
7256  N N   . PRO D 159 ? 0.3049 0.2906 0.3084 0.0931  -0.0085 -0.0555 159 PRO D N   
7257  C CA  . PRO D 159 ? 0.3195 0.2962 0.3100 0.0983  -0.0157 -0.0590 159 PRO D CA  
7258  C C   . PRO D 159 ? 0.3288 0.3007 0.3051 0.0996  -0.0158 -0.0626 159 PRO D C   
7259  O O   . PRO D 159 ? 0.3236 0.2993 0.3034 0.0968  -0.0142 -0.0635 159 PRO D O   
7260  C CB  . PRO D 159 ? 0.3187 0.2953 0.3188 0.0987  -0.0236 -0.0607 159 PRO D CB  
7261  C CG  . PRO D 159 ? 0.3052 0.2903 0.3192 0.0935  -0.0198 -0.0593 159 PRO D CG  
7262  C CD  . PRO D 159 ? 0.2963 0.2870 0.3144 0.0903  -0.0105 -0.0550 159 PRO D CD  
7263  N N   . PRO D 160 ? 0.3586 0.3210 0.3187 0.1038  -0.0173 -0.0646 160 PRO D N   
7264  C CA  . PRO D 160 ? 0.3708 0.3273 0.3182 0.1054  -0.0174 -0.0686 160 PRO D CA  
7265  C C   . PRO D 160 ? 0.3751 0.3280 0.3223 0.1063  -0.0255 -0.0724 160 PRO D C   
7266  O O   . PRO D 160 ? 0.3817 0.3323 0.3235 0.1066  -0.0250 -0.0755 160 PRO D O   
7267  C CB  . PRO D 160 ? 0.3892 0.3340 0.3186 0.1094  -0.0172 -0.0701 160 PRO D CB  
7268  C CG  . PRO D 160 ? 0.3841 0.3301 0.3173 0.1100  -0.0162 -0.0660 160 PRO D CG  
7269  C CD  . PRO D 160 ? 0.3681 0.3231 0.3202 0.1077  -0.0194 -0.0637 160 PRO D CD  
7270  N N   . GLU D 161 ? 0.4090 0.3611 0.3633 0.1066  -0.0330 -0.0725 161 GLU D N   
7271  C CA  . GLU D 161 ? 0.4130 0.3608 0.3685 0.1069  -0.0415 -0.0762 161 GLU D CA  
7272  C C   . GLU D 161 ? 0.4028 0.3581 0.3676 0.1033  -0.0388 -0.0764 161 GLU D C   
7273  O O   . GLU D 161 ? 0.4125 0.3627 0.3749 0.1039  -0.0446 -0.0799 161 GLU D O   
7274  C CB  . GLU D 161 ? 0.4098 0.3570 0.3761 0.1069  -0.0492 -0.0756 161 GLU D CB  
7275  C CG  . GLU D 161 ? 0.4323 0.3656 0.3857 0.1115  -0.0578 -0.0774 161 GLU D CG  
7276  C CD  . GLU D 161 ? 0.4314 0.3644 0.3816 0.1135  -0.0538 -0.0739 161 GLU D CD  
7277  O OE1 . GLU D 161 ? 0.4193 0.3628 0.3765 0.1112  -0.0438 -0.0704 161 GLU D OE1 
7278  O OE2 . GLU D 161 ? 0.4483 0.3683 0.3857 0.1195  -0.0641 -0.0760 161 GLU D OE2 
7279  N N   . LEU D 162 ? 0.3254 0.2912 0.3000 0.0995  -0.0306 -0.0728 162 LEU D N   
7280  C CA  . LEU D 162 ? 0.3180 0.2888 0.2989 0.0963  -0.0283 -0.0730 162 LEU D CA  
7281  C C   . LEU D 162 ? 0.3304 0.2957 0.2996 0.0989  -0.0285 -0.0765 162 LEU D C   
7282  O O   . LEU D 162 ? 0.3302 0.2956 0.3019 0.0981  -0.0305 -0.0784 162 LEU D O   
7283  C CB  . LEU D 162 ? 0.3036 0.2837 0.2939 0.0920  -0.0197 -0.0685 162 LEU D CB  
7284  C CG  . LEU D 162 ? 0.2912 0.2772 0.2959 0.0887  -0.0183 -0.0650 162 LEU D CG  
7285  C CD1 . LEU D 162 ? 0.2791 0.2719 0.2919 0.0840  -0.0107 -0.0613 162 LEU D CD1 
7286  C CD2 . LEU D 162 ? 0.2906 0.2755 0.3031 0.0881  -0.0249 -0.0671 162 LEU D CD2 
7287  N N   . GLY D 163 ? 0.3640 0.3237 0.3207 0.1022  -0.0263 -0.0778 163 GLY D N   
7288  C CA  . GLY D 163 ? 0.3791 0.3322 0.3248 0.1049  -0.0260 -0.0821 163 GLY D CA  
7289  C C   . GLY D 163 ? 0.3929 0.3359 0.3316 0.1076  -0.0347 -0.0866 163 GLY D C   
7290  O O   . GLY D 163 ? 0.4052 0.3429 0.3370 0.1095  -0.0349 -0.0906 163 GLY D O   
7291  N N   . LYS D 164 ? 0.4014 0.3408 0.3423 0.1077  -0.0422 -0.0864 164 LYS D N   
7292  C CA  . LYS D 164 ? 0.4154 0.3435 0.3501 0.1096  -0.0517 -0.0906 164 LYS D CA  
7293  C C   . LYS D 164 ? 0.4078 0.3393 0.3531 0.1072  -0.0547 -0.0911 164 LYS D C   
7294  O O   . LYS D 164 ? 0.4188 0.3406 0.3608 0.1081  -0.0631 -0.0942 164 LYS D O   
7295  C CB  . LYS D 164 ? 0.4191 0.3408 0.3528 0.1103  -0.0597 -0.0905 164 LYS D CB  
7296  C CG  . LYS D 164 ? 0.4357 0.3469 0.3526 0.1134  -0.0599 -0.0917 164 LYS D CG  
7297  C CD  . LYS D 164 ? 0.4478 0.3464 0.3591 0.1144  -0.0717 -0.0934 164 LYS D CD  
7298  C CE  . LYS D 164 ? 0.4302 0.3376 0.3590 0.1128  -0.0746 -0.0896 164 LYS D CE  
7299  N NZ  . LYS D 164 ? 0.4614 0.3547 0.3836 0.1194  -0.0958 -0.0947 164 LYS D NZ  
7300  N N   . LEU D 165 ? 0.3605 0.3037 0.3173 0.1040  -0.0485 -0.0881 165 LEU D N   
7301  C CA  . LEU D 165 ? 0.3542 0.2998 0.3199 0.1016  -0.0505 -0.0885 165 LEU D CA  
7302  C C   . LEU D 165 ? 0.3649 0.3067 0.3231 0.1040  -0.0493 -0.0915 165 LEU D C   
7303  O O   . LEU D 165 ? 0.3568 0.3057 0.3200 0.1024  -0.0440 -0.0901 165 LEU D O   
7304  C CB  . LEU D 165 ? 0.3334 0.2915 0.3140 0.0966  -0.0446 -0.0840 165 LEU D CB  
7305  C CG  . LEU D 165 ? 0.3233 0.2857 0.3136 0.0942  -0.0448 -0.0812 165 LEU D CG  
7306  C CD1 . LEU D 165 ? 0.3057 0.2791 0.3087 0.0894  -0.0370 -0.0768 165 LEU D CD1 
7307  C CD2 . LEU D 165 ? 0.3271 0.2838 0.3227 0.0938  -0.0536 -0.0834 165 LEU D CD2 
7308  N N   . SER D 166 ? 0.3576 0.2868 0.3031 0.1079  -0.0547 -0.0961 166 SER D N   
7309  C CA  . SER D 166 ? 0.3719 0.2959 0.3091 0.1110  -0.0535 -0.1001 166 SER D CA  
7310  C C   . SER D 166 ? 0.3656 0.2931 0.3108 0.1096  -0.0542 -0.1000 166 SER D C   
7311  O O   . SER D 166 ? 0.3673 0.2980 0.3120 0.1110  -0.0501 -0.1013 166 SER D O   
7312  C CB  . SER D 166 ? 0.3967 0.3043 0.3192 0.1145  -0.0603 -0.1055 166 SER D CB  
7313  O OG  . SER D 166 ? 0.3998 0.3001 0.3248 0.1132  -0.0694 -0.1061 166 SER D OG  
7314  N N   . ASN D 167 ? 0.3453 0.2718 0.2981 0.1069  -0.0594 -0.0987 167 ASN D N   
7315  C CA  . ASN D 167 ? 0.3426 0.2694 0.3011 0.1057  -0.0609 -0.0988 167 ASN D CA  
7316  C C   . ASN D 167 ? 0.3215 0.2615 0.2924 0.1013  -0.0543 -0.0942 167 ASN D C   
7317  O O   . ASN D 167 ? 0.3184 0.2586 0.2942 0.0998  -0.0550 -0.0939 167 ASN D O   
7318  C CB  . ASN D 167 ? 0.3490 0.2659 0.3089 0.1043  -0.0695 -0.0999 167 ASN D CB  
7319  C CG  . ASN D 167 ? 0.3743 0.2749 0.3205 0.1084  -0.0769 -0.1052 167 ASN D CG  
7320  O OD1 . ASN D 167 ? 0.3856 0.2819 0.3259 0.1116  -0.0769 -0.1082 167 ASN D OD1 
7321  N ND2 . ASN D 167 ? 0.3848 0.2755 0.3259 0.1083  -0.0835 -0.1066 167 ASN D ND2 
7322  N N   . LEU D 168 ? 0.3273 0.2767 0.3025 0.0992  -0.0481 -0.0908 168 LEU D N   
7323  C CA  . LEU D 168 ? 0.3091 0.2692 0.2952 0.0945  -0.0418 -0.0864 168 LEU D CA  
7324  C C   . LEU D 168 ? 0.3093 0.2725 0.2944 0.0952  -0.0382 -0.0868 168 LEU D C   
7325  O O   . LEU D 168 ? 0.3178 0.2803 0.2960 0.0986  -0.0364 -0.0890 168 LEU D O   
7326  C CB  . LEU D 168 ? 0.2987 0.2659 0.2880 0.0924  -0.0364 -0.0829 168 LEU D CB  
7327  C CG  . LEU D 168 ? 0.2810 0.2570 0.2824 0.0870  -0.0309 -0.0782 168 LEU D CG  
7328  C CD1 . LEU D 168 ? 0.2758 0.2513 0.2861 0.0844  -0.0340 -0.0775 168 LEU D CD1 
7329  C CD2 . LEU D 168 ? 0.2743 0.2562 0.2760 0.0859  -0.0246 -0.0749 168 LEU D CD2 
7330  N N   . ASP D 169 ? 0.3153 0.2814 0.3075 0.0922  -0.0371 -0.0849 169 ASP D N   
7331  C CA  . ASP D 169 ? 0.3145 0.2836 0.3069 0.0925  -0.0345 -0.0851 169 ASP D CA  
7332  C C   . ASP D 169 ? 0.2991 0.2775 0.2986 0.0881  -0.0272 -0.0805 169 ASP D C   
7333  O O   . ASP D 169 ? 0.2992 0.2811 0.2974 0.0888  -0.0240 -0.0807 169 ASP D O   
7334  C CB  . ASP D 169 ? 0.3189 0.2825 0.3124 0.0928  -0.0389 -0.0865 169 ASP D CB  
7335  C CG  . ASP D 169 ? 0.3139 0.2818 0.3103 0.0918  -0.0359 -0.0854 169 ASP D CG  
7336  O OD1 . ASP D 169 ? 0.3182 0.2886 0.3114 0.0945  -0.0343 -0.0872 169 ASP D OD1 
7337  O OD2 . ASP D 169 ? 0.3065 0.2748 0.3086 0.0884  -0.0349 -0.0829 169 ASP D OD2 
7338  N N   . THR D 170 ? 0.2603 0.2420 0.2674 0.0835  -0.0246 -0.0767 170 THR D N   
7339  C CA  . THR D 170 ? 0.2472 0.2358 0.2606 0.0791  -0.0179 -0.0722 170 THR D CA  
7340  C C   . THR D 170 ? 0.2399 0.2315 0.2573 0.0768  -0.0150 -0.0692 170 THR D C   
7341  O O   . THR D 170 ? 0.2401 0.2297 0.2604 0.0766  -0.0178 -0.0697 170 THR D O   
7342  C CB  . THR D 170 ? 0.2409 0.2296 0.2605 0.0759  -0.0168 -0.0703 170 THR D CB  
7343  O OG1 . THR D 170 ? 0.2488 0.2342 0.2642 0.0787  -0.0201 -0.0732 170 THR D OG1 
7344  C CG2 . THR D 170 ? 0.2291 0.2235 0.2543 0.0717  -0.0099 -0.0657 170 THR D CG2 
7345  N N   . LEU D 171 ? 0.2240 0.2199 0.2419 0.0753  -0.0096 -0.0664 171 LEU D N   
7346  C CA  . LEU D 171 ? 0.2183 0.2165 0.2395 0.0736  -0.0064 -0.0634 171 LEU D CA  
7347  C C   . LEU D 171 ? 0.2082 0.2104 0.2353 0.0695  -0.0001 -0.0588 171 LEU D C   
7348  O O   . LEU D 171 ? 0.2080 0.2114 0.2326 0.0693  0.0028  -0.0581 171 LEU D O   
7349  C CB  . LEU D 171 ? 0.2254 0.2225 0.2392 0.0769  -0.0065 -0.0647 171 LEU D CB  
7350  C CG  . LEU D 171 ? 0.2209 0.2199 0.2370 0.0759  -0.0031 -0.0615 171 LEU D CG  
7351  C CD1 . LEU D 171 ? 0.2180 0.2168 0.2403 0.0752  -0.0058 -0.0611 171 LEU D CD1 
7352  C CD2 . LEU D 171 ? 0.2298 0.2264 0.2371 0.0795  -0.0030 -0.0630 171 LEU D CD2 
7353  N N   . HIS D 172 ? 0.2389 0.2426 0.2738 0.0666  0.0020  -0.0559 172 HIS D N   
7354  C CA  . HIS D 172 ? 0.2309 0.2370 0.2708 0.0632  0.0079  -0.0514 172 HIS D CA  
7355  C C   . HIS D 172 ? 0.2275 0.2353 0.2724 0.0626  0.0105  -0.0485 172 HIS D C   
7356  O O   . HIS D 172 ? 0.2263 0.2348 0.2773 0.0624  0.0090  -0.0485 172 HIS D O   
7357  C CB  . HIS D 172 ? 0.2270 0.2330 0.2718 0.0608  0.0086  -0.0505 172 HIS D CB  
7358  C CG  . HIS D 172 ? 0.2301 0.2346 0.2706 0.0615  0.0068  -0.0526 172 HIS D CG  
7359  N ND1 . HIS D 172 ? 0.2289 0.2320 0.2720 0.0602  0.0065  -0.0525 172 HIS D ND1 
7360  C CD2 . HIS D 172 ? 0.2354 0.2394 0.2695 0.0638  0.0051  -0.0551 172 HIS D CD2 
7361  C CE1 . HIS D 172 ? 0.2333 0.2350 0.2716 0.0618  0.0043  -0.0548 172 HIS D CE1 
7362  N NE2 . HIS D 172 ? 0.2373 0.2399 0.2705 0.0641  0.0033  -0.0566 172 HIS D NE2 
7363  N N   . LEU D 173 ? 0.2424 0.2508 0.2853 0.0626  0.0142  -0.0462 173 LEU D N   
7364  C CA  . LEU D 173 ? 0.2405 0.2500 0.2875 0.0628  0.0169  -0.0431 173 LEU D CA  
7365  C C   . LEU D 173 ? 0.2361 0.2462 0.2846 0.0608  0.0227  -0.0387 173 LEU D C   
7366  O O   . LEU D 173 ? 0.2367 0.2463 0.2845 0.0614  0.0257  -0.0367 173 LEU D O   
7367  C CB  . LEU D 173 ? 0.2462 0.2544 0.2882 0.0658  0.0152  -0.0449 173 LEU D CB  
7368  C CG  . LEU D 173 ? 0.1544 0.1613 0.1944 0.0687  0.0088  -0.0489 173 LEU D CG  
7369  C CD1 . LEU D 173 ? 0.1618 0.1664 0.1938 0.0723  0.0071  -0.0507 173 LEU D CD1 
7370  C CD2 . LEU D 173 ? 0.1516 0.1602 0.2012 0.0684  0.0073  -0.0480 173 LEU D CD2 
7371  N N   . VAL D 174 ? 0.2382 0.2489 0.2883 0.0588  0.0239  -0.0374 174 VAL D N   
7372  C CA  . VAL D 174 ? 0.2357 0.2461 0.2840 0.0574  0.0278  -0.0344 174 VAL D CA  
7373  C C   . VAL D 174 ? 0.2328 0.2458 0.2845 0.0575  0.0299  -0.0309 174 VAL D C   
7374  O O   . VAL D 174 ? 0.2329 0.2487 0.2906 0.0572  0.0284  -0.0313 174 VAL D O   
7375  C CB  . VAL D 174 ? 0.2347 0.2446 0.2815 0.0558  0.0267  -0.0358 174 VAL D CB  
7376  C CG1 . VAL D 174 ? 0.2333 0.2428 0.2775 0.0550  0.0296  -0.0337 174 VAL D CG1 
7377  C CG2 . VAL D 174 ? 0.2420 0.2509 0.2854 0.0570  0.0227  -0.0404 174 VAL D CG2 
7378  N N   . GLU D 175 ? 0.2502 0.2633 0.2986 0.0578  0.0323  -0.0284 175 GLU D N   
7379  C CA  . GLU D 175 ? 0.2474 0.2650 0.2991 0.0576  0.0322  -0.0276 175 GLU D CA  
7380  C C   . GLU D 175 ? 0.2508 0.2712 0.3085 0.0593  0.0316  -0.0274 175 GLU D C   
7381  O O   . GLU D 175 ? 0.2491 0.2728 0.3159 0.0573  0.0311  -0.0284 175 GLU D O   
7382  C CB  . GLU D 175 ? 0.2457 0.2651 0.3024 0.0539  0.0314  -0.0288 175 GLU D CB  
7383  C CG  . GLU D 175 ? 0.2469 0.2647 0.2986 0.0527  0.0319  -0.0288 175 GLU D CG  
7384  C CD  . GLU D 175 ? 0.2476 0.2664 0.3045 0.0489  0.0321  -0.0294 175 GLU D CD  
7385  O OE1 . GLU D 175 ? 0.2465 0.2669 0.3116 0.0466  0.0332  -0.0293 175 GLU D OE1 
7386  O OE2 . GLU D 175 ? 0.2476 0.2648 0.3007 0.0484  0.0319  -0.0296 175 GLU D OE2 
7387  N N   . ASN D 176 ? 0.2249 0.2426 0.2789 0.0616  0.0323  -0.0260 176 ASN D N   
7388  C CA  . ASN D 176 ? 0.2271 0.2469 0.2859 0.0643  0.0319  -0.0254 176 ASN D CA  
7389  C C   . ASN D 176 ? 0.2303 0.2487 0.2832 0.0656  0.0332  -0.0232 176 ASN D C   
7390  O O   . ASN D 176 ? 0.2299 0.2473 0.2760 0.0645  0.0335  -0.0229 176 ASN D O   
7391  C CB  . ASN D 176 ? 0.2294 0.2470 0.2916 0.0656  0.0309  -0.0268 176 ASN D CB  
7392  C CG  . ASN D 176 ? 0.2271 0.2480 0.2967 0.0640  0.0275  -0.0294 176 ASN D CG  
7393  O OD1 . ASN D 176 ? 0.2264 0.2518 0.3052 0.0641  0.0264  -0.0296 176 ASN D OD1 
7394  N ND2 . ASN D 176 ? 0.2265 0.2450 0.2934 0.0621  0.0258  -0.0318 176 ASN D ND2 
7395  N N   . LYS D 177 ? 0.2372 0.2561 0.2931 0.0684  0.0332  -0.0220 177 LYS D N   
7396  C CA  . LYS D 177 ? 0.2411 0.2586 0.2912 0.0704  0.0342  -0.0199 177 LYS D CA  
7397  C C   . LYS D 177 ? 0.2424 0.2521 0.3044 0.0663  0.0389  -0.0201 177 LYS D C   
7398  O O   . LYS D 177 ? 0.2440 0.2535 0.3138 0.0666  0.0392  -0.0206 177 LYS D O   
7399  C CB  . LYS D 177 ? 0.2402 0.2659 0.2978 0.0729  0.0304  -0.0236 177 LYS D CB  
7400  C CG  . LYS D 177 ? 0.2343 0.2636 0.2996 0.0691  0.0314  -0.0261 177 LYS D CG  
7401  C CD  . LYS D 177 ? 0.2314 0.2589 0.2898 0.0658  0.0315  -0.0274 177 LYS D CD  
7402  C CE  . LYS D 177 ? 0.2344 0.2621 0.2985 0.0619  0.0343  -0.0271 177 LYS D CE  
7403  N NZ  . LYS D 177 ? 0.2246 0.2509 0.2855 0.0603  0.0337  -0.0271 177 LYS D NZ  
7404  N N   . LEU D 178 ? 0.2365 0.2455 0.2978 0.0653  0.0366  -0.0252 178 LEU D N   
7405  C CA  . LEU D 178 ? 0.2404 0.2484 0.3002 0.0684  0.0337  -0.0301 178 LEU D CA  
7406  C C   . LEU D 178 ? 0.2421 0.2490 0.2981 0.0677  0.0350  -0.0326 178 LEU D C   
7407  O O   . LEU D 178 ? 0.2400 0.2469 0.2929 0.0645  0.0367  -0.0335 178 LEU D O   
7408  C CB  . LEU D 178 ? 0.2422 0.2497 0.2946 0.0692  0.0296  -0.0336 178 LEU D CB  
7409  C CG  . LEU D 178 ? 0.2398 0.2493 0.2958 0.0691  0.0271  -0.0333 178 LEU D CG  
7410  C CD1 . LEU D 178 ? 0.2422 0.2509 0.2914 0.0692  0.0223  -0.0378 178 LEU D CD1 
7411  C CD2 . LEU D 178 ? 0.2414 0.2532 0.3049 0.0722  0.0246  -0.0322 178 LEU D CD2 
7412  N N   . ASN D 179 ? 0.3099 0.3160 0.3647 0.0712  0.0335  -0.0333 179 ASN D N   
7413  C CA  . ASN D 179 ? 0.3133 0.3179 0.3601 0.0720  0.0343  -0.0347 179 ASN D CA  
7414  C C   . ASN D 179 ? 0.3235 0.3239 0.3561 0.0768  0.0313  -0.0362 179 ASN D C   
7415  O O   . ASN D 179 ? 0.3271 0.3263 0.3579 0.0798  0.0271  -0.0370 179 ASN D O   
7416  C CB  . ASN D 179 ? 0.3128 0.3188 0.3667 0.0727  0.0352  -0.0338 179 ASN D CB  
7417  C CG  . ASN D 179 ? 0.3189 0.3236 0.3777 0.0771  0.0326  -0.0322 179 ASN D CG  
7418  O OD1 . ASN D 179 ? 0.3186 0.3227 0.3781 0.0791  0.0300  -0.0316 179 ASN D OD1 
7419  N ND2 . ASN D 179 ? 0.3198 0.3241 0.3816 0.0794  0.0324  -0.0314 179 ASN D ND2 
7420  N N   . GLY D 180 ? 0.3058 0.3037 0.3286 0.0776  0.0334  -0.0370 180 GLY D N   
7421  C CA  . GLY D 180 ? 0.3176 0.3102 0.3258 0.0819  0.0318  -0.0387 180 GLY D CA  
7422  C C   . GLY D 180 ? 0.3208 0.3131 0.3228 0.0804  0.0337  -0.0414 180 GLY D C   
7423  O O   . GLY D 180 ? 0.3165 0.3125 0.3251 0.0763  0.0360  -0.0416 180 GLY D O   
7424  N N   . SER D 181 ? 0.3348 0.3220 0.3240 0.0841  0.0328  -0.0438 181 SER D N   
7425  C CA  . SER D 181 ? 0.3411 0.3277 0.3253 0.0834  0.0348  -0.0474 181 SER D CA  
7426  C C   . SER D 181 ? 0.3409 0.3281 0.3247 0.0843  0.0299  -0.0496 181 SER D C   
7427  O O   . SER D 181 ? 0.3471 0.3330 0.3299 0.0868  0.0245  -0.0494 181 SER D O   
7428  C CB  . SER D 181 ? 0.3554 0.3356 0.3261 0.0865  0.0376  -0.0499 181 SER D CB  
7429  O OG  . SER D 181 ? 0.3623 0.3427 0.3337 0.0846  0.0433  -0.0490 181 SER D OG  
7430  N N   . ILE D 182 ? 0.3158 0.3049 0.3007 0.0826  0.0314  -0.0521 182 ILE D N   
7431  C CA  . ILE D 182 ? 0.3173 0.3063 0.3006 0.0840  0.0265  -0.0546 182 ILE D CA  
7432  C C   . ILE D 182 ? 0.3328 0.3152 0.3031 0.0887  0.0243  -0.0585 182 ILE D C   
7433  O O   . ILE D 182 ? 0.3436 0.3227 0.3067 0.0895  0.0290  -0.0612 182 ILE D O   
7434  C CB  . ILE D 182 ? 0.3143 0.3066 0.3020 0.0815  0.0284  -0.0563 182 ILE D CB  
7435  C CG1 . ILE D 182 ? 0.3015 0.2982 0.2999 0.0768  0.0312  -0.0526 182 ILE D CG1 
7436  C CG2 . ILE D 182 ? 0.3156 0.3078 0.3022 0.0830  0.0227  -0.0588 182 ILE D CG2 
7437  C CD1 . ILE D 182 ? 0.2991 0.2982 0.3011 0.0748  0.0326  -0.0540 182 ILE D CD1 
7438  N N   . PRO D 183 ? 0.3343 0.3139 0.3011 0.0915  0.0176  -0.0594 183 PRO D N   
7439  C CA  . PRO D 183 ? 0.3512 0.3224 0.3038 0.0960  0.0150  -0.0633 183 PRO D CA  
7440  C C   . PRO D 183 ? 0.3617 0.3308 0.3088 0.0966  0.0173  -0.0684 183 PRO D C   
7441  O O   . PRO D 183 ? 0.3557 0.3294 0.3097 0.0951  0.0166  -0.0693 183 PRO D O   
7442  C CB  . PRO D 183 ? 0.3500 0.3194 0.3032 0.0982  0.0063  -0.0637 183 PRO D CB  
7443  C CG  . PRO D 183 ? 0.3333 0.3103 0.3008 0.0949  0.0060  -0.0594 183 PRO D CG  
7444  C CD  . PRO D 183 ? 0.3237 0.3069 0.2993 0.0904  0.0124  -0.0575 183 PRO D CD  
7445  N N   . SER D 184 ? 0.3967 0.3583 0.3308 0.0988  0.0206  -0.0722 184 SER D N   
7446  C CA  . SER D 184 ? 0.4104 0.3689 0.3383 0.0995  0.0233  -0.0784 184 SER D CA  
7447  C C   . SER D 184 ? 0.4141 0.3700 0.3401 0.1020  0.0157  -0.0811 184 SER D C   
7448  O O   . SER D 184 ? 0.4198 0.3761 0.3460 0.1024  0.0167  -0.0854 184 SER D O   
7449  C CB  . SER D 184 ? 0.4314 0.3809 0.3435 0.1005  0.0285  -0.0829 184 SER D CB  
7450  O OG  . SER D 184 ? 0.4427 0.3940 0.3558 0.0982  0.0350  -0.0804 184 SER D OG  
7451  N N   . GLU D 185 ? 0.4396 0.3924 0.3641 0.1039  0.0078  -0.0792 185 GLU D N   
7452  C CA  . GLU D 185 ? 0.4446 0.3933 0.3666 0.1061  -0.0001 -0.0823 185 GLU D CA  
7453  C C   . GLU D 185 ? 0.4305 0.3876 0.3657 0.1041  -0.0024 -0.0812 185 GLU D C   
7454  O O   . GLU D 185 ? 0.4358 0.3894 0.3693 0.1058  -0.0082 -0.0843 185 GLU D O   
7455  C CB  . GLU D 185 ? 0.4456 0.3888 0.3641 0.1081  -0.0082 -0.0808 185 GLU D CB  
7456  C CG  . GLU D 185 ? 0.4667 0.3972 0.3672 0.1108  -0.0087 -0.0834 185 GLU D CG  
7457  C CD  . GLU D 185 ? 0.4651 0.3967 0.3639 0.1100  -0.0024 -0.0799 185 GLU D CD  
7458  O OE1 . GLU D 185 ? 0.4496 0.3916 0.3625 0.1076  0.0005  -0.0749 185 GLU D OE1 
7459  O OE2 . GLU D 185 ? 0.4848 0.4057 0.3670 0.1112  -0.0003 -0.0825 185 GLU D OE2 
7460  N N   . ILE D 186 ? 0.3771 0.3435 0.3241 0.1004  0.0019  -0.0771 186 ILE D N   
7461  C CA  . ILE D 186 ? 0.3665 0.3392 0.3236 0.0981  0.0005  -0.0766 186 ILE D CA  
7462  C C   . ILE D 186 ? 0.3780 0.3485 0.3309 0.1001  0.0016  -0.0818 186 ILE D C   
7463  O O   . ILE D 186 ? 0.3763 0.3479 0.3329 0.1004  -0.0025 -0.0834 186 ILE D O   
7464  C CB  . ILE D 186 ? 0.3504 0.3313 0.3185 0.0935  0.0055  -0.0717 186 ILE D CB  
7465  C CG1 . ILE D 186 ? 0.3412 0.3237 0.3134 0.0919  0.0049  -0.0672 186 ILE D CG1 
7466  C CG2 . ILE D 186 ? 0.3408 0.3267 0.3176 0.0910  0.0037  -0.0712 186 ILE D CG2 
7467  C CD1 . ILE D 186 ? 0.3366 0.3190 0.3128 0.0919  -0.0019 -0.0670 186 ILE D CD1 
7468  N N   . GLY D 187 ? 0.3829 0.3499 0.3282 0.1016  0.0074  -0.0852 187 GLY D N   
7469  C CA  . GLY D 187 ? 0.3969 0.3613 0.3378 0.1038  0.0092  -0.0914 187 GLY D CA  
7470  C C   . GLY D 187 ? 0.4106 0.3668 0.3433 0.1076  0.0024  -0.0961 187 GLY D C   
7471  O O   . GLY D 187 ? 0.4225 0.3763 0.3523 0.1098  0.0029  -0.1016 187 GLY D O   
7472  N N   . ARG D 188 ? 0.4426 0.3937 0.3713 0.1085  -0.0041 -0.0946 188 ARG D N   
7473  C CA  . ARG D 188 ? 0.4559 0.3978 0.3770 0.1116  -0.0115 -0.0988 188 ARG D CA  
7474  C C   . ARG D 188 ? 0.4465 0.3918 0.3767 0.1112  -0.0177 -0.0980 188 ARG D C   
7475  O O   . ARG D 188 ? 0.4614 0.3987 0.3861 0.1137  -0.0241 -0.1018 188 ARG D O   
7476  C CB  . ARG D 188 ? 0.4612 0.3951 0.3742 0.1126  -0.0169 -0.0979 188 ARG D CB  
7477  C CG  . ARG D 188 ? 0.4756 0.4028 0.3756 0.1133  -0.0119 -0.0997 188 ARG D CG  
7478  C CD  . ARG D 188 ? 0.4882 0.4033 0.3760 0.1150  -0.0193 -0.1008 188 ARG D CD  
7479  N NE  . ARG D 188 ? 0.5061 0.4140 0.3798 0.1150  -0.0146 -0.1021 188 ARG D NE  
7480  C CZ  . ARG D 188 ? 0.5254 0.4188 0.3813 0.1161  -0.0192 -0.1058 188 ARG D CZ  
7481  N NH1 . ARG D 188 ? 0.5404 0.4245 0.3910 0.1174  -0.0288 -0.1085 188 ARG D NH1 
7482  N NH2 . ARG D 188 ? 0.5386 0.4255 0.3805 0.1151  -0.0143 -0.1070 188 ARG D NH2 
7483  N N   . LEU D 189 ? 0.3981 0.3539 0.3410 0.1077  -0.0158 -0.0934 189 LEU D N   
7484  C CA  . LEU D 189 ? 0.3885 0.3470 0.3395 0.1064  -0.0209 -0.0926 189 LEU D CA  
7485  C C   . LEU D 189 ? 0.3985 0.3565 0.3488 0.1087  -0.0204 -0.0970 189 LEU D C   
7486  O O   . LEU D 189 ? 0.3928 0.3580 0.3507 0.1069  -0.0175 -0.0956 189 LEU D O   
7487  C CB  . LEU D 189 ? 0.3674 0.3357 0.3304 0.1014  -0.0184 -0.0866 189 LEU D CB  
7488  C CG  . LEU D 189 ? 0.3582 0.3281 0.3240 0.0992  -0.0185 -0.0825 189 LEU D CG  
7489  C CD1 . LEU D 189 ? 0.3396 0.3181 0.3174 0.0940  -0.0155 -0.0775 189 LEU D CD1 
7490  C CD2 . LEU D 189 ? 0.3646 0.3275 0.3270 0.1009  -0.0263 -0.0844 189 LEU D CD2 
7491  N N   . THR D 190 ? 0.3825 0.3307 0.3228 0.1130  -0.0237 -0.1028 190 THR D N   
7492  C CA  . THR D 190 ? 0.3947 0.3412 0.3330 0.1162  -0.0231 -0.1083 190 THR D CA  
7493  C C   . THR D 190 ? 0.3863 0.3363 0.3329 0.1156  -0.0273 -0.1073 190 THR D C   
7494  O O   . THR D 190 ? 0.3879 0.3418 0.3378 0.1168  -0.0252 -0.1096 190 THR D O   
7495  C CB  . THR D 190 ? 0.4190 0.3525 0.3442 0.1207  -0.0266 -0.1150 190 THR D CB  
7496  O OG1 . THR D 190 ? 0.4300 0.3599 0.3460 0.1211  -0.0208 -0.1172 190 THR D OG1 
7497  C CG2 . THR D 190 ? 0.4352 0.3659 0.3589 0.1245  -0.0277 -0.1213 190 THR D CG2 
7498  N N   . LYS D 191 ? 0.3580 0.3067 0.3083 0.1134  -0.0331 -0.1041 191 LYS D N   
7499  C CA  . LYS D 191 ? 0.3529 0.3025 0.3092 0.1126  -0.0372 -0.1036 191 LYS D CA  
7500  C C   . LYS D 191 ? 0.3320 0.2923 0.2992 0.1075  -0.0333 -0.0980 191 LYS D C   
7501  O O   . LYS D 191 ? 0.3274 0.2883 0.2993 0.1063  -0.0359 -0.0972 191 LYS D O   
7502  C CB  . LYS D 191 ? 0.3580 0.2985 0.3119 0.1128  -0.0452 -0.1040 191 LYS D CB  
7503  C CG  . LYS D 191 ? 0.3819 0.3091 0.3244 0.1180  -0.0506 -0.1103 191 LYS D CG  
7504  C CD  . LYS D 191 ? 0.3877 0.3047 0.3285 0.1175  -0.0592 -0.1106 191 LYS D CD  
7505  C CE  . LYS D 191 ? 0.4136 0.3153 0.3413 0.1221  -0.0649 -0.1168 191 LYS D CE  
7506  N NZ  . LYS D 191 ? 0.4208 0.3109 0.3464 0.1209  -0.0738 -0.1169 191 LYS D NZ  
7507  N N   . VAL D 192 ? 0.3329 0.3001 0.3034 0.1044  -0.0272 -0.0941 192 VAL D N   
7508  C CA  . VAL D 192 ? 0.3147 0.2903 0.2946 0.0992  -0.0235 -0.0889 192 VAL D CA  
7509  C C   . VAL D 192 ? 0.3138 0.2938 0.2968 0.0994  -0.0210 -0.0899 192 VAL D C   
7510  O O   . VAL D 192 ? 0.3237 0.3037 0.3033 0.1027  -0.0189 -0.0937 192 VAL D O   
7511  C CB  . VAL D 192 ? 0.3053 0.2853 0.2871 0.0961  -0.0183 -0.0847 192 VAL D CB  
7512  C CG1 . VAL D 192 ? 0.3082 0.2914 0.2882 0.0969  -0.0120 -0.0854 192 VAL D CG1 
7513  C CG2 . VAL D 192 ? 0.2882 0.2738 0.2792 0.0906  -0.0162 -0.0794 192 VAL D CG2 
7514  N N   . THR D 193 ? 0.2751 0.2585 0.2647 0.0961  -0.0213 -0.0871 193 THR D N   
7515  C CA  . THR D 193 ? 0.2734 0.2608 0.2662 0.0960  -0.0197 -0.0878 193 THR D CA  
7516  C C   . THR D 193 ? 0.3157 0.3098 0.3150 0.0907  -0.0141 -0.0827 193 THR D C   
7517  O O   . THR D 193 ? 0.3151 0.3131 0.3164 0.0908  -0.0115 -0.0834 193 THR D O   
7518  C CB  . THR D 193 ? 0.2774 0.2608 0.2705 0.0975  -0.0253 -0.0897 193 THR D CB  
7519  O OG1 . THR D 193 ? 0.2679 0.2501 0.2647 0.0934  -0.0262 -0.0858 193 THR D OG1 
7520  C CG2 . THR D 193 ? 0.2953 0.2706 0.2813 0.1034  -0.0312 -0.0954 193 THR D CG2 
7521  N N   . GLU D 194 ? 0.2971 0.2921 0.3000 0.0864  -0.0124 -0.0780 194 GLU D N   
7522  C CA  . GLU D 194 ? 0.2843 0.2843 0.2929 0.0815  -0.0070 -0.0731 194 GLU D CA  
7523  C C   . GLU D 194 ? 0.2790 0.2795 0.2882 0.0793  -0.0041 -0.0699 194 GLU D C   
7524  O O   . GLU D 194 ? 0.2794 0.2773 0.2883 0.0794  -0.0067 -0.0698 194 GLU D O   
7525  C CB  . GLU D 194 ? 0.2764 0.2766 0.2899 0.0781  -0.0073 -0.0707 194 GLU D CB  
7526  C CG  . GLU D 194 ? 0.2645 0.2683 0.2834 0.0732  -0.0016 -0.0656 194 GLU D CG  
7527  C CD  . GLU D 194 ? 0.2593 0.2631 0.2818 0.0707  -0.0011 -0.0638 194 GLU D CD  
7528  O OE1 . GLU D 194 ? 0.2627 0.2671 0.2842 0.0723  -0.0025 -0.0659 194 GLU D OE1 
7529  O OE2 . GLU D 194 ? 0.2527 0.2559 0.2794 0.0674  0.0009  -0.0606 194 GLU D OE2 
7530  N N   . ILE D 195 ? 0.2481 0.2515 0.2586 0.0775  0.0011  -0.0674 195 ILE D N   
7531  C CA  . ILE D 195 ? 0.2433 0.2471 0.2547 0.0756  0.0043  -0.0640 195 ILE D CA  
7532  C C   . ILE D 195 ? 0.2335 0.2400 0.2503 0.0714  0.0094  -0.0596 195 ILE D C   
7533  O O   . ILE D 195 ? 0.2341 0.2422 0.2509 0.0711  0.0125  -0.0596 195 ILE D O   
7534  C CB  . ILE D 195 ? 0.2519 0.2542 0.2573 0.0787  0.0057  -0.0659 195 ILE D CB  
7535  C CG1 . ILE D 195 ? 0.2634 0.2615 0.2624 0.0833  0.0006  -0.0704 195 ILE D CG1 
7536  C CG2 . ILE D 195 ? 0.2470 0.2495 0.2536 0.0769  0.0090  -0.0622 195 ILE D CG2 
7537  C CD1 . ILE D 195 ? 0.2746 0.2701 0.2665 0.0868  0.0027  -0.0731 195 ILE D CD1 
7538  N N   . ALA D 196 ? 0.2422 0.2490 0.2642 0.0682  0.0104  -0.0561 196 ALA D N   
7539  C CA  . ALA D 196 ? 0.2341 0.2424 0.2609 0.0645  0.0153  -0.0517 196 ALA D CA  
7540  C C   . ALA D 196 ? 0.2308 0.2387 0.2600 0.0634  0.0180  -0.0485 196 ALA D C   
7541  O O   . ALA D 196 ? 0.2288 0.2365 0.2611 0.0631  0.0165  -0.0479 196 ALA D O   
7542  C CB  . ALA D 196 ? 0.2290 0.2373 0.2598 0.0621  0.0151  -0.0504 196 ALA D CB  
7543  N N   . ILE D 197 ? 0.2430 0.2510 0.2716 0.0631  0.0218  -0.0468 197 ILE D N   
7544  C CA  . ILE D 197 ? 0.2408 0.2483 0.2719 0.0626  0.0246  -0.0438 197 ILE D CA  
7545  C C   . ILE D 197 ? 0.2362 0.2435 0.2707 0.0600  0.0299  -0.0400 197 ILE D C   
7546  O O   . ILE D 197 ? 0.2360 0.2426 0.2721 0.0599  0.0330  -0.0380 197 ILE D O   
7547  C CB  . ILE D 197 ? 0.2476 0.2539 0.2736 0.0657  0.0237  -0.0459 197 ILE D CB  
7548  C CG1 . ILE D 197 ? 0.2550 0.2605 0.2750 0.0690  0.0185  -0.0504 197 ILE D CG1 
7549  C CG2 . ILE D 197 ? 0.2462 0.2522 0.2752 0.0661  0.0240  -0.0439 197 ILE D CG2 
7550  C CD1 . ILE D 197 ? 0.2642 0.2676 0.2769 0.0725  0.0185  -0.0528 197 ILE D CD1 
7551  N N   . TYR D 198 ? 0.2403 0.2479 0.2757 0.0583  0.0307  -0.0391 198 TYR D N   
7552  C CA  . TYR D 198 ? 0.2378 0.2447 0.2744 0.0567  0.0352  -0.0360 198 TYR D CA  
7553  C C   . TYR D 198 ? 0.2339 0.2405 0.2727 0.0555  0.0369  -0.0308 198 TYR D C   
7554  O O   . TYR D 198 ? 0.2374 0.2449 0.2782 0.0562  0.0355  -0.0301 198 TYR D O   
7555  C CB  . TYR D 198 ? 0.2379 0.2457 0.2735 0.0559  0.0344  -0.0369 198 TYR D CB  
7556  C CG  . TYR D 198 ? 0.2337 0.2421 0.2708 0.0550  0.0322  -0.0365 198 TYR D CG  
7557  C CD1 . TYR D 198 ? 0.2297 0.2380 0.2677 0.0539  0.0340  -0.0326 198 TYR D CD1 
7558  C CD2 . TYR D 198 ? 0.2356 0.2447 0.2721 0.0558  0.0280  -0.0401 198 TYR D CD2 
7559  C CE1 . TYR D 198 ? 0.2273 0.2363 0.2667 0.0531  0.0323  -0.0327 198 TYR D CE1 
7560  C CE2 . TYR D 198 ? 0.2331 0.2422 0.2713 0.0548  0.0266  -0.0397 198 TYR D CE2 
7561  C CZ  . TYR D 198 ? 0.2288 0.2377 0.2688 0.0531  0.0292  -0.0360 198 TYR D CZ  
7562  O OH  . TYR D 198 ? 0.2270 0.2357 0.2685 0.0523  0.0281  -0.0358 198 TYR D OH  
7563  N N   . ASP D 199 ? 0.2351 0.2412 0.2717 0.0547  0.0391  -0.0274 199 ASP D N   
7564  C CA  . ASP D 199 ? 0.2336 0.2431 0.2665 0.0570  0.0371  -0.0240 199 ASP D CA  
7565  C C   . ASP D 199 ? 0.2353 0.2446 0.2701 0.0585  0.0375  -0.0228 199 ASP D C   
7566  O O   . ASP D 199 ? 0.2332 0.2464 0.2714 0.0596  0.0349  -0.0237 199 ASP D O   
7567  C CB  . ASP D 199 ? 0.2308 0.2447 0.2672 0.0561  0.0342  -0.0259 199 ASP D CB  
7568  C CG  . ASP D 199 ? 0.2243 0.2435 0.2665 0.0549  0.0332  -0.0275 199 ASP D CG  
7569  O OD1 . ASP D 199 ? 0.2247 0.2456 0.2679 0.0555  0.0332  -0.0280 199 ASP D OD1 
7570  O OD2 . ASP D 199 ? 0.2219 0.2419 0.2694 0.0525  0.0338  -0.0280 199 ASP D OD2 
7571  N N   . ASN D 200 ? 0.2254 0.2298 0.2650 0.0558  0.0420  -0.0227 200 ASN D N   
7572  C CA  . ASN D 200 ? 0.2253 0.2301 0.2737 0.0549  0.0423  -0.0247 200 ASN D CA  
7573  C C   . ASN D 200 ? 0.2210 0.2317 0.2816 0.0503  0.0399  -0.0332 200 ASN D C   
7574  O O   . ASN D 200 ? 0.2167 0.2385 0.2752 0.0508  0.0319  -0.0409 200 ASN D O   
7575  C CB  . ASN D 200 ? 0.2274 0.2334 0.2751 0.0575  0.0390  -0.0300 200 ASN D CB  
7576  C CG  . ASN D 200 ? 0.2268 0.2339 0.2751 0.0598  0.0365  -0.0292 200 ASN D CG  
7577  O OD1 . ASN D 200 ? 0.2275 0.2357 0.2793 0.0617  0.0358  -0.0278 200 ASN D OD1 
7578  N ND2 . ASN D 200 ? 0.2256 0.2331 0.2718 0.0597  0.0348  -0.0308 200 ASN D ND2 
7579  N N   . LEU D 201 ? 0.2119 0.2229 0.2716 0.0540  0.0389  -0.0341 201 LEU D N   
7580  C CA  . LEU D 201 ? 0.2140 0.2282 0.2716 0.0566  0.0372  -0.0371 201 LEU D CA  
7581  C C   . LEU D 201 ? 0.2219 0.2315 0.2706 0.0607  0.0396  -0.0372 201 LEU D C   
7582  O O   . LEU D 201 ? 0.2267 0.2352 0.2726 0.0645  0.0399  -0.0374 201 LEU D O   
7583  C CB  . LEU D 201 ? 0.2138 0.2310 0.2765 0.0588  0.0346  -0.0372 201 LEU D CB  
7584  C CG  . LEU D 201 ? 0.2105 0.2352 0.2712 0.0609  0.0292  -0.0379 201 LEU D CG  
7585  C CD1 . LEU D 201 ? 0.2132 0.2402 0.2766 0.0652  0.0267  -0.0370 201 LEU D CD1 
7586  C CD2 . LEU D 201 ? 0.2114 0.2351 0.2671 0.0618  0.0329  -0.0349 201 LEU D CD2 
7587  N N   . LEU D 202 ? 0.2430 0.2504 0.2863 0.0609  0.0406  -0.0380 202 LEU D N   
7588  C CA  . LEU D 202 ? 0.2520 0.2566 0.2849 0.0648  0.0404  -0.0398 202 LEU D CA  
7589  C C   . LEU D 202 ? 0.2564 0.2609 0.2854 0.0651  0.0431  -0.0411 202 LEU D C   
7590  O O   . LEU D 202 ? 0.2522 0.2595 0.2859 0.0621  0.0449  -0.0421 202 LEU D O   
7591  C CB  . LEU D 202 ? 0.2544 0.2581 0.2825 0.0651  0.0394  -0.0413 202 LEU D CB  
7592  C CG  . LEU D 202 ? 0.2568 0.2597 0.2811 0.0678  0.0347  -0.0418 202 LEU D CG  
7593  C CD1 . LEU D 202 ? 0.2509 0.2550 0.2829 0.0671  0.0334  -0.0393 202 LEU D CD1 
7594  C CD2 . LEU D 202 ? 0.2572 0.2605 0.2793 0.0675  0.0330  -0.0437 202 LEU D CD2 
7595  N N   . THR D 203 ? 0.2869 0.2881 0.3065 0.0690  0.0431  -0.0416 203 THR D N   
7596  C CA  . THR D 203 ? 0.2939 0.2936 0.3077 0.0699  0.0465  -0.0426 203 THR D CA  
7597  C C   . THR D 203 ? 0.3065 0.3028 0.3105 0.0723  0.0478  -0.0459 203 THR D C   
7598  O O   . THR D 203 ? 0.3093 0.3046 0.3106 0.0737  0.0453  -0.0473 203 THR D O   
7599  C CB  . THR D 203 ? 0.2973 0.2943 0.3078 0.0727  0.0464  -0.0395 203 THR D CB  
7600  O OG1 . THR D 203 ? 0.3042 0.2969 0.3074 0.0770  0.0435  -0.0390 203 THR D OG1 
7601  C CG2 . THR D 203 ? 0.2878 0.2883 0.3086 0.0707  0.0450  -0.0370 203 THR D CG2 
7602  N N   . GLY D 204 ? 0.3237 0.3182 0.3219 0.0730  0.0519  -0.0477 204 GLY D N   
7603  C CA  . GLY D 204 ? 0.3358 0.3269 0.3245 0.0750  0.0544  -0.0520 204 GLY D CA  
7604  C C   . GLY D 204 ? 0.3358 0.3302 0.3291 0.0725  0.0569  -0.0568 204 GLY D C   
7605  O O   . GLY D 204 ? 0.3259 0.3245 0.3291 0.0692  0.0567  -0.0562 204 GLY D O   
7606  N N   . PRO D 205 ? 0.3417 0.3333 0.3272 0.0741  0.0596  -0.0617 205 PRO D N   
7607  C CA  . PRO D 205 ? 0.3446 0.3382 0.3337 0.0724  0.0628  -0.0664 205 PRO D CA  
7608  C C   . PRO D 205 ? 0.3431 0.3359 0.3319 0.0744  0.0573  -0.0651 205 PRO D C   
7609  O O   . PRO D 205 ? 0.3390 0.3302 0.3246 0.0768  0.0514  -0.0621 205 PRO D O   
7610  C CB  . PRO D 205 ? 0.3620 0.3528 0.3415 0.0734  0.0684  -0.0730 205 PRO D CB  
7611  C CG  . PRO D 205 ? 0.3690 0.3538 0.3366 0.0772  0.0649  -0.0708 205 PRO D CG  
7612  C CD  . PRO D 205 ? 0.3566 0.3421 0.3284 0.0775  0.0607  -0.0635 205 PRO D CD  
7613  N N   . ILE D 206 ? 0.3076 0.3016 0.2992 0.0739  0.0591  -0.0677 206 ILE D N   
7614  C CA  . ILE D 206 ? 0.3085 0.3024 0.2977 0.0767  0.0535  -0.0684 206 ILE D CA  
7615  C C   . ILE D 206 ? 0.3244 0.3139 0.3030 0.0803  0.0539  -0.0736 206 ILE D C   
7616  O O   . ILE D 206 ? 0.3370 0.3245 0.3116 0.0800  0.0610  -0.0787 206 ILE D O   
7617  C CB  . ILE D 206 ? 0.3065 0.3034 0.3010 0.0761  0.0542  -0.0696 206 ILE D CB  
7618  C CG1 . ILE D 206 ? 0.2915 0.2915 0.2944 0.0729  0.0523  -0.0642 206 ILE D CG1 
7619  C CG2 . ILE D 206 ? 0.3115 0.3086 0.3025 0.0797  0.0488  -0.0727 206 ILE D CG2 
7620  C CD1 . ILE D 206 ? 0.2908 0.2931 0.2978 0.0722  0.0544  -0.0649 206 ILE D CD1 
7621  N N   . PRO D 207 ? 0.3441 0.3313 0.3174 0.0834  0.0473  -0.0732 207 PRO D N   
7622  C CA  . PRO D 207 ? 0.3611 0.3424 0.3225 0.0868  0.0475  -0.0784 207 PRO D CA  
7623  C C   . PRO D 207 ? 0.3730 0.3540 0.3327 0.0879  0.0510  -0.0849 207 PRO D C   
7624  O O   . PRO D 207 ? 0.3684 0.3527 0.3332 0.0889  0.0471  -0.0853 207 PRO D O   
7625  C CB  . PRO D 207 ? 0.3579 0.3371 0.3164 0.0897  0.0384  -0.0763 207 PRO D CB  
7626  C CG  . PRO D 207 ? 0.3402 0.3240 0.3079 0.0872  0.0353  -0.0696 207 PRO D CG  
7627  C CD  . PRO D 207 ? 0.3315 0.3206 0.3088 0.0835  0.0397  -0.0684 207 PRO D CD  
7628  N N   . SER D 208 ? 0.3972 0.3743 0.3491 0.0877  0.0587  -0.0907 208 SER D N   
7629  C CA  . SER D 208 ? 0.4117 0.3878 0.3609 0.0890  0.0632  -0.0979 208 SER D CA  
7630  C C   . SER D 208 ? 0.4199 0.3926 0.3630 0.0933  0.0565  -0.1013 208 SER D C   
7631  O O   . SER D 208 ? 0.4290 0.4022 0.3721 0.0954  0.0576  -0.1066 208 SER D O   
7632  C CB  . SER D 208 ? 0.4336 0.4054 0.3741 0.0867  0.0741  -0.1043 208 SER D CB  
7633  O OG  . SER D 208 ? 0.4541 0.4204 0.3831 0.0868  0.0731  -0.1053 208 SER D OG  
7634  N N   . SER D 209 ? 0.4042 0.3732 0.3421 0.0951  0.0493  -0.0986 209 SER D N   
7635  C CA  . SER D 209 ? 0.4107 0.3759 0.3436 0.0990  0.0418  -0.1012 209 SER D CA  
7636  C C   . SER D 209 ? 0.3972 0.3685 0.3408 0.0998  0.0351  -0.0988 209 SER D C   
7637  O O   . SER D 209 ? 0.4023 0.3707 0.3431 0.1029  0.0287  -0.1013 209 SER D O   
7638  C CB  . SER D 209 ? 0.4114 0.3706 0.3363 0.1005  0.0354  -0.0985 209 SER D CB  
7639  O OG  . SER D 209 ? 0.3913 0.3555 0.3252 0.0990  0.0309  -0.0907 209 SER D OG  
7640  N N   . PHE D 210 ? 0.3862 0.3650 0.3412 0.0969  0.0365  -0.0944 210 PHE D N   
7641  C CA  . PHE D 210 ? 0.3749 0.3590 0.3385 0.0969  0.0306  -0.0927 210 PHE D CA  
7642  C C   . PHE D 210 ? 0.3863 0.3710 0.3498 0.1000  0.0307  -0.0993 210 PHE D C   
7643  O O   . PHE D 210 ? 0.3813 0.3684 0.3491 0.1013  0.0244  -0.0994 210 PHE D O   
7644  C CB  . PHE D 210 ? 0.3580 0.3486 0.3318 0.0926  0.0326  -0.0870 210 PHE D CB  
7645  C CG  . PHE D 210 ? 0.3432 0.3349 0.3204 0.0902  0.0284  -0.0803 210 PHE D CG  
7646  C CD1 . PHE D 210 ? 0.3458 0.3331 0.3170 0.0916  0.0250  -0.0793 210 PHE D CD1 
7647  C CD2 . PHE D 210 ? 0.3291 0.3258 0.3151 0.0865  0.0280  -0.0756 210 PHE D CD2 
7648  C CE1 . PHE D 210 ? 0.3330 0.3217 0.3081 0.0896  0.0214  -0.0739 210 PHE D CE1 
7649  C CE2 . PHE D 210 ? 0.3163 0.3137 0.3055 0.0840  0.0252  -0.0703 210 PHE D CE2 
7650  C CZ  . PHE D 210 ? 0.3185 0.3125 0.3029 0.0856  0.0220  -0.0696 210 PHE D CZ  
7651  N N   . GLY D 211 ? 0.3798 0.3621 0.3382 0.1012  0.0381  -0.1053 211 GLY D N   
7652  C CA  . GLY D 211 ? 0.3938 0.3759 0.3509 0.1051  0.0381  -0.1128 211 GLY D CA  
7653  C C   . GLY D 211 ? 0.4030 0.3792 0.3536 0.1091  0.0307  -0.1161 211 GLY D C   
7654  O O   . GLY D 211 ? 0.4094 0.3862 0.3616 0.1125  0.0270  -0.1207 211 GLY D O   
7655  N N   . ASN D 212 ? 0.4088 0.3785 0.3516 0.1089  0.0280  -0.1141 212 ASN D N   
7656  C CA  . ASN D 212 ? 0.4181 0.3807 0.3538 0.1125  0.0204  -0.1168 212 ASN D CA  
7657  C C   . ASN D 212 ? 0.4039 0.3698 0.3474 0.1128  0.0111  -0.1129 212 ASN D C   
7658  O O   . ASN D 212 ? 0.4120 0.3716 0.3507 0.1158  0.0043  -0.1155 212 ASN D O   
7659  C CB  . ASN D 212 ? 0.4238 0.3785 0.3490 0.1121  0.0195  -0.1155 212 ASN D CB  
7660  C CG  . ASN D 212 ? 0.4434 0.3922 0.3570 0.1117  0.0284  -0.1213 212 ASN D CG  
7661  O OD1 . ASN D 212 ? 0.4548 0.4048 0.3679 0.1120  0.0356  -0.1271 212 ASN D OD1 
7662  N ND2 . ASN D 212 ? 0.4513 0.3934 0.3549 0.1108  0.0282  -0.1200 212 ASN D ND2 
7663  N N   . LEU D 213 ? 0.3816 0.3558 0.3359 0.1094  0.0109  -0.1072 213 LEU D N   
7664  C CA  . LEU D 213 ? 0.3688 0.3459 0.3298 0.1086  0.0035  -0.1037 213 LEU D CA  
7665  C C   . LEU D 213 ? 0.3727 0.3528 0.3382 0.1109  0.0019  -0.1079 213 LEU D C   
7666  O O   . LEU D 213 ? 0.3611 0.3479 0.3348 0.1085  0.0023  -0.1053 213 LEU D O   
7667  C CB  . LEU D 213 ? 0.3484 0.3316 0.3173 0.1033  0.0046  -0.0960 213 LEU D CB  
7668  C CG  . LEU D 213 ? 0.3441 0.3255 0.3099 0.1013  0.0066  -0.0919 213 LEU D CG  
7669  C CD1 . LEU D 213 ? 0.3263 0.3139 0.3004 0.0963  0.0094  -0.0854 213 LEU D CD1 
7670  C CD2 . LEU D 213 ? 0.3465 0.3221 0.3075 0.1028  -0.0003 -0.0916 213 LEU D CD2 
7671  N N   . THR D 214 ? 0.3875 0.3616 0.3467 0.1159  -0.0003 -0.1150 214 THR D N   
7672  C CA  . THR D 214 ? 0.3952 0.3715 0.3577 0.1193  -0.0017 -0.1204 214 THR D CA  
7673  C C   . THR D 214 ? 0.3839 0.3628 0.3530 0.1186  -0.0088 -0.1175 214 THR D C   
7674  O O   . THR D 214 ? 0.3824 0.3666 0.3575 0.1194  -0.0091 -0.1194 214 THR D O   
7675  C CB  . THR D 214 ? 0.4187 0.3864 0.3722 0.1250  -0.0032 -0.1288 214 THR D CB  
7676  O OG1 . THR D 214 ? 0.4223 0.3813 0.3694 0.1261  -0.0105 -0.1278 214 THR D OG1 
7677  C CG2 . THR D 214 ? 0.4326 0.3978 0.3790 0.1253  0.0056  -0.1331 214 THR D CG2 
7678  N N   . LYS D 215 ? 0.3777 0.3528 0.3455 0.1170  -0.0144 -0.1134 215 LYS D N   
7679  C CA  . LYS D 215 ? 0.3691 0.3449 0.3418 0.1159  -0.0204 -0.1109 215 LYS D CA  
7680  C C   . LYS D 215 ? 0.3489 0.3329 0.3298 0.1100  -0.0175 -0.1043 215 LYS D C   
7681  O O   . LYS D 215 ? 0.3418 0.3264 0.3265 0.1085  -0.0212 -0.1022 215 LYS D O   
7682  C CB  . LYS D 215 ? 0.3716 0.3392 0.3397 0.1163  -0.0271 -0.1098 215 LYS D CB  
7683  C CG  . LYS D 215 ? 0.3934 0.3506 0.3521 0.1219  -0.0310 -0.1164 215 LYS D CG  
7684  C CD  . LYS D 215 ? 0.4052 0.3580 0.3633 0.1264  -0.0369 -0.1214 215 LYS D CD  
7685  C CE  . LYS D 215 ? 0.4296 0.3736 0.3788 0.1326  -0.0382 -0.1296 215 LYS D CE  
7686  N NZ  . LYS D 215 ? 0.4425 0.3832 0.3920 0.1377  -0.0432 -0.1353 215 LYS D NZ  
7687  N N   . LEU D 216 ? 0.3342 0.3230 0.3172 0.1067  -0.0109 -0.1011 216 LEU D N   
7688  C CA  . LEU D 216 ? 0.3167 0.3116 0.3066 0.1012  -0.0079 -0.0950 216 LEU D CA  
7689  C C   . LEU D 216 ? 0.3142 0.3139 0.3096 0.1011  -0.0080 -0.0963 216 LEU D C   
7690  O O   . LEU D 216 ? 0.3235 0.3253 0.3193 0.1042  -0.0062 -0.1013 216 LEU D O   
7691  C CB  . LEU D 216 ? 0.3124 0.3098 0.3024 0.0985  -0.0009 -0.0922 216 LEU D CB  
7692  C CG  . LEU D 216 ? 0.2959 0.2975 0.2917 0.0927  0.0024  -0.0855 216 LEU D CG  
7693  C CD1 . LEU D 216 ? 0.2869 0.2866 0.2834 0.0901  -0.0007 -0.0812 216 LEU D CD1 
7694  C CD2 . LEU D 216 ? 0.2957 0.2986 0.2910 0.0913  0.0094  -0.0840 216 LEU D CD2 
7695  N N   . VAL D 217 ? 0.3020 0.3035 0.3019 0.0975  -0.0098 -0.0922 217 VAL D N   
7696  C CA  . VAL D 217 ? 0.2991 0.3049 0.3037 0.0972  -0.0100 -0.0930 217 VAL D CA  
7697  C C   . VAL D 217 ? 0.2843 0.2943 0.2939 0.0913  -0.0054 -0.0872 217 VAL D C   
7698  O O   . VAL D 217 ? 0.2822 0.2965 0.2956 0.0906  -0.0036 -0.0878 217 VAL D O   
7699  C CB  . VAL D 217 ? 0.3024 0.3046 0.3065 0.0992  -0.0168 -0.0947 217 VAL D CB  
7700  C CG1 . VAL D 217 ? 0.3185 0.3144 0.3168 0.1052  -0.0218 -0.1003 217 VAL D CG1 
7701  C CG2 . VAL D 217 ? 0.2909 0.2911 0.2964 0.0946  -0.0174 -0.0890 217 VAL D CG2 
7702  N N   . ASN D 218 ? 0.2734 0.2821 0.2831 0.0873  -0.0036 -0.0819 218 ASN D N   
7703  C CA  . ASN D 218 ? 0.2604 0.2717 0.2746 0.0818  0.0006  -0.0763 218 ASN D CA  
7704  C C   . ASN D 218 ? 0.2567 0.2676 0.2701 0.0797  0.0050  -0.0729 218 ASN D C   
7705  O O   . ASN D 218 ? 0.2559 0.2641 0.2674 0.0795  0.0036  -0.0716 218 ASN D O   
7706  C CB  . ASN D 218 ? 0.2527 0.2623 0.2691 0.0790  -0.0015 -0.0731 218 ASN D CB  
7707  C CG  . ASN D 218 ? 0.2557 0.2653 0.2728 0.0807  -0.0052 -0.0756 218 ASN D CG  
7708  O OD1 . ASN D 218 ? 0.2624 0.2742 0.2794 0.0838  -0.0064 -0.0796 218 ASN D OD1 
7709  N ND2 . ASN D 218 ? 0.2514 0.2584 0.2697 0.0788  -0.0068 -0.0734 218 ASN D ND2 
7710  N N   . LEU D 219 ? 0.2243 0.2376 0.2393 0.0783  0.0100  -0.0718 219 LEU D N   
7711  C CA  . LEU D 219 ? 0.2214 0.2337 0.2356 0.0764  0.0145  -0.0685 219 LEU D CA  
7712  C C   . LEU D 219 ? 0.2111 0.2248 0.2299 0.0719  0.0184  -0.0636 219 LEU D C   
7713  O O   . LEU D 219 ? 0.2110 0.2269 0.2321 0.0713  0.0208  -0.0641 219 LEU D O   
7714  C CB  . LEU D 219 ? 0.2314 0.2435 0.2424 0.0792  0.0180  -0.0719 219 LEU D CB  
7715  C CG  . LEU D 219 ? 0.2313 0.2412 0.2400 0.0782  0.0223  -0.0692 219 LEU D CG  
7716  C CD1 . LEU D 219 ? 0.2282 0.2355 0.2349 0.0780  0.0189  -0.0670 219 LEU D CD1 
7717  C CD2 . LEU D 219 ? 0.2442 0.2527 0.2483 0.0815  0.0258  -0.0737 219 LEU D CD2 
7718  N N   . TYR D 220 ? 0.2405 0.2528 0.2610 0.0690  0.0190  -0.0592 220 TYR D N   
7719  C CA  . TYR D 220 ? 0.2318 0.2443 0.2564 0.0650  0.0227  -0.0544 220 TYR D CA  
7720  C C   . TYR D 220 ? 0.2299 0.2407 0.2545 0.0640  0.0263  -0.0512 220 TYR D C   
7721  O O   . TYR D 220 ? 0.2282 0.2378 0.2529 0.0639  0.0249  -0.0500 220 TYR D O   
7722  C CB  . TYR D 220 ? 0.2253 0.2374 0.2528 0.0628  0.0208  -0.0523 220 TYR D CB  
7723  C CG  . TYR D 220 ? 0.2278 0.2409 0.2550 0.0641  0.0169  -0.0555 220 TYR D CG  
7724  C CD1 . TYR D 220 ? 0.2317 0.2472 0.2588 0.0657  0.0166  -0.0585 220 TYR D CD1 
7725  C CD2 . TYR D 220 ? 0.2268 0.2386 0.2545 0.0641  0.0136  -0.0559 220 TYR D CD2 
7726  C CE1 . TYR D 220 ? 0.2349 0.2512 0.2619 0.0675  0.0126  -0.0618 220 TYR D CE1 
7727  C CE2 . TYR D 220 ? 0.2301 0.2420 0.2572 0.0658  0.0099  -0.0588 220 TYR D CE2 
7728  C CZ  . TYR D 220 ? 0.2342 0.2484 0.2608 0.0677  0.0092  -0.0618 220 TYR D CZ  
7729  O OH  . TYR D 220 ? 0.2385 0.2527 0.2646 0.0699  0.0050  -0.0650 220 TYR D OH  
7730  N N   . LEU D 221 ? 0.2174 0.2279 0.2424 0.0633  0.0308  -0.0502 221 LEU D N   
7731  C CA  . LEU D 221 ? 0.2170 0.2255 0.2421 0.0627  0.0345  -0.0477 221 LEU D CA  
7732  C C   . LEU D 221 ? 0.2125 0.2200 0.2411 0.0600  0.0394  -0.0439 221 LEU D C   
7733  O O   . LEU D 221 ? 0.2142 0.2202 0.2434 0.0596  0.0433  -0.0432 221 LEU D O   
7734  C CB  . LEU D 221 ? 0.2262 0.2338 0.2467 0.0655  0.0358  -0.0510 221 LEU D CB  
7735  C CG  . LEU D 221 ? 0.2332 0.2405 0.2487 0.0691  0.0314  -0.0548 221 LEU D CG  
7736  C CD1 . LEU D 221 ? 0.2440 0.2496 0.2544 0.0718  0.0344  -0.0582 221 LEU D CD1 
7737  C CD2 . LEU D 221 ? 0.2297 0.2359 0.2451 0.0691  0.0283  -0.0529 221 LEU D CD2 
7738  N N   . PHE D 222 ? 0.2163 0.2244 0.2471 0.0582  0.0391  -0.0418 222 PHE D N   
7739  C CA  . PHE D 222 ? 0.2140 0.2209 0.2459 0.0565  0.0428  -0.0383 222 PHE D CA  
7740  C C   . PHE D 222 ? 0.2095 0.2147 0.2425 0.0543  0.0434  -0.0329 222 PHE D C   
7741  O O   . PHE D 222 ? 0.2074 0.2126 0.2420 0.0542  0.0419  -0.0324 222 PHE D O   
7742  C CB  . PHE D 222 ? 0.2120 0.2207 0.2443 0.0564  0.0416  -0.0387 222 PHE D CB  
7743  C CG  . PHE D 222 ? 0.2078 0.2175 0.2414 0.0554  0.0379  -0.0386 222 PHE D CG  
7744  C CD1 . PHE D 222 ? 0.2100 0.2214 0.2432 0.0565  0.0337  -0.0426 222 PHE D CD1 
7745  C CD2 . PHE D 222 ? 0.2029 0.2119 0.2369 0.0541  0.0384  -0.0345 222 PHE D CD2 
7746  C CE1 . PHE D 222 ? 0.2068 0.2184 0.2411 0.0556  0.0310  -0.0423 222 PHE D CE1 
7747  C CE2 . PHE D 222 ? 0.1998 0.2093 0.2351 0.0533  0.0361  -0.0345 222 PHE D CE2 
7748  C CZ  . PHE D 222 ? 0.2016 0.2119 0.2374 0.0537  0.0327  -0.0383 222 PHE D CZ  
7749  N N   . ILE D 223 ? 0.2207 0.2250 0.2504 0.0543  0.0450  -0.0288 223 ILE D N   
7750  C CA  . ILE D 223 ? 0.2192 0.2271 0.2416 0.0580  0.0411  -0.0249 223 ILE D CA  
7751  C C   . ILE D 223 ? 0.2194 0.2204 0.2542 0.0518  0.0478  -0.0249 223 ILE D C   
7752  O O   . ILE D 223 ? 0.2169 0.2187 0.2552 0.0515  0.0463  -0.0248 223 ILE D O   
7753  C CB  . ILE D 223 ? 0.2125 0.2257 0.2382 0.0573  0.0366  -0.0265 223 ILE D CB  
7754  C CG1 . ILE D 223 ? 0.2102 0.2234 0.2384 0.0553  0.0371  -0.0275 223 ILE D CG1 
7755  C CG2 . ILE D 223 ? 0.2065 0.2268 0.2395 0.0559  0.0334  -0.0300 223 ILE D CG2 
7756  C CD1 . ILE D 223 ? 0.2052 0.2202 0.2375 0.0536  0.0354  -0.0280 223 ILE D CD1 
7757  N N   . ASN D 224 ? 0.2418 0.2521 0.2929 0.0457  0.0449  -0.0382 224 ASN D N   
7758  C CA  . ASN D 224 ? 0.2446 0.2571 0.2936 0.0491  0.0431  -0.0407 224 ASN D CA  
7759  C C   . ASN D 224 ? 0.2473 0.2650 0.2934 0.0514  0.0418  -0.0445 224 ASN D C   
7760  O O   . ASN D 224 ? 0.2541 0.2775 0.2976 0.0524  0.0392  -0.0460 224 ASN D O   
7761  C CB  . ASN D 224 ? 0.2521 0.2588 0.2928 0.0535  0.0452  -0.0388 224 ASN D CB  
7762  C CG  . ASN D 224 ? 0.2501 0.2560 0.2907 0.0551  0.0430  -0.0366 224 ASN D CG  
7763  O OD1 . ASN D 224 ? 0.2492 0.2557 0.2925 0.0558  0.0418  -0.0363 224 ASN D OD1 
7764  N ND2 . ASN D 224 ? 0.2498 0.2550 0.2876 0.0561  0.0417  -0.0360 224 ASN D ND2 
7765  N N   . SER D 225 ? 0.2938 0.3085 0.3357 0.0546  0.0441  -0.0440 225 SER D N   
7766  C CA  . SER D 225 ? 0.2988 0.3143 0.3361 0.0570  0.0462  -0.0453 225 SER D CA  
7767  C C   . SER D 225 ? 0.3093 0.3211 0.3413 0.0590  0.0498  -0.0476 225 SER D C   
7768  O O   . SER D 225 ? 0.3160 0.3257 0.3424 0.0621  0.0520  -0.0478 225 SER D O   
7769  C CB  . SER D 225 ? 0.2991 0.3135 0.3348 0.0598  0.0465  -0.0422 225 SER D CB  
7770  O OG  . SER D 225 ? 0.2968 0.3134 0.3342 0.0591  0.0456  -0.0399 225 SER D OG  
7771  N N   . LEU D 226 ? 0.2808 0.2901 0.3123 0.0581  0.0511  -0.0487 226 LEU D N   
7772  C CA  . LEU D 226 ? 0.2917 0.2981 0.3163 0.0609  0.0543  -0.0518 226 LEU D CA  
7773  C C   . LEU D 226 ? 0.2967 0.3061 0.3215 0.0595  0.0576  -0.0557 226 LEU D C   
7774  O O   . LEU D 226 ? 0.2918 0.3058 0.3225 0.0563  0.0570  -0.0566 226 LEU D O   
7775  C CB  . LEU D 226 ? 0.2947 0.2984 0.3169 0.0621  0.0544  -0.0522 226 LEU D CB  
7776  C CG  . LEU D 226 ? 0.2898 0.2929 0.3113 0.0636  0.0494  -0.0495 226 LEU D CG  
7777  C CD1 . LEU D 226 ? 0.2920 0.2951 0.3108 0.0650  0.0473  -0.0506 226 LEU D CD1 
7778  C CD2 . LEU D 226 ? 0.2945 0.2959 0.3097 0.0669  0.0463  -0.0495 226 LEU D CD2 
7779  N N   . SER D 227 ? 0.3314 0.3392 0.3491 0.0623  0.0606  -0.0587 227 SER D N   
7780  C CA  . SER D 227 ? 0.3375 0.3492 0.3534 0.0621  0.0636  -0.0624 227 SER D CA  
7781  C C   . SER D 227 ? 0.3504 0.3612 0.3622 0.0620  0.0684  -0.0684 227 SER D C   
7782  O O   . SER D 227 ? 0.3555 0.3607 0.3639 0.0631  0.0696  -0.0687 227 SER D O   
7783  C CB  . SER D 227 ? 0.3412 0.3495 0.3499 0.0655  0.0647  -0.0593 227 SER D CB  
7784  O OG  . SER D 227 ? 0.3484 0.3496 0.3482 0.0684  0.0641  -0.0572 227 SER D OG  
7785  N N   . GLY D 228 ? 0.3729 0.3897 0.3828 0.0621  0.0708  -0.0729 228 GLY D N   
7786  C CA  . GLY D 228 ? 0.3903 0.4090 0.3968 0.0616  0.0755  -0.0801 228 GLY D CA  
7787  C C   . GLY D 228 ? 0.3879 0.4030 0.4025 0.0564  0.0802  -0.0816 228 GLY D C   
7788  O O   . GLY D 228 ? 0.3857 0.3914 0.4033 0.0550  0.0819  -0.0735 228 GLY D O   
7789  N N   . SER D 229 ? 0.3861 0.3922 0.3934 0.0557  0.0897  -0.0843 229 SER D N   
7790  C CA  . SER D 229 ? 0.4110 0.3948 0.3957 0.0679  0.0972  -0.0709 229 SER D CA  
7791  C C   . SER D 229 ? 0.3987 0.3880 0.3888 0.0692  0.0903  -0.0751 229 SER D C   
7792  O O   . SER D 229 ? 0.3940 0.3855 0.3859 0.0677  0.0862  -0.0782 229 SER D O   
7793  C CB  . SER D 229 ? 0.4360 0.4158 0.4015 0.0775  0.1024  -0.0720 229 SER D CB  
7794  O OG  . SER D 229 ? 0.4437 0.4412 0.3949 0.0918  0.0932  -0.0704 229 SER D OG  
7795  N N   . ILE D 230 ? 0.3668 0.3598 0.3575 0.0743  0.0875  -0.0754 230 ILE D N   
7796  C CA  . ILE D 230 ? 0.3625 0.3588 0.3562 0.0766  0.0816  -0.0792 230 ILE D CA  
7797  C C   . ILE D 230 ? 0.3797 0.3732 0.3656 0.0797  0.0849  -0.0865 230 ILE D C   
7798  O O   . ILE D 230 ? 0.3947 0.3877 0.3756 0.0821  0.0910  -0.0904 230 ILE D O   
7799  C CB  . ILE D 230 ? 0.3556 0.3588 0.3559 0.0786  0.0769  -0.0796 230 ILE D CB  
7800  C CG1 . ILE D 230 ? 0.3432 0.3476 0.3483 0.0760  0.0761  -0.0732 230 ILE D CG1 
7801  C CG2 . ILE D 230 ? 0.3490 0.3558 0.3523 0.0794  0.0678  -0.0810 230 ILE D CG2 
7802  C CD1 . ILE D 230 ? 0.3361 0.3484 0.3484 0.0762  0.0707  -0.0745 230 ILE D CD1 
7803  N N   . PRO D 231 ? 0.3772 0.3695 0.3606 0.0803  0.0803  -0.0884 231 PRO D N   
7804  C CA  . PRO D 231 ? 0.3950 0.3842 0.3699 0.0834  0.0825  -0.0956 231 PRO D CA  
7805  C C   . PRO D 231 ? 0.4019 0.3958 0.3789 0.0875  0.0810  -0.1005 231 PRO D C   
7806  O O   . PRO D 231 ? 0.3907 0.3907 0.3752 0.0885  0.0728  -0.0993 231 PRO D O   
7807  C CB  . PRO D 231 ? 0.3899 0.3783 0.3625 0.0843  0.0740  -0.0947 231 PRO D CB  
7808  C CG  . PRO D 231 ? 0.3717 0.3620 0.3502 0.0813  0.0696  -0.0873 231 PRO D CG  
7809  C CD  . PRO D 231 ? 0.3619 0.3559 0.3489 0.0791  0.0716  -0.0836 231 PRO D CD  
7810  N N   . SER D 232 ? 0.4245 0.4161 0.3948 0.0897  0.0891  -0.1067 232 SER D N   
7811  C CA  . SER D 232 ? 0.4325 0.4304 0.4062 0.0939  0.0875  -0.1133 232 SER D CA  
7812  C C   . SER D 232 ? 0.4325 0.4314 0.4069 0.0967  0.0789  -0.1167 232 SER D C   
7813  O O   . SER D 232 ? 0.4316 0.4373 0.4128 0.0996  0.0738  -0.1204 232 SER D O   
7814  C CB  . SER D 232 ? 0.4561 0.4511 0.4207 0.0964  0.0980  -0.1201 232 SER D CB  
7815  O OG  . SER D 232 ? 0.4700 0.4535 0.4204 0.0949  0.1051  -0.1207 232 SER D OG  
7816  N N   . GLU D 233 ? 0.4356 0.4279 0.4028 0.0962  0.0768  -0.1157 233 GLU D N   
7817  C CA  . GLU D 233 ? 0.4374 0.4292 0.4032 0.0996  0.0684  -0.1185 233 GLU D CA  
7818  C C   . GLU D 233 ? 0.4191 0.4175 0.3952 0.0999  0.0580  -0.1143 233 GLU D C   
7819  O O   . GLU D 233 ? 0.4222 0.4215 0.3989 0.1035  0.0513  -0.1178 233 GLU D O   
7820  C CB  . GLU D 233 ? 0.4403 0.4245 0.3968 0.0988  0.0668  -0.1171 233 GLU D CB  
7821  C CG  . GLU D 233 ? 0.4628 0.4388 0.4061 0.0985  0.0762  -0.1234 233 GLU D CG  
7822  C CD  . GLU D 233 ? 0.4642 0.4380 0.4052 0.0938  0.0863  -0.1213 233 GLU D CD  
7823  O OE1 . GLU D 233 ? 0.4477 0.4232 0.3937 0.0905  0.0839  -0.1143 233 GLU D OE1 
7824  O OE2 . GLU D 233 ? 0.4903 0.4604 0.4240 0.0938  0.0968  -0.1268 233 GLU D OE2 
7825  N N   . ILE D 234 ? 0.3924 0.3945 0.3755 0.0961  0.0568  -0.1072 234 ILE D N   
7826  C CA  . ILE D 234 ? 0.3768 0.3840 0.3678 0.0954  0.0482  -0.1035 234 ILE D CA  
7827  C C   . ILE D 234 ? 0.3817 0.3949 0.3782 0.0985  0.0458  -0.1093 234 ILE D C   
7828  O O   . ILE D 234 ? 0.3773 0.3925 0.3767 0.1002  0.0379  -0.1099 234 ILE D O   
7829  C CB  . ILE D 234 ? 0.3768 0.3861 0.3733 0.0905  0.0491  -0.0958 234 ILE D CB  
7830  C CG1 . ILE D 234 ? 0.3727 0.3767 0.3647 0.0880  0.0510  -0.0908 234 ILE D CG1 
7831  C CG2 . ILE D 234 ? 0.3626 0.3762 0.3657 0.0893  0.0412  -0.0925 234 ILE D CG2 
7832  C CD1 . ILE D 234 ? 0.3459 0.3490 0.3377 0.0877  0.0429  -0.0868 234 ILE D CD1 
7833  N N   . GLY D 235 ? 0.4121 0.4281 0.4099 0.0995  0.0526  -0.1143 235 GLY D N   
7834  C CA  . GLY D 235 ? 0.4198 0.4425 0.4237 0.1030  0.0504  -0.1211 235 GLY D CA  
7835  C C   . GLY D 235 ? 0.4354 0.4562 0.4357 0.1084  0.0467  -0.1284 235 GLY D C   
7836  O O   . GLY D 235 ? 0.4383 0.4644 0.4443 0.1118  0.0427  -0.1340 235 GLY D O   
7837  N N   . ASN D 236 ? 0.4454 0.4582 0.4362 0.1096  0.0475  -0.1289 236 ASN D N   
7838  C CA  . ASN D 236 ? 0.4631 0.4722 0.4489 0.1149  0.0442  -0.1360 236 ASN D CA  
7839  C C   . ASN D 236 ? 0.4544 0.4603 0.4392 0.1158  0.0338  -0.1325 236 ASN D C   
7840  O O   . ASN D 236 ? 0.4743 0.4747 0.4531 0.1200  0.0304  -0.1373 236 ASN D O   
7841  C CB  . ASN D 236 ? 0.4861 0.4874 0.4603 0.1158  0.0521  -0.1403 236 ASN D CB  
7842  C CG  . ASN D 236 ? 0.5002 0.5039 0.4737 0.1160  0.0629  -0.1459 236 ASN D CG  
7843  O OD1 . ASN D 236 ? 0.5019 0.5130 0.4828 0.1188  0.0630  -0.1515 236 ASN D OD1 
7844  N ND2 . ASN D 236 ? 0.5006 0.4981 0.4652 0.1130  0.0721  -0.1445 236 ASN D ND2 
7845  N N   . LEU D 237 ? 0.4175 0.4260 0.4075 0.1120  0.0291  -0.1246 237 LEU D N   
7846  C CA  . LEU D 237 ? 0.4100 0.4158 0.3994 0.1126  0.0198  -0.1214 237 LEU D CA  
7847  C C   . LEU D 237 ? 0.4127 0.4220 0.4073 0.1162  0.0135  -0.1259 237 LEU D C   
7848  O O   . LEU D 237 ? 0.4037 0.4196 0.4059 0.1144  0.0129  -0.1246 237 LEU D O   
7849  C CB  . LEU D 237 ? 0.3899 0.3970 0.3823 0.1069  0.0184  -0.1121 237 LEU D CB  
7850  C CG  . LEU D 237 ? 0.3874 0.3908 0.3750 0.1038  0.0237  -0.1078 237 LEU D CG  
7851  C CD1 . LEU D 237 ? 0.3685 0.3746 0.3610 0.0984  0.0237  -0.0994 237 LEU D CD1 
7852  C CD2 . LEU D 237 ? 0.3954 0.3914 0.3743 0.1062  0.0204  -0.1088 237 LEU D CD2 
7853  N N   . PRO D 238 ? 0.4550 0.4594 0.4453 0.1214  0.0083  -0.1313 238 PRO D N   
7854  C CA  . PRO D 238 ? 0.4613 0.4684 0.4563 0.1259  0.0027  -0.1370 238 PRO D CA  
7855  C C   . PRO D 238 ? 0.4472 0.4557 0.4464 0.1239  -0.0047 -0.1319 238 PRO D C   
7856  O O   . PRO D 238 ? 0.4456 0.4595 0.4512 0.1250  -0.0071 -0.1342 238 PRO D O   
7857  C CB  . PRO D 238 ? 0.4811 0.4801 0.4685 0.1319  -0.0006 -0.1439 238 PRO D CB  
7858  C CG  . PRO D 238 ? 0.4785 0.4699 0.4578 0.1296  -0.0008 -0.1390 238 PRO D CG  
7859  C CD  . PRO D 238 ? 0.4660 0.4612 0.4466 0.1237  0.0068  -0.1329 238 PRO D CD  
7860  N N   . ASN D 239 ? 0.4488 0.4525 0.4445 0.1210  -0.0082 -0.1256 239 ASN D N   
7861  C CA  . ASN D 239 ? 0.4349 0.4383 0.4332 0.1191  -0.0145 -0.1213 239 ASN D CA  
7862  C C   . ASN D 239 ? 0.4157 0.4244 0.4191 0.1124  -0.0112 -0.1138 239 ASN D C   
7863  O O   . ASN D 239 ? 0.4064 0.4147 0.4116 0.1100  -0.0150 -0.1100 239 ASN D O   
7864  C CB  . ASN D 239 ? 0.4369 0.4317 0.4289 0.1198  -0.0201 -0.1193 239 ASN D CB  
7865  C CG  . ASN D 239 ? 0.4575 0.4449 0.4431 0.1264  -0.0235 -0.1266 239 ASN D CG  
7866  O OD1 . ASN D 239 ? 0.4756 0.4647 0.4620 0.1310  -0.0224 -0.1337 239 ASN D OD1 
7867  N ND2 . ASN D 239 ? 0.4630 0.4419 0.4422 0.1269  -0.0277 -0.1253 239 ASN D ND2 
7868  N N   . LEU D 240 ? 0.3588 0.3714 0.3639 0.1092  -0.0039 -0.1118 240 LEU D N   
7869  C CA  . LEU D 240 ? 0.3423 0.3586 0.3517 0.1031  -0.0006 -0.1049 240 LEU D CA  
7870  C C   . LEU D 240 ? 0.3373 0.3582 0.3525 0.1025  -0.0032 -0.1054 240 LEU D C   
7871  O O   . LEU D 240 ? 0.3459 0.3705 0.3641 0.1061  -0.0038 -0.1115 240 LEU D O   
7872  C CB  . LEU D 240 ? 0.3418 0.3605 0.3517 0.1009  0.0075  -0.1039 240 LEU D CB  
7873  C CG  . LEU D 240 ? 0.3264 0.3469 0.3395 0.0947  0.0113  -0.0965 240 LEU D CG  
7874  C CD1 . LEU D 240 ? 0.3184 0.3345 0.3282 0.0919  0.0099  -0.0907 240 LEU D CD1 
7875  C CD2 . LEU D 240 ? 0.3288 0.3512 0.3427 0.0934  0.0191  -0.0968 240 LEU D CD2 
7876  N N   . ARG D 241 ? 0.3671 0.3877 0.3839 0.0981  -0.0045 -0.0994 241 ARG D N   
7877  C CA  . ARG D 241 ? 0.3620 0.3858 0.3831 0.0971  -0.0068 -0.0992 241 ARG D CA  
7878  C C   . ARG D 241 ? 0.3496 0.3765 0.3745 0.0912  -0.0019 -0.0937 241 ARG D C   
7879  O O   . ARG D 241 ? 0.3552 0.3864 0.3843 0.0909  -0.0014 -0.0953 241 ARG D O   
7880  C CB  . ARG D 241 ? 0.3609 0.3801 0.3798 0.0977  -0.0130 -0.0980 241 ARG D CB  
7881  C CG  . ARG D 241 ? 0.3793 0.3932 0.3935 0.1033  -0.0184 -0.1027 241 ARG D CG  
7882  C CD  . ARG D 241 ? 0.4010 0.4142 0.4158 0.1082  -0.0248 -0.1080 241 ARG D CD  
7883  N NE  . ARG D 241 ? 0.3852 0.4001 0.4030 0.1052  -0.0257 -0.1049 241 ARG D NE  
7884  C CZ  . ARG D 241 ? 0.3987 0.4165 0.4193 0.1082  -0.0290 -0.1090 241 ARG D CZ  
7885  N NH1 . ARG D 241 ? 0.4041 0.4239 0.4260 0.1142  -0.0317 -0.1167 241 ARG D NH1 
7886  N NH2 . ARG D 241 ? 0.3915 0.4099 0.4137 0.1053  -0.0294 -0.1056 241 ARG D NH2 
7887  N N   . GLU D 242 ? 0.2809 0.3052 0.3043 0.0869  0.0013  -0.0875 242 GLU D N   
7888  C CA  . GLU D 242 ? 0.2698 0.2957 0.2962 0.0816  0.0059  -0.0821 242 GLU D CA  
7889  C C   . GLU D 242 ? 0.2682 0.2927 0.2930 0.0797  0.0113  -0.0792 242 GLU D C   
7890  O O   . GLU D 242 ? 0.2682 0.2892 0.2896 0.0798  0.0108  -0.0774 242 GLU D O   
7891  C CB  . GLU D 242 ? 0.2600 0.2835 0.2869 0.0780  0.0045  -0.0771 242 GLU D CB  
7892  C CG  . GLU D 242 ? 0.2634 0.2858 0.2897 0.0805  -0.0012 -0.0796 242 GLU D CG  
7893  C CD  . GLU D 242 ? 0.2544 0.2756 0.2824 0.0767  -0.0008 -0.0753 242 GLU D CD  
7894  O OE1 . GLU D 242 ? 0.2464 0.2654 0.2746 0.0727  0.0024  -0.0700 242 GLU D OE1 
7895  O OE2 . GLU D 242 ? 0.2561 0.2786 0.2853 0.0780  -0.0034 -0.0773 242 GLU D OE2 
7896  N N   . LEU D 243 ? 0.2272 0.2541 0.2544 0.0783  0.0162  -0.0789 243 LEU D N   
7897  C CA  . LEU D 243 ? 0.2269 0.2518 0.2523 0.0768  0.0219  -0.0761 243 LEU D CA  
7898  C C   . LEU D 243 ? 0.2173 0.2422 0.2457 0.0723  0.0255  -0.0708 243 LEU D C   
7899  O O   . LEU D 243 ? 0.2172 0.2451 0.2490 0.0717  0.0270  -0.0721 243 LEU D O   
7900  C CB  . LEU D 243 ? 0.2383 0.2648 0.2630 0.0799  0.0255  -0.0813 243 LEU D CB  
7901  C CG  . LEU D 243 ? 0.2403 0.2638 0.2622 0.0788  0.0320  -0.0789 243 LEU D CG  
7902  C CD1 . LEU D 243 ? 0.2384 0.2573 0.2558 0.0785  0.0306  -0.0759 243 LEU D CD1 
7903  C CD2 . LEU D 243 ? 0.2538 0.2784 0.2743 0.0821  0.0363  -0.0849 243 LEU D CD2 
7904  N N   . CYS D 244 ? 0.2234 0.2447 0.2507 0.0694  0.0268  -0.0653 244 CYS D N   
7905  C CA  . CYS D 244 ? 0.2151 0.2353 0.2448 0.0656  0.0301  -0.0600 244 CYS D CA  
7906  C C   . CYS D 244 ? 0.2150 0.2319 0.2430 0.0647  0.0349  -0.0567 244 CYS D C   
7907  O O   . CYS D 244 ? 0.2111 0.2254 0.2382 0.0635  0.0346  -0.0536 244 CYS D O   
7908  C CB  . CYS D 244 ? 0.2070 0.2261 0.2380 0.0631  0.0275  -0.0567 244 CYS D CB  
7909  S SG  . CYS D 244 ? 0.2074 0.2295 0.2401 0.0642  0.0223  -0.0602 244 CYS D SG  
7910  N N   . LEU D 245 ? 0.2155 0.2323 0.2431 0.0653  0.0395  -0.0577 245 LEU D N   
7911  C CA  . LEU D 245 ? 0.2167 0.2297 0.2426 0.0647  0.0448  -0.0548 245 LEU D CA  
7912  C C   . LEU D 245 ? 0.2122 0.2236 0.2397 0.0625  0.0486  -0.0503 245 LEU D C   
7913  O O   . LEU D 245 ? 0.2153 0.2238 0.2412 0.0624  0.0534  -0.0484 245 LEU D O   
7914  C CB  . LEU D 245 ? 0.2279 0.2406 0.2508 0.0674  0.0483  -0.0591 245 LEU D CB  
7915  C CG  . LEU D 245 ? 0.2350 0.2487 0.2549 0.0706  0.0448  -0.0640 245 LEU D CG  
7916  C CD1 . LEU D 245 ? 0.2477 0.2599 0.2637 0.0731  0.0500  -0.0681 245 LEU D CD1 
7917  C CD2 . LEU D 245 ? 0.2306 0.2422 0.2486 0.0702  0.0410  -0.0617 245 LEU D CD2 
7918  N N   . ASP D 246 ? 0.2303 0.2435 0.2603 0.0609  0.0461  -0.0486 246 ASP D N   
7919  C CA  . ASP D 246 ? 0.2271 0.2397 0.2574 0.0599  0.0485  -0.0450 246 ASP D CA  
7920  C C   . ASP D 246 ? 0.2235 0.2325 0.2513 0.0582  0.0492  -0.0388 246 ASP D C   
7921  O O   . ASP D 246 ? 0.2216 0.2285 0.2500 0.0572  0.0486  -0.0376 246 ASP D O   
7922  C CB  . ASP D 246 ? 0.2215 0.2372 0.2549 0.0582  0.0448  -0.0454 246 ASP D CB  
7923  C CG  . ASP D 246 ? 0.2164 0.2313 0.2504 0.0569  0.0414  -0.0441 246 ASP D CG  
7924  O OD1 . ASP D 246 ? 0.2188 0.2348 0.2526 0.0580  0.0384  -0.0475 246 ASP D OD1 
7925  O OD2 . ASP D 246 ? 0.2109 0.2243 0.2448 0.0555  0.0414  -0.0401 246 ASP D OD2 
7926  N N   . ARG D 247 ? 0.2382 0.2484 0.2632 0.0588  0.0494  -0.0359 247 ARG D N   
7927  C CA  . ARG D 247 ? 0.2343 0.2468 0.2552 0.0599  0.0459  -0.0325 247 ARG D CA  
7928  C C   . ARG D 247 ? 0.2386 0.2487 0.2541 0.0622  0.0463  -0.0305 247 ARG D C   
7929  O O   . ARG D 247 ? 0.2363 0.2446 0.2509 0.0620  0.0449  -0.0279 247 ARG D O   
7930  C CB  . ARG D 247 ? 0.2267 0.2408 0.2503 0.0581  0.0425  -0.0313 247 ARG D CB  
7931  C CG  . ARG D 247 ? 0.2222 0.2390 0.2504 0.0560  0.0419  -0.0330 247 ARG D CG  
7932  C CD  . ARG D 247 ? 0.2166 0.2335 0.2471 0.0542  0.0398  -0.0319 247 ARG D CD  
7933  N NE  . ARG D 247 ? 0.2179 0.2317 0.2490 0.0539  0.0406  -0.0322 247 ARG D NE  
7934  C CZ  . ARG D 247 ? 0.2142 0.2281 0.2469 0.0527  0.0389  -0.0319 247 ARG D CZ  
7935  N NH1 . ARG D 247 ? 0.2095 0.2255 0.2437 0.0516  0.0373  -0.0309 247 ARG D NH1 
7936  N NH2 . ARG D 247 ? 0.2153 0.2280 0.2497 0.0528  0.0387  -0.0342 247 ARG D NH2 
7937  N N   . ASN D 248 ? 0.2931 0.3030 0.3051 0.0644  0.0484  -0.0321 248 ASN D N   
7938  C CA  . ASN D 248 ? 0.2755 0.3011 0.3232 0.0482  0.0449  -0.0544 248 ASN D CA  
7939  C C   . ASN D 248 ? 0.2870 0.3189 0.3167 0.0596  0.0419  -0.0524 248 ASN D C   
7940  O O   . ASN D 248 ? 0.2925 0.3215 0.3158 0.0627  0.0448  -0.0473 248 ASN D O   
7941  C CB  . ASN D 248 ? 0.2930 0.2954 0.3262 0.0525  0.0584  -0.0423 248 ASN D CB  
7942  C CG  . ASN D 248 ? 0.2870 0.2910 0.3208 0.0536  0.0537  -0.0423 248 ASN D CG  
7943  O OD1 . ASN D 248 ? 0.2849 0.2913 0.3210 0.0537  0.0515  -0.0442 248 ASN D OD1 
7944  N ND2 . ASN D 248 ? 0.2855 0.2892 0.3162 0.0558  0.0514  -0.0404 248 ASN D ND2 
7945  N N   . ASN D 249 ? 0.4301 0.4589 0.4650 0.0564  0.0471  -0.0559 249 ASN D N   
7946  C CA  . ASN D 249 ? 0.4362 0.4649 0.4647 0.0599  0.0510  -0.0556 249 ASN D CA  
7947  C C   . ASN D 249 ? 0.4448 0.4763 0.4721 0.0604  0.0533  -0.0618 249 ASN D C   
7948  O O   . ASN D 249 ? 0.4581 0.4868 0.4812 0.0615  0.0582  -0.0628 249 ASN D O   
7949  C CB  . ASN D 249 ? 0.4416 0.4639 0.4686 0.0602  0.0547  -0.0519 249 ASN D CB  
7950  C CG  . ASN D 249 ? 0.4418 0.4620 0.4693 0.0603  0.0561  -0.0471 249 ASN D CG  
7951  O OD1 . ASN D 249 ? 0.4500 0.4680 0.4754 0.0600  0.0602  -0.0457 249 ASN D OD1 
7952  N ND2 . ASN D 249 ? 0.4335 0.4525 0.4639 0.0591  0.0531  -0.0435 249 ASN D ND2 
7953  N N   . LEU D 250 ? 0.3389 0.3759 0.3698 0.0595  0.0501  -0.0663 250 LEU D N   
7954  C CA  . LEU D 250 ? 0.3695 0.3628 0.3868 0.0566  0.0788  -0.0505 250 LEU D CA  
7955  C C   . LEU D 250 ? 0.3775 0.3975 0.3714 0.0787  0.0628  -0.0530 250 LEU D C   
7956  O O   . LEU D 250 ? 0.3740 0.3933 0.3740 0.0760  0.0657  -0.0522 250 LEU D O   
7957  C CB  . LEU D 250 ? 0.3702 0.3662 0.3808 0.0639  0.0743  -0.0507 250 LEU D CB  
7958  C CG  . LEU D 250 ? 0.3604 0.3597 0.3782 0.0612  0.0690  -0.0537 250 LEU D CG  
7959  C CD1 . LEU D 250 ? 0.3601 0.3626 0.3768 0.0653  0.0651  -0.0558 250 LEU D CD1 
7960  C CD2 . LEU D 250 ? 0.3650 0.3653 0.3820 0.0611  0.0691  -0.0592 250 LEU D CD2 
7961  N N   . THR D 251 ? 0.3833 0.4138 0.3788 0.0789  0.0625  -0.0625 251 THR D N   
7962  C CA  . THR D 251 ? 0.3937 0.4232 0.3882 0.0790  0.0711  -0.0644 251 THR D CA  
7963  C C   . THR D 251 ? 0.4126 0.4328 0.3982 0.0830  0.0796  -0.0646 251 THR D C   
7964  O O   . THR D 251 ? 0.4187 0.4252 0.3997 0.0829  0.0836  -0.0615 251 THR D O   
7965  C CB  . THR D 251 ? 0.3976 0.4324 0.3968 0.0743  0.0738  -0.0701 251 THR D CB  
7966  O OG1 . THR D 251 ? 0.4091 0.4457 0.4052 0.0739  0.0744  -0.0759 251 THR D OG1 
7967  C CG2 . THR D 251 ? 0.3786 0.4107 0.3854 0.0692  0.0716  -0.0671 251 THR D CG2 
7968  N N   . GLY D 252 ? 0.3716 0.3967 0.3596 0.0824  0.0862  -0.0704 252 GLY D N   
7969  C CA  . GLY D 252 ? 0.3885 0.4111 0.3724 0.0846  0.0937  -0.0756 252 GLY D CA  
7970  C C   . GLY D 252 ? 0.3878 0.4112 0.3809 0.0833  0.0962  -0.0792 252 GLY D C   
7971  O O   . GLY D 252 ? 0.3749 0.4003 0.3769 0.0809  0.0925  -0.0772 252 GLY D O   
7972  N N   . LYS D 253 ? 0.3923 0.4164 0.3837 0.0854  0.1016  -0.0864 253 LYS D N   
7973  C CA  . LYS D 253 ? 0.3921 0.4225 0.3947 0.0839  0.1011  -0.0928 253 LYS D CA  
7974  C C   . LYS D 253 ? 0.3851 0.4115 0.3901 0.0838  0.0955  -0.0917 253 LYS D C   
7975  O O   . LYS D 253 ? 0.3847 0.4020 0.3822 0.0848  0.0949  -0.0875 253 LYS D O   
7976  C CB  . LYS D 253 ? 0.4106 0.4463 0.4122 0.0854  0.1078  -0.1023 253 LYS D CB  
7977  C CG  . LYS D 253 ? 0.4158 0.4601 0.4224 0.0826  0.1131  -0.1065 253 LYS D CG  
7978  C CD  . LYS D 253 ? 0.4352 0.4856 0.4415 0.0836  0.1204  -0.1167 253 LYS D CD  
7979  C CE  . LYS D 253 ? 0.4339 0.4960 0.4562 0.0811  0.1196  -0.1246 253 LYS D CE  
7980  N NZ  . LYS D 253 ? 0.4391 0.5095 0.4680 0.0768  0.1258  -0.1292 253 LYS D NZ  
7981  N N   . ILE D 254 ? 0.3478 0.3822 0.3643 0.0823  0.0910  -0.0962 254 ILE D N   
7982  C CA  . ILE D 254 ? 0.3427 0.3768 0.3622 0.0827  0.0846  -0.0973 254 ILE D CA  
7983  C C   . ILE D 254 ? 0.3586 0.3938 0.3751 0.0863  0.0873  -0.1053 254 ILE D C   
7984  O O   . ILE D 254 ? 0.3695 0.4120 0.3897 0.0876  0.0911  -0.1129 254 ILE D O   
7985  C CB  . ILE D 254 ? 0.3317 0.3739 0.3629 0.0807  0.0779  -0.0991 254 ILE D CB  
7986  C CG1 . ILE D 254 ? 0.3166 0.3564 0.3493 0.0771  0.0751  -0.0911 254 ILE D CG1 
7987  C CG2 . ILE D 254 ? 0.3295 0.3734 0.3633 0.0823  0.0710  -0.1020 254 ILE D CG2 
7988  C CD1 . ILE D 254 ? 0.3073 0.3540 0.3499 0.0748  0.0694  -0.0930 254 ILE D CD1 
7989  N N   . PRO D 255 ? 0.3730 0.4015 0.3832 0.0878  0.0857  -0.1045 255 PRO D N   
7990  C CA  . PRO D 255 ? 0.3904 0.4183 0.3957 0.0915  0.0888  -0.1123 255 PRO D CA  
7991  C C   . PRO D 255 ? 0.3946 0.4332 0.4096 0.0938  0.0855  -0.1211 255 PRO D C   
7992  O O   . PRO D 255 ? 0.3837 0.4267 0.4065 0.0936  0.0772  -0.1210 255 PRO D O   
7993  C CB  . PRO D 255 ? 0.3873 0.4076 0.3871 0.0917  0.0846  -0.1095 255 PRO D CB  
7994  C CG  . PRO D 255 ? 0.3723 0.3872 0.3713 0.0878  0.0831  -0.0999 255 PRO D CG  
7995  C CD  . PRO D 255 ? 0.3607 0.3822 0.3684 0.0858  0.0810  -0.0972 255 PRO D CD  
7996  N N   . SER D 256 ? 0.4236 0.4665 0.4377 0.0962  0.0922  -0.1291 256 SER D N   
7997  C CA  . SER D 256 ? 0.4312 0.4840 0.4542 0.0993  0.0898  -0.1391 256 SER D CA  
7998  C C   . SER D 256 ? 0.4346 0.4844 0.4554 0.1029  0.0839  -0.1420 256 SER D C   
7999  O O   . SER D 256 ? 0.4371 0.4943 0.4660 0.1059  0.0788  -0.1488 256 SER D O   
8000  C CB  . SER D 256 ? 0.4511 0.5088 0.4727 0.1011  0.0993  -0.1477 256 SER D CB  
8001  O OG  . SER D 256 ? 0.4662 0.5139 0.4725 0.1027  0.1066  -0.1473 256 SER D OG  
8002  N N   . SER D 257 ? 0.4530 0.4919 0.4629 0.1029  0.0841  -0.1373 257 SER D N   
8003  C CA  . SER D 257 ? 0.4552 0.4907 0.4626 0.1059  0.0776  -0.1394 257 SER D CA  
8004  C C   . SER D 257 ? 0.4381 0.4780 0.4544 0.1054  0.0664  -0.1364 257 SER D C   
8005  O O   . SER D 257 ? 0.4412 0.4807 0.4576 0.1089  0.0599  -0.1398 257 SER D O   
8006  C CB  . SER D 257 ? 0.4571 0.4806 0.4522 0.1047  0.0796  -0.1345 257 SER D CB  
8007  O OG  . SER D 257 ? 0.4878 0.5053 0.4722 0.1046  0.0905  -0.1365 257 SER D OG  
8008  N N   . PHE D 258 ? 0.4077 0.4508 0.4301 0.1013  0.0643  -0.1303 258 PHE D N   
8009  C CA  . PHE D 258 ? 0.3929 0.4390 0.4217 0.1004  0.0546  -0.1272 258 PHE D CA  
8010  C C   . PHE D 258 ? 0.3987 0.4530 0.4354 0.1045  0.0495  -0.1356 258 PHE D C   
8011  O O   . PHE D 258 ? 0.3910 0.4462 0.4306 0.1052  0.0410  -0.1346 258 PHE D O   
8012  C CB  . PHE D 258 ? 0.3772 0.4248 0.4102 0.0952  0.0547  -0.1201 258 PHE D CB  
8013  C CG  . PHE D 258 ? 0.3661 0.4057 0.3933 0.0916  0.0547  -0.1106 258 PHE D CG  
8014  C CD1 . PHE D 258 ? 0.3724 0.4045 0.3908 0.0922  0.0582  -0.1090 258 PHE D CD1 
8015  C CD2 . PHE D 258 ? 0.3502 0.3900 0.3808 0.0876  0.0511  -0.1039 258 PHE D CD2 
8016  C CE1 . PHE D 258 ? 0.3624 0.3881 0.3767 0.0890  0.0578  -0.1011 258 PHE D CE1 
8017  C CE2 . PHE D 258 ? 0.3408 0.3741 0.3670 0.0846  0.0512  -0.0959 258 PHE D CE2 
8018  C CZ  . PHE D 258 ? 0.3465 0.3732 0.3652 0.0853  0.0543  -0.0946 258 PHE D CZ  
8019  N N   . GLY D 259 ? 0.4227 0.4829 0.4629 0.1073  0.0546  -0.1443 259 GLY D N   
8020  C CA  . GLY D 259 ? 0.4305 0.4986 0.4786 0.1120  0.0498  -0.1535 259 GLY D CA  
8021  C C   . GLY D 259 ? 0.4376 0.5014 0.4817 0.1170  0.0434  -0.1566 259 GLY D C   
8022  O O   . GLY D 259 ? 0.4396 0.5078 0.4896 0.1208  0.0360  -0.1617 259 GLY D O   
8023  N N   . ASN D 260 ? 0.4226 0.4772 0.4563 0.1174  0.0456  -0.1539 260 ASN D N   
8024  C CA  . ASN D 260 ? 0.4299 0.4791 0.4587 0.1220  0.0394  -0.1566 260 ASN D CA  
8025  C C   . ASN D 260 ? 0.4144 0.4604 0.4430 0.1204  0.0297  -0.1495 260 ASN D C   
8026  O O   . ASN D 260 ? 0.4199 0.4622 0.4459 0.1246  0.0229  -0.1520 260 ASN D O   
8027  C CB  . ASN D 260 ? 0.4415 0.4815 0.4586 0.1226  0.0453  -0.1567 260 ASN D CB  
8028  C CG  . ASN D 260 ? 0.4588 0.5004 0.4736 0.1236  0.0563  -0.1634 260 ASN D CG  
8029  O OD1 . ASN D 260 ? 0.4695 0.5189 0.4911 0.1271  0.0579  -0.1722 260 ASN D OD1 
8030  N ND2 . ASN D 260 ? 0.4627 0.4968 0.4675 0.1208  0.0641  -0.1598 260 ASN D ND2 
8031  N N   . LEU D 261 ? 0.4075 0.4543 0.4384 0.1147  0.0292  -0.1411 261 LEU D N   
8032  C CA  . LEU D 261 ? 0.3933 0.4370 0.4234 0.1126  0.0214  -0.1342 261 LEU D CA  
8033  C C   . LEU D 261 ? 0.3923 0.4413 0.4292 0.1152  0.0139  -0.1381 261 LEU D C   
8034  O O   . LEU D 261 ? 0.3811 0.4341 0.4232 0.1119  0.0124  -0.1350 261 LEU D O   
8035  C CB  . LEU D 261 ? 0.3768 0.4193 0.4067 0.1058  0.0244  -0.1248 261 LEU D CB  
8036  C CG  . LEU D 261 ? 0.3767 0.4129 0.3994 0.1034  0.0304  -0.1201 261 LEU D CG  
8037  C CD1 . LEU D 261 ? 0.3634 0.3997 0.3877 0.0975  0.0346  -0.1126 261 LEU D CD1 
8038  C CD2 . LEU D 261 ? 0.3754 0.4048 0.3916 0.1042  0.0254  -0.1172 261 LEU D CD2 
8039  N N   . LYS D 262 ? 0.3910 0.4390 0.4271 0.1215  0.0091  -0.1452 262 LYS D N   
8040  C CA  . LYS D 262 ? 0.3941 0.4462 0.4361 0.1254  0.0017  -0.1504 262 LYS D CA  
8041  C C   . LYS D 262 ? 0.3847 0.4319 0.4240 0.1245  -0.0067 -0.1450 262 LYS D C   
8042  O O   . LYS D 262 ? 0.3860 0.4355 0.4292 0.1271  -0.0131 -0.1480 262 LYS D O   
8043  C CB  . LYS D 262 ? 0.4146 0.4672 0.4572 0.1332  -0.0001 -0.1612 262 LYS D CB  
8044  C CG  . LYS D 262 ? 0.4268 0.4838 0.4713 0.1344  0.0092  -0.1676 262 LYS D CG  
8045  C CD  . LYS D 262 ? 0.4261 0.4942 0.4813 0.1338  0.0119  -0.1723 262 LYS D CD  
8046  C CE  . LYS D 262 ? 0.4318 0.5048 0.4943 0.1393  0.0032  -0.1795 262 LYS D CE  
8047  N NZ  . LYS D 262 ? 0.4422 0.5261 0.5150 0.1420  0.0068  -0.1895 262 LYS D NZ  
8048  N N   . ASN D 263 ? 0.4784 0.5186 0.5109 0.1211  -0.0067 -0.1374 263 ASN D N   
8049  C CA  . ASN D 263 ? 0.4695 0.5049 0.4992 0.1195  -0.0132 -0.1319 263 ASN D CA  
8050  C C   . ASN D 263 ? 0.4546 0.4910 0.4854 0.1121  -0.0104 -0.1230 263 ASN D C   
8051  O O   . ASN D 263 ? 0.4446 0.4775 0.4736 0.1102  -0.0147 -0.1185 263 ASN D O   
8052  C CB  . ASN D 263 ? 0.4748 0.5013 0.4965 0.1213  -0.0161 -0.1306 263 ASN D CB  
8053  C CG  . ASN D 263 ? 0.4954 0.5179 0.5150 0.1289  -0.0232 -0.1382 263 ASN D CG  
8054  O OD1 . ASN D 263 ? 0.5075 0.5323 0.5310 0.1323  -0.0283 -0.1424 263 ASN D OD1 
8055  N ND2 . ASN D 263 ? 0.5109 0.5265 0.5241 0.1319  -0.0238 -0.1402 263 ASN D ND2 
8056  N N   . VAL D 264 ? 0.3548 0.3949 0.3881 0.1081  -0.0032 -0.1206 264 VAL D N   
8057  C CA  . VAL D 264 ? 0.3389 0.3789 0.3728 0.1014  -0.0001 -0.1124 264 VAL D CA  
8058  C C   . VAL D 264 ? 0.3328 0.3770 0.3720 0.1000  -0.0027 -0.1123 264 VAL D C   
8059  O O   . VAL D 264 ? 0.3383 0.3886 0.3830 0.1021  -0.0024 -0.1181 264 VAL D O   
8060  C CB  . VAL D 264 ? 0.3369 0.3780 0.3710 0.0982  0.0082  -0.1101 264 VAL D CB  
8061  C CG1 . VAL D 264 ? 0.3227 0.3645 0.3591 0.0921  0.0111  -0.1032 264 VAL D CG1 
8062  C CG2 . VAL D 264 ? 0.3402 0.3756 0.3678 0.0985  0.0105  -0.1082 264 VAL D CG2 
8063  N N   . THR D 265 ? 0.2994 0.3405 0.3370 0.0964  -0.0048 -0.1063 265 THR D N   
8064  C CA  . THR D 265 ? 0.2937 0.3375 0.3349 0.0948  -0.0070 -0.1056 265 THR D CA  
8065  C C   . THR D 265 ? 0.2810 0.3252 0.3236 0.0884  -0.0018 -0.0989 265 THR D C   
8066  O O   . THR D 265 ? 0.2773 0.3246 0.3236 0.0870  -0.0023 -0.0992 265 THR D O   
8067  C CB  . THR D 265 ? 0.2937 0.3329 0.3316 0.0963  -0.0134 -0.1046 265 THR D CB  
8068  O OG1 . THR D 265 ? 0.2864 0.3197 0.3198 0.0928  -0.0121 -0.0980 265 THR D OG1 
8069  C CG2 . THR D 265 ? 0.3082 0.3462 0.3448 0.1035  -0.0196 -0.1119 265 THR D CG2 
8070  N N   . LEU D 266 ? 0.2528 0.2936 0.2927 0.0848  0.0029  -0.0934 266 LEU D N   
8071  C CA  . LEU D 266 ? 0.2422 0.2823 0.2832 0.0793  0.0078  -0.0872 266 LEU D CA  
8072  C C   . LEU D 266 ? 0.2432 0.2825 0.2832 0.0781  0.0138  -0.0857 266 LEU D C   
8073  O O   . LEU D 266 ? 0.2458 0.2817 0.2819 0.0791  0.0143  -0.0848 266 LEU D O   
8074  C CB  . LEU D 266 ? 0.2331 0.2682 0.2713 0.0758  0.0072  -0.0807 266 LEU D CB  
8075  C CG  . LEU D 266 ? 0.2237 0.2566 0.2623 0.0707  0.0127  -0.0742 266 LEU D CG  
8076  C CD1 . LEU D 266 ? 0.2201 0.2559 0.2624 0.0686  0.0143  -0.0738 266 LEU D CD1 
8077  C CD2 . LEU D 266 ? 0.2168 0.2450 0.2531 0.0680  0.0125  -0.0688 266 LEU D CD2 
8078  N N   . LEU D 267 ? 0.2260 0.2679 0.2693 0.0761  0.0182  -0.0854 267 LEU D N   
8079  C CA  . LEU D 267 ? 0.2276 0.2681 0.2696 0.0749  0.0245  -0.0837 267 LEU D CA  
8080  C C   . LEU D 267 ? 0.2189 0.2577 0.2621 0.0704  0.0282  -0.0780 267 LEU D C   
8081  O O   . LEU D 267 ? 0.2190 0.2615 0.2663 0.0696  0.0297  -0.0798 267 LEU D O   
8082  C CB  . LEU D 267 ? 0.2386 0.2837 0.2832 0.0782  0.0270  -0.0906 267 LEU D CB  
8083  C CG  . LEU D 267 ? 0.2427 0.2856 0.2849 0.0775  0.0342  -0.0893 267 LEU D CG  
8084  C CD1 . LEU D 267 ? 0.2424 0.2789 0.2782 0.0776  0.0351  -0.0853 267 LEU D CD1 
8085  C CD2 . LEU D 267 ? 0.2556 0.3033 0.3001 0.0811  0.0372  -0.0970 267 LEU D CD2 
8086  N N   . ASN D 268 ? 0.2313 0.2649 0.2714 0.0678  0.0295  -0.0716 268 ASN D N   
8087  C CA  . ASN D 268 ? 0.2243 0.2553 0.2647 0.0642  0.0333  -0.0659 268 ASN D CA  
8088  C C   . ASN D 268 ? 0.2271 0.2545 0.2645 0.0643  0.0386  -0.0634 268 ASN D C   
8089  O O   . ASN D 268 ? 0.2271 0.2510 0.2612 0.0646  0.0387  -0.0614 268 ASN D O   
8090  C CB  . ASN D 268 ? 0.2157 0.2433 0.2552 0.0616  0.0314  -0.0608 268 ASN D CB  
8091  C CG  . ASN D 268 ? 0.2128 0.2430 0.2549 0.0610  0.0276  -0.0623 268 ASN D CG  
8092  O OD1 . ASN D 268 ? 0.2157 0.2502 0.2609 0.0619  0.0266  -0.0664 268 ASN D OD1 
8093  N ND2 . ASN D 268 ? 0.2077 0.2352 0.2486 0.0596  0.0257  -0.0592 268 ASN D ND2 
8094  N N   . MET D 269 ? 0.2362 0.2646 0.2747 0.0641  0.0429  -0.0639 269 MET D N   
8095  C CA  . MET D 269 ? 0.2396 0.2639 0.2744 0.0645  0.0485  -0.0610 269 MET D CA  
8096  C C   . MET D 269 ? 0.2364 0.2601 0.2718 0.0628  0.0514  -0.0575 269 MET D C   
8097  O O   . MET D 269 ? 0.2415 0.2640 0.2744 0.0640  0.0560  -0.0570 269 MET D O   
8098  C CB  . MET D 269 ? 0.2511 0.2771 0.2846 0.0675  0.0517  -0.0664 269 MET D CB  
8099  C CG  . MET D 269 ? 0.2562 0.2832 0.2885 0.0700  0.0483  -0.0708 269 MET D CG  
8100  S SD  . MET D 269 ? 0.2710 0.2966 0.2988 0.0735  0.0539  -0.0754 269 MET D SD  
8101  C CE  . MET D 269 ? 0.2783 0.3106 0.3109 0.0745  0.0573  -0.0812 269 MET D CE  
8102  N N   . PHE D 270 ? 0.2409 0.2656 0.2790 0.0605  0.0486  -0.0555 270 PHE D N   
8103  C CA  . PHE D 270 ? 0.2378 0.2630 0.2770 0.0590  0.0502  -0.0532 270 PHE D CA  
8104  C C   . PHE D 270 ? 0.2354 0.2562 0.2694 0.0595  0.0520  -0.0472 270 PHE D C   
8105  O O   . PHE D 270 ? 0.2346 0.2516 0.2650 0.0603  0.0518  -0.0440 270 PHE D O   
8106  C CB  . PHE D 270 ? 0.2311 0.2584 0.2743 0.0564  0.0466  -0.0533 270 PHE D CB  
8107  C CG  . PHE D 270 ? 0.2253 0.2498 0.2668 0.0555  0.0437  -0.0500 270 PHE D CG  
8108  C CD1 . PHE D 270 ? 0.2201 0.2412 0.2590 0.0545  0.0442  -0.0445 270 PHE D CD1 
8109  C CD2 . PHE D 270 ? 0.2257 0.2517 0.2683 0.0561  0.0402  -0.0530 270 PHE D CD2 
8110  C CE1 . PHE D 270 ? 0.2156 0.2346 0.2535 0.0537  0.0421  -0.0419 270 PHE D CE1 
8111  C CE2 . PHE D 270 ? 0.2209 0.2444 0.2622 0.0551  0.0379  -0.0502 270 PHE D CE2 
8112  C CZ  . PHE D 270 ? 0.2158 0.2358 0.2551 0.0537  0.0394  -0.0446 270 PHE D CZ  
8113  N N   . GLU D 271 ? 0.2709 0.2936 0.3058 0.0588  0.0530  -0.0465 271 GLU D N   
8114  C CA  . GLU D 271 ? 0.2679 0.2903 0.2997 0.0591  0.0524  -0.0431 271 GLU D CA  
8115  C C   . GLU D 271 ? 0.2736 0.2945 0.2995 0.0616  0.0531  -0.0423 271 GLU D C   
8116  O O   . GLU D 271 ? 0.2711 0.2909 0.2936 0.0621  0.0502  -0.0397 271 GLU D O   
8117  C CB  . GLU D 271 ? 0.2598 0.2813 0.2920 0.0571  0.0487  -0.0398 271 GLU D CB  
8118  C CG  . GLU D 271 ? 0.2572 0.2795 0.2943 0.0540  0.0476  -0.0404 271 GLU D CG  
8119  C CD  . GLU D 271 ? 0.2525 0.2746 0.2919 0.0511  0.0458  -0.0381 271 GLU D CD  
8120  O OE1 . GLU D 271 ? 0.2599 0.2817 0.2992 0.0508  0.0460  -0.0369 271 GLU D OE1 
8121  O OE2 . GLU D 271 ? 0.2477 0.2695 0.2897 0.0488  0.0447  -0.0378 271 GLU D OE2 
8122  N N   . ASN D 272 ? 0.2870 0.3088 0.3122 0.0634  0.0569  -0.0455 272 ASN D N   
8123  C CA  . ASN D 272 ? 0.2941 0.3152 0.3133 0.0662  0.0581  -0.0457 272 ASN D CA  
8124  C C   . ASN D 272 ? 0.2988 0.3242 0.3202 0.0662  0.0617  -0.0498 272 ASN D C   
8125  O O   . ASN D 272 ? 0.3008 0.3283 0.3281 0.0639  0.0636  -0.0513 272 ASN D O   
8126  C CB  . ASN D 272 ? 0.3022 0.3174 0.3192 0.0674  0.0616  -0.0465 272 ASN D CB  
8127  C CG  . ASN D 272 ? 0.3001 0.3088 0.3161 0.0655  0.0606  -0.0430 272 ASN D CG  
8128  O OD1 . ASN D 272 ? 0.3018 0.3050 0.3141 0.0652  0.0625  -0.0401 272 ASN D OD1 
8129  N ND2 . ASN D 272 ? 0.2926 0.3026 0.3144 0.0635  0.0582  -0.0445 272 ASN D ND2 
8130  N N   . GLN D 273 ? 0.3567 0.3830 0.3735 0.0685  0.0633  -0.0518 273 GLN D N   
8131  C CA  . GLN D 273 ? 0.3648 0.3940 0.3831 0.0682  0.0688  -0.0559 273 GLN D CA  
8132  C C   . GLN D 273 ? 0.3776 0.4064 0.3923 0.0713  0.0740  -0.0596 273 GLN D C   
8133  O O   . GLN D 273 ? 0.3899 0.4208 0.4024 0.0721  0.0786  -0.0633 273 GLN D O   
8134  C CB  . GLN D 273 ? 0.3704 0.4005 0.3885 0.0668  0.0690  -0.0569 273 GLN D CB  
8135  C CG  . GLN D 273 ? 0.3523 0.3798 0.3754 0.0631  0.0671  -0.0534 273 GLN D CG  
8136  C CD  . GLN D 273 ? 0.3700 0.3921 0.3929 0.0602  0.0717  -0.0517 273 GLN D CD  
8137  O OE1 . GLN D 273 ? 0.3789 0.3988 0.4021 0.0583  0.0772  -0.0520 273 GLN D OE1 
8138  N NE2 . GLN D 273 ? 0.3648 0.3832 0.3864 0.0599  0.0701  -0.0492 273 GLN D NE2 
8139  N N   . LEU D 274 ? 0.3116 0.3374 0.3270 0.0721  0.0744  -0.0600 274 LEU D N   
8140  C CA  . LEU D 274 ? 0.3239 0.3506 0.3392 0.0742  0.0799  -0.0659 274 LEU D CA  
8141  C C   . LEU D 274 ? 0.3286 0.3620 0.3505 0.0717  0.0840  -0.0714 274 LEU D C   
8142  O O   . LEU D 274 ? 0.3210 0.3571 0.3503 0.0676  0.0825  -0.0711 274 LEU D O   
8143  C CB  . LEU D 274 ? 0.3219 0.3481 0.3422 0.0733  0.0778  -0.0682 274 LEU D CB  
8144  C CG  . LEU D 274 ? 0.3172 0.3367 0.3342 0.0734  0.0746  -0.0641 274 LEU D CG  
8145  C CD1 . LEU D 274 ? 0.3104 0.3336 0.3353 0.0713  0.0695  -0.0669 274 LEU D CD1 
8146  C CD2 . LEU D 274 ? 0.3285 0.3428 0.3386 0.0753  0.0780  -0.0657 274 LEU D CD2 
8147  N N   . SER D 275 ? 0.3391 0.3746 0.3584 0.0733  0.0897  -0.0768 275 SER D N   
8148  C CA  . SER D 275 ? 0.3458 0.3873 0.3709 0.0701  0.0951  -0.0823 275 SER D CA  
8149  C C   . SER D 275 ? 0.3585 0.4049 0.3863 0.0712  0.0993  -0.0906 275 SER D C   
8150  O O   . SER D 275 ? 0.3602 0.4056 0.3872 0.0738  0.0971  -0.0921 275 SER D O   
8151  C CB  . SER D 275 ? 0.3512 0.3916 0.3700 0.0698  0.0992  -0.0813 275 SER D CB  
8152  O OG  . SER D 275 ? 0.3630 0.4015 0.3712 0.0743  0.1020  -0.0829 275 SER D OG  
8153  N N   . GLY D 276 ? 0.3784 0.4307 0.4105 0.0685  0.1055  -0.0966 276 GLY D N   
8154  C CA  . GLY D 276 ? 0.3909 0.4503 0.4276 0.0690  0.1097  -0.1059 276 GLY D CA  
8155  C C   . GLY D 276 ? 0.3838 0.4501 0.4334 0.0674  0.1049  -0.1102 276 GLY D C   
8156  O O   . GLY D 276 ? 0.3709 0.4371 0.4263 0.0645  0.1000  -0.1067 276 GLY D O   
8157  N N   . GLU D 277 ? 0.3936 0.4663 0.4472 0.0695  0.1061  -0.1183 277 GLU D N   
8158  C CA  . GLU D 277 ? 0.3892 0.4704 0.4551 0.0688  0.1011  -0.1242 277 GLU D CA  
8159  C C   . GLU D 277 ? 0.3856 0.4642 0.4494 0.0727  0.0946  -0.1233 277 GLU D C   
8160  O O   . GLU D 277 ? 0.3917 0.4642 0.4460 0.0761  0.0959  -0.1216 277 GLU D O   
8161  C CB  . GLU D 277 ? 0.4031 0.4958 0.4777 0.0684  0.1067  -0.1358 277 GLU D CB  
8162  C CG  . GLU D 277 ? 0.4118 0.5065 0.4858 0.0646  0.1156  -0.1377 277 GLU D CG  
8163  C CD  . GLU D 277 ? 0.4211 0.5291 0.5081 0.0622  0.1199  -0.1491 277 GLU D CD  
8164  O OE1 . GLU D 277 ? 0.4279 0.5437 0.5208 0.0653  0.1187  -0.1572 277 GLU D OE1 
8165  O OE2 . GLU D 277 ? 0.4222 0.5329 0.5137 0.0572  0.1245  -0.1504 277 GLU D OE2 
8166  N N   . ILE D 278 ? 0.3350 0.4180 0.4074 0.0720  0.0874  -0.1248 278 ILE D N   
8167  C CA  . ILE D 278 ? 0.3319 0.4138 0.4037 0.0752  0.0805  -0.1250 278 ILE D CA  
8168  C C   . ILE D 278 ? 0.3471 0.4352 0.4210 0.0793  0.0829  -0.1348 278 ILE D C   
8169  O O   . ILE D 278 ? 0.3542 0.4529 0.4379 0.0793  0.0846  -0.1438 278 ILE D O   
8170  C CB  . ILE D 278 ? 0.3200 0.4057 0.3999 0.0736  0.0725  -0.1250 278 ILE D CB  
8171  C CG1 . ILE D 278 ? 0.3062 0.3849 0.3828 0.0697  0.0706  -0.1154 278 ILE D CG1 
8172  C CG2 . ILE D 278 ? 0.3187 0.4044 0.3982 0.0771  0.0654  -0.1265 278 ILE D CG2 
8173  C CD1 . ILE D 278 ? 0.2962 0.3785 0.3800 0.0675  0.0642  -0.1158 278 ILE D CD1 
8174  N N   . PRO D 279 ? 0.3729 0.4552 0.4384 0.0829  0.0831  -0.1339 279 PRO D N   
8175  C CA  . PRO D 279 ? 0.3893 0.4767 0.4557 0.0872  0.0859  -0.1435 279 PRO D CA  
8176  C C   . PRO D 279 ? 0.3890 0.4860 0.4667 0.0896  0.0791  -0.1513 279 PRO D C   
8177  O O   . PRO D 279 ? 0.3780 0.4729 0.4568 0.0900  0.0705  -0.1479 279 PRO D O   
8178  C CB  . PRO D 279 ? 0.3926 0.4695 0.4468 0.0901  0.0857  -0.1392 279 PRO D CB  
8179  C CG  . PRO D 279 ? 0.3753 0.4443 0.4260 0.0875  0.0799  -0.1287 279 PRO D CG  
8180  C CD  . PRO D 279 ? 0.3659 0.4365 0.4206 0.0831  0.0812  -0.1244 279 PRO D CD  
8181  N N   . PRO D 280 ? 0.4247 0.5324 0.5107 0.0915  0.0825  -0.1622 280 PRO D N   
8182  C CA  . PRO D 280 ? 0.4264 0.5434 0.5232 0.0949  0.0755  -0.1707 280 PRO D CA  
8183  C C   . PRO D 280 ? 0.4290 0.5414 0.5210 0.1000  0.0694  -0.1711 280 PRO D C   
8184  O O   . PRO D 280 ? 0.4257 0.5422 0.5240 0.1027  0.0609  -0.1745 280 PRO D O   
8185  C CB  . PRO D 280 ? 0.4431 0.5718 0.5483 0.0964  0.0825  -0.1828 280 PRO D CB  
8186  C CG  . PRO D 280 ? 0.4451 0.5722 0.5465 0.0915  0.0921  -0.1796 280 PRO D CG  
8187  C CD  . PRO D 280 ? 0.4386 0.5512 0.5252 0.0904  0.0930  -0.1678 280 PRO D CD  
8188  N N   . GLU D 281 ? 0.4642 0.5677 0.5446 0.1017  0.0732  -0.1681 281 GLU D N   
8189  C CA  . GLU D 281 ? 0.4666 0.5645 0.5416 0.1061  0.0673  -0.1682 281 GLU D CA  
8190  C C   . GLU D 281 ? 0.4492 0.5420 0.5232 0.1046  0.0577  -0.1600 281 GLU D C   
8191  O O   . GLU D 281 ? 0.4505 0.5404 0.5221 0.1083  0.0512  -0.1609 281 GLU D O   
8192  C CB  . GLU D 281 ? 0.4762 0.5641 0.5379 0.1072  0.0737  -0.1655 281 GLU D CB  
8193  C CG  . GLU D 281 ? 0.4956 0.5868 0.5552 0.1086  0.0846  -0.1731 281 GLU D CG  
8194  C CD  . GLU D 281 ? 0.4937 0.5848 0.5512 0.1036  0.0928  -0.1689 281 GLU D CD  
8195  O OE1 . GLU D 281 ? 0.4792 0.5731 0.5432 0.0994  0.0900  -0.1643 281 GLU D OE1 
8196  O OE2 . GLU D 281 ? 0.5081 0.5957 0.5567 0.1039  0.1021  -0.1706 281 GLU D OE2 
8197  N N   . ILE D 282 ? 0.4115 0.5030 0.4866 0.0993  0.0568  -0.1524 282 ILE D N   
8198  C CA  . ILE D 282 ? 0.3962 0.4834 0.4702 0.0975  0.0484  -0.1453 282 ILE D CA  
8199  C C   . ILE D 282 ? 0.3968 0.4909 0.4787 0.1009  0.0400  -0.1517 282 ILE D C   
8200  O O   . ILE D 282 ? 0.3911 0.4812 0.4702 0.1022  0.0325  -0.1488 282 ILE D O   
8201  C CB  . ILE D 282 ? 0.3822 0.4667 0.4559 0.0914  0.0501  -0.1369 282 ILE D CB  
8202  C CG1 . ILE D 282 ? 0.3788 0.4530 0.4421 0.0891  0.0548  -0.1282 282 ILE D CG1 
8203  C CG2 . ILE D 282 ? 0.3689 0.4533 0.4453 0.0897  0.0419  -0.1331 282 ILE D CG2 
8204  C CD1 . ILE D 282 ? 0.3674 0.4383 0.4298 0.0839  0.0572  -0.1203 282 ILE D CD1 
8205  N N   . GLY D 283 ? 0.3871 0.4916 0.4790 0.1026  0.0410  -0.1609 283 GLY D N   
8206  C CA  . GLY D 283 ? 0.3900 0.5011 0.4897 0.1068  0.0328  -0.1681 283 GLY D CA  
8207  C C   . GLY D 283 ? 0.3992 0.5072 0.4951 0.1131  0.0276  -0.1718 283 GLY D C   
8208  O O   . GLY D 283 ? 0.3981 0.5068 0.4962 0.1163  0.0187  -0.1738 283 GLY D O   
8209  N N   . ASN D 284 ? 0.4642 0.5680 0.5537 0.1152  0.0330  -0.1729 284 ASN D N   
8210  C CA  . ASN D 284 ? 0.4739 0.5734 0.5588 0.1211  0.0283  -0.1763 284 ASN D CA  
8211  C C   . ASN D 284 ? 0.4625 0.5523 0.5394 0.1199  0.0214  -0.1674 284 ASN D C   
8212  O O   . ASN D 284 ? 0.4696 0.5555 0.5430 0.1248  0.0158  -0.1700 284 ASN D O   
8213  C CB  . ASN D 284 ? 0.4886 0.5850 0.5675 0.1232  0.0367  -0.1797 284 ASN D CB  
8214  C CG  . ASN D 284 ? 0.5081 0.6131 0.5942 0.1292  0.0389  -0.1932 284 ASN D CG  
8215  O OD1 . ASN D 284 ? 0.5138 0.6230 0.6061 0.1346  0.0313  -0.2001 284 ASN D OD1 
8216  N ND2 . ASN D 284 ? 0.5195 0.6272 0.6048 0.1286  0.0495  -0.1973 284 ASN D ND2 
8217  N N   . MET D 285 ? 0.3896 0.4756 0.4635 0.1137  0.0219  -0.1573 285 MET D N   
8218  C CA  . MET D 285 ? 0.3784 0.4564 0.4457 0.1119  0.0158  -0.1491 285 MET D CA  
8219  C C   . MET D 285 ? 0.3752 0.4560 0.4470 0.1139  0.0067  -0.1512 285 MET D C   
8220  O O   . MET D 285 ? 0.3628 0.4434 0.4355 0.1098  0.0046  -0.1457 285 MET D O   
8221  C CB  . MET D 285 ? 0.3636 0.4370 0.4269 0.1049  0.0200  -0.1386 285 MET D CB  
8222  C CG  . MET D 285 ? 0.3666 0.4351 0.4237 0.1032  0.0280  -0.1355 285 MET D CG  
8223  S SD  . MET D 285 ? 0.3500 0.4099 0.4003 0.0969  0.0292  -0.1227 285 MET D SD  
8224  C CE  . MET D 285 ? 0.3454 0.4084 0.3995 0.0921  0.0368  -0.1203 285 MET D CE  
8225  N N   . THR D 286 ? 0.3674 0.4500 0.4413 0.1208  0.0014  -0.1595 286 THR D N   
8226  C CA  . THR D 286 ? 0.3687 0.4542 0.4472 0.1243  -0.0075 -0.1636 286 THR D CA  
8227  C C   . THR D 286 ? 0.3592 0.4368 0.4310 0.1228  -0.0142 -0.1562 286 THR D C   
8228  O O   . THR D 286 ? 0.3606 0.4390 0.4345 0.1256  -0.0216 -0.1587 286 THR D O   
8229  C CB  . THR D 286 ? 0.3873 0.4756 0.4693 0.1328  -0.0116 -0.1748 286 THR D CB  
8230  O OG1 . THR D 286 ? 0.3941 0.4738 0.4676 0.1358  -0.0131 -0.1737 286 THR D OG1 
8231  C CG2 . THR D 286 ? 0.3979 0.4953 0.4876 0.1342  -0.0043 -0.1833 286 THR D CG2 
8232  N N   . ALA D 287 ? 0.3374 0.4074 0.4012 0.1187  -0.0116 -0.1474 287 ALA D N   
8233  C CA  . ALA D 287 ? 0.3286 0.3914 0.3864 0.1168  -0.0167 -0.1404 287 ALA D CA  
8234  C C   . ALA D 287 ? 0.3118 0.3739 0.3690 0.1092  -0.0130 -0.1314 287 ALA D C   
8235  O O   . ALA D 287 ? 0.3039 0.3601 0.3561 0.1068  -0.0156 -0.1251 287 ALA D O   
8236  C CB  . ALA D 287 ? 0.3321 0.3867 0.3819 0.1182  -0.0177 -0.1378 287 ALA D CB  
8237  N N   . LEU D 288 ? 0.3273 0.3946 0.3891 0.1056  -0.0068 -0.1310 288 LEU D N   
8238  C CA  . LEU D 288 ? 0.3129 0.3784 0.3737 0.0987  -0.0029 -0.1226 288 LEU D CA  
8239  C C   . LEU D 288 ? 0.3064 0.3723 0.3686 0.0974  -0.0076 -0.1210 288 LEU D C   
8240  O O   . LEU D 288 ? 0.3116 0.3831 0.3793 0.1004  -0.0114 -0.1273 288 LEU D O   
8241  C CB  . LEU D 288 ? 0.3119 0.3821 0.3772 0.0957  0.0045  -0.1232 288 LEU D CB  
8242  C CG  . LEU D 288 ? 0.3113 0.3775 0.3723 0.0934  0.0115  -0.1191 288 LEU D CG  
8243  C CD1 . LEU D 288 ? 0.3120 0.3825 0.3774 0.0909  0.0185  -0.1203 288 LEU D CD1 
8244  C CD2 . LEU D 288 ? 0.2996 0.3583 0.3544 0.0890  0.0120  -0.1095 288 LEU D CD2 
8245  N N   . ASP D 289 ? 0.2756 0.3355 0.3328 0.0932  -0.0073 -0.1129 289 ASP D N   
8246  C CA  . ASP D 289 ? 0.2686 0.3277 0.3260 0.0911  -0.0100 -0.1100 289 ASP D CA  
8247  C C   . ASP D 289 ? 0.2579 0.3173 0.3168 0.0849  -0.0043 -0.1044 289 ASP D C   
8248  O O   . ASP D 289 ? 0.2550 0.3172 0.3171 0.0838  -0.0054 -0.1051 289 ASP D O   
8249  C CB  . ASP D 289 ? 0.2660 0.3178 0.3169 0.0911  -0.0135 -0.1055 289 ASP D CB  
8250  C CG  . ASP D 289 ? 0.2563 0.3054 0.3059 0.0869  -0.0128 -0.0997 289 ASP D CG  
8251  O OD1 . ASP D 289 ? 0.2585 0.3093 0.3095 0.0889  -0.0171 -0.1024 289 ASP D OD1 
8252  O OD2 . ASP D 289 ? 0.2472 0.2925 0.2944 0.0820  -0.0081 -0.0927 289 ASP D OD2 
8253  N N   . THR D 290 ? 0.2431 0.2994 0.2997 0.0813  0.0015  -0.0992 290 THR D N   
8254  C CA  . THR D 290 ? 0.2341 0.2893 0.2916 0.0759  0.0068  -0.0936 290 THR D CA  
8255  C C   . THR D 290 ? 0.2360 0.2913 0.2936 0.0749  0.0128  -0.0930 290 THR D C   
8256  O O   . THR D 290 ? 0.2373 0.2888 0.2908 0.0754  0.0142  -0.0909 290 THR D O   
8257  C CB  . THR D 290 ? 0.2249 0.2735 0.2777 0.0723  0.0076  -0.0858 290 THR D CB  
8258  O OG1 . THR D 290 ? 0.2235 0.2718 0.2761 0.0728  0.0034  -0.0860 290 THR D OG1 
8259  C CG2 . THR D 290 ? 0.2174 0.2639 0.2705 0.0674  0.0135  -0.0801 290 THR D CG2 
8260  N N   . LEU D 291 ? 0.2381 0.2975 0.3003 0.0735  0.0163  -0.0950 291 LEU D N   
8261  C CA  . LEU D 291 ? 0.2406 0.2997 0.3029 0.0725  0.0226  -0.0944 291 LEU D CA  
8262  C C   . LEU D 291 ? 0.2330 0.2897 0.2956 0.0678  0.0267  -0.0889 291 LEU D C   
8263  O O   . LEU D 291 ? 0.2310 0.2914 0.2982 0.0665  0.0260  -0.0907 291 LEU D O   
8264  C CB  . LEU D 291 ? 0.2512 0.3176 0.3189 0.0757  0.0237  -0.1029 291 LEU D CB  
8265  C CG  . LEU D 291 ? 0.2555 0.3223 0.3237 0.0746  0.0311  -0.1032 291 LEU D CG  
8266  C CD1 . LEU D 291 ? 0.2576 0.3180 0.3187 0.0753  0.0343  -0.0993 291 LEU D CD1 
8267  C CD2 . LEU D 291 ? 0.2664 0.3417 0.3415 0.0777  0.0323  -0.1127 291 LEU D CD2 
8268  N N   . SER D 292 ? 0.2429 0.2934 0.3007 0.0658  0.0308  -0.0825 292 SER D N   
8269  C CA  . SER D 292 ? 0.2364 0.2836 0.2936 0.0620  0.0344  -0.0769 292 SER D CA  
8270  C C   . SER D 292 ? 0.2398 0.2839 0.2941 0.0621  0.0403  -0.0746 292 SER D C   
8271  O O   . SER D 292 ? 0.2394 0.2784 0.2886 0.0626  0.0415  -0.0708 292 SER D O   
8272  C CB  . SER D 292 ? 0.2278 0.2695 0.2815 0.0598  0.0329  -0.0704 292 SER D CB  
8273  O OG  . SER D 292 ? 0.2228 0.2613 0.2759 0.0569  0.0363  -0.0653 292 SER D OG  
8274  N N   . LEU D 293 ? 0.2426 0.2900 0.3003 0.0616  0.0439  -0.0773 293 LEU D N   
8275  C CA  . LEU D 293 ? 0.2466 0.2909 0.3010 0.0618  0.0498  -0.0750 293 LEU D CA  
8276  C C   . LEU D 293 ? 0.2419 0.2849 0.2974 0.0588  0.0522  -0.0714 293 LEU D C   
8277  O O   . LEU D 293 ? 0.2465 0.2895 0.3014 0.0589  0.0567  -0.0717 293 LEU D O   
8278  C CB  . LEU D 293 ? 0.2578 0.3071 0.3146 0.0642  0.0530  -0.0820 293 LEU D CB  
8279  C CG  . LEU D 293 ? 0.2640 0.3164 0.3212 0.0676  0.0500  -0.0875 293 LEU D CG  
8280  C CD1 . LEU D 293 ? 0.2747 0.3350 0.3376 0.0697  0.0522  -0.0964 293 LEU D CD1 
8281  C CD2 . LEU D 293 ? 0.2667 0.3128 0.3165 0.0695  0.0514  -0.0843 293 LEU D CD2 
8282  N N   . HIS D 294 ? 0.2517 0.2936 0.3084 0.0564  0.0491  -0.0684 294 HIS D N   
8283  C CA  . HIS D 294 ? 0.2479 0.2892 0.3065 0.0536  0.0507  -0.0662 294 HIS D CA  
8284  C C   . HIS D 294 ? 0.2464 0.2822 0.2993 0.0536  0.0536  -0.0601 294 HIS D C   
8285  O O   . HIS D 294 ? 0.2466 0.2785 0.2937 0.0557  0.0537  -0.0567 294 HIS D O   
8286  C CB  . HIS D 294 ? 0.2407 0.2821 0.3016 0.0513  0.0469  -0.0650 294 HIS D CB  
8287  C CG  . HIS D 294 ? 0.2344 0.2702 0.2902 0.0508  0.0454  -0.0587 294 HIS D CG  
8288  N ND1 . HIS D 294 ? 0.2306 0.2626 0.2837 0.0495  0.0471  -0.0535 294 HIS D ND1 
8289  C CD2 . HIS D 294 ? 0.2315 0.2658 0.2852 0.0514  0.0423  -0.0573 294 HIS D CD2 
8290  C CE1 . HIS D 294 ? 0.2260 0.2546 0.2757 0.0495  0.0452  -0.0494 294 HIS D CE1 
8291  N NE2 . HIS D 294 ? 0.2264 0.2559 0.2763 0.0504  0.0427  -0.0514 294 HIS D NE2 
8292  N N   . THR D 295 ? 0.2700 0.3060 0.3252 0.0513  0.0556  -0.0595 295 THR D N   
8293  C CA  . THR D 295 ? 0.2688 0.3012 0.3202 0.0512  0.0576  -0.0552 295 THR D CA  
8294  C C   . THR D 295 ? 0.2781 0.3096 0.3242 0.0546  0.0605  -0.0553 295 THR D C   
8295  O O   . THR D 295 ? 0.2747 0.3033 0.3148 0.0570  0.0595  -0.0516 295 THR D O   
8296  C CB  . THR D 295 ? 0.2612 0.2900 0.3096 0.0505  0.0546  -0.0499 295 THR D CB  
8297  O OG1 . THR D 295 ? 0.2567 0.2863 0.3090 0.0480  0.0521  -0.0502 295 THR D OG1 
8298  C CG2 . THR D 295 ? 0.2620 0.2887 0.3103 0.0487  0.0560  -0.0472 295 THR D CG2 
8299  N N   . ASN D 296 ? 0.2831 0.3180 0.3318 0.0551  0.0640  -0.0603 296 ASN D N   
8300  C CA  . ASN D 296 ? 0.2846 0.3191 0.3283 0.0583  0.0677  -0.0614 296 ASN D CA  
8301  C C   . ASN D 296 ? 0.2921 0.3294 0.3396 0.0562  0.0727  -0.0652 296 ASN D C   
8302  O O   . ASN D 296 ? 0.2948 0.3333 0.3485 0.0523  0.0730  -0.0660 296 ASN D O   
8303  C CB  . ASN D 296 ? 0.2906 0.3262 0.3332 0.0612  0.0678  -0.0649 296 ASN D CB  
8304  C CG  . ASN D 296 ? 0.2884 0.3186 0.3244 0.0637  0.0654  -0.0606 296 ASN D CG  
8305  O OD1 . ASN D 296 ? 0.2937 0.3205 0.3226 0.0668  0.0677  -0.0589 296 ASN D OD1 
8306  N ND2 . ASN D 296 ? 0.2808 0.3103 0.3190 0.0621  0.0610  -0.0591 296 ASN D ND2 
8307  N N   . LYS D 297 ? 0.3114 0.3494 0.3551 0.0587  0.0771  -0.0677 297 LYS D N   
8308  C CA  . LYS D 297 ? 0.3187 0.3594 0.3656 0.0564  0.0829  -0.0718 297 LYS D CA  
8309  C C   . LYS D 297 ? 0.3295 0.3759 0.3794 0.0575  0.0866  -0.0793 297 LYS D C   
8310  O O   . LYS D 297 ? 0.3399 0.3883 0.3889 0.0573  0.0927  -0.0830 297 LYS D O   
8311  C CB  . LYS D 297 ? 0.3224 0.3597 0.3626 0.0572  0.0859  -0.0691 297 LYS D CB  
8312  C CG  . LYS D 297 ? 0.3131 0.3459 0.3541 0.0543  0.0834  -0.0637 297 LYS D CG  
8313  C CD  . LYS D 297 ? 0.3208 0.3499 0.3564 0.0544  0.0862  -0.0618 297 LYS D CD  
8314  C CE  . LYS D 297 ? 0.3086 0.3322 0.3462 0.0513  0.0842  -0.0564 297 LYS D CE  
8315  N NZ  . LYS D 297 ? 0.3224 0.3413 0.3544 0.0520  0.0853  -0.0537 297 LYS D NZ  
8316  N N   . LEU D 298 ? 0.3090 0.3585 0.3630 0.0584  0.0831  -0.0821 298 LEU D N   
8317  C CA  . LEU D 298 ? 0.3189 0.3752 0.3775 0.0595  0.0856  -0.0904 298 LEU D CA  
8318  C C   . LEU D 298 ? 0.3232 0.3865 0.3912 0.0556  0.0894  -0.0968 298 LEU D C   
8319  O O   . LEU D 298 ? 0.3159 0.3793 0.3892 0.0518  0.0878  -0.0955 298 LEU D O   
8320  C CB  . LEU D 298 ? 0.3145 0.3733 0.3768 0.0609  0.0796  -0.0924 298 LEU D CB  
8321  C CG  . LEU D 298 ? 0.3169 0.3718 0.3722 0.0650  0.0777  -0.0909 298 LEU D CG  
8322  C CD1 . LEU D 298 ? 0.3134 0.3591 0.3584 0.0664  0.0780  -0.0825 298 LEU D CD1 
8323  C CD2 . LEU D 298 ? 0.3096 0.3665 0.3692 0.0650  0.0707  -0.0918 298 LEU D CD2 
8324  N N   . THR D 299 ? 0.3513 0.4205 0.4215 0.0564  0.0949  -0.1042 299 THR D N   
8325  C CA  . THR D 299 ? 0.3578 0.4346 0.4372 0.0526  0.0997  -0.1116 299 THR D CA  
8326  C C   . THR D 299 ? 0.3667 0.4537 0.4535 0.0543  0.1004  -0.1215 299 THR D C   
8327  O O   . THR D 299 ? 0.3685 0.4556 0.4524 0.0585  0.0974  -0.1225 299 THR D O   
8328  C CB  . THR D 299 ? 0.3672 0.4418 0.4419 0.0506  0.1079  -0.1114 299 THR D CB  
8329  O OG1 . THR D 299 ? 0.3772 0.4494 0.4420 0.0547  0.1113  -0.1113 299 THR D OG1 
8330  C CG2 . THR D 299 ? 0.3583 0.4245 0.4289 0.0482  0.1068  -0.1031 299 THR D CG2 
8331  N N   . GLY D 300 ? 0.3480 0.4438 0.4449 0.0510  0.1043  -0.1296 300 GLY D N   
8332  C CA  . GLY D 300 ? 0.3573 0.4644 0.4629 0.0526  0.1051  -0.1403 300 GLY D CA  
8333  C C   . GLY D 300 ? 0.3485 0.4607 0.4627 0.0535  0.0965  -0.1430 300 GLY D C   
8334  O O   . GLY D 300 ? 0.3355 0.4422 0.4484 0.0524  0.0905  -0.1364 300 GLY D O   
8335  N N   . PRO D 301 ? 0.3292 0.4522 0.4521 0.0558  0.0959  -0.1530 301 PRO D N   
8336  C CA  . PRO D 301 ? 0.3224 0.4515 0.4542 0.0569  0.0875  -0.1569 301 PRO D CA  
8337  C C   . PRO D 301 ? 0.3167 0.4408 0.4423 0.0615  0.0801  -0.1527 301 PRO D C   
8338  O O   . PRO D 301 ? 0.3207 0.4391 0.4372 0.0646  0.0816  -0.1495 301 PRO D O   
8339  C CB  . PRO D 301 ? 0.3353 0.4787 0.4791 0.0581  0.0904  -0.1703 301 PRO D CB  
8340  C CG  . PRO D 301 ? 0.3489 0.4920 0.4866 0.0602  0.0982  -0.1724 301 PRO D CG  
8341  C CD  . PRO D 301 ? 0.3459 0.4771 0.4716 0.0574  0.1031  -0.1623 301 PRO D CD  
8342  N N   . ILE D 302 ? 0.2923 0.4183 0.4226 0.0618  0.0720  -0.1530 302 ILE D N   
8343  C CA  . ILE D 302 ? 0.2882 0.4114 0.4145 0.0660  0.0644  -0.1509 302 ILE D CA  
8344  C C   . ILE D 302 ? 0.3008 0.4323 0.4318 0.0711  0.0643  -0.1607 302 ILE D C   
8345  O O   . ILE D 302 ? 0.3088 0.4517 0.4509 0.0716  0.0654  -0.1710 302 ILE D O   
8346  C CB  . ILE D 302 ? 0.2779 0.4021 0.4083 0.0650  0.0563  -0.1501 302 ILE D CB  
8347  C CG1 . ILE D 302 ? 0.2665 0.3824 0.3923 0.0601  0.0570  -0.1408 302 ILE D CG1 
8348  C CG2 . ILE D 302 ? 0.2749 0.3965 0.4011 0.0692  0.0486  -0.1485 302 ILE D CG2 
8349  C CD1 . ILE D 302 ? 0.2579 0.3752 0.3878 0.0586  0.0504  -0.1407 302 ILE D CD1 
8350  N N   . PRO D 303 ? 0.3180 0.4444 0.4412 0.0751  0.0631  -0.1585 303 PRO D N   
8351  C CA  . PRO D 303 ? 0.3317 0.4656 0.4590 0.0804  0.0634  -0.1683 303 PRO D CA  
8352  C C   . PRO D 303 ? 0.3318 0.4738 0.4685 0.0838  0.0548  -0.1757 303 PRO D C   
8353  O O   . PRO D 303 ? 0.3226 0.4601 0.4562 0.0847  0.0469  -0.1711 303 PRO D O   
8354  C CB  . PRO D 303 ? 0.3330 0.4572 0.4483 0.0834  0.0633  -0.1626 303 PRO D CB  
8355  C CG  . PRO D 303 ? 0.3176 0.4314 0.4253 0.0806  0.0589  -0.1510 303 PRO D CG  
8356  C CD  . PRO D 303 ? 0.3101 0.4240 0.4208 0.0750  0.0617  -0.1476 303 PRO D CD  
8357  N N   . SER D 304 ? 0.3413 0.4958 0.4896 0.0858  0.0566  -0.1877 304 SER D N   
8358  C CA  . SER D 304 ? 0.3440 0.5072 0.5021 0.0901  0.0484  -0.1963 304 SER D CA  
8359  C C   . SER D 304 ? 0.3478 0.5073 0.5008 0.0965  0.0421  -0.1968 304 SER D C   
8360  O O   . SER D 304 ? 0.3479 0.5111 0.5058 0.1004  0.0333  -0.2013 304 SER D O   
8361  C CB  . SER D 304 ? 0.3575 0.5354 0.5296 0.0915  0.0524  -0.2099 304 SER D CB  
8362  O OG  . SER D 304 ? 0.3717 0.5517 0.5421 0.0940  0.0601  -0.2147 304 SER D OG  
8363  N N   . THR D 305 ? 0.3622 0.5142 0.5052 0.0977  0.0462  -0.1926 305 THR D N   
8364  C CA  . THR D 305 ? 0.3666 0.5140 0.5040 0.1035  0.0407  -0.1929 305 THR D CA  
8365  C C   . THR D 305 ? 0.3529 0.4910 0.4829 0.1028  0.0324  -0.1836 305 THR D C   
8366  O O   . THR D 305 ? 0.3560 0.4905 0.4820 0.1075  0.0264  -0.1841 305 THR D O   
8367  C CB  . THR D 305 ? 0.3750 0.5163 0.5032 0.1046  0.0481  -0.1909 305 THR D CB  
8368  O OG1 . THR D 305 ? 0.3639 0.4945 0.4816 0.0993  0.0518  -0.1788 305 THR D OG1 
8369  C CG2 . THR D 305 ? 0.3901 0.5405 0.5246 0.1050  0.0575  -0.2003 305 THR D CG2 
8370  N N   . LEU D 306 ? 0.3421 0.4763 0.4700 0.0970  0.0321  -0.1754 306 LEU D N   
8371  C CA  . LEU D 306 ? 0.3298 0.4558 0.4509 0.0959  0.0250  -0.1670 306 LEU D CA  
8372  C C   . LEU D 306 ? 0.3319 0.4623 0.4581 0.1005  0.0153  -0.1729 306 LEU D C   
8373  O O   . LEU D 306 ? 0.3270 0.4508 0.4467 0.1019  0.0089  -0.1681 306 LEU D O   
8374  C CB  . LEU D 306 ? 0.3164 0.4383 0.4354 0.0892  0.0272  -0.1586 306 LEU D CB  
8375  C CG  . LEU D 306 ? 0.3117 0.4254 0.4227 0.0849  0.0348  -0.1498 306 LEU D CG  
8376  C CD1 . LEU D 306 ? 0.2975 0.4048 0.4046 0.0796  0.0338  -0.1404 306 LEU D CD1 
8377  C CD2 . LEU D 306 ? 0.3149 0.4213 0.4167 0.0876  0.0353  -0.1463 306 LEU D CD2 
8378  N N   . GLY D 307 ? 0.3153 0.4568 0.4532 0.1029  0.0139  -0.1834 307 GLY D N   
8379  C CA  . GLY D 307 ? 0.3192 0.4650 0.4623 0.1081  0.0042  -0.1899 307 GLY D CA  
8380  C C   . GLY D 307 ? 0.3287 0.4715 0.4679 0.1151  -0.0011 -0.1931 307 GLY D C   
8381  O O   . GLY D 307 ? 0.3301 0.4716 0.4690 0.1193  -0.0103 -0.1950 307 GLY D O   
8382  N N   . ASN D 308 ? 0.3812 0.5219 0.5168 0.1167  0.0046  -0.1938 308 ASN D N   
8383  C CA  . ASN D 308 ? 0.3912 0.5280 0.5225 0.1233  -0.0001 -0.1968 308 ASN D CA  
8384  C C   . ASN D 308 ? 0.3818 0.5071 0.5020 0.1226  -0.0061 -0.1872 308 ASN D C   
8385  O O   . ASN D 308 ? 0.3888 0.5109 0.5066 0.1285  -0.0137 -0.1902 308 ASN D O   
8386  C CB  . ASN D 308 ? 0.4010 0.5369 0.5294 0.1244  0.0083  -0.1987 308 ASN D CB  
8387  C CG  . ASN D 308 ? 0.4143 0.5623 0.5540 0.1265  0.0141  -0.2104 308 ASN D CG  
8388  O OD1 . ASN D 308 ? 0.4162 0.5739 0.5672 0.1274  0.0113  -0.2176 308 ASN D OD1 
8389  N ND2 . ASN D 308 ? 0.4245 0.5719 0.5612 0.1273  0.0224  -0.2126 308 ASN D ND2 
8390  N N   . ILE D 309 ? 0.3255 0.4442 0.4389 0.1158  -0.0028 -0.1761 309 ILE D N   
8391  C CA  . ILE D 309 ? 0.3165 0.4247 0.4196 0.1144  -0.0071 -0.1668 309 ILE D CA  
8392  C C   . ILE D 309 ? 0.3123 0.4210 0.4170 0.1153  -0.0153 -0.1671 309 ILE D C   
8393  O O   . ILE D 309 ? 0.3019 0.4115 0.4079 0.1103  -0.0142 -0.1629 309 ILE D O   
8394  C CB  . ILE D 309 ? 0.3036 0.4051 0.3996 0.1072  -0.0005 -0.1557 309 ILE D CB  
8395  C CG1 . ILE D 309 ? 0.3090 0.4112 0.4045 0.1062  0.0085  -0.1565 309 ILE D CG1 
8396  C CG2 . ILE D 309 ? 0.2969 0.3883 0.3830 0.1065  -0.0041 -0.1475 309 ILE D CG2 
8397  C CD1 . ILE D 309 ? 0.2979 0.3950 0.3887 0.0993  0.0153  -0.1470 309 ILE D CD1 
8398  N N   . LYS D 310 ? 0.3262 0.4337 0.4304 0.1219  -0.0237 -0.1721 310 LYS D N   
8399  C CA  . LYS D 310 ? 0.3247 0.4318 0.4296 0.1237  -0.0320 -0.1730 310 LYS D CA  
8400  C C   . LYS D 310 ? 0.3142 0.4108 0.4084 0.1205  -0.0344 -0.1626 310 LYS D C   
8401  O O   . LYS D 310 ? 0.3113 0.4065 0.4046 0.1207  -0.0397 -0.1616 310 LYS D O   
8402  C CB  . LYS D 310 ? 0.3410 0.4503 0.4497 0.1329  -0.0407 -0.1834 310 LYS D CB  
8403  C CG  . LYS D 310 ? 0.3535 0.4738 0.4737 0.1369  -0.0385 -0.1951 310 LYS D CG  
8404  C CD  . LYS D 310 ? 0.3479 0.4778 0.4775 0.1326  -0.0344 -0.1976 310 LYS D CD  
8405  C CE  . LYS D 310 ? 0.3624 0.5043 0.5054 0.1383  -0.0356 -0.2115 310 LYS D CE  
8406  N NZ  . LYS D 310 ? 0.3575 0.5091 0.5104 0.1340  -0.0317 -0.2145 310 LYS D NZ  
8407  N N   . THR D 311 ? 0.3168 0.4062 0.4032 0.1176  -0.0303 -0.1553 311 THR D N   
8408  C CA  . THR D 311 ? 0.3070 0.3871 0.3843 0.1142  -0.0315 -0.1457 311 THR D CA  
8409  C C   . THR D 311 ? 0.2919 0.3710 0.3679 0.1061  -0.0247 -0.1371 311 THR D C   
8410  O O   . THR D 311 ? 0.2833 0.3559 0.3532 0.1028  -0.0250 -0.1295 311 THR D O   
8411  C CB  . THR D 311 ? 0.3102 0.3829 0.3802 0.1157  -0.0315 -0.1429 311 THR D CB  
8412  O OG1 . THR D 311 ? 0.3108 0.3856 0.3819 0.1140  -0.0242 -0.1428 311 THR D OG1 
8413  C CG2 . THR D 311 ? 0.3256 0.3964 0.3949 0.1240  -0.0397 -0.1504 311 THR D CG2 
8414  N N   . LEU D 312 ? 0.2870 0.3721 0.3688 0.1030  -0.0184 -0.1382 312 LEU D N   
8415  C CA  . LEU D 312 ? 0.2745 0.3573 0.3546 0.0957  -0.0118 -0.1302 312 LEU D CA  
8416  C C   . LEU D 312 ? 0.2673 0.3504 0.3484 0.0932  -0.0141 -0.1279 312 LEU D C   
8417  O O   . LEU D 312 ? 0.2708 0.3608 0.3588 0.0947  -0.0164 -0.1341 312 LEU D O   
8418  C CB  . LEU D 312 ? 0.2762 0.3644 0.3618 0.0937  -0.0047 -0.1327 312 LEU D CB  
8419  C CG  . LEU D 312 ? 0.2653 0.3501 0.3488 0.0869  0.0022  -0.1246 312 LEU D CG  
8420  C CD1 . LEU D 312 ? 0.2610 0.3376 0.3363 0.0850  0.0051  -0.1171 312 LEU D CD1 
8421  C CD2 . LEU D 312 ? 0.2688 0.3597 0.3588 0.0855  0.0082  -0.1286 312 LEU D CD2 
8422  N N   . ALA D 313 ? 0.2522 0.3281 0.3268 0.0894  -0.0132 -0.1193 313 ALA D N   
8423  C CA  . ALA D 313 ? 0.2457 0.3207 0.3199 0.0869  -0.0145 -0.1164 313 ALA D CA  
8424  C C   . ALA D 313 ? 0.2352 0.3082 0.3091 0.0803  -0.0077 -0.1096 313 ALA D C   
8425  O O   . ALA D 313 ? 0.2310 0.3050 0.3066 0.0782  -0.0079 -0.1087 313 ALA D O   
8426  C CB  . ALA D 313 ? 0.2446 0.3126 0.3117 0.0882  -0.0189 -0.1126 313 ALA D CB  
8427  N N   . VAL D 314 ? 0.2203 0.2901 0.2920 0.0773  -0.0020 -0.1050 314 VAL D N   
8428  C CA  . VAL D 314 ? 0.2119 0.2789 0.2831 0.0718  0.0043  -0.0987 314 VAL D CA  
8429  C C   . VAL D 314 ? 0.2150 0.2845 0.2890 0.0711  0.0094  -0.1004 314 VAL D C   
8430  O O   . VAL D 314 ? 0.2185 0.2861 0.2898 0.0726  0.0108  -0.1002 314 VAL D O   
8431  C CB  . VAL D 314 ? 0.2045 0.2631 0.2688 0.0688  0.0064  -0.0901 314 VAL D CB  
8432  C CG1 . VAL D 314 ? 0.1973 0.2529 0.2614 0.0638  0.0124  -0.0842 314 VAL D CG1 
8433  C CG2 . VAL D 314 ? 0.2026 0.2584 0.2639 0.0696  0.0022  -0.0885 314 VAL D CG2 
8434  N N   . LEU D 315 ? 0.2068 0.2803 0.2861 0.0689  0.0123  -0.1023 315 LEU D N   
8435  C CA  . LEU D 315 ? 0.2100 0.2853 0.2918 0.0678  0.0181  -0.1036 315 LEU D CA  
8436  C C   . LEU D 315 ? 0.2028 0.2744 0.2839 0.0628  0.0229  -0.0976 315 LEU D C   
8437  O O   . LEU D 315 ? 0.2002 0.2744 0.2853 0.0610  0.0221  -0.0989 315 LEU D O   
8438  C CB  . LEU D 315 ? 0.2187 0.3036 0.3090 0.0704  0.0173  -0.1133 315 LEU D CB  
8439  C CG  . LEU D 315 ? 0.2240 0.3119 0.3177 0.0696  0.0238  -0.1160 315 LEU D CG  
8440  C CD1 . LEU D 315 ? 0.2272 0.3101 0.3147 0.0709  0.0272  -0.1130 315 LEU D CD1 
8441  C CD2 . LEU D 315 ? 0.2334 0.3319 0.3367 0.0725  0.0227  -0.1268 315 LEU D CD2 
8442  N N   . HIS D 316 ? 0.2203 0.2857 0.2963 0.0611  0.0274  -0.0915 316 HIS D N   
8443  C CA  . HIS D 316 ? 0.2147 0.2757 0.2894 0.0572  0.0318  -0.0857 316 HIS D CA  
8444  C C   . HIS D 316 ? 0.2197 0.2809 0.2947 0.0571  0.0375  -0.0864 316 HIS D C   
8445  O O   . HIS D 316 ? 0.2209 0.2774 0.2906 0.0579  0.0400  -0.0828 316 HIS D O   
8446  C CB  . HIS D 316 ? 0.2076 0.2606 0.2755 0.0556  0.0320  -0.0775 316 HIS D CB  
8447  C CG  . HIS D 316 ? 0.2028 0.2549 0.2702 0.0549  0.0279  -0.0763 316 HIS D CG  
8448  N ND1 . HIS D 316 ? 0.1971 0.2431 0.2595 0.0536  0.0279  -0.0699 316 HIS D ND1 
8449  C CD2 . HIS D 316 ? 0.2035 0.2603 0.2747 0.0557  0.0239  -0.0807 316 HIS D CD2 
8450  C CE1 . HIS D 316 ? 0.1948 0.2413 0.2575 0.0535  0.0247  -0.0703 316 HIS D CE1 
8451  N NE2 . HIS D 316 ? 0.1986 0.2514 0.2663 0.0549  0.0220  -0.0767 316 HIS D NE2 
8452  N N   . LEU D 317 ? 0.2276 0.2942 0.3089 0.0560  0.0396  -0.0912 317 LEU D N   
8453  C CA  . LEU D 317 ? 0.2332 0.3004 0.3154 0.0556  0.0456  -0.0924 317 LEU D CA  
8454  C C   . LEU D 317 ? 0.2293 0.2939 0.3123 0.0519  0.0490  -0.0889 317 LEU D C   
8455  O O   . LEU D 317 ? 0.2345 0.3006 0.3195 0.0510  0.0539  -0.0909 317 LEU D O   
8456  C CB  . LEU D 317 ? 0.2425 0.3191 0.3323 0.0576  0.0462  -0.1021 317 LEU D CB  
8457  C CG  . LEU D 317 ? 0.2486 0.3287 0.3384 0.0620  0.0430  -0.1070 317 LEU D CG  
8458  C CD1 . LEU D 317 ? 0.2594 0.3490 0.3571 0.0640  0.0450  -0.1169 317 LEU D CD1 
8459  C CD2 . LEU D 317 ? 0.2496 0.3227 0.3308 0.0637  0.0449  -0.1018 317 LEU D CD2 
8460  N N   . TYR D 318 ? 0.2575 0.3181 0.3389 0.0496  0.0468  -0.0841 318 TYR D N   
8461  C CA  . TYR D 318 ? 0.2544 0.3132 0.3377 0.0461  0.0494  -0.0819 318 TYR D CA  
8462  C C   . TYR D 318 ? 0.2543 0.3066 0.3318 0.0457  0.0537  -0.0760 318 TYR D C   
8463  O O   . TYR D 318 ? 0.2553 0.3041 0.3267 0.0481  0.0542  -0.0727 318 TYR D O   
8464  C CB  . TYR D 318 ? 0.2471 0.3039 0.3305 0.0442  0.0459  -0.0792 318 TYR D CB  
8465  C CG  . TYR D 318 ? 0.2414 0.2916 0.3175 0.0447  0.0442  -0.0722 318 TYR D CG  
8466  C CD1 . TYR D 318 ? 0.2379 0.2819 0.3097 0.0433  0.0467  -0.0658 318 TYR D CD1 
8467  C CD2 . TYR D 318 ? 0.2400 0.2906 0.3143 0.0466  0.0401  -0.0725 318 TYR D CD2 
8468  C CE1 . TYR D 318 ? 0.2332 0.2723 0.2994 0.0438  0.0452  -0.0603 318 TYR D CE1 
8469  C CE2 . TYR D 318 ? 0.2353 0.2803 0.3037 0.0467  0.0391  -0.0666 318 TYR D CE2 
8470  C CZ  . TYR D 318 ? 0.2319 0.2714 0.2965 0.0453  0.0417  -0.0606 318 TYR D CZ  
8471  O OH  . TYR D 318 ? 0.2278 0.2626 0.2875 0.0454  0.0408  -0.0554 318 TYR D OH  
8472  N N   . LEU D 319 ? 0.2618 0.3127 0.3416 0.0427  0.0565  -0.0750 319 LEU D N   
8473  C CA  . LEU D 319 ? 0.2614 0.3069 0.3368 0.0421  0.0602  -0.0702 319 LEU D CA  
8474  C C   . LEU D 319 ? 0.2699 0.3163 0.3425 0.0448  0.0639  -0.0718 319 LEU D C   
8475  O O   . LEU D 319 ? 0.2680 0.3103 0.3335 0.0473  0.0642  -0.0677 319 LEU D O   
8476  C CB  . LEU D 319 ? 0.2530 0.2923 0.3221 0.0425  0.0579  -0.0630 319 LEU D CB  
8477  C CG  . LEU D 319 ? 0.2469 0.2835 0.3180 0.0391  0.0570  -0.0603 319 LEU D CG  
8478  C CD1 . LEU D 319 ? 0.2423 0.2745 0.3083 0.0397  0.0545  -0.0546 319 LEU D CD1 
8479  C CD2 . LEU D 319 ? 0.2489 0.2833 0.3226 0.0364  0.0612  -0.0600 319 LEU D CD2 
8480  N N   . ASN D 320 ? 0.2907 0.3429 0.3692 0.0442  0.0668  -0.0785 320 ASN D N   
8481  C CA  . ASN D 320 ? 0.2983 0.3522 0.3748 0.0463  0.0714  -0.0814 320 ASN D CA  
8482  C C   . ASN D 320 ? 0.3036 0.3615 0.3869 0.0432  0.0765  -0.0867 320 ASN D C   
8483  O O   . ASN D 320 ? 0.3030 0.3608 0.3913 0.0394  0.0764  -0.0869 320 ASN D O   
8484  C CB  . ASN D 320 ? 0.3051 0.3633 0.3818 0.0498  0.0695  -0.0857 320 ASN D CB  
8485  C CG  . ASN D 320 ? 0.2998 0.3524 0.3675 0.0533  0.0677  -0.0804 320 ASN D CG  
8486  O OD1 . ASN D 320 ? 0.3045 0.3540 0.3661 0.0554  0.0712  -0.0785 320 ASN D OD1 
8487  N ND2 . ASN D 320 ? 0.2927 0.3440 0.3596 0.0538  0.0624  -0.0784 320 ASN D ND2 
8488  N N   . GLN D 321 ? 0.3403 0.4018 0.4237 0.0445  0.0814  -0.0914 321 GLN D N   
8489  C CA  . GLN D 321 ? 0.3479 0.4140 0.4379 0.0412  0.0872  -0.0973 321 GLN D CA  
8490  C C   . GLN D 321 ? 0.3566 0.4328 0.4537 0.0423  0.0885  -0.1069 321 GLN D C   
8491  O O   . GLN D 321 ? 0.3671 0.4476 0.4669 0.0411  0.0950  -0.1125 321 GLN D O   
8492  C CB  . GLN D 321 ? 0.3570 0.4183 0.4407 0.0409  0.0935  -0.0948 321 GLN D CB  
8493  C CG  . GLN D 321 ? 0.3511 0.4031 0.4266 0.0416  0.0915  -0.0856 321 GLN D CG  
8494  C CD  . GLN D 321 ? 0.3666 0.4140 0.4388 0.0395  0.0976  -0.0839 321 GLN D CD  
8495  O OE1 . GLN D 321 ? 0.3775 0.4264 0.4553 0.0353  0.1024  -0.0876 321 GLN D OE1 
8496  N NE2 . GLN D 321 ? 0.3543 0.3962 0.4174 0.0423  0.0975  -0.0786 321 GLN D NE2 
8497  N N   . LEU D 322 ? 0.3090 0.3895 0.4095 0.0443  0.0826  -0.1095 322 LEU D N   
8498  C CA  . LEU D 322 ? 0.3171 0.4080 0.4254 0.0458  0.0829  -0.1194 322 LEU D CA  
8499  C C   . LEU D 322 ? 0.3195 0.4184 0.4394 0.0418  0.0848  -0.1267 322 LEU D C   
8500  O O   . LEU D 322 ? 0.3114 0.4091 0.4348 0.0390  0.0814  -0.1250 322 LEU D O   
8501  C CB  . LEU D 322 ? 0.3123 0.4053 0.4212 0.0492  0.0753  -0.1201 322 LEU D CB  
8502  C CG  . LEU D 322 ? 0.3083 0.3931 0.4066 0.0525  0.0725  -0.1126 322 LEU D CG  
8503  C CD1 . LEU D 322 ? 0.3033 0.3901 0.4030 0.0548  0.0649  -0.1137 322 LEU D CD1 
8504  C CD2 . LEU D 322 ? 0.3188 0.4028 0.4114 0.0556  0.0776  -0.1139 322 LEU D CD2 
8505  N N   . ASN D 323 ? 0.3836 0.4908 0.5095 0.0414  0.0904  -0.1353 323 ASN D N   
8506  C CA  . ASN D 323 ? 0.3877 0.5037 0.5255 0.0375  0.0929  -0.1437 323 ASN D CA  
8507  C C   . ASN D 323 ? 0.3953 0.5243 0.5429 0.0402  0.0913  -0.1548 323 ASN D C   
8508  O O   . ASN D 323 ? 0.3965 0.5268 0.5415 0.0451  0.0877  -0.1556 323 ASN D O   
8509  C CB  . ASN D 323 ? 0.3961 0.5108 0.5334 0.0334  0.1022  -0.1446 323 ASN D CB  
8510  C CG  . ASN D 323 ? 0.4094 0.5266 0.5425 0.0356  0.1091  -0.1479 323 ASN D CG  
8511  O OD1 . ASN D 323 ? 0.4117 0.5297 0.5407 0.0405  0.1069  -0.1481 323 ASN D OD1 
8512  N ND2 . ASN D 323 ? 0.4193 0.5374 0.5530 0.0317  0.1179  -0.1507 323 ASN D ND2 
8513  N N   . GLY D 324 ? 0.3459 0.4849 0.5054 0.0371  0.0940  -0.1640 324 GLY D N   
8514  C CA  . GLY D 324 ? 0.3533 0.5059 0.5240 0.0397  0.0921  -0.1756 324 GLY D CA  
8515  C C   . GLY D 324 ? 0.3445 0.5004 0.5209 0.0413  0.0823  -0.1773 324 GLY D C   
8516  O O   . GLY D 324 ? 0.3332 0.4819 0.5063 0.0393  0.0779  -0.1705 324 GLY D O   
8517  N N   . SER D 325 ? 0.3147 0.4819 0.4998 0.0452  0.0789  -0.1871 325 SER D N   
8518  C CA  . SER D 325 ? 0.3091 0.4810 0.5003 0.0475  0.0695  -0.1906 325 SER D CA  
8519  C C   . SER D 325 ? 0.3048 0.4716 0.4880 0.0531  0.0624  -0.1859 325 SER D C   
8520  O O   . SER D 325 ? 0.3091 0.4722 0.4852 0.0559  0.0648  -0.1833 325 SER D O   
8521  C CB  . SER D 325 ? 0.3194 0.5075 0.5264 0.0489  0.0693  -0.2052 325 SER D CB  
8522  O OG  . SER D 325 ? 0.3232 0.5167 0.5386 0.0433  0.0757  -0.2102 325 SER D OG  
8523  N N   . ILE D 326 ? 0.2941 0.4604 0.4781 0.0544  0.0537  -0.1849 326 ILE D N   
8524  C CA  . ILE D 326 ? 0.2906 0.4527 0.4678 0.0595  0.0463  -0.1813 326 ILE D CA  
8525  C C   . ILE D 326 ? 0.3021 0.4750 0.4872 0.0653  0.0439  -0.1924 326 ILE D C   
8526  O O   . ILE D 326 ? 0.3075 0.4919 0.5050 0.0664  0.0414  -0.2029 326 ILE D O   
8527  C CB  . ILE D 326 ? 0.2802 0.4387 0.4556 0.0591  0.0383  -0.1774 326 ILE D CB  
8528  C CG1 . ILE D 326 ? 0.2697 0.4174 0.4373 0.0537  0.0411  -0.1667 326 ILE D CG1 
8529  C CG2 . ILE D 326 ? 0.2783 0.4332 0.4472 0.0643  0.0309  -0.1748 326 ILE D CG2 
8530  C CD1 . ILE D 326 ? 0.2608 0.4058 0.4274 0.0527  0.0347  -0.1637 326 ILE D CD1 
8531  N N   . PRO D 327 ? 0.2898 0.4598 0.4687 0.0693  0.0444  -0.1909 327 PRO D N   
8532  C CA  . PRO D 327 ? 0.3020 0.4817 0.4882 0.0755  0.0421  -0.2017 327 PRO D CA  
8533  C C   . PRO D 327 ? 0.3004 0.4841 0.4913 0.0798  0.0313  -0.2062 327 PRO D C   
8534  O O   . PRO D 327 ? 0.2914 0.4664 0.4735 0.0806  0.0251  -0.1984 327 PRO D O   
8535  C CB  . PRO D 327 ? 0.3049 0.4769 0.4801 0.0785  0.0441  -0.1964 327 PRO D CB  
8536  C CG  . PRO D 327 ? 0.2974 0.4584 0.4622 0.0733  0.0504  -0.1852 327 PRO D CG  
8537  C CD  . PRO D 327 ? 0.2853 0.4428 0.4503 0.0686  0.0476  -0.1798 327 PRO D CD  
8538  N N   . PRO D 328 ? 0.2959 0.4928 0.5005 0.0829  0.0288  -0.2191 328 PRO D N   
8539  C CA  . PRO D 328 ? 0.2962 0.4967 0.5051 0.0880  0.0178  -0.2241 328 PRO D CA  
8540  C C   . PRO D 328 ? 0.2987 0.4938 0.5000 0.0943  0.0117  -0.2221 328 PRO D C   
8541  O O   . PRO D 328 ? 0.2963 0.4895 0.4961 0.0979  0.0023  -0.2222 328 PRO D O   
8542  C CB  . PRO D 328 ? 0.3086 0.5253 0.5348 0.0906  0.0179  -0.2396 328 PRO D CB  
8543  C CG  . PRO D 328 ? 0.3104 0.5311 0.5412 0.0843  0.0289  -0.2408 328 PRO D CG  
8544  C CD  . PRO D 328 ? 0.3068 0.5160 0.5240 0.0816  0.0360  -0.2298 328 PRO D CD  
8545  N N   . GLU D 329 ? 0.3150 0.5070 0.5110 0.0959  0.0168  -0.2205 329 GLU D N   
8546  C CA  . GLU D 329 ? 0.3180 0.5039 0.5062 0.1017  0.0115  -0.2185 329 GLU D CA  
8547  C C   . GLU D 329 ? 0.3046 0.4767 0.4788 0.0994  0.0077  -0.2052 329 GLU D C   
8548  O O   . GLU D 329 ? 0.3060 0.4728 0.4739 0.1040  0.0018  -0.2034 329 GLU D O   
8549  C CB  . GLU D 329 ? 0.3279 0.5138 0.5137 0.1036  0.0188  -0.2202 329 GLU D CB  
8550  C CG  . GLU D 329 ? 0.3433 0.5433 0.5429 0.1064  0.0233  -0.2342 329 GLU D CG  
8551  C CD  . GLU D 329 ? 0.3431 0.5479 0.5475 0.0997  0.0337  -0.2349 329 GLU D CD  
8552  O OE1 . GLU D 329 ? 0.3307 0.5297 0.5309 0.0934  0.0351  -0.2265 329 GLU D OE1 
8553  O OE2 . GLU D 329 ? 0.3563 0.5707 0.5687 0.1009  0.0406  -0.2443 329 GLU D OE2 
8554  N N   . LEU D 330 ? 0.3182 0.4846 0.4877 0.0926  0.0112  -0.1963 330 LEU D N   
8555  C CA  . LEU D 330 ? 0.3059 0.4603 0.4634 0.0904  0.0080  -0.1845 330 LEU D CA  
8556  C C   . LEU D 330 ? 0.3043 0.4588 0.4620 0.0938  -0.0022 -0.1862 330 LEU D C   
8557  O O   . LEU D 330 ? 0.2989 0.4445 0.4468 0.0947  -0.0063 -0.1790 330 LEU D O   
8558  C CB  . LEU D 330 ? 0.2949 0.4441 0.4491 0.0829  0.0137  -0.1761 330 LEU D CB  
8559  C CG  . LEU D 330 ? 0.2941 0.4383 0.4432 0.0791  0.0231  -0.1703 330 LEU D CG  
8560  C CD1 . LEU D 330 ? 0.2818 0.4171 0.4242 0.0730  0.0259  -0.1597 330 LEU D CD1 
8561  C CD2 . LEU D 330 ? 0.2981 0.4366 0.4390 0.0825  0.0238  -0.1674 330 LEU D CD2 
8562  N N   . GLY D 331 ? 0.3074 0.4717 0.4761 0.0960  -0.0064 -0.1959 331 GLY D N   
8563  C CA  . GLY D 331 ? 0.3081 0.4727 0.4772 0.1003  -0.0166 -0.1987 331 GLY D CA  
8564  C C   . GLY D 331 ? 0.3167 0.4791 0.4824 0.1078  -0.0234 -0.2017 331 GLY D C   
8565  O O   . GLY D 331 ? 0.3170 0.4761 0.4793 0.1114  -0.0320 -0.2016 331 GLY D O   
8566  N N   . GLU D 332 ? 0.3330 0.4965 0.4991 0.1104  -0.0197 -0.2045 332 GLU D N   
8567  C CA  . GLU D 332 ? 0.3424 0.5031 0.5052 0.1177  -0.0257 -0.2076 332 GLU D CA  
8568  C C   . GLU D 332 ? 0.3350 0.4825 0.4831 0.1163  -0.0258 -0.1960 332 GLU D C   
8569  O O   . GLU D 332 ? 0.3425 0.4860 0.4864 0.1219  -0.0307 -0.1975 332 GLU D O   
8570  C CB  . GLU D 332 ? 0.3559 0.5242 0.5262 0.1216  -0.0214 -0.2168 332 GLU D CB  
8571  C CG  . GLU D 332 ? 0.3623 0.5443 0.5476 0.1211  -0.0180 -0.2275 332 GLU D CG  
8572  C CD  . GLU D 332 ? 0.3718 0.5621 0.5677 0.1277  -0.0277 -0.2391 332 GLU D CD  
8573  O OE1 . GLU D 332 ? 0.3758 0.5608 0.5670 0.1336  -0.0370 -0.2395 332 GLU D OE1 
8574  O OE2 . GLU D 332 ? 0.3760 0.5778 0.5849 0.1271  -0.0261 -0.2480 332 GLU D OE2 
8575  N N   . MET D 333 ? 0.3175 0.4582 0.4583 0.1091  -0.0208 -0.1850 333 MET D N   
8576  C CA  . MET D 333 ? 0.3096 0.4384 0.4375 0.1073  -0.0211 -0.1741 333 MET D CA  
8577  C C   . MET D 333 ? 0.3076 0.4322 0.4313 0.1096  -0.0299 -0.1725 333 MET D C   
8578  O O   . MET D 333 ? 0.2978 0.4197 0.4189 0.1053  -0.0297 -0.1668 333 MET D O   
8579  C CB  . MET D 333 ? 0.2970 0.4205 0.4198 0.0994  -0.0129 -0.1638 333 MET D CB  
8580  C CG  . MET D 333 ? 0.2998 0.4249 0.4240 0.0973  -0.0042 -0.1641 333 MET D CG  
8581  S SD  . MET D 333 ? 0.2869 0.4058 0.4062 0.0887  0.0046  -0.1532 333 MET D SD  
8582  C CE  . MET D 333 ? 0.2781 0.3982 0.4002 0.0855  0.0008  -0.1517 333 MET D CE  
8583  N N   . GLU D 334 ? 0.3220 0.4455 0.4448 0.1168  -0.0376 -0.1778 334 GLU D N   
8584  C CA  . GLU D 334 ? 0.3238 0.4437 0.4433 0.1204  -0.0468 -0.1784 334 GLU D CA  
8585  C C   . GLU D 334 ? 0.3119 0.4212 0.4198 0.1157  -0.0458 -0.1664 334 GLU D C   
8586  O O   . GLU D 334 ? 0.3076 0.4153 0.4136 0.1146  -0.0490 -0.1643 334 GLU D O   
8587  C CB  . GLU D 334 ? 0.3386 0.4569 0.4575 0.1292  -0.0550 -0.1854 334 GLU D CB  
8588  C CG  . GLU D 334 ? 0.3499 0.4749 0.4764 0.1331  -0.0526 -0.1939 334 GLU D CG  
8589  C CD  . GLU D 334 ? 0.3664 0.4897 0.4932 0.1426  -0.0617 -0.2020 334 GLU D CD  
8590  O OE1 . GLU D 334 ? 0.3675 0.4802 0.4841 0.1447  -0.0668 -0.1971 334 GLU D OE1 
8591  O OE2 . GLU D 334 ? 0.3791 0.5113 0.5166 0.1480  -0.0636 -0.2135 334 GLU D OE2 
8592  N N   . SER D 335 ? 0.2994 0.4018 0.3998 0.1130  -0.0412 -0.1590 335 SER D N   
8593  C CA  . SER D 335 ? 0.2897 0.3822 0.3797 0.1093  -0.0403 -0.1485 335 SER D CA  
8594  C C   . SER D 335 ? 0.2759 0.3675 0.3652 0.1013  -0.0328 -0.1406 335 SER D C   
8595  O O   . SER D 335 ? 0.2676 0.3516 0.3493 0.0977  -0.0309 -0.1320 335 SER D O   
8596  C CB  . SER D 335 ? 0.2910 0.3764 0.3739 0.1100  -0.0391 -0.1444 335 SER D CB  
8597  O OG  . SER D 335 ? 0.3049 0.3897 0.3878 0.1177  -0.0463 -0.1515 335 SER D OG  
8598  N N   . MET D 336 ? 0.2687 0.3676 0.3658 0.0985  -0.0284 -0.1437 336 MET D N   
8599  C CA  . MET D 336 ? 0.2572 0.3543 0.3534 0.0912  -0.0210 -0.1365 336 MET D CA  
8600  C C   . MET D 336 ? 0.2499 0.3429 0.3421 0.0888  -0.0227 -0.1313 336 MET D C   
8601  O O   . MET D 336 ? 0.2534 0.3501 0.3488 0.0915  -0.0282 -0.1363 336 MET D O   
8602  C CB  . MET D 336 ? 0.2588 0.3645 0.3646 0.0894  -0.0169 -0.1419 336 MET D CB  
8603  C CG  . MET D 336 ? 0.2487 0.3519 0.3537 0.0824  -0.0096 -0.1351 336 MET D CG  
8604  S SD  . MET D 336 ? 0.2408 0.3336 0.3361 0.0781  -0.0031 -0.1238 336 MET D SD  
8605  C CE  . MET D 336 ? 0.2503 0.3453 0.3465 0.0820  -0.0017 -0.1284 336 MET D CE  
8606  N N   . ILE D 337 ? 0.2532 0.3386 0.3386 0.0839  -0.0179 -0.1217 337 ILE D N   
8607  C CA  . ILE D 337 ? 0.2463 0.3269 0.3273 0.0813  -0.0180 -0.1159 337 ILE D CA  
8608  C C   . ILE D 337 ? 0.2372 0.3164 0.3190 0.0749  -0.0109 -0.1103 337 ILE D C   
8609  O O   . ILE D 337 ? 0.2341 0.3144 0.3175 0.0731  -0.0109 -0.1100 337 ILE D O   
8610  C CB  . ILE D 337 ? 0.2447 0.3166 0.3167 0.0819  -0.0191 -0.1099 337 ILE D CB  
8611  C CG1 . ILE D 337 ? 0.2545 0.3264 0.3247 0.0887  -0.0276 -0.1154 337 ILE D CG1 
8612  C CG2 . ILE D 337 ? 0.2361 0.3022 0.3035 0.0776  -0.0157 -0.1021 337 ILE D CG2 
8613  C CD1 . ILE D 337 ? 0.2555 0.3190 0.3175 0.0900  -0.0290 -0.1108 337 ILE D CD1 
8614  N N   . ASP D 338 ? 0.2454 0.3219 0.3260 0.0718  -0.0050 -0.1061 338 ASP D N   
8615  C CA  . ASP D 338 ? 0.2380 0.3118 0.3186 0.0663  0.0016  -0.1005 338 ASP D CA  
8616  C C   . ASP D 338 ? 0.2410 0.3192 0.3269 0.0654  0.0054  -0.1039 338 ASP D C   
8617  O O   . ASP D 338 ? 0.2423 0.3181 0.3257 0.0656  0.0082  -0.1021 338 ASP D O   
8618  C CB  . ASP D 338 ? 0.2317 0.2966 0.3049 0.0636  0.0051  -0.0915 338 ASP D CB  
8619  C CG  . ASP D 338 ? 0.2255 0.2868 0.2984 0.0587  0.0114  -0.0859 338 ASP D CG  
8620  O OD1 . ASP D 338 ? 0.2248 0.2895 0.3023 0.0570  0.0125  -0.0880 338 ASP D OD1 
8621  O OD2 . ASP D 338 ? 0.2217 0.2770 0.2901 0.0568  0.0149  -0.0797 338 ASP D OD2 
8622  N N   . LEU D 339 ? 0.2307 0.3151 0.3237 0.0646  0.0058  -0.1089 339 LEU D N   
8623  C CA  . LEU D 339 ? 0.2349 0.3245 0.3340 0.0639  0.0097  -0.1133 339 LEU D CA  
8624  C C   . LEU D 339 ? 0.2295 0.3163 0.3293 0.0588  0.0154  -0.1090 339 LEU D C   
8625  O O   . LEU D 339 ? 0.2271 0.3159 0.3302 0.0570  0.0146  -0.1102 339 LEU D O   
8626  C CB  . LEU D 339 ? 0.2428 0.3427 0.3510 0.0673  0.0057  -0.1240 339 LEU D CB  
8627  C CG  . LEU D 339 ? 0.2483 0.3548 0.3642 0.0665  0.0104  -0.1298 339 LEU D CG  
8628  C CD1 . LEU D 339 ? 0.2519 0.3558 0.3644 0.0675  0.0145  -0.1282 339 LEU D CD1 
8629  C CD2 . LEU D 339 ? 0.2566 0.3741 0.3826 0.0702  0.0060  -0.1412 339 LEU D CD2 
8630  N N   . GLU D 340 ? 0.2368 0.3189 0.3333 0.0568  0.0210  -0.1043 340 GLU D N   
8631  C CA  . GLU D 340 ? 0.2325 0.3107 0.3286 0.0525  0.0263  -0.0996 340 GLU D CA  
8632  C C   . GLU D 340 ? 0.2375 0.3170 0.3355 0.0520  0.0317  -0.1012 340 GLU D C   
8633  O O   . GLU D 340 ? 0.2390 0.3148 0.3321 0.0533  0.0338  -0.0982 340 GLU D O   
8634  C CB  . GLU D 340 ? 0.2253 0.2941 0.3133 0.0505  0.0278  -0.0902 340 GLU D CB  
8635  C CG  . GLU D 340 ? 0.2222 0.2886 0.3062 0.0519  0.0232  -0.0880 340 GLU D CG  
8636  C CD  . GLU D 340 ? 0.2153 0.2740 0.2938 0.0492  0.0253  -0.0800 340 GLU D CD  
8637  O OE1 . GLU D 340 ? 0.2133 0.2676 0.2897 0.0471  0.0297  -0.0754 340 GLU D OE1 
8638  O OE2 . GLU D 340 ? 0.2128 0.2699 0.2891 0.0496  0.0226  -0.0785 340 GLU D OE2 
8639  N N   . ILE D 341 ? 0.2091 0.2939 0.3143 0.0502  0.0341  -0.1062 341 ILE D N   
8640  C CA  . ILE D 341 ? 0.2144 0.3003 0.3216 0.0493  0.0401  -0.1077 341 ILE D CA  
8641  C C   . ILE D 341 ? 0.2114 0.2947 0.3204 0.0449  0.0441  -0.1052 341 ILE D C   
8642  O O   . ILE D 341 ? 0.2166 0.3033 0.3305 0.0433  0.0486  -0.1091 341 ILE D O   
8643  C CB  . ILE D 341 ? 0.2238 0.3200 0.3394 0.0517  0.0401  -0.1180 341 ILE D CB  
8644  C CG1 . ILE D 341 ? 0.2241 0.3284 0.3479 0.0521  0.0350  -0.1251 341 ILE D CG1 
8645  C CG2 . ILE D 341 ? 0.2287 0.3256 0.3410 0.0561  0.0384  -0.1195 341 ILE D CG2 
8646  C CD1 . ILE D 341 ? 0.2337 0.3492 0.3680 0.0536  0.0359  -0.1361 341 ILE D CD1 
8647  N N   . SER D 342 ? 0.2603 0.3376 0.3654 0.0428  0.0427  -0.0991 342 SER D N   
8648  C CA  . SER D 342 ? 0.2574 0.3320 0.3644 0.0388  0.0458  -0.0970 342 SER D CA  
8649  C C   . SER D 342 ? 0.2591 0.3281 0.3624 0.0375  0.0516  -0.0926 342 SER D C   
8650  O O   . SER D 342 ? 0.2617 0.3285 0.3601 0.0398  0.0532  -0.0905 342 SER D O   
8651  C CB  . SER D 342 ? 0.2499 0.3190 0.3529 0.0376  0.0432  -0.0913 342 SER D CB  
8652  O OG  . SER D 342 ? 0.2496 0.3230 0.3545 0.0392  0.0377  -0.0947 342 SER D OG  
8653  N N   . GLU D 343 ? 0.2716 0.3384 0.3773 0.0340  0.0547  -0.0916 343 GLU D N   
8654  C CA  . GLU D 343 ? 0.2728 0.3335 0.3751 0.0325  0.0598  -0.0871 343 GLU D CA  
8655  C C   . GLU D 343 ? 0.2829 0.3463 0.3850 0.0342  0.0637  -0.0901 343 GLU D C   
8656  O O   . GLU D 343 ? 0.2842 0.3431 0.3792 0.0365  0.0651  -0.0857 343 GLU D O   
8657  C CB  . GLU D 343 ? 0.2667 0.3191 0.3606 0.0331  0.0587  -0.0785 343 GLU D CB  
8658  C CG  . GLU D 343 ? 0.2647 0.3138 0.3592 0.0305  0.0570  -0.0756 343 GLU D CG  
8659  C CD  . GLU D 343 ? 0.2574 0.3012 0.3450 0.0318  0.0543  -0.0691 343 GLU D CD  
8660  O OE1 . GLU D 343 ? 0.2550 0.2930 0.3383 0.0315  0.0562  -0.0638 343 GLU D OE1 
8661  O OE2 . GLU D 343 ? 0.2584 0.3041 0.3453 0.0332  0.0504  -0.0697 343 GLU D OE2 
8662  N N   . ASN D 344 ? 0.2764 0.3475 0.3865 0.0333  0.0656  -0.0982 344 ASN D N   
8663  C CA  . ASN D 344 ? 0.2856 0.3609 0.3970 0.0347  0.0700  -0.1027 344 ASN D CA  
8664  C C   . ASN D 344 ? 0.2915 0.3720 0.4117 0.0310  0.0747  -0.1093 344 ASN D C   
8665  O O   . ASN D 344 ? 0.2879 0.3669 0.4118 0.0274  0.0747  -0.1090 344 ASN D O   
8666  C CB  . ASN D 344 ? 0.2889 0.3709 0.4018 0.0387  0.0666  -0.1077 344 ASN D CB  
8667  C CG  . ASN D 344 ? 0.2883 0.3649 0.3917 0.0425  0.0656  -0.1022 344 ASN D CG  
8668  O OD1 . ASN D 344 ? 0.2944 0.3694 0.3938 0.0439  0.0700  -0.1016 344 ASN D OD1 
8669  N ND2 . ASN D 344 ? 0.2815 0.3554 0.3813 0.0440  0.0599  -0.0986 344 ASN D ND2 
8670  N N   . LYS D 345 ? 0.2981 0.3847 0.4217 0.0317  0.0791  -0.1156 345 LYS D N   
8671  C CA  . LYS D 345 ? 0.3054 0.3981 0.4379 0.0279  0.0844  -0.1230 345 LYS D CA  
8672  C C   . LYS D 345 ? 0.3119 0.4173 0.4542 0.0293  0.0833  -0.1338 345 LYS D C   
8673  O O   . LYS D 345 ? 0.3220 0.4343 0.4703 0.0279  0.0890  -0.1412 345 LYS D O   
8674  C CB  . LYS D 345 ? 0.3134 0.4022 0.4417 0.0266  0.0924  -0.1216 345 LYS D CB  
8675  C CG  . LYS D 345 ? 0.3081 0.3852 0.4288 0.0248  0.0937  -0.1123 345 LYS D CG  
8676  C CD  . LYS D 345 ? 0.3170 0.3901 0.4323 0.0242  0.1012  -0.1109 345 LYS D CD  
8677  C CE  . LYS D 345 ? 0.3117 0.3732 0.4191 0.0235  0.1015  -0.1016 345 LYS D CE  
8678  N NZ  . LYS D 345 ? 0.3203 0.3775 0.4205 0.0241  0.1077  -0.0996 345 LYS D NZ  
8679  N N   . LEU D 346 ? 0.2876 0.3965 0.4317 0.0320  0.0759  -0.1352 346 LEU D N   
8680  C CA  . LEU D 346 ? 0.2935 0.4148 0.4474 0.0341  0.0736  -0.1458 346 LEU D CA  
8681  C C   . LEU D 346 ? 0.2955 0.4247 0.4613 0.0302  0.0744  -0.1537 346 LEU D C   
8682  O O   . LEU D 346 ? 0.2895 0.4140 0.4555 0.0265  0.0741  -0.1504 346 LEU D O   
8683  C CB  . LEU D 346 ? 0.2876 0.4097 0.4396 0.0382  0.0650  -0.1448 346 LEU D CB  
8684  C CG  . LEU D 346 ? 0.2853 0.4000 0.4262 0.0420  0.0633  -0.1376 346 LEU D CG  
8685  C CD1 . LEU D 346 ? 0.2806 0.3965 0.4206 0.0455  0.0550  -0.1377 346 LEU D CD1 
8686  C CD2 . LEU D 346 ? 0.2959 0.4138 0.4360 0.0445  0.0684  -0.1413 346 LEU D CD2 
8687  N N   . THR D 347 ? 0.3004 0.4420 0.4765 0.0312  0.0756  -0.1648 347 THR D N   
8688  C CA  . THR D 347 ? 0.3041 0.4552 0.4930 0.0278  0.0768  -0.1741 347 THR D CA  
8689  C C   . THR D 347 ? 0.3082 0.4722 0.5072 0.0317  0.0711  -0.1846 347 THR D C   
8690  O O   . THR D 347 ? 0.3093 0.4746 0.5051 0.0369  0.0671  -0.1847 347 THR D O   
8691  C CB  . THR D 347 ? 0.3146 0.4691 0.5079 0.0237  0.0868  -0.1789 347 THR D CB  
8692  O OG1 . THR D 347 ? 0.3252 0.4861 0.5192 0.0269  0.0905  -0.1841 347 THR D OG1 
8693  C CG2 . THR D 347 ? 0.3116 0.4529 0.4950 0.0202  0.0921  -0.1690 347 THR D CG2 
8694  N N   . GLY D 348 ? 0.3372 0.5108 0.5485 0.0294  0.0705  -0.1937 348 GLY D N   
8695  C CA  . GLY D 348 ? 0.3428 0.5299 0.5655 0.0332  0.0654  -0.2052 348 GLY D CA  
8696  C C   . GLY D 348 ? 0.3345 0.5205 0.5556 0.0367  0.0548  -0.2035 348 GLY D C   
8697  O O   . GLY D 348 ? 0.3242 0.4990 0.5352 0.0359  0.0518  -0.1932 348 GLY D O   
8698  N N   . PRO D 349 ? 0.3106 0.5084 0.5417 0.0410  0.0491  -0.2140 349 PRO D N   
8699  C CA  . PRO D 349 ? 0.3045 0.5022 0.5348 0.0445  0.0388  -0.2137 349 PRO D CA  
8700  C C   . PRO D 349 ? 0.3015 0.4928 0.5212 0.0499  0.0336  -0.2074 349 PRO D C   
8701  O O   . PRO D 349 ? 0.3061 0.4961 0.5218 0.0521  0.0369  -0.2061 349 PRO D O   
8702  C CB  . PRO D 349 ? 0.3137 0.5273 0.5601 0.0473  0.0352  -0.2288 349 PRO D CB  
8703  C CG  . PRO D 349 ? 0.3254 0.5468 0.5777 0.0484  0.0421  -0.2357 349 PRO D CG  
8704  C CD  . PRO D 349 ? 0.3238 0.5361 0.5679 0.0429  0.0521  -0.2272 349 PRO D CD  
8705  N N   . VAL D 350 ? 0.3099 0.4970 0.5249 0.0518  0.0256  -0.2036 350 VAL D N   
8706  C CA  . VAL D 350 ? 0.3080 0.4901 0.5142 0.0572  0.0195  -0.1991 350 VAL D CA  
8707  C C   . VAL D 350 ? 0.3183 0.5120 0.5339 0.0637  0.0138  -0.2110 350 VAL D C   
8708  O O   . VAL D 350 ? 0.3224 0.5259 0.5493 0.0648  0.0098  -0.2208 350 VAL D O   
8709  C CB  . VAL D 350 ? 0.2980 0.4719 0.4958 0.0569  0.0136  -0.1914 350 VAL D CB  
8710  C CG1 . VAL D 350 ? 0.2976 0.4674 0.4874 0.0626  0.0069  -0.1883 350 VAL D CG1 
8711  C CG2 . VAL D 350 ? 0.2889 0.4510 0.4773 0.0511  0.0194  -0.1798 350 VAL D CG2 
8712  N N   . PRO D 351 ? 0.2944 0.4874 0.5063 0.0684  0.0131  -0.2111 351 PRO D N   
8713  C CA  . PRO D 351 ? 0.3055 0.5093 0.5268 0.0752  0.0074  -0.2229 351 PRO D CA  
8714  C C   . PRO D 351 ? 0.3041 0.5082 0.5252 0.0798  -0.0037 -0.2251 351 PRO D C   
8715  O O   . PRO D 351 ? 0.2951 0.4890 0.5049 0.0792  -0.0074 -0.2155 351 PRO D O   
8716  C CB  . PRO D 351 ? 0.3098 0.5095 0.5240 0.0787  0.0095  -0.2199 351 PRO D CB  
8717  C CG  . PRO D 351 ? 0.3034 0.4937 0.5084 0.0729  0.0185  -0.2094 351 PRO D CG  
8718  C CD  . PRO D 351 ? 0.2916 0.4745 0.4916 0.0677  0.0179  -0.2013 351 PRO D CD  
8719  N N   . ASP D 352 ? 0.3687 0.5849 0.6028 0.0847  -0.0091 -0.2382 352 ASP D N   
8720  C CA  . ASP D 352 ? 0.3706 0.5875 0.6048 0.0907  -0.0206 -0.2419 352 ASP D CA  
8721  C C   . ASP D 352 ? 0.3713 0.5797 0.5942 0.0960  -0.0258 -0.2364 352 ASP D C   
8722  O O   . ASP D 352 ? 0.3698 0.5736 0.5871 0.0996  -0.0345 -0.2346 352 ASP D O   
8723  C CB  . ASP D 352 ? 0.3836 0.6154 0.6348 0.0959  -0.0255 -0.2582 352 ASP D CB  
8724  C CG  . ASP D 352 ? 0.3848 0.6265 0.6490 0.0907  -0.0198 -0.2653 352 ASP D CG  
8725  O OD1 . ASP D 352 ? 0.3838 0.6259 0.6488 0.0852  -0.0094 -0.2629 352 ASP D OD1 
8726  O OD2 . ASP D 352 ? 0.3876 0.6364 0.6612 0.0923  -0.0259 -0.2735 352 ASP D OD2 
8727  N N   . SER D 353 ? 0.3201 0.5260 0.5391 0.0966  -0.0205 -0.2339 353 SER D N   
8728  C CA  . SER D 353 ? 0.3223 0.5209 0.5316 0.1019  -0.0251 -0.2299 353 SER D CA  
8729  C C   . SER D 353 ? 0.3101 0.4948 0.5039 0.0992  -0.0267 -0.2162 353 SER D C   
8730  O O   . SER D 353 ? 0.3118 0.4900 0.4974 0.1037  -0.0321 -0.2132 353 SER D O   
8731  C CB  . SER D 353 ? 0.3278 0.5267 0.5364 0.1024  -0.0178 -0.2300 353 SER D CB  
8732  O OG  . SER D 353 ? 0.3208 0.5167 0.5265 0.0949  -0.0074 -0.2232 353 SER D OG  
8733  N N   . PHE D 354 ? 0.3190 0.4990 0.5088 0.0922  -0.0220 -0.2083 354 PHE D N   
8734  C CA  . PHE D 354 ? 0.3082 0.4759 0.4843 0.0897  -0.0231 -0.1961 354 PHE D CA  
8735  C C   . PHE D 354 ? 0.3097 0.4756 0.4828 0.0946  -0.0333 -0.1976 354 PHE D C   
8736  O O   . PHE D 354 ? 0.3036 0.4595 0.4650 0.0943  -0.0352 -0.1886 354 PHE D O   
8737  C CB  . PHE D 354 ? 0.2977 0.4617 0.4719 0.0819  -0.0165 -0.1890 354 PHE D CB  
8738  C CG  . PHE D 354 ? 0.2933 0.4516 0.4625 0.0771  -0.0071 -0.1815 354 PHE D CG  
8739  C CD1 . PHE D 354 ? 0.3008 0.4631 0.4737 0.0786  -0.0028 -0.1856 354 PHE D CD1 
8740  C CD2 . PHE D 354 ? 0.2827 0.4315 0.4435 0.0715  -0.0027 -0.1706 354 PHE D CD2 
8741  C CE1 . PHE D 354 ? 0.2978 0.4543 0.4652 0.0746  0.0055  -0.1788 354 PHE D CE1 
8742  C CE2 . PHE D 354 ? 0.2797 0.4227 0.4357 0.0677  0.0053  -0.1639 354 PHE D CE2 
8743  C CZ  . PHE D 354 ? 0.2872 0.4339 0.4462 0.0693  0.0092  -0.1679 354 PHE D CZ  
8744  N N   . GLY D 355 ? 0.3071 0.4825 0.4908 0.0991  -0.0399 -0.2091 355 GLY D N   
8745  C CA  . GLY D 355 ? 0.3115 0.4848 0.4921 0.1051  -0.0506 -0.2116 355 GLY D CA  
8746  C C   . GLY D 355 ? 0.3182 0.4859 0.4917 0.1114  -0.0557 -0.2108 355 GLY D C   
8747  O O   . GLY D 355 ? 0.3193 0.4801 0.4846 0.1151  -0.0630 -0.2081 355 GLY D O   
8748  N N   . LYS D 356 ? 0.2999 0.4700 0.4761 0.1127  -0.0518 -0.2132 356 LYS D N   
8749  C CA  . LYS D 356 ? 0.3072 0.4718 0.4771 0.1188  -0.0563 -0.2130 356 LYS D CA  
8750  C C   . LYS D 356 ? 0.2975 0.4491 0.4522 0.1155  -0.0534 -0.1995 356 LYS D C   
8751  O O   . LYS D 356 ? 0.3028 0.4481 0.4505 0.1203  -0.0582 -0.1983 356 LYS D O   
8752  C CB  . LYS D 356 ? 0.3165 0.4882 0.4944 0.1213  -0.0525 -0.2203 356 LYS D CB  
8753  C CG  . LYS D 356 ? 0.3293 0.5144 0.5233 0.1263  -0.0562 -0.2354 356 LYS D CG  
8754  C CD  . LYS D 356 ? 0.3395 0.5310 0.5404 0.1292  -0.0515 -0.2422 356 LYS D CD  
8755  C CE  . LYS D 356 ? 0.3557 0.5590 0.5715 0.1370  -0.0579 -0.2581 356 LYS D CE  
8756  N NZ  . LYS D 356 ? 0.3676 0.5758 0.5886 0.1413  -0.0542 -0.2648 356 LYS D NZ  
8757  N N   . LEU D 357 ? 0.3145 0.4618 0.4642 0.1076  -0.0459 -0.1899 357 LEU D N   
8758  C CA  . LEU D 357 ? 0.3051 0.4404 0.4414 0.1042  -0.0430 -0.1774 357 LEU D CA  
8759  C C   . LEU D 357 ? 0.3034 0.4328 0.4326 0.1060  -0.0498 -0.1742 357 LEU D C   
8760  O O   . LEU D 357 ? 0.2951 0.4225 0.4221 0.1017  -0.0478 -0.1694 357 LEU D O   
8761  C CB  . LEU D 357 ? 0.2935 0.4264 0.4280 0.0960  -0.0330 -0.1692 357 LEU D CB  
8762  C CG  . LEU D 357 ? 0.2959 0.4349 0.4377 0.0937  -0.0257 -0.1727 357 LEU D CG  
8763  C CD1 . LEU D 357 ? 0.2855 0.4212 0.4255 0.0859  -0.0172 -0.1651 357 LEU D CD1 
8764  C CD2 . LEU D 357 ? 0.3012 0.4375 0.4394 0.0967  -0.0243 -0.1723 357 LEU D CD2 
8765  N N   . THR D 358 ? 0.3094 0.4353 0.4346 0.1129  -0.0579 -0.1772 358 THR D N   
8766  C CA  . THR D 358 ? 0.3112 0.4315 0.4298 0.1160  -0.0654 -0.1758 358 THR D CA  
8767  C C   . THR D 358 ? 0.3017 0.4105 0.4072 0.1121  -0.0619 -0.1634 358 THR D C   
8768  O O   . THR D 358 ? 0.3015 0.4052 0.4010 0.1133  -0.0659 -0.1608 358 THR D O   
8769  C CB  . THR D 358 ? 0.3267 0.4461 0.4454 0.1254  -0.0761 -0.1839 358 THR D CB  
8770  O OG1 . THR D 358 ? 0.3305 0.4460 0.4457 0.1273  -0.0748 -0.1826 358 THR D OG1 
8771  C CG2 . THR D 358 ? 0.3371 0.4682 0.4697 0.1301  -0.0812 -0.1973 358 THR D CG2 
8772  N N   . ALA D 359 ? 0.2947 0.3993 0.3961 0.1077  -0.0544 -0.1561 359 ALA D N   
8773  C CA  . ALA D 359 ? 0.2861 0.3804 0.3765 0.1038  -0.0506 -0.1449 359 ALA D CA  
8774  C C   . ALA D 359 ? 0.2732 0.3668 0.3636 0.0956  -0.0408 -0.1373 359 ALA D C   
8775  O O   . ALA D 359 ? 0.2659 0.3518 0.3489 0.0919  -0.0360 -0.1284 359 ALA D O   
8776  C CB  . ALA D 359 ? 0.2899 0.3780 0.3741 0.1063  -0.0513 -0.1425 359 ALA D CB  
8777  N N   . LEU D 360 ? 0.2687 0.3700 0.3678 0.0929  -0.0380 -0.1411 360 LEU D N   
8778  C CA  . LEU D 360 ? 0.2584 0.3584 0.3578 0.0856  -0.0292 -0.1347 360 LEU D CA  
8779  C C   . LEU D 360 ? 0.2507 0.3445 0.3440 0.0823  -0.0275 -0.1273 360 LEU D C   
8780  O O   . LEU D 360 ? 0.2532 0.3481 0.3463 0.0848  -0.0324 -0.1299 360 LEU D O   
8781  C CB  . LEU D 360 ? 0.2598 0.3692 0.3701 0.0840  -0.0272 -0.1414 360 LEU D CB  
8782  C CG  . LEU D 360 ? 0.2522 0.3605 0.3639 0.0773  -0.0182 -0.1364 360 LEU D CG  
8783  C CD1 . LEU D 360 ? 0.2518 0.3564 0.3601 0.0765  -0.0136 -0.1326 360 LEU D CD1 
8784  C CD2 . LEU D 360 ? 0.2550 0.3728 0.3779 0.0761  -0.0169 -0.1442 360 LEU D CD2 
8785  N N   . GLU D 361 ? 0.2771 0.3643 0.3653 0.0771  -0.0205 -0.1183 361 GLU D N   
8786  C CA  . GLU D 361 ? 0.2700 0.3511 0.3529 0.0737  -0.0174 -0.1110 361 GLU D CA  
8787  C C   . GLU D 361 ? 0.2626 0.3428 0.3477 0.0676  -0.0100 -0.1066 361 GLU D C   
8788  O O   . GLU D 361 ? 0.2589 0.3378 0.3438 0.0653  -0.0084 -0.1043 361 GLU D O   
8789  C CB  . GLU D 361 ? 0.2680 0.3402 0.3417 0.0739  -0.0164 -0.1039 361 GLU D CB  
8790  C CG  . GLU D 361 ? 0.2761 0.3471 0.3461 0.0801  -0.0239 -0.1074 361 GLU D CG  
8791  C CD  . GLU D 361 ? 0.2744 0.3361 0.3356 0.0798  -0.0223 -0.1002 361 GLU D CD  
8792  O OE1 . GLU D 361 ? 0.2665 0.3233 0.3247 0.0751  -0.0160 -0.0929 361 GLU D OE1 
8793  O OE2 . GLU D 361 ? 0.2811 0.3403 0.3386 0.0844  -0.0274 -0.1023 361 GLU D OE2 
8794  N N   . TRP D 362 ? 0.2664 0.3467 0.3534 0.0653  -0.0055 -0.1055 362 TRP D N   
8795  C CA  . TRP D 362 ? 0.2613 0.3404 0.3505 0.0602  0.0010  -0.1022 362 TRP D CA  
8796  C C   . TRP D 362 ? 0.2657 0.3522 0.3629 0.0604  0.0019  -0.1089 362 TRP D C   
8797  O O   . TRP D 362 ? 0.2698 0.3578 0.3675 0.0625  0.0017  -0.1111 362 TRP D O   
8798  C CB  . TRP D 362 ? 0.2561 0.3269 0.3390 0.0573  0.0064  -0.0936 362 TRP D CB  
8799  C CG  . TRP D 362 ? 0.2517 0.3153 0.3278 0.0564  0.0072  -0.0868 362 TRP D CG  
8800  C CD1 . TRP D 362 ? 0.2502 0.3098 0.3247 0.0533  0.0108  -0.0820 362 TRP D CD1 
8801  C CD2 . TRP D 362 ? 0.2544 0.3138 0.3246 0.0588  0.0049  -0.0843 362 TRP D CD2 
8802  N NE1 . TRP D 362 ? 0.2491 0.3026 0.3175 0.0536  0.0112  -0.0768 362 TRP D NE1 
8803  C CE2 . TRP D 362 ? 0.2480 0.3012 0.3137 0.0567  0.0078  -0.0780 362 TRP D CE2 
8804  C CE3 . TRP D 362 ? 0.2594 0.3197 0.3280 0.0626  0.0009  -0.0871 362 TRP D CE3 
8805  C CZ2 . TRP D 362 ? 0.2480 0.2959 0.3079 0.0581  0.0072  -0.0744 362 TRP D CZ2 
8806  C CZ3 . TRP D 362 ? 0.2572 0.3118 0.3196 0.0639  -0.0003 -0.0834 362 TRP D CZ3 
8807  C CH2 . TRP D 362 ? 0.2524 0.3010 0.3107 0.0615  0.0030  -0.0771 362 TRP D CH2 
8808  N N   . LEU D 363 ? 0.2351 0.3262 0.3387 0.0582  0.0031  -0.1124 363 LEU D N   
8809  C CA  . LEU D 363 ? 0.2391 0.3369 0.3509 0.0573  0.0055  -0.1184 363 LEU D CA  
8810  C C   . LEU D 363 ? 0.2343 0.3281 0.3463 0.0520  0.0121  -0.1137 363 LEU D C   
8811  O O   . LEU D 363 ? 0.2319 0.3265 0.3466 0.0498  0.0122  -0.1141 363 LEU D O   
8812  C CB  . LEU D 363 ? 0.2451 0.3531 0.3661 0.0600  0.0005  -0.1287 363 LEU D CB  
8813  C CG  . LEU D 363 ? 0.2500 0.3658 0.3807 0.0588  0.0037  -0.1358 363 LEU D CG  
8814  C CD1 . LEU D 363 ? 0.2551 0.3717 0.3855 0.0610  0.0056  -0.1372 363 LEU D CD1 
8815  C CD2 . LEU D 363 ? 0.2558 0.3820 0.3966 0.0613  -0.0014 -0.1464 363 LEU D CD2 
8816  N N   . PHE D 364 ? 0.2314 0.3209 0.3405 0.0504  0.0172  -0.1094 364 PHE D N   
8817  C CA  . PHE D 364 ? 0.2280 0.3128 0.3364 0.0460  0.0232  -0.1046 364 PHE D CA  
8818  C C   . PHE D 364 ? 0.2335 0.3241 0.3493 0.0451  0.0266  -0.1105 364 PHE D C   
8819  O O   . PHE D 364 ? 0.2373 0.3281 0.3523 0.0464  0.0290  -0.1110 364 PHE D O   
8820  C CB  . PHE D 364 ? 0.2241 0.2996 0.3238 0.0452  0.0264  -0.0957 364 PHE D CB  
8821  C CG  . PHE D 364 ? 0.2179 0.2865 0.3118 0.0438  0.0262  -0.0889 364 PHE D CG  
8822  C CD1 . PHE D 364 ? 0.2166 0.2841 0.3066 0.0461  0.0221  -0.0878 364 PHE D CD1 
8823  C CD2 . PHE D 364 ? 0.2142 0.2775 0.3066 0.0404  0.0304  -0.0838 364 PHE D CD2 
8824  C CE1 . PHE D 364 ? 0.2118 0.2733 0.2968 0.0448  0.0228  -0.0817 364 PHE D CE1 
8825  C CE2 . PHE D 364 ? 0.2095 0.2671 0.2971 0.0394  0.0306  -0.0781 364 PHE D CE2 
8826  C CZ  . PHE D 364 ? 0.2084 0.2651 0.2923 0.0415  0.0271  -0.0770 364 PHE D CZ  
8827  N N   . LEU D 365 ? 0.2396 0.3351 0.3629 0.0428  0.0272  -0.1153 365 LEU D N   
8828  C CA  . LEU D 365 ? 0.2451 0.3464 0.3762 0.0412  0.0312  -0.1213 365 LEU D CA  
8829  C C   . LEU D 365 ? 0.2425 0.3393 0.3743 0.0364  0.0365  -0.1179 365 LEU D C   
8830  O O   . LEU D 365 ? 0.2472 0.3481 0.3856 0.0343  0.0404  -0.1227 365 LEU D O   
8831  C CB  . LEU D 365 ? 0.2506 0.3633 0.3921 0.0429  0.0273  -0.1322 365 LEU D CB  
8832  C CG  . LEU D 365 ? 0.2557 0.3746 0.3988 0.0482  0.0219  -0.1379 365 LEU D CG  
8833  C CD1 . LEU D 365 ? 0.2617 0.3925 0.4164 0.0498  0.0182  -0.1493 365 LEU D CD1 
8834  C CD2 . LEU D 365 ? 0.2605 0.3790 0.4016 0.0500  0.0253  -0.1377 365 LEU D CD2 
8835  N N   . ARG D 366 ? 0.2399 0.3283 0.3652 0.0347  0.0368  -0.1101 366 ARG D N   
8836  C CA  . ARG D 366 ? 0.2377 0.3219 0.3641 0.0304  0.0409  -0.1074 366 ARG D CA  
8837  C C   . ARG D 366 ? 0.2404 0.3206 0.3654 0.0288  0.0471  -0.1048 366 ARG D C   
8838  O O   . ARG D 366 ? 0.2427 0.3216 0.3635 0.0311  0.0483  -0.1031 366 ARG D O   
8839  C CB  . ARG D 366 ? 0.2311 0.3075 0.3507 0.0296  0.0399  -0.0999 366 ARG D CB  
8840  C CG  . ARG D 366 ? 0.2281 0.2981 0.3384 0.0319  0.0393  -0.0927 366 ARG D CG  
8841  C CD  . ARG D 366 ? 0.2226 0.2849 0.3271 0.0305  0.0398  -0.0855 366 ARG D CD  
8842  N NE  . ARG D 366 ? 0.2221 0.2818 0.3296 0.0269  0.0434  -0.0847 366 ARG D NE  
8843  C CZ  . ARG D 366 ? 0.2230 0.2782 0.3297 0.0250  0.0479  -0.0818 366 ARG D CZ  
8844  N NH1 . ARG D 366 ? 0.2244 0.2772 0.3269 0.0266  0.0494  -0.0791 366 ARG D NH1 
8845  N NH2 . ARG D 366 ? 0.2231 0.2760 0.3332 0.0217  0.0508  -0.0817 366 ARG D NH2 
8846  N N   . ASP D 367 ? 0.2597 0.3377 0.3879 0.0250  0.0510  -0.1047 367 ASP D N   
8847  C CA  . ASP D 367 ? 0.2624 0.3355 0.3889 0.0231  0.0571  -0.1018 367 ASP D CA  
8848  C C   . ASP D 367 ? 0.2717 0.3505 0.4013 0.0244  0.0599  -0.1071 367 ASP D C   
8849  O O   . ASP D 367 ? 0.2719 0.3474 0.3956 0.0265  0.0618  -0.1036 367 ASP D O   
8850  C CB  . ASP D 367 ? 0.2581 0.3215 0.3746 0.0240  0.0577  -0.0923 367 ASP D CB  
8851  C CG  . ASP D 367 ? 0.2596 0.3165 0.3749 0.0213  0.0632  -0.0886 367 ASP D CG  
8852  O OD1 . ASP D 367 ? 0.2653 0.3249 0.3859 0.0193  0.0674  -0.0931 367 ASP D OD1 
8853  O OD2 . ASP D 367 ? 0.2639 0.3132 0.3732 0.0211  0.0634  -0.0816 367 ASP D OD2 
8854  N N   . ASN D 368 ? 0.2773 0.3652 0.4167 0.0233  0.0602  -0.1161 368 ASN D N   
8855  C CA  . ASN D 368 ? 0.2859 0.3808 0.4300 0.0242  0.0635  -0.1227 368 ASN D CA  
8856  C C   . ASN D 368 ? 0.2911 0.3927 0.4460 0.0204  0.0668  -0.1308 368 ASN D C   
8857  O O   . ASN D 368 ? 0.2907 0.3893 0.4478 0.0168  0.0674  -0.1299 368 ASN D O   
8858  C CB  . ASN D 368 ? 0.2878 0.3898 0.4330 0.0288  0.0585  -0.1272 368 ASN D CB  
8859  C CG  . ASN D 368 ? 0.2879 0.3850 0.4239 0.0324  0.0586  -0.1217 368 ASN D CG  
8860  O OD1 . ASN D 368 ? 0.2943 0.3919 0.4293 0.0331  0.0634  -0.1227 368 ASN D OD1 
8861  N ND2 . ASN D 368 ? 0.2813 0.3737 0.4106 0.0346  0.0536  -0.1161 368 ASN D ND2 
8862  N N   . GLN D 369 ? 0.3199 0.4306 0.4816 0.0210  0.0694  -0.1392 369 GLN D N   
8863  C CA  . GLN D 369 ? 0.3262 0.4447 0.4992 0.0172  0.0732  -0.1482 369 GLN D CA  
8864  C C   . GLN D 369 ? 0.3308 0.4630 0.5143 0.0195  0.0693  -0.1592 369 GLN D C   
8865  O O   . GLN D 369 ? 0.3436 0.4850 0.5369 0.0177  0.0733  -0.1685 369 GLN D O   
8866  C CB  . GLN D 369 ? 0.3347 0.4517 0.5074 0.0148  0.0820  -0.1489 369 GLN D CB  
8867  C CG  . GLN D 369 ? 0.3316 0.4361 0.4967 0.0117  0.0862  -0.1400 369 GLN D CG  
8868  C CD  . GLN D 369 ? 0.3446 0.4466 0.5069 0.0103  0.0945  -0.1397 369 GLN D CD  
8869  O OE1 . GLN D 369 ? 0.3599 0.4695 0.5249 0.0118  0.0976  -0.1457 369 GLN D OE1 
8870  N NE2 . GLN D 369 ? 0.3536 0.4450 0.5102 0.0076  0.0984  -0.1330 369 GLN D NE2 
8871  N N   . LEU D 370 ? 0.3010 0.4348 0.4825 0.0236  0.0616  -0.1586 370 LEU D N   
8872  C CA  . LEU D 370 ? 0.3053 0.4517 0.4965 0.0265  0.0567  -0.1690 370 LEU D CA  
8873  C C   . LEU D 370 ? 0.3054 0.4584 0.5072 0.0234  0.0552  -0.1762 370 LEU D C   
8874  O O   . LEU D 370 ? 0.3001 0.4466 0.5000 0.0196  0.0563  -0.1718 370 LEU D O   
8875  C CB  . LEU D 370 ? 0.3003 0.4452 0.4856 0.0316  0.0486  -0.1659 370 LEU D CB  
8876  C CG  . LEU D 370 ? 0.2989 0.4361 0.4730 0.0346  0.0493  -0.1580 370 LEU D CG  
8877  C CD1 . LEU D 370 ? 0.2921 0.4250 0.4590 0.0381  0.0418  -0.1530 370 LEU D CD1 
8878  C CD2 . LEU D 370 ? 0.3089 0.4534 0.4867 0.0376  0.0520  -0.1646 370 LEU D CD2 
8879  N N   . SER D 371 ? 0.3044 0.4706 0.5178 0.0254  0.0527  -0.1879 371 SER D N   
8880  C CA  . SER D 371 ? 0.3066 0.4811 0.5320 0.0224  0.0521  -0.1968 371 SER D CA  
8881  C C   . SER D 371 ? 0.3109 0.4983 0.5460 0.0272  0.0448  -0.2075 371 SER D C   
8882  O O   . SER D 371 ? 0.3123 0.5014 0.5443 0.0326  0.0403  -0.2077 371 SER D O   
8883  C CB  . SER D 371 ? 0.3147 0.4931 0.5475 0.0174  0.0613  -0.2021 371 SER D CB  
8884  O OG  . SER D 371 ? 0.3246 0.5111 0.5618 0.0197  0.0650  -0.2086 371 SER D OG  
8885  N N   . GLY D 372 ? 0.3127 0.5091 0.5597 0.0252  0.0433  -0.2169 372 GLY D N   
8886  C CA  . GLY D 372 ? 0.3178 0.5271 0.5756 0.0298  0.0361  -0.2283 372 GLY D CA  
8887  C C   . GLY D 372 ? 0.3104 0.5165 0.5632 0.0332  0.0264  -0.2251 372 GLY D C   
8888  O O   . GLY D 372 ? 0.3013 0.4956 0.5430 0.0314  0.0259  -0.2142 372 GLY D O   
8889  N N   . PRO D 373 ? 0.2963 0.5127 0.5573 0.0384  0.0186  -0.2348 373 PRO D N   
8890  C CA  . PRO D 373 ? 0.2909 0.5044 0.5465 0.0423  0.0090  -0.2322 373 PRO D CA  
8891  C C   . PRO D 373 ? 0.2871 0.4918 0.5293 0.0466  0.0059  -0.2230 373 PRO D C   
8892  O O   . PRO D 373 ? 0.2904 0.4941 0.5298 0.0481  0.0094  -0.2213 373 PRO D O   
8893  C CB  . PRO D 373 ? 0.2998 0.5277 0.5696 0.0471  0.0019  -0.2469 373 PRO D CB  
8894  C CG  . PRO D 373 ? 0.3098 0.5467 0.5884 0.0483  0.0067  -0.2547 373 PRO D CG  
8895  C CD  . PRO D 373 ? 0.3081 0.5395 0.5838 0.0414  0.0182  -0.2489 373 PRO D CD  
8896  N N   . ILE D 374 ? 0.2941 0.4924 0.5277 0.0486  -0.0004 -0.2170 374 ILE D N   
8897  C CA  . ILE D 374 ? 0.2909 0.4810 0.5119 0.0528  -0.0041 -0.2089 374 ILE D CA  
8898  C C   . ILE D 374 ? 0.2987 0.4970 0.5247 0.0604  -0.0132 -0.2180 374 ILE D C   
8899  O O   . ILE D 374 ? 0.3004 0.5036 0.5312 0.0629  -0.0203 -0.2240 374 ILE D O   
8900  C CB  . ILE D 374 ? 0.2811 0.4602 0.4902 0.0512  -0.0056 -0.1980 374 ILE D CB  
8901  C CG1 . ILE D 374 ? 0.2743 0.4434 0.4766 0.0449  0.0032  -0.1878 374 ILE D CG1 
8902  C CG2 . ILE D 374 ? 0.2797 0.4528 0.4780 0.0564  -0.0113 -0.1925 374 ILE D CG2 
8903  C CD1 . ILE D 374 ? 0.2751 0.4392 0.4717 0.0448  0.0085  -0.1826 374 ILE D CD1 
8904  N N   . PRO D 375 ? 0.3029 0.5027 0.5284 0.0645  -0.0136 -0.2197 375 PRO D N   
8905  C CA  . PRO D 375 ? 0.3116 0.5186 0.5420 0.0723  -0.0227 -0.2287 375 PRO D CA  
8906  C C   . PRO D 375 ? 0.3078 0.5073 0.5275 0.0762  -0.0309 -0.2231 375 PRO D C   
8907  O O   . PRO D 375 ? 0.2993 0.4872 0.5057 0.0740  -0.0286 -0.2109 375 PRO D O   
8908  C CB  . PRO D 375 ? 0.3172 0.5245 0.5465 0.0751  -0.0196 -0.2290 375 PRO D CB  
8909  C CG  . PRO D 375 ? 0.3129 0.5160 0.5396 0.0683  -0.0085 -0.2225 375 PRO D CG  
8910  C CD  . PRO D 375 ? 0.3021 0.4966 0.5219 0.0625  -0.0059 -0.2133 375 PRO D CD  
8911  N N   . PRO D 376 ? 0.3441 0.5497 0.5693 0.0823  -0.0406 -0.2320 376 PRO D N   
8912  C CA  . PRO D 376 ? 0.3420 0.5399 0.5563 0.0864  -0.0487 -0.2270 376 PRO D CA  
8913  C C   . PRO D 376 ? 0.3415 0.5304 0.5436 0.0896  -0.0497 -0.2193 376 PRO D C   
8914  O O   . PRO D 376 ? 0.3374 0.5172 0.5276 0.0909  -0.0532 -0.2116 376 PRO D O   
8915  C CB  . PRO D 376 ? 0.3529 0.5603 0.5775 0.0933  -0.0592 -0.2403 376 PRO D CB  
8916  C CG  . PRO D 376 ? 0.3576 0.5776 0.5990 0.0907  -0.0555 -0.2513 376 PRO D CG  
8917  C CD  . PRO D 376 ? 0.3552 0.5747 0.5970 0.0859  -0.0448 -0.2474 376 PRO D CD  
8918  N N   . GLY D 377 ? 0.3511 0.5422 0.5558 0.0907  -0.0463 -0.2212 377 GLY D N   
8919  C CA  . GLY D 377 ? 0.3515 0.5344 0.5454 0.0938  -0.0472 -0.2147 377 GLY D CA  
8920  C C   . GLY D 377 ? 0.3400 0.5113 0.5210 0.0882  -0.0398 -0.2004 377 GLY D C   
8921  O O   . GLY D 377 ? 0.3394 0.5029 0.5104 0.0905  -0.0411 -0.1943 377 GLY D O   
8922  N N   . ILE D 378 ? 0.3279 0.4975 0.5091 0.0810  -0.0324 -0.1954 378 ILE D N   
8923  C CA  . ILE D 378 ? 0.3179 0.4762 0.4875 0.0759  -0.0257 -0.1823 378 ILE D CA  
8924  C C   . ILE D 378 ? 0.3131 0.4622 0.4709 0.0774  -0.0299 -0.1745 378 ILE D C   
8925  O O   . ILE D 378 ? 0.3097 0.4501 0.4573 0.0775  -0.0283 -0.1662 378 ILE D O   
8926  C CB  . ILE D 378 ? 0.3116 0.4696 0.4845 0.0686  -0.0179 -0.1794 378 ILE D CB  
8927  C CG1 . ILE D 378 ? 0.3150 0.4768 0.4939 0.0661  -0.0106 -0.1822 378 ILE D CG1 
8928  C CG2 . ILE D 378 ? 0.3014 0.4473 0.4624 0.0644  -0.0137 -0.1666 378 ILE D CG2 
8929  C CD1 . ILE D 378 ? 0.3105 0.4716 0.4928 0.0593  -0.0032 -0.1800 378 ILE D CD1 
8930  N N   . ALA D 379 ? 0.3538 0.5050 0.5130 0.0788  -0.0353 -0.1774 379 ALA D N   
8931  C CA  . ALA D 379 ? 0.3508 0.4939 0.4991 0.0807  -0.0392 -0.1709 379 ALA D CA  
8932  C C   . ALA D 379 ? 0.3610 0.5053 0.5079 0.0888  -0.0493 -0.1768 379 ALA D C   
8933  O O   . ALA D 379 ? 0.3715 0.5106 0.5109 0.0915  -0.0541 -0.1739 379 ALA D O   
8934  C CB  . ALA D 379 ? 0.3460 0.4889 0.4949 0.0775  -0.0386 -0.1696 379 ALA D CB  
8935  N N   . ASN D 380 ? 0.3857 0.5363 0.5396 0.0932  -0.0526 -0.1851 380 ASN D N   
8936  C CA  . ASN D 380 ? 0.3969 0.5483 0.5502 0.1016  -0.0630 -0.1918 380 ASN D CA  
8937  C C   . ASN D 380 ? 0.3963 0.5363 0.5356 0.1041  -0.0650 -0.1834 380 ASN D C   
8938  O O   . ASN D 380 ? 0.4051 0.5421 0.5402 0.1107  -0.0741 -0.1864 380 ASN D O   
8939  C CB  . ASN D 380 ? 0.4069 0.5673 0.5712 0.1055  -0.0648 -0.2023 380 ASN D CB  
8940  C CG  . ASN D 380 ? 0.4208 0.5843 0.5885 0.1148  -0.0767 -0.2125 380 ASN D CG  
8941  O OD1 . ASN D 380 ? 0.4284 0.5912 0.5949 0.1179  -0.0840 -0.2151 380 ASN D OD1 
8942  N ND2 . ASN D 380 ? 0.4302 0.5967 0.6021 0.1196  -0.0789 -0.2185 380 ASN D ND2 
8943  N N   . SER D 381 ? 0.3460 0.4790 0.4779 0.0992  -0.0571 -0.1732 381 SER D N   
8944  C CA  . SER D 381 ? 0.3458 0.4682 0.4652 0.1012  -0.0583 -0.1657 381 SER D CA  
8945  C C   . SER D 381 ? 0.3430 0.4582 0.4532 0.1015  -0.0606 -0.1600 381 SER D C   
8946  O O   . SER D 381 ? 0.3346 0.4489 0.4441 0.0964  -0.0555 -0.1551 381 SER D O   
8947  C CB  . SER D 381 ? 0.3372 0.4545 0.4521 0.0957  -0.0491 -0.1568 381 SER D CB  
8948  O OG  . SER D 381 ? 0.3350 0.4419 0.4380 0.0963  -0.0491 -0.1485 381 SER D OG  
8949  N N   . THR D 382 ? 0.3560 0.4653 0.4588 0.1078  -0.0683 -0.1606 382 THR D N   
8950  C CA  . THR D 382 ? 0.3552 0.4563 0.4478 0.1086  -0.0702 -0.1548 382 THR D CA  
8951  C C   . THR D 382 ? 0.3450 0.4369 0.4281 0.1032  -0.0615 -0.1425 382 THR D C   
8952  O O   . THR D 382 ? 0.3424 0.4283 0.4184 0.1020  -0.0599 -0.1366 382 THR D O   
8953  C CB  . THR D 382 ? 0.3692 0.4652 0.4559 0.1174  -0.0813 -0.1594 382 THR D CB  
8954  O OG1 . THR D 382 ? 0.3741 0.4667 0.4584 0.1200  -0.0825 -0.1595 382 THR D OG1 
8955  C CG2 . THR D 382 ? 0.3807 0.4849 0.4767 0.1231  -0.0909 -0.1717 382 THR D CG2 
8956  N N   . GLU D 383 ? 0.3573 0.4479 0.4403 0.1001  -0.0559 -0.1388 383 GLU D N   
8957  C CA  . GLU D 383 ? 0.3493 0.4316 0.4246 0.0951  -0.0479 -0.1279 383 GLU D CA  
8958  C C   . GLU D 383 ? 0.3399 0.4245 0.4196 0.0875  -0.0385 -0.1234 383 GLU D C   
8959  O O   . GLU D 383 ? 0.3300 0.4082 0.4047 0.0832  -0.0317 -0.1151 383 GLU D O   
8960  C CB  . GLU D 383 ? 0.3513 0.4291 0.4225 0.0970  -0.0484 -0.1264 383 GLU D CB  
8961  C CG  . GLU D 383 ? 0.3698 0.4449 0.4373 0.1051  -0.0585 -0.1319 383 GLU D CG  
8962  C CD  . GLU D 383 ? 0.3769 0.4437 0.4348 0.1078  -0.0619 -0.1285 383 GLU D CD  
8963  O OE1 . GLU D 383 ? 0.3729 0.4310 0.4225 0.1053  -0.0572 -0.1201 383 GLU D OE1 
8964  O OE2 . GLU D 383 ? 0.3879 0.4567 0.4468 0.1124  -0.0693 -0.1344 383 GLU D OE2 
8965  N N   . LEU D 384 ? 0.2754 0.3683 0.3643 0.0860  -0.0383 -0.1291 384 LEU D N   
8966  C CA  . LEU D 384 ? 0.2667 0.3606 0.3593 0.0792  -0.0301 -0.1253 384 LEU D CA  
8967  C C   . LEU D 384 ? 0.2597 0.3470 0.3464 0.0755  -0.0254 -0.1173 384 LEU D C   
8968  O O   . LEU D 384 ? 0.2620 0.3487 0.3464 0.0778  -0.0290 -0.1182 384 LEU D O   
8969  C CB  . LEU D 384 ? 0.2690 0.3730 0.3729 0.0787  -0.0313 -0.1338 384 LEU D CB  
8970  C CG  . LEU D 384 ? 0.2625 0.3678 0.3712 0.0723  -0.0232 -0.1313 384 LEU D CG  
8971  C CD1 . LEU D 384 ? 0.2638 0.3697 0.3740 0.0718  -0.0201 -0.1316 384 LEU D CD1 
8972  C CD2 . LEU D 384 ? 0.2641 0.3779 0.3828 0.0711  -0.0240 -0.1387 384 LEU D CD2 
8973  N N   . THR D 385 ? 0.2765 0.3585 0.3606 0.0702  -0.0176 -0.1096 385 THR D N   
8974  C CA  . THR D 385 ? 0.2704 0.3460 0.3498 0.0666  -0.0123 -0.1021 385 THR D CA  
8975  C C   . THR D 385 ? 0.2644 0.3399 0.3476 0.0609  -0.0055 -0.0993 385 THR D C   
8976  O O   . THR D 385 ? 0.2610 0.3332 0.3426 0.0585  -0.0022 -0.0956 385 THR D O   
8977  C CB  . THR D 385 ? 0.2682 0.3347 0.3388 0.0665  -0.0094 -0.0944 385 THR D CB  
8978  O OG1 . THR D 385 ? 0.2666 0.3319 0.3373 0.0650  -0.0069 -0.0926 385 THR D OG1 
8979  C CG2 . THR D 385 ? 0.2779 0.3425 0.3431 0.0721  -0.0158 -0.0962 385 THR D CG2 
8980  N N   . VAL D 386 ? 0.2491 0.3274 0.3369 0.0590  -0.0033 -0.1010 386 VAL D N   
8981  C CA  . VAL D 386 ? 0.2448 0.3223 0.3359 0.0541  0.0028  -0.0986 386 VAL D CA  
8982  C C   . VAL D 386 ? 0.2483 0.3340 0.3484 0.0539  0.0018  -0.1063 386 VAL D C   
8983  O O   . VAL D 386 ? 0.2521 0.3410 0.3540 0.0562  0.0000  -0.1098 386 VAL D O   
8984  C CB  . VAL D 386 ? 0.2406 0.3103 0.3263 0.0514  0.0085  -0.0907 386 VAL D CB  
8985  C CG1 . VAL D 386 ? 0.2376 0.3061 0.3264 0.0470  0.0140  -0.0887 386 VAL D CG1 
8986  C CG2 . VAL D 386 ? 0.2377 0.2998 0.3158 0.0514  0.0100  -0.0838 386 VAL D CG2 
8987  N N   . LEU D 387 ? 0.2415 0.3308 0.3476 0.0513  0.0033  -0.1092 387 LEU D N   
8988  C CA  . LEU D 387 ? 0.2451 0.3424 0.3607 0.0505  0.0035  -0.1168 387 LEU D CA  
8989  C C   . LEU D 387 ? 0.2416 0.3360 0.3593 0.0452  0.0100  -0.1137 387 LEU D C   
8990  O O   . LEU D 387 ? 0.2403 0.3360 0.3613 0.0432  0.0104  -0.1150 387 LEU D O   
8991  C CB  . LEU D 387 ? 0.2498 0.3562 0.3725 0.0534  -0.0028 -0.1260 387 LEU D CB  
8992  C CG  . LEU D 387 ? 0.2546 0.3706 0.3887 0.0529  -0.0029 -0.1353 387 LEU D CG  
8993  C CD1 . LEU D 387 ? 0.2587 0.3768 0.3942 0.0547  -0.0020 -0.1375 387 LEU D CD1 
8994  C CD2 . LEU D 387 ? 0.2597 0.3847 0.4009 0.0564  -0.0099 -0.1447 387 LEU D CD2 
8995  N N   . GLN D 388 ? 0.2474 0.3379 0.3633 0.0433  0.0148  -0.1098 388 GLN D N   
8996  C CA  . GLN D 388 ? 0.2471 0.3339 0.3643 0.0389  0.0209  -0.1067 388 GLN D CA  
8997  C C   . GLN D 388 ? 0.2504 0.3444 0.3767 0.0378  0.0225  -0.1141 388 GLN D C   
8998  O O   . GLN D 388 ? 0.2537 0.3502 0.3811 0.0393  0.0233  -0.1163 388 GLN D O   
8999  C CB  . GLN D 388 ? 0.2423 0.3201 0.3517 0.0379  0.0251  -0.0982 388 GLN D CB  
9000  C CG  . GLN D 388 ? 0.2384 0.3099 0.3394 0.0392  0.0238  -0.0917 388 GLN D CG  
9001  C CD  . GLN D 388 ? 0.2345 0.3004 0.3330 0.0366  0.0264  -0.0866 388 GLN D CD  
9002  O OE1 . GLN D 388 ? 0.2341 0.2980 0.3349 0.0335  0.0303  -0.0855 388 GLN D OE1 
9003  N NE2 . GLN D 388 ? 0.2328 0.2960 0.3265 0.0381  0.0245  -0.0838 388 GLN D NE2 
9004  N N   . LEU D 389 ? 0.2545 0.3523 0.3877 0.0351  0.0234  -0.1183 389 LEU D N   
9005  C CA  . LEU D 389 ? 0.2616 0.3670 0.4047 0.0336  0.0253  -0.1262 389 LEU D CA  
9006  C C   . LEU D 389 ? 0.2602 0.3624 0.4062 0.0286  0.0311  -0.1248 389 LEU D C   
9007  O O   . LEU D 389 ? 0.2646 0.3730 0.4193 0.0267  0.0333  -0.1316 389 LEU D O   
9008  C CB  . LEU D 389 ? 0.2636 0.3797 0.4153 0.0358  0.0196  -0.1362 389 LEU D CB  
9009  C CG  . LEU D 389 ? 0.2668 0.3876 0.4177 0.0414  0.0132  -0.1399 389 LEU D CG  
9010  C CD1 . LEU D 389 ? 0.2707 0.4015 0.4302 0.0438  0.0070  -0.1496 389 LEU D CD1 
9011  C CD2 . LEU D 389 ? 0.2718 0.3954 0.4243 0.0431  0.0150  -0.1424 389 LEU D CD2 
9012  N N   . ASP D 390 ? 0.2685 0.3615 0.4079 0.0265  0.0337  -0.1167 390 ASP D N   
9013  C CA  . ASP D 390 ? 0.2681 0.3576 0.4103 0.0220  0.0386  -0.1155 390 ASP D CA  
9014  C C   . ASP D 390 ? 0.2717 0.3595 0.4152 0.0202  0.0442  -0.1153 390 ASP D C   
9015  O O   . ASP D 390 ? 0.2764 0.3644 0.4170 0.0225  0.0447  -0.1145 390 ASP D O   
9016  C CB  . ASP D 390 ? 0.2629 0.3428 0.3975 0.0208  0.0399  -0.1070 390 ASP D CB  
9017  C CG  . ASP D 390 ? 0.2618 0.3338 0.3874 0.0221  0.0419  -0.0988 390 ASP D CG  
9018  O OD1 . ASP D 390 ? 0.2654 0.3373 0.3860 0.0254  0.0386  -0.0969 390 ASP D OD1 
9019  O OD2 . ASP D 390 ? 0.2624 0.3283 0.3863 0.0198  0.0465  -0.0947 390 ASP D OD2 
9020  N N   . THR D 391 ? 0.2628 0.3488 0.4107 0.0161  0.0487  -0.1162 391 THR D N   
9021  C CA  . THR D 391 ? 0.2669 0.3502 0.4157 0.0139  0.0548  -0.1156 391 THR D CA  
9022  C C   . THR D 391 ? 0.2734 0.3654 0.4279 0.0153  0.0554  -0.1231 391 THR D C   
9023  O O   . THR D 391 ? 0.2757 0.3664 0.4260 0.0174  0.0572  -0.1209 391 THR D O   
9024  C CB  . THR D 391 ? 0.2642 0.3373 0.4029 0.0148  0.0571  -0.1060 391 THR D CB  
9025  O OG1 . THR D 391 ? 0.2584 0.3251 0.3920 0.0145  0.0554  -0.0999 391 THR D OG1 
9026  C CG2 . THR D 391 ? 0.2681 0.3365 0.4074 0.0119  0.0637  -0.1046 391 THR D CG2 
9027  N N   . ASN D 392 ? 0.2970 0.3987 0.4616 0.0144  0.0538  -0.1324 392 ASN D N   
9028  C CA  . ASN D 392 ? 0.3043 0.4162 0.4765 0.0156  0.0544  -0.1413 392 ASN D CA  
9029  C C   . ASN D 392 ? 0.3092 0.4288 0.4934 0.0120  0.0561  -0.1505 392 ASN D C   
9030  O O   . ASN D 392 ? 0.3140 0.4298 0.4997 0.0084  0.0575  -0.1491 392 ASN D O   
9031  C CB  . ASN D 392 ? 0.3050 0.4232 0.4769 0.0208  0.0476  -0.1443 392 ASN D CB  
9032  C CG  . ASN D 392 ? 0.3039 0.4177 0.4671 0.0242  0.0479  -0.1387 392 ASN D CG  
9033  O OD1 . ASN D 392 ? 0.3109 0.4270 0.4754 0.0248  0.0519  -0.1411 392 ASN D OD1 
9034  N ND2 . ASN D 392 ? 0.2976 0.4051 0.4519 0.0265  0.0440  -0.1316 392 ASN D ND2 
9035  N N   . ASN D 393 ? 0.3526 0.4834 0.5460 0.0129  0.0564  -0.1603 393 ASN D N   
9036  C CA  . ASN D 393 ? 0.3578 0.4978 0.5640 0.0096  0.0580  -0.1706 393 ASN D CA  
9037  C C   . ASN D 393 ? 0.3600 0.5125 0.5749 0.0131  0.0511  -0.1804 393 ASN D C   
9038  O O   . ASN D 393 ? 0.3732 0.5370 0.5995 0.0126  0.0524  -0.1911 393 ASN D O   
9039  C CB  . ASN D 393 ? 0.3685 0.5113 0.5796 0.0067  0.0663  -0.1750 393 ASN D CB  
9040  C CG  . ASN D 393 ? 0.3752 0.5053 0.5773 0.0039  0.0729  -0.1656 393 ASN D CG  
9041  O OD1 . ASN D 393 ? 0.3819 0.5075 0.5859 -0.0009 0.0772  -0.1649 393 ASN D OD1 
9042  N ND2 . ASN D 393 ? 0.3727 0.4970 0.5651 0.0070  0.0736  -0.1587 393 ASN D ND2 
9043  N N   . PHE D 394 ? 0.3191 0.4700 0.5287 0.0167  0.0437  -0.1771 394 PHE D N   
9044  C CA  . PHE D 394 ? 0.3216 0.4834 0.5383 0.0208  0.0362  -0.1858 394 PHE D CA  
9045  C C   . PHE D 394 ? 0.3227 0.4916 0.5500 0.0183  0.0343  -0.1939 394 PHE D C   
9046  O O   . PHE D 394 ? 0.3193 0.4826 0.5459 0.0138  0.0374  -0.1907 394 PHE D O   
9047  C CB  . PHE D 394 ? 0.3155 0.4727 0.5226 0.0255  0.0292  -0.1796 394 PHE D CB  
9048  C CG  . PHE D 394 ? 0.3159 0.4688 0.5146 0.0290  0.0295  -0.1742 394 PHE D CG  
9049  C CD1 . PHE D 394 ? 0.3237 0.4845 0.5281 0.0315  0.0305  -0.1811 394 PHE D CD1 
9050  C CD2 . PHE D 394 ? 0.3089 0.4505 0.4947 0.0298  0.0291  -0.1629 394 PHE D CD2 
9051  C CE1 . PHE D 394 ? 0.3244 0.4814 0.5212 0.0348  0.0308  -0.1765 394 PHE D CE1 
9052  C CE2 . PHE D 394 ? 0.3094 0.4472 0.4879 0.0329  0.0293  -0.1584 394 PHE D CE2 
9053  C CZ  . PHE D 394 ? 0.3170 0.4624 0.5008 0.0354  0.0300  -0.1651 394 PHE D CZ  
9054  N N   . THR D 395 ? 0.3222 0.5036 0.5596 0.0216  0.0289  -0.2050 395 THR D N   
9055  C CA  . THR D 395 ? 0.3248 0.5152 0.5743 0.0198  0.0266  -0.2148 395 THR D CA  
9056  C C   . THR D 395 ? 0.3259 0.5242 0.5787 0.0259  0.0163  -0.2212 395 THR D C   
9057  O O   . THR D 395 ? 0.3274 0.5265 0.5762 0.0314  0.0120  -0.2206 395 THR D O   
9058  C CB  . THR D 395 ? 0.3341 0.5348 0.5973 0.0168  0.0324  -0.2258 395 THR D CB  
9059  O OG1 . THR D 395 ? 0.3415 0.5511 0.6095 0.0214  0.0310  -0.2325 395 THR D OG1 
9060  C CG2 . THR D 395 ? 0.3344 0.5269 0.5940 0.0108  0.0427  -0.2199 395 THR D CG2 
9061  N N   . GLY D 396 ? 0.2382 0.5710 0.6452 -0.0787 0.0404  -0.2178 396 GLY D N   
9062  C CA  . GLY D 396 ? 0.2355 0.5730 0.6707 -0.0564 0.0265  -0.2307 396 GLY D CA  
9063  C C   . GLY D 396 ? 0.2208 0.5336 0.6504 -0.0377 0.0087  -0.2192 396 GLY D C   
9064  O O   . GLY D 396 ? 0.2109 0.5048 0.6187 -0.0415 0.0048  -0.2014 396 GLY D O   
9065  N N   . PHE D 397 ? 0.2583 0.5698 0.7072 -0.0171 -0.0030 -0.2307 397 PHE D N   
9066  C CA  . PHE D 397 ? 0.2517 0.5382 0.6963 0.0024  -0.0219 -0.2226 397 PHE D CA  
9067  C C   . PHE D 397 ? 0.2448 0.5158 0.6764 0.0081  -0.0188 -0.2180 397 PHE D C   
9068  O O   . PHE D 397 ? 0.2468 0.5283 0.6779 0.0005  -0.0041 -0.2249 397 PHE D O   
9069  C CB  . PHE D 397 ? 0.2648 0.5532 0.7332 0.0220  -0.0388 -0.2367 397 PHE D CB  
9070  C CG  . PHE D 397 ? 0.2726 0.5756 0.7553 0.0187  -0.0445 -0.2421 397 PHE D CG  
9071  C CD1 . PHE D 397 ? 0.2794 0.6115 0.7756 0.0020  -0.0295 -0.2531 397 PHE D CD1 
9072  C CD2 . PHE D 397 ? 0.2764 0.5631 0.7579 0.0320  -0.0649 -0.2369 397 PHE D CD2 
9073  C CE1 . PHE D 397 ? 0.2880 0.6346 0.7986 -0.0020 -0.0341 -0.2590 397 PHE D CE1 
9074  C CE2 . PHE D 397 ? 0.2847 0.5855 0.7798 0.0287  -0.0703 -0.2427 397 PHE D CE2 
9075  C CZ  . PHE D 397 ? 0.2897 0.6215 0.8009 0.0116  -0.0547 -0.2540 397 PHE D CZ  
9076  N N   . LEU D 398 ? 0.2610 0.5060 0.6806 0.0209  -0.0326 -0.2065 398 LEU D N   
9077  C CA  . LEU D 398 ? 0.2577 0.4865 0.6674 0.0285  -0.0314 -0.2038 398 LEU D CA  
9078  C C   . LEU D 398 ? 0.2738 0.4963 0.6984 0.0474  -0.0415 -0.2173 398 LEU D C   
9079  O O   . LEU D 398 ? 0.2865 0.5035 0.7207 0.0605  -0.0580 -0.2217 398 LEU D O   
9080  C CB  . LEU D 398 ? 0.2490 0.4512 0.6382 0.0341  -0.0412 -0.1866 398 LEU D CB  
9081  C CG  . LEU D 398 ? 0.2350 0.4382 0.6054 0.0164  -0.0326 -0.1720 398 LEU D CG  
9082  C CD1 . LEU D 398 ? 0.2381 0.4038 0.5745 0.0231  -0.0400 -0.1544 398 LEU D CD1 
9083  C CD2 . LEU D 398 ? 0.2319 0.4505 0.5954 -0.0005 -0.0124 -0.1741 398 LEU D CD2 
9084  N N   . PRO D 399 ? 0.2827 0.5042 0.7072 0.0488  -0.0329 -0.2238 399 PRO D N   
9085  C CA  . PRO D 399 ? 0.3057 0.5164 0.7402 0.0667  -0.0437 -0.2349 399 PRO D CA  
9086  C C   . PRO D 399 ? 0.3160 0.4875 0.7311 0.0846  -0.0627 -0.2230 399 PRO D C   
9087  O O   . PRO D 399 ? 0.3065 0.4568 0.6986 0.0832  -0.0623 -0.2078 399 PRO D O   
9088  C CB  . PRO D 399 ? 0.3027 0.5180 0.7353 0.0605  -0.0277 -0.2414 399 PRO D CB  
9089  C CG  . PRO D 399 ? 0.2860 0.5236 0.7129 0.0375  -0.0079 -0.2385 399 PRO D CG  
9090  C CD  . PRO D 399 ? 0.2725 0.5028 0.6860 0.0328  -0.0130 -0.2219 399 PRO D CD  
9091  N N   . ASP D 400 ? 0.3675 0.5277 0.7887 0.1013  -0.0794 -0.2299 400 ASP D N   
9092  C CA  . ASP D 400 ? 0.3914 0.5087 0.7856 0.1174  -0.0977 -0.2176 400 ASP D CA  
9093  C C   . ASP D 400 ? 0.4022 0.4883 0.7716 0.1212  -0.0922 -0.2110 400 ASP D C   
9094  O O   . ASP D 400 ? 0.4282 0.4726 0.7655 0.1306  -0.1033 -0.1980 400 ASP D O   
9095  C CB  . ASP D 400 ? 0.4240 0.5382 0.8291 0.1333  -0.1178 -0.2269 400 ASP D CB  
9096  C CG  . ASP D 400 ? 0.4274 0.5676 0.8533 0.1297  -0.1239 -0.2335 400 ASP D CG  
9097  O OD1 . ASP D 400 ? 0.4215 0.5995 0.8779 0.1211  -0.1136 -0.2495 400 ASP D OD1 
9098  O OD2 . ASP D 400 ? 0.4206 0.5417 0.8298 0.1341  -0.1378 -0.2228 400 ASP D OD2 
9099  N N   . THR D 401 ? 0.3447 0.4482 0.7248 0.1124  -0.0745 -0.2198 401 THR D N   
9100  C CA  . THR D 401 ? 0.3553 0.4318 0.7124 0.1125  -0.0659 -0.2151 401 THR D CA  
9101  C C   . THR D 401 ? 0.3366 0.4020 0.6710 0.0999  -0.0535 -0.2026 401 THR D C   
9102  O O   . THR D 401 ? 0.3401 0.3923 0.6595 0.0944  -0.0414 -0.2020 401 THR D O   
9103  C CB  . THR D 401 ? 0.3552 0.4559 0.7332 0.1078  -0.0524 -0.2316 401 THR D CB  
9104  O OG1 . THR D 401 ? 0.3262 0.4685 0.7242 0.0897  -0.0358 -0.2388 401 THR D OG1 
9105  C CG2 . THR D 401 ? 0.3792 0.4869 0.7784 0.1222  -0.0654 -0.2453 401 THR D CG2 
9106  N N   . ILE D 402 ? 0.3704 0.4411 0.7023 0.0952  -0.0564 -0.1936 402 ILE D N   
9107  C CA  . ILE D 402 ? 0.3498 0.4221 0.6671 0.0806  -0.0428 -0.1843 402 ILE D CA  
9108  C C   . ILE D 402 ? 0.3782 0.4074 0.6562 0.0801  -0.0410 -0.1725 402 ILE D C   
9109  O O   . ILE D 402 ? 0.3815 0.4137 0.6465 0.0662  -0.0258 -0.1697 402 ILE D O   
9110  C CB  . ILE D 402 ? 0.3344 0.4168 0.6496 0.0742  -0.0486 -0.1731 402 ILE D CB  
9111  C CG1 . ILE D 402 ? 0.3215 0.4050 0.6125 0.0556  -0.0359 -0.1589 402 ILE D CG1 
9112  C CG2 . ILE D 402 ? 0.3584 0.4084 0.6590 0.0895  -0.0689 -0.1652 402 ILE D CG2 
9113  C CD1 . ILE D 402 ? 0.3061 0.4200 0.6071 0.0399  -0.0177 -0.1656 402 ILE D CD1 
9114  N N   . CYS D 403 ? 0.3874 0.3765 0.6441 0.0937  -0.0561 -0.1656 403 CYS D N   
9115  C CA  . CYS D 403 ? 0.4079 0.3528 0.6251 0.0919  -0.0537 -0.1554 403 CYS D CA  
9116  C C   . CYS D 403 ? 0.4467 0.3604 0.6487 0.1037  -0.0618 -0.1560 403 CYS D C   
9117  O O   . CYS D 403 ? 0.4782 0.3491 0.6451 0.1086  -0.0700 -0.1446 403 CYS D O   
9118  C CB  . CYS D 403 ? 0.4180 0.3389 0.6063 0.0899  -0.0607 -0.1391 403 CYS D CB  
9119  S SG  . CYS D 403 ? 0.4445 0.3266 0.5872 0.0776  -0.0491 -0.1274 403 CYS D SG  
9120  N N   . ARG D 404 ? 0.3864 0.3214 0.6140 0.1078  -0.0591 -0.1698 404 ARG D N   
9121  C CA  . ARG D 404 ? 0.4248 0.3332 0.6428 0.1210  -0.0679 -0.1726 404 ARG D CA  
9122  C C   . ARG D 404 ? 0.4568 0.3151 0.6320 0.1176  -0.0622 -0.1635 404 ARG D C   
9123  O O   . ARG D 404 ? 0.4968 0.3136 0.6436 0.1273  -0.0734 -0.1556 404 ARG D O   
9124  C CB  . ARG D 404 ? 0.4174 0.3597 0.6703 0.1225  -0.0613 -0.1906 404 ARG D CB  
9125  C CG  . ARG D 404 ? 0.4568 0.3776 0.7071 0.1384  -0.0721 -0.1962 404 ARG D CG  
9126  C CD  . ARG D 404 ? 0.4459 0.4104 0.7393 0.1412  -0.0693 -0.2160 404 ARG D CD  
9127  N NE  . ARG D 404 ? 0.4421 0.4144 0.7391 0.1317  -0.0510 -0.2249 404 ARG D NE  
9128  C CZ  . ARG D 404 ? 0.4749 0.4117 0.7495 0.1359  -0.0484 -0.2248 404 ARG D CZ  
9129  N NH1 . ARG D 404 ? 0.5168 0.4057 0.7622 0.1494  -0.0623 -0.2158 404 ARG D NH1 
9130  N NH2 . ARG D 404 ? 0.4687 0.4170 0.7480 0.1252  -0.0312 -0.2339 404 ARG D NH2 
9131  N N   . GLY D 405 ? 0.4040 0.2658 0.5732 0.1022  -0.0442 -0.1653 405 GLY D N   
9132  C CA  . GLY D 405 ? 0.4345 0.2513 0.5647 0.0954  -0.0366 -0.1591 405 GLY D CA  
9133  C C   . GLY D 405 ? 0.4451 0.2295 0.5396 0.0887  -0.0378 -0.1442 405 GLY D C   
9134  O O   . GLY D 405 ? 0.4773 0.2198 0.5360 0.0821  -0.0318 -0.1389 405 GLY D O   
9135  N N   . GLY D 406 ? 0.4251 0.2273 0.5278 0.0889  -0.0443 -0.1382 406 GLY D N   
9136  C CA  . GLY D 406 ? 0.4354 0.2093 0.5050 0.0825  -0.0452 -0.1250 406 GLY D CA  
9137  C C   . GLY D 406 ? 0.4213 0.1973 0.4805 0.0633  -0.0279 -0.1253 406 GLY D C   
9138  O O   . GLY D 406 ? 0.4402 0.1866 0.4653 0.0551  -0.0248 -0.1154 406 GLY D O   
9139  N N   . LYS D 407 ? 0.3949 0.2124 0.4793 0.0529  -0.0143 -0.1332 407 LYS D N   
9140  C CA  . LYS D 407 ? 0.3800 0.2116 0.4551 0.0330  0.0030  -0.1310 407 LYS D CA  
9141  C C   . LYS D 407 ? 0.3359 0.2176 0.4340 0.0251  0.0076  -0.1290 407 LYS D C   
9142  O O   . LYS D 407 ? 0.3221 0.2196 0.4149 0.0104  0.0194  -0.1274 407 LYS D O   
9143  C CB  . LYS D 407 ? 0.3902 0.2197 0.4665 0.0255  0.0155  -0.1423 407 LYS D CB  
9144  C CG  . LYS D 407 ? 0.4399 0.2137 0.4877 0.0304  0.0130  -0.1440 407 LYS D CG  
9145  C CD  . LYS D 407 ? 0.4493 0.2216 0.4954 0.0187  0.0279  -0.1548 407 LYS D CD  
9146  C CE  . LYS D 407 ? 0.5041 0.2202 0.5162 0.0237  0.0239  -0.1528 407 LYS D CE  
9147  N NZ  . LYS D 407 ? 0.5153 0.2306 0.5213 0.0103  0.0375  -0.1605 407 LYS D NZ  
9148  N N   . LEU D 408 ? 0.3337 0.2398 0.4562 0.0341  -0.0018 -0.1297 408 LEU D N   
9149  C CA  . LEU D 408 ? 0.2980 0.2467 0.4390 0.0260  0.0023  -0.1277 408 LEU D CA  
9150  C C   . LEU D 408 ? 0.2906 0.2366 0.4133 0.0186  0.0033  -0.1158 408 LEU D C   
9151  O O   . LEU D 408 ? 0.3040 0.2255 0.4106 0.0248  -0.0056 -0.1079 408 LEU D O   
9152  C CB  . LEU D 408 ? 0.2852 0.2547 0.4522 0.0358  -0.0081 -0.1305 408 LEU D CB  
9153  C CG  . LEU D 408 ? 0.2544 0.2654 0.4396 0.0261  -0.0029 -0.1299 408 LEU D CG  
9154  C CD1 . LEU D 408 ? 0.2452 0.2824 0.4448 0.0171  0.0100  -0.1409 408 LEU D CD1 
9155  C CD2 . LEU D 408 ? 0.2463 0.2714 0.4515 0.0337  -0.0139 -0.1305 408 LEU D CD2 
9156  N N   . GLU D 409 ? 0.2978 0.2692 0.4227 0.0059  0.0136  -0.1155 409 GLU D N   
9157  C CA  . GLU D 409 ? 0.2962 0.2699 0.4077 -0.0005 0.0152  -0.1069 409 GLU D CA  
9158  C C   . GLU D 409 ? 0.2817 0.2837 0.4066 -0.0009 0.0106  -0.1019 409 GLU D C   
9159  O O   . GLU D 409 ? 0.2870 0.2818 0.4049 0.0030  0.0033  -0.0939 409 GLU D O   
9160  C CB  . GLU D 409 ? 0.2955 0.2761 0.3987 -0.0136 0.0282  -0.1109 409 GLU D CB  
9161  C CG  . GLU D 409 ? 0.3175 0.2632 0.3980 -0.0171 0.0340  -0.1130 409 GLU D CG  
9162  C CD  . GLU D 409 ? 0.3173 0.2745 0.3930 -0.0320 0.0476  -0.1190 409 GLU D CD  
9163  O OE1 . GLU D 409 ? 0.2955 0.2881 0.3853 -0.0377 0.0505  -0.1212 409 GLU D OE1 
9164  O OE2 . GLU D 409 ? 0.3498 0.2796 0.4063 -0.0385 0.0549  -0.1220 409 GLU D OE2 
9165  N N   . ASN D 410 ? 0.2455 0.2770 0.3869 -0.0064 0.0149  -0.1065 410 ASN D N   
9166  C CA  . ASN D 410 ? 0.2281 0.2827 0.3759 -0.0099 0.0122  -0.1012 410 ASN D CA  
9167  C C   . ASN D 410 ? 0.2211 0.2939 0.3882 -0.0096 0.0109  -0.1058 410 ASN D C   
9168  O O   . ASN D 410 ? 0.2209 0.3069 0.3979 -0.0139 0.0184  -0.1151 410 ASN D O   
9169  C CB  . ASN D 410 ? 0.2205 0.2930 0.3631 -0.0199 0.0194  -0.1016 410 ASN D CB  
9170  C CG  . ASN D 410 ? 0.2274 0.2869 0.3555 -0.0213 0.0220  -0.1001 410 ASN D CG  
9171  O OD1 . ASN D 410 ? 0.2339 0.2746 0.3527 -0.0157 0.0170  -0.0944 410 ASN D OD1 
9172  N ND2 . ASN D 410 ? 0.2284 0.2975 0.3541 -0.0296 0.0307  -0.1064 410 ASN D ND2 
9173  N N   . LEU D 411 ? 0.2035 0.2776 0.3760 -0.0057 0.0024  -0.1005 411 LEU D N   
9174  C CA  . LEU D 411 ? 0.1984 0.2910 0.3905 -0.0070 0.0016  -0.1058 411 LEU D CA  
9175  C C   . LEU D 411 ? 0.1911 0.2951 0.3795 -0.0143 -0.0005 -0.0977 411 LEU D C   
9176  O O   . LEU D 411 ? 0.1918 0.2827 0.3694 -0.0107 -0.0083 -0.0884 411 LEU D O   
9177  C CB  . LEU D 411 ? 0.2058 0.2870 0.4099 0.0051  -0.0080 -0.1095 411 LEU D CB  
9178  C CG  . LEU D 411 ? 0.2009 0.3038 0.4299 0.0045  -0.0101 -0.1169 411 LEU D CG  
9179  C CD1 . LEU D 411 ? 0.1984 0.3248 0.4437 -0.0021 0.0015  -0.1298 411 LEU D CD1 
9180  C CD2 . LEU D 411 ? 0.2104 0.3005 0.4504 0.0192  -0.0230 -0.1208 411 LEU D CD2 
9181  N N   . THR D 412 ? 0.2133 0.3389 0.4080 -0.0250 0.0066  -0.1014 412 THR D N   
9182  C CA  . THR D 412 ? 0.2172 0.3490 0.4022 -0.0340 0.0053  -0.0932 412 THR D CA  
9183  C C   . THR D 412 ? 0.2161 0.3655 0.4166 -0.0423 0.0092  -0.0995 412 THR D C   
9184  O O   . THR D 412 ? 0.2069 0.3739 0.4174 -0.0492 0.0193  -0.1099 412 THR D O   
9185  C CB  . THR D 412 ? 0.2236 0.3613 0.3919 -0.0421 0.0106  -0.0900 412 THR D CB  
9186  O OG1 . THR D 412 ? 0.2227 0.3503 0.3830 -0.0358 0.0098  -0.0890 412 THR D OG1 
9187  C CG2 . THR D 412 ? 0.2445 0.3781 0.3965 -0.0471 0.0049  -0.0787 412 THR D CG2 
9188  N N   . LEU D 413 ? 0.2179 0.3632 0.4206 -0.0427 0.0022  -0.0946 413 LEU D N   
9189  C CA  . LEU D 413 ? 0.2136 0.3765 0.4335 -0.0518 0.0061  -0.1021 413 LEU D CA  
9190  C C   . LEU D 413 ? 0.2356 0.3939 0.4398 -0.0639 0.0047  -0.0924 413 LEU D C   
9191  O O   . LEU D 413 ? 0.2354 0.4026 0.4523 -0.0711 0.0052  -0.0966 413 LEU D O   
9192  C CB  . LEU D 413 ? 0.2078 0.3722 0.4522 -0.0404 -0.0018 -0.1100 413 LEU D CB  
9193  C CG  . LEU D 413 ? 0.2052 0.3665 0.4623 -0.0261 -0.0035 -0.1190 413 LEU D CG  
9194  C CD1 . LEU D 413 ? 0.2073 0.3613 0.4798 -0.0123 -0.0166 -0.1226 413 LEU D CD1 
9195  C CD2 . LEU D 413 ? 0.2047 0.3895 0.4798 -0.0313 0.0088  -0.1340 413 LEU D CD2 
9196  N N   . ASP D 414 ? 0.2481 0.3920 0.4251 -0.0663 0.0024  -0.0803 414 ASP D N   
9197  C CA  . ASP D 414 ? 0.2805 0.4110 0.4381 -0.0744 -0.0022 -0.0692 414 ASP D CA  
9198  C C   . ASP D 414 ? 0.2980 0.4408 0.4537 -0.0942 0.0080  -0.0729 414 ASP D C   
9199  O O   . ASP D 414 ? 0.2951 0.4558 0.4552 -0.1029 0.0196  -0.0814 414 ASP D O   
9200  C CB  . ASP D 414 ? 0.3083 0.4226 0.4381 -0.0713 -0.0074 -0.0575 414 ASP D CB  
9201  C CG  . ASP D 414 ? 0.2952 0.3955 0.4243 -0.0546 -0.0170 -0.0533 414 ASP D CG  
9202  O OD1 . ASP D 414 ? 0.2649 0.3688 0.4111 -0.0457 -0.0168 -0.0601 414 ASP D OD1 
9203  O OD2 . ASP D 414 ? 0.3156 0.4002 0.4260 -0.0504 -0.0247 -0.0438 414 ASP D OD2 
9204  N N   . ASP D 415 ? 0.3053 0.4371 0.4529 -0.1025 0.0044  -0.0672 415 ASP D N   
9205  C CA  . ASP D 415 ? 0.3346 0.4693 0.4697 -0.1245 0.0138  -0.0671 415 ASP D CA  
9206  C C   . ASP D 415 ? 0.3066 0.4734 0.4678 -0.1356 0.0288  -0.0844 415 ASP D C   
9207  O O   . ASP D 415 ? 0.3144 0.4914 0.4655 -0.1485 0.0408  -0.0882 415 ASP D O   
9208  C CB  . ASP D 415 ? 0.3835 0.5008 0.4803 -0.1314 0.0139  -0.0553 415 ASP D CB  
9209  C CG  . ASP D 415 ? 0.4199 0.5072 0.4936 -0.1195 -0.0016 -0.0402 415 ASP D CG  
9210  O OD1 . ASP D 415 ? 0.4147 0.4882 0.4907 -0.1166 -0.0092 -0.0364 415 ASP D OD1 
9211  O OD2 . ASP D 415 ? 0.4368 0.5158 0.4918 -0.1126 -0.0064 -0.0337 415 ASP D OD2 
9212  N N   . ASN D 416 ? 0.3260 0.5093 0.5216 -0.1296 0.0272  -0.0961 416 ASN D N   
9213  C CA  . ASN D 416 ? 0.2930 0.5100 0.5215 -0.1355 0.0392  -0.1157 416 ASN D CA  
9214  C C   . ASN D 416 ? 0.2979 0.5209 0.5433 -0.1381 0.0369  -0.1210 416 ASN D C   
9215  O O   . ASN D 416 ? 0.3160 0.5242 0.5526 -0.1449 0.0295  -0.1131 416 ASN D O   
9216  C CB  . ASN D 416 ? 0.2700 0.4954 0.5190 -0.1142 0.0360  -0.1240 416 ASN D CB  
9217  C CG  . ASN D 416 ? 0.2725 0.5029 0.5096 -0.1167 0.0463  -0.1263 416 ASN D CG  
9218  O OD1 . ASN D 416 ? 0.2920 0.5283 0.5136 -0.1328 0.0588  -0.1278 416 ASN D OD1 
9219  N ND2 . ASN D 416 ? 0.2587 0.4854 0.5010 -0.1016 0.0414  -0.1271 416 ASN D ND2 
9220  N N   . HIS D 417 ? 0.3197 0.5641 0.5890 -0.1330 0.0429  -0.1358 417 HIS D N   
9221  C CA  . HIS D 417 ? 0.3273 0.5831 0.6166 -0.1349 0.0412  -0.1441 417 HIS D CA  
9222  C C   . HIS D 417 ? 0.3096 0.5783 0.6313 -0.1123 0.0321  -0.1566 417 HIS D C   
9223  O O   . HIS D 417 ? 0.3175 0.6068 0.6617 -0.1109 0.0364  -0.1719 417 HIS D O   
9224  C CB  . HIS D 417 ? 0.3538 0.6246 0.6393 -0.1548 0.0584  -0.1526 417 HIS D CB  
9225  C CG  . HIS D 417 ? 0.3776 0.6305 0.6268 -0.1784 0.0662  -0.1400 417 HIS D CG  
9226  N ND1 . HIS D 417 ? 0.3934 0.6477 0.6201 -0.1939 0.0816  -0.1410 417 HIS D ND1 
9227  C CD2 . HIS D 417 ? 0.3910 0.6206 0.6194 -0.1895 0.0598  -0.1264 417 HIS D CD2 
9228  C CE1 . HIS D 417 ? 0.4258 0.6572 0.6174 -0.2134 0.0840  -0.1275 417 HIS D CE1 
9229  N NE2 . HIS D 417 ? 0.4270 0.6423 0.6192 -0.2111 0.0710  -0.1185 417 HIS D NE2 
9230  N N   . PHE D 418 ? 0.2671 0.5220 0.5902 -0.0944 0.0189  -0.1510 418 PHE D N   
9231  C CA  . PHE D 418 ? 0.2584 0.5178 0.6064 -0.0723 0.0078  -0.1611 418 PHE D CA  
9232  C C   . PHE D 418 ? 0.2609 0.5193 0.6220 -0.0672 -0.0056 -0.1623 418 PHE D C   
9233  O O   . PHE D 418 ? 0.2641 0.5111 0.6122 -0.0772 -0.0097 -0.1522 418 PHE D O   
9234  C CB  . PHE D 418 ? 0.2441 0.4856 0.5851 -0.0565 -0.0011 -0.1544 418 PHE D CB  
9235  C CG  . PHE D 418 ? 0.2420 0.4870 0.5760 -0.0577 0.0106  -0.1571 418 PHE D CG  
9236  C CD1 . PHE D 418 ? 0.2485 0.5106 0.5988 -0.0547 0.0190  -0.1729 418 PHE D CD1 
9237  C CD2 . PHE D 418 ? 0.2355 0.4667 0.5469 -0.0617 0.0125  -0.1453 418 PHE D CD2 
9238  C CE1 . PHE D 418 ? 0.2487 0.5124 0.5912 -0.0563 0.0294  -0.1762 418 PHE D CE1 
9239  C CE2 . PHE D 418 ? 0.2352 0.4700 0.5393 -0.0633 0.0229  -0.1484 418 PHE D CE2 
9240  C CZ  . PHE D 418 ? 0.2419 0.4920 0.5607 -0.0609 0.0315  -0.1636 418 PHE D CZ  
9241  N N   . GLU D 419 ? 0.2675 0.5364 0.6538 -0.0512 -0.0134 -0.1758 419 GLU D N   
9242  C CA  . GLU D 419 ? 0.2719 0.5420 0.6725 -0.0441 -0.0273 -0.1796 419 GLU D CA  
9243  C C   . GLU D 419 ? 0.2691 0.5280 0.6805 -0.0184 -0.0448 -0.1840 419 GLU D C   
9244  O O   . GLU D 419 ? 0.2668 0.5165 0.6746 -0.0076 -0.0453 -0.1838 419 GLU D O   
9245  C CB  . GLU D 419 ? 0.2863 0.5843 0.7085 -0.0537 -0.0190 -0.1953 419 GLU D CB  
9246  C CG  . GLU D 419 ? 0.2965 0.6037 0.7061 -0.0805 -0.0010 -0.1924 419 GLU D CG  
9247  C CD  . GLU D 419 ? 0.3163 0.6533 0.7488 -0.0891 0.0097  -0.2111 419 GLU D CD  
9248  O OE1 . GLU D 419 ? 0.3276 0.6738 0.7730 -0.0932 0.0048  -0.2163 419 GLU D OE1 
9249  O OE2 . GLU D 419 ? 0.3219 0.6734 0.7596 -0.0921 0.0231  -0.2218 419 GLU D OE2 
9250  N N   . GLY D 420 ? 0.2753 0.5331 0.6977 -0.0093 -0.0597 -0.1881 420 GLY D N   
9251  C CA  . GLY D 420 ? 0.2811 0.5282 0.7131 0.0144  -0.0775 -0.1945 420 GLY D CA  
9252  C C   . GLY D 420 ? 0.2763 0.4893 0.6852 0.0273  -0.0915 -0.1801 420 GLY D C   
9253  O O   . GLY D 420 ? 0.2664 0.4654 0.6542 0.0186  -0.0886 -0.1655 420 GLY D O   
9254  N N   . PRO D 421 ? 0.2610 0.4580 0.6714 0.0482  -0.1075 -0.1843 421 PRO D N   
9255  C CA  . PRO D 421 ? 0.2641 0.4246 0.6481 0.0607  -0.1217 -0.1706 421 PRO D CA  
9256  C C   . PRO D 421 ? 0.2569 0.4043 0.6288 0.0645  -0.1151 -0.1652 421 PRO D C   
9257  O O   . PRO D 421 ? 0.2487 0.4152 0.6328 0.0578  -0.0999 -0.1724 421 PRO D O   
9258  C CB  . PRO D 421 ? 0.2883 0.4349 0.6743 0.0795  -0.1417 -0.1778 421 PRO D CB  
9259  C CG  . PRO D 421 ? 0.2944 0.4679 0.7098 0.0820  -0.1363 -0.1966 421 PRO D CG  
9260  C CD  . PRO D 421 ? 0.2778 0.4865 0.7109 0.0610  -0.1150 -0.2018 421 PRO D CD  
9261  N N   . VAL D 422 ? 0.2850 0.3983 0.6304 0.0748  -0.1256 -0.1528 422 VAL D N   
9262  C CA  . VAL D 422 ? 0.2842 0.3794 0.6151 0.0807  -0.1202 -0.1477 422 VAL D CA  
9263  C C   . VAL D 422 ? 0.3090 0.3877 0.6378 0.0966  -0.1292 -0.1554 422 VAL D C   
9264  O O   . VAL D 422 ? 0.3327 0.3903 0.6487 0.1075  -0.1464 -0.1541 422 VAL D O   
9265  C CB  . VAL D 422 ? 0.3123 0.3687 0.5991 0.0793  -0.1213 -0.1286 422 VAL D CB  
9266  C CG1 . VAL D 422 ? 0.3135 0.3523 0.5781 0.0770  -0.1083 -0.1224 422 VAL D CG1 
9267  C CG2 . VAL D 422 ? 0.2989 0.3637 0.5784 0.0633  -0.1153 -0.1198 422 VAL D CG2 
9268  N N   . PRO D 423 ? 0.3464 0.4335 0.6853 0.0973  -0.1186 -0.1634 423 PRO D N   
9269  C CA  . PRO D 423 ? 0.3760 0.4468 0.7118 0.1116  -0.1282 -0.1703 423 PRO D CA  
9270  C C   . PRO D 423 ? 0.4048 0.4263 0.6988 0.1220  -0.1405 -0.1560 423 PRO D C   
9271  O O   . PRO D 423 ? 0.4009 0.3993 0.6674 0.1174  -0.1348 -0.1425 423 PRO D O   
9272  C CB  . PRO D 423 ? 0.3643 0.4496 0.7126 0.1071  -0.1112 -0.1786 423 PRO D CB  
9273  C CG  . PRO D 423 ? 0.3335 0.4561 0.7017 0.0890  -0.0937 -0.1816 423 PRO D CG  
9274  C CD  . PRO D 423 ? 0.3226 0.4360 0.6753 0.0836  -0.0977 -0.1670 423 PRO D CD  
9275  N N   . LYS D 424 ? 0.4478 0.4527 0.7350 0.1353  -0.1569 -0.1595 424 LYS D N   
9276  C CA  . LYS D 424 ? 0.4795 0.4364 0.7225 0.1435  -0.1684 -0.1458 424 LYS D CA  
9277  C C   . LYS D 424 ? 0.4868 0.4156 0.7022 0.1408  -0.1556 -0.1367 424 LYS D C   
9278  O O   . LYS D 424 ? 0.5079 0.3996 0.6830 0.1392  -0.1562 -0.1222 424 LYS D O   
9279  C CB  . LYS D 424 ? 0.5206 0.4664 0.7631 0.1587  -0.1876 -0.1530 424 LYS D CB  
9280  C CG  . LYS D 424 ? 0.5273 0.4877 0.7844 0.1623  -0.2035 -0.1598 424 LYS D CG  
9281  C CD  . LYS D 424 ? 0.5838 0.5199 0.8263 0.1784  -0.2250 -0.1630 424 LYS D CD  
9282  C CE  . LYS D 424 ? 0.5962 0.5616 0.8784 0.1875  -0.2302 -0.1836 424 LYS D CE  
9283  N NZ  . LYS D 424 ? 0.6294 0.5694 0.8971 0.2049  -0.2528 -0.1871 424 LYS D NZ  
9284  N N   . SER D 425 ? 0.4687 0.4145 0.7042 0.1387  -0.1428 -0.1461 425 SER D N   
9285  C CA  . SER D 425 ? 0.4801 0.3996 0.6904 0.1344  -0.1295 -0.1394 425 SER D CA  
9286  C C   . SER D 425 ? 0.4539 0.3731 0.6527 0.1206  -0.1153 -0.1307 425 SER D C   
9287  O O   . SER D 425 ? 0.4663 0.3536 0.6322 0.1158  -0.1077 -0.1215 425 SER D O   
9288  C CB  . SER D 425 ? 0.4733 0.4128 0.7089 0.1349  -0.1193 -0.1534 425 SER D CB  
9289  O OG  . SER D 425 ? 0.4344 0.4123 0.6978 0.1223  -0.1026 -0.1610 425 SER D OG  
9290  N N   . LEU D 426 ? 0.4422 0.3958 0.6671 0.1135  -0.1114 -0.1342 426 LEU D N   
9291  C CA  . LEU D 426 ? 0.4213 0.3740 0.6332 0.1010  -0.1004 -0.1250 426 LEU D CA  
9292  C C   . LEU D 426 ? 0.4377 0.3583 0.6172 0.1035  -0.1111 -0.1115 426 LEU D C   
9293  O O   . LEU D 426 ? 0.4381 0.3430 0.5895 0.0932  -0.1016 -0.1005 426 LEU D O   
9294  C CB  . LEU D 426 ? 0.3861 0.3852 0.6268 0.0880  -0.0912 -0.1287 426 LEU D CB  
9295  C CG  . LEU D 426 ? 0.3764 0.3818 0.6002 0.0705  -0.0768 -0.1174 426 LEU D CG  
9296  C CD1 . LEU D 426 ? 0.3958 0.3848 0.5984 0.0650  -0.0641 -0.1141 426 LEU D CD1 
9297  C CD2 . LEU D 426 ? 0.3468 0.3937 0.5964 0.0575  -0.0670 -0.1225 426 LEU D CD2 
9298  N N   . ARG D 427 ? 0.4396 0.3564 0.6181 0.1120  -0.1282 -0.1107 427 ARG D N   
9299  C CA  . ARG D 427 ? 0.4568 0.3424 0.5994 0.1131  -0.1378 -0.0981 427 ARG D CA  
9300  C C   . ARG D 427 ? 0.4901 0.3317 0.5894 0.1137  -0.1349 -0.0888 427 ARG D C   
9301  O O   . ARG D 427 ? 0.5001 0.3174 0.5673 0.1074  -0.1307 -0.0783 427 ARG D O   
9302  C CB  . ARG D 427 ? 0.4710 0.3616 0.6216 0.1221  -0.1572 -0.1019 427 ARG D CB  
9303  C CG  . ARG D 427 ? 0.5068 0.3613 0.6167 0.1251  -0.1689 -0.0909 427 ARG D CG  
9304  C CD  . ARG D 427 ? 0.5241 0.3836 0.6436 0.1349  -0.1891 -0.0980 427 ARG D CD  
9305  N NE  . ARG D 427 ? 0.5610 0.3997 0.6683 0.1463  -0.1992 -0.1008 427 ARG D NE  
9306  C CZ  . ARG D 427 ? 0.5769 0.4283 0.7056 0.1569  -0.2144 -0.1127 427 ARG D CZ  
9307  N NH1 . ARG D 427 ? 0.5631 0.4488 0.7270 0.1564  -0.2202 -0.1237 427 ARG D NH1 
9308  N NH2 . ARG D 427 ? 0.6156 0.4441 0.7299 0.1680  -0.2238 -0.1144 427 ARG D NH2 
9309  N N   . ASP D 428 ? 0.4827 0.3133 0.5805 0.1204  -0.1360 -0.0933 428 ASP D N   
9310  C CA  . ASP D 428 ? 0.5198 0.3063 0.5766 0.1203  -0.1328 -0.0854 428 ASP D CA  
9311  C C   . ASP D 428 ? 0.5109 0.2919 0.5620 0.1095  -0.1128 -0.0860 428 ASP D C   
9312  O O   . ASP D 428 ? 0.5476 0.2916 0.5644 0.1061  -0.1071 -0.0803 428 ASP D O   
9313  C CB  . ASP D 428 ? 0.5536 0.3260 0.6086 0.1336  -0.1458 -0.0899 428 ASP D CB  
9314  C CG  . ASP D 428 ? 0.5611 0.3480 0.6320 0.1446  -0.1665 -0.0948 428 ASP D CG  
9315  O OD1 . ASP D 428 ? 0.5456 0.3425 0.6173 0.1411  -0.1714 -0.0915 428 ASP D OD1 
9316  O OD2 . ASP D 428 ? 0.5871 0.3752 0.6699 0.1565  -0.1782 -0.1031 428 ASP D OD2 
9317  N N   . CYS D 429 ? 0.4636 0.2799 0.5466 0.1028  -0.1019 -0.0938 429 CYS D N   
9318  C CA  . CYS D 429 ? 0.4540 0.2701 0.5352 0.0919  -0.0837 -0.0974 429 CYS D CA  
9319  C C   . CYS D 429 ? 0.4605 0.2589 0.5108 0.0792  -0.0743 -0.0873 429 CYS D C   
9320  O O   . CYS D 429 ? 0.4368 0.2616 0.4955 0.0711  -0.0696 -0.0832 429 CYS D O   
9321  C CB  . CYS D 429 ? 0.4167 0.2831 0.5388 0.0856  -0.0740 -0.1071 429 CYS D CB  
9322  S SG  . CYS D 429 ? 0.4153 0.2956 0.5352 0.0680  -0.0504 -0.1096 429 CYS D SG  
9323  N N   . LYS D 430 ? 0.4637 0.2194 0.4770 0.0758  -0.0701 -0.0831 430 LYS D N   
9324  C CA  . LYS D 430 ? 0.4722 0.2109 0.4535 0.0629  -0.0604 -0.0742 430 LYS D CA  
9325  C C   . LYS D 430 ? 0.4482 0.2124 0.4358 0.0455  -0.0393 -0.0766 430 LYS D C   
9326  O O   . LYS D 430 ? 0.4570 0.2171 0.4257 0.0344  -0.0300 -0.0719 430 LYS D O   
9327  C CB  . LYS D 430 ? 0.5240 0.2094 0.4601 0.0631  -0.0624 -0.0674 430 LYS D CB  
9328  C CG  . LYS D 430 ? 0.5473 0.2187 0.4716 0.0758  -0.0808 -0.0600 430 LYS D CG  
9329  C CD  . LYS D 430 ? 0.6005 0.2251 0.4825 0.0752  -0.0825 -0.0533 430 LYS D CD  
9330  C CE  . LYS D 430 ? 0.6273 0.2367 0.4929 0.0870  -0.1025 -0.0467 430 LYS D CE  
9331  N NZ  . LYS D 430 ? 0.5988 0.2339 0.4796 0.0894  -0.1100 -0.0456 430 LYS D NZ  
9332  N N   . SER D 431 ? 0.4204 0.2118 0.4343 0.0429  -0.0318 -0.0851 431 SER D N   
9333  C CA  . SER D 431 ? 0.4024 0.2161 0.4208 0.0270  -0.0136 -0.0885 431 SER D CA  
9334  C C   . SER D 431 ? 0.3597 0.2215 0.4049 0.0218  -0.0099 -0.0885 431 SER D C   
9335  O O   . SER D 431 ? 0.3426 0.2287 0.3968 0.0109  0.0024  -0.0927 431 SER D O   
9336  C CB  . SER D 431 ? 0.4097 0.2224 0.4365 0.0256  -0.0069 -0.0981 431 SER D CB  
9337  O OG  . SER D 431 ? 0.3928 0.2297 0.4515 0.0361  -0.0145 -0.1049 431 SER D OG  
9338  N N   . LEU D 432 ? 0.3610 0.2346 0.4168 0.0291  -0.0209 -0.0839 432 LEU D N   
9339  C CA  . LEU D 432 ? 0.3267 0.2401 0.4045 0.0244  -0.0186 -0.0832 432 LEU D CA  
9340  C C   . LEU D 432 ? 0.3192 0.2395 0.3851 0.0144  -0.0097 -0.0794 432 LEU D C   
9341  O O   . LEU D 432 ? 0.3369 0.2335 0.3796 0.0135  -0.0093 -0.0751 432 LEU D O   
9342  C CB  . LEU D 432 ? 0.3191 0.2387 0.4084 0.0334  -0.0325 -0.0797 432 LEU D CB  
9343  C CG  . LEU D 432 ? 0.3224 0.2454 0.4318 0.0439  -0.0423 -0.0863 432 LEU D CG  
9344  C CD1 . LEU D 432 ? 0.3105 0.2486 0.4357 0.0488  -0.0537 -0.0845 432 LEU D CD1 
9345  C CD2 . LEU D 432 ? 0.3086 0.2575 0.4402 0.0392  -0.0326 -0.0958 432 LEU D CD2 
9346  N N   . ILE D 433 ? 0.2900 0.2434 0.3717 0.0071  -0.0028 -0.0818 433 ILE D N   
9347  C CA  . ILE D 433 ? 0.2815 0.2474 0.3575 -0.0003 0.0038  -0.0803 433 ILE D CA  
9348  C C   . ILE D 433 ? 0.2599 0.2509 0.3496 0.0011  -0.0020 -0.0762 433 ILE D C   
9349  O O   . ILE D 433 ? 0.2591 0.2476 0.3421 0.0034  -0.0060 -0.0714 433 ILE D O   
9350  C CB  . ILE D 433 ? 0.2797 0.2585 0.3572 -0.0109 0.0166  -0.0877 433 ILE D CB  
9351  C CG1 . ILE D 433 ? 0.3066 0.2552 0.3670 -0.0141 0.0231  -0.0916 433 ILE D CG1 
9352  C CG2 . ILE D 433 ? 0.2708 0.2673 0.3470 -0.0169 0.0216  -0.0883 433 ILE D CG2 
9353  C CD1 . ILE D 433 ? 0.3087 0.2673 0.3678 -0.0269 0.0368  -0.0998 433 ILE D CD1 
9354  N N   . ARG D 434 ? 0.2591 0.2723 0.3658 -0.0008 -0.0020 -0.0786 434 ARG D N   
9355  C CA  . ARG D 434 ? 0.2393 0.2710 0.3551 -0.0009 -0.0075 -0.0742 434 ARG D CA  
9356  C C   . ARG D 434 ? 0.2365 0.2713 0.3659 0.0021  -0.0130 -0.0751 434 ARG D C   
9357  O O   . ARG D 434 ? 0.2355 0.2790 0.3760 0.0001  -0.0085 -0.0820 434 ARG D O   
9358  C CB  . ARG D 434 ? 0.2283 0.2848 0.3486 -0.0087 -0.0019 -0.0764 434 ARG D CB  
9359  C CG  . ARG D 434 ? 0.2258 0.2879 0.3389 -0.0083 -0.0042 -0.0727 434 ARG D CG  
9360  C CD  . ARG D 434 ? 0.2193 0.3048 0.3356 -0.0141 -0.0021 -0.0748 434 ARG D CD  
9361  N NE  . ARG D 434 ? 0.2178 0.3089 0.3334 -0.0136 -0.0100 -0.0680 434 ARG D NE  
9362  C CZ  . ARG D 434 ? 0.2204 0.3090 0.3296 -0.0087 -0.0178 -0.0624 434 ARG D CZ  
9363  N NH1 . ARG D 434 ? 0.2219 0.3064 0.3280 -0.0034 -0.0185 -0.0639 434 ARG D NH1 
9364  N NH2 . ARG D 434 ? 0.2244 0.3135 0.3293 -0.0098 -0.0246 -0.0559 434 ARG D NH2 
9365  N N   . VAL D 435 ? 0.2280 0.2573 0.3579 0.0066  -0.0224 -0.0696 435 VAL D N   
9366  C CA  . VAL D 435 ? 0.2260 0.2619 0.3715 0.0084  -0.0280 -0.0718 435 VAL D CA  
9367  C C   . VAL D 435 ? 0.2193 0.2673 0.3668 0.0029  -0.0309 -0.0665 435 VAL D C   
9368  O O   . VAL D 435 ? 0.2216 0.2600 0.3569 0.0046  -0.0357 -0.0595 435 VAL D O   
9369  C CB  . VAL D 435 ? 0.2381 0.2527 0.3814 0.0187  -0.0383 -0.0714 435 VAL D CB  
9370  C CG1 . VAL D 435 ? 0.2354 0.2626 0.4003 0.0207  -0.0444 -0.0766 435 VAL D CG1 
9371  C CG2 . VAL D 435 ? 0.2526 0.2469 0.3859 0.0237  -0.0362 -0.0747 435 VAL D CG2 
9372  N N   . ARG D 436 ? 0.2356 0.3029 0.3968 -0.0043 -0.0273 -0.0705 436 ARG D N   
9373  C CA  . ARG D 436 ? 0.2372 0.3123 0.3958 -0.0124 -0.0286 -0.0652 436 ARG D CA  
9374  C C   . ARG D 436 ? 0.2321 0.3204 0.4094 -0.0172 -0.0287 -0.0713 436 ARG D C   
9375  O O   . ARG D 436 ? 0.2235 0.3305 0.4129 -0.0243 -0.0202 -0.0792 436 ARG D O   
9376  C CB  . ARG D 436 ? 0.2409 0.3273 0.3904 -0.0209 -0.0215 -0.0635 436 ARG D CB  
9377  C CG  . ARG D 436 ? 0.2471 0.3257 0.3816 -0.0166 -0.0224 -0.0591 436 ARG D CG  
9378  C CD  . ARG D 436 ? 0.2574 0.3411 0.3791 -0.0224 -0.0236 -0.0533 436 ARG D CD  
9379  N NE  . ARG D 436 ? 0.2753 0.3481 0.3895 -0.0234 -0.0314 -0.0456 436 ARG D NE  
9380  C CZ  . ARG D 436 ? 0.2963 0.3609 0.3946 -0.0223 -0.0377 -0.0382 436 ARG D CZ  
9381  N NH1 . ARG D 436 ? 0.3060 0.3756 0.3966 -0.0195 -0.0382 -0.0381 436 ARG D NH1 
9382  N NH2 . ARG D 436 ? 0.3171 0.3677 0.4075 -0.0238 -0.0446 -0.0316 436 ARG D NH2 
9383  N N   . PHE D 437 ? 0.2295 0.3097 0.4099 -0.0142 -0.0378 -0.0690 437 PHE D N   
9384  C CA  . PHE D 437 ? 0.2305 0.3253 0.4307 -0.0198 -0.0387 -0.0759 437 PHE D CA  
9385  C C   . PHE D 437 ? 0.2378 0.3335 0.4294 -0.0329 -0.0379 -0.0699 437 PHE D C   
9386  O O   . PHE D 437 ? 0.2411 0.3483 0.4476 -0.0404 -0.0380 -0.0756 437 PHE D O   
9387  C CB  . PHE D 437 ? 0.2333 0.3190 0.4437 -0.0082 -0.0507 -0.0791 437 PHE D CB  
9388  C CG  . PHE D 437 ? 0.2326 0.3211 0.4580 0.0027  -0.0522 -0.0889 437 PHE D CG  
9389  C CD1 . PHE D 437 ? 0.2314 0.3148 0.4492 0.0063  -0.0457 -0.0896 437 PHE D CD1 
9390  C CD2 . PHE D 437 ? 0.2361 0.3309 0.4828 0.0100  -0.0615 -0.0980 437 PHE D CD2 
9391  C CE1 . PHE D 437 ? 0.2361 0.3164 0.4645 0.0168  -0.0479 -0.0983 437 PHE D CE1 
9392  C CE2 . PHE D 437 ? 0.2403 0.3339 0.4992 0.0224  -0.0653 -0.1071 437 PHE D CE2 
9393  C CZ  . PHE D 437 ? 0.2415 0.3257 0.4898 0.0258  -0.0583 -0.1067 437 PHE D CZ  
9394  N N   . LYS D 438 ? 0.2567 0.3398 0.4244 -0.0359 -0.0375 -0.0594 438 LYS D N   
9395  C CA  . LYS D 438 ? 0.2704 0.3434 0.4230 -0.0455 -0.0402 -0.0514 438 LYS D CA  
9396  C C   . LYS D 438 ? 0.2785 0.3677 0.4377 -0.0634 -0.0311 -0.0562 438 LYS D C   
9397  O O   . LYS D 438 ? 0.2746 0.3826 0.4418 -0.0697 -0.0208 -0.0632 438 LYS D O   
9398  C CB  . LYS D 438 ? 0.2774 0.3358 0.4042 -0.0436 -0.0419 -0.0411 438 LYS D CB  
9399  C CG  . LYS D 438 ? 0.2953 0.3321 0.4024 -0.0465 -0.0496 -0.0313 438 LYS D CG  
9400  C CD  . LYS D 438 ? 0.3090 0.3368 0.3919 -0.0493 -0.0499 -0.0231 438 LYS D CD  
9401  C CE  . LYS D 438 ? 0.3261 0.3270 0.3889 -0.0436 -0.0611 -0.0137 438 LYS D CE  
9402  N NZ  . LYS D 438 ? 0.3151 0.3097 0.3811 -0.0267 -0.0674 -0.0144 438 LYS D NZ  
9403  N N   . GLY D 439 ? 0.3176 0.3988 0.4725 -0.0727 -0.0342 -0.0533 439 GLY D N   
9404  C CA  . GLY D 439 ? 0.3338 0.4269 0.4906 -0.0932 -0.0245 -0.0575 439 GLY D CA  
9405  C C   . GLY D 439 ? 0.2997 0.4251 0.4906 -0.0979 -0.0161 -0.0742 439 GLY D C   
9406  O O   . GLY D 439 ? 0.2931 0.4370 0.4884 -0.1076 -0.0036 -0.0809 439 GLY D O   
9407  N N   . ASN D 440 ? 0.3163 0.4493 0.5318 -0.0903 -0.0236 -0.0822 440 ASN D N   
9408  C CA  . ASN D 440 ? 0.2830 0.4484 0.5354 -0.0920 -0.0185 -0.1003 440 ASN D CA  
9409  C C   . ASN D 440 ? 0.2755 0.4451 0.5466 -0.0924 -0.0278 -0.1064 440 ASN D C   
9410  O O   . ASN D 440 ? 0.2993 0.4468 0.5519 -0.0965 -0.0347 -0.0966 440 ASN D O   
9411  C CB  . ASN D 440 ? 0.2556 0.4290 0.5236 -0.0735 -0.0207 -0.1070 440 ASN D CB  
9412  C CG  . ASN D 440 ? 0.2547 0.4384 0.5171 -0.0788 -0.0072 -0.1093 440 ASN D CG  
9413  O OD1 . ASN D 440 ? 0.2532 0.4635 0.5339 -0.0899 0.0049  -0.1223 440 ASN D OD1 
9414  N ND2 . ASN D 440 ? 0.2658 0.4304 0.5036 -0.0717 -0.0088 -0.0981 440 ASN D ND2 
9415  N N   . SER D 441 ? 0.2706 0.4673 0.5768 -0.0869 -0.0285 -0.1229 441 SER D N   
9416  C CA  . SER D 441 ? 0.2755 0.4768 0.5970 -0.0833 -0.0380 -0.1289 441 SER D CA  
9417  C C   . SER D 441 ? 0.2648 0.4686 0.6047 -0.0586 -0.0509 -0.1361 441 SER D C   
9418  O O   . SER D 441 ? 0.2705 0.4906 0.6319 -0.0529 -0.0543 -0.1479 441 SER D O   
9419  C CB  . SER D 441 ? 0.2896 0.5146 0.6231 -0.0999 -0.0251 -0.1389 441 SER D CB  
9420  O OG  . SER D 441 ? 0.3070 0.5221 0.6183 -0.1239 -0.0156 -0.1307 441 SER D OG  
9421  N N   . PHE D 442 ? 0.2837 0.4697 0.6139 -0.0441 -0.0587 -0.1296 442 PHE D N   
9422  C CA  . PHE D 442 ? 0.2801 0.4596 0.6203 -0.0213 -0.0729 -0.1342 442 PHE D CA  
9423  C C   . PHE D 442 ? 0.2904 0.4583 0.6302 -0.0147 -0.0894 -0.1331 442 PHE D C   
9424  O O   . PHE D 442 ? 0.2930 0.4472 0.6179 -0.0238 -0.0930 -0.1244 442 PHE D O   
9425  C CB  . PHE D 442 ? 0.2762 0.4301 0.5929 -0.0094 -0.0751 -0.1232 442 PHE D CB  
9426  C CG  . PHE D 442 ? 0.2702 0.4352 0.5894 -0.0115 -0.0612 -0.1269 442 PHE D CG  
9427  C CD1 . PHE D 442 ? 0.2663 0.4495 0.6126 -0.0019 -0.0611 -0.1421 442 PHE D CD1 
9428  C CD2 . PHE D 442 ? 0.2694 0.4261 0.5639 -0.0221 -0.0494 -0.1161 442 PHE D CD2 
9429  C CE1 . PHE D 442 ? 0.2639 0.4562 0.6117 -0.0043 -0.0479 -0.1465 442 PHE D CE1 
9430  C CE2 . PHE D 442 ? 0.2647 0.4319 0.5605 -0.0247 -0.0371 -0.1203 442 PHE D CE2 
9431  C CZ  . PHE D 442 ? 0.2605 0.4452 0.5826 -0.0165 -0.0356 -0.1355 442 PHE D CZ  
9432  N N   . SER D 443 ? 0.2808 0.4519 0.6357 0.0017  -0.1003 -0.1425 443 SER D N   
9433  C CA  . SER D 443 ? 0.2932 0.4573 0.6497 0.0079  -0.1156 -0.1443 443 SER D CA  
9434  C C   . SER D 443 ? 0.3025 0.4463 0.6542 0.0315  -0.1332 -0.1452 443 SER D C   
9435  O O   . SER D 443 ? 0.3006 0.4385 0.6514 0.0424  -0.1328 -0.1464 443 SER D O   
9436  C CB  . SER D 443 ? 0.3014 0.4957 0.6837 -0.0007 -0.1104 -0.1583 443 SER D CB  
9437  O OG  . SER D 443 ? 0.3015 0.5175 0.7057 0.0049  -0.1030 -0.1719 443 SER D OG  
9438  N N   . GLY D 444 ? 0.3808 0.5108 0.7258 0.0384  -0.1488 -0.1443 444 GLY D N   
9439  C CA  . GLY D 444 ? 0.4001 0.5059 0.7339 0.0591  -0.1668 -0.1446 444 GLY D CA  
9440  C C   . GLY D 444 ? 0.4048 0.4749 0.7047 0.0631  -0.1784 -0.1307 444 GLY D C   
9441  O O   . GLY D 444 ? 0.3957 0.4601 0.6829 0.0514  -0.1735 -0.1213 444 GLY D O   
9442  N N   . ASP D 445 ? 0.4281 0.4713 0.7101 0.0795  -0.1940 -0.1298 445 ASP D N   
9443  C CA  . ASP D 445 ? 0.4429 0.4487 0.6873 0.0839  -0.2041 -0.1174 445 ASP D CA  
9444  C C   . ASP D 445 ? 0.4360 0.4212 0.6562 0.0850  -0.1962 -0.1054 445 ASP D C   
9445  O O   . ASP D 445 ? 0.4407 0.4183 0.6569 0.0928  -0.1936 -0.1061 445 ASP D O   
9446  C CB  . ASP D 445 ? 0.4753 0.4573 0.7033 0.0983  -0.2216 -0.1206 445 ASP D CB  
9447  C CG  . ASP D 445 ? 0.4948 0.4421 0.6848 0.0996  -0.2312 -0.1103 445 ASP D CG  
9448  O OD1 . ASP D 445 ? 0.4904 0.4200 0.6562 0.0947  -0.2242 -0.0985 445 ASP D OD1 
9449  O OD2 . ASP D 445 ? 0.5184 0.4565 0.7027 0.1056  -0.2453 -0.1151 445 ASP D OD2 
9450  N N   . ILE D 446 ? 0.4468 0.4221 0.6499 0.0766  -0.1914 -0.0949 446 ILE D N   
9451  C CA  . ILE D 446 ? 0.4427 0.3996 0.6193 0.0736  -0.1761 -0.0837 446 ILE D CA  
9452  C C   . ILE D 446 ? 0.4672 0.3880 0.6126 0.0869  -0.1832 -0.0785 446 ILE D C   
9453  O O   . ILE D 446 ? 0.4689 0.3801 0.6028 0.0878  -0.1725 -0.0749 446 ILE D O   
9454  C CB  . ILE D 446 ? 0.4368 0.3861 0.5951 0.0616  -0.1671 -0.0743 446 ILE D CB  
9455  C CG1 . ILE D 446 ? 0.4323 0.3679 0.5678 0.0593  -0.1520 -0.0651 446 ILE D CG1 
9456  C CG2 . ILE D 446 ? 0.4563 0.3827 0.5941 0.0652  -0.1809 -0.0714 446 ILE D CG2 
9457  C CD1 . ILE D 446 ? 0.4120 0.3729 0.5656 0.0500  -0.1363 -0.0665 446 ILE D CD1 
9458  N N   . SER D 447 ? 0.4876 0.3868 0.6128 0.0929  -0.1976 -0.0782 447 SER D N   
9459  C CA  . SER D 447 ? 0.5179 0.3828 0.6049 0.0993  -0.2007 -0.0730 447 SER D CA  
9460  C C   . SER D 447 ? 0.5304 0.3978 0.6270 0.1081  -0.2061 -0.0801 447 SER D C   
9461  O O   . SER D 447 ? 0.5555 0.3965 0.6228 0.1121  -0.2052 -0.0748 447 SER D O   
9462  C CB  . SER D 447 ? 0.5453 0.3864 0.6041 0.1011  -0.2136 -0.0707 447 SER D CB  
9463  O OG  . SER D 447 ? 0.5621 0.4151 0.6410 0.1064  -0.2290 -0.0811 447 SER D OG  
9464  N N   . GLU D 448 ? 0.5063 0.4049 0.6428 0.1105  -0.2110 -0.0925 448 GLU D N   
9465  C CA  . GLU D 448 ? 0.5172 0.4216 0.6673 0.1194  -0.2152 -0.1014 448 GLU D CA  
9466  C C   . GLU D 448 ? 0.4934 0.4176 0.6655 0.1167  -0.1999 -0.1041 448 GLU D C   
9467  O O   . GLU D 448 ? 0.5075 0.4296 0.6834 0.1240  -0.2010 -0.1093 448 GLU D O   
9468  C CB  . GLU D 448 ? 0.5217 0.4512 0.7049 0.1238  -0.2270 -0.1162 448 GLU D CB  
9469  C CG  . GLU D 448 ? 0.5667 0.4725 0.7290 0.1336  -0.2465 -0.1182 448 GLU D CG  
9470  C CD  . GLU D 448 ? 0.5690 0.5028 0.7667 0.1366  -0.2564 -0.1334 448 GLU D CD  
9471  O OE1 . GLU D 448 ? 0.5397 0.5117 0.7785 0.1324  -0.2473 -0.1440 448 GLU D OE1 
9472  O OE2 . GLU D 448 ? 0.5915 0.5099 0.7755 0.1426  -0.2721 -0.1353 448 GLU D OE2 
9473  N N   . ALA D 449 ? 0.4392 0.3812 0.6246 0.1066  -0.1862 -0.1010 449 ALA D N   
9474  C CA  . ALA D 449 ? 0.4157 0.3812 0.6257 0.1029  -0.1715 -0.1057 449 ALA D CA  
9475  C C   . ALA D 449 ? 0.4224 0.3610 0.6042 0.1037  -0.1612 -0.0971 449 ALA D C   
9476  O O   . ALA D 449 ? 0.4219 0.3662 0.6140 0.1061  -0.1543 -0.1027 449 ALA D O   
9477  C CB  . ALA D 449 ? 0.3851 0.3823 0.6170 0.0880  -0.1597 -0.1059 449 ALA D CB  
9478  N N   . PHE D 450 ? 0.4040 0.3136 0.5501 0.1002  -0.1586 -0.0847 450 PHE D N   
9479  C CA  . PHE D 450 ? 0.4093 0.2962 0.5293 0.0969  -0.1456 -0.0776 450 PHE D CA  
9480  C C   . PHE D 450 ? 0.4462 0.2930 0.5223 0.1006  -0.1510 -0.0694 450 PHE D C   
9481  O O   . PHE D 450 ? 0.4629 0.2958 0.5204 0.1023  -0.1618 -0.0653 450 PHE D O   
9482  C CB  . PHE D 450 ? 0.3906 0.2869 0.5020 0.0822  -0.1303 -0.0700 450 PHE D CB  
9483  C CG  . PHE D 450 ? 0.3624 0.2987 0.5051 0.0719  -0.1201 -0.0744 450 PHE D CG  
9484  C CD1 . PHE D 450 ? 0.3544 0.3081 0.5105 0.0668  -0.1068 -0.0788 450 PHE D CD1 
9485  C CD2 . PHE D 450 ? 0.3497 0.3034 0.5053 0.0661  -0.1236 -0.0743 450 PHE D CD2 
9486  C CE1 . PHE D 450 ? 0.3348 0.3222 0.5145 0.0561  -0.0972 -0.0825 450 PHE D CE1 
9487  C CE2 . PHE D 450 ? 0.3288 0.3142 0.5074 0.0547  -0.1137 -0.0776 450 PHE D CE2 
9488  C CZ  . PHE D 450 ? 0.3215 0.3236 0.5111 0.0496  -0.1005 -0.0815 450 PHE D CZ  
9489  N N   . GLY D 451 ? 0.4320 0.2595 0.4909 0.1010  -0.1432 -0.0677 451 GLY D N   
9490  C CA  . GLY D 451 ? 0.4701 0.2569 0.4847 0.1020  -0.1449 -0.0594 451 GLY D CA  
9491  C C   . GLY D 451 ? 0.4717 0.2399 0.4583 0.0915  -0.1304 -0.0520 451 GLY D C   
9492  O O   . GLY D 451 ? 0.4498 0.2317 0.4439 0.0858  -0.1258 -0.0509 451 GLY D O   
9493  N N   . VAL D 452 ? 0.4840 0.2201 0.4383 0.0884  -0.1229 -0.0479 452 VAL D N   
9494  C CA  . VAL D 452 ? 0.4894 0.2075 0.4175 0.0768  -0.1073 -0.0438 452 VAL D CA  
9495  C C   . VAL D 452 ? 0.4744 0.2008 0.4155 0.0702  -0.0921 -0.0495 452 VAL D C   
9496  O O   . VAL D 452 ? 0.4793 0.2062 0.4307 0.0744  -0.0927 -0.0536 452 VAL D O   
9497  C CB  . VAL D 452 ? 0.5366 0.2111 0.4160 0.0743  -0.1076 -0.0366 452 VAL D CB  
9498  C CG1 . VAL D 452 ? 0.5502 0.2167 0.4134 0.0781  -0.1206 -0.0322 452 VAL D CG1 
9499  C CG2 . VAL D 452 ? 0.5677 0.2212 0.4360 0.0806  -0.1137 -0.0365 452 VAL D CG2 
9500  N N   . TYR D 453 ? 0.4714 0.2163 0.4145 0.0575  -0.0758 -0.0491 453 TYR D N   
9501  C CA  . TYR D 453 ? 0.4649 0.2319 0.4229 0.0475  -0.0589 -0.0539 453 TYR D CA  
9502  C C   . TYR D 453 ? 0.4809 0.2394 0.4152 0.0337  -0.0423 -0.0525 453 TYR D C   
9503  O O   . TYR D 453 ? 0.4695 0.2526 0.4128 0.0280  -0.0357 -0.0525 453 TYR D O   
9504  C CB  . TYR D 453 ? 0.4308 0.2464 0.4292 0.0462  -0.0567 -0.0575 453 TYR D CB  
9505  C CG  . TYR D 453 ? 0.4090 0.2390 0.4335 0.0573  -0.0715 -0.0604 453 TYR D CG  
9506  C CD1 . TYR D 453 ? 0.4065 0.2384 0.4466 0.0637  -0.0749 -0.0671 453 TYR D CD1 
9507  C CD2 . TYR D 453 ? 0.3952 0.2382 0.4302 0.0606  -0.0813 -0.0580 453 TYR D CD2 
9508  C CE1 . TYR D 453 ? 0.3909 0.2408 0.4589 0.0733  -0.0873 -0.0724 453 TYR D CE1 
9509  C CE2 . TYR D 453 ? 0.3796 0.2392 0.4409 0.0686  -0.0936 -0.0626 453 TYR D CE2 
9510  C CZ  . TYR D 453 ? 0.3777 0.2425 0.4566 0.0749  -0.0963 -0.0703 453 TYR D CZ  
9511  O OH  . TYR D 453 ? 0.3655 0.2513 0.4744 0.0825  -0.1075 -0.0776 453 TYR D OH  
9512  N N   . PRO D 454 ? 0.4763 0.1994 0.3798 0.0278  -0.0351 -0.0524 454 PRO D N   
9513  C CA  . PRO D 454 ? 0.4886 0.2041 0.3690 0.0126  -0.0177 -0.0531 454 PRO D CA  
9514  C C   . PRO D 454 ? 0.4701 0.2278 0.3770 0.0019  -0.0020 -0.0599 454 PRO D C   
9515  O O   . PRO D 454 ? 0.4735 0.2402 0.3735 -0.0085 0.0104  -0.0624 454 PRO D O   
9516  C CB  . PRO D 454 ? 0.5384 0.2040 0.3800 0.0076  -0.0139 -0.0519 454 PRO D CB  
9517  C CG  . PRO D 454 ? 0.5558 0.1980 0.3967 0.0243  -0.0338 -0.0491 454 PRO D CG  
9518  C CD  . PRO D 454 ? 0.5089 0.1977 0.3979 0.0341  -0.0418 -0.0528 454 PRO D CD  
9519  N N   . THR D 455 ? 0.4337 0.2180 0.3704 0.0041  -0.0022 -0.0640 455 THR D N   
9520  C CA  . THR D 455 ? 0.4167 0.2400 0.3767 -0.0053 0.0105  -0.0705 455 THR D CA  
9521  C C   . THR D 455 ? 0.3812 0.2451 0.3733 0.0005  0.0039  -0.0699 455 THR D C   
9522  O O   . THR D 455 ? 0.3569 0.2531 0.3694 -0.0048 0.0107  -0.0747 455 THR D O   
9523  C CB  . THR D 455 ? 0.4174 0.2396 0.3829 -0.0101 0.0174  -0.0765 455 THR D CB  
9524  O OG1 . THR D 455 ? 0.4119 0.2340 0.3930 0.0021  0.0051  -0.0761 455 THR D OG1 
9525  C CG2 . THR D 455 ? 0.4533 0.2320 0.3831 -0.0188 0.0259  -0.0772 455 THR D CG2 
9526  N N   . LEU D 456 ? 0.4035 0.2645 0.3982 0.0105  -0.0095 -0.0643 456 LEU D N   
9527  C CA  . LEU D 456 ? 0.3699 0.2636 0.3908 0.0145  -0.0155 -0.0631 456 LEU D CA  
9528  C C   . LEU D 456 ? 0.3634 0.2777 0.3872 0.0093  -0.0089 -0.0640 456 LEU D C   
9529  O O   . LEU D 456 ? 0.3775 0.2783 0.3837 0.0079  -0.0063 -0.0632 456 LEU D O   
9530  C CB  . LEU D 456 ? 0.3695 0.2530 0.3911 0.0248  -0.0311 -0.0580 456 LEU D CB  
9531  C CG  . LEU D 456 ? 0.3439 0.2561 0.3918 0.0277  -0.0380 -0.0572 456 LEU D CG  
9532  C CD1 . LEU D 456 ? 0.3321 0.2646 0.4019 0.0260  -0.0350 -0.0623 456 LEU D CD1 
9533  C CD2 . LEU D 456 ? 0.3404 0.2407 0.3873 0.0362  -0.0528 -0.0536 456 LEU D CD2 
9534  N N   . ASN D 457 ? 0.3371 0.2835 0.3822 0.0069  -0.0068 -0.0663 457 ASN D N   
9535  C CA  . ASN D 457 ? 0.3298 0.2981 0.3807 0.0044  -0.0032 -0.0681 457 ASN D CA  
9536  C C   . ASN D 457 ? 0.3178 0.3002 0.3807 0.0104  -0.0136 -0.0631 457 ASN D C   
9537  O O   . ASN D 457 ? 0.3170 0.2993 0.3761 0.0140  -0.0170 -0.0616 457 ASN D O   
9538  C CB  . ASN D 457 ? 0.3178 0.3095 0.3791 -0.0038 0.0071  -0.0754 457 ASN D CB  
9539  C CG  . ASN D 457 ? 0.3089 0.3268 0.3798 -0.0040 0.0077  -0.0784 457 ASN D CG  
9540  O OD1 . ASN D 457 ? 0.2962 0.3329 0.3793 -0.0013 0.0013  -0.0762 457 ASN D OD1 
9541  N ND2 . ASN D 457 ? 0.3115 0.3299 0.3759 -0.0072 0.0152  -0.0843 457 ASN D ND2 
9542  N N   . PHE D 458 ? 0.2794 0.2728 0.3558 0.0107  -0.0181 -0.0613 458 PHE D N   
9543  C CA  . PHE D 458 ? 0.2648 0.2697 0.3498 0.0131  -0.0264 -0.0566 458 PHE D CA  
9544  C C   . PHE D 458 ? 0.2641 0.2649 0.3570 0.0145  -0.0326 -0.0546 458 PHE D C   
9545  O O   . PHE D 458 ? 0.2627 0.2674 0.3634 0.0123  -0.0289 -0.0587 458 PHE D O   
9546  C CB  . PHE D 458 ? 0.2535 0.2833 0.3474 0.0084  -0.0232 -0.0584 458 PHE D CB  
9547  C CG  . PHE D 458 ? 0.2508 0.2865 0.3463 0.0100  -0.0316 -0.0526 458 PHE D CG  
9548  C CD1 . PHE D 458 ? 0.2494 0.2855 0.3501 0.0074  -0.0358 -0.0489 458 PHE D CD1 
9549  C CD2 . PHE D 458 ? 0.2526 0.2933 0.3441 0.0137  -0.0351 -0.0517 458 PHE D CD2 
9550  C CE1 . PHE D 458 ? 0.2526 0.2895 0.3503 0.0065  -0.0426 -0.0431 458 PHE D CE1 
9551  C CE2 . PHE D 458 ? 0.2563 0.2962 0.3450 0.0155  -0.0439 -0.0456 458 PHE D CE2 
9552  C CZ  . PHE D 458 ? 0.2576 0.2936 0.3472 0.0109  -0.0472 -0.0406 458 PHE D CZ  
9553  N N   . ILE D 459 ? 0.2838 0.2779 0.3762 0.0181  -0.0419 -0.0497 459 ILE D N   
9554  C CA  . ILE D 459 ? 0.2745 0.2691 0.3778 0.0187  -0.0483 -0.0496 459 ILE D CA  
9555  C C   . ILE D 459 ? 0.2660 0.2650 0.3714 0.0165  -0.0546 -0.0448 459 ILE D C   
9556  O O   . ILE D 459 ? 0.2727 0.2608 0.3670 0.0197  -0.0591 -0.0407 459 ILE D O   
9557  C CB  . ILE D 459 ? 0.2879 0.2610 0.3852 0.0258  -0.0552 -0.0503 459 ILE D CB  
9558  C CG1 . ILE D 459 ? 0.2756 0.2546 0.3893 0.0272  -0.0633 -0.0525 459 ILE D CG1 
9559  C CG2 . ILE D 459 ? 0.2987 0.2521 0.3775 0.0301  -0.0599 -0.0461 459 ILE D CG2 
9560  C CD1 . ILE D 459 ? 0.2845 0.2479 0.3977 0.0355  -0.0703 -0.0562 459 ILE D CD1 
9561  N N   . ASP D 460 ? 0.2837 0.2974 0.4021 0.0101  -0.0540 -0.0460 460 ASP D N   
9562  C CA  . ASP D 460 ? 0.2884 0.3038 0.4058 0.0047  -0.0584 -0.0413 460 ASP D CA  
9563  C C   . ASP D 460 ? 0.2849 0.3092 0.4189 -0.0001 -0.0603 -0.0456 460 ASP D C   
9564  O O   . ASP D 460 ? 0.2822 0.3246 0.4285 -0.0074 -0.0533 -0.0505 460 ASP D O   
9565  C CB  . ASP D 460 ? 0.2938 0.3197 0.4056 -0.0020 -0.0534 -0.0384 460 ASP D CB  
9566  C CG  . ASP D 460 ? 0.3139 0.3315 0.4155 -0.0063 -0.0593 -0.0315 460 ASP D CG  
9567  O OD1 . ASP D 460 ? 0.3219 0.3269 0.4224 -0.0049 -0.0662 -0.0296 460 ASP D OD1 
9568  O OD2 . ASP D 460 ? 0.3279 0.3493 0.4204 -0.0113 -0.0577 -0.0280 460 ASP D OD2 
9569  N N   . LEU D 461 ? 0.2666 0.2798 0.4017 0.0034  -0.0694 -0.0452 461 LEU D N   
9570  C CA  . LEU D 461 ? 0.2603 0.2842 0.4142 -0.0005 -0.0729 -0.0513 461 LEU D CA  
9571  C C   . LEU D 461 ? 0.2744 0.2980 0.4262 -0.0111 -0.0750 -0.0480 461 LEU D C   
9572  O O   . LEU D 461 ? 0.2712 0.3014 0.4373 -0.0150 -0.0794 -0.0533 461 LEU D O   
9573  C CB  . LEU D 461 ? 0.2568 0.2690 0.4139 0.0106  -0.0834 -0.0547 461 LEU D CB  
9574  C CG  . LEU D 461 ? 0.2573 0.2590 0.4079 0.0212  -0.0830 -0.0562 461 LEU D CG  
9575  C CD1 . LEU D 461 ? 0.2647 0.2473 0.4095 0.0317  -0.0958 -0.0572 461 LEU D CD1 
9576  C CD2 . LEU D 461 ? 0.2464 0.2661 0.4148 0.0203  -0.0759 -0.0643 461 LEU D CD2 
9577  N N   . SER D 462 ? 0.2951 0.3103 0.4289 -0.0160 -0.0724 -0.0399 462 SER D N   
9578  C CA  . SER D 462 ? 0.3172 0.3221 0.4411 -0.0252 -0.0758 -0.0348 462 SER D CA  
9579  C C   . SER D 462 ? 0.3213 0.3439 0.4586 -0.0414 -0.0692 -0.0399 462 SER D C   
9580  O O   . SER D 462 ? 0.3095 0.3532 0.4598 -0.0463 -0.0601 -0.0460 462 SER D O   
9581  C CB  . SER D 462 ? 0.3403 0.3305 0.4406 -0.0249 -0.0757 -0.0255 462 SER D CB  
9582  O OG  . SER D 462 ? 0.3297 0.3129 0.4229 -0.0113 -0.0779 -0.0241 462 SER D OG  
9583  N N   . ASN D 463 ? 0.3522 0.3657 0.4858 -0.0509 -0.0730 -0.0385 463 ASN D N   
9584  C CA  . ASN D 463 ? 0.3621 0.3904 0.5060 -0.0699 -0.0656 -0.0439 463 ASN D CA  
9585  C C   . ASN D 463 ? 0.3275 0.3873 0.5059 -0.0699 -0.0619 -0.0585 463 ASN D C   
9586  O O   . ASN D 463 ? 0.3188 0.4009 0.5093 -0.0783 -0.0507 -0.0652 463 ASN D O   
9587  C CB  . ASN D 463 ? 0.3930 0.4198 0.5182 -0.0827 -0.0557 -0.0379 463 ASN D CB  
9588  C CG  . ASN D 463 ? 0.4277 0.4226 0.5194 -0.0793 -0.0621 -0.0241 463 ASN D CG  
9589  O OD1 . ASN D 463 ? 0.4375 0.4103 0.5190 -0.0752 -0.0715 -0.0196 463 ASN D OD1 
9590  N ND2 . ASN D 463 ? 0.4520 0.4448 0.5269 -0.0802 -0.0579 -0.0184 463 ASN D ND2 
9591  N N   . ASN D 464 ? 0.3657 0.4262 0.5592 -0.0592 -0.0724 -0.0642 464 ASN D N   
9592  C CA  . ASN D 464 ? 0.3338 0.4213 0.5608 -0.0547 -0.0735 -0.0789 464 ASN D CA  
9593  C C   . ASN D 464 ? 0.3290 0.4168 0.5691 -0.0542 -0.0853 -0.0851 464 ASN D C   
9594  O O   . ASN D 464 ? 0.3502 0.4182 0.5734 -0.0602 -0.0901 -0.0783 464 ASN D O   
9595  C CB  . ASN D 464 ? 0.3152 0.4010 0.5444 -0.0359 -0.0765 -0.0797 464 ASN D CB  
9596  C CG  . ASN D 464 ? 0.3094 0.4095 0.5410 -0.0392 -0.0634 -0.0817 464 ASN D CG  
9597  O OD1 . ASN D 464 ? 0.2932 0.4202 0.5492 -0.0448 -0.0560 -0.0939 464 ASN D OD1 
9598  N ND2 . ASN D 464 ? 0.3210 0.4050 0.5284 -0.0357 -0.0602 -0.0712 464 ASN D ND2 
9599  N N   . ASN D 465 ? 0.3606 0.4704 0.6312 -0.0461 -0.0912 -0.0988 465 ASN D N   
9600  C CA  . ASN D 465 ? 0.3657 0.4828 0.6547 -0.0455 -0.1035 -0.1081 465 ASN D CA  
9601  C C   . ASN D 465 ? 0.3630 0.4703 0.6548 -0.0227 -0.1203 -0.1102 465 ASN D C   
9602  O O   . ASN D 465 ? 0.3714 0.4938 0.6840 -0.0152 -0.1277 -0.1213 465 ASN D O   
9603  C CB  . ASN D 465 ? 0.3661 0.5194 0.6853 -0.0573 -0.0942 -0.1231 465 ASN D CB  
9604  C CG  . ASN D 465 ? 0.3880 0.5433 0.7019 -0.0817 -0.0860 -0.1224 465 ASN D CG  
9605  O OD1 . ASN D 465 ? 0.4030 0.5515 0.7158 -0.0850 -0.0945 -0.1234 465 ASN D OD1 
9606  N ND2 . ASN D 465 ? 0.3937 0.5558 0.7013 -0.0998 -0.0693 -0.1206 465 ASN D ND2 
9607  N N   . PHE D 466 ? 0.3512 0.4286 0.6133 -0.0105 -0.1233 -0.0976 466 PHE D N   
9608  C CA  . PHE D 466 ? 0.3567 0.4167 0.6117 0.0089  -0.1385 -0.0974 466 PHE D CA  
9609  C C   . PHE D 466 ? 0.3713 0.4139 0.6149 0.0099  -0.1523 -0.0954 466 PHE D C   
9610  O O   . PHE D 466 ? 0.3777 0.4015 0.5987 0.0021  -0.1494 -0.0859 466 PHE D O   
9611  C CB  . PHE D 466 ? 0.3561 0.3909 0.5823 0.0185  -0.1341 -0.0859 466 PHE D CB  
9612  C CG  . PHE D 466 ? 0.3445 0.3935 0.5808 0.0201  -0.1230 -0.0891 466 PHE D CG  
9613  C CD1 . PHE D 466 ? 0.3443 0.4055 0.6021 0.0310  -0.1286 -0.1002 466 PHE D CD1 
9614  C CD2 . PHE D 466 ? 0.3375 0.3863 0.5613 0.0116  -0.1083 -0.0818 466 PHE D CD2 
9615  C CE1 . PHE D 466 ? 0.3359 0.4083 0.6023 0.0325  -0.1182 -0.1041 466 PHE D CE1 
9616  C CE2 . PHE D 466 ? 0.3284 0.3899 0.5605 0.0123  -0.0981 -0.0857 466 PHE D CE2 
9617  C CZ  . PHE D 466 ? 0.3270 0.3999 0.5803 0.0224  -0.1024 -0.0969 466 PHE D CZ  
9618  N N   . HIS D 467 ? 0.3915 0.4398 0.6506 0.0201  -0.1684 -0.1052 467 HIS D N   
9619  C CA  . HIS D 467 ? 0.4091 0.4390 0.6543 0.0233  -0.1823 -0.1038 467 HIS D CA  
9620  C C   . HIS D 467 ? 0.4232 0.4244 0.6451 0.0427  -0.1961 -0.0995 467 HIS D C   
9621  O O   . HIS D 467 ? 0.4205 0.4168 0.6390 0.0532  -0.1951 -0.0981 467 HIS D O   
9622  C CB  . HIS D 467 ? 0.4169 0.4712 0.6874 0.0187  -0.1846 -0.1160 467 HIS D CB  
9623  C CG  . HIS D 467 ? 0.4295 0.4957 0.7177 0.0343  -0.1919 -0.1265 467 HIS D CG  
9624  N ND1 . HIS D 467 ? 0.4132 0.5065 0.7273 0.0348  -0.1823 -0.1356 467 HIS D ND1 
9625  C CD2 . HIS D 467 ? 0.4513 0.5033 0.7327 0.0498  -0.2084 -0.1299 467 HIS D CD2 
9626  C CE1 . HIS D 467 ? 0.4268 0.5213 0.7503 0.0509  -0.1934 -0.1446 467 HIS D CE1 
9627  N NE2 . HIS D 467 ? 0.4459 0.5150 0.7492 0.0601  -0.2097 -0.1409 467 HIS D NE2 
9628  N N   . GLY D 468 ? 0.4411 0.4209 0.6437 0.0462  -0.2080 -0.0972 468 GLY D N   
9629  C CA  . GLY D 468 ? 0.4618 0.4095 0.6350 0.0618  -0.2198 -0.0925 468 GLY D CA  
9630  C C   . GLY D 468 ? 0.4671 0.3834 0.6031 0.0614  -0.2165 -0.0800 468 GLY D C   
9631  O O   . GLY D 468 ? 0.4573 0.3736 0.5877 0.0500  -0.2035 -0.0743 468 GLY D O   
9632  N N   . GLN D 469 ? 0.5170 0.4031 0.6228 0.0735  -0.2243 -0.0755 469 GLN D N   
9633  C CA  . GLN D 469 ? 0.5281 0.3828 0.5949 0.0734  -0.2172 -0.0651 469 GLN D CA  
9634  C C   . GLN D 469 ? 0.5243 0.3696 0.5778 0.0772  -0.2045 -0.0593 469 GLN D C   
9635  O O   . GLN D 469 ? 0.5242 0.3758 0.5877 0.0831  -0.2059 -0.0626 469 GLN D O   
9636  C CB  . GLN D 469 ? 0.5606 0.3850 0.5958 0.0796  -0.2309 -0.0648 469 GLN D CB  
9637  C CG  . GLN D 469 ? 0.5700 0.4041 0.6209 0.0784  -0.2449 -0.0734 469 GLN D CG  
9638  C CD  . GLN D 469 ? 0.6044 0.4070 0.6206 0.0817  -0.2553 -0.0724 469 GLN D CD  
9639  O OE1 . GLN D 469 ? 0.6196 0.3937 0.5984 0.0837  -0.2517 -0.0659 469 GLN D OE1 
9640  N NE2 . GLN D 469 ? 0.6204 0.4299 0.6488 0.0812  -0.2664 -0.0793 469 GLN D NE2 
9641  N N   . LEU D 470 ? 0.4911 0.3225 0.5219 0.0726  -0.1910 -0.0519 470 LEU D N   
9642  C CA  . LEU D 470 ? 0.4877 0.3120 0.5060 0.0736  -0.1773 -0.0475 470 LEU D CA  
9643  C C   . LEU D 470 ? 0.5165 0.3151 0.5042 0.0797  -0.1818 -0.0459 470 LEU D C   
9644  O O   . LEU D 470 ? 0.5412 0.3175 0.5001 0.0805  -0.1878 -0.0442 470 LEU D O   
9645  C CB  . LEU D 470 ? 0.4840 0.3039 0.4878 0.0669  -0.1623 -0.0424 470 LEU D CB  
9646  C CG  . LEU D 470 ? 0.4606 0.3060 0.4876 0.0583  -0.1531 -0.0420 470 LEU D CG  
9647  C CD1 . LEU D 470 ? 0.4579 0.3014 0.4731 0.0555  -0.1381 -0.0380 470 LEU D CD1 
9648  C CD2 . LEU D 470 ? 0.4407 0.3138 0.4990 0.0556  -0.1511 -0.0457 470 LEU D CD2 
9649  N N   . SER D 471 ? 0.5205 0.3213 0.5124 0.0829  -0.1784 -0.0466 471 SER D N   
9650  C CA  . SER D 471 ? 0.5517 0.3252 0.5109 0.0869  -0.1807 -0.0438 471 SER D CA  
9651  C C   . SER D 471 ? 0.5623 0.3136 0.4890 0.0818  -0.1658 -0.0374 471 SER D C   
9652  O O   . SER D 471 ? 0.5427 0.3045 0.4790 0.0766  -0.1516 -0.0366 471 SER D O   
9653  C CB  . SER D 471 ? 0.5512 0.3313 0.5243 0.0919  -0.1812 -0.0469 471 SER D CB  
9654  O OG  . SER D 471 ? 0.5868 0.3358 0.5243 0.0946  -0.1812 -0.0427 471 SER D OG  
9655  N N   . ALA D 472 ? 0.5542 0.2736 0.4416 0.0830  -0.1695 -0.0342 472 ALA D N   
9656  C CA  . ALA D 472 ? 0.5707 0.2658 0.4253 0.0772  -0.1544 -0.0300 472 ALA D CA  
9657  C C   . ALA D 472 ? 0.5717 0.2618 0.4245 0.0752  -0.1430 -0.0289 472 ALA D C   
9658  O O   . ALA D 472 ? 0.5890 0.2572 0.4141 0.0687  -0.1293 -0.0269 472 ALA D O   
9659  C CB  . ALA D 472 ? 0.6154 0.2738 0.4241 0.0777  -0.1614 -0.0272 472 ALA D CB  
9660  N N   . ASN D 473 ? 0.5906 0.2995 0.4718 0.0799  -0.1476 -0.0315 473 ASN D N   
9661  C CA  . ASN D 473 ? 0.5920 0.2961 0.4732 0.0783  -0.1373 -0.0314 473 ASN D CA  
9662  C C   . ASN D 473 ? 0.5710 0.2863 0.4622 0.0700  -0.1187 -0.0330 473 ASN D C   
9663  O O   . ASN D 473 ? 0.5915 0.2924 0.4687 0.0647  -0.1064 -0.0332 473 ASN D O   
9664  C CB  . ASN D 473 ? 0.5845 0.3100 0.4986 0.0859  -0.1463 -0.0362 473 ASN D CB  
9665  C CG  . ASN D 473 ? 0.6175 0.3261 0.5175 0.0949  -0.1639 -0.0366 473 ASN D CG  
9666  O OD1 . ASN D 473 ? 0.6526 0.3293 0.5136 0.0949  -0.1690 -0.0321 473 ASN D OD1 
9667  N ND2 . ASN D 473 ? 0.6007 0.3302 0.5321 0.1025  -0.1738 -0.0434 473 ASN D ND2 
9668  N N   . TRP D 474 ? 0.5363 0.2767 0.4508 0.0681  -0.1168 -0.0351 474 TRP D N   
9669  C CA  . TRP D 474 ? 0.5170 0.2832 0.4460 0.0588  -0.0985 -0.0367 474 TRP D CA  
9670  C C   . TRP D 474 ? 0.5395 0.2880 0.4384 0.0506  -0.0838 -0.0363 474 TRP D C   
9671  O O   . TRP D 474 ? 0.5353 0.3003 0.4423 0.0429  -0.0682 -0.0390 474 TRP D O   
9672  C CB  . TRP D 474 ? 0.4888 0.2844 0.4431 0.0578  -0.1000 -0.0374 474 TRP D CB  
9673  C CG  . TRP D 474 ? 0.4668 0.2841 0.4523 0.0618  -0.1109 -0.0392 474 TRP D CG  
9674  C CD1 . TRP D 474 ? 0.4659 0.2836 0.4587 0.0665  -0.1258 -0.0398 474 TRP D CD1 
9675  C CD2 . TRP D 474 ? 0.4488 0.2920 0.4628 0.0601  -0.1063 -0.0424 474 TRP D CD2 
9676  N NE1 . TRP D 474 ? 0.4500 0.2941 0.4756 0.0669  -0.1299 -0.0438 474 TRP D NE1 
9677  C CE2 . TRP D 474 ? 0.4340 0.2935 0.4722 0.0632  -0.1179 -0.0453 474 TRP D CE2 
9678  C CE3 . TRP D 474 ? 0.4467 0.3017 0.4679 0.0552  -0.0931 -0.0442 474 TRP D CE3 
9679  C CZ2 . TRP D 474 ? 0.4176 0.3048 0.4863 0.0613  -0.1153 -0.0502 474 TRP D CZ2 
9680  C CZ3 . TRP D 474 ? 0.4310 0.3116 0.4808 0.0542  -0.0917 -0.0484 474 TRP D CZ3 
9681  C CH2 . TRP D 474 ? 0.4168 0.3133 0.4898 0.0571  -0.1022 -0.0514 474 TRP D CH2 
9682  N N   . GLU D 475 ? 0.5815 0.2977 0.4456 0.0512  -0.0880 -0.0340 475 GLU D N   
9683  C CA  . GLU D 475 ? 0.6079 0.3076 0.4421 0.0414  -0.0720 -0.0354 475 GLU D CA  
9684  C C   . GLU D 475 ? 0.6261 0.3113 0.4461 0.0340  -0.0601 -0.0359 475 GLU D C   
9685  O O   . GLU D 475 ? 0.6359 0.3265 0.4491 0.0228  -0.0415 -0.0401 475 GLU D O   
9686  C CB  . GLU D 475 ? 0.6413 0.3047 0.4359 0.0426  -0.0793 -0.0329 475 GLU D CB  
9687  C CG  . GLU D 475 ? 0.6723 0.3171 0.4328 0.0306  -0.0613 -0.0357 475 GLU D CG  
9688  C CD  . GLU D 475 ? 0.7275 0.3247 0.4378 0.0302  -0.0684 -0.0319 475 GLU D CD  
9689  O OE1 . GLU D 475 ? 0.7453 0.3178 0.4432 0.0392  -0.0871 -0.0263 475 GLU D OE1 
9690  O OE2 . GLU D 475 ? 0.7555 0.3402 0.4384 0.0210  -0.0558 -0.0353 475 GLU D OE2 
9691  N N   . GLN D 476 ? 0.6176 0.2852 0.4345 0.0403  -0.0704 -0.0331 476 GLN D N   
9692  C CA  . GLN D 476 ? 0.6355 0.2855 0.4382 0.0337  -0.0602 -0.0337 476 GLN D CA  
9693  C C   . GLN D 476 ? 0.6080 0.2971 0.4458 0.0276  -0.0463 -0.0391 476 GLN D C   
9694  O O   . GLN D 476 ? 0.6267 0.3057 0.4536 0.0186  -0.0336 -0.0414 476 GLN D O   
9695  C CB  . GLN D 476 ? 0.6540 0.2789 0.4483 0.0445  -0.0768 -0.0298 476 GLN D CB  
9696  C CG  . GLN D 476 ? 0.6828 0.2836 0.4483 0.0507  -0.0921 -0.0236 476 GLN D CG  
9697  C CD  . GLN D 476 ? 0.7299 0.2989 0.4673 0.0538  -0.0991 -0.0191 476 GLN D CD  
9698  O OE1 . GLN D 476 ? 0.7292 0.2994 0.4773 0.0542  -0.0956 -0.0207 476 GLN D OE1 
9699  N NE2 . GLN D 476 ? 0.7781 0.3164 0.4771 0.0560  -0.1098 -0.0142 476 GLN D NE2 
9700  N N   . SER D 477 ? 0.5623 0.2929 0.4388 0.0314  -0.0489 -0.0413 477 SER D N   
9701  C CA  . SER D 477 ? 0.5451 0.3136 0.4515 0.0251  -0.0363 -0.0463 477 SER D CA  
9702  C C   . SER D 477 ? 0.5489 0.3310 0.4512 0.0159  -0.0219 -0.0502 477 SER D C   
9703  O O   . SER D 477 ? 0.5349 0.3473 0.4598 0.0176  -0.0218 -0.0521 477 SER D O   
9704  C CB  . SER D 477 ? 0.5085 0.3107 0.4524 0.0322  -0.0457 -0.0464 477 SER D CB  
9705  O OG  . SER D 477 ? 0.5052 0.3002 0.4575 0.0403  -0.0575 -0.0458 477 SER D OG  
9706  N N   . GLN D 478 ? 0.5557 0.3134 0.4275 0.0060  -0.0095 -0.0523 478 GLN D N   
9707  C CA  . GLN D 478 ? 0.5648 0.3333 0.4304 -0.0028 0.0047  -0.0584 478 GLN D CA  
9708  C C   . GLN D 478 ? 0.5462 0.3584 0.4441 -0.0079 0.0160  -0.0663 478 GLN D C   
9709  O O   . GLN D 478 ? 0.5465 0.3777 0.4501 -0.0113 0.0245  -0.0730 478 GLN D O   
9710  C CB  . GLN D 478 ? 0.6013 0.3330 0.4250 -0.0154 0.0176  -0.0599 478 GLN D CB  
9711  C CG  . GLN D 478 ? 0.6284 0.3197 0.4144 -0.0119 0.0086  -0.0539 478 GLN D CG  
9712  C CD  . GLN D 478 ? 0.6293 0.3357 0.4191 -0.0094 0.0089  -0.0573 478 GLN D CD  
9713  O OE1 . GLN D 478 ? 0.6172 0.3545 0.4249 -0.0150 0.0222  -0.0663 478 GLN D OE1 
9714  N NE2 . GLN D 478 ? 0.6352 0.3200 0.4091 -0.0002 -0.0067 -0.0514 478 GLN D NE2 
9715  N N   . LYS D 479 ? 0.5129 0.3418 0.4321 -0.0079 0.0155  -0.0667 479 LYS D N   
9716  C CA  . LYS D 479 ? 0.4863 0.3559 0.4347 -0.0119 0.0236  -0.0739 479 LYS D CA  
9717  C C   . LYS D 479 ? 0.4529 0.3510 0.4308 -0.0015 0.0113  -0.0708 479 LYS D C   
9718  O O   . LYS D 479 ? 0.4279 0.3575 0.4286 -0.0032 0.0144  -0.0752 479 LYS D O   
9719  C CB  . LYS D 479 ? 0.4826 0.3523 0.4327 -0.0209 0.0327  -0.0777 479 LYS D CB  
9720  C CG  . LYS D 479 ? 0.5139 0.3528 0.4320 -0.0342 0.0468  -0.0811 479 LYS D CG  
9721  C CD  . LYS D 479 ? 0.5032 0.3508 0.4276 -0.0459 0.0591  -0.0881 479 LYS D CD  
9722  C CE  . LYS D 479 ? 0.5344 0.3497 0.4244 -0.0623 0.0751  -0.0921 479 LYS D CE  
9723  N NZ  . LYS D 479 ? 0.5382 0.3635 0.4350 -0.0760 0.0885  -0.1006 479 LYS D NZ  
9724  N N   . LEU D 480 ? 0.4494 0.3355 0.4251 0.0082  -0.0028 -0.0637 480 LEU D N   
9725  C CA  . LEU D 480 ? 0.4182 0.3266 0.4176 0.0157  -0.0137 -0.0604 480 LEU D CA  
9726  C C   . LEU D 480 ? 0.4085 0.3370 0.4169 0.0177  -0.0124 -0.0637 480 LEU D C   
9727  O O   . LEU D 480 ? 0.4235 0.3414 0.4182 0.0186  -0.0104 -0.0659 480 LEU D O   
9728  C CB  . LEU D 480 ? 0.4185 0.3081 0.4128 0.0238  -0.0284 -0.0534 480 LEU D CB  
9729  C CG  . LEU D 480 ? 0.3940 0.3023 0.4110 0.0285  -0.0388 -0.0500 480 LEU D CG  
9730  C CD1 . LEU D 480 ? 0.3841 0.3078 0.4183 0.0258  -0.0366 -0.0515 480 LEU D CD1 
9731  C CD2 . LEU D 480 ? 0.4016 0.2924 0.4130 0.0351  -0.0526 -0.0455 480 LEU D CD2 
9732  N N   . VAL D 481 ? 0.3595 0.3159 0.3894 0.0189  -0.0142 -0.0647 481 VAL D N   
9733  C CA  . VAL D 481 ? 0.3518 0.3265 0.3913 0.0234  -0.0161 -0.0679 481 VAL D CA  
9734  C C   . VAL D 481 ? 0.3427 0.3210 0.3910 0.0303  -0.0295 -0.0608 481 VAL D C   
9735  O O   . VAL D 481 ? 0.3405 0.3226 0.3907 0.0367  -0.0346 -0.0616 481 VAL D O   
9736  C CB  . VAL D 481 ? 0.3420 0.3456 0.3957 0.0189  -0.0074 -0.0765 481 VAL D CB  
9737  C CG1 . VAL D 481 ? 0.3505 0.3512 0.3947 0.0100  0.0077  -0.0855 481 VAL D CG1 
9738  C CG2 . VAL D 481 ? 0.3328 0.3498 0.3981 0.0152  -0.0084 -0.0742 481 VAL D CG2 
9739  N N   . ALA D 482 ? 0.3307 0.3071 0.3841 0.0290  -0.0350 -0.0549 482 ALA D N   
9740  C CA  . ALA D 482 ? 0.3182 0.2956 0.3774 0.0321  -0.0459 -0.0484 482 ALA D CA  
9741  C C   . ALA D 482 ? 0.3205 0.2829 0.3779 0.0317  -0.0518 -0.0441 482 ALA D C   
9742  O O   . ALA D 482 ? 0.3158 0.2821 0.3798 0.0281  -0.0493 -0.0448 482 ALA D O   
9743  C CB  . ALA D 482 ? 0.3005 0.2994 0.3717 0.0288  -0.0457 -0.0478 482 ALA D CB  
9744  N N   . PHE D 483 ? 0.3560 0.3020 0.4056 0.0360  -0.0602 -0.0410 483 PHE D N   
9745  C CA  . PHE D 483 ? 0.3517 0.2866 0.4023 0.0364  -0.0686 -0.0380 483 PHE D CA  
9746  C C   . PHE D 483 ? 0.3436 0.2817 0.4004 0.0353  -0.0764 -0.0340 483 PHE D C   
9747  O O   . PHE D 483 ? 0.3505 0.2777 0.3985 0.0388  -0.0815 -0.0323 483 PHE D O   
9748  C CB  . PHE D 483 ? 0.3637 0.2745 0.3971 0.0408  -0.0726 -0.0384 483 PHE D CB  
9749  C CG  . PHE D 483 ? 0.3644 0.2651 0.3997 0.0424  -0.0823 -0.0373 483 PHE D CG  
9750  C CD1 . PHE D 483 ? 0.3612 0.2752 0.4138 0.0402  -0.0830 -0.0386 483 PHE D CD1 
9751  C CD2 . PHE D 483 ? 0.3729 0.2524 0.3936 0.0467  -0.0913 -0.0365 483 PHE D CD2 
9752  C CE1 . PHE D 483 ? 0.3599 0.2687 0.4186 0.0432  -0.0930 -0.0399 483 PHE D CE1 
9753  C CE2 . PHE D 483 ? 0.3750 0.2477 0.3994 0.0493  -0.1024 -0.0368 483 PHE D CE2 
9754  C CZ  . PHE D 483 ? 0.3615 0.2500 0.4065 0.0481  -0.1035 -0.0390 483 PHE D CZ  
9755  N N   . ILE D 484 ? 0.2900 0.2417 0.3603 0.0295  -0.0766 -0.0330 484 ILE D N   
9756  C CA  . ILE D 484 ? 0.2926 0.2464 0.3659 0.0247  -0.0816 -0.0290 484 ILE D CA  
9757  C C   . ILE D 484 ? 0.2918 0.2496 0.3775 0.0196  -0.0853 -0.0306 484 ILE D C   
9758  O O   . ILE D 484 ? 0.2822 0.2557 0.3815 0.0156  -0.0804 -0.0343 484 ILE D O   
9759  C CB  . ILE D 484 ? 0.2922 0.2606 0.3676 0.0199  -0.0767 -0.0271 484 ILE D CB  
9760  C CG1 . ILE D 484 ? 0.2891 0.2594 0.3574 0.0262  -0.0736 -0.0284 484 ILE D CG1 
9761  C CG2 . ILE D 484 ? 0.3096 0.2721 0.3802 0.0142  -0.0822 -0.0217 484 ILE D CG2 
9762  C CD1 . ILE D 484 ? 0.2878 0.2730 0.3574 0.0230  -0.0710 -0.0274 484 ILE D CD1 
9763  N N   . LEU D 485 ? 0.3302 0.2755 0.4128 0.0197  -0.0940 -0.0295 485 LEU D N   
9764  C CA  . LEU D 485 ? 0.3262 0.2776 0.4234 0.0156  -0.0990 -0.0334 485 LEU D CA  
9765  C C   . LEU D 485 ? 0.3428 0.2885 0.4385 0.0076  -0.1041 -0.0310 485 LEU D C   
9766  O O   . LEU D 485 ? 0.3497 0.2877 0.4472 0.0078  -0.1126 -0.0334 485 LEU D O   
9767  C CB  . LEU D 485 ? 0.3226 0.2624 0.4173 0.0246  -0.1063 -0.0369 485 LEU D CB  
9768  C CG  . LEU D 485 ? 0.3145 0.2638 0.4275 0.0259  -0.1126 -0.0439 485 LEU D CG  
9769  C CD1 . LEU D 485 ? 0.3206 0.2519 0.4218 0.0373  -0.1194 -0.0452 485 LEU D CD1 
9770  C CD2 . LEU D 485 ? 0.3184 0.2747 0.4449 0.0192  -0.1201 -0.0473 485 LEU D CD2 
9771  N N   . SER D 486 ? 0.3532 0.2989 0.4419 0.0005  -0.1000 -0.0260 486 SER D N   
9772  C CA  . SER D 486 ? 0.3790 0.3105 0.4586 -0.0071 -0.1049 -0.0223 486 SER D CA  
9773  C C   . SER D 486 ? 0.3782 0.3238 0.4726 -0.0224 -0.1022 -0.0260 486 SER D C   
9774  O O   . SER D 486 ? 0.3619 0.3308 0.4735 -0.0273 -0.0951 -0.0311 486 SER D O   
9775  C CB  . SER D 486 ? 0.4010 0.3195 0.4615 -0.0069 -0.1040 -0.0147 486 SER D CB  
9776  O OG  . SER D 486 ? 0.4102 0.3443 0.4733 -0.0132 -0.0959 -0.0133 486 SER D OG  
9777  N N   . ASN D 487 ? 0.4537 0.3852 0.5414 -0.0308 -0.1073 -0.0246 487 ASN D N   
9778  C CA  . ASN D 487 ? 0.4576 0.4007 0.5581 -0.0483 -0.1043 -0.0294 487 ASN D CA  
9779  C C   . ASN D 487 ? 0.4257 0.3979 0.5572 -0.0478 -0.1037 -0.0412 487 ASN D C   
9780  O O   . ASN D 487 ? 0.4144 0.4112 0.5633 -0.0572 -0.0948 -0.0472 487 ASN D O   
9781  C CB  . ASN D 487 ? 0.4814 0.4269 0.5725 -0.0630 -0.0943 -0.0247 487 ASN D CB  
9782  C CG  . ASN D 487 ? 0.4997 0.4489 0.5955 -0.0847 -0.0901 -0.0285 487 ASN D CG  
9783  O OD1 . ASN D 487 ? 0.5078 0.4493 0.6073 -0.0886 -0.0967 -0.0320 487 ASN D OD1 
9784  N ND2 . ASN D 487 ? 0.5080 0.4693 0.6031 -0.1002 -0.0785 -0.0287 487 ASN D ND2 
9785  N N   . ASN D 488 ? 0.4264 0.3943 0.5635 -0.0360 -0.1141 -0.0454 488 ASN D N   
9786  C CA  . ASN D 488 ? 0.3986 0.3895 0.5636 -0.0329 -0.1183 -0.0571 488 ASN D CA  
9787  C C   . ASN D 488 ? 0.4022 0.3865 0.5714 -0.0339 -0.1307 -0.0623 488 ASN D C   
9788  O O   . ASN D 488 ? 0.4324 0.3950 0.5835 -0.0400 -0.1336 -0.0570 488 ASN D O   
9789  C CB  . ASN D 488 ? 0.3814 0.3730 0.5475 -0.0153 -0.1208 -0.0578 488 ASN D CB  
9790  C CG  . ASN D 488 ? 0.3719 0.3830 0.5486 -0.0164 -0.1091 -0.0597 488 ASN D CG  
9791  O OD1 . ASN D 488 ? 0.3514 0.3857 0.5533 -0.0157 -0.1081 -0.0699 488 ASN D OD1 
9792  N ND2 . ASN D 488 ? 0.3803 0.3828 0.5388 -0.0174 -0.1010 -0.0511 488 ASN D ND2 
9793  N N   . SER D 489 ? 0.4176 0.4196 0.6104 -0.0275 -0.1391 -0.0733 489 SER D N   
9794  C CA  . SER D 489 ? 0.4278 0.4259 0.6262 -0.0264 -0.1534 -0.0799 489 SER D CA  
9795  C C   . SER D 489 ? 0.4312 0.4090 0.6141 -0.0069 -0.1665 -0.0776 489 SER D C   
9796  O O   . SER D 489 ? 0.4441 0.4268 0.6386 0.0000  -0.1805 -0.0861 489 SER D O   
9797  C CB  . SER D 489 ? 0.4241 0.4580 0.6611 -0.0334 -0.1558 -0.0960 489 SER D CB  
9798  O OG  . SER D 489 ? 0.4275 0.4793 0.6760 -0.0545 -0.1415 -0.0989 489 SER D OG  
9799  N N   . ILE D 490 ? 0.4328 0.3876 0.5886 0.0016  -0.1622 -0.0668 490 ILE D N   
9800  C CA  . ILE D 490 ? 0.4413 0.3748 0.5779 0.0177  -0.1715 -0.0644 490 ILE D CA  
9801  C C   . ILE D 490 ? 0.4642 0.3762 0.5843 0.0182  -0.1833 -0.0644 490 ILE D C   
9802  O O   . ILE D 490 ? 0.4714 0.3686 0.5767 0.0110  -0.1798 -0.0595 490 ILE D O   
9803  C CB  . ILE D 490 ? 0.4441 0.3624 0.5582 0.0236  -0.1611 -0.0549 490 ILE D CB  
9804  C CG1 . ILE D 490 ? 0.4239 0.3637 0.5542 0.0220  -0.1498 -0.0558 490 ILE D CG1 
9805  C CG2 . ILE D 490 ? 0.4540 0.3487 0.5451 0.0372  -0.1684 -0.0530 490 ILE D CG2 
9806  C CD1 . ILE D 490 ? 0.4141 0.3701 0.5659 0.0289  -0.1557 -0.0647 490 ILE D CD1 
9807  N N   . THR D 491 ? 0.4387 0.3469 0.5597 0.0274  -0.1983 -0.0704 491 THR D N   
9808  C CA  . THR D 491 ? 0.4602 0.3487 0.5652 0.0288  -0.2116 -0.0722 491 THR D CA  
9809  C C   . THR D 491 ? 0.4762 0.3348 0.5479 0.0426  -0.2168 -0.0670 491 THR D C   
9810  O O   . THR D 491 ? 0.4705 0.3235 0.5320 0.0494  -0.2089 -0.0619 491 THR D O   
9811  C CB  . THR D 491 ? 0.4658 0.3744 0.5966 0.0274  -0.2251 -0.0841 491 THR D CB  
9812  O OG1 . THR D 491 ? 0.4673 0.3818 0.6049 0.0418  -0.2313 -0.0876 491 THR D OG1 
9813  C CG2 . THR D 491 ? 0.4518 0.3922 0.6147 0.0115  -0.2148 -0.0899 491 THR D CG2 
9814  N N   . GLY D 492 ? 0.5028 0.3414 0.5561 0.0450  -0.2294 -0.0691 492 GLY D N   
9815  C CA  . GLY D 492 ? 0.5272 0.3356 0.5452 0.0559  -0.2345 -0.0653 492 GLY D CA  
9816  C C   . GLY D 492 ? 0.5297 0.3179 0.5210 0.0548  -0.2201 -0.0576 492 GLY D C   
9817  O O   . GLY D 492 ? 0.5220 0.3151 0.5193 0.0471  -0.2100 -0.0553 492 GLY D O   
9818  N N   . ALA D 493 ? 0.5069 0.2713 0.4675 0.0628  -0.2195 -0.0545 493 ALA D N   
9819  C CA  . ALA D 493 ? 0.5118 0.2588 0.4474 0.0627  -0.2060 -0.0501 493 ALA D CA  
9820  C C   . ALA D 493 ? 0.4986 0.2506 0.4330 0.0650  -0.1917 -0.0457 493 ALA D C   
9821  O O   . ALA D 493 ? 0.4914 0.2531 0.4372 0.0679  -0.1934 -0.0454 493 ALA D O   
9822  C CB  . ALA D 493 ? 0.5448 0.2627 0.4434 0.0663  -0.2122 -0.0513 493 ALA D CB  
9823  N N   . ILE D 494 ? 0.4888 0.2363 0.4102 0.0635  -0.1771 -0.0435 494 ILE D N   
9824  C CA  . ILE D 494 ? 0.4787 0.2306 0.3973 0.0642  -0.1624 -0.0409 494 ILE D CA  
9825  C C   . ILE D 494 ? 0.5052 0.2342 0.3909 0.0669  -0.1611 -0.0405 494 ILE D C   
9826  O O   . ILE D 494 ? 0.5282 0.2373 0.3873 0.0671  -0.1606 -0.0422 494 ILE D O   
9827  C CB  . ILE D 494 ? 0.4675 0.2254 0.3887 0.0624  -0.1492 -0.0410 494 ILE D CB  
9828  C CG1 . ILE D 494 ? 0.4475 0.2244 0.3953 0.0584  -0.1506 -0.0396 494 ILE D CG1 
9829  C CG2 . ILE D 494 ? 0.4580 0.2236 0.3777 0.0622  -0.1341 -0.0401 494 ILE D CG2 
9830  C CD1 . ILE D 494 ? 0.4385 0.2218 0.3894 0.0585  -0.1402 -0.0390 494 ILE D CD1 
9831  N N   . PRO D 495 ? 0.5267 0.2548 0.4106 0.0686  -0.1605 -0.0384 495 PRO D N   
9832  C CA  . PRO D 495 ? 0.5587 0.2585 0.4056 0.0698  -0.1594 -0.0369 495 PRO D CA  
9833  C C   . PRO D 495 ? 0.5702 0.2555 0.3942 0.0661  -0.1429 -0.0386 495 PRO D C   
9834  O O   . PRO D 495 ? 0.5517 0.2569 0.3938 0.0632  -0.1290 -0.0400 495 PRO D O   
9835  C CB  . PRO D 495 ? 0.5532 0.2585 0.4087 0.0714  -0.1582 -0.0346 495 PRO D CB  
9836  C CG  . PRO D 495 ? 0.5222 0.2585 0.4194 0.0725  -0.1641 -0.0364 495 PRO D CG  
9837  C CD  . PRO D 495 ? 0.5030 0.2534 0.4167 0.0689  -0.1598 -0.0377 495 PRO D CD  
9838  N N   . PRO D 496 ? 0.6059 0.2615 0.3912 0.0651  -0.1430 -0.0397 496 PRO D N   
9839  C CA  . PRO D 496 ? 0.6170 0.2649 0.3821 0.0594  -0.1242 -0.0439 496 PRO D CA  
9840  C C   . PRO D 496 ? 0.6121 0.2650 0.3763 0.0540  -0.1075 -0.0433 496 PRO D C   
9841  O O   . PRO D 496 ? 0.6069 0.2705 0.3717 0.0486  -0.0897 -0.0486 496 PRO D O   
9842  C CB  . PRO D 496 ? 0.6638 0.2741 0.3824 0.0582  -0.1292 -0.0450 496 PRO D CB  
9843  C CG  . PRO D 496 ? 0.6683 0.2763 0.3918 0.0644  -0.1521 -0.0420 496 PRO D CG  
9844  C CD  . PRO D 496 ? 0.6391 0.2711 0.3977 0.0681  -0.1596 -0.0381 496 PRO D CD  
9845  N N   . GLU D 497 ? 0.6571 0.3035 0.4215 0.0554  -0.1131 -0.0382 497 GLU D N   
9846  C CA  . GLU D 497 ? 0.6603 0.3087 0.4226 0.0492  -0.0977 -0.0378 497 GLU D CA  
9847  C C   . GLU D 497 ? 0.6180 0.3069 0.4212 0.0475  -0.0864 -0.0407 497 GLU D C   
9848  O O   . GLU D 497 ? 0.6208 0.3167 0.4236 0.0405  -0.0700 -0.0433 497 GLU D O   
9849  C CB  . GLU D 497 ? 0.6725 0.3020 0.4262 0.0532  -0.1089 -0.0322 497 GLU D CB  
9850  C CG  . GLU D 497 ? 0.7243 0.3092 0.4287 0.0533  -0.1173 -0.0283 497 GLU D CG  
9851  C CD  . GLU D 497 ? 0.7298 0.3140 0.4345 0.0618  -0.1395 -0.0265 497 GLU D CD  
9852  O OE1 . GLU D 497 ? 0.6932 0.3092 0.4383 0.0676  -0.1496 -0.0279 497 GLU D OE1 
9853  O OE2 . GLU D 497 ? 0.7703 0.3209 0.4330 0.0615  -0.1466 -0.0246 497 GLU D OE2 
9854  N N   . ILE D 498 ? 0.5681 0.2820 0.4041 0.0528  -0.0950 -0.0406 498 ILE D N   
9855  C CA  . ILE D 498 ? 0.5314 0.2803 0.4020 0.0515  -0.0864 -0.0423 498 ILE D CA  
9856  C C   . ILE D 498 ? 0.5297 0.2887 0.3979 0.0475  -0.0704 -0.0488 498 ILE D C   
9857  O O   . ILE D 498 ? 0.5111 0.2925 0.3962 0.0441  -0.0587 -0.0518 498 ILE D O   
9858  C CB  . ILE D 498 ? 0.5083 0.2753 0.4070 0.0561  -0.0988 -0.0405 498 ILE D CB  
9859  C CG1 . ILE D 498 ? 0.5084 0.2721 0.4154 0.0595  -0.1134 -0.0371 498 ILE D CG1 
9860  C CG2 . ILE D 498 ? 0.4770 0.2752 0.4048 0.0544  -0.0908 -0.0414 498 ILE D CG2 
9861  C CD1 . ILE D 498 ? 0.4891 0.2706 0.4170 0.0582  -0.1090 -0.0362 498 ILE D CD1 
9862  N N   . TRP D 499 ? 0.5486 0.2933 0.3973 0.0482  -0.0700 -0.0527 499 TRP D N   
9863  C CA  . TRP D 499 ? 0.5541 0.3105 0.4028 0.0456  -0.0548 -0.0617 499 TRP D CA  
9864  C C   . TRP D 499 ? 0.5773 0.3284 0.4078 0.0357  -0.0369 -0.0662 499 TRP D C   
9865  O O   . TRP D 499 ? 0.5796 0.3518 0.4211 0.0324  -0.0222 -0.0753 499 TRP D O   
9866  C CB  . TRP D 499 ? 0.5703 0.3116 0.4023 0.0490  -0.0586 -0.0661 499 TRP D CB  
9867  C CG  . TRP D 499 ? 0.5561 0.2935 0.3979 0.0560  -0.0773 -0.0609 499 TRP D CG  
9868  C CD1 . TRP D 499 ? 0.5725 0.2845 0.3935 0.0575  -0.0907 -0.0579 499 TRP D CD1 
9869  C CD2 . TRP D 499 ? 0.5258 0.2846 0.3993 0.0608  -0.0847 -0.0584 499 TRP D CD2 
9870  N NE1 . TRP D 499 ? 0.5629 0.2818 0.4036 0.0622  -0.1049 -0.0549 499 TRP D NE1 
9871  C CE2 . TRP D 499 ? 0.5305 0.2761 0.4016 0.0636  -0.1009 -0.0547 499 TRP D CE2 
9872  C CE3 . TRP D 499 ? 0.5026 0.2888 0.4038 0.0622  -0.0795 -0.0592 499 TRP D CE3 
9873  C CZ2 . TRP D 499 ? 0.5083 0.2659 0.4027 0.0659  -0.1101 -0.0516 499 TRP D CZ2 
9874  C CZ3 . TRP D 499 ? 0.4832 0.2788 0.4045 0.0658  -0.0899 -0.0550 499 TRP D CZ3 
9875  C CH2 . TRP D 499 ? 0.4873 0.2679 0.4045 0.0666  -0.1041 -0.0512 499 TRP D CH2 
9876  N N   . ASN D 500 ? 0.6781 0.4007 0.4806 0.0309  -0.0383 -0.0609 500 ASN D N   
9877  C CA  . ASN D 500 ? 0.7025 0.4161 0.4857 0.0193  -0.0211 -0.0640 500 ASN D CA  
9878  C C   . ASN D 500 ? 0.6876 0.4246 0.4975 0.0168  -0.0156 -0.0632 500 ASN D C   
9879  O O   . ASN D 500 ? 0.7134 0.4423 0.5087 0.0061  -0.0018 -0.0655 500 ASN D O   
9880  C CB  . ASN D 500 ? 0.7366 0.4038 0.4737 0.0153  -0.0258 -0.0577 500 ASN D CB  
9881  C CG  . ASN D 500 ? 0.7735 0.4165 0.4716 0.0080  -0.0163 -0.0633 500 ASN D CG  
9882  O OD1 . ASN D 500 ? 0.7672 0.4313 0.4756 0.0050  -0.0031 -0.0738 500 ASN D OD1 
9883  N ND2 . ASN D 500 ? 0.8144 0.4129 0.4671 0.0055  -0.0233 -0.0572 500 ASN D ND2 
9884  N N   . MET D 501 ? 0.5776 0.3416 0.4236 0.0248  -0.0254 -0.0603 501 MET D N   
9885  C CA  . MET D 501 ? 0.5617 0.3524 0.4349 0.0224  -0.0195 -0.0612 501 MET D CA  
9886  C C   . MET D 501 ? 0.5536 0.3780 0.4489 0.0206  -0.0075 -0.0711 501 MET D C   
9887  O O   . MET D 501 ? 0.5233 0.3739 0.4471 0.0275  -0.0136 -0.0713 501 MET D O   
9888  C CB  . MET D 501 ? 0.5316 0.3340 0.4298 0.0305  -0.0349 -0.0542 501 MET D CB  
9889  C CG  . MET D 501 ? 0.5444 0.3192 0.4275 0.0352  -0.0499 -0.0469 501 MET D CG  
9890  S SD  . MET D 501 ? 0.5102 0.3047 0.4269 0.0416  -0.0634 -0.0424 501 MET D SD  
9891  C CE  . MET D 501 ? 0.4796 0.3150 0.4291 0.0394  -0.0547 -0.0459 501 MET D CE  
9892  N N   . THR D 502 ? 0.5375 0.3598 0.4176 0.0108  0.0096  -0.0800 502 THR D N   
9893  C CA  . THR D 502 ? 0.5287 0.3828 0.4283 0.0102  0.0208  -0.0926 502 THR D CA  
9894  C C   . THR D 502 ? 0.4962 0.3877 0.4315 0.0119  0.0217  -0.0956 502 THR D C   
9895  O O   . THR D 502 ? 0.4719 0.3922 0.4303 0.0178  0.0223  -0.1039 502 THR D O   
9896  C CB  . THR D 502 ? 0.5485 0.3955 0.4260 -0.0039 0.0416  -0.1034 502 THR D CB  
9897  O OG1 . THR D 502 ? 0.5476 0.3918 0.4197 -0.0161 0.0521  -0.1032 502 THR D OG1 
9898  C CG2 . THR D 502 ? 0.5785 0.3844 0.4143 -0.0069 0.0409  -0.1000 502 THR D CG2 
9899  N N   . GLN D 503 ? 0.4845 0.3754 0.4239 0.0077  0.0208  -0.0897 503 GLN D N   
9900  C CA  . GLN D 503 ? 0.4550 0.3799 0.4243 0.0075  0.0226  -0.0932 503 GLN D CA  
9901  C C   . GLN D 503 ? 0.4318 0.3709 0.4231 0.0193  0.0062  -0.0862 503 GLN D C   
9902  O O   . GLN D 503 ? 0.4122 0.3771 0.4253 0.0196  0.0056  -0.0877 503 GLN D O   
9903  C CB  . GLN D 503 ? 0.4620 0.3793 0.4252 -0.0027 0.0295  -0.0912 503 GLN D CB  
9904  C CG  . GLN D 503 ? 0.4732 0.3897 0.4236 -0.0178 0.0495  -0.1017 503 GLN D CG  
9905  C CD  . GLN D 503 ? 0.4518 0.4118 0.4311 -0.0208 0.0588  -0.1154 503 GLN D CD  
9906  O OE1 . GLN D 503 ? 0.4482 0.4229 0.4315 -0.0219 0.0670  -0.1267 503 GLN D OE1 
9907  N NE2 . GLN D 503 ? 0.4295 0.4115 0.4299 -0.0217 0.0571  -0.1158 503 GLN D NE2 
9908  N N   . LEU D 504 ? 0.4293 0.3513 0.4137 0.0276  -0.0067 -0.0789 504 LEU D N   
9909  C CA  . LEU D 504 ? 0.4064 0.3382 0.4080 0.0362  -0.0210 -0.0722 504 LEU D CA  
9910  C C   . LEU D 504 ? 0.3933 0.3504 0.4133 0.0428  -0.0222 -0.0788 504 LEU D C   
9911  O O   . LEU D 504 ? 0.4037 0.3623 0.4209 0.0463  -0.0185 -0.0869 504 LEU D O   
9912  C CB  . LEU D 504 ? 0.4112 0.3181 0.4001 0.0418  -0.0335 -0.0649 504 LEU D CB  
9913  C CG  . LEU D 504 ? 0.4048 0.3006 0.3942 0.0415  -0.0434 -0.0556 504 LEU D CG  
9914  C CD1 . LEU D 504 ? 0.4040 0.2823 0.3862 0.0471  -0.0566 -0.0508 504 LEU D CD1 
9915  C CD2 . LEU D 504 ? 0.3886 0.3073 0.4003 0.0406  -0.0454 -0.0530 504 LEU D CD2 
9916  N N   . SER D 505 ? 0.3669 0.3430 0.4046 0.0448  -0.0278 -0.0759 505 SER D N   
9917  C CA  . SER D 505 ? 0.3610 0.3566 0.4136 0.0535  -0.0336 -0.0802 505 SER D CA  
9918  C C   . SER D 505 ? 0.3591 0.3461 0.4128 0.0600  -0.0490 -0.0701 505 SER D C   
9919  O O   . SER D 505 ? 0.3641 0.3543 0.4221 0.0696  -0.0569 -0.0720 505 SER D O   
9920  C CB  . SER D 505 ? 0.3484 0.3743 0.4180 0.0501  -0.0277 -0.0871 505 SER D CB  
9921  O OG  . SER D 505 ? 0.3478 0.3930 0.4310 0.0603  -0.0337 -0.0942 505 SER D OG  
9922  N N   . GLN D 506 ? 0.3522 0.3279 0.4019 0.0549  -0.0532 -0.0603 506 GLN D N   
9923  C CA  . GLN D 506 ? 0.3449 0.3098 0.3931 0.0575  -0.0656 -0.0511 506 GLN D CA  
9924  C C   . GLN D 506 ? 0.3488 0.2942 0.3887 0.0532  -0.0685 -0.0452 506 GLN D C   
9925  O O   . GLN D 506 ? 0.3488 0.2963 0.3908 0.0469  -0.0638 -0.0442 506 GLN D O   
9926  C CB  . GLN D 506 ? 0.3311 0.3113 0.3882 0.0543  -0.0683 -0.0470 506 GLN D CB  
9927  C CG  . GLN D 506 ? 0.3300 0.2974 0.3828 0.0515  -0.0776 -0.0373 506 GLN D CG  
9928  C CD  . GLN D 506 ? 0.3294 0.3073 0.3844 0.0497  -0.0817 -0.0334 506 GLN D CD  
9929  O OE1 . GLN D 506 ? 0.3236 0.3214 0.3856 0.0493  -0.0773 -0.0378 506 GLN D OE1 
9930  N NE2 . GLN D 506 ? 0.3408 0.3039 0.3873 0.0475  -0.0901 -0.0254 506 GLN D NE2 
9931  N N   . LEU D 507 ? 0.3307 0.2571 0.3619 0.0571  -0.0770 -0.0423 507 LEU D N   
9932  C CA  . LEU D 507 ? 0.3358 0.2456 0.3612 0.0538  -0.0824 -0.0378 507 LEU D CA  
9933  C C   . LEU D 507 ? 0.3408 0.2430 0.3671 0.0528  -0.0926 -0.0317 507 LEU D C   
9934  O O   . LEU D 507 ? 0.3521 0.2453 0.3728 0.0583  -0.0980 -0.0315 507 LEU D O   
9935  C CB  . LEU D 507 ? 0.3514 0.2422 0.3613 0.0571  -0.0823 -0.0414 507 LEU D CB  
9936  C CG  . LEU D 507 ? 0.3607 0.2333 0.3630 0.0553  -0.0908 -0.0379 507 LEU D CG  
9937  C CD1 . LEU D 507 ? 0.3521 0.2304 0.3613 0.0506  -0.0896 -0.0361 507 LEU D CD1 
9938  C CD2 . LEU D 507 ? 0.3806 0.2327 0.3631 0.0587  -0.0911 -0.0417 507 LEU D CD2 
9939  N N   . ASP D 508 ? 0.3405 0.2455 0.3737 0.0455  -0.0950 -0.0278 508 ASP D N   
9940  C CA  . ASP D 508 ? 0.3471 0.2463 0.3810 0.0404  -0.1022 -0.0226 508 ASP D CA  
9941  C C   . ASP D 508 ? 0.3474 0.2433 0.3867 0.0346  -0.1062 -0.0228 508 ASP D C   
9942  O O   . ASP D 508 ? 0.3358 0.2467 0.3880 0.0290  -0.1028 -0.0237 508 ASP D O   
9943  C CB  . ASP D 508 ? 0.3404 0.2543 0.3805 0.0348  -0.0991 -0.0193 508 ASP D CB  
9944  C CG  . ASP D 508 ? 0.3539 0.2576 0.3890 0.0272  -0.1051 -0.0134 508 ASP D CG  
9945  O OD1 . ASP D 508 ? 0.3681 0.2532 0.3961 0.0270  -0.1119 -0.0124 508 ASP D OD1 
9946  O OD2 . ASP D 508 ? 0.3532 0.2659 0.3894 0.0200  -0.1025 -0.0101 508 ASP D OD2 
9947  N N   . LEU D 509 ? 0.3671 0.2448 0.3979 0.0366  -0.1139 -0.0233 509 LEU D N   
9948  C CA  . LEU D 509 ? 0.3730 0.2481 0.4098 0.0315  -0.1205 -0.0247 509 LEU D CA  
9949  C C   . LEU D 509 ? 0.3987 0.2637 0.4334 0.0241  -0.1267 -0.0221 509 LEU D C   
9950  O O   . LEU D 509 ? 0.4083 0.2649 0.4432 0.0213  -0.1342 -0.0245 509 LEU D O   
9951  C CB  . LEU D 509 ? 0.3703 0.2312 0.3969 0.0384  -0.1255 -0.0283 509 LEU D CB  
9952  C CG  . LEU D 509 ? 0.3603 0.2231 0.3816 0.0442  -0.1189 -0.0304 509 LEU D CG  
9953  C CD1 . LEU D 509 ? 0.3719 0.2153 0.3772 0.0492  -0.1252 -0.0330 509 LEU D CD1 
9954  C CD2 . LEU D 509 ? 0.3521 0.2341 0.3899 0.0409  -0.1142 -0.0311 509 LEU D CD2 
9955  N N   . SER D 510 ? 0.3973 0.2613 0.4279 0.0203  -0.1242 -0.0174 510 SER D N   
9956  C CA  . SER D 510 ? 0.4176 0.2643 0.4391 0.0129  -0.1296 -0.0137 510 SER D CA  
9957  C C   . SER D 510 ? 0.4173 0.2745 0.4518 -0.0024 -0.1291 -0.0151 510 SER D C   
9958  O O   . SER D 510 ? 0.3999 0.2809 0.4522 -0.0065 -0.1238 -0.0185 510 SER D O   
9959  C CB  . SER D 510 ? 0.4274 0.2666 0.4370 0.0138  -0.1283 -0.0076 510 SER D CB  
9960  O OG  . SER D 510 ? 0.4170 0.2760 0.4348 0.0064  -0.1210 -0.0055 510 SER D OG  
9961  N N   . SER D 511 ? 0.4481 0.2872 0.4741 -0.0113 -0.1343 -0.0138 511 SER D N   
9962  C CA  . SER D 511 ? 0.4513 0.2995 0.4886 -0.0290 -0.1327 -0.0163 511 SER D CA  
9963  C C   . SER D 511 ? 0.4234 0.2946 0.4850 -0.0290 -0.1347 -0.0258 511 SER D C   
9964  O O   . SER D 511 ? 0.4137 0.3107 0.4959 -0.0377 -0.1290 -0.0306 511 SER D O   
9965  C CB  . SER D 511 ? 0.4628 0.3227 0.5010 -0.0406 -0.1232 -0.0123 511 SER D CB  
9966  O OG  . SER D 511 ? 0.4921 0.3276 0.5051 -0.0390 -0.1243 -0.0032 511 SER D OG  
9967  N N   . ASN D 512 ? 0.4814 0.3425 0.5396 -0.0186 -0.1435 -0.0292 512 ASN D N   
9968  C CA  . ASN D 512 ? 0.4592 0.3361 0.5360 -0.0164 -0.1496 -0.0380 512 ASN D CA  
9969  C C   . ASN D 512 ? 0.4739 0.3338 0.5439 -0.0177 -0.1610 -0.0419 512 ASN D C   
9970  O O   . ASN D 512 ? 0.4928 0.3293 0.5454 -0.0225 -0.1626 -0.0383 512 ASN D O   
9971  C CB  . ASN D 512 ? 0.4437 0.3253 0.5202 -0.0007 -0.1497 -0.0386 512 ASN D CB  
9972  C CG  . ASN D 512 ? 0.4268 0.3313 0.5175 -0.0011 -0.1397 -0.0384 512 ASN D CG  
9973  O OD1 . ASN D 512 ? 0.4088 0.3361 0.5223 -0.0049 -0.1392 -0.0450 512 ASN D OD1 
9974  N ND2 . ASN D 512 ? 0.4346 0.3346 0.5132 0.0033  -0.1320 -0.0322 512 ASN D ND2 
9975  N N   . ARG D 513 ? 0.5527 0.4225 0.6351 -0.0129 -0.1701 -0.0498 513 ARG D N   
9976  C CA  . ARG D 513 ? 0.5606 0.4155 0.6359 -0.0125 -0.1827 -0.0548 513 ARG D CA  
9977  C C   . ARG D 513 ? 0.5623 0.4032 0.6216 0.0042  -0.1903 -0.0550 513 ARG D C   
9978  O O   . ARG D 513 ? 0.5760 0.4162 0.6374 0.0080  -0.2029 -0.0616 513 ARG D O   
9979  C CB  . ARG D 513 ? 0.5594 0.4377 0.6623 -0.0231 -0.1892 -0.0658 513 ARG D CB  
9980  C CG  . ARG D 513 ? 0.5684 0.4513 0.6790 -0.0442 -0.1825 -0.0670 513 ARG D CG  
9981  C CD  . ARG D 513 ? 0.5625 0.4748 0.6953 -0.0536 -0.1699 -0.0683 513 ARG D CD  
9982  N NE  . ARG D 513 ? 0.5636 0.5115 0.7319 -0.0573 -0.1739 -0.0823 513 ARG D NE  
9983  C CZ  . ARG D 513 ? 0.5487 0.5258 0.7420 -0.0724 -0.1638 -0.0892 513 ARG D CZ  
9984  N NH1 . ARG D 513 ? 0.5495 0.5221 0.7324 -0.0867 -0.1492 -0.0821 513 ARG D NH1 
9985  N NH2 . ARG D 513 ? 0.5241 0.5357 0.7480 -0.0713 -0.1650 -0.1020 513 ARG D NH2 
9986  N N   . ILE D 514 ? 0.4873 0.3166 0.5291 0.0136  -0.1828 -0.0482 514 ILE D N   
9987  C CA  . ILE D 514 ? 0.4945 0.3081 0.5166 0.0269  -0.1867 -0.0480 514 ILE D CA  
9988  C C   . ILE D 514 ? 0.5187 0.3049 0.5173 0.0284  -0.1932 -0.0492 514 ILE D C   
9989  O O   . ILE D 514 ? 0.5261 0.2996 0.5157 0.0250  -0.1889 -0.0464 514 ILE D O   
9990  C CB  . ILE D 514 ? 0.4866 0.3006 0.5004 0.0338  -0.1744 -0.0425 514 ILE D CB  
9991  C CG1 . ILE D 514 ? 0.4679 0.3070 0.5031 0.0329  -0.1687 -0.0426 514 ILE D CG1 
9992  C CG2 . ILE D 514 ? 0.4967 0.2907 0.4852 0.0441  -0.1756 -0.0428 514 ILE D CG2 
9993  C CD1 . ILE D 514 ? 0.4593 0.3056 0.4940 0.0333  -0.1549 -0.0374 514 ILE D CD1 
9994  N N   . THR D 515 ? 0.5101 0.2852 0.4969 0.0341  -0.2043 -0.0536 515 THR D N   
9995  C CA  . THR D 515 ? 0.5360 0.2852 0.4994 0.0353  -0.2115 -0.0565 515 THR D CA  
9996  C C   . THR D 515 ? 0.5476 0.2788 0.4823 0.0458  -0.2076 -0.0548 515 THR D C   
9997  O O   . THR D 515 ? 0.5369 0.2727 0.4695 0.0510  -0.1995 -0.0517 515 THR D O   
9998  C CB  . THR D 515 ? 0.5496 0.3014 0.5198 0.0317  -0.2276 -0.0637 515 THR D CB  
9999  O OG1 . THR D 515 ? 0.5492 0.3079 0.5218 0.0397  -0.2363 -0.0661 515 THR D OG1 
10000 C CG2 . THR D 515 ? 0.5396 0.3129 0.5392 0.0184  -0.2278 -0.0666 515 THR D CG2 
10001 N N   . GLY D 516 ? 0.5637 0.2777 0.4759 0.0474  -0.2109 -0.0567 516 GLY D N   
10002 C CA  . GLY D 516 ? 0.5806 0.2797 0.4638 0.0542  -0.2046 -0.0561 516 GLY D CA  
10003 C C   . GLY D 516 ? 0.5769 0.2731 0.4533 0.0553  -0.1906 -0.0553 516 GLY D C   
10004 O O   . GLY D 516 ? 0.5687 0.2701 0.4587 0.0519  -0.1879 -0.0540 516 GLY D O   
10005 N N   . GLU D 517 ? 0.6031 0.2889 0.4570 0.0603  -0.1821 -0.0569 517 GLU D N   
10006 C CA  . GLU D 517 ? 0.6075 0.2913 0.4564 0.0634  -0.1695 -0.0592 517 GLU D CA  
10007 C C   . GLU D 517 ? 0.5977 0.2866 0.4425 0.0670  -0.1561 -0.0597 517 GLU D C   
10008 O O   . GLU D 517 ? 0.6016 0.2854 0.4341 0.0668  -0.1558 -0.0587 517 GLU D O   
10009 C CB  . GLU D 517 ? 0.6386 0.3030 0.4642 0.0650  -0.1708 -0.0650 517 GLU D CB  
10010 C CG  . GLU D 517 ? 0.6588 0.3062 0.4582 0.0646  -0.1780 -0.0668 517 GLU D CG  
10011 C CD  . GLU D 517 ? 0.6936 0.3225 0.4702 0.0654  -0.1777 -0.0730 517 GLU D CD  
10012 O OE1 . GLU D 517 ? 0.7232 0.3453 0.4839 0.0682  -0.1650 -0.0782 517 GLU D OE1 
10013 O OE2 . GLU D 517 ? 0.7089 0.3308 0.4846 0.0628  -0.1893 -0.0739 517 GLU D OE2 
10014 N N   . LEU D 518 ? 0.5590 0.2565 0.4137 0.0704  -0.1459 -0.0617 518 LEU D N   
10015 C CA  . LEU D 518 ? 0.5506 0.2554 0.4053 0.0735  -0.1328 -0.0643 518 LEU D CA  
10016 C C   . LEU D 518 ? 0.5764 0.2654 0.4038 0.0750  -0.1242 -0.0728 518 LEU D C   
10017 O O   . LEU D 518 ? 0.5934 0.2738 0.4120 0.0775  -0.1235 -0.0788 518 LEU D O   
10018 C CB  . LEU D 518 ? 0.5337 0.2539 0.4091 0.0780  -0.1270 -0.0654 518 LEU D CB  
10019 C CG  . LEU D 518 ? 0.5120 0.2461 0.4104 0.0749  -0.1331 -0.0571 518 LEU D CG  
10020 C CD1 . LEU D 518 ? 0.5020 0.2474 0.4148 0.0804  -0.1287 -0.0579 518 LEU D CD1 
10021 C CD2 . LEU D 518 ? 0.4958 0.2395 0.4019 0.0707  -0.1330 -0.0523 518 LEU D CD2 
10022 N N   . PRO D 519 ? 0.5636 0.2469 0.3754 0.0724  -0.1167 -0.0739 519 PRO D N   
10023 C CA  . PRO D 519 ? 0.5931 0.2599 0.3742 0.0706  -0.1063 -0.0823 519 PRO D CA  
10024 C C   . PRO D 519 ? 0.5890 0.2699 0.3782 0.0737  -0.0895 -0.0934 519 PRO D C   
10025 O O   . PRO D 519 ? 0.5618 0.2675 0.3798 0.0769  -0.0854 -0.0926 519 PRO D O   
10026 C CB  . PRO D 519 ? 0.6039 0.2584 0.3642 0.0649  -0.1048 -0.0775 519 PRO D CB  
10027 C CG  . PRO D 519 ? 0.5696 0.2479 0.3605 0.0651  -0.1049 -0.0702 519 PRO D CG  
10028 C CD  . PRO D 519 ? 0.5484 0.2387 0.3674 0.0695  -0.1171 -0.0672 519 PRO D CD  
10029 N N   . GLU D 520 ? 0.6475 0.3161 0.4121 0.0720  -0.0792 -0.1041 520 GLU D N   
10030 C CA  . GLU D 520 ? 0.6461 0.3337 0.4189 0.0728  -0.0602 -0.1168 520 GLU D CA  
10031 C C   . GLU D 520 ? 0.6366 0.3384 0.4108 0.0646  -0.0461 -0.1150 520 GLU D C   
10032 O O   . GLU D 520 ? 0.6296 0.3553 0.4191 0.0644  -0.0305 -0.1255 520 GLU D O   
10033 C CB  . GLU D 520 ? 0.6817 0.3537 0.4269 0.0709  -0.0508 -0.1300 520 GLU D CB  
10034 C CG  . GLU D 520 ? 0.6946 0.3592 0.4432 0.0769  -0.0622 -0.1304 520 GLU D CG  
10035 C CD  . GLU D 520 ? 0.6785 0.3635 0.4601 0.0886  -0.0624 -0.1375 520 GLU D CD  
10036 O OE1 . GLU D 520 ? 0.6576 0.3655 0.4594 0.0927  -0.0523 -0.1451 520 GLU D OE1 
10037 O OE2 . GLU D 520 ? 0.6838 0.3617 0.4707 0.0935  -0.0733 -0.1355 520 GLU D OE2 
10038 N N   . SER D 521 ? 0.6230 0.3107 0.3822 0.0580  -0.0517 -0.1032 521 SER D N   
10039 C CA  . SER D 521 ? 0.6150 0.3127 0.3761 0.0503  -0.0406 -0.0999 521 SER D CA  
10040 C C   . SER D 521 ? 0.5774 0.3071 0.3795 0.0548  -0.0422 -0.0961 521 SER D C   
10041 O O   . SER D 521 ? 0.5728 0.3152 0.3811 0.0487  -0.0317 -0.0953 521 SER D O   
10042 C CB  . SER D 521 ? 0.6337 0.3025 0.3658 0.0446  -0.0493 -0.0884 521 SER D CB  
10043 O OG  . SER D 521 ? 0.6384 0.3120 0.3694 0.0370  -0.0387 -0.0853 521 SER D OG  
10044 N N   . ILE D 522 ? 0.5707 0.3109 0.3977 0.0643  -0.0549 -0.0936 522 ILE D N   
10045 C CA  . ILE D 522 ? 0.5386 0.3069 0.4006 0.0684  -0.0568 -0.0901 522 ILE D CA  
10046 C C   . ILE D 522 ? 0.5331 0.3289 0.4115 0.0686  -0.0407 -0.1015 522 ILE D C   
10047 O O   . ILE D 522 ? 0.5133 0.3332 0.4167 0.0698  -0.0398 -0.0994 522 ILE D O   
10048 C CB  . ILE D 522 ? 0.5260 0.2942 0.4042 0.0773  -0.0723 -0.0866 522 ILE D CB  
10049 C CG1 . ILE D 522 ? 0.4981 0.2870 0.4040 0.0786  -0.0775 -0.0786 522 ILE D CG1 
10050 C CG2 . ILE D 522 ? 0.5344 0.3059 0.4167 0.0858  -0.0692 -0.0985 522 ILE D CG2 
10051 C CD1 . ILE D 522 ? 0.4924 0.2766 0.4092 0.0844  -0.0918 -0.0737 522 ILE D CD1 
10052 N N   . SER D 523 ? 0.5469 0.3414 0.4125 0.0670  -0.0278 -0.1149 523 SER D N   
10053 C CA  . SER D 523 ? 0.5407 0.3653 0.4243 0.0663  -0.0113 -0.1289 523 SER D CA  
10054 C C   . SER D 523 ? 0.5411 0.3777 0.4261 0.0545  0.0009  -0.1270 523 SER D C   
10055 O O   . SER D 523 ? 0.5328 0.4009 0.4414 0.0540  0.0113  -0.1367 523 SER D O   
10056 C CB  . SER D 523 ? 0.5660 0.3855 0.4325 0.0642  0.0024  -0.1451 523 SER D CB  
10057 O OG  . SER D 523 ? 0.5681 0.4222 0.4588 0.0657  0.0170  -0.1621 523 SER D OG  
10058 N N   . ASN D 524 ? 0.5651 0.3770 0.4257 0.0456  -0.0011 -0.1154 524 ASN D N   
10059 C CA  . ASN D 524 ? 0.5779 0.3915 0.4310 0.0330  0.0113  -0.1139 524 ASN D CA  
10060 C C   . ASN D 524 ? 0.5486 0.3887 0.4333 0.0347  0.0082  -0.1091 524 ASN D C   
10061 O O   . ASN D 524 ? 0.5556 0.3969 0.4357 0.0244  0.0178  -0.1079 524 ASN D O   
10062 C CB  . ASN D 524 ? 0.5944 0.3682 0.4098 0.0260  0.0060  -0.1024 524 ASN D CB  
10063 C CG  . ASN D 524 ? 0.6278 0.3749 0.4025 0.0164  0.0182  -0.1091 524 ASN D CG  
10064 O OD1 . ASN D 524 ? 0.6344 0.3960 0.4109 0.0127  0.0340  -0.1239 524 ASN D OD1 
10065 N ND2 . ASN D 524 ? 0.6534 0.3613 0.3904 0.0123  0.0106  -0.0991 524 ASN D ND2 
10066 N N   . ILE D 525 ? 0.5117 0.3700 0.4247 0.0465  -0.0046 -0.1063 525 ILE D N   
10067 C CA  . ILE D 525 ? 0.4829 0.3635 0.4218 0.0477  -0.0088 -0.1008 525 ILE D CA  
10068 C C   . ILE D 525 ? 0.4663 0.3820 0.4351 0.0547  -0.0059 -0.1118 525 ILE D C   
10069 O O   . ILE D 525 ? 0.4455 0.3766 0.4355 0.0613  -0.0160 -0.1068 525 ILE D O   
10070 C CB  . ILE D 525 ? 0.4704 0.3403 0.4141 0.0535  -0.0273 -0.0866 525 ILE D CB  
10071 C CG1 . ILE D 525 ? 0.4766 0.3358 0.4195 0.0634  -0.0397 -0.0859 525 ILE D CG1 
10072 C CG2 . ILE D 525 ? 0.4818 0.3260 0.4043 0.0469  -0.0304 -0.0772 525 ILE D CG2 
10073 C CD1 . ILE D 525 ? 0.4640 0.3181 0.4159 0.0672  -0.0561 -0.0740 525 ILE D CD1 
10074 N N   . ASN D 526 ? 0.4975 0.4259 0.4674 0.0533  0.0076  -0.1275 526 ASN D N   
10075 C CA  . ASN D 526 ? 0.4786 0.4396 0.4775 0.0637  0.0078  -0.1409 526 ASN D CA  
10076 C C   . ASN D 526 ? 0.4525 0.4433 0.4788 0.0656  0.0044  -0.1400 526 ASN D C   
10077 O O   . ASN D 526 ? 0.4323 0.4457 0.4822 0.0781  -0.0032 -0.1468 526 ASN D O   
10078 C CB  . ASN D 526 ? 0.4862 0.4623 0.4845 0.0577  0.0274  -0.1608 526 ASN D CB  
10079 C CG  . ASN D 526 ? 0.4890 0.4697 0.4777 0.0387  0.0463  -0.1643 526 ASN D CG  
10080 O OD1 . ASN D 526 ? 0.4880 0.4596 0.4708 0.0317  0.0438  -0.1518 526 ASN D OD1 
10081 N ND2 . ASN D 526 ? 0.5069 0.5013 0.4938 0.0297  0.0660  -0.1823 526 ASN D ND2 
10082 N N   . ARG D 527 ? 0.4910 0.4809 0.5134 0.0542  0.0088  -0.1323 527 ARG D N   
10083 C CA  . ARG D 527 ? 0.4651 0.4800 0.5102 0.0552  0.0044  -0.1301 527 ARG D CA  
10084 C C   . ARG D 527 ? 0.4577 0.4642 0.5075 0.0650  -0.0151 -0.1158 527 ARG D C   
10085 O O   . ARG D 527 ? 0.4426 0.4672 0.5078 0.0659  -0.0199 -0.1129 527 ARG D O   
10086 C CB  . ARG D 527 ? 0.4688 0.4820 0.5063 0.0395  0.0157  -0.1269 527 ARG D CB  
10087 C CG  . ARG D 527 ? 0.4721 0.5006 0.5093 0.0268  0.0366  -0.1426 527 ARG D CG  
10088 C CD  . ARG D 527 ? 0.4712 0.5026 0.5068 0.0127  0.0456  -0.1403 527 ARG D CD  
10089 N NE  . ARG D 527 ? 0.4714 0.5267 0.5148 0.0000  0.0650  -0.1575 527 ARG D NE  
10090 C CZ  . ARG D 527 ? 0.4532 0.5483 0.5262 -0.0001 0.0674  -0.1690 527 ARG D CZ  
10091 N NH1 . ARG D 527 ? 0.4252 0.5383 0.5196 0.0123  0.0512  -0.1640 527 ARG D NH1 
10092 N NH2 . ARG D 527 ? 0.4438 0.5609 0.5238 -0.0138 0.0865  -0.1863 527 ARG D NH2 
10093 N N   . ILE D 528 ? 0.4386 0.4180 0.4742 0.0708  -0.0256 -0.1074 528 ILE D N   
10094 C CA  . ILE D 528 ? 0.4307 0.4000 0.4684 0.0771  -0.0422 -0.0944 528 ILE D CA  
10095 C C   . ILE D 528 ? 0.4166 0.4037 0.4721 0.0895  -0.0519 -0.0985 528 ILE D C   
10096 O O   . ILE D 528 ? 0.4121 0.4105 0.4760 0.0984  -0.0504 -0.1112 528 ILE D O   
10097 C CB  . ILE D 528 ? 0.4421 0.3793 0.4609 0.0792  -0.0504 -0.0872 528 ILE D CB  
10098 C CG1 . ILE D 528 ? 0.4313 0.3569 0.4506 0.0808  -0.0650 -0.0737 528 ILE D CG1 
10099 C CG2 . ILE D 528 ? 0.4505 0.3824 0.4663 0.0889  -0.0514 -0.0971 528 ILE D CG2 
10100 C CD1 . ILE D 528 ? 0.4252 0.3567 0.4484 0.0715  -0.0635 -0.0656 528 ILE D CD1 
10101 N N   . SER D 529 ? 0.4060 0.3953 0.4665 0.0903  -0.0620 -0.0884 529 SER D N   
10102 C CA  . SER D 529 ? 0.3950 0.3945 0.4663 0.1024  -0.0741 -0.0898 529 SER D CA  
10103 C C   . SER D 529 ? 0.3968 0.3717 0.4566 0.1047  -0.0891 -0.0753 529 SER D C   
10104 O O   . SER D 529 ? 0.4032 0.3711 0.4623 0.1165  -0.1018 -0.0748 529 SER D O   
10105 C CB  . SER D 529 ? 0.3806 0.4114 0.4684 0.1001  -0.0710 -0.0945 529 SER D CB  
10106 O OG  . SER D 529 ? 0.3777 0.4073 0.4613 0.0874  -0.0675 -0.0846 529 SER D OG  
10107 N N   . LYS D 530 ? 0.3983 0.3593 0.4486 0.0933  -0.0880 -0.0642 530 LYS D N   
10108 C CA  . LYS D 530 ? 0.4015 0.3388 0.4404 0.0917  -0.0993 -0.0518 530 LYS D CA  
10109 C C   . LYS D 530 ? 0.4085 0.3262 0.4371 0.0849  -0.0971 -0.0481 530 LYS D C   
10110 O O   . LYS D 530 ? 0.4078 0.3305 0.4377 0.0757  -0.0894 -0.0468 530 LYS D O   
10111 C CB  . LYS D 530 ? 0.3951 0.3403 0.4359 0.0837  -0.1013 -0.0432 530 LYS D CB  
10112 C CG  . LYS D 530 ? 0.3991 0.3550 0.4430 0.0912  -0.1092 -0.0437 530 LYS D CG  
10113 C CD  . LYS D 530 ? 0.4087 0.3600 0.4449 0.0820  -0.1136 -0.0325 530 LYS D CD  
10114 C CE  . LYS D 530 ? 0.4057 0.3687 0.4422 0.0884  -0.1214 -0.0330 530 LYS D CE  
10115 N NZ  . LYS D 530 ? 0.4120 0.3825 0.4446 0.0759  -0.1188 -0.0260 530 LYS D NZ  
10116 N N   . LEU D 531 ? 0.3743 0.2685 0.3922 0.0900  -0.1049 -0.0470 531 LEU D N   
10117 C CA  . LEU D 531 ? 0.3805 0.2553 0.3878 0.0848  -0.1053 -0.0448 531 LEU D CA  
10118 C C   . LEU D 531 ? 0.3927 0.2468 0.3923 0.0812  -0.1163 -0.0357 531 LEU D C   
10119 O O   . LEU D 531 ? 0.4122 0.2485 0.4039 0.0881  -0.1248 -0.0356 531 LEU D O   
10120 C CB  . LEU D 531 ? 0.3941 0.2596 0.3938 0.0923  -0.1026 -0.0545 531 LEU D CB  
10121 C CG  . LEU D 531 ? 0.4008 0.2512 0.3874 0.0870  -0.0995 -0.0556 531 LEU D CG  
10122 C CD1 . LEU D 531 ? 0.4128 0.2622 0.3926 0.0926  -0.0917 -0.0675 531 LEU D CD1 
10123 C CD2 . LEU D 531 ? 0.4144 0.2404 0.3911 0.0850  -0.1109 -0.0494 531 LEU D CD2 
10124 N N   . GLN D 532 ? 0.3893 0.2455 0.3916 0.0698  -0.1160 -0.0291 532 GLN D N   
10125 C CA  . GLN D 532 ? 0.4006 0.2412 0.3976 0.0623  -0.1239 -0.0216 532 GLN D CA  
10126 C C   . GLN D 532 ? 0.4020 0.2349 0.3982 0.0553  -0.1253 -0.0219 532 GLN D C   
10127 O O   . GLN D 532 ? 0.3978 0.2445 0.4040 0.0479  -0.1216 -0.0211 532 GLN D O   
10128 C CB  . GLN D 532 ? 0.4009 0.2546 0.4039 0.0540  -0.1222 -0.0154 532 GLN D CB  
10129 C CG  . GLN D 532 ? 0.4010 0.2625 0.4034 0.0615  -0.1231 -0.0152 532 GLN D CG  
10130 C CD  . GLN D 532 ? 0.4041 0.2832 0.4121 0.0528  -0.1189 -0.0109 532 GLN D CD  
10131 O OE1 . GLN D 532 ? 0.3856 0.2876 0.4041 0.0543  -0.1120 -0.0151 532 GLN D OE1 
10132 N NE2 . GLN D 532 ? 0.4318 0.2998 0.4315 0.0421  -0.1222 -0.0034 532 GLN D NE2 
10133 N N   . LEU D 533 ? 0.4045 0.2156 0.3895 0.0585  -0.1317 -0.0240 533 LEU D N   
10134 C CA  . LEU D 533 ? 0.4099 0.2114 0.3926 0.0522  -0.1363 -0.0248 533 LEU D CA  
10135 C C   . LEU D 533 ? 0.4290 0.2116 0.4058 0.0450  -0.1446 -0.0212 533 LEU D C   
10136 O O   . LEU D 533 ? 0.4395 0.2105 0.4125 0.0409  -0.1505 -0.0236 533 LEU D O   
10137 C CB  . LEU D 533 ? 0.4189 0.2094 0.3905 0.0596  -0.1364 -0.0313 533 LEU D CB  
10138 C CG  . LEU D 533 ? 0.4071 0.2112 0.3795 0.0645  -0.1267 -0.0355 533 LEU D CG  
10139 C CD1 . LEU D 533 ? 0.4227 0.2115 0.3786 0.0686  -0.1265 -0.0416 533 LEU D CD1 
10140 C CD2 . LEU D 533 ? 0.3879 0.2101 0.3724 0.0583  -0.1226 -0.0329 533 LEU D CD2 
10141 N N   . ASN D 534 ? 0.4593 0.2367 0.4328 0.0425  -0.1457 -0.0157 534 ASN D N   
10142 C CA  . ASN D 534 ? 0.4846 0.2380 0.4470 0.0344  -0.1528 -0.0118 534 ASN D CA  
10143 C C   . ASN D 534 ? 0.4977 0.2598 0.4700 0.0173  -0.1521 -0.0107 534 ASN D C   
10144 O O   . ASN D 534 ? 0.4867 0.2748 0.4757 0.0126  -0.1464 -0.0118 534 ASN D O   
10145 C CB  . ASN D 534 ? 0.4998 0.2420 0.4516 0.0364  -0.1546 -0.0053 534 ASN D CB  
10146 C CG  . ASN D 534 ? 0.4921 0.2583 0.4536 0.0305  -0.1478 -0.0010 534 ASN D CG  
10147 O OD1 . ASN D 534 ? 0.4719 0.2617 0.4451 0.0375  -0.1418 -0.0041 534 ASN D OD1 
10148 N ND2 . ASN D 534 ? 0.5242 0.2837 0.4794 0.0162  -0.1476 0.0056  534 ASN D ND2 
10149 N N   . GLY D 535 ? 0.5336 0.2737 0.4964 0.0076  -0.1580 -0.0098 535 GLY D N   
10150 C CA  . GLY D 535 ? 0.5442 0.2939 0.5182 -0.0103 -0.1570 -0.0111 535 GLY D CA  
10151 C C   . GLY D 535 ? 0.5250 0.2943 0.5166 -0.0095 -0.1588 -0.0191 535 GLY D C   
10152 O O   . GLY D 535 ? 0.5131 0.3096 0.5247 -0.0157 -0.1545 -0.0216 535 GLY D O   
10153 N N   . ASN D 536 ? 0.5319 0.2863 0.5149 -0.0011 -0.1658 -0.0236 536 ASN D N   
10154 C CA  . ASN D 536 ? 0.5139 0.2811 0.5074 0.0018  -0.1703 -0.0307 536 ASN D CA  
10155 C C   . ASN D 536 ? 0.5320 0.2762 0.5130 0.0008  -0.1802 -0.0356 536 ASN D C   
10156 O O   . ASN D 536 ? 0.5520 0.2720 0.5192 -0.0041 -0.1826 -0.0339 536 ASN D O   
10157 C CB  . ASN D 536 ? 0.4970 0.2729 0.4889 0.0166  -0.1664 -0.0311 536 ASN D CB  
10158 C CG  . ASN D 536 ? 0.4852 0.2897 0.4962 0.0151  -0.1596 -0.0304 536 ASN D CG  
10159 O OD1 . ASN D 536 ? 0.4789 0.2990 0.5052 0.0121  -0.1629 -0.0348 536 ASN D OD1 
10160 N ND2 . ASN D 536 ? 0.4802 0.2920 0.4911 0.0181  -0.1510 -0.0257 536 ASN D ND2 
10161 N N   . ARG D 537 ? 0.5612 0.3102 0.5447 0.0058  -0.1867 -0.0419 537 ARG D N   
10162 C CA  . ARG D 537 ? 0.5815 0.3113 0.5518 0.0060  -0.1964 -0.0473 537 ARG D CA  
10163 C C   . ARG D 537 ? 0.5865 0.3069 0.5371 0.0210  -0.1954 -0.0479 537 ARG D C   
10164 O O   . ARG D 537 ? 0.6054 0.3204 0.5471 0.0234  -0.2028 -0.0525 537 ARG D O   
10165 C CB  . ARG D 537 ? 0.5839 0.3298 0.5714 -0.0020 -0.2057 -0.0546 537 ARG D CB  
10166 C CG  . ARG D 537 ? 0.5781 0.3476 0.5917 -0.0171 -0.2026 -0.0559 537 ARG D CG  
10167 C CD  . ARG D 537 ? 0.5921 0.3678 0.6160 -0.0300 -0.2087 -0.0630 537 ARG D CD  
10168 N NE  . ARG D 537 ? 0.5931 0.3844 0.6275 -0.0230 -0.2188 -0.0705 537 ARG D NE  
10169 C CZ  . ARG D 537 ? 0.6199 0.4073 0.6509 -0.0251 -0.2269 -0.0762 537 ARG D CZ  
10170 N NH1 . ARG D 537 ? 0.6406 0.4097 0.6593 -0.0353 -0.2253 -0.0761 537 ARG D NH1 
10171 N NH2 . ARG D 537 ? 0.6098 0.4101 0.6487 -0.0165 -0.2372 -0.0822 537 ARG D NH2 
10172 N N   . LEU D 538 ? 0.5394 0.2599 0.4829 0.0299  -0.1859 -0.0440 538 LEU D N   
10173 C CA  . LEU D 538 ? 0.5452 0.2602 0.4708 0.0409  -0.1817 -0.0461 538 LEU D CA  
10174 C C   . LEU D 538 ? 0.5701 0.2664 0.4783 0.0422  -0.1837 -0.0490 538 LEU D C   
10175 O O   . LEU D 538 ? 0.5795 0.2671 0.4868 0.0397  -0.1829 -0.0469 538 LEU D O   
10176 C CB  . LEU D 538 ? 0.5301 0.2545 0.4569 0.0482  -0.1700 -0.0436 538 LEU D CB  
10177 C CG  . LEU D 538 ? 0.5060 0.2485 0.4500 0.0470  -0.1664 -0.0405 538 LEU D CG  
10178 C CD1 . LEU D 538 ? 0.4943 0.2448 0.4439 0.0504  -0.1575 -0.0369 538 LEU D CD1 
10179 C CD2 . LEU D 538 ? 0.5022 0.2488 0.4402 0.0518  -0.1647 -0.0428 538 LEU D CD2 
10180 N N   . SER D 539 ? 0.5686 0.2562 0.4606 0.0464  -0.1866 -0.0537 539 SER D N   
10181 C CA  . SER D 539 ? 0.5947 0.2641 0.4702 0.0471  -0.1896 -0.0578 539 SER D CA  
10182 C C   . SER D 539 ? 0.6048 0.2672 0.4616 0.0564  -0.1820 -0.0623 539 SER D C   
10183 O O   . SER D 539 ? 0.5914 0.2632 0.4493 0.0616  -0.1731 -0.0620 539 SER D O   
10184 C CB  . SER D 539 ? 0.6093 0.2724 0.4821 0.0406  -0.2022 -0.0610 539 SER D CB  
10185 O OG  . SER D 539 ? 0.6070 0.2745 0.4748 0.0439  -0.2068 -0.0624 539 SER D OG  
10186 N N   . GLY D 540 ? 0.6181 0.2637 0.4582 0.0578  -0.1842 -0.0675 540 GLY D N   
10187 C CA  . GLY D 540 ? 0.6320 0.2696 0.4542 0.0654  -0.1759 -0.0738 540 GLY D CA  
10188 C C   . GLY D 540 ? 0.6272 0.2691 0.4566 0.0728  -0.1659 -0.0758 540 GLY D C   
10189 O O   . GLY D 540 ? 0.6168 0.2643 0.4610 0.0724  -0.1666 -0.0712 540 GLY D O   
10190 N N   . LYS D 541 ? 0.6427 0.2810 0.4602 0.0797  -0.1566 -0.0838 541 LYS D N   
10191 C CA  . LYS D 541 ? 0.6404 0.2849 0.4669 0.0887  -0.1479 -0.0886 541 LYS D CA  
10192 C C   . LYS D 541 ? 0.6139 0.2785 0.4552 0.0914  -0.1404 -0.0862 541 LYS D C   
10193 O O   . LYS D 541 ? 0.6024 0.2729 0.4412 0.0871  -0.1384 -0.0833 541 LYS D O   
10194 C CB  . LYS D 541 ? 0.6641 0.2997 0.4755 0.0948  -0.1396 -0.1011 541 LYS D CB  
10195 C CG  . LYS D 541 ? 0.6647 0.3045 0.4638 0.0940  -0.1286 -0.1068 541 LYS D CG  
10196 C CD  . LYS D 541 ? 0.6899 0.3231 0.4757 0.0987  -0.1178 -0.1214 541 LYS D CD  
10197 C CE  . LYS D 541 ? 0.7025 0.3312 0.4646 0.0928  -0.1079 -0.1265 541 LYS D CE  
10198 N NZ  . LYS D 541 ? 0.7220 0.3310 0.4590 0.0850  -0.1177 -0.1214 541 LYS D NZ  
10199 N N   . ILE D 542 ? 0.5856 0.2594 0.4417 0.0989  -0.1374 -0.0874 542 ILE D N   
10200 C CA  . ILE D 542 ? 0.5632 0.2570 0.4343 0.1029  -0.1300 -0.0875 542 ILE D CA  
10201 C C   . ILE D 542 ? 0.5695 0.2681 0.4334 0.1074  -0.1171 -0.0999 542 ILE D C   
10202 O O   . ILE D 542 ? 0.5880 0.2828 0.4479 0.1141  -0.1124 -0.1108 542 ILE D O   
10203 C CB  . ILE D 542 ? 0.5588 0.2601 0.4459 0.1105  -0.1328 -0.0858 542 ILE D CB  
10204 C CG1 . ILE D 542 ? 0.5546 0.2499 0.4451 0.1027  -0.1430 -0.0733 542 ILE D CG1 
10205 C CG2 . ILE D 542 ? 0.5391 0.2630 0.4419 0.1167  -0.1248 -0.0894 542 ILE D CG2 
10206 C CD1 . ILE D 542 ? 0.5500 0.2518 0.4522 0.1078  -0.1457 -0.0691 542 ILE D CD1 
10207 N N   . PRO D 543 ? 0.5907 0.2971 0.4520 0.1030  -0.1101 -0.0997 543 PRO D N   
10208 C CA  . PRO D 543 ? 0.6046 0.3122 0.4528 0.1034  -0.0958 -0.1123 543 PRO D CA  
10209 C C   . PRO D 543 ? 0.6000 0.3271 0.4657 0.1135  -0.0857 -0.1253 543 PRO D C   
10210 O O   . PRO D 543 ? 0.5800 0.3250 0.4684 0.1192  -0.0878 -0.1230 543 PRO D O   
10211 C CB  . PRO D 543 ? 0.5906 0.3011 0.4331 0.0958  -0.0920 -0.1070 543 PRO D CB  
10212 C CG  . PRO D 543 ? 0.5638 0.2861 0.4286 0.0960  -0.1009 -0.0953 543 PRO D CG  
10213 C CD  . PRO D 543 ? 0.5680 0.2824 0.4375 0.0968  -0.1137 -0.0888 543 PRO D CD  
10214 N N   . SER D 544 ? 0.6244 0.3498 0.4798 0.1154  -0.0749 -0.1398 544 SER D N   
10215 C CA  . SER D 544 ? 0.6232 0.3723 0.4980 0.1247  -0.0639 -0.1553 544 SER D CA  
10216 C C   . SER D 544 ? 0.6059 0.3791 0.4909 0.1218  -0.0511 -0.1612 544 SER D C   
10217 O O   . SER D 544 ? 0.6007 0.4016 0.5096 0.1295  -0.0436 -0.1730 544 SER D O   
10218 C CB  . SER D 544 ? 0.6523 0.3959 0.5140 0.1252  -0.0530 -0.1710 544 SER D CB  
10219 O OG  . SER D 544 ? 0.6675 0.4055 0.5040 0.1131  -0.0384 -0.1774 544 SER D OG  
10220 N N   . GLY D 545 ? 0.6190 0.3830 0.4872 0.1108  -0.0490 -0.1535 545 GLY D N   
10221 C CA  . GLY D 545 ? 0.6010 0.3908 0.4801 0.1031  -0.0356 -0.1539 545 GLY D CA  
10222 C C   . GLY D 545 ? 0.5742 0.3885 0.4851 0.1091  -0.0423 -0.1471 545 GLY D C   
10223 O O   . GLY D 545 ? 0.5589 0.3987 0.4832 0.1040  -0.0310 -0.1503 545 GLY D O   
10224 N N   . ILE D 546 ? 0.5627 0.3679 0.4833 0.1181  -0.0600 -0.1380 546 ILE D N   
10225 C CA  . ILE D 546 ? 0.5392 0.3647 0.4859 0.1241  -0.0670 -0.1321 546 ILE D CA  
10226 C C   . ILE D 546 ? 0.5374 0.3912 0.5081 0.1362  -0.0615 -0.1486 546 ILE D C   
10227 O O   . ILE D 546 ? 0.5181 0.3967 0.5104 0.1392  -0.0625 -0.1474 546 ILE D O   
10228 C CB  . ILE D 546 ? 0.5410 0.3447 0.4864 0.1291  -0.0863 -0.1191 546 ILE D CB  
10229 C CG1 . ILE D 546 ? 0.5418 0.3237 0.4684 0.1168  -0.0916 -0.1057 546 ILE D CG1 
10230 C CG2 . ILE D 546 ? 0.5222 0.3425 0.4886 0.1338  -0.0939 -0.1118 546 ILE D CG2 
10231 C CD1 . ILE D 546 ? 0.5366 0.3085 0.4667 0.1146  -0.1063 -0.0908 546 ILE D CD1 
10232 N N   . ARG D 547 ? 0.5552 0.4089 0.5237 0.1424  -0.0552 -0.1640 547 ARG D N   
10233 C CA  . ARG D 547 ? 0.5545 0.4413 0.5492 0.1519  -0.0486 -0.1798 547 ARG D CA  
10234 C C   . ARG D 547 ? 0.5369 0.4578 0.5472 0.1452  -0.0330 -0.1899 547 ARG D C   
10235 O O   . ARG D 547 ? 0.5265 0.4805 0.5652 0.1525  -0.0328 -0.1979 547 ARG D O   
10236 C CB  . ARG D 547 ? 0.5807 0.4639 0.5685 0.1542  -0.0398 -0.1941 547 ARG D CB  
10237 C CG  . ARG D 547 ? 0.5919 0.4751 0.5606 0.1398  -0.0186 -0.2050 547 ARG D CG  
10238 C CD  . ARG D 547 ? 0.6203 0.5003 0.5810 0.1409  -0.0083 -0.2197 547 ARG D CD  
10239 N NE  . ARG D 547 ? 0.6448 0.5398 0.5968 0.1270  0.0161  -0.2341 547 ARG D NE  
10240 C CZ  . ARG D 547 ? 0.6607 0.5313 0.5762 0.1114  0.0265  -0.2325 547 ARG D CZ  
10241 N NH1 . ARG D 547 ? 0.6534 0.4866 0.5410 0.1087  0.0133  -0.2177 547 ARG D NH1 
10242 N NH2 . ARG D 547 ? 0.6628 0.5461 0.5681 0.0972  0.0497  -0.2449 547 ARG D NH2 
10243 N N   . LEU D 548 ? 0.4960 0.4101 0.4867 0.1279  -0.0202 -0.1862 548 LEU D N   
10244 C CA  . LEU D 548 ? 0.4845 0.4278 0.4849 0.1157  -0.0023 -0.1935 548 LEU D CA  
10245 C C   . LEU D 548 ? 0.4578 0.4123 0.4700 0.1113  -0.0084 -0.1790 548 LEU D C   
10246 O O   . LEU D 548 ? 0.4483 0.4245 0.4674 0.0998  0.0056  -0.1836 548 LEU D O   
10247 C CB  . LEU D 548 ? 0.5038 0.4294 0.4718 0.0971  0.0151  -0.1946 548 LEU D CB  
10248 C CG  . LEU D 548 ? 0.5341 0.4500 0.4862 0.0976  0.0256  -0.2111 548 LEU D CG  
10249 C CD1 . LEU D 548 ? 0.5573 0.4560 0.4739 0.0768  0.0444  -0.2122 548 LEU D CD1 
10250 C CD2 . LEU D 548 ? 0.5338 0.4878 0.5184 0.1068  0.0336  -0.2312 548 LEU D CD2 
10251 N N   . LEU D 549 ? 0.4985 0.4383 0.5121 0.1185  -0.0277 -0.1626 549 LEU D N   
10252 C CA  . LEU D 549 ? 0.4765 0.4286 0.5024 0.1153  -0.0336 -0.1504 549 LEU D CA  
10253 C C   . LEU D 549 ? 0.4654 0.4460 0.5210 0.1299  -0.0416 -0.1586 549 LEU D C   
10254 O O   . LEU D 549 ? 0.4662 0.4383 0.5260 0.1400  -0.0591 -0.1487 549 LEU D O   
10255 C CB  . LEU D 549 ? 0.4800 0.4026 0.4908 0.1131  -0.0484 -0.1298 549 LEU D CB  
10256 C CG  . LEU D 549 ? 0.4960 0.3860 0.4779 0.1046  -0.0477 -0.1228 549 LEU D CG  
10257 C CD1 . LEU D 549 ? 0.4891 0.3577 0.4641 0.1033  -0.0633 -0.1052 549 LEU D CD1 
10258 C CD2 . LEU D 549 ? 0.5037 0.3943 0.4715 0.0896  -0.0317 -0.1242 549 LEU D CD2 
10259 N N   . THR D 550 ? 0.4408 0.4556 0.5161 0.1304  -0.0286 -0.1776 550 THR D N   
10260 C CA  . THR D 550 ? 0.4369 0.4816 0.5424 0.1472  -0.0372 -0.1899 550 THR D CA  
10261 C C   . THR D 550 ? 0.4178 0.4764 0.5356 0.1476  -0.0474 -0.1793 550 THR D C   
10262 O O   . THR D 550 ? 0.4195 0.4874 0.5528 0.1640  -0.0634 -0.1811 550 THR D O   
10263 C CB  . THR D 550 ? 0.4402 0.5222 0.5655 0.1440  -0.0196 -0.2129 550 THR D CB  
10264 O OG1 . THR D 550 ? 0.4249 0.5291 0.5558 0.1278  -0.0036 -0.2172 550 THR D OG1 
10265 C CG2 . THR D 550 ? 0.4625 0.5291 0.5703 0.1389  -0.0067 -0.2212 550 THR D CG2 
10266 N N   . ASN D 551 ? 0.4468 0.5051 0.5563 0.1304  -0.0393 -0.1686 551 ASN D N   
10267 C CA  . ASN D 551 ? 0.4332 0.5037 0.5519 0.1289  -0.0475 -0.1588 551 ASN D CA  
10268 C C   . ASN D 551 ? 0.4391 0.4794 0.5431 0.1336  -0.0660 -0.1385 551 ASN D C   
10269 O O   . ASN D 551 ? 0.4210 0.4674 0.5284 0.1312  -0.0729 -0.1290 551 ASN D O   
10270 C CB  . ASN D 551 ? 0.4170 0.4956 0.5312 0.1088  -0.0318 -0.1556 551 ASN D CB  
10271 C CG  . ASN D 551 ? 0.4140 0.5333 0.5509 0.1036  -0.0174 -0.1749 551 ASN D CG  
10272 O OD1 . ASN D 551 ? 0.4244 0.5502 0.5589 0.0945  0.0005  -0.1878 551 ASN D OD1 
10273 N ND2 . ASN D 551 ? 0.4063 0.5532 0.5641 0.1082  -0.0248 -0.1777 551 ASN D ND2 
10274 N N   . LEU D 552 ? 0.4353 0.4434 0.5222 0.1385  -0.0731 -0.1324 552 LEU D N   
10275 C CA  . LEU D 552 ? 0.4373 0.4156 0.5094 0.1403  -0.0890 -0.1144 552 LEU D CA  
10276 C C   . LEU D 552 ? 0.4457 0.4290 0.5267 0.1545  -0.1058 -0.1128 552 LEU D C   
10277 O O   . LEU D 552 ? 0.4578 0.4487 0.5499 0.1711  -0.1126 -0.1250 552 LEU D O   
10278 C CB  . LEU D 552 ? 0.4564 0.4013 0.5103 0.1435  -0.0933 -0.1120 552 LEU D CB  
10279 C CG  . LEU D 552 ? 0.4562 0.3757 0.4898 0.1294  -0.0909 -0.0988 552 LEU D CG  
10280 C CD1 . LEU D 552 ? 0.4769 0.3653 0.4941 0.1340  -0.0972 -0.0986 552 LEU D CD1 
10281 C CD2 . LEU D 552 ? 0.4505 0.3640 0.4814 0.1221  -0.0988 -0.0826 552 LEU D CD2 
10282 N N   . GLU D 553 ? 0.4487 0.4267 0.5237 0.1482  -0.1129 -0.0982 553 GLU D N   
10283 C CA  . GLU D 553 ? 0.4582 0.4307 0.5318 0.1593  -0.1307 -0.0925 553 GLU D CA  
10284 C C   . GLU D 553 ? 0.4811 0.4130 0.5299 0.1563  -0.1423 -0.0755 553 GLU D C   
10285 O O   . GLU D 553 ? 0.5032 0.4192 0.5407 0.1625  -0.1536 -0.0717 553 GLU D O   
10286 C CB  . GLU D 553 ? 0.4423 0.4398 0.5245 0.1526  -0.1297 -0.0896 553 GLU D CB  
10287 C CG  . GLU D 553 ? 0.4249 0.4648 0.5321 0.1528  -0.1183 -0.1067 553 GLU D CG  
10288 C CD  . GLU D 553 ? 0.4080 0.4692 0.5206 0.1419  -0.1147 -0.1029 553 GLU D CD  
10289 O OE1 . GLU D 553 ? 0.4118 0.4560 0.5092 0.1364  -0.1226 -0.0876 553 GLU D OE1 
10290 O OE2 . GLU D 553 ? 0.3930 0.4878 0.5244 0.1375  -0.1033 -0.1160 553 GLU D OE2 
10291 N N   . TYR D 554 ? 0.4454 0.3619 0.4829 0.1415  -0.1361 -0.0654 554 TYR D N   
10292 C CA  . TYR D 554 ? 0.4591 0.3417 0.4760 0.1350  -0.1452 -0.0503 554 TYR D CA  
10293 C C   . TYR D 554 ? 0.4592 0.3251 0.4684 0.1263  -0.1387 -0.0489 554 TYR D C   
10294 O O   . TYR D 554 ? 0.4433 0.3215 0.4571 0.1146  -0.1272 -0.0487 554 TYR D O   
10295 C CB  . TYR D 554 ? 0.4497 0.3385 0.4631 0.1218  -0.1445 -0.0389 554 TYR D CB  
10296 C CG  . TYR D 554 ? 0.4690 0.3266 0.4618 0.1119  -0.1517 -0.0245 554 TYR D CG  
10297 C CD1 . TYR D 554 ? 0.4643 0.3121 0.4531 0.0978  -0.1452 -0.0195 554 TYR D CD1 
10298 C CD2 . TYR D 554 ? 0.4951 0.3330 0.4715 0.1158  -0.1650 -0.0164 554 TYR D CD2 
10299 C CE1 . TYR D 554 ? 0.4786 0.3018 0.4513 0.0865  -0.1502 -0.0085 554 TYR D CE1 
10300 C CE2 . TYR D 554 ? 0.5160 0.3240 0.4710 0.1036  -0.1695 -0.0037 554 TYR D CE2 
10301 C CZ  . TYR D 554 ? 0.5056 0.3085 0.4607 0.0882  -0.1611 -0.0006 554 TYR D CZ  
10302 O OH  . TYR D 554 ? 0.5362 0.3129 0.4726 0.0740  -0.1640 0.0099  554 TYR D OH  
10303 N N   . LEU D 555 ? 0.4395 0.2791 0.4350 0.1293  -0.1446 -0.0481 555 LEU D N   
10304 C CA  . LEU D 555 ? 0.4422 0.2653 0.4292 0.1224  -0.1408 -0.0480 555 LEU D CA  
10305 C C   . LEU D 555 ? 0.4609 0.2559 0.4306 0.1125  -0.1482 -0.0364 555 LEU D C   
10306 O O   . LEU D 555 ? 0.4857 0.2642 0.4444 0.1164  -0.1562 -0.0338 555 LEU D O   
10307 C CB  . LEU D 555 ? 0.4538 0.2758 0.4409 0.1322  -0.1379 -0.0606 555 LEU D CB  
10308 C CG  . LEU D 555 ? 0.4578 0.2646 0.4345 0.1257  -0.1335 -0.0622 555 LEU D CG  
10309 C CD1 . LEU D 555 ? 0.4365 0.2517 0.4169 0.1170  -0.1257 -0.0612 555 LEU D CD1 
10310 C CD2 . LEU D 555 ? 0.4709 0.2784 0.4475 0.1358  -0.1295 -0.0760 555 LEU D CD2 
10311 N N   . ASP D 556 ? 0.4793 0.2686 0.4469 0.0997  -0.1459 -0.0306 556 ASP D N   
10312 C CA  . ASP D 556 ? 0.4959 0.2615 0.4504 0.0882  -0.1519 -0.0215 556 ASP D CA  
10313 C C   . ASP D 556 ? 0.4925 0.2523 0.4456 0.0807  -0.1494 -0.0240 556 ASP D C   
10314 O O   . ASP D 556 ? 0.4739 0.2439 0.4356 0.0738  -0.1458 -0.0230 556 ASP D O   
10315 C CB  . ASP D 556 ? 0.4902 0.2571 0.4459 0.0786  -0.1540 -0.0116 556 ASP D CB  
10316 C CG  . ASP D 556 ? 0.5174 0.2555 0.4559 0.0675  -0.1611 -0.0024 556 ASP D CG  
10317 O OD1 . ASP D 556 ? 0.5361 0.2556 0.4644 0.0654  -0.1636 -0.0042 556 ASP D OD1 
10318 O OD2 . ASP D 556 ? 0.5202 0.2599 0.4546 0.0577  -0.1607 0.0054  556 ASP D OD2 
10319 N N   . LEU D 557 ? 0.4820 0.2251 0.4241 0.0827  -0.1523 -0.0275 557 LEU D N   
10320 C CA  . LEU D 557 ? 0.4846 0.2198 0.4222 0.0762  -0.1522 -0.0301 557 LEU D CA  
10321 C C   . LEU D 557 ? 0.5079 0.2194 0.4339 0.0665  -0.1596 -0.0252 557 LEU D C   
10322 O O   . LEU D 557 ? 0.5175 0.2192 0.4375 0.0628  -0.1618 -0.0285 557 LEU D O   
10323 C CB  . LEU D 557 ? 0.4905 0.2260 0.4239 0.0859  -0.1486 -0.0401 557 LEU D CB  
10324 C CG  . LEU D 557 ? 0.4729 0.2286 0.4157 0.0943  -0.1400 -0.0472 557 LEU D CG  
10325 C CD1 . LEU D 557 ? 0.4859 0.2371 0.4215 0.1024  -0.1361 -0.0581 557 LEU D CD1 
10326 C CD2 . LEU D 557 ? 0.4518 0.2188 0.4009 0.0868  -0.1357 -0.0449 557 LEU D CD2 
10327 N N   . SER D 558 ? 0.5605 0.2608 0.4813 0.0616  -0.1638 -0.0175 558 SER D N   
10328 C CA  . SER D 558 ? 0.5900 0.2632 0.4959 0.0521  -0.1700 -0.0130 558 SER D CA  
10329 C C   . SER D 558 ? 0.5853 0.2568 0.4964 0.0347  -0.1709 -0.0101 558 SER D C   
10330 O O   . SER D 558 ? 0.5596 0.2504 0.4863 0.0314  -0.1677 -0.0113 558 SER D O   
10331 C CB  . SER D 558 ? 0.6121 0.2699 0.5054 0.0532  -0.1741 -0.0057 558 SER D CB  
10332 O OG  . SER D 558 ? 0.5988 0.2659 0.4978 0.0469  -0.1724 0.0011  558 SER D OG  
10333 N N   . SER D 559 ? 0.6283 0.2764 0.5270 0.0229  -0.1752 -0.0075 559 SER D N   
10334 C CA  . SER D 559 ? 0.6270 0.2742 0.5324 0.0042  -0.1760 -0.0076 559 SER D CA  
10335 C C   . SER D 559 ? 0.6033 0.2705 0.5246 0.0066  -0.1761 -0.0159 559 SER D C   
10336 O O   . SER D 559 ? 0.5819 0.2681 0.5209 0.0009  -0.1747 -0.0177 559 SER D O   
10337 C CB  . SER D 559 ? 0.6225 0.2743 0.5340 -0.0101 -0.1732 -0.0014 559 SER D CB  
10338 O OG  . SER D 559 ? 0.6559 0.2817 0.5461 -0.0193 -0.1741 0.0067  559 SER D OG  
10339 N N   . ASN D 560 ? 0.6028 0.2639 0.5161 0.0155  -0.1782 -0.0214 560 ASN D N   
10340 C CA  . ASN D 560 ? 0.5868 0.2615 0.5071 0.0202  -0.1791 -0.0285 560 ASN D CA  
10341 C C   . ASN D 560 ? 0.6120 0.2698 0.5193 0.0197  -0.1840 -0.0334 560 ASN D C   
10342 O O   . ASN D 560 ? 0.6357 0.2733 0.5325 0.0128  -0.1865 -0.0314 560 ASN D O   
10343 C CB  . ASN D 560 ? 0.5666 0.2567 0.4890 0.0354  -0.1730 -0.0306 560 ASN D CB  
10344 C CG  . ASN D 560 ? 0.5407 0.2526 0.4796 0.0344  -0.1698 -0.0299 560 ASN D CG  
10345 O OD1 . ASN D 560 ? 0.5368 0.2560 0.4830 0.0304  -0.1732 -0.0334 560 ASN D OD1 
10346 N ND2 . ASN D 560 ? 0.5291 0.2511 0.4738 0.0387  -0.1642 -0.0261 560 ASN D ND2 
10347 N N   . ARG D 561 ? 0.5952 0.2589 0.5008 0.0264  -0.1853 -0.0396 561 ARG D N   
10348 C CA  . ARG D 561 ? 0.6185 0.2669 0.5113 0.0256  -0.1905 -0.0450 561 ARG D CA  
10349 C C   . ARG D 561 ? 0.6243 0.2689 0.5040 0.0395  -0.1869 -0.0500 561 ARG D C   
10350 O O   . ARG D 561 ? 0.6386 0.2751 0.5077 0.0405  -0.1906 -0.0556 561 ARG D O   
10351 C CB  . ARG D 561 ? 0.6157 0.2717 0.5165 0.0174  -0.1979 -0.0492 561 ARG D CB  
10352 C CG  . ARG D 561 ? 0.6093 0.2746 0.5280 0.0019  -0.2003 -0.0475 561 ARG D CG  
10353 C CD  . ARG D 561 ? 0.6149 0.2872 0.5419 -0.0064 -0.2090 -0.0545 561 ARG D CD  
10354 N NE  . ARG D 561 ? 0.6074 0.2936 0.5382 0.0029  -0.2135 -0.0580 561 ARG D NE  
10355 C CZ  . ARG D 561 ? 0.6019 0.3014 0.5445 -0.0009 -0.2224 -0.0639 561 ARG D CZ  
10356 N NH1 . ARG D 561 ? 0.6142 0.3202 0.5696 -0.0146 -0.2265 -0.0684 561 ARG D NH1 
10357 N NH2 . ARG D 561 ? 0.5916 0.2983 0.5323 0.0094  -0.2271 -0.0657 561 ARG D NH2 
10358 N N   . PHE D 562 ? 0.6127 0.2637 0.4932 0.0496  -0.1796 -0.0490 562 PHE D N   
10359 C CA  . PHE D 562 ? 0.6214 0.2690 0.4915 0.0616  -0.1747 -0.0557 562 PHE D CA  
10360 C C   . PHE D 562 ? 0.6529 0.2776 0.5094 0.0627  -0.1787 -0.0594 562 PHE D C   
10361 O O   . PHE D 562 ? 0.6673 0.2791 0.5223 0.0593  -0.1820 -0.0554 562 PHE D O   
10362 C CB  . PHE D 562 ? 0.6085 0.2679 0.4859 0.0717  -0.1672 -0.0554 562 PHE D CB  
10363 C CG  . PHE D 562 ? 0.5795 0.2606 0.4692 0.0713  -0.1619 -0.0528 562 PHE D CG  
10364 C CD1 . PHE D 562 ? 0.5719 0.2601 0.4580 0.0732  -0.1577 -0.0572 562 PHE D CD1 
10365 C CD2 . PHE D 562 ? 0.5638 0.2551 0.4659 0.0687  -0.1612 -0.0460 562 PHE D CD2 
10366 C CE1 . PHE D 562 ? 0.5488 0.2539 0.4446 0.0727  -0.1528 -0.0549 562 PHE D CE1 
10367 C CE2 . PHE D 562 ? 0.5385 0.2491 0.4523 0.0684  -0.1562 -0.0442 562 PHE D CE2 
10368 C CZ  . PHE D 562 ? 0.5307 0.2483 0.4419 0.0705  -0.1519 -0.0487 562 PHE D CZ  
10369 N N   . SER D 563 ? 0.6723 0.2898 0.5167 0.0670  -0.1780 -0.0672 563 SER D N   
10370 C CA  . SER D 563 ? 0.7032 0.2984 0.5343 0.0647  -0.1833 -0.0712 563 SER D CA  
10371 C C   . SER D 563 ? 0.7254 0.3103 0.5459 0.0763  -0.1788 -0.0801 563 SER D C   
10372 O O   . SER D 563 ? 0.7552 0.3201 0.5668 0.0761  -0.1827 -0.0828 563 SER D O   
10373 C CB  . SER D 563 ? 0.7093 0.3011 0.5340 0.0558  -0.1900 -0.0733 563 SER D CB  
10374 O OG  . SER D 563 ? 0.7141 0.3097 0.5288 0.0614  -0.1866 -0.0791 563 SER D OG  
10375 N N   . PHE D 564 ? 0.7037 0.3005 0.5251 0.0856  -0.1703 -0.0859 564 PHE D N   
10376 C CA  . PHE D 564 ? 0.7249 0.3135 0.5380 0.0958  -0.1649 -0.0970 564 PHE D CA  
10377 C C   . PHE D 564 ? 0.7213 0.3179 0.5469 0.1080  -0.1606 -0.0992 564 PHE D C   
10378 O O   . PHE D 564 ? 0.7086 0.3143 0.5461 0.1079  -0.1626 -0.0912 564 PHE D O   
10379 C CB  . PHE D 564 ? 0.7256 0.3187 0.5278 0.0966  -0.1576 -0.1048 564 PHE D CB  
10380 C CG  . PHE D 564 ? 0.7442 0.3225 0.5285 0.0881  -0.1638 -0.1061 564 PHE D CG  
10381 C CD1 . PHE D 564 ? 0.7755 0.3348 0.5464 0.0895  -0.1653 -0.1141 564 PHE D CD1 
10382 C CD2 . PHE D 564 ? 0.7325 0.3155 0.5137 0.0794  -0.1693 -0.1000 564 PHE D CD2 
10383 C CE1 . PHE D 564 ? 0.7942 0.3402 0.5483 0.0816  -0.1720 -0.1157 564 PHE D CE1 
10384 C CE2 . PHE D 564 ? 0.7516 0.3218 0.5169 0.0727  -0.1771 -0.1017 564 PHE D CE2 
10385 C CZ  . PHE D 564 ? 0.7823 0.3342 0.5337 0.0734  -0.1784 -0.1095 564 PHE D CZ  
10386 N N   . GLU D 565 ? 0.7573 0.3507 0.5802 0.1188  -0.1549 -0.1112 565 GLU D N   
10387 C CA  . GLU D 565 ? 0.7613 0.3605 0.5966 0.1324  -0.1535 -0.1155 565 GLU D CA  
10388 C C   . GLU D 565 ? 0.7320 0.3583 0.5840 0.1372  -0.1467 -0.1154 565 GLU D C   
10389 O O   . GLU D 565 ? 0.7149 0.3544 0.5667 0.1329  -0.1386 -0.1176 565 GLU D O   
10390 C CB  . GLU D 565 ? 0.7882 0.3804 0.6193 0.1429  -0.1483 -0.1310 565 GLU D CB  
10391 C CG  . GLU D 565 ? 0.7937 0.3864 0.6121 0.1383  -0.1388 -0.1408 565 GLU D CG  
10392 C CD  . GLU D 565 ? 0.8190 0.3870 0.6176 0.1301  -0.1448 -0.1408 565 GLU D CD  
10393 O OE1 . GLU D 565 ? 0.8205 0.3759 0.6157 0.1221  -0.1556 -0.1297 565 GLU D OE1 
10394 O OE2 . GLU D 565 ? 0.8413 0.4030 0.6275 0.1307  -0.1380 -0.1528 565 GLU D OE2 
10395 N N   . ILE D 566 ? 0.7035 0.3361 0.5682 0.1458  -0.1505 -0.1130 566 ILE D N   
10396 C CA  . ILE D 566 ? 0.6776 0.3367 0.5599 0.1512  -0.1455 -0.1134 566 ILE D CA  
10397 C C   . ILE D 566 ? 0.6758 0.3530 0.5655 0.1592  -0.1326 -0.1298 566 ILE D C   
10398 O O   . ILE D 566 ? 0.6993 0.3713 0.5879 0.1680  -0.1301 -0.1422 566 ILE D O   
10399 C CB  . ILE D 566 ? 0.6838 0.3434 0.5753 0.1604  -0.1540 -0.1094 566 ILE D CB  
10400 C CG1 . ILE D 566 ? 0.6883 0.3289 0.5695 0.1494  -0.1642 -0.0936 566 ILE D CG1 
10401 C CG2 . ILE D 566 ? 0.6595 0.3487 0.5705 0.1673  -0.1493 -0.1123 566 ILE D CG2 
10402 C CD1 . ILE D 566 ? 0.6854 0.3305 0.5732 0.1535  -0.1705 -0.0861 566 ILE D CD1 
10403 N N   . PRO D 567 ? 0.6751 0.3731 0.5718 0.1559  -0.1230 -0.1318 567 PRO D N   
10404 C CA  . PRO D 567 ? 0.6767 0.3924 0.5788 0.1607  -0.1079 -0.1490 567 PRO D CA  
10405 C C   . PRO D 567 ? 0.6847 0.4174 0.6070 0.1764  -0.1069 -0.1613 567 PRO D C   
10406 O O   . PRO D 567 ? 0.6728 0.4213 0.6124 0.1831  -0.1125 -0.1577 567 PRO D O   
10407 C CB  . PRO D 567 ? 0.6484 0.3824 0.5554 0.1535  -0.1001 -0.1460 567 PRO D CB  
10408 C CG  . PRO D 567 ? 0.6372 0.3566 0.5344 0.1425  -0.1103 -0.1280 567 PRO D CG  
10409 C CD  . PRO D 567 ? 0.6483 0.3532 0.5465 0.1457  -0.1243 -0.1192 567 PRO D CD  
10410 N N   . PRO D 568 ? 0.7077 0.4387 0.6286 0.1828  -0.1002 -0.1768 568 PRO D N   
10411 C CA  . PRO D 568 ? 0.7204 0.4699 0.6631 0.1990  -0.1001 -0.1902 568 PRO D CA  
10412 C C   . PRO D 568 ? 0.6985 0.4870 0.6640 0.2019  -0.0872 -0.2024 568 PRO D C   
10413 O O   . PRO D 568 ? 0.7072 0.5170 0.6951 0.2153  -0.0885 -0.2137 568 PRO D O   
10414 C CB  . PRO D 568 ? 0.7557 0.4917 0.6888 0.2024  -0.0944 -0.2042 568 PRO D CB  
10415 C CG  . PRO D 568 ? 0.7552 0.4694 0.6606 0.1867  -0.0890 -0.1996 568 PRO D CG  
10416 C CD  . PRO D 568 ? 0.7258 0.4425 0.6260 0.1748  -0.0904 -0.1848 568 PRO D CD  
10417 N N   . THR D 569 ? 0.6951 0.4935 0.6553 0.1893  -0.0753 -0.2012 569 THR D N   
10418 C CA  . THR D 569 ? 0.6777 0.5130 0.6575 0.1885  -0.0609 -0.2130 569 THR D CA  
10419 C C   . THR D 569 ? 0.6491 0.5012 0.6451 0.1898  -0.0690 -0.2023 569 THR D C   
10420 O O   . THR D 569 ? 0.6327 0.5161 0.6450 0.1869  -0.0575 -0.2106 569 THR D O   
10421 C CB  . THR D 569 ? 0.6804 0.5147 0.6408 0.1725  -0.0415 -0.2190 569 THR D CB  
10422 O OG1 . THR D 569 ? 0.6664 0.4807 0.6077 0.1613  -0.0475 -0.2016 569 THR D OG1 
10423 C CG2 . THR D 569 ? 0.7101 0.5249 0.6497 0.1696  -0.0335 -0.2291 569 THR D CG2 
10424 N N   . LEU D 570 ? 0.6618 0.4940 0.6526 0.1922  -0.0874 -0.1846 570 LEU D N   
10425 C CA  . LEU D 570 ? 0.6427 0.4872 0.6451 0.1923  -0.0954 -0.1735 570 LEU D CA  
10426 C C   . LEU D 570 ? 0.6450 0.5105 0.6706 0.2077  -0.1040 -0.1804 570 LEU D C   
10427 O O   . LEU D 570 ? 0.6559 0.5049 0.6776 0.2146  -0.1207 -0.1704 570 LEU D O   
10428 C CB  . LEU D 570 ? 0.6398 0.4537 0.6236 0.1850  -0.1090 -0.1520 570 LEU D CB  
10429 C CG  . LEU D 570 ? 0.6165 0.4243 0.5887 0.1700  -0.1044 -0.1412 570 LEU D CG  
10430 C CD1 . LEU D 570 ? 0.5900 0.4215 0.5784 0.1691  -0.1036 -0.1374 570 LEU D CD1 
10431 C CD2 . LEU D 570 ? 0.6305 0.4373 0.5907 0.1621  -0.0890 -0.1513 570 LEU D CD2 
10432 N N   . ASN D 571 ? 0.6014 0.5038 0.6500 0.2118  -0.0921 -0.1984 571 ASN D N   
10433 C CA  . ASN D 571 ? 0.6080 0.5350 0.6811 0.2266  -0.1006 -0.2078 571 ASN D CA  
10434 C C   . ASN D 571 ? 0.5847 0.5565 0.6842 0.2245  -0.0910 -0.2184 571 ASN D C   
10435 O O   . ASN D 571 ? 0.5918 0.5927 0.7155 0.2351  -0.0930 -0.2330 571 ASN D O   
10436 C CB  . ASN D 571 ? 0.6366 0.5651 0.7160 0.2375  -0.0986 -0.2244 571 ASN D CB  
10437 C CG  . ASN D 571 ? 0.6373 0.5812 0.7181 0.2286  -0.0751 -0.2410 571 ASN D CG  
10438 O OD1 . ASN D 571 ? 0.6185 0.5923 0.7111 0.2193  -0.0594 -0.2490 571 ASN D OD1 
10439 N ND2 . ASN D 571 ? 0.6624 0.5842 0.7284 0.2299  -0.0717 -0.2462 571 ASN D ND2 
10440 N N   . ASN D 572 ? 0.5920 0.5707 0.6879 0.2108  -0.0809 -0.2124 572 ASN D N   
10441 C CA  . ASN D 572 ? 0.5689 0.5902 0.6881 0.2051  -0.0683 -0.2238 572 ASN D CA  
10442 C C   . ASN D 572 ? 0.5437 0.5662 0.6614 0.1983  -0.0728 -0.2095 572 ASN D C   
10443 O O   . ASN D 572 ? 0.5251 0.5633 0.6449 0.1851  -0.0576 -0.2122 572 ASN D O   
10444 C CB  . ASN D 572 ? 0.5731 0.6077 0.6899 0.1913  -0.0429 -0.2378 572 ASN D CB  
10445 C CG  . ASN D 572 ? 0.5567 0.6391 0.7009 0.1851  -0.0287 -0.2539 572 ASN D CG  
10446 O OD1 . ASN D 572 ? 0.5579 0.6686 0.7287 0.1959  -0.0374 -0.2629 572 ASN D OD1 
10447 N ND2 . ASN D 572 ? 0.5512 0.6409 0.6868 0.1662  -0.0073 -0.2574 572 ASN D ND2 
10448 N N   . LEU D 573 ? 0.5224 0.5257 0.6333 0.2056  -0.0929 -0.1938 573 LEU D N   
10449 C CA  . LEU D 573 ? 0.5010 0.5058 0.6105 0.1992  -0.0973 -0.1804 573 LEU D CA  
10450 C C   . LEU D 573 ? 0.5007 0.5289 0.6283 0.2085  -0.1095 -0.1826 573 LEU D C   
10451 O O   . LEU D 573 ? 0.5144 0.5208 0.6303 0.2151  -0.1273 -0.1698 573 LEU D O   
10452 C CB  . LEU D 573 ? 0.5057 0.4675 0.5880 0.1949  -0.1085 -0.1586 573 LEU D CB  
10453 C CG  . LEU D 573 ? 0.5134 0.4465 0.5744 0.1871  -0.1014 -0.1556 573 LEU D CG  
10454 C CD1 . LEU D 573 ? 0.5192 0.4146 0.5569 0.1813  -0.1137 -0.1347 573 LEU D CD1 
10455 C CD2 . LEU D 573 ? 0.4966 0.4422 0.5574 0.1749  -0.0822 -0.1628 573 LEU D CD2 
10456 N N   . PRO D 574 ? 0.5085 0.5797 0.6620 0.2074  -0.0998 -0.1989 574 PRO D N   
10457 C CA  . PRO D 574 ? 0.5141 0.6089 0.6851 0.2175  -0.1126 -0.2044 574 PRO D CA  
10458 C C   . PRO D 574 ? 0.5040 0.5928 0.6676 0.2152  -0.1238 -0.1887 574 PRO D C   
10459 O O   . PRO D 574 ? 0.5124 0.6162 0.6856 0.2232  -0.1355 -0.1922 574 PRO D O   
10460 C CB  . PRO D 574 ? 0.5019 0.6453 0.7017 0.2114  -0.0956 -0.2264 574 PRO D CB  
10461 C CG  . PRO D 574 ? 0.5004 0.6402 0.6946 0.2007  -0.0747 -0.2333 574 PRO D CG  
10462 C CD  . PRO D 574 ? 0.4961 0.5948 0.6614 0.1948  -0.0761 -0.2137 574 PRO D CD  
10463 N N   . ARG D 575 ? 0.5251 0.5931 0.6719 0.2043  -0.1206 -0.1725 575 ARG D N   
10464 C CA  . ARG D 575 ? 0.5170 0.5788 0.6559 0.2007  -0.1301 -0.1572 575 ARG D CA  
10465 C C   . ARG D 575 ? 0.5308 0.5465 0.6400 0.1983  -0.1410 -0.1356 575 ARG D C   
10466 O O   . ARG D 575 ? 0.5269 0.5338 0.6261 0.1935  -0.1483 -0.1217 575 ARG D O   
10467 C CB  . ARG D 575 ? 0.4853 0.5719 0.6353 0.1870  -0.1153 -0.1587 575 ARG D CB  
10468 C CG  . ARG D 575 ? 0.4738 0.6075 0.6519 0.1843  -0.1028 -0.1795 575 ARG D CG  
10469 C CD  . ARG D 575 ? 0.4557 0.6079 0.6405 0.1678  -0.0845 -0.1814 575 ARG D CD  
10470 N NE  . ARG D 575 ? 0.4525 0.6452 0.6598 0.1599  -0.0681 -0.2018 575 ARG D NE  
10471 C CZ  . ARG D 575 ? 0.4540 0.6544 0.6655 0.1553  -0.0527 -0.2157 575 ARG D CZ  
10472 N NH1 . ARG D 575 ? 0.4611 0.6321 0.6561 0.1590  -0.0514 -0.2125 575 ARG D NH1 
10473 N NH2 . ARG D 575 ? 0.4512 0.6882 0.6819 0.1448  -0.0378 -0.2331 575 ARG D NH2 
10474 N N   . LEU D 576 ? 0.5041 0.4910 0.5987 0.1996  -0.1415 -0.1329 576 LEU D N   
10475 C CA  . LEU D 576 ? 0.5166 0.4613 0.5836 0.1935  -0.1494 -0.1137 576 LEU D CA  
10476 C C   . LEU D 576 ? 0.5463 0.4696 0.5987 0.2006  -0.1667 -0.1050 576 LEU D C   
10477 O O   . LEU D 576 ? 0.5712 0.4909 0.6250 0.2133  -0.1745 -0.1133 576 LEU D O   
10478 C CB  . LEU D 576 ? 0.5269 0.4488 0.5826 0.1919  -0.1445 -0.1152 576 LEU D CB  
10479 C CG  . LEU D 576 ? 0.5362 0.4189 0.5659 0.1815  -0.1497 -0.0970 576 LEU D CG  
10480 C CD1 . LEU D 576 ? 0.5104 0.3948 0.5387 0.1676  -0.1400 -0.0904 576 LEU D CD1 
10481 C CD2 . LEU D 576 ? 0.5598 0.4174 0.5766 0.1843  -0.1515 -0.0994 576 LEU D CD2 
10482 N N   . TYR D 577 ? 0.5441 0.4521 0.5814 0.1923  -0.1726 -0.0887 577 TYR D N   
10483 C CA  . TYR D 577 ? 0.5773 0.4578 0.5940 0.1962  -0.1878 -0.0784 577 TYR D CA  
10484 C C   . TYR D 577 ? 0.5918 0.4318 0.5808 0.1838  -0.1905 -0.0611 577 TYR D C   
10485 O O   . TYR D 577 ? 0.6244 0.4367 0.5921 0.1845  -0.2020 -0.0515 577 TYR D O   
10486 C CB  . TYR D 577 ? 0.5744 0.4719 0.5947 0.1972  -0.1937 -0.0755 577 TYR D CB  
10487 C CG  . TYR D 577 ? 0.5494 0.4523 0.5668 0.1822  -0.1875 -0.0641 577 TYR D CG  
10488 C CD1 . TYR D 577 ? 0.5651 0.4374 0.5567 0.1720  -0.1936 -0.0464 577 TYR D CD1 
10489 C CD2 . TYR D 577 ? 0.5126 0.4516 0.5531 0.1777  -0.1755 -0.0720 577 TYR D CD2 
10490 C CE1 . TYR D 577 ? 0.5438 0.4227 0.5338 0.1585  -0.1884 -0.0372 577 TYR D CE1 
10491 C CE2 . TYR D 577 ? 0.4913 0.4360 0.5302 0.1648  -0.1708 -0.0626 577 TYR D CE2 
10492 C CZ  . TYR D 577 ? 0.5066 0.4220 0.5209 0.1557  -0.1776 -0.0453 577 TYR D CZ  
10493 O OH  . TYR D 577 ? 0.4867 0.4095 0.5004 0.1429  -0.1735 -0.0372 577 TYR D OH  
10494 N N   . TYR D 578 ? 0.5493 0.3847 0.5374 0.1722  -0.1804 -0.0578 578 TYR D N   
10495 C CA  . TYR D 578 ? 0.5615 0.3631 0.5270 0.1588  -0.1820 -0.0436 578 TYR D CA  
10496 C C   . TYR D 578 ? 0.5558 0.3495 0.5214 0.1546  -0.1745 -0.0476 578 TYR D C   
10497 O O   . TYR D 578 ? 0.5329 0.3486 0.5145 0.1552  -0.1644 -0.0566 578 TYR D O   
10498 C CB  . TYR D 578 ? 0.5427 0.3483 0.5056 0.1448  -0.1788 -0.0320 578 TYR D CB  
10499 C CG  . TYR D 578 ? 0.5569 0.3305 0.4984 0.1296  -0.1805 -0.0185 578 TYR D CG  
10500 C CD1 . TYR D 578 ? 0.5430 0.3120 0.4864 0.1194  -0.1730 -0.0179 578 TYR D CD1 
10501 C CD2 . TYR D 578 ? 0.5871 0.3346 0.5058 0.1246  -0.1897 -0.0069 578 TYR D CD2 
10502 C CE1 . TYR D 578 ? 0.5564 0.2995 0.4834 0.1047  -0.1748 -0.0075 578 TYR D CE1 
10503 C CE2 . TYR D 578 ? 0.6025 0.3213 0.5019 0.1088  -0.1903 0.0042  578 TYR D CE2 
10504 C CZ  . TYR D 578 ? 0.5859 0.3043 0.4916 0.0989  -0.1828 0.0033  578 TYR D CZ  
10505 O OH  . TYR D 578 ? 0.6091 0.3015 0.4986 0.0823  -0.1836 0.0127  578 TYR D OH  
10506 N N   . MET D 579 ? 0.5740 0.3349 0.5198 0.1495  -0.1795 -0.0412 579 MET D N   
10507 C CA  . MET D 579 ? 0.5721 0.3228 0.5148 0.1439  -0.1739 -0.0439 579 MET D CA  
10508 C C   . MET D 579 ? 0.5962 0.3125 0.5165 0.1319  -0.1794 -0.0325 579 MET D C   
10509 O O   . MET D 579 ? 0.6303 0.3224 0.5355 0.1365  -0.1882 -0.0307 579 MET D O   
10510 C CB  . MET D 579 ? 0.5837 0.3381 0.5326 0.1579  -0.1736 -0.0579 579 MET D CB  
10511 C CG  . MET D 579 ? 0.5991 0.3334 0.5373 0.1533  -0.1716 -0.0595 579 MET D CG  
10512 S SD  . MET D 579 ? 0.5948 0.3442 0.5454 0.1658  -0.1642 -0.0781 579 MET D SD  
10513 C CE  . MET D 579 ? 0.5555 0.3420 0.5269 0.1644  -0.1515 -0.0846 579 MET D CE  
10514 N N   . ASN D 580 ? 0.5815 0.2957 0.5003 0.1165  -0.1745 -0.0257 580 ASN D N   
10515 C CA  . ASN D 580 ? 0.6018 0.2872 0.5029 0.1026  -0.1782 -0.0170 580 ASN D CA  
10516 C C   . ASN D 580 ? 0.5944 0.2789 0.4981 0.0979  -0.1735 -0.0224 580 ASN D C   
10517 O O   . ASN D 580 ? 0.5668 0.2690 0.4823 0.0927  -0.1667 -0.0242 580 ASN D O   
10518 C CB  . ASN D 580 ? 0.5933 0.2777 0.4918 0.0880  -0.1776 -0.0059 580 ASN D CB  
10519 C CG  . ASN D 580 ? 0.6281 0.2782 0.5032 0.0752  -0.1839 0.0043  580 ASN D CG  
10520 O OD1 . ASN D 580 ? 0.6563 0.2829 0.5177 0.0755  -0.1881 0.0031  580 ASN D OD1 
10521 N ND2 . ASN D 580 ? 0.6287 0.2747 0.4979 0.0627  -0.1840 0.0141  580 ASN D ND2 
10522 N N   . LEU D 581 ? 0.5978 0.2602 0.4890 0.1001  -0.1778 -0.0252 581 LEU D N   
10523 C CA  . LEU D 581 ? 0.5973 0.2550 0.4871 0.0956  -0.1751 -0.0302 581 LEU D CA  
10524 C C   . LEU D 581 ? 0.6241 0.2528 0.4974 0.0828  -0.1806 -0.0242 581 LEU D C   
10525 O O   . LEU D 581 ? 0.6343 0.2531 0.5025 0.0807  -0.1811 -0.0289 581 LEU D O   
10526 C CB  . LEU D 581 ? 0.6059 0.2659 0.4975 0.1102  -0.1740 -0.0420 581 LEU D CB  
10527 C CG  . LEU D 581 ? 0.5861 0.2733 0.4940 0.1235  -0.1678 -0.0515 581 LEU D CG  
10528 C CD1 . LEU D 581 ? 0.5954 0.2820 0.5031 0.1322  -0.1644 -0.0638 581 LEU D CD1 
10529 C CD2 . LEU D 581 ? 0.5513 0.2623 0.4719 0.1172  -0.1601 -0.0498 581 LEU D CD2 
10530 N N   . SER D 582 ? 0.6683 0.2824 0.5319 0.0731  -0.1844 -0.0142 582 SER D N   
10531 C CA  . SER D 582 ? 0.7014 0.2843 0.5465 0.0604  -0.1893 -0.0088 582 SER D CA  
10532 C C   . SER D 582 ? 0.6888 0.2753 0.5398 0.0434  -0.1864 -0.0082 582 SER D C   
10533 O O   . SER D 582 ? 0.6556 0.2669 0.5238 0.0412  -0.1817 -0.0102 582 SER D O   
10534 C CB  . SER D 582 ? 0.7268 0.2897 0.5554 0.0546  -0.1937 0.0017  582 SER D CB  
10535 O OG  . SER D 582 ? 0.7036 0.2825 0.5407 0.0459  -0.1899 0.0078  582 SER D OG  
10536 N N   . ARG D 583 ? 0.7424 0.3032 0.5793 0.0313  -0.1896 -0.0063 583 ARG D N   
10537 C CA  . ARG D 583 ? 0.7368 0.2996 0.5798 0.0131  -0.1881 -0.0068 583 ARG D CA  
10538 C C   . ARG D 583 ? 0.7101 0.2947 0.5686 0.0187  -0.1866 -0.0160 583 ARG D C   
10539 O O   . ARG D 583 ? 0.6817 0.2884 0.5568 0.0137  -0.1842 -0.0173 583 ARG D O   
10540 C CB  . ARG D 583 ? 0.7248 0.2959 0.5745 -0.0023 -0.1848 0.0001  583 ARG D CB  
10541 C CG  . ARG D 583 ? 0.7573 0.3031 0.5856 -0.0094 -0.1861 0.0100  583 ARG D CG  
10542 C CD  . ARG D 583 ? 0.7432 0.3002 0.5768 -0.0203 -0.1819 0.0168  583 ARG D CD  
10543 N NE  . ARG D 583 ? 0.7621 0.3052 0.5777 -0.0123 -0.1847 0.0247  583 ARG D NE  
10544 C CZ  . ARG D 583 ? 0.8071 0.3168 0.5943 -0.0182 -0.1882 0.0316  583 ARG D CZ  
10545 N NH1 . ARG D 583 ? 0.8382 0.3244 0.6116 -0.0339 -0.1876 0.0321  583 ARG D NH1 
10546 N NH2 . ARG D 583 ? 0.8237 0.3232 0.5954 -0.0083 -0.1926 0.0377  583 ARG D NH2 
10547 N N   . ASN D 584 ? 0.7113 0.2874 0.5623 0.0293  -0.1885 -0.0225 584 ASN D N   
10548 C CA  . ASN D 584 ? 0.6945 0.2858 0.5531 0.0361  -0.1872 -0.0312 584 ASN D CA  
10549 C C   . ASN D 584 ? 0.7247 0.2942 0.5693 0.0370  -0.1910 -0.0367 584 ASN D C   
10550 O O   . ASN D 584 ? 0.7557 0.3002 0.5874 0.0296  -0.1945 -0.0337 584 ASN D O   
10551 C CB  . ASN D 584 ? 0.6727 0.2839 0.5390 0.0525  -0.1821 -0.0348 584 ASN D CB  
10552 C CG  . ASN D 584 ? 0.6378 0.2751 0.5205 0.0505  -0.1776 -0.0325 584 ASN D CG  
10553 O OD1 . ASN D 584 ? 0.6209 0.2718 0.5102 0.0499  -0.1759 -0.0367 584 ASN D OD1 
10554 N ND2 . ASN D 584 ? 0.6303 0.2725 0.5174 0.0496  -0.1763 -0.0259 584 ASN D ND2 
10555 N N   . ASP D 585 ? 0.7483 0.3250 0.5931 0.0453  -0.1899 -0.0450 585 ASP D N   
10556 C CA  . ASP D 585 ? 0.7767 0.3337 0.6083 0.0460  -0.1933 -0.0514 585 ASP D CA  
10557 C C   . ASP D 585 ? 0.7828 0.3397 0.6096 0.0628  -0.1900 -0.0593 585 ASP D C   
10558 O O   . ASP D 585 ? 0.7996 0.3474 0.6175 0.0649  -0.1908 -0.0669 585 ASP D O   
10559 C CB  . ASP D 585 ? 0.7732 0.3346 0.6064 0.0360  -0.1965 -0.0553 585 ASP D CB  
10560 C CG  . ASP D 585 ? 0.8042 0.3540 0.6374 0.0180  -0.2012 -0.0521 585 ASP D CG  
10561 O OD1 . ASP D 585 ? 0.8376 0.3624 0.6579 0.0137  -0.2034 -0.0522 585 ASP D OD1 
10562 O OD2 . ASP D 585 ? 0.7846 0.3508 0.6316 0.0077  -0.2023 -0.0505 585 ASP D OD2 
10563 N N   . LEU D 586 ? 0.7140 0.2810 0.5470 0.0747  -0.1861 -0.0588 586 LEU D N   
10564 C CA  . LEU D 586 ? 0.7203 0.2900 0.5524 0.0903  -0.1822 -0.0684 586 LEU D CA  
10565 C C   . LEU D 586 ? 0.7591 0.3017 0.5783 0.0956  -0.1869 -0.0723 586 LEU D C   
10566 O O   . LEU D 586 ? 0.7795 0.3035 0.5919 0.0926  -0.1925 -0.0658 586 LEU D O   
10567 C CB  . LEU D 586 ? 0.7011 0.2906 0.5460 0.1017  -0.1776 -0.0686 586 LEU D CB  
10568 C CG  . LEU D 586 ? 0.6651 0.2796 0.5235 0.0974  -0.1731 -0.0633 586 LEU D CG  
10569 C CD1 . LEU D 586 ? 0.6628 0.2741 0.5233 0.0904  -0.1773 -0.0523 586 LEU D CD1 
10570 C CD2 . LEU D 586 ? 0.6481 0.2844 0.5179 0.1101  -0.1655 -0.0704 586 LEU D CD2 
10571 N N   . ASP D 587 ? 0.8123 0.3507 0.6264 0.1032  -0.1843 -0.0832 587 ASP D N   
10572 C CA  . ASP D 587 ? 0.8510 0.3631 0.6527 0.1081  -0.1883 -0.0889 587 ASP D CA  
10573 C C   . ASP D 587 ? 0.8594 0.3771 0.6665 0.1267  -0.1842 -0.1001 587 ASP D C   
10574 O O   . ASP D 587 ? 0.8356 0.3777 0.6565 0.1349  -0.1782 -0.1032 587 ASP D O   
10575 C CB  . ASP D 587 ? 0.8679 0.3669 0.6575 0.0985  -0.1896 -0.0934 587 ASP D CB  
10576 C CG  . ASP D 587 ? 0.8574 0.3723 0.6476 0.1016  -0.1825 -0.1025 587 ASP D CG  
10577 O OD1 . ASP D 587 ? 0.8310 0.3687 0.6320 0.1080  -0.1757 -0.1039 587 ASP D OD1 
10578 O OD2 . ASP D 587 ? 0.8844 0.3876 0.6624 0.0967  -0.1835 -0.1085 587 ASP D OD2 
10579 N N   . GLN D 588 ? 0.8645 0.3592 0.6618 0.1331  -0.1874 -0.1072 588 GLN D N   
10580 C CA  . GLN D 588 ? 0.8801 0.3772 0.6830 0.1512  -0.1843 -0.1202 588 GLN D CA  
10581 C C   . GLN D 588 ? 0.8775 0.3835 0.6924 0.1640  -0.1879 -0.1178 588 GLN D C   
10582 O O   . GLN D 588 ? 0.8723 0.3743 0.6854 0.1583  -0.1939 -0.1052 588 GLN D O   
10583 C CB  . GLN D 588 ? 0.8625 0.3819 0.6720 0.1544  -0.1725 -0.1322 588 GLN D CB  
10584 C CG  . GLN D 588 ? 0.8677 0.3778 0.6623 0.1418  -0.1703 -0.1344 588 GLN D CG  
10585 C CD  . GLN D 588 ? 0.8736 0.3919 0.6660 0.1472  -0.1593 -0.1502 588 GLN D CD  
10586 O OE1 . GLN D 588 ? 0.8731 0.4060 0.6776 0.1603  -0.1519 -0.1609 588 GLN D OE1 
10587 N NE2 . GLN D 588 ? 0.8818 0.3912 0.6584 0.1367  -0.1579 -0.1528 588 GLN D NE2 
10588 N N   . THR D 589 ? 0.8140 0.3324 0.6407 0.1812  -0.1843 -0.1309 589 THR D N   
10589 C CA  . THR D 589 ? 0.8222 0.3454 0.6592 0.1962  -0.1906 -0.1314 589 THR D CA  
10590 C C   . THR D 589 ? 0.7835 0.3411 0.6391 0.1981  -0.1859 -0.1293 589 THR D C   
10591 O O   . THR D 589 ? 0.7543 0.3356 0.6188 0.1937  -0.1748 -0.1339 589 THR D O   
10592 C CB  . THR D 589 ? 0.8501 0.3724 0.6943 0.2149  -0.1900 -0.1486 589 THR D CB  
10593 O OG1 . THR D 589 ? 0.8517 0.3884 0.7112 0.2309  -0.1956 -0.1514 589 THR D OG1 
10594 C CG2 . THR D 589 ? 0.8356 0.3799 0.6891 0.2159  -0.1751 -0.1638 589 THR D CG2 
10595 N N   . ILE D 590 ? 0.7849 0.3426 0.6440 0.2043  -0.1947 -0.1224 590 ILE D N   
10596 C CA  . ILE D 590 ? 0.7523 0.3425 0.6299 0.2080  -0.1914 -0.1218 590 ILE D CA  
10597 C C   . ILE D 590 ? 0.7456 0.3649 0.6448 0.2231  -0.1832 -0.1404 590 ILE D C   
10598 O O   . ILE D 590 ? 0.7748 0.3888 0.6783 0.2385  -0.1877 -0.1517 590 ILE D O   
10599 C CB  . ILE D 590 ? 0.7657 0.3467 0.6397 0.2127  -0.2039 -0.1120 590 ILE D CB  
10600 C CG1 . ILE D 590 ? 0.7707 0.3258 0.6239 0.1948  -0.2088 -0.0943 590 ILE D CG1 
10601 C CG2 . ILE D 590 ? 0.7360 0.3520 0.6308 0.2190  -0.2013 -0.1142 590 ILE D CG2 
10602 C CD1 . ILE D 590 ? 0.8183 0.3321 0.6489 0.1949  -0.2194 -0.0900 590 ILE D CD1 
10603 N N   . PRO D 591 ? 0.7712 0.4213 0.6846 0.2191  -0.1709 -0.1453 591 PRO D N   
10604 C CA  . PRO D 591 ? 0.7672 0.4459 0.7006 0.2307  -0.1602 -0.1649 591 PRO D CA  
10605 C C   . PRO D 591 ? 0.7716 0.4712 0.7258 0.2476  -0.1668 -0.1722 591 PRO D C   
10606 O O   . PRO D 591 ? 0.7628 0.4656 0.7189 0.2478  -0.1757 -0.1617 591 PRO D O   
10607 C CB  . PRO D 591 ? 0.7309 0.4327 0.6694 0.2189  -0.1458 -0.1652 591 PRO D CB  
10608 C CG  . PRO D 591 ? 0.7106 0.4068 0.6423 0.2076  -0.1526 -0.1461 591 PRO D CG  
10609 C CD  . PRO D 591 ? 0.7366 0.3966 0.6481 0.2034  -0.1656 -0.1339 591 PRO D CD  
10610 N N   . GLU D 592 ? 0.8954 0.6102 0.8651 0.2615  -0.1621 -0.1917 592 GLU D N   
10611 C CA  . GLU D 592 ? 0.8993 0.6385 0.8922 0.2788  -0.1686 -0.2024 592 GLU D CA  
10612 C C   . GLU D 592 ? 0.8549 0.6342 0.8691 0.2760  -0.1612 -0.2047 592 GLU D C   
10613 O O   . GLU D 592 ? 0.8559 0.6529 0.8855 0.2869  -0.1705 -0.2073 592 GLU D O   
10614 C CB  . GLU D 592 ? 0.9180 0.6680 0.9252 0.2927  -0.1629 -0.2249 592 GLU D CB  
10615 C CG  . GLU D 592 ? 0.9235 0.7065 0.9600 0.3109  -0.1678 -0.2407 592 GLU D CG  
10616 C CD  . GLU D 592 ? 0.9694 0.7279 1.0009 0.3283  -0.1884 -0.2404 592 GLU D CD  
10617 O OE1 . GLU D 592 ? 0.9896 0.7048 0.9931 0.3241  -0.1993 -0.2247 592 GLU D OE1 
10618 O OE2 . GLU D 592 ? 0.9859 0.7681 1.0408 0.3456  -0.1937 -0.2567 592 GLU D OE2 
10619 N N   . GLY D 593 ? 0.7715 0.5638 0.7848 0.2614  -0.1453 -0.2038 593 GLY D N   
10620 C CA  . GLY D 593 ? 0.7381 0.5679 0.7710 0.2575  -0.1364 -0.2072 593 GLY D CA  
10621 C C   . GLY D 593 ? 0.7214 0.5491 0.7515 0.2539  -0.1478 -0.1900 593 GLY D C   
10622 O O   . GLY D 593 ? 0.6995 0.5596 0.7489 0.2548  -0.1446 -0.1942 593 GLY D O   
10623 N N   . LEU D 594 ? 0.7456 0.5365 0.7516 0.2485  -0.1601 -0.1716 594 LEU D N   
10624 C CA  . LEU D 594 ? 0.7350 0.5218 0.7358 0.2441  -0.1701 -0.1556 594 LEU D CA  
10625 C C   . LEU D 594 ? 0.7533 0.5519 0.7667 0.2598  -0.1829 -0.1607 594 LEU D C   
10626 O O   . LEU D 594 ? 0.7359 0.5474 0.7544 0.2582  -0.1870 -0.1543 594 LEU D O   
10627 C CB  . LEU D 594 ? 0.7496 0.4946 0.7215 0.2332  -0.1787 -0.1367 594 LEU D CB  
10628 C CG  . LEU D 594 ? 0.7211 0.4630 0.6836 0.2144  -0.1724 -0.1226 594 LEU D CG  
10629 C CD1 . LEU D 594 ? 0.7007 0.4575 0.6687 0.2074  -0.1565 -0.1307 594 LEU D CD1 
10630 C CD2 . LEU D 594 ? 0.7392 0.4430 0.6759 0.2031  -0.1803 -0.1067 594 LEU D CD2 
10631 N N   . THR D 595 ? 0.7906 0.5846 0.8089 0.2754  -0.1899 -0.1728 595 THR D N   
10632 C CA  . THR D 595 ? 0.8082 0.6129 0.8384 0.2923  -0.2038 -0.1797 595 THR D CA  
10633 C C   . THR D 595 ? 0.7829 0.6385 0.8458 0.2973  -0.1964 -0.1952 595 THR D C   
10634 O O   . THR D 595 ? 0.7983 0.6674 0.8728 0.3099  -0.2084 -0.2009 595 THR D O   
10635 C CB  . THR D 595 ? 0.8528 0.6408 0.8818 0.3086  -0.2127 -0.1909 595 THR D CB  
10636 O OG1 . THR D 595 ? 0.8512 0.6724 0.9062 0.3153  -0.1998 -0.2131 595 THR D OG1 
10637 C CG2 . THR D 595 ? 0.8760 0.6175 0.8750 0.3010  -0.2153 -0.1790 595 THR D CG2 
10638 N N   . LYS D 596 ? 0.7224 0.6056 0.7993 0.2873  -0.1770 -0.2031 596 LYS D N   
10639 C CA  . LYS D 596 ? 0.6973 0.6298 0.8045 0.2879  -0.1672 -0.2178 596 LYS D CA  
10640 C C   . LYS D 596 ? 0.6656 0.6088 0.7721 0.2761  -0.1653 -0.2054 596 LYS D C   
10641 O O   . LYS D 596 ? 0.6453 0.6290 0.7758 0.2746  -0.1571 -0.2165 596 LYS D O   
10642 C CB  . LYS D 596 ? 0.6849 0.6408 0.8058 0.2817  -0.1450 -0.2344 596 LYS D CB  
10643 C CG  . LYS D 596 ? 0.7169 0.6654 0.8405 0.2931  -0.1449 -0.2489 596 LYS D CG  
10644 C CD  . LYS D 596 ? 0.7108 0.6643 0.8324 0.2824  -0.1224 -0.2589 596 LYS D CD  
10645 C CE  . LYS D 596 ? 0.7461 0.6792 0.8611 0.2921  -0.1240 -0.2683 596 LYS D CE  
10646 N NZ  . LYS D 596 ? 0.7455 0.6706 0.8472 0.2794  -0.1037 -0.2737 596 LYS D NZ  
10647 N N   . LEU D 597 ? 0.7084 0.6175 0.7885 0.2669  -0.1719 -0.1836 597 LEU D N   
10648 C CA  . LEU D 597 ? 0.6819 0.5981 0.7598 0.2564  -0.1715 -0.1709 597 LEU D CA  
10649 C C   . LEU D 597 ? 0.7002 0.6186 0.7800 0.2668  -0.1884 -0.1685 597 LEU D C   
10650 O O   . LEU D 597 ? 0.7236 0.6073 0.7795 0.2670  -0.2020 -0.1531 597 LEU D O   
10651 C CB  . LEU D 597 ? 0.6763 0.5568 0.7267 0.2416  -0.1711 -0.1502 597 LEU D CB  
10652 C CG  . LEU D 597 ? 0.6701 0.5406 0.7124 0.2309  -0.1573 -0.1504 597 LEU D CG  
10653 C CD1 . LEU D 597 ? 0.6505 0.4996 0.6736 0.2146  -0.1562 -0.1315 597 LEU D CD1 
10654 C CD2 . LEU D 597 ? 0.6443 0.5519 0.7088 0.2294  -0.1393 -0.1680 597 LEU D CD2 
10655 N N   . SER D 598 ? 0.6790 0.6387 0.7864 0.2742  -0.1868 -0.1844 598 SER D N   
10656 C CA  . SER D 598 ? 0.7048 0.6686 0.8156 0.2871  -0.2041 -0.1864 598 SER D CA  
10657 C C   . SER D 598 ? 0.6947 0.6434 0.7877 0.2791  -0.2115 -0.1672 598 SER D C   
10658 O O   . SER D 598 ? 0.7281 0.6516 0.8037 0.2868  -0.2285 -0.1588 598 SER D O   
10659 C CB  . SER D 598 ? 0.6907 0.7063 0.8374 0.2946  -0.1995 -0.2095 598 SER D CB  
10660 O OG  . SER D 598 ? 0.6508 0.6988 0.8125 0.2802  -0.1828 -0.2119 598 SER D OG  
10661 N N   . GLN D 599 ? 0.7021 0.6644 0.7979 0.2638  -0.1986 -0.1605 599 GLN D N   
10662 C CA  . GLN D 599 ? 0.6948 0.6523 0.7796 0.2559  -0.2033 -0.1456 599 GLN D CA  
10663 C C   . GLN D 599 ? 0.7035 0.6157 0.7553 0.2450  -0.2072 -0.1229 599 GLN D C   
10664 O O   . GLN D 599 ? 0.6959 0.6028 0.7372 0.2357  -0.2087 -0.1095 599 GLN D O   
10665 C CB  . GLN D 599 ? 0.6535 0.6494 0.7589 0.2447  -0.1878 -0.1506 599 GLN D CB  
10666 C CG  . GLN D 599 ? 0.6475 0.6917 0.7867 0.2510  -0.1806 -0.1743 599 GLN D CG  
10667 C CD  . GLN D 599 ? 0.6787 0.7341 0.8265 0.2667  -0.1968 -0.1835 599 GLN D CD  
10668 O OE1 . GLN D 599 ? 0.6967 0.7344 0.8283 0.2696  -0.2108 -0.1714 599 GLN D OE1 
10669 N NE2 . GLN D 599 ? 0.6847 0.7693 0.8575 0.2768  -0.1949 -0.2055 599 GLN D NE2 
10670 N N   . LEU D 600 ? 0.6958 0.5766 0.7317 0.2450  -0.2084 -0.1192 600 LEU D N   
10671 C CA  . LEU D 600 ? 0.7085 0.5483 0.7146 0.2325  -0.2108 -0.0996 600 LEU D CA  
10672 C C   . LEU D 600 ? 0.7406 0.5540 0.7244 0.2344  -0.2263 -0.0871 600 LEU D C   
10673 O O   . LEU D 600 ? 0.7727 0.5783 0.7536 0.2493  -0.2397 -0.0927 600 LEU D O   
10674 C CB  . LEU D 600 ? 0.7263 0.5394 0.7208 0.2333  -0.2103 -0.1008 600 LEU D CB  
10675 C CG  . LEU D 600 ? 0.7177 0.5034 0.6926 0.2162  -0.2040 -0.0871 600 LEU D CG  
10676 C CD1 . LEU D 600 ? 0.6750 0.4843 0.6623 0.2038  -0.1894 -0.0861 600 LEU D CD1 
10677 C CD2 . LEU D 600 ? 0.7371 0.5031 0.7050 0.2194  -0.2033 -0.0925 600 LEU D CD2 
10678 N N   . GLN D 601 ? 0.7355 0.5345 0.7027 0.2194  -0.2247 -0.0706 601 GLN D N   
10679 C CA  . GLN D 601 ? 0.7685 0.5374 0.7089 0.2172  -0.2374 -0.0565 601 GLN D CA  
10680 C C   . GLN D 601 ? 0.7921 0.5170 0.7022 0.2038  -0.2385 -0.0415 601 GLN D C   
10681 O O   . GLN D 601 ? 0.8380 0.5274 0.7225 0.2066  -0.2509 -0.0345 601 GLN D O   
10682 C CB  . GLN D 601 ? 0.7474 0.5359 0.6913 0.2099  -0.2354 -0.0500 601 GLN D CB  
10683 C CG  . GLN D 601 ? 0.7888 0.5459 0.7022 0.2062  -0.2479 -0.0350 601 GLN D CG  
10684 C CD  . GLN D 601 ? 0.7722 0.5483 0.6873 0.1971  -0.2450 -0.0280 601 GLN D CD  
10685 O OE1 . GLN D 601 ? 0.7341 0.5515 0.6763 0.2010  -0.2393 -0.0382 601 GLN D OE1 
10686 N NE2 . GLN D 601 ? 0.7861 0.5321 0.6713 0.1839  -0.2485 -0.0113 601 GLN D NE2 
10687 N N   . MET D 602 ? 0.7586 0.4847 0.6708 0.1888  -0.2261 -0.0370 602 MET D N   
10688 C CA  . MET D 602 ? 0.7770 0.4661 0.6644 0.1744  -0.2257 -0.0249 602 MET D CA  
10689 C C   . MET D 602 ? 0.7601 0.4521 0.6571 0.1716  -0.2165 -0.0318 602 MET D C   
10690 O O   . MET D 602 ? 0.7226 0.4450 0.6418 0.1709  -0.2057 -0.0394 602 MET D O   
10691 C CB  . MET D 602 ? 0.7626 0.4477 0.6398 0.1558  -0.2211 -0.0109 602 MET D CB  
10692 C CG  . MET D 602 ? 0.7935 0.4600 0.6481 0.1543  -0.2316 -0.0003 602 MET D CG  
10693 S SD  . MET D 602 ? 0.7709 0.4551 0.6268 0.1387  -0.2250 0.0100  602 MET D SD  
10694 C CE  . MET D 602 ? 0.7942 0.4357 0.6177 0.1150  -0.2235 0.0261  602 MET D CE  
10695 N N   . LEU D 603 ? 0.6995 0.3581 0.5777 0.1695  -0.2211 -0.0291 603 LEU D N   
10696 C CA  . LEU D 603 ? 0.6919 0.3498 0.5760 0.1683  -0.2144 -0.0363 603 LEU D CA  
10697 C C   . LEU D 603 ? 0.7196 0.3389 0.5783 0.1549  -0.2172 -0.0263 603 LEU D C   
10698 O O   . LEU D 603 ? 0.7624 0.3508 0.6016 0.1598  -0.2273 -0.0242 603 LEU D O   
10699 C CB  . LEU D 603 ? 0.7060 0.3711 0.6010 0.1878  -0.2183 -0.0512 603 LEU D CB  
10700 C CG  . LEU D 603 ? 0.7115 0.3680 0.6066 0.1887  -0.2140 -0.0588 603 LEU D CG  
10701 C CD1 . LEU D 603 ? 0.6710 0.3509 0.5808 0.1794  -0.1998 -0.0623 603 LEU D CD1 
10702 C CD2 . LEU D 603 ? 0.7317 0.3941 0.6369 0.2091  -0.2193 -0.0738 603 LEU D CD2 
10703 N N   . ASP D 604 ? 0.7044 0.3251 0.5634 0.1379  -0.2087 -0.0207 604 ASP D N   
10704 C CA  . ASP D 604 ? 0.7275 0.3161 0.5657 0.1227  -0.2101 -0.0126 604 ASP D CA  
10705 C C   . ASP D 604 ? 0.7161 0.3081 0.5617 0.1204  -0.2040 -0.0202 604 ASP D C   
10706 O O   . ASP D 604 ? 0.6799 0.2966 0.5421 0.1159  -0.1951 -0.0236 604 ASP D O   
10707 C CB  . ASP D 604 ? 0.7172 0.3030 0.5489 0.1036  -0.2066 -0.0006 604 ASP D CB  
10708 C CG  . ASP D 604 ? 0.7493 0.2994 0.5573 0.0867  -0.2090 0.0079  604 ASP D CG  
10709 O OD1 . ASP D 604 ? 0.7795 0.3063 0.5754 0.0902  -0.2136 0.0049  604 ASP D OD1 
10710 O OD2 . ASP D 604 ? 0.7458 0.2914 0.5477 0.0691  -0.2059 0.0169  604 ASP D OD2 
10711 N N   . LEU D 605 ? 0.7041 0.2695 0.5357 0.1236  -0.2093 -0.0228 605 LEU D N   
10712 C CA  . LEU D 605 ? 0.7016 0.2642 0.5351 0.1204  -0.2051 -0.0293 605 LEU D CA  
10713 C C   . LEU D 605 ? 0.7319 0.2605 0.5441 0.1051  -0.2085 -0.0221 605 LEU D C   
10714 O O   . LEU D 605 ? 0.7464 0.2622 0.5536 0.1048  -0.2087 -0.0276 605 LEU D O   
10715 C CB  . LEU D 605 ? 0.7148 0.2792 0.5537 0.1389  -0.2071 -0.0421 605 LEU D CB  
10716 C CG  . LEU D 605 ? 0.6899 0.2882 0.5511 0.1545  -0.2033 -0.0521 605 LEU D CG  
10717 C CD1 . LEU D 605 ? 0.7079 0.3058 0.5742 0.1711  -0.2047 -0.0661 605 LEU D CD1 
10718 C CD2 . LEU D 605 ? 0.6453 0.2739 0.5233 0.1471  -0.1918 -0.0539 605 LEU D CD2 
10719 N N   . SER D 606 ? 0.7800 0.2934 0.5788 0.0913  -0.2106 -0.0104 606 SER D N   
10720 C CA  . SER D 606 ? 0.8165 0.2946 0.5926 0.0758  -0.2138 -0.0036 606 SER D CA  
10721 C C   . SER D 606 ? 0.7980 0.2830 0.5817 0.0598  -0.2075 -0.0051 606 SER D C   
10722 O O   . SER D 606 ? 0.7575 0.2729 0.5618 0.0596  -0.2013 -0.0094 606 SER D O   
10723 C CB  . SER D 606 ? 0.8382 0.2975 0.5957 0.0643  -0.2168 0.0090  606 SER D CB  
10724 O OG  . SER D 606 ? 0.8020 0.2863 0.5731 0.0546  -0.2102 0.0133  606 SER D OG  
10725 N N   . TYR D 607 ? 0.8814 0.3365 0.6473 0.0463  -0.2097 -0.0022 607 TYR D N   
10726 C CA  . TYR D 607 ? 0.8696 0.3281 0.6413 0.0285  -0.2052 -0.0036 607 TYR D CA  
10727 C C   . TYR D 607 ? 0.8402 0.3222 0.6299 0.0374  -0.2025 -0.0146 607 TYR D C   
10728 O O   . TYR D 607 ? 0.8007 0.3095 0.6081 0.0329  -0.1980 -0.0168 607 TYR D O   
10729 C CB  . TYR D 607 ? 0.8436 0.3166 0.6234 0.0112  -0.2001 0.0033  607 TYR D CB  
10730 C CG  . TYR D 607 ? 0.8795 0.3245 0.6366 -0.0043 -0.2010 0.0141  607 TYR D CG  
10731 C CD1 . TYR D 607 ? 0.8941 0.3302 0.6383 0.0038  -0.2045 0.0211  607 TYR D CD1 
10732 C CD2 . TYR D 607 ? 0.9115 0.3391 0.6590 -0.0280 -0.1979 0.0165  607 TYR D CD2 
10733 C CE1 . TYR D 607 ? 0.9316 0.3390 0.6499 -0.0113 -0.2052 0.0315  607 TYR D CE1 
10734 C CE2 . TYR D 607 ? 0.9429 0.3439 0.6665 -0.0446 -0.1967 0.0262  607 TYR D CE2 
10735 C CZ  . TYR D 607 ? 0.9554 0.3447 0.6624 -0.0361 -0.2005 0.0342  607 TYR D CZ  
10736 O OH  . TYR D 607 ? 1.0001 0.3604 0.6787 -0.0535 -0.1993 0.0442  607 TYR D OH  
10737 N N   . ASN D 608 ? 0.8458 0.3154 0.6288 0.0501  -0.2057 -0.0218 608 ASN D N   
10738 C CA  . ASN D 608 ? 0.8262 0.3138 0.6211 0.0596  -0.2028 -0.0326 608 ASN D CA  
10739 C C   . ASN D 608 ? 0.8626 0.3235 0.6433 0.0612  -0.2066 -0.0386 608 ASN D C   
10740 O O   . ASN D 608 ? 0.8999 0.3299 0.6630 0.0525  -0.2109 -0.0341 608 ASN D O   
10741 C CB  . ASN D 608 ? 0.8039 0.3151 0.6118 0.0787  -0.2002 -0.0377 608 ASN D CB  
10742 C CG  . ASN D 608 ? 0.7593 0.3039 0.5858 0.0764  -0.1939 -0.0366 608 ASN D CG  
10743 O OD1 . ASN D 608 ? 0.7407 0.2962 0.5736 0.0667  -0.1911 -0.0377 608 ASN D OD1 
10744 N ND2 . ASN D 608 ? 0.7442 0.3045 0.5791 0.0857  -0.1925 -0.0349 608 ASN D ND2 
10745 N N   . GLN D 609 ? 0.8673 0.3386 0.6539 0.0716  -0.2044 -0.0491 609 GLN D N   
10746 C CA  . GLN D 609 ? 0.9005 0.3486 0.6747 0.0743  -0.2072 -0.0566 609 GLN D CA  
10747 C C   . GLN D 609 ? 0.9102 0.3593 0.6862 0.0955  -0.2070 -0.0658 609 GLN D C   
10748 O O   . GLN D 609 ? 0.9292 0.3728 0.7020 0.1009  -0.2059 -0.0758 609 GLN D O   
10749 C CB  . GLN D 609 ? 0.8901 0.3456 0.6668 0.0648  -0.2051 -0.0623 609 GLN D CB  
10750 C CG  . GLN D 609 ? 0.9091 0.3463 0.6771 0.0448  -0.2084 -0.0584 609 GLN D CG  
10751 C CD  . GLN D 609 ? 0.9012 0.3511 0.6746 0.0360  -0.2080 -0.0644 609 GLN D CD  
10752 O OE1 . GLN D 609 ? 0.9119 0.3593 0.6806 0.0428  -0.2080 -0.0736 609 GLN D OE1 
10753 N NE2 . GLN D 609 ? 0.8825 0.3461 0.6658 0.0211  -0.2081 -0.0600 609 GLN D NE2 
10754 N N   . LEU D 610 ? 0.8847 0.3414 0.6663 0.1075  -0.2082 -0.0635 610 LEU D N   
10755 C CA  . LEU D 610 ? 0.8939 0.3552 0.6813 0.1282  -0.2084 -0.0737 610 LEU D CA  
10756 C C   . LEU D 610 ? 0.9446 0.3699 0.7151 0.1347  -0.2163 -0.0762 610 LEU D C   
10757 O O   . LEU D 610 ? 0.9728 0.3714 0.7276 0.1286  -0.2233 -0.0669 610 LEU D O   
10758 C CB  . LEU D 610 ? 0.8749 0.3570 0.6750 0.1387  -0.2087 -0.0713 610 LEU D CB  
10759 C CG  . LEU D 610 ? 0.8269 0.3434 0.6436 0.1330  -0.2009 -0.0685 610 LEU D CG  
10760 C CD1 . LEU D 610 ? 0.8183 0.3398 0.6368 0.1310  -0.2041 -0.0580 610 LEU D CD1 
10761 C CD2 . LEU D 610 ? 0.8049 0.3497 0.6388 0.1462  -0.1933 -0.0810 610 LEU D CD2 
10762 N N   . ASP D 611 ? 1.0008 0.4236 0.7730 0.1467  -0.2148 -0.0892 611 ASP D N   
10763 C CA  . ASP D 611 ? 1.0502 0.4402 0.8086 0.1560  -0.2220 -0.0941 611 ASP D CA  
10764 C C   . ASP D 611 ? 1.0575 0.4605 0.8295 0.1796  -0.2226 -0.1062 611 ASP D C   
10765 O O   . ASP D 611 ? 1.0218 0.4587 0.8132 0.1871  -0.2170 -0.1102 611 ASP D O   
10766 C CB  . ASP D 611 ? 1.0710 0.4417 0.8178 0.1475  -0.2202 -0.1001 611 ASP D CB  
10767 C CG  . ASP D 611 ? 1.0495 0.4436 0.8080 0.1523  -0.2108 -0.1134 611 ASP D CG  
10768 O OD1 . ASP D 611 ? 1.0145 0.4412 0.7901 0.1587  -0.2043 -0.1167 611 ASP D OD1 
10769 O OD2 . ASP D 611 ? 1.0742 0.4527 0.8231 0.1487  -0.2096 -0.1211 611 ASP D OD2 
10770 N N   . GLY D 612 ? 1.0972 0.4731 0.8596 0.1913  -0.2293 -0.1129 612 GLY D N   
10771 C CA  . GLY D 612 ? 1.1090 0.4954 0.8851 0.2146  -0.2316 -0.1254 612 GLY D CA  
10772 C C   . GLY D 612 ? 1.1270 0.5049 0.9002 0.2249  -0.2435 -0.1183 612 GLY D C   
10773 O O   . GLY D 612 ? 1.1352 0.4944 0.8922 0.2134  -0.2496 -0.1032 612 GLY D O   
10774 N N   . GLU D 613 ? 1.1474 0.5398 0.9365 0.2469  -0.2469 -0.1303 613 GLU D N   
10775 C CA  . GLU D 613 ? 1.1681 0.5504 0.9540 0.2607  -0.2607 -0.1267 613 GLU D CA  
10776 C C   . GLU D 613 ? 1.1266 0.5480 0.9326 0.2637  -0.2584 -0.1248 613 GLU D C   
10777 O O   . GLU D 613 ? 1.0854 0.5461 0.9151 0.2648  -0.2467 -0.1338 613 GLU D O   
10778 C CB  . GLU D 613 ? 1.2088 0.5821 1.0007 0.2848  -0.2684 -0.1425 613 GLU D CB  
10779 C CG  . GLU D 613 ? 1.2550 0.5871 1.0265 0.2835  -0.2713 -0.1455 613 GLU D CG  
10780 C CD  . GLU D 613 ? 1.3025 0.6207 1.0776 0.3084  -0.2815 -0.1598 613 GLU D CD  
10781 O OE1 . GLU D 613 ? 1.2912 0.6408 1.0925 0.3232  -0.2750 -0.1780 613 GLU D OE1 
10782 O OE2 . GLU D 613 ? 1.3589 0.6341 1.1103 0.3130  -0.2958 -0.1535 613 GLU D OE2 
10783 N N   . ILE D 614 ? 1.1380 0.5463 0.9323 0.2643  -0.2696 -0.1132 614 ILE D N   
10784 C CA  . ILE D 614 ? 1.1050 0.5470 0.9164 0.2679  -0.2693 -0.1115 614 ILE D CA  
10785 C C   . ILE D 614 ? 1.1077 0.5775 0.9450 0.2923  -0.2723 -0.1297 614 ILE D C   
10786 O O   . ILE D 614 ? 1.1534 0.6036 0.9853 0.3098  -0.2860 -0.1354 614 ILE D O   
10787 C CB  . ILE D 614 ? 1.1272 0.5443 0.9163 0.2626  -0.2810 -0.0953 614 ILE D CB  
10788 C CG1 . ILE D 614 ? 1.1309 0.5191 0.8944 0.2377  -0.2774 -0.0791 614 ILE D CG1 
10789 C CG2 . ILE D 614 ? 1.0916 0.5443 0.8981 0.2649  -0.2798 -0.0936 614 ILE D CG2 
10790 C CD1 . ILE D 614 ? 1.1755 0.5260 0.9090 0.2321  -0.2895 -0.0643 614 ILE D CD1 
10791 N N   . SER D 615 ? 1.0816 0.5971 0.9474 0.2935  -0.2597 -0.1397 615 SER D N   
10792 C CA  . SER D 615 ? 1.0810 0.6291 0.9754 0.3145  -0.2598 -0.1595 615 SER D CA  
10793 C C   . SER D 615 ? 1.1009 0.6516 0.9985 0.3295  -0.2757 -0.1591 615 SER D C   
10794 O O   . SER D 615 ? 1.0850 0.6391 0.9768 0.3215  -0.2787 -0.1464 615 SER D O   
10795 C CB  . SER D 615 ? 1.0280 0.6238 0.9495 0.3091  -0.2419 -0.1685 615 SER D CB  
10796 O OG  . SER D 615 ? 1.0269 0.6582 0.9782 0.3276  -0.2407 -0.1887 615 SER D OG  
10797 N N   . SER D 616 ? 1.1159 0.6646 1.0226 0.3519  -0.2864 -0.1738 616 SER D N   
10798 C CA  . SER D 616 ? 1.1374 0.6926 1.0503 0.3691  -0.3027 -0.1770 616 SER D CA  
10799 C C   . SER D 616 ? 1.0934 0.7048 1.0407 0.3728  -0.2952 -0.1877 616 SER D C   
10800 O O   . SER D 616 ? 1.1032 0.7244 1.0560 0.3834  -0.3077 -0.1887 616 SER D O   
10801 C CB  . SER D 616 ? 1.1915 0.7307 1.1068 0.3932  -0.3168 -0.1918 616 SER D CB  
10802 O OG  . SER D 616 ? 1.1781 0.7518 1.1247 0.4029  -0.3053 -0.2140 616 SER D OG  
10803 N N   . GLN D 617 ? 1.0877 0.7343 1.0565 0.3638  -0.2753 -0.1961 617 GLN D N   
10804 C CA  . GLN D 617 ? 1.0449 0.7445 1.0451 0.3639  -0.2657 -0.2060 617 GLN D CA  
10805 C C   . GLN D 617 ? 1.0166 0.7201 1.0082 0.3498  -0.2659 -0.1887 617 GLN D C   
10806 O O   . GLN D 617 ? 0.9787 0.7238 0.9945 0.3499  -0.2599 -0.1956 617 GLN D O   
10807 C CB  . GLN D 617 ? 1.0054 0.7344 1.0244 0.3553  -0.2431 -0.2178 617 GLN D CB  
10808 C CG  . GLN D 617 ? 0.9840 0.7688 1.0419 0.3638  -0.2338 -0.2395 617 GLN D CG  
10809 C CD  . GLN D 617 ? 1.0285 0.8237 1.1054 0.3879  -0.2451 -0.2598 617 GLN D CD  
10810 O OE1 . GLN D 617 ? 1.0577 0.8346 1.1307 0.3961  -0.2457 -0.2684 617 GLN D OE1 
10811 N NE2 . GLN D 617 ? 1.0248 0.8498 1.1227 0.3994  -0.2545 -0.2684 617 GLN D NE2 
10812 N N   . PHE D 618 ? 1.0595 0.7217 1.0180 0.3370  -0.2718 -0.1673 618 PHE D N   
10813 C CA  . PHE D 618 ? 1.0360 0.6987 0.9846 0.3244  -0.2730 -0.1510 618 PHE D CA  
10814 C C   . PHE D 618 ? 1.0531 0.7285 1.0094 0.3388  -0.2875 -0.1546 618 PHE D C   
10815 O O   . PHE D 618 ? 1.0266 0.7123 0.9812 0.3301  -0.2869 -0.1449 618 PHE D O   
10816 C CB  . PHE D 618 ? 1.0625 0.6761 0.9733 0.3090  -0.2778 -0.1296 618 PHE D CB  
10817 C CG  . PHE D 618 ? 1.0336 0.6458 0.9386 0.2872  -0.2619 -0.1207 618 PHE D CG  
10818 C CD1 . PHE D 618 ? 0.9968 0.6364 0.9221 0.2850  -0.2465 -0.1324 618 PHE D CD1 
10819 C CD2 . PHE D 618 ? 1.0344 0.6178 0.9131 0.2686  -0.2624 -0.1015 618 PHE D CD2 
10820 C CE1 . PHE D 618 ? 0.9625 0.5991 0.8808 0.2659  -0.2336 -0.1246 618 PHE D CE1 
10821 C CE2 . PHE D 618 ? 0.9952 0.5791 0.8704 0.2493  -0.2491 -0.0946 618 PHE D CE2 
10822 C CZ  . PHE D 618 ? 0.9620 0.5719 0.8566 0.2486  -0.2356 -0.1059 618 PHE D CZ  
10823 N N   . ARG D 619 ? 1.0846 0.7597 1.0496 0.3608  -0.3007 -0.1691 619 ARG D N   
10824 C CA  . ARG D 619 ? 1.0975 0.7866 1.0720 0.3768  -0.3160 -0.1754 619 ARG D CA  
10825 C C   . ARG D 619 ? 1.0470 0.7929 1.0555 0.3751  -0.3055 -0.1859 619 ARG D C   
10826 O O   . ARG D 619 ? 1.0525 0.8109 1.0656 0.3819  -0.3160 -0.1865 619 ARG D O   
10827 C CB  . ARG D 619 ? 1.1443 0.8280 1.1274 0.4018  -0.3306 -0.1928 619 ARG D CB  
10828 C CG  . ARG D 619 ? 1.1865 0.8663 1.1678 0.4205  -0.3528 -0.1965 619 ARG D CG  
10829 C CD  . ARG D 619 ? 1.2141 0.9124 1.2213 0.4462  -0.3624 -0.2214 619 ARG D CD  
10830 N NE  . ARG D 619 ? 1.2733 0.9521 1.2699 0.4667  -0.3882 -0.2237 619 ARG D NE  
10831 C CZ  . ARG D 619 ? 1.2876 1.0003 1.3143 0.4884  -0.3988 -0.2456 619 ARG D CZ  
10832 N NH1 . ARG D 619 ? 1.2498 1.0192 1.3201 0.4915  -0.3849 -0.2678 619 ARG D NH1 
10833 N NH2 . ARG D 619 ? 1.3395 1.0280 1.3516 0.5070  -0.4241 -0.2458 619 ARG D NH2 
10834 N N   . SER D 620 ? 0.9695 0.7483 1.0002 0.3656  -0.2851 -0.1944 620 SER D N   
10835 C CA  . SER D 620 ? 0.9252 0.7583 0.9886 0.3630  -0.2736 -0.2063 620 SER D CA  
10836 C C   . SER D 620 ? 0.8922 0.7286 0.9463 0.3471  -0.2700 -0.1897 620 SER D C   
10837 O O   . SER D 620 ? 0.8685 0.7440 0.9453 0.3480  -0.2672 -0.1978 620 SER D O   
10838 C CB  . SER D 620 ? 0.8896 0.7511 0.9741 0.3554  -0.2517 -0.2189 620 SER D CB  
10839 O OG  . SER D 620 ? 0.9189 0.7715 1.0076 0.3676  -0.2531 -0.2321 620 SER D OG  
10840 N N   . LEU D 621 ? 0.8663 0.6639 0.8887 0.3322  -0.2697 -0.1677 621 LEU D N   
10841 C CA  . LEU D 621 ? 0.8372 0.6371 0.8507 0.3157  -0.2647 -0.1518 621 LEU D CA  
10842 C C   . LEU D 621 ? 0.8640 0.6541 0.8664 0.3237  -0.2821 -0.1458 621 LEU D C   
10843 O O   . LEU D 621 ? 0.8969 0.6436 0.8669 0.3208  -0.2935 -0.1297 621 LEU D O   
10844 C CB  . LEU D 621 ? 0.8319 0.5956 0.8173 0.2968  -0.2583 -0.1325 621 LEU D CB  
10845 C CG  . LEU D 621 ? 0.7895 0.5705 0.7853 0.2823  -0.2382 -0.1338 621 LEU D CG  
10846 C CD1 . LEU D 621 ? 0.7830 0.5919 0.8045 0.2921  -0.2296 -0.1548 621 LEU D CD1 
10847 C CD2 . LEU D 621 ? 0.7969 0.5382 0.7649 0.2675  -0.2355 -0.1183 621 LEU D CD2 
10848 N N   . GLN D 622 ? 0.8295 0.6607 0.8588 0.3329  -0.2838 -0.1594 622 GLN D N   
10849 C CA  . GLN D 622 ? 0.8591 0.6851 0.8813 0.3439  -0.3018 -0.1576 622 GLN D CA  
10850 C C   . GLN D 622 ? 0.8490 0.6604 0.8494 0.3288  -0.3019 -0.1372 622 GLN D C   
10851 O O   . GLN D 622 ? 0.8836 0.6746 0.8653 0.3354  -0.3182 -0.1299 622 GLN D O   
10852 C CB  . GLN D 622 ? 0.8476 0.7261 0.9077 0.3571  -0.3027 -0.1803 622 GLN D CB  
10853 C CG  . GLN D 622 ? 0.8678 0.7618 0.9504 0.3751  -0.3063 -0.2028 622 GLN D CG  
10854 C CD  . GLN D 622 ? 0.9277 0.7947 0.9974 0.3968  -0.3312 -0.2061 622 GLN D CD  
10855 O OE1 . GLN D 622 ? 0.9652 0.7809 1.0012 0.3981  -0.3418 -0.1919 622 GLN D OE1 
10856 N NE2 . GLN D 622 ? 0.9396 0.8409 1.0359 0.4136  -0.3409 -0.2256 622 GLN D NE2 
10857 N N   . ASN D 623 ? 0.8578 0.6787 0.8595 0.3092  -0.2846 -0.1282 623 ASN D N   
10858 C CA  . ASN D 623 ? 0.8443 0.6574 0.8296 0.2944  -0.2828 -0.1106 623 ASN D CA  
10859 C C   . ASN D 623 ? 0.8547 0.6223 0.8060 0.2781  -0.2806 -0.0899 623 ASN D C   
10860 O O   . ASN D 623 ? 0.8463 0.6051 0.7822 0.2644  -0.2786 -0.0749 623 ASN D O   
10861 C CB  . ASN D 623 ? 0.7911 0.6501 0.8035 0.2837  -0.2656 -0.1159 623 ASN D CB  
10862 C CG  . ASN D 623 ? 0.7812 0.6847 0.8229 0.2954  -0.2688 -0.1332 623 ASN D CG  
10863 O OD1 . ASN D 623 ? 0.7981 0.7011 0.8330 0.2998  -0.2805 -0.1293 623 ASN D OD1 
10864 N ND2 . ASN D 623 ? 0.7579 0.7004 0.8320 0.2995  -0.2580 -0.1530 623 ASN D ND2 
10865 N N   . LEU D 624 ? 0.8521 0.5923 0.7919 0.2787  -0.2807 -0.0895 624 LEU D N   
10866 C CA  . LEU D 624 ? 0.8611 0.5614 0.7712 0.2616  -0.2774 -0.0720 624 LEU D CA  
10867 C C   . LEU D 624 ? 0.9043 0.5645 0.7792 0.2583  -0.2912 -0.0561 624 LEU D C   
10868 O O   . LEU D 624 ? 0.9515 0.5902 0.8132 0.2731  -0.3078 -0.0584 624 LEU D O   
10869 C CB  . LEU D 624 ? 0.8792 0.5580 0.7839 0.2648  -0.2766 -0.0767 624 LEU D CB  
10870 C CG  . LEU D 624 ? 0.8680 0.5244 0.7571 0.2452  -0.2659 -0.0653 624 LEU D CG  
10871 C CD1 . LEU D 624 ? 0.8706 0.5244 0.7671 0.2501  -0.2613 -0.0758 624 LEU D CD1 
10872 C CD2 . LEU D 624 ? 0.9089 0.5167 0.7599 0.2352  -0.2750 -0.0480 624 LEU D CD2 
10873 N N   . GLU D 625 ? 0.9099 0.5592 0.7685 0.2387  -0.2845 -0.0402 625 GLU D N   
10874 C CA  . GLU D 625 ? 0.9511 0.5604 0.7727 0.2310  -0.2948 -0.0238 625 GLU D CA  
10875 C C   . GLU D 625 ? 0.9698 0.5378 0.7624 0.2128  -0.2909 -0.0104 625 GLU D C   
10876 O O   . GLU D 625 ? 1.0222 0.5462 0.7799 0.2104  -0.3021 -0.0005 625 GLU D O   
10877 C CB  . GLU D 625 ? 0.9283 0.5572 0.7514 0.2218  -0.2915 -0.0161 625 GLU D CB  
10878 C CG  . GLU D 625 ? 0.9125 0.5824 0.7627 0.2378  -0.2959 -0.0289 625 GLU D CG  
10879 C CD  . GLU D 625 ? 0.8998 0.5832 0.7457 0.2292  -0.2953 -0.0202 625 GLU D CD  
10880 O OE1 . GLU D 625 ? 0.9317 0.5799 0.7427 0.2182  -0.3009 -0.0043 625 GLU D OE1 
10881 O OE2 . GLU D 625 ? 0.8603 0.5892 0.7364 0.2324  -0.2889 -0.0297 625 GLU D OE2 
10882 N N   . ARG D 626 ? 0.9654 0.5458 0.7705 0.1996  -0.2758 -0.0104 626 ARG D N   
10883 C CA  . ARG D 626 ? 0.9786 0.5249 0.7599 0.1809  -0.2712 0.0008  626 ARG D CA  
10884 C C   . ARG D 626 ? 0.9615 0.5128 0.7573 0.1824  -0.2639 -0.0084 626 ARG D C   
10885 O O   . ARG D 626 ? 0.9170 0.5056 0.7428 0.1857  -0.2538 -0.0185 626 ARG D O   
10886 C CB  . ARG D 626 ? 0.9471 0.5013 0.7259 0.1593  -0.2602 0.0120  626 ARG D CB  
10887 C CG  . ARG D 626 ? 0.9832 0.5117 0.7310 0.1498  -0.2672 0.0261  626 ARG D CG  
10888 C CD  . ARG D 626 ? 0.9425 0.4952 0.6986 0.1352  -0.2572 0.0327  626 ARG D CD  
10889 N NE  . ARG D 626 ? 0.9832 0.5049 0.7037 0.1193  -0.2608 0.0478  626 ARG D NE  
10890 C CZ  . ARG D 626 ? 1.0190 0.5039 0.7106 0.0997  -0.2583 0.0582  626 ARG D CZ  
10891 N NH1 . ARG D 626 ? 1.0168 0.4918 0.7121 0.0937  -0.2529 0.0554  626 ARG D NH1 
10892 N NH2 . ARG D 626 ? 1.0484 0.5059 0.7056 0.0845  -0.2608 0.0712  626 ARG D NH2 
10893 N N   . LEU D 627 ? 0.8835 0.3954 0.6557 0.1790  -0.2690 -0.0048 627 LEU D N   
10894 C CA  . LEU D 627 ? 0.8776 0.3887 0.6589 0.1805  -0.2637 -0.0131 627 LEU D CA  
10895 C C   . LEU D 627 ? 0.9024 0.3756 0.6569 0.1614  -0.2620 -0.0024 627 LEU D C   
10896 O O   . LEU D 627 ? 0.9518 0.3849 0.6746 0.1571  -0.2714 0.0069  627 LEU D O   
10897 C CB  . LEU D 627 ? 0.9086 0.4131 0.6932 0.2032  -0.2746 -0.0253 627 LEU D CB  
10898 C CG  . LEU D 627 ? 0.8961 0.4115 0.6979 0.2097  -0.2684 -0.0381 627 LEU D CG  
10899 C CD1 . LEU D 627 ? 0.8370 0.3927 0.6659 0.2017  -0.2522 -0.0429 627 LEU D CD1 
10900 C CD2 . LEU D 627 ? 0.9171 0.4403 0.7315 0.2347  -0.2780 -0.0530 627 LEU D CD2 
10901 N N   . ASP D 628 ? 0.8770 0.3621 0.6432 0.1494  -0.2502 -0.0041 628 ASP D N   
10902 C CA  . ASP D 628 ? 0.8969 0.3513 0.6425 0.1304  -0.2476 0.0038  628 ASP D CA  
10903 C C   . ASP D 628 ? 0.8855 0.3457 0.6437 0.1330  -0.2424 -0.0063 628 ASP D C   
10904 O O   . ASP D 628 ? 0.8406 0.3330 0.6224 0.1309  -0.2323 -0.0122 628 ASP D O   
10905 C CB  . ASP D 628 ? 0.8715 0.3338 0.6164 0.1083  -0.2386 0.0138  628 ASP D CB  
10906 C CG  . ASP D 628 ? 0.9033 0.3296 0.6223 0.0869  -0.2376 0.0230  628 ASP D CG  
10907 O OD1 . ASP D 628 ? 0.9411 0.3377 0.6441 0.0889  -0.2429 0.0213  628 ASP D OD1 
10908 O OD2 . ASP D 628 ? 0.8920 0.3200 0.6071 0.0674  -0.2312 0.0314  628 ASP D OD2 
10909 N N   . LEU D 629 ? 0.8779 0.3049 0.6183 0.1375  -0.2496 -0.0082 629 LEU D N   
10910 C CA  . LEU D 629 ? 0.8764 0.3021 0.6234 0.1391  -0.2458 -0.0173 629 LEU D CA  
10911 C C   . LEU D 629 ? 0.9068 0.2968 0.6303 0.1205  -0.2456 -0.0102 629 LEU D C   
10912 O O   . LEU D 629 ? 0.9257 0.3006 0.6452 0.1231  -0.2465 -0.0165 629 LEU D O   
10913 C CB  . LEU D 629 ? 0.9017 0.3223 0.6521 0.1623  -0.2538 -0.0289 629 LEU D CB  
10914 C CG  . LEU D 629 ? 0.8674 0.3290 0.6488 0.1803  -0.2498 -0.0432 629 LEU D CG  
10915 C CD1 . LEU D 629 ? 0.8242 0.3220 0.6240 0.1789  -0.2442 -0.0411 629 LEU D CD1 
10916 C CD2 . LEU D 629 ? 0.9038 0.3557 0.6848 0.2035  -0.2613 -0.0527 629 LEU D CD2 
10917 N N   . SER D 630 ? 0.9642 0.3409 0.6724 0.1010  -0.2439 0.0021  630 SER D N   
10918 C CA  . SER D 630 ? 1.0009 0.3409 0.6843 0.0818  -0.2440 0.0090  630 SER D CA  
10919 C C   . SER D 630 ? 0.9731 0.3275 0.6709 0.0689  -0.2347 0.0042  630 SER D C   
10920 O O   . SER D 630 ? 0.9239 0.3158 0.6481 0.0716  -0.2278 -0.0017 630 SER D O   
10921 C CB  . SER D 630 ? 1.0186 0.3413 0.6809 0.0632  -0.2435 0.0228  630 SER D CB  
10922 O OG  . SER D 630 ? 0.9699 0.3263 0.6519 0.0519  -0.2341 0.0252  630 SER D OG  
10923 N N   . HIS D 631 ? 1.0507 0.3731 0.7295 0.0546  -0.2353 0.0065  631 HIS D N   
10924 C CA  . HIS D 631 ? 1.0349 0.3656 0.7236 0.0394  -0.2281 0.0024  631 HIS D CA  
10925 C C   . HIS D 631 ? 1.0019 0.3575 0.7124 0.0543  -0.2261 -0.0106 631 HIS D C   
10926 O O   . HIS D 631 ? 0.9567 0.3458 0.6894 0.0522  -0.2196 -0.0147 631 HIS D O   
10927 C CB  . HIS D 631 ? 0.9974 0.3502 0.6975 0.0199  -0.2200 0.0080  631 HIS D CB  
10928 C CG  . HIS D 631 ? 1.0301 0.3571 0.7067 0.0007  -0.2195 0.0199  631 HIS D CG  
10929 N ND1 . HIS D 631 ? 1.0326 0.3594 0.7009 0.0036  -0.2215 0.0281  631 HIS D ND1 
10930 C CD2 . HIS D 631 ? 1.0676 0.3678 0.7259 -0.0229 -0.2165 0.0245  631 HIS D CD2 
10931 C CE1 . HIS D 631 ? 1.0685 0.3681 0.7120 -0.0176 -0.2196 0.0378  631 HIS D CE1 
10932 N NE2 . HIS D 631 ? 1.0883 0.3721 0.7260 -0.0345 -0.2159 0.0355  631 HIS D NE2 
10933 N N   . ASN D 632 ? 1.0430 0.3796 0.7452 0.0695  -0.2320 -0.0172 632 ASN D N   
10934 C CA  . ASN D 632 ? 1.0254 0.3799 0.7436 0.0834  -0.2298 -0.0302 632 ASN D CA  
10935 C C   . ASN D 632 ? 1.0743 0.3931 0.7748 0.0878  -0.2354 -0.0354 632 ASN D C   
10936 O O   . ASN D 632 ? 1.1196 0.4008 0.7960 0.0788  -0.2405 -0.0286 632 ASN D O   
10937 C CB  . ASN D 632 ? 0.9993 0.3826 0.7357 0.1048  -0.2298 -0.0361 632 ASN D CB  
10938 C CG  . ASN D 632 ? 0.9451 0.3684 0.7032 0.1007  -0.2219 -0.0347 632 ASN D CG  
10939 O OD1 . ASN D 632 ? 0.9138 0.3608 0.6871 0.0997  -0.2152 -0.0414 632 ASN D OD1 
10940 N ND2 . ASN D 632 ? 0.9372 0.3660 0.6947 0.0981  -0.2231 -0.0258 632 ASN D ND2 
10941 N N   . ASN D 633 ? 1.1377 0.4669 0.8489 0.1011  -0.2339 -0.0480 633 ASN D N   
10942 C CA  . ASN D 633 ? 1.1823 0.4804 0.8794 0.1074  -0.2385 -0.0552 633 ASN D CA  
10943 C C   . ASN D 633 ? 1.1976 0.4958 0.8994 0.1331  -0.2436 -0.0639 633 ASN D C   
10944 O O   . ASN D 633 ? 1.2151 0.5064 0.9179 0.1436  -0.2438 -0.0754 633 ASN D O   
10945 C CB  . ASN D 633 ? 1.1705 0.4764 0.8737 0.1004  -0.2326 -0.0643 633 ASN D CB  
10946 C CG  . ASN D 633 ? 1.2200 0.4859 0.9023 0.0921  -0.2363 -0.0665 633 ASN D CG  
10947 O OD1 . ASN D 633 ? 1.2607 0.4922 0.9224 0.0850  -0.2419 -0.0586 633 ASN D OD1 
10948 N ND2 . ASN D 633 ? 1.2191 0.4883 0.9050 0.0924  -0.2330 -0.0776 633 ASN D ND2 
10949 N N   . LEU D 634 ? 1.1596 0.4665 0.8651 0.1435  -0.2480 -0.0593 634 LEU D N   
10950 C CA  . LEU D 634 ? 1.1805 0.4906 0.8933 0.1685  -0.2542 -0.0685 634 LEU D CA  
10951 C C   . LEU D 634 ? 1.2409 0.5046 0.9301 0.1760  -0.2652 -0.0694 634 LEU D C   
10952 O O   . LEU D 634 ? 1.2760 0.5042 0.9396 0.1646  -0.2713 -0.0578 634 LEU D O   
10953 C CB  . LEU D 634 ? 1.1619 0.4919 0.8836 0.1765  -0.2575 -0.0634 634 LEU D CB  
10954 C CG  . LEU D 634 ? 1.0948 0.4713 0.8413 0.1724  -0.2472 -0.0636 634 LEU D CG  
10955 C CD1 . LEU D 634 ? 1.0825 0.4617 0.8234 0.1612  -0.2485 -0.0497 634 LEU D CD1 
10956 C CD2 . LEU D 634 ? 1.0759 0.4844 0.8468 0.1938  -0.2457 -0.0772 634 LEU D CD2 
10957 N N   . SER D 635 ? 1.2460 0.5091 0.9430 0.1950  -0.2674 -0.0835 635 SER D N   
10958 C CA  . SER D 635 ? 1.3089 0.5292 0.9860 0.2059  -0.2784 -0.0868 635 SER D CA  
10959 C C   . SER D 635 ? 1.3236 0.5524 1.0122 0.2331  -0.2876 -0.0955 635 SER D C   
10960 O O   . SER D 635 ? 1.2851 0.5528 0.9965 0.2418  -0.2849 -0.0987 635 SER D O   
10961 C CB  . SER D 635 ? 1.3247 0.5322 0.9999 0.2041  -0.2735 -0.0976 635 SER D CB  
10962 O OG  . SER D 635 ? 1.3047 0.5425 1.0046 0.2215  -0.2680 -0.1145 635 SER D OG  
10963 N N   . GLY D 636 ? 1.3547 0.5465 1.0277 0.2468  -0.2989 -0.1002 636 GLY D N   
10964 C CA  . GLY D 636 ? 1.3778 0.5732 1.0599 0.2736  -0.3104 -0.1090 636 GLY D CA  
10965 C C   . GLY D 636 ? 1.4007 0.5787 1.0651 0.2753  -0.3234 -0.0958 636 GLY D C   
10966 O O   . GLY D 636 ? 1.4003 0.5620 1.0442 0.2550  -0.3225 -0.0796 636 GLY D O   
10967 N N   . GLN D 637 ? 1.4164 0.5983 1.0889 0.3001  -0.3358 -0.1039 637 GLN D N   
10968 C CA  . GLN D 637 ? 1.4439 0.6088 1.0991 0.3052  -0.3502 -0.0934 637 GLN D CA  
10969 C C   . GLN D 637 ? 1.3880 0.6031 1.0694 0.3070  -0.3455 -0.0935 637 GLN D C   
10970 O O   . GLN D 637 ? 1.3423 0.6047 1.0589 0.3153  -0.3361 -0.1070 637 GLN D O   
10971 C CB  . GLN D 637 ? 1.5079 0.6447 1.1545 0.3321  -0.3694 -0.1022 637 GLN D CB  
10972 C CG  . GLN D 637 ? 1.5654 0.6542 1.1897 0.3342  -0.3742 -0.1053 637 GLN D CG  
10973 C CD  . GLN D 637 ? 1.6448 0.6849 1.2416 0.3526  -0.3966 -0.1042 637 GLN D CD  
10974 O OE1 . GLN D 637 ? 1.6578 0.7009 1.2525 0.3651  -0.4095 -0.1018 637 GLN D OE1 
10975 N NE2 . GLN D 637 ? 1.7014 0.6948 1.2757 0.3547  -0.4019 -0.1063 637 GLN D NE2 
10976 N N   . ILE D 638 ? 1.4049 0.6082 1.0676 0.2978  -0.3513 -0.0785 638 ILE D N   
10977 C CA  . ILE D 638 ? 1.3591 0.6051 1.0431 0.2997  -0.3486 -0.0778 638 ILE D CA  
10978 C C   . ILE D 638 ? 1.3697 0.6380 1.0771 0.3294  -0.3595 -0.0944 638 ILE D C   
10979 O O   . ILE D 638 ? 1.4303 0.6649 1.1200 0.3462  -0.3775 -0.0964 638 ILE D O   
10980 C CB  . ILE D 638 ? 1.3760 0.5982 1.0311 0.2861  -0.3548 -0.0593 638 ILE D CB  
10981 C CG1 . ILE D 638 ? 1.3882 0.5755 1.0137 0.2584  -0.3476 -0.0444 638 ILE D CG1 
10982 C CG2 . ILE D 638 ? 1.3181 0.5874 0.9967 0.2820  -0.3472 -0.0577 638 ILE D CG2 
10983 C CD1 . ILE D 638 ? 1.4250 0.5758 1.0137 0.2452  -0.3552 -0.0268 638 ILE D CD1 
10984 N N   . PRO D 639 ? 1.3402 0.6638 1.0868 0.3366  -0.3496 -0.1074 639 PRO D N   
10985 C CA  . PRO D 639 ? 1.3497 0.6993 1.1233 0.3644  -0.3582 -0.1267 639 PRO D CA  
10986 C C   . PRO D 639 ? 1.3893 0.7243 1.1505 0.3790  -0.3784 -0.1234 639 PRO D C   
10987 O O   . PRO D 639 ? 1.3692 0.7146 1.1264 0.3702  -0.3786 -0.1128 639 PRO D O   
10988 C CB  . PRO D 639 ? 1.2794 0.6915 1.0929 0.3618  -0.3412 -0.1368 639 PRO D CB  
10989 C CG  . PRO D 639 ? 1.2377 0.6535 1.0413 0.3350  -0.3287 -0.1197 639 PRO D CG  
10990 C CD  . PRO D 639 ? 1.2706 0.6355 1.0384 0.3192  -0.3299 -0.1058 639 PRO D CD  
10991 N N   . PRO D 640 ? 1.3792 0.6885 1.1329 0.4019  -0.3964 -0.1325 640 PRO D N   
10992 C CA  . PRO D 640 ? 1.4237 0.7167 1.1640 0.4180  -0.4181 -0.1305 640 PRO D CA  
10993 C C   . PRO D 640 ? 1.3848 0.7329 1.1600 0.4289  -0.4183 -0.1410 640 PRO D C   
10994 O O   . PRO D 640 ? 1.4158 0.7542 1.1801 0.4398  -0.4354 -0.1382 640 PRO D O   
10995 C CB  . PRO D 640 ? 1.4905 0.7524 1.2239 0.4427  -0.4353 -0.1428 640 PRO D CB  
10996 C CG  . PRO D 640 ? 1.4955 0.7328 1.2180 0.4308  -0.4240 -0.1411 640 PRO D CG  
10997 C CD  . PRO D 640 ? 1.4169 0.7018 1.1675 0.4124  -0.3989 -0.1428 640 PRO D CD  
10998 N N   . SER D 641 ? 1.4125 0.8164 1.2275 0.4259  -0.4002 -0.1532 641 SER D N   
10999 C CA  . SER D 641 ? 1.3751 0.8334 1.2239 0.4330  -0.3981 -0.1634 641 SER D CA  
11000 C C   . SER D 641 ? 1.3481 0.8102 1.1842 0.4147  -0.3943 -0.1456 641 SER D C   
11001 O O   . SER D 641 ? 1.3093 0.8155 1.1715 0.4183  -0.3918 -0.1526 641 SER D O   
11002 C CB  . SER D 641 ? 1.3176 0.8309 1.2088 0.4319  -0.3778 -0.1807 641 SER D CB  
11003 O OG  . SER D 641 ? 1.2824 0.8489 1.2079 0.4401  -0.3762 -0.1934 641 SER D OG  
11004 N N   . PHE D 642 ? 1.3968 0.8156 1.1948 0.3948  -0.3932 -0.1241 642 PHE D N   
11005 C CA  . PHE D 642 ? 1.3689 0.7902 1.1542 0.3757  -0.3880 -0.1072 642 PHE D CA  
11006 C C   . PHE D 642 ? 1.4181 0.8142 1.1792 0.3846  -0.4082 -0.0996 642 PHE D C   
11007 O O   . PHE D 642 ? 1.3956 0.7934 1.1455 0.3702  -0.4051 -0.0863 642 PHE D O   
11008 C CB  . PHE D 642 ? 1.3666 0.7563 1.1239 0.3485  -0.3762 -0.0889 642 PHE D CB  
11009 C CG  . PHE D 642 ? 1.3081 0.7317 1.0898 0.3339  -0.3537 -0.0925 642 PHE D CG  
11010 C CD1 . PHE D 642 ? 1.2697 0.7418 1.0916 0.3453  -0.3450 -0.1114 642 PHE D CD1 
11011 C CD2 . PHE D 642 ? 1.2816 0.6885 1.0456 0.3083  -0.3415 -0.0776 642 PHE D CD2 
11012 C CE1 . PHE D 642 ? 1.2104 0.7098 1.0509 0.3317  -0.3249 -0.1143 642 PHE D CE1 
11013 C CE2 . PHE D 642 ? 1.2260 0.6621 1.0107 0.2958  -0.3226 -0.0811 642 PHE D CE2 
11014 C CZ  . PHE D 642 ? 1.1913 0.6719 1.0127 0.3076  -0.3145 -0.0989 642 PHE D CZ  
11015 N N   . LYS D 643 ? 1.4002 0.7720 1.1521 0.4082  -0.4293 -0.1079 643 LYS D N   
11016 C CA  . LYS D 643 ? 1.4467 0.7975 1.1774 0.4193  -0.4501 -0.1027 643 LYS D CA  
11017 C C   . LYS D 643 ? 1.4040 0.8094 1.1675 0.4251  -0.4482 -0.1111 643 LYS D C   
11018 O O   . LYS D 643 ? 1.4239 0.8183 1.1694 0.4250  -0.4591 -0.1021 643 LYS D O   
11019 C CB  . LYS D 643 ? 1.5199 0.8394 1.2398 0.4469  -0.4742 -0.1134 643 LYS D CB  
11020 C CG  . LYS D 643 ? 1.5896 0.8367 1.2600 0.4428  -0.4849 -0.0999 643 LYS D CG  
11021 C CD  . LYS D 643 ? 1.5964 0.8355 1.2758 0.4477  -0.4795 -0.1100 643 LYS D CD  
11022 C CE  . LYS D 643 ? 1.6367 0.8137 1.2702 0.4294  -0.4781 -0.0924 643 LYS D CE  
11023 N NZ  . LYS D 643 ? 1.6066 0.7918 1.2546 0.4197  -0.4604 -0.0974 643 LYS D NZ  
11024 N N   . ASP D 644 ? 1.3855 0.8488 1.1956 0.4292  -0.4344 -0.1285 644 ASP D N   
11025 C CA  . ASP D 644 ? 1.3504 0.8693 1.1962 0.4369  -0.4327 -0.1408 644 ASP D CA  
11026 C C   . ASP D 644 ? 1.2936 0.8402 1.1464 0.4129  -0.4134 -0.1296 644 ASP D C   
11027 O O   . ASP D 644 ? 1.2520 0.8497 1.1379 0.4158  -0.4074 -0.1405 644 ASP D O   
11028 C CB  . ASP D 644 ? 1.3236 0.8915 1.2161 0.4532  -0.4272 -0.1672 644 ASP D CB  
11029 C CG  . ASP D 644 ? 1.3831 0.9248 1.2713 0.4764  -0.4441 -0.1794 644 ASP D CG  
11030 O OD1 . ASP D 644 ? 1.4476 0.9412 1.3020 0.4868  -0.4658 -0.1715 644 ASP D OD1 
11031 O OD2 . ASP D 644 ? 1.3683 0.9363 1.2858 0.4841  -0.4356 -0.1972 644 ASP D OD2 
11032 N N   . MET D 645 ? 1.3266 0.8418 1.1500 0.3893  -0.4036 -0.1092 645 MET D N   
11033 C CA  . MET D 645 ? 1.2664 0.8054 1.0955 0.3666  -0.3857 -0.0984 645 MET D CA  
11034 C C   . MET D 645 ? 1.2889 0.8092 1.0921 0.3623  -0.3965 -0.0841 645 MET D C   
11035 O O   . MET D 645 ? 1.3207 0.7948 1.0840 0.3481  -0.3994 -0.0653 645 MET D O   
11036 C CB  . MET D 645 ? 1.2450 0.7640 1.0593 0.3436  -0.3694 -0.0858 645 MET D CB  
11037 C CG  . MET D 645 ? 1.2380 0.7659 1.0705 0.3481  -0.3609 -0.0985 645 MET D CG  
11038 S SD  . MET D 645 ? 1.1722 0.7205 1.0162 0.3224  -0.3343 -0.0928 645 MET D SD  
11039 C CE  . MET D 645 ? 1.1468 0.7295 1.0275 0.3368  -0.3261 -0.1165 645 MET D CE  
11040 N N   . LEU D 646 ? 1.2128 0.7701 1.0387 0.3738  -0.4020 -0.0937 646 LEU D N   
11041 C CA  . LEU D 646 ? 1.2358 0.7789 1.0390 0.3716  -0.4131 -0.0817 646 LEU D CA  
11042 C C   . LEU D 646 ? 1.1896 0.7436 0.9880 0.3458  -0.3959 -0.0664 646 LEU D C   
11043 O O   . LEU D 646 ? 1.2164 0.7389 0.9805 0.3353  -0.4017 -0.0493 646 LEU D O   
11044 C CB  . LEU D 646 ? 1.2393 0.8203 1.0700 0.3932  -0.4256 -0.0987 646 LEU D CB  
11045 C CG  . LEU D 646 ? 1.2859 0.8624 1.1263 0.4214  -0.4444 -0.1169 646 LEU D CG  
11046 C CD1 . LEU D 646 ? 1.2415 0.8791 1.1351 0.4321  -0.4344 -0.1420 646 LEU D CD1 
11047 C CD2 . LEU D 646 ? 1.3431 0.9018 1.1659 0.4389  -0.4699 -0.1170 646 LEU D CD2 
11048 N N   . ALA D 647 ? 1.1345 0.7316 0.9654 0.3355  -0.3751 -0.0724 647 ALA D N   
11049 C CA  . ALA D 647 ? 1.0896 0.7000 0.9193 0.3125  -0.3590 -0.0595 647 ALA D CA  
11050 C C   . ALA D 647 ? 1.0980 0.6664 0.8952 0.2909  -0.3513 -0.0413 647 ALA D C   
11051 O O   . ALA D 647 ? 1.0826 0.6465 0.8657 0.2721  -0.3437 -0.0270 647 ALA D O   
11052 C CB  . ALA D 647 ? 1.0217 0.6892 0.8953 0.3091  -0.3402 -0.0726 647 ALA D CB  
11053 N N   . LEU D 648 ? 1.1159 0.6549 0.9016 0.2929  -0.3530 -0.0425 648 LEU D N   
11054 C CA  . LEU D 648 ? 1.1186 0.6256 0.8805 0.2716  -0.3432 -0.0286 648 LEU D CA  
11055 C C   . LEU D 648 ? 1.1656 0.6238 0.8814 0.2593  -0.3521 -0.0097 648 LEU D C   
11056 O O   . LEU D 648 ? 1.2235 0.6503 0.9149 0.2717  -0.3706 -0.0080 648 LEU D O   
11057 C CB  . LEU D 648 ? 1.1408 0.6280 0.9013 0.2784  -0.3446 -0.0358 648 LEU D CB  
11058 C CG  . LEU D 648 ? 1.1175 0.5935 0.8734 0.2596  -0.3297 -0.0302 648 LEU D CG  
11059 C CD1 . LEU D 648 ? 1.1424 0.6025 0.8997 0.2712  -0.3336 -0.0403 648 LEU D CD1 
11060 C CD2 . LEU D 648 ? 1.1440 0.5790 0.8619 0.2369  -0.3281 -0.0107 648 LEU D CD2 
11061 N N   . THR D 649 ? 1.1344 0.5857 0.8373 0.2346  -0.3391 0.0040  649 THR D N   
11062 C CA  . THR D 649 ? 1.1779 0.5853 0.8366 0.2185  -0.3441 0.0219  649 THR D CA  
11063 C C   . THR D 649 ? 1.1910 0.5635 0.8246 0.1959  -0.3352 0.0329  649 THR D C   
11064 O O   . THR D 649 ? 1.2486 0.5716 0.8394 0.1864  -0.3431 0.0448  649 THR D O   
11065 C CB  . THR D 649 ? 1.1482 0.5801 0.8104 0.2076  -0.3380 0.0292  649 THR D CB  
11066 O OG1 . THR D 649 ? 1.0837 0.5508 0.7728 0.1931  -0.3185 0.0284  649 THR D OG1 
11067 C CG2 . THR D 649 ? 1.1409 0.6056 0.8250 0.2287  -0.3479 0.0188  649 THR D CG2 
11068 N N   . HIS D 650 ? 1.1541 0.5498 0.8118 0.1863  -0.3194 0.0288  650 HIS D N   
11069 C CA  . HIS D 650 ? 1.1630 0.5307 0.8009 0.1640  -0.3105 0.0378  650 HIS D CA  
11070 C C   . HIS D 650 ? 1.1521 0.5236 0.8074 0.1705  -0.3067 0.0272  650 HIS D C   
11071 O O   . HIS D 650 ? 1.1029 0.5165 0.7956 0.1801  -0.2993 0.0150  650 HIS D O   
11072 C CB  . HIS D 650 ? 1.1160 0.5064 0.7632 0.1414  -0.2942 0.0450  650 HIS D CB  
11073 C CG  . HIS D 650 ? 1.1308 0.5139 0.7567 0.1309  -0.2962 0.0567  650 HIS D CG  
11074 N ND1 . HIS D 650 ? 1.1252 0.5290 0.7597 0.1456  -0.3039 0.0539  650 HIS D ND1 
11075 C CD2 . HIS D 650 ? 1.1570 0.5146 0.7523 0.1061  -0.2909 0.0707  650 HIS D CD2 
11076 C CE1 . HIS D 650 ? 1.1424 0.5328 0.7514 0.1308  -0.3038 0.0662  650 HIS D CE1 
11077 N NE2 . HIS D 650 ? 1.1621 0.5242 0.7465 0.1063  -0.2955 0.0765  650 HIS D NE2 
11078 N N   . VAL D 651 ? 1.1792 0.5059 0.8055 0.1642  -0.3112 0.0318  651 VAL D N   
11079 C CA  . VAL D 651 ? 1.1754 0.4996 0.8126 0.1675  -0.3076 0.0233  651 VAL D CA  
11080 C C   . VAL D 651 ? 1.1899 0.4860 0.8052 0.1415  -0.2990 0.0332  651 VAL D C   
11081 O O   . VAL D 651 ? 1.2360 0.4941 0.8150 0.1263  -0.3023 0.0459  651 VAL D O   
11082 C CB  . VAL D 651 ? 1.2291 0.5247 0.8540 0.1891  -0.3237 0.0162  651 VAL D CB  
11083 C CG1 . VAL D 651 ? 1.2246 0.5237 0.8647 0.1935  -0.3187 0.0058  651 VAL D CG1 
11084 C CG2 . VAL D 651 ? 1.2273 0.5468 0.8701 0.2141  -0.3346 0.0066  651 VAL D CG2 
11085 N N   . ASP D 652 ? 1.1273 0.4421 0.7640 0.1357  -0.2877 0.0270  652 ASP D N   
11086 C CA  . ASP D 652 ? 1.1437 0.4317 0.7625 0.1138  -0.2811 0.0331  652 ASP D CA  
11087 C C   . ASP D 652 ? 1.1318 0.4274 0.7685 0.1218  -0.2782 0.0214  652 ASP D C   
11088 O O   . ASP D 652 ? 1.0780 0.4141 0.7474 0.1250  -0.2689 0.0129  652 ASP D O   
11089 C CB  . ASP D 652 ? 1.1054 0.4122 0.7311 0.0897  -0.2675 0.0404  652 ASP D CB  
11090 C CG  . ASP D 652 ? 1.1416 0.4112 0.7374 0.0636  -0.2634 0.0502  652 ASP D CG  
11091 O OD1 . ASP D 652 ? 1.1794 0.4181 0.7596 0.0632  -0.2672 0.0484  652 ASP D OD1 
11092 O OD2 . ASP D 652 ? 1.1340 0.4055 0.7221 0.0427  -0.2558 0.0591  652 ASP D OD2 
11093 N N   . VAL D 653 ? 1.1133 0.3683 0.7266 0.1249  -0.2863 0.0209  653 VAL D N   
11094 C CA  . VAL D 653 ? 1.1116 0.3667 0.7363 0.1312  -0.2842 0.0104  653 VAL D CA  
11095 C C   . VAL D 653 ? 1.1482 0.3641 0.7467 0.1104  -0.2817 0.0168  653 VAL D C   
11096 O O   . VAL D 653 ? 1.1694 0.3687 0.7651 0.1149  -0.2835 0.0101  653 VAL D O   
11097 C CB  . VAL D 653 ? 1.1407 0.3881 0.7679 0.1590  -0.2967 -0.0001 653 VAL D CB  
11098 C CG1 . VAL D 653 ? 1.1266 0.3861 0.7733 0.1675  -0.2922 -0.0135 653 VAL D CG1 
11099 C CG2 . VAL D 653 ? 1.1159 0.3968 0.7638 0.1775  -0.3010 -0.0051 653 VAL D CG2 
11100 N N   . SER D 654 ? 1.2103 0.4116 0.7896 0.0866  -0.2769 0.0291  654 SER D N   
11101 C CA  . SER D 654 ? 1.2486 0.4130 0.8021 0.0639  -0.2736 0.0352  654 SER D CA  
11102 C C   . SER D 654 ? 1.2131 0.3985 0.7897 0.0552  -0.2632 0.0272  654 SER D C   
11103 O O   . SER D 654 ? 1.1546 0.3843 0.7647 0.0610  -0.2564 0.0200  654 SER D O   
11104 C CB  . SER D 654 ? 1.2610 0.4126 0.7930 0.0386  -0.2682 0.0486  654 SER D CB  
11105 O OG  . SER D 654 ? 1.1987 0.3951 0.7590 0.0301  -0.2572 0.0486  654 SER D OG  
11106 N N   . HIS D 655 ? 1.2895 0.4405 0.8459 0.0406  -0.2623 0.0285  655 HIS D N   
11107 C CA  . HIS D 655 ? 1.2680 0.4321 0.8409 0.0289  -0.2535 0.0215  655 HIS D CA  
11108 C C   . HIS D 655 ? 1.2363 0.4279 0.8369 0.0511  -0.2543 0.0076  655 HIS D C   
11109 O O   . HIS D 655 ? 1.1795 0.4119 0.8092 0.0513  -0.2467 0.0016  655 HIS D O   
11110 C CB  . HIS D 655 ? 1.2223 0.4163 0.8116 0.0067  -0.2415 0.0251  655 HIS D CB  
11111 C CG  . HIS D 655 ? 1.2567 0.4245 0.8191 -0.0188 -0.2380 0.0371  655 HIS D CG  
11112 N ND1 . HIS D 655 ? 1.2958 0.4383 0.8423 -0.0435 -0.2326 0.0387  655 HIS D ND1 
11113 C CD2 . HIS D 655 ? 1.2657 0.4287 0.8134 -0.0245 -0.2383 0.0473  655 HIS D CD2 
11114 C CE1 . HIS D 655 ? 1.3210 0.4450 0.8441 -0.0642 -0.2286 0.0493  655 HIS D CE1 
11115 N NE2 . HIS D 655 ? 1.3048 0.4398 0.8269 -0.0530 -0.2323 0.0550  655 HIS D NE2 
11116 N N   . ASN D 656 ? 1.2816 0.4486 0.8710 0.0696  -0.2638 0.0024  656 ASN D N   
11117 C CA  . ASN D 656 ? 1.2599 0.4485 0.8719 0.0914  -0.2648 -0.0116 656 ASN D CA  
11118 C C   . ASN D 656 ? 1.3153 0.4633 0.9081 0.0972  -0.2715 -0.0169 656 ASN D C   
11119 O O   . ASN D 656 ? 1.3724 0.4798 0.9373 0.0813  -0.2735 -0.0101 656 ASN D O   
11120 C CB  . ASN D 656 ? 1.2408 0.4545 0.8684 0.1150  -0.2698 -0.0151 656 ASN D CB  
11121 C CG  . ASN D 656 ? 1.1740 0.4413 0.8357 0.1170  -0.2601 -0.0201 656 ASN D CG  
11122 O OD1 . ASN D 656 ? 1.1449 0.4356 0.8270 0.1252  -0.2550 -0.0315 656 ASN D OD1 
11123 N ND2 . ASN D 656 ? 1.1442 0.4293 0.8101 0.1091  -0.2571 -0.0116 656 ASN D ND2 
11124 N N   . ASN D 657 ? 1.3641 0.5231 0.9718 0.1192  -0.2743 -0.0297 657 ASN D N   
11125 C CA  . ASN D 657 ? 1.4201 0.5441 1.0135 0.1272  -0.2801 -0.0371 657 ASN D CA  
11126 C C   . ASN D 657 ? 1.4457 0.5628 1.0400 0.1559  -0.2914 -0.0441 657 ASN D C   
11127 O O   . ASN D 657 ? 1.4548 0.5707 1.0574 0.1716  -0.2930 -0.0571 657 ASN D O   
11128 C CB  . ASN D 657 ? 1.3886 0.5305 0.9992 0.1240  -0.2713 -0.0488 657 ASN D CB  
11129 C CG  . ASN D 657 ? 1.4438 0.5442 1.0351 0.1239  -0.2754 -0.0546 657 ASN D CG  
11130 O OD1 . ASN D 657 ? 1.5006 0.5577 1.0631 0.1118  -0.2803 -0.0463 657 ASN D OD1 
11131 N ND2 . ASN D 657 ? 1.4404 0.5528 1.0464 0.1366  -0.2728 -0.0691 657 ASN D ND2 
11132 N N   . LEU D 658 ? 1.4352 0.5478 1.0211 0.1632  -0.2996 -0.0365 658 LEU D N   
11133 C CA  . LEU D 658 ? 1.4551 0.5664 1.0453 0.1913  -0.3116 -0.0438 658 LEU D CA  
11134 C C   . LEU D 658 ? 1.5410 0.5934 1.0955 0.1975  -0.3262 -0.0403 658 LEU D C   
11135 O O   . LEU D 658 ? 1.5828 0.5942 1.1076 0.1787  -0.3263 -0.0313 658 LEU D O   
11136 C CB  . LEU D 658 ? 1.4248 0.5643 1.0259 0.1978  -0.3141 -0.0390 658 LEU D CB  
11137 C CG  . LEU D 658 ? 1.3520 0.5500 0.9888 0.1957  -0.3015 -0.0432 658 LEU D CG  
11138 C CD1 . LEU D 658 ? 1.3359 0.5541 0.9804 0.2065  -0.3073 -0.0403 658 LEU D CD1 
11139 C CD2 . LEU D 658 ? 1.3271 0.5554 0.9929 0.2099  -0.2952 -0.0602 658 LEU D CD2 
11140 N N   . GLN D 659 ? 1.4989 0.5466 1.0564 0.2244  -0.3391 -0.0481 659 GLN D N   
11141 C CA  . GLN D 659 ? 1.5792 0.5709 1.1035 0.2350  -0.3555 -0.0460 659 GLN D CA  
11142 C C   . GLN D 659 ? 1.5962 0.5942 1.1260 0.2619  -0.3706 -0.0504 659 GLN D C   
11143 O O   . GLN D 659 ? 1.5448 0.5928 1.1078 0.2733  -0.3672 -0.0577 659 GLN D O   
11144 C CB  . GLN D 659 ? 1.6108 0.5804 1.1338 0.2421  -0.3557 -0.0577 659 GLN D CB  
11145 C CG  . GLN D 659 ? 1.5806 0.5900 1.1414 0.2662  -0.3534 -0.0774 659 GLN D CG  
11146 C CD  . GLN D 659 ? 1.5965 0.5924 1.1593 0.2663  -0.3477 -0.0888 659 GLN D CD  
11147 O OE1 . GLN D 659 ? 1.5846 0.5740 1.1404 0.2435  -0.3369 -0.0847 659 GLN D OE1 
11148 N NE2 . GLN D 659 ? 1.6251 0.6172 1.1982 0.2920  -0.3553 -0.1043 659 GLN D NE2 
11149 N N   . GLY D 660 ? 1.6746 0.6201 1.1702 0.2715  -0.3881 -0.0459 660 GLY D N   
11150 C CA  . GLY D 660 ? 1.7028 0.6484 1.2019 0.3001  -0.4056 -0.0524 660 GLY D CA  
11151 C C   . GLY D 660 ? 1.7143 0.6523 1.1940 0.2966  -0.4144 -0.0391 660 GLY D C   
11152 O O   . GLY D 660 ? 1.6891 0.6307 1.1583 0.2718  -0.4045 -0.0254 660 GLY D O   
11153 N N   . PRO D 661 ? 1.7275 0.6544 1.2022 0.3220  -0.4337 -0.0437 661 PRO D N   
11154 C CA  . PRO D 661 ? 1.7436 0.6618 1.1985 0.3208  -0.4438 -0.0321 661 PRO D CA  
11155 C C   . PRO D 661 ? 1.6631 0.6457 1.1552 0.3177  -0.4323 -0.0341 661 PRO D C   
11156 O O   . PRO D 661 ? 1.6104 0.6454 1.1469 0.3312  -0.4256 -0.0495 661 PRO D O   
11157 C CB  . PRO D 661 ? 1.8089 0.7019 1.2540 0.3528  -0.4687 -0.0406 661 PRO D CB  
11158 C CG  . PRO D 661 ? 1.7905 0.7127 1.2740 0.3743  -0.4668 -0.0616 661 PRO D CG  
11159 C CD  . PRO D 661 ? 1.7653 0.6857 1.2515 0.3534  -0.4480 -0.0606 661 PRO D CD  
11160 N N   . ILE D 662 ? 1.6786 0.6555 1.1510 0.2991  -0.4297 -0.0186 662 ILE D N   
11161 C CA  . ILE D 662 ? 1.6065 0.6392 1.1093 0.2932  -0.4186 -0.0183 662 ILE D CA  
11162 C C   . ILE D 662 ? 1.6040 0.6654 1.1295 0.3214  -0.4321 -0.0297 662 ILE D C   
11163 O O   . ILE D 662 ? 1.6701 0.6964 1.1734 0.3403  -0.4531 -0.0311 662 ILE D O   
11164 C CB  . ILE D 662 ? 1.6079 0.6228 1.0809 0.2656  -0.4126 0.0011  662 ILE D CB  
11165 C CG1 . ILE D 662 ? 1.6943 0.6470 1.1151 0.2669  -0.4316 0.0129  662 ILE D CG1 
11166 C CG2 . ILE D 662 ? 1.5873 0.5948 1.0535 0.2365  -0.3946 0.0085  662 ILE D CG2 
11167 C CD1 . ILE D 662 ? 1.7077 0.6697 1.1289 0.2857  -0.4471 0.0117  662 ILE D CD1 
11168 N N   . PRO D 663 ? 1.5496 0.6737 1.1190 0.3255  -0.4214 -0.0389 663 PRO D N   
11169 C CA  . PRO D 663 ? 1.5458 0.7003 1.1376 0.3498  -0.4335 -0.0499 663 PRO D CA  
11170 C C   . PRO D 663 ? 1.5766 0.7094 1.1390 0.3462  -0.4452 -0.0364 663 PRO D C   
11171 O O   . PRO D 663 ? 1.5766 0.6888 1.1118 0.3215  -0.4379 -0.0193 663 PRO D O   
11172 C CB  . PRO D 663 ? 1.4590 0.6833 1.1004 0.3473  -0.4149 -0.0602 663 PRO D CB  
11173 C CG  . PRO D 663 ? 1.4278 0.6555 1.0761 0.3306  -0.3969 -0.0600 663 PRO D CG  
11174 C CD  . PRO D 663 ? 1.4733 0.6430 1.0755 0.3104  -0.3985 -0.0425 663 PRO D CD  
11175 N N   . ASP D 664 ? 1.5656 0.7032 1.1336 0.3715  -0.4639 -0.0453 664 ASP D N   
11176 C CA  . ASP D 664 ? 1.6068 0.7195 1.1444 0.3728  -0.4791 -0.0344 664 ASP D CA  
11177 C C   . ASP D 664 ? 1.5461 0.7174 1.1184 0.3746  -0.4727 -0.0391 664 ASP D C   
11178 O O   . ASP D 664 ? 1.5326 0.7424 1.1393 0.3980  -0.4801 -0.0563 664 ASP D O   
11179 C CB  . ASP D 664 ? 1.6894 0.7626 1.2056 0.4004  -0.5068 -0.0406 664 ASP D CB  
11180 C CG  . ASP D 664 ? 1.7401 0.7826 1.2206 0.4026  -0.5244 -0.0292 664 ASP D CG  
11181 O OD1 . ASP D 664 ? 1.7237 0.7611 1.1849 0.3784  -0.5145 -0.0131 664 ASP D OD1 
11182 O OD2 . ASP D 664 ? 1.7986 0.8220 1.2701 0.4288  -0.5485 -0.0369 664 ASP D OD2 
11183 N N   . ASN D 665 ? 1.6117 0.7904 1.1753 0.3495  -0.4588 -0.0246 665 ASN D N   
11184 C CA  . ASN D 665 ? 1.5649 0.7888 1.1515 0.3489  -0.4545 -0.0255 665 ASN D CA  
11185 C C   . ASN D 665 ? 1.5765 0.7714 1.1247 0.3245  -0.4513 -0.0044 665 ASN D C   
11186 O O   . ASN D 665 ? 1.6183 0.7619 1.1251 0.3076  -0.4510 0.0096  665 ASN D O   
11187 C CB  . ASN D 665 ? 1.4740 0.7640 1.1126 0.3445  -0.4330 -0.0368 665 ASN D CB  
11188 C CG  . ASN D 665 ? 1.4400 0.7275 1.0765 0.3188  -0.4120 -0.0284 665 ASN D CG  
11189 O OD1 . ASN D 665 ? 1.4611 0.7127 1.0628 0.2970  -0.4082 -0.0113 665 ASN D OD1 
11190 N ND2 . ASN D 665 ? 1.3936 0.7198 1.0674 0.3210  -0.3983 -0.0412 665 ASN D ND2 
11191 N N   . ALA D 666 ? 1.5473 0.7759 1.1093 0.3221  -0.4484 -0.0026 666 ALA D N   
11192 C CA  . ALA D 666 ? 1.5637 0.7679 1.0903 0.2999  -0.4455 0.0164  666 ALA D CA  
11193 C C   . ALA D 666 ? 1.5344 0.7331 1.0531 0.2691  -0.4239 0.0279  666 ALA D C   
11194 O O   . ALA D 666 ? 1.5690 0.7244 1.0445 0.2484  -0.4230 0.0443  666 ALA D O   
11195 C CB  . ALA D 666 ? 1.5234 0.7719 1.0724 0.3034  -0.4445 0.0143  666 ALA D CB  
11196 N N   . ALA D 667 ? 1.4635 0.7052 1.0225 0.2654  -0.4064 0.0189  667 ALA D N   
11197 C CA  . ALA D 667 ? 1.4272 0.6689 0.9830 0.2374  -0.3864 0.0283  667 ALA D CA  
11198 C C   . ALA D 667 ? 1.4767 0.6664 0.9998 0.2276  -0.3880 0.0343  667 ALA D C   
11199 O O   . ALA D 667 ? 1.4925 0.6525 0.9852 0.2023  -0.3804 0.0482  667 ALA D O   
11200 C CB  . ALA D 667 ? 1.3461 0.6469 0.9528 0.2376  -0.3689 0.0166  667 ALA D CB  
11201 N N   . PHE D 668 ? 1.4562 0.6349 0.9852 0.2468  -0.3973 0.0232  668 PHE D N   
11202 C CA  . PHE D 668 ? 1.5060 0.6344 1.0038 0.2388  -0.3996 0.0280  668 PHE D CA  
11203 C C   . PHE D 668 ? 1.5905 0.6543 1.0314 0.2329  -0.4146 0.0420  668 PHE D C   
11204 O O   . PHE D 668 ? 1.6272 0.6477 1.0335 0.2127  -0.4106 0.0525  668 PHE D O   
11205 C CB  . PHE D 668 ? 1.5162 0.6481 1.0339 0.2626  -0.4070 0.0120  668 PHE D CB  
11206 C CG  . PHE D 668 ? 1.4488 0.6255 1.0084 0.2599  -0.3894 0.0012  668 PHE D CG  
11207 C CD1 . PHE D 668 ? 1.4325 0.5998 0.9856 0.2367  -0.3744 0.0076  668 PHE D CD1 
11208 C CD2 . PHE D 668 ? 1.4052 0.6328 1.0095 0.2802  -0.3879 -0.0159 668 PHE D CD2 
11209 C CE1 . PHE D 668 ? 1.3751 0.5808 0.9639 0.2346  -0.3594 -0.0023 668 PHE D CE1 
11210 C CE2 . PHE D 668 ? 1.3485 0.6140 0.9872 0.2770  -0.3716 -0.0256 668 PHE D CE2 
11211 C CZ  . PHE D 668 ? 1.3339 0.5875 0.9641 0.2546  -0.3578 -0.0184 668 PHE D CZ  
11212 N N   . ARG D 669 ? 1.5822 0.6377 1.0113 0.2496  -0.4319 0.0420  669 ARG D N   
11213 C CA  . ARG D 669 ? 1.6674 0.6593 1.0386 0.2442  -0.4471 0.0557  669 ARG D CA  
11214 C C   . ARG D 669 ? 1.6651 0.6424 1.0076 0.2107  -0.4334 0.0729  669 ARG D C   
11215 O O   . ARG D 669 ? 1.7217 0.6450 1.0180 0.1913  -0.4333 0.0847  669 ARG D O   
11216 C CB  . ARG D 669 ? 1.6998 0.6922 1.0683 0.2698  -0.4684 0.0511  669 ARG D CB  
11217 C CG  . ARG D 669 ? 1.7411 0.7211 1.1165 0.3018  -0.4883 0.0370  669 ARG D CG  
11218 C CD  . ARG D 669 ? 1.7964 0.7595 1.1544 0.3243  -0.5132 0.0355  669 ARG D CD  
11219 N NE  . ARG D 669 ? 1.7375 0.7630 1.1389 0.3362  -0.5113 0.0259  669 ARG D NE  
11220 C CZ  . ARG D 669 ? 1.7229 0.7604 1.1167 0.3248  -0.5082 0.0352  669 ARG D CZ  
11221 N NH1 . ARG D 669 ? 1.7625 0.7549 1.1067 0.3008  -0.5063 0.0543  669 ARG D NH1 
11222 N NH2 . ARG D 669 ? 1.6692 0.7654 1.1055 0.3370  -0.5066 0.0247  669 ARG D NH2 
11223 N N   . ASN D 670 ? 1.6750 0.6998 1.0440 0.2028  -0.4214 0.0738  670 ASN D N   
11224 C CA  . ASN D 670 ? 1.6718 0.6888 1.0177 0.1718  -0.4079 0.0885  670 ASN D CA  
11225 C C   . ASN D 670 ? 1.6261 0.6587 0.9867 0.1470  -0.3855 0.0904  670 ASN D C   
11226 O O   . ASN D 670 ? 1.6127 0.6448 0.9595 0.1201  -0.3722 0.1009  670 ASN D O   
11227 C CB  . ASN D 670 ? 1.6247 0.6851 0.9919 0.1745  -0.4053 0.0886  670 ASN D CB  
11228 C CG  . ASN D 670 ? 1.6903 0.7160 1.0175 0.1807  -0.4234 0.0965  670 ASN D CG  
11229 O OD1 . ASN D 670 ? 1.6999 0.7391 1.0408 0.2076  -0.4396 0.0880  670 ASN D OD1 
11230 N ND2 . ASN D 670 ? 1.7396 0.7206 1.0165 0.1553  -0.4207 0.1122  670 ASN D ND2 
11231 N N   . ALA D 671 ? 1.5771 0.6241 0.9651 0.1551  -0.3812 0.0799  671 ALA D N   
11232 C CA  . ALA D 671 ? 1.5336 0.5964 0.9370 0.1330  -0.3614 0.0806  671 ALA D CA  
11233 C C   . ALA D 671 ? 1.5926 0.6002 0.9473 0.1056  -0.3579 0.0935  671 ALA D C   
11234 O O   . ALA D 671 ? 1.6716 0.6269 0.9896 0.1106  -0.3711 0.0963  671 ALA D O   
11235 C CB  . ALA D 671 ? 1.5014 0.5874 0.9407 0.1488  -0.3593 0.0662  671 ALA D CB  
11236 N N   . PRO D 672 ? 1.5395 0.5562 0.8921 0.0763  -0.3403 0.1009  672 PRO D N   
11237 C CA  . PRO D 672 ? 1.5946 0.5625 0.9030 0.0473  -0.3345 0.1118  672 PRO D CA  
11238 C C   . PRO D 672 ? 1.6068 0.5579 0.9179 0.0463  -0.3325 0.1063  672 PRO D C   
11239 O O   . PRO D 672 ? 1.5590 0.5443 0.9110 0.0635  -0.3312 0.0942  672 PRO D O   
11240 C CB  . PRO D 672 ? 1.5479 0.5455 0.8671 0.0189  -0.3145 0.1173  672 PRO D CB  
11241 C CG  . PRO D 672 ? 1.4604 0.5228 0.8369 0.0339  -0.3083 0.1070  672 PRO D CG  
11242 C CD  . PRO D 672 ? 1.4616 0.5340 0.8515 0.0679  -0.3251 0.0994  672 PRO D CD  
11243 N N   . PRO D 673 ? 1.6183 0.5160 0.8850 0.0256  -0.3316 0.1144  673 PRO D N   
11244 C CA  . PRO D 673 ? 1.6370 0.5144 0.9034 0.0249  -0.3309 0.1091  673 PRO D CA  
11245 C C   . PRO D 673 ? 1.5652 0.4881 0.8756 0.0153  -0.3138 0.1014  673 PRO D C   
11246 O O   . PRO D 673 ? 1.5604 0.4834 0.8863 0.0251  -0.3150 0.0926  673 PRO D O   
11247 C CB  . PRO D 673 ? 1.7206 0.5347 0.9287 -0.0019 -0.3300 0.1209  673 PRO D CB  
11248 C CG  . PRO D 673 ? 1.7640 0.5540 0.9358 -0.0027 -0.3390 0.1308  673 PRO D CG  
11249 C CD  . PRO D 673 ? 1.6871 0.5369 0.8986 0.0030  -0.3325 0.1282  673 PRO D CD  
11250 N N   . ASP D 674 ? 1.6331 0.5936 0.9633 -0.0035 -0.2983 0.1039  674 ASP D N   
11251 C CA  . ASP D 674 ? 1.5695 0.5712 0.9400 -0.0127 -0.2833 0.0964  674 ASP D CA  
11252 C C   . ASP D 674 ? 1.4995 0.5509 0.9191 0.0150  -0.2857 0.0839  674 ASP D C   
11253 O O   . ASP D 674 ? 1.4597 0.5393 0.9105 0.0127  -0.2767 0.0760  674 ASP D O   
11254 C CB  . ASP D 674 ? 1.5301 0.5559 0.9068 -0.0413 -0.2665 0.1022  674 ASP D CB  
11255 C CG  . ASP D 674 ? 1.5222 0.5597 0.8925 -0.0389 -0.2687 0.1087  674 ASP D CG  
11256 O OD1 . ASP D 674 ? 1.5141 0.5614 0.8937 -0.0113 -0.2815 0.1054  674 ASP D OD1 
11257 O OD2 . ASP D 674 ? 1.5248 0.5634 0.8817 -0.0652 -0.2571 0.1162  674 ASP D OD2 
11258 N N   . ALA D 675 ? 1.4303 0.4933 0.8571 0.0401  -0.2973 0.0814  675 ALA D N   
11259 C CA  . ALA D 675 ? 1.3720 0.4822 0.8441 0.0656  -0.2986 0.0685  675 ALA D CA  
11260 C C   . ALA D 675 ? 1.3903 0.4894 0.8695 0.0841  -0.3058 0.0579  675 ALA D C   
11261 O O   . ALA D 675 ? 1.3470 0.4828 0.8615 0.1053  -0.3067 0.0459  675 ALA D O   
11262 C CB  . ALA D 675 ? 1.3650 0.4916 0.8430 0.0855  -0.3084 0.0680  675 ALA D CB  
11263 N N   . PHE D 676 ? 1.3518 0.4014 0.7979 0.0757  -0.3101 0.0615  676 PHE D N   
11264 C CA  . PHE D 676 ? 1.3730 0.4077 0.8229 0.0914  -0.3165 0.0517  676 PHE D CA  
11265 C C   . PHE D 676 ? 1.3929 0.4030 0.8296 0.0692  -0.3080 0.0533  676 PHE D C   
11266 O O   . PHE D 676 ? 1.4287 0.4121 0.8567 0.0778  -0.3141 0.0477  676 PHE D O   
11267 C CB  . PHE D 676 ? 1.4438 0.4346 0.8632 0.1113  -0.3359 0.0525  676 PHE D CB  
11268 C CG  . PHE D 676 ? 1.4319 0.4445 0.8632 0.1339  -0.3463 0.0498  676 PHE D CG  
11269 C CD1 . PHE D 676 ? 1.3922 0.4451 0.8627 0.1603  -0.3494 0.0353  676 PHE D CD1 
11270 C CD2 . PHE D 676 ? 1.4635 0.4559 0.8656 0.1280  -0.3528 0.0612  676 PHE D CD2 
11271 C CE1 . PHE D 676 ? 1.3826 0.4573 0.8657 0.1804  -0.3588 0.0317  676 PHE D CE1 
11272 C CE2 . PHE D 676 ? 1.4544 0.4670 0.8678 0.1488  -0.3630 0.0581  676 PHE D CE2 
11273 C CZ  . PHE D 676 ? 1.4132 0.4680 0.8683 0.1751  -0.3661 0.0431  676 PHE D CZ  
11274 N N   . GLU D 677 ? 1.4408 0.4598 0.8768 0.0409  -0.2941 0.0600  677 GLU D N   
11275 C CA  . GLU D 677 ? 1.4655 0.4598 0.8867 0.0163  -0.2857 0.0619  677 GLU D CA  
11276 C C   . GLU D 677 ? 1.4327 0.4485 0.8843 0.0236  -0.2815 0.0491  677 GLU D C   
11277 O O   . GLU D 677 ? 1.3773 0.4363 0.8655 0.0418  -0.2804 0.0395  677 GLU D O   
11278 C CB  . GLU D 677 ? 1.4420 0.4515 0.8640 -0.0147 -0.2707 0.0693  677 GLU D CB  
11279 C CG  . GLU D 677 ? 1.5023 0.4698 0.8787 -0.0357 -0.2711 0.0828  677 GLU D CG  
11280 C CD  . GLU D 677 ? 1.4774 0.4646 0.8586 -0.0676 -0.2541 0.0879  677 GLU D CD  
11281 O OE1 . GLU D 677 ? 1.4220 0.4482 0.8394 -0.0750 -0.2432 0.0806  677 GLU D OE1 
11282 O OE2 . GLU D 677 ? 1.5154 0.4790 0.8638 -0.0854 -0.2518 0.0983  677 GLU D OE2 
11283 N N   . GLY D 678 ? 1.4905 0.4741 0.9246 0.0082  -0.2788 0.0487  678 GLY D N   
11284 C CA  . GLY D 678 ? 1.4626 0.4641 0.9216 0.0071  -0.2724 0.0377  678 GLY D CA  
11285 C C   . GLY D 678 ? 1.4416 0.4616 0.9244 0.0371  -0.2790 0.0249  678 GLY D C   
11286 O O   . GLY D 678 ? 1.3861 0.4469 0.9027 0.0407  -0.2717 0.0156  678 GLY D O   
11287 N N   . ASN D 679 ? 1.4771 0.4675 0.9422 0.0584  -0.2926 0.0236  679 ASN D N   
11288 C CA  . ASN D 679 ? 1.4680 0.4710 0.9533 0.0861  -0.2987 0.0101  679 ASN D CA  
11289 C C   . ASN D 679 ? 1.5315 0.4862 0.9926 0.0875  -0.3049 0.0065  679 ASN D C   
11290 O O   . ASN D 679 ? 1.5808 0.4934 1.0101 0.0666  -0.3042 0.0146  679 ASN D O   
11291 C CB  . ASN D 679 ? 1.4668 0.4809 0.9578 0.1126  -0.3098 0.0086  679 ASN D CB  
11292 C CG  . ASN D 679 ? 1.3926 0.4649 0.9191 0.1168  -0.3023 0.0064  679 ASN D CG  
11293 O OD1 . ASN D 679 ? 1.3551 0.4632 0.9124 0.1365  -0.3017 -0.0054 679 ASN D OD1 
11294 N ND2 . ASN D 679 ? 1.3736 0.4549 0.8953 0.0975  -0.2958 0.0173  679 ASN D ND2 
11295 N N   . LYS D 680 ? 1.5689 0.5293 1.0451 0.1115  -0.3103 -0.0065 680 LYS D N   
11296 C CA  . LYS D 680 ? 1.6273 0.5451 1.0844 0.1129  -0.3149 -0.0119 680 LYS D CA  
11297 C C   . LYS D 680 ? 1.7112 0.5730 1.1302 0.1235  -0.3309 -0.0060 680 LYS D C   
11298 O O   . LYS D 680 ? 1.7686 0.5805 1.1513 0.1059  -0.3327 0.0021  680 LYS D O   
11299 C CB  . LYS D 680 ? 1.5979 0.5423 1.0851 0.1332  -0.3133 -0.0291 680 LYS D CB  
11300 C CG  . LYS D 680 ? 1.6587 0.5621 1.1296 0.1362  -0.3172 -0.0369 680 LYS D CG  
11301 C CD  . LYS D 680 ? 1.6970 0.5643 1.1412 0.1059  -0.3119 -0.0290 680 LYS D CD  
11302 C CE  . LYS D 680 ? 1.6431 0.5418 1.1106 0.0893  -0.2979 -0.0361 680 LYS D CE  
11303 N NZ  . LYS D 680 ? 1.6442 0.5324 1.0978 0.0559  -0.2897 -0.0261 680 LYS D NZ  
11304 N N   . ASP D 681 ? 1.6892 0.5574 1.1149 0.1518  -0.3430 -0.0106 681 ASP D N   
11305 C CA  . ASP D 681 ? 1.7665 0.5823 1.1552 0.1637  -0.3605 -0.0047 681 ASP D CA  
11306 C C   . ASP D 681 ? 1.7480 0.5904 1.1512 0.1871  -0.3703 -0.0062 681 ASP D C   
11307 O O   . ASP D 681 ? 1.7416 0.6024 1.1677 0.2149  -0.3775 -0.0195 681 ASP D O   
11308 C CB  . ASP D 681 ? 1.8236 0.6010 1.2006 0.1789  -0.3695 -0.0144 681 ASP D CB  
11309 C CG  . ASP D 681 ? 1.9125 0.6284 1.2464 0.1897  -0.3885 -0.0077 681 ASP D CG  
11310 O OD1 . ASP D 681 ? 1.9566 0.6318 1.2509 0.1685  -0.3899 0.0072  681 ASP D OD1 
11311 O OD2 . ASP D 681 ? 1.9412 0.6489 1.2801 0.2191  -0.4023 -0.0180 681 ASP D OD2 
11312 N N   . LEU D 682 ? 1.7773 0.6190 1.1655 0.1759  -0.3711 0.0068  682 LEU D N   
11313 C CA  . LEU D 682 ? 1.7598 0.6238 1.1587 0.1962  -0.3811 0.0060  682 LEU D CA  
11314 C C   . LEU D 682 ? 1.8468 0.6536 1.2039 0.2095  -0.4021 0.0116  682 LEU D C   
11315 O O   . LEU D 682 ? 1.9228 0.6736 1.2446 0.2051  -0.4088 0.0150  682 LEU D O   
11316 C CB  . LEU D 682 ? 1.7070 0.6057 1.1156 0.1784  -0.3704 0.0155  682 LEU D CB  
11317 C CG  . LEU D 682 ? 1.6221 0.5917 1.0823 0.1869  -0.3596 0.0054  682 LEU D CG  
11318 C CD1 . LEU D 682 ? 1.5894 0.5830 1.0775 0.1855  -0.3478 -0.0063 682 LEU D CD1 
11319 C CD2 . LEU D 682 ? 1.5707 0.5684 1.0368 0.1666  -0.3485 0.0157  682 LEU D CD2 
11320 N N   . CYS D 683 ? 1.8236 0.6432 1.1836 0.2260  -0.4133 0.0124  683 CYS D N   
11321 C CA  . CYS D 683 ? 1.9054 0.6738 1.2264 0.2408  -0.4353 0.0174  683 CYS D CA  
11322 C C   . CYS D 683 ? 1.9634 0.6980 1.2772 0.2647  -0.4498 0.0065  683 CYS D C   
11323 O O   . CYS D 683 ? 1.9332 0.7038 1.2857 0.2886  -0.4515 -0.0101 683 CYS D O   
11324 C CB  . CYS D 683 ? 1.9629 0.6759 1.2292 0.2133  -0.4357 0.0365  683 CYS D CB  
11325 S SG  . CYS D 683 ? 1.8972 0.6451 1.1709 0.1774  -0.4131 0.0486  683 CYS D SG  
11326 N N   . ASN E 26  ? 0.4042 0.5847 0.3853 0.1082  -0.1110 -0.1620 26  ASN E N   
11327 C CA  . ASN E 26  ? 0.4167 0.5885 0.3850 0.1241  -0.1132 -0.1636 26  ASN E CA  
11328 C C   . ASN E 26  ? 0.4185 0.5807 0.3989 0.1243  -0.1176 -0.1729 26  ASN E C   
11329 O O   . ASN E 26  ? 0.4130 0.5755 0.4116 0.1144  -0.1203 -0.1785 26  ASN E O   
11330 C CB  . ASN E 26  ? 0.4144 0.5975 0.3685 0.1223  -0.1060 -0.1532 26  ASN E CB  
11331 C CG  . ASN E 26  ? 0.4034 0.5899 0.3653 0.1038  -0.1017 -0.1522 26  ASN E CG  
11332 O OD1 . ASN E 26  ? 0.3938 0.5807 0.3716 0.0924  -0.1011 -0.1567 26  ASN E OD1 
11333 N ND2 . ASN E 26  ? 0.4088 0.5968 0.3571 0.1018  -0.0996 -0.1458 26  ASN E ND2 
11334 N N   . ALA E 27  ? 0.4082 0.5647 0.3779 0.1363  -0.1183 -0.1735 27  ALA E N   
11335 C CA  . ALA E 27  ? 0.4116 0.5615 0.3909 0.1398  -0.1227 -0.1817 27  ALA E CA  
11336 C C   . ALA E 27  ? 0.3986 0.5563 0.3910 0.1234  -0.1180 -0.1825 27  ALA E C   
11337 O O   . ALA E 27  ? 0.3961 0.5569 0.4057 0.1199  -0.1216 -0.1896 27  ALA E O   
11338 C CB  . ALA E 27  ? 0.4244 0.5680 0.3870 0.1559  -0.1235 -0.1802 27  ALA E CB  
11339 N N   . GLU E 28  ? 0.4485 0.6100 0.4316 0.1140  -0.1109 -0.1753 28  GLU E N   
11340 C CA  . GLU E 28  ? 0.4412 0.6075 0.4319 0.1020  -0.1071 -0.1764 28  GLU E CA  
11341 C C   . GLU E 28  ? 0.4285 0.6073 0.4379 0.0903  -0.1058 -0.1779 28  GLU E C   
11342 O O   . GLU E 28  ? 0.4247 0.6116 0.4470 0.0869  -0.1058 -0.1831 28  GLU E O   
11343 C CB  . GLU E 28  ? 0.4443 0.6073 0.4180 0.0935  -0.1024 -0.1686 28  GLU E CB  
11344 C CG  . GLU E 28  ? 0.4611 0.6108 0.4143 0.1027  -0.1044 -0.1666 28  GLU E CG  
11345 C CD  . GLU E 28  ? 0.4705 0.6124 0.4065 0.0912  -0.1029 -0.1608 28  GLU E CD  
11346 O OE1 . GLU E 28  ? 0.4627 0.6130 0.4008 0.0769  -0.1002 -0.1556 28  GLU E OE1 
11347 O OE2 . GLU E 28  ? 0.4886 0.6144 0.4079 0.0964  -0.1055 -0.1616 28  GLU E OE2 
11348 N N   . GLY E 29  ? 0.4003 0.5831 0.4103 0.0856  -0.1049 -0.1733 29  GLY E N   
11349 C CA  . GLY E 29  ? 0.3906 0.5845 0.4169 0.0744  -0.1042 -0.1736 29  GLY E CA  
11350 C C   . GLY E 29  ? 0.3947 0.5883 0.4389 0.0761  -0.1121 -0.1815 29  GLY E C   
11351 O O   . GLY E 29  ? 0.3882 0.5951 0.4502 0.0664  -0.1120 -0.1831 29  GLY E O   
11352 N N   . ASP E 30  ? 0.3887 0.5685 0.4286 0.0883  -0.1202 -0.1861 30  ASP E N   
11353 C CA  . ASP E 30  ? 0.3977 0.5746 0.4541 0.0886  -0.1305 -0.1938 30  ASP E CA  
11354 C C   . ASP E 30  ? 0.3955 0.5834 0.4636 0.0886  -0.1303 -0.1993 30  ASP E C   
11355 O O   . ASP E 30  ? 0.3959 0.5951 0.4851 0.0803  -0.1355 -0.2025 30  ASP E O   
11356 C CB  . ASP E 30  ? 0.4168 0.5740 0.4621 0.1042  -0.1403 -0.1983 30  ASP E CB  
11357 C CG  . ASP E 30  ? 0.4248 0.5716 0.4605 0.1063  -0.1442 -0.1954 30  ASP E CG  
11358 O OD1 . ASP E 30  ? 0.4277 0.5736 0.4763 0.0953  -0.1503 -0.1960 30  ASP E OD1 
11359 O OD2 . ASP E 30  ? 0.4303 0.5711 0.4451 0.1199  -0.1418 -0.1921 30  ASP E OD2 
11360 N N   . ALA E 31  ? 0.3908 0.5769 0.4456 0.0979  -0.1254 -0.1997 31  ALA E N   
11361 C CA  . ALA E 31  ? 0.3912 0.5881 0.4531 0.1016  -0.1255 -0.2059 31  ALA E CA  
11362 C C   . ALA E 31  ? 0.3798 0.5986 0.4549 0.0897  -0.1203 -0.2049 31  ALA E C   
11363 O O   . ALA E 31  ? 0.3798 0.6168 0.4736 0.0875  -0.1240 -0.2099 31  ALA E O   
11364 C CB  . ALA E 31  ? 0.3965 0.5838 0.4383 0.1135  -0.1220 -0.2046 31  ALA E CB  
11365 N N   . LEU E 32  ? 0.3669 0.5870 0.4328 0.0825  -0.1122 -0.1980 32  LEU E N   
11366 C CA  . LEU E 32  ? 0.3577 0.5997 0.4340 0.0736  -0.1072 -0.1971 32  LEU E CA  
11367 C C   . LEU E 32  ? 0.3513 0.6099 0.4531 0.0614  -0.1103 -0.1946 32  LEU E C   
11368 O O   . LEU E 32  ? 0.3454 0.6306 0.4649 0.0561  -0.1086 -0.1940 32  LEU E O   
11369 C CB  . LEU E 32  ? 0.3537 0.5903 0.4129 0.0683  -0.0994 -0.1901 32  LEU E CB  
11370 C CG  . LEU E 32  ? 0.3645 0.5845 0.4000 0.0758  -0.0974 -0.1896 32  LEU E CG  
11371 C CD1 . LEU E 32  ? 0.3645 0.5782 0.3850 0.0665  -0.0920 -0.1819 32  LEU E CD1 
11372 C CD2 . LEU E 32  ? 0.3718 0.6012 0.4080 0.0861  -0.0990 -0.1978 32  LEU E CD2 
11373 N N   . SER E 33  ? 0.3527 0.5967 0.4565 0.0575  -0.1156 -0.1917 33  SER E N   
11374 C CA  . SER E 33  ? 0.3522 0.6063 0.4806 0.0449  -0.1214 -0.1880 33  SER E CA  
11375 C C   . SER E 33  ? 0.3603 0.6253 0.5112 0.0434  -0.1306 -0.1918 33  SER E C   
11376 O O   . SER E 33  ? 0.3579 0.6440 0.5366 0.0304  -0.1332 -0.1856 33  SER E O   
11377 C CB  . SER E 33  ? 0.3603 0.5918 0.4805 0.0443  -0.1274 -0.1860 33  SER E CB  
11378 O OG  . SER E 33  ? 0.3519 0.5813 0.4562 0.0434  -0.1190 -0.1803 33  SER E OG  
11379 N N   . ALA E 34  ? 0.3718 0.6253 0.5131 0.0561  -0.1355 -0.2001 34  ALA E N   
11380 C CA  . ALA E 34  ? 0.3805 0.6477 0.5427 0.0553  -0.1445 -0.2038 34  ALA E CA  
11381 C C   . ALA E 34  ? 0.3703 0.6747 0.5494 0.0527  -0.1380 -0.2013 34  ALA E C   
11382 O O   . ALA E 34  ? 0.3718 0.7016 0.5812 0.0422  -0.1429 -0.1954 34  ALA E O   
11383 C CB  . ALA E 34  ? 0.3935 0.6425 0.5389 0.0726  -0.1497 -0.2139 34  ALA E CB  
11384 N N   . LEU E 35  ? 0.3591 0.6683 0.5190 0.0628  -0.1276 -0.2045 35  LEU E N   
11385 C CA  . LEU E 35  ? 0.3525 0.6977 0.5231 0.0650  -0.1212 -0.2031 35  LEU E CA  
11386 C C   . LEU E 35  ? 0.3414 0.7119 0.5354 0.0496  -0.1157 -0.1901 35  LEU E C   
11387 O O   . LEU E 35  ? 0.3389 0.7464 0.5580 0.0466  -0.1131 -0.1828 35  LEU E O   
11388 C CB  . LEU E 35  ? 0.3530 0.6908 0.4924 0.0804  -0.1143 -0.2105 35  LEU E CB  
11389 C CG  . LEU E 35  ? 0.3522 0.7221 0.4902 0.0906  -0.1087 -0.2127 35  LEU E CG  
11390 C CD1 . LEU E 35  ? 0.3645 0.7141 0.4680 0.1096  -0.1087 -0.2233 35  LEU E CD1 
11391 C CD2 . LEU E 35  ? 0.3414 0.7286 0.4835 0.0824  -0.1005 -0.2044 35  LEU E CD2 
11392 N N   . LYS E 36  ? 0.3256 0.6791 0.5122 0.0410  -0.1128 -0.1854 36  LYS E N   
11393 C CA  . LYS E 36  ? 0.3160 0.6917 0.5234 0.0274  -0.1070 -0.1727 36  LYS E CA  
11394 C C   . LYS E 36  ? 0.3204 0.7137 0.5660 0.0126  -0.1143 -0.1622 36  LYS E C   
11395 O O   . LYS E 36  ? 0.3143 0.7405 0.5856 0.0037  -0.1078 -0.1489 36  LYS E O   
11396 C CB  . LYS E 36  ? 0.3119 0.6635 0.5029 0.0219  -0.1047 -0.1705 36  LYS E CB  
11397 C CG  . LYS E 36  ? 0.3034 0.6748 0.5147 0.0084  -0.0991 -0.1576 36  LYS E CG  
11398 C CD  . LYS E 36  ? 0.3012 0.6492 0.4942 0.0053  -0.0980 -0.1568 36  LYS E CD  
11399 C CE  . LYS E 36  ? 0.3034 0.6525 0.5193 -0.0088 -0.1031 -0.1478 36  LYS E CE  
11400 N NZ  . LYS E 36  ? 0.2923 0.6605 0.5119 -0.0147 -0.0920 -0.1381 36  LYS E NZ  
11401 N N   . ASN E 37  ? 0.3815 0.7538 0.6314 0.0100  -0.1282 -0.1668 37  ASN E N   
11402 C CA  . ASN E 37  ? 0.3910 0.7764 0.6771 -0.0065 -0.1393 -0.1569 37  ASN E CA  
11403 C C   . ASN E 37  ? 0.3942 0.8152 0.7047 -0.0054 -0.1409 -0.1530 37  ASN E C   
11404 O O   . ASN E 37  ? 0.3992 0.8458 0.7472 -0.0216 -0.1464 -0.1386 37  ASN E O   
11405 C CB  . ASN E 37  ? 0.4099 0.7556 0.6873 -0.0093 -0.1560 -0.1641 37  ASN E CB  
11406 C CG  . ASN E 37  ? 0.4104 0.7258 0.6688 -0.0110 -0.1559 -0.1651 37  ASN E CG  
11407 O OD1 . ASN E 37  ? 0.4152 0.7302 0.6916 -0.0261 -0.1612 -0.1566 37  ASN E OD1 
11408 N ND2 . ASN E 37  ? 0.4072 0.6984 0.6299 0.0048  -0.1503 -0.1745 37  ASN E ND2 
11409 N N   . SER E 38  ? 0.4159 0.8405 0.7069 0.0132  -0.1368 -0.1641 38  SER E N   
11410 C CA  . SER E 38  ? 0.4203 0.8808 0.7313 0.0179  -0.1378 -0.1612 38  SER E CA  
11411 C C   . SER E 38  ? 0.4101 0.9136 0.7287 0.0248  -0.1219 -0.1520 38  SER E C   
11412 O O   . SER E 38  ? 0.4148 0.9542 0.7505 0.0306  -0.1206 -0.1468 38  SER E O   
11413 C CB  . SER E 38  ? 0.4292 0.8713 0.7136 0.0371  -0.1427 -0.1789 38  SER E CB  
11414 O OG  . SER E 38  ? 0.4294 0.9066 0.7162 0.0511  -0.1363 -0.1797 38  SER E OG  
11415 N N   . LEU E 39  ? 0.3702 0.8719 0.6745 0.0261  -0.1099 -0.1495 39  LEU E N   
11416 C CA  . LEU E 39  ? 0.3648 0.9044 0.6708 0.0350  -0.0944 -0.1405 39  LEU E CA  
11417 C C   . LEU E 39  ? 0.3587 0.9194 0.6937 0.0176  -0.0873 -0.1200 39  LEU E C   
11418 O O   . LEU E 39  ? 0.3541 0.8901 0.6884 0.0045  -0.0901 -0.1186 39  LEU E O   
11419 C CB  . LEU E 39  ? 0.3612 0.8840 0.6241 0.0533  -0.0865 -0.1543 39  LEU E CB  
11420 C CG  . LEU E 39  ? 0.3706 0.8938 0.6055 0.0777  -0.0870 -0.1693 39  LEU E CG  
11421 C CD1 . LEU E 39  ? 0.3790 0.8826 0.6131 0.0797  -0.0998 -0.1801 39  LEU E CD1 
11422 C CD2 . LEU E 39  ? 0.3702 0.8694 0.5646 0.0913  -0.0840 -0.1823 39  LEU E CD2 
11423 N N   . ALA E 40  ? 0.3331 0.9395 0.6921 0.0192  -0.0776 -0.1032 40  ALA E N   
11424 C CA  . ALA E 40  ? 0.3296 0.9590 0.7109 0.0075  -0.0666 -0.0824 40  ALA E CA  
11425 C C   . ALA E 40  ? 0.3247 0.9544 0.6709 0.0239  -0.0511 -0.0858 40  ALA E C   
11426 O O   . ALA E 40  ? 0.3303 0.9719 0.6508 0.0465  -0.0445 -0.0933 40  ALA E O   
11427 C CB  . ALA E 40  ? 0.3387 1.0171 0.7599 0.0035  -0.0616 -0.0611 40  ALA E CB  
11428 N N   . ASP E 41  ? 0.3428 0.9589 0.6863 0.0135  -0.0467 -0.0806 41  ASP E N   
11429 C CA  . ASP E 41  ? 0.3390 0.9488 0.6476 0.0267  -0.0355 -0.0857 41  ASP E CA  
11430 C C   . ASP E 41  ? 0.3406 0.9775 0.6649 0.0215  -0.0210 -0.0632 41  ASP E C   
11431 O O   . ASP E 41  ? 0.3346 0.9583 0.6645 0.0074  -0.0200 -0.0568 41  ASP E O   
11432 C CB  . ASP E 41  ? 0.3305 0.8965 0.6153 0.0215  -0.0434 -0.1014 41  ASP E CB  
11433 C CG  . ASP E 41  ? 0.3283 0.8875 0.5765 0.0357  -0.0356 -0.1099 41  ASP E CG  
11434 O OD1 . ASP E 41  ? 0.3347 0.9205 0.5744 0.0498  -0.0238 -0.1031 41  ASP E OD1 
11435 O OD2 . ASP E 41  ? 0.3233 0.8497 0.5500 0.0334  -0.0422 -0.1227 41  ASP E OD2 
11436 N N   . PRO E 42  ? 0.3023 0.8878 0.7272 -0.0065 0.0975  -0.1440 42  PRO E N   
11437 C CA  . PRO E 42  ? 0.3208 0.9193 0.7471 -0.0093 0.1283  -0.1266 42  PRO E CA  
11438 C C   . PRO E 42  ? 0.3215 0.8906 0.7025 0.0095  0.1342  -0.1257 42  PRO E C   
11439 O O   . PRO E 42  ? 0.3358 0.8982 0.7080 0.0029  0.1577  -0.1122 42  PRO E O   
11440 C CB  . PRO E 42  ? 0.3410 0.9877 0.7891 0.0049  0.1401  -0.1231 42  PRO E CB  
11441 C CG  . PRO E 42  ? 0.3324 0.9806 0.7680 0.0277  0.1136  -0.1417 42  PRO E CG  
11442 C CD  . PRO E 42  ? 0.3099 0.9267 0.7432 0.0136  0.0882  -0.1534 42  PRO E CD  
11443 N N   . ASN E 43  ? 0.3471 0.8957 0.6968 0.0331  0.1130  -0.1396 43  ASN E N   
11444 C CA  . ASN E 43  ? 0.3736 0.8921 0.6793 0.0534  0.1134  -0.1408 43  ASN E CA  
11445 C C   . ASN E 43  ? 0.3771 0.8562 0.6693 0.0414  0.1015  -0.1463 43  ASN E C   
11446 O O   . ASN E 43  ? 0.3892 0.8406 0.6464 0.0581  0.0972  -0.1498 43  ASN E O   
11447 C CB  . ASN E 43  ? 0.3617 0.8754 0.6389 0.0858  0.0957  -0.1523 43  ASN E CB  
11448 C CG  . ASN E 43  ? 0.3885 0.9336 0.6642 0.1057  0.1114  -0.1456 43  ASN E CG  
11449 O OD1 . ASN E 43  ? 0.3949 0.9596 0.6756 0.1193  0.1004  -0.1535 43  ASN E OD1 
11450 N ND2 . ASN E 43  ? 0.4107 0.9593 0.6768 0.1086  0.1381  -0.1311 43  ASN E ND2 
11451 N N   . LYS E 44  ? 0.3518 0.8257 0.6696 0.0143  0.0947  -0.1474 44  LYS E N   
11452 C CA  . LYS E 44  ? 0.3493 0.7869 0.6572 0.0015  0.0849  -0.1516 44  LYS E CA  
11453 C C   . LYS E 44  ? 0.3333 0.7452 0.6150 0.0204  0.0618  -0.1650 44  LYS E C   
11454 O O   . LYS E 44  ? 0.3485 0.7217 0.6028 0.0216  0.0560  -0.1638 44  LYS E O   
11455 C CB  . LYS E 44  ? 0.3968 0.8120 0.6854 -0.0055 0.1042  -0.1388 44  LYS E CB  
11456 C CG  . LYS E 44  ? 0.4167 0.8475 0.7316 -0.0318 0.1274  -0.1250 44  LYS E CG  
11457 C CD  . LYS E 44  ? 0.3745 0.8296 0.7314 -0.0514 0.1187  -0.1276 44  LYS E CD  
11458 C CE  . LYS E 44  ? 0.3847 0.8244 0.7588 -0.0840 0.1257  -0.1188 44  LYS E CE  
11459 N NZ  . LYS E 44  ? 0.3276 0.7713 0.7279 -0.0979 0.1058  -0.1240 44  LYS E NZ  
11460 N N   . VAL E 45  ? 0.3056 0.7259 0.5861 0.0342  0.0461  -0.1738 45  VAL E N   
11461 C CA  . VAL E 45  ? 0.3004 0.6938 0.5567 0.0499  0.0241  -0.1861 45  VAL E CA  
11462 C C   . VAL E 45  ? 0.2824 0.6492 0.5433 0.0324  0.0111  -0.1901 45  VAL E C   
11463 O O   . VAL E 45  ? 0.2810 0.6130 0.5190 0.0349  0.0013  -0.1918 45  VAL E O   
11464 C CB  . VAL E 45  ? 0.3114 0.7181 0.5626 0.0688  0.0117  -0.1947 45  VAL E CB  
11465 C CG1 . VAL E 45  ? 0.3078 0.6834 0.5392 0.0782  -0.0121 -0.2074 45  VAL E CG1 
11466 C CG2 . VAL E 45  ? 0.3348 0.7562 0.5680 0.0926  0.0208  -0.1913 45  VAL E CG2 
11467 N N   . LEU E 46  ? 0.2844 0.6564 0.5658 0.0141  0.0099  -0.1881 46  LEU E N   
11468 C CA  . LEU E 46  ? 0.2606 0.6027 0.5392 0.0000  -0.0017 -0.1898 46  LEU E CA  
11469 C C   . LEU E 46  ? 0.2682 0.5924 0.5468 -0.0175 0.0074  -0.1813 46  LEU E C   
11470 O O   . LEU E 46  ? 0.2503 0.5491 0.5245 -0.0293 0.0006  -0.1797 46  LEU E O   
11471 C CB  . LEU E 46  ? 0.2616 0.6113 0.5554 -0.0076 -0.0078 -0.1918 46  LEU E CB  
11472 C CG  . LEU E 46  ? 0.2692 0.6380 0.5635 0.0106  -0.0180 -0.2022 46  LEU E CG  
11473 C CD1 . LEU E 46  ? 0.2769 0.6600 0.5917 0.0029  -0.0224 -0.2044 46  LEU E CD1 
11474 C CD2 . LEU E 46  ? 0.2687 0.6096 0.5368 0.0260  -0.0347 -0.2120 46  LEU E CD2 
11475 N N   . GLN E 47  ? 0.2486 0.5787 0.5231 -0.0158 0.0229  -0.1744 47  GLN E N   
11476 C CA  . GLN E 47  ? 0.2793 0.5831 0.5428 -0.0295 0.0318  -0.1643 47  GLN E CA  
11477 C C   . GLN E 47  ? 0.2557 0.5232 0.4995 -0.0302 0.0180  -0.1670 47  GLN E C   
11478 O O   . GLN E 47  ? 0.2459 0.4949 0.4894 -0.0442 0.0178  -0.1636 47  GLN E O   
11479 C CB  . GLN E 47  ? 0.3345 0.6354 0.5776 -0.0191 0.0477  -0.1552 47  GLN E CB  
11480 C CG  . GLN E 47  ? 0.3751 0.6417 0.5954 -0.0255 0.0540  -0.1463 47  GLN E CG  
11481 C CD  . GLN E 47  ? 0.4166 0.6837 0.6490 -0.0461 0.0703  -0.1354 47  GLN E CD  
11482 O OE1 . GLN E 47  ? 0.4039 0.7027 0.6629 -0.0547 0.0821  -0.1322 47  GLN E OE1 
11483 N NE2 . GLN E 47  ? 0.4422 0.6743 0.6556 -0.0542 0.0710  -0.1298 47  GLN E NE2 
11484 N N   . SER E 48  ? 0.2567 0.5136 0.4842 -0.0152 0.0064  -0.1733 48  SER E N   
11485 C CA  . SER E 48  ? 0.2521 0.4796 0.4644 -0.0162 -0.0041 -0.1749 48  SER E CA  
11486 C C   . SER E 48  ? 0.2440 0.4629 0.4642 -0.0264 -0.0130 -0.1779 48  SER E C   
11487 O O   . SER E 48  ? 0.2453 0.4379 0.4504 -0.0282 -0.0159 -0.1735 48  SER E O   
11488 C CB  . SER E 48  ? 0.2554 0.4742 0.4522 -0.0005 -0.0149 -0.1810 48  SER E CB  
11489 O OG  . SER E 48  ? 0.2510 0.4476 0.4411 -0.0044 -0.0253 -0.1831 48  SER E OG  
11490 N N   . TRP E 49  ? 0.2394 0.4684 0.4691 -0.0276 -0.0143 -0.1785 49  TRP E N   
11491 C CA  . TRP E 49  ? 0.2441 0.4529 0.4652 -0.0281 -0.0222 -0.1768 49  TRP E CA  
11492 C C   . TRP E 49  ? 0.2483 0.4422 0.4683 -0.0404 -0.0187 -0.1697 49  TRP E C   
11493 O O   . TRP E 49  ? 0.2548 0.4571 0.4880 -0.0489 -0.0175 -0.1689 49  TRP E O   
11494 C CB  . TRP E 49  ? 0.2484 0.4760 0.4809 -0.0224 -0.0278 -0.1834 49  TRP E CB  
11495 C CG  . TRP E 49  ? 0.2490 0.4844 0.4761 -0.0065 -0.0354 -0.1923 49  TRP E CG  
11496 C CD1 . TRP E 49  ? 0.2466 0.4824 0.4661 0.0015  -0.0364 -0.1953 49  TRP E CD1 
11497 C CD2 . TRP E 49  ? 0.2567 0.4983 0.4833 0.0054  -0.0460 -0.2010 49  TRP E CD2 
11498 N NE1 . TRP E 49  ? 0.2541 0.4931 0.4664 0.0173  -0.0474 -0.2047 49  TRP E NE1 
11499 C CE2 . TRP E 49  ? 0.2601 0.5031 0.4763 0.0205  -0.0528 -0.2083 49  TRP E CE2 
11500 C CE3 . TRP E 49  ? 0.2643 0.5093 0.4968 0.0067  -0.0523 -0.2046 49  TRP E CE3 
11501 C CZ2 . TRP E 49  ? 0.2722 0.5177 0.4811 0.0373  -0.0652 -0.2184 49  TRP E CZ2 
11502 C CZ3 . TRP E 49  ? 0.2742 0.5251 0.5019 0.0236  -0.0640 -0.2155 49  TRP E CZ3 
11503 C CH2 . TRP E 49  ? 0.2785 0.5288 0.4935 0.0390  -0.0700 -0.2219 49  TRP E CH2 
11504 N N   . ASP E 50  ? 0.2313 0.4031 0.4358 -0.0410 -0.0183 -0.1650 50  ASP E N   
11505 C CA  . ASP E 50  ? 0.2379 0.3936 0.4372 -0.0496 -0.0167 -0.1602 50  ASP E CA  
11506 C C   . ASP E 50  ? 0.2438 0.3833 0.4329 -0.0461 -0.0249 -0.1591 50  ASP E C   
11507 O O   . ASP E 50  ? 0.2416 0.3700 0.4184 -0.0394 -0.0275 -0.1578 50  ASP E O   
11508 C CB  . ASP E 50  ? 0.2356 0.3810 0.4248 -0.0495 -0.0126 -0.1585 50  ASP E CB  
11509 C CG  . ASP E 50  ? 0.2454 0.3714 0.4250 -0.0551 -0.0129 -0.1560 50  ASP E CG  
11510 O OD1 . ASP E 50  ? 0.2563 0.3761 0.4385 -0.0622 -0.0154 -0.1553 50  ASP E OD1 
11511 O OD2 . ASP E 50  ? 0.2448 0.3617 0.4140 -0.0516 -0.0121 -0.1562 50  ASP E OD2 
11512 N N   . ALA E 51  ? 0.2484 0.3874 0.4439 -0.0516 -0.0293 -0.1602 51  ALA E N   
11513 C CA  . ALA E 51  ? 0.2576 0.3827 0.4432 -0.0466 -0.0391 -0.1620 51  ALA E CA  
11514 C C   . ALA E 51  ? 0.2627 0.3651 0.4293 -0.0450 -0.0396 -0.1591 51  ALA E C   
11515 O O   . ALA E 51  ? 0.2692 0.3598 0.4233 -0.0378 -0.0455 -0.1610 51  ALA E O   
11516 C CB  . ALA E 51  ? 0.2712 0.4005 0.4688 -0.0532 -0.0458 -0.1653 51  ALA E CB  
11517 N N   . THR E 52  ? 0.2482 0.3447 0.4117 -0.0505 -0.0335 -0.1563 52  THR E N   
11518 C CA  . THR E 52  ? 0.2562 0.3335 0.4027 -0.0478 -0.0344 -0.1562 52  THR E CA  
11519 C C   . THR E 52  ? 0.2452 0.3253 0.3865 -0.0410 -0.0300 -0.1555 52  THR E C   
11520 O O   . THR E 52  ? 0.2499 0.3212 0.3813 -0.0386 -0.0284 -0.1572 52  THR E O   
11521 C CB  . THR E 52  ? 0.2665 0.3333 0.4096 -0.0554 -0.0314 -0.1561 52  THR E CB  
11522 O OG1 . THR E 52  ? 0.2546 0.3333 0.4042 -0.0569 -0.0228 -0.1553 52  THR E OG1 
11523 C CG2 . THR E 52  ? 0.2810 0.3452 0.4335 -0.0668 -0.0351 -0.1562 52  THR E CG2 
11524 N N   . LEU E 53  ? 0.2319 0.3237 0.3799 -0.0381 -0.0288 -0.1545 53  LEU E N   
11525 C CA  . LEU E 53  ? 0.2260 0.3190 0.3719 -0.0348 -0.0261 -0.1541 53  LEU E CA  
11526 C C   . LEU E 53  ? 0.2360 0.3183 0.3724 -0.0311 -0.0304 -0.1568 53  LEU E C   
11527 O O   . LEU E 53  ? 0.2451 0.3214 0.3766 -0.0281 -0.0372 -0.1589 53  LEU E O   
11528 C CB  . LEU E 53  ? 0.2160 0.3206 0.3702 -0.0339 -0.0243 -0.1526 53  LEU E CB  
11529 C CG  . LEU E 53  ? 0.2101 0.3245 0.3709 -0.0356 -0.0202 -0.1527 53  LEU E CG  
11530 C CD1 . LEU E 53  ? 0.2048 0.3282 0.3703 -0.0318 -0.0210 -0.1540 53  LEU E CD1 
11531 C CD2 . LEU E 53  ? 0.2104 0.3227 0.3685 -0.0364 -0.0171 -0.1536 53  LEU E CD2 
11532 N N   . VAL E 54  ? 0.2543 0.3345 0.3884 -0.0315 -0.0266 -0.1586 54  VAL E N   
11533 C CA  . VAL E 54  ? 0.2703 0.3360 0.3911 -0.0282 -0.0278 -0.1619 54  VAL E CA  
11534 C C   . VAL E 54  ? 0.2749 0.3355 0.3933 -0.0263 -0.0343 -0.1629 54  VAL E C   
11535 O O   . VAL E 54  ? 0.2901 0.3379 0.3945 -0.0192 -0.0415 -0.1661 54  VAL E O   
11536 C CB  . VAL E 54  ? 0.2738 0.3417 0.3941 -0.0291 -0.0164 -0.1534 54  VAL E CB  
11537 C CG1 . VAL E 54  ? 0.2992 0.3476 0.3969 -0.0223 -0.0118 -0.1482 54  VAL E CG1 
11538 C CG2 . VAL E 54  ? 0.2676 0.3466 0.3922 -0.0275 -0.0105 -0.1513 54  VAL E CG2 
11539 N N   . THR E 55  ? 0.3084 0.3771 0.4370 -0.0299 -0.0331 -0.1598 55  THR E N   
11540 C CA  . THR E 55  ? 0.3159 0.3783 0.4392 -0.0259 -0.0399 -0.1609 55  THR E CA  
11541 C C   . THR E 55  ? 0.3014 0.3808 0.4369 -0.0243 -0.0407 -0.1587 55  THR E C   
11542 O O   . THR E 55  ? 0.2884 0.3798 0.4340 -0.0275 -0.0352 -0.1556 55  THR E O   
11543 C CB  . THR E 55  ? 0.3300 0.3770 0.4479 -0.0307 -0.0392 -0.1622 55  THR E CB  
11544 O OG1 . THR E 55  ? 0.3182 0.3772 0.4512 -0.0368 -0.0367 -0.1581 55  THR E OG1 
11545 C CG2 . THR E 55  ? 0.3454 0.3796 0.4519 -0.0324 -0.0291 -0.1554 55  THR E CG2 
11546 N N   . PRO E 56  ? 0.3271 0.4077 0.4603 -0.0174 -0.0477 -0.1625 56  PRO E N   
11547 C CA  . PRO E 56  ? 0.3168 0.4150 0.4613 -0.0143 -0.0478 -0.1641 56  PRO E CA  
11548 C C   . PRO E 56  ? 0.3196 0.4133 0.4620 -0.0135 -0.0495 -0.1639 56  PRO E C   
11549 O O   . PRO E 56  ? 0.3174 0.4223 0.4642 -0.0072 -0.0522 -0.1683 56  PRO E O   
11550 C CB  . PRO E 56  ? 0.3244 0.4282 0.4685 -0.0052 -0.0559 -0.1714 56  PRO E CB  
11551 C CG  . PRO E 56  ? 0.3449 0.4241 0.4689 -0.0012 -0.0627 -0.1726 56  PRO E CG  
11552 C CD  . PRO E 56  ? 0.3458 0.4125 0.4644 -0.0095 -0.0564 -0.1677 56  PRO E CD  
11553 N N   . CYS E 57  ? 0.3414 0.4198 0.4784 -0.0200 -0.0487 -0.1604 57  CYS E N   
11554 C CA  . CYS E 57  ? 0.3512 0.4200 0.4854 -0.0208 -0.0533 -0.1608 57  CYS E CA  
11555 C C   . CYS E 57  ? 0.3392 0.4230 0.4838 -0.0195 -0.0514 -0.1604 57  CYS E C   
11556 O O   . CYS E 57  ? 0.3488 0.4270 0.4898 -0.0153 -0.0585 -0.1633 57  CYS E O   
11557 C CB  . CYS E 57  ? 0.3644 0.4158 0.4963 -0.0320 -0.0519 -0.1583 57  CYS E CB  
11558 S SG  . CYS E 57  ? 0.3901 0.4135 0.5013 -0.0315 -0.0549 -0.1620 57  CYS E SG  
11559 N N   . THR E 58  ? 0.2843 0.3829 0.4380 -0.0214 -0.0436 -0.1581 58  THR E N   
11560 C CA  . THR E 58  ? 0.2774 0.3875 0.4370 -0.0182 -0.0424 -0.1599 58  THR E CA  
11561 C C   . THR E 58  ? 0.2726 0.3974 0.4346 -0.0109 -0.0419 -0.1659 58  THR E C   
11562 O O   . THR E 58  ? 0.2692 0.4044 0.4345 -0.0077 -0.0405 -0.1697 58  THR E O   
11563 C CB  . THR E 58  ? 0.2685 0.3850 0.4340 -0.0230 -0.0353 -0.1567 58  THR E CB  
11564 O OG1 . THR E 58  ? 0.2625 0.3829 0.4277 -0.0247 -0.0295 -0.1554 58  THR E OG1 
11565 C CG2 . THR E 58  ? 0.2729 0.3829 0.4417 -0.0305 -0.0346 -0.1533 58  THR E CG2 
11566 N N   . TRP E 59  ? 0.2738 0.4021 0.4355 -0.0080 -0.0437 -0.1688 59  TRP E N   
11567 C CA  . TRP E 59  ? 0.2703 0.4198 0.4398 -0.0020 -0.0432 -0.1770 59  TRP E CA  
11568 C C   . TRP E 59  ? 0.2804 0.4317 0.4436 0.0103  -0.0519 -0.1852 59  TRP E C   
11569 O O   . TRP E 59  ? 0.2938 0.4243 0.4449 0.0136  -0.0601 -0.1836 59  TRP E O   
11570 C CB  . TRP E 59  ? 0.2705 0.4275 0.4450 -0.0018 -0.0439 -0.1792 59  TRP E CB  
11571 C CG  . TRP E 59  ? 0.2664 0.4185 0.4434 -0.0114 -0.0383 -0.1725 59  TRP E CG  
11572 C CD1 . TRP E 59  ? 0.2626 0.4057 0.4369 -0.0189 -0.0323 -0.1655 59  TRP E CD1 
11573 C CD2 . TRP E 59  ? 0.2697 0.4247 0.4505 -0.0121 -0.0407 -0.1741 59  TRP E CD2 
11574 N NE1 . TRP E 59  ? 0.2643 0.4027 0.4386 -0.0240 -0.0310 -0.1626 59  TRP E NE1 
11575 C CE2 . TRP E 59  ? 0.2690 0.4138 0.4475 -0.0204 -0.0365 -0.1675 59  TRP E CE2 
11576 C CE3 . TRP E 59  ? 0.2756 0.4416 0.4613 -0.0047 -0.0477 -0.1820 59  TRP E CE3 
11577 C CZ2 . TRP E 59  ? 0.2753 0.4178 0.4554 -0.0223 -0.0401 -0.1684 59  TRP E CZ2 
11578 C CZ3 . TRP E 59  ? 0.2805 0.4466 0.4701 -0.0067 -0.0508 -0.1828 59  TRP E CZ3 
11579 C CH2 . TRP E 59  ? 0.2810 0.4341 0.4672 -0.0158 -0.0474 -0.1759 59  TRP E CH2 
11580 N N   . PHE E 60  ? 0.2662 0.4421 0.4362 0.0171  -0.0506 -0.1948 60  PHE E N   
11581 C CA  . PHE E 60  ? 0.2807 0.4591 0.4391 0.0341  -0.0598 -0.2048 60  PHE E CA  
11582 C C   . PHE E 60  ? 0.2875 0.4744 0.4452 0.0438  -0.0659 -0.2112 60  PHE E C   
11583 O O   . PHE E 60  ? 0.2773 0.4812 0.4506 0.0377  -0.0616 -0.2107 60  PHE E O   
11584 C CB  . PHE E 60  ? 0.2840 0.4804 0.4405 0.0436  -0.0490 -0.2021 60  PHE E CB  
11585 C CG  . PHE E 60  ? 0.2824 0.4689 0.4348 0.0382  -0.0442 -0.1970 60  PHE E CG  
11586 C CD1 . PHE E 60  ? 0.2828 0.4475 0.4316 0.0322  -0.0544 -0.1988 60  PHE E CD1 
11587 C CD2 . PHE E 60  ? 0.3086 0.5079 0.4606 0.0398  -0.0291 -0.1902 60  PHE E CD2 
11588 C CE1 . PHE E 60  ? 0.2826 0.4421 0.4289 0.0301  -0.0518 -0.1961 60  PHE E CE1 
11589 C CE2 . PHE E 60  ? 0.3052 0.4920 0.4483 0.0384  -0.0263 -0.1865 60  PHE E CE2 
11590 C CZ  . PHE E 60  ? 0.2859 0.4547 0.4268 0.0348  -0.0387 -0.1904 60  PHE E CZ  
11591 N N   . HIS E 61  ? 0.3059 0.4778 0.4440 0.0605  -0.0768 -0.2150 61  HIS E N   
11592 C CA  . HIS E 61  ? 0.3206 0.4932 0.4501 0.0751  -0.0856 -0.2208 61  HIS E CA  
11593 C C   . HIS E 61  ? 0.3253 0.4724 0.4501 0.0665  -0.0895 -0.2130 61  HIS E C   
11594 O O   . HIS E 61  ? 0.3411 0.4839 0.4557 0.0791  -0.0981 -0.2173 61  HIS E O   
11595 C CB  . HIS E 61  ? 0.3179 0.5360 0.4654 0.0838  -0.0783 -0.2283 61  HIS E CB  
11596 C CG  . HIS E 61  ? 0.3295 0.5740 0.4859 0.0866  -0.0628 -0.2229 61  HIS E CG  
11597 N ND1 . HIS E 61  ? 0.3435 0.5827 0.4785 0.1059  -0.0647 -0.2253 61  HIS E ND1 
11598 C CD2 . HIS E 61  ? 0.3259 0.5972 0.5057 0.0733  -0.0451 -0.2146 61  HIS E CD2 
11599 C CE1 . HIS E 61  ? 0.3464 0.6091 0.4900 0.1057  -0.0473 -0.2180 61  HIS E CE1 
11600 N NE2 . HIS E 61  ? 0.3371 0.6187 0.5082 0.0848  -0.0346 -0.2109 61  HIS E NE2 
11601 N N   . VAL E 62  ? 0.3924 0.6182 0.3062 0.1348  -0.0769 -0.0601 62  VAL E N   
11602 C CA  . VAL E 62  ? 0.4057 0.6004 0.3102 0.1305  -0.0818 -0.0512 62  VAL E CA  
11603 C C   . VAL E 62  ? 0.4298 0.5834 0.3307 0.1250  -0.0847 -0.0424 62  VAL E C   
11604 O O   . VAL E 62  ? 0.4363 0.5876 0.3461 0.1131  -0.0768 -0.0373 62  VAL E O   
11605 C CB  . VAL E 62  ? 0.3980 0.6037 0.3058 0.1144  -0.0687 -0.0434 62  VAL E CB  
11606 C CG1 . VAL E 62  ? 0.4245 0.5930 0.3153 0.1075  -0.0694 -0.0320 62  VAL E CG1 
11607 C CG2 . VAL E 62  ? 0.3827 0.6249 0.2997 0.1213  -0.0698 -0.0541 62  VAL E CG2 
11608 N N   . THR E 63  ? 0.4703 0.5914 0.3627 0.1339  -0.0965 -0.0400 63  THR E N   
11609 C CA  . THR E 63  ? 0.5045 0.5840 0.4006 0.1285  -0.0980 -0.0310 63  THR E CA  
11610 C C   . THR E 63  ? 0.5343 0.5821 0.4154 0.1230  -0.0935 -0.0148 63  THR E C   
11611 O O   . THR E 63  ? 0.5381 0.5862 0.4021 0.1334  -0.1010 -0.0139 63  THR E O   
11612 C CB  . THR E 63  ? 0.5103 0.5744 0.4148 0.1451  -0.1151 -0.0423 63  THR E CB  
11613 O OG1 . THR E 63  ? 0.5414 0.5825 0.4381 0.1574  -0.1258 -0.0385 63  THR E OG1 
11614 C CG2 . THR E 63  ? 0.4786 0.5801 0.3860 0.1579  -0.1209 -0.0620 63  THR E CG2 
11615 N N   . CYS E 64  ? 0.5308 0.5517 0.4180 0.1073  -0.0812 -0.0021 64  CYS E N   
11616 C CA  . CYS E 64  ? 0.5673 0.5560 0.4376 0.1003  -0.0714 0.0151  64  CYS E CA  
11617 C C   . CYS E 64  ? 0.5998 0.5434 0.4821 0.1017  -0.0732 0.0248  64  CYS E C   
11618 O O   . CYS E 64  ? 0.5974 0.5356 0.5069 0.1045  -0.0815 0.0163  64  CYS E O   
11619 C CB  . CYS E 64  ? 0.5687 0.5626 0.4408 0.0794  -0.0499 0.0221  64  CYS E CB  
11620 S SG  . CYS E 64  ? 0.5438 0.5817 0.4028 0.0757  -0.0447 0.0140  64  CYS E SG  
11621 N N   . ASN E 65  ? 0.5859 0.4969 0.4477 0.1002  -0.0652 0.0426  65  ASN E N   
11622 C CA  . ASN E 65  ? 0.6151 0.4799 0.4919 0.0983  -0.0606 0.0566  65  ASN E CA  
11623 C C   . ASN E 65  ? 0.6075 0.4576 0.5003 0.0763  -0.0358 0.0665  65  ASN E C   
11624 O O   . ASN E 65  ? 0.5781 0.4542 0.4722 0.0638  -0.0251 0.0611  65  ASN E O   
11625 C CB  . ASN E 65  ? 0.6643 0.4990 0.5099 0.1104  -0.0642 0.0738  65  ASN E CB  
11626 C CG  . ASN E 65  ? 0.6834 0.5198 0.4834 0.1049  -0.0508 0.0862  65  ASN E CG  
11627 O OD1 . ASN E 65  ? 0.6593 0.5163 0.4563 0.0901  -0.0357 0.0818  65  ASN E OD1 
11628 N ND2 . ASN E 65  ? 0.7309 0.5447 0.4952 0.1177  -0.0572 0.1014  65  ASN E ND2 
11629 N N   . SER E 66  ? 0.6589 0.4666 0.5698 0.0713  -0.0255 0.0812  66  SER E N   
11630 C CA  . SER E 66  ? 0.6437 0.4361 0.5791 0.0506  -0.0007 0.0896  66  SER E CA  
11631 C C   . SER E 66  ? 0.6531 0.4486 0.5521 0.0394  0.0230  0.1006  66  SER E C   
11632 O O   . SER E 66  ? 0.6268 0.4200 0.5466 0.0215  0.0446  0.1028  66  SER E O   
11633 C CB  . SER E 66  ? 0.6432 0.3884 0.6100 0.0483  0.0074  0.1038  66  SER E CB  
11634 O OG  . SER E 66  ? 0.6875 0.4032 0.6201 0.0591  0.0095  0.1232  66  SER E OG  
11635 N N   . ASP E 67  ? 0.6871 0.4883 0.5347 0.0502  0.0183  0.1054  67  ASP E N   
11636 C CA  . ASP E 67  ? 0.6952 0.5025 0.5028 0.0421  0.0367  0.1111  67  ASP E CA  
11637 C C   . ASP E 67  ? 0.6732 0.5289 0.4763 0.0398  0.0297  0.0915  67  ASP E C   
11638 O O   . ASP E 67  ? 0.6769 0.5428 0.4492 0.0345  0.0411  0.0909  67  ASP E O   
11639 C CB  . ASP E 67  ? 0.7391 0.5237 0.4901 0.0559  0.0337  0.1277  67  ASP E CB  
11640 C CG  . ASP E 67  ? 0.7658 0.4994 0.5207 0.0581  0.0439  0.1517  67  ASP E CG  
11641 O OD1 . ASP E 67  ? 0.7470 0.4607 0.5442 0.0439  0.0630  0.1569  67  ASP E OD1 
11642 O OD2 . ASP E 67  ? 0.8006 0.5135 0.5202 0.0743  0.0326  0.1661  67  ASP E OD2 
11643 N N   . ASN E 68  ? 0.6241 0.5092 0.4571 0.0442  0.0118  0.0752  68  ASN E N   
11644 C CA  . ASN E 68  ? 0.5961 0.5275 0.4309 0.0432  0.0053  0.0584  68  ASN E CA  
11645 C C   . ASN E 68  ? 0.5989 0.5479 0.3944 0.0576  -0.0087 0.0535  68  ASN E C   
11646 O O   . ASN E 68  ? 0.5726 0.5531 0.3624 0.0536  -0.0068 0.0429  68  ASN E O   
11647 C CB  . ASN E 68  ? 0.5691 0.5127 0.4192 0.0229  0.0275  0.0561  68  ASN E CB  
11648 C CG  . ASN E 68  ? 0.5529 0.4802 0.4475 0.0090  0.0395  0.0602  68  ASN E CG  
11649 O OD1 . ASN E 68  ? 0.5320 0.4782 0.4602 0.0072  0.0306  0.0516  68  ASN E OD1 
11650 N ND2 . ASN E 68  ? 0.5614 0.4535 0.4567 -0.0004 0.0598  0.0735  68  ASN E ND2 
11651 N N   . SER E 69  ? 0.6492 0.5779 0.4227 0.0747  -0.0240 0.0606  69  SER E N   
11652 C CA  . SER E 69  ? 0.6450 0.5912 0.3893 0.0918  -0.0437 0.0544  69  SER E CA  
11653 C C   . SER E 69  ? 0.6192 0.5909 0.3894 0.1056  -0.0648 0.0392  69  SER E C   
11654 O O   . SER E 69  ? 0.6256 0.5822 0.4188 0.1099  -0.0703 0.0397  69  SER E O   
11655 C CB  . SER E 69  ? 0.6902 0.5981 0.3936 0.1040  -0.0491 0.0731  69  SER E CB  
11656 O OG  . SER E 69  ? 0.6879 0.6121 0.3540 0.1154  -0.0631 0.0684  69  SER E OG  
11657 N N   . VAL E 70  ? 0.6290 0.6401 0.3980 0.1125  -0.0758 0.0238  70  VAL E N   
11658 C CA  . VAL E 70  ? 0.5918 0.6313 0.3852 0.1254  -0.0916 0.0080  70  VAL E CA  
11659 C C   . VAL E 70  ? 0.6150 0.6324 0.4004 0.1460  -0.1117 0.0112  70  VAL E C   
11660 O O   . VAL E 70  ? 0.6366 0.6396 0.3931 0.1564  -0.1223 0.0192  70  VAL E O   
11661 C CB  . VAL E 70  ? 0.5533 0.6395 0.3530 0.1274  -0.0958 -0.0082 70  VAL E CB  
11662 C CG1 . VAL E 70  ? 0.5299 0.6438 0.3518 0.1436  -0.1109 -0.0238 70  VAL E CG1 
11663 C CG2 . VAL E 70  ? 0.5354 0.6444 0.3542 0.1073  -0.0760 -0.0118 70  VAL E CG2 
11664 N N   . THR E 71  ? 0.5918 0.6054 0.4028 0.1528  -0.1183 0.0046  71  THR E N   
11665 C CA  . THR E 71  ? 0.6183 0.6121 0.4322 0.1725  -0.1375 0.0045  71  THR E CA  
11666 C C   . THR E 71  ? 0.5996 0.6271 0.4379 0.1875  -0.1513 -0.0184 71  THR E C   
11667 O O   . THR E 71  ? 0.6231 0.6407 0.4669 0.2061  -0.1692 -0.0224 71  THR E O   
11668 C CB  . THR E 71  ? 0.6370 0.5868 0.4633 0.1694  -0.1337 0.0162  71  THR E CB  
11669 O OG1 . THR E 71  ? 0.6104 0.5722 0.4652 0.1600  -0.1268 0.0045  71  THR E OG1 
11670 C CG2 . THR E 71  ? 0.6702 0.5832 0.4732 0.1562  -0.1171 0.0408  71  THR E CG2 
11671 N N   . ARG E 72  ? 0.5604 0.6263 0.4140 0.1804  -0.1424 -0.0328 72  ARG E N   
11672 C CA  . ARG E 72  ? 0.5316 0.6311 0.4058 0.1939  -0.1503 -0.0543 72  ARG E CA  
11673 C C   . ARG E 72  ? 0.5016 0.6481 0.3827 0.1863  -0.1385 -0.0634 72  ARG E C   
11674 O O   . ARG E 72  ? 0.4966 0.6486 0.3750 0.1681  -0.1225 -0.0557 72  ARG E O   
11675 C CB  . ARG E 72  ? 0.5306 0.6217 0.4209 0.1955  -0.1505 -0.0632 72  ARG E CB  
11676 C CG  . ARG E 72  ? 0.5581 0.6083 0.4557 0.2069  -0.1648 -0.0610 72  ARG E CG  
11677 C CD  . ARG E 72  ? 0.5501 0.6030 0.4679 0.2138  -0.1702 -0.0797 72  ARG E CD  
11678 N NE  . ARG E 72  ? 0.5322 0.6235 0.4578 0.2295  -0.1757 -0.1030 72  ARG E NE  
11679 C CZ  . ARG E 72  ? 0.5469 0.6345 0.4883 0.2494  -0.1911 -0.1195 72  ARG E CZ  
11680 N NH1 . ARG E 72  ? 0.5746 0.6209 0.5278 0.2565  -0.2044 -0.1144 72  ARG E NH1 
11681 N NH2 . ARG E 72  ? 0.5412 0.6672 0.4905 0.2625  -0.1917 -0.1414 72  ARG E NH2 
11682 N N   . VAL E 73  ? 0.4919 0.6717 0.3873 0.2005  -0.1457 -0.0798 73  VAL E N   
11683 C CA  . VAL E 73  ? 0.4634 0.6891 0.3756 0.1947  -0.1318 -0.0901 73  VAL E CA  
11684 C C   . VAL E 73  ? 0.4644 0.7123 0.3946 0.2101  -0.1335 -0.1091 73  VAL E C   
11685 O O   . VAL E 73  ? 0.4789 0.7334 0.4219 0.2242  -0.1431 -0.1205 73  VAL E O   
11686 C CB  . VAL E 73  ? 0.4620 0.7056 0.3799 0.1922  -0.1322 -0.0914 73  VAL E CB  
11687 C CG1 . VAL E 73  ? 0.4320 0.7253 0.3754 0.1874  -0.1179 -0.1020 73  VAL E CG1 
11688 C CG2 . VAL E 73  ? 0.4688 0.6895 0.3627 0.1793  -0.1312 -0.0753 73  VAL E CG2 
11689 N N   . ASP E 74  ? 0.4611 0.7198 0.3910 0.2077  -0.1242 -0.1131 74  ASP E N   
11690 C CA  . ASP E 74  ? 0.4619 0.7403 0.4010 0.2233  -0.1247 -0.1324 74  ASP E CA  
11691 C C   . ASP E 74  ? 0.4512 0.7774 0.4026 0.2199  -0.1047 -0.1384 74  ASP E C   
11692 O O   . ASP E 74  ? 0.4514 0.7883 0.3944 0.2108  -0.0896 -0.1338 74  ASP E O   
11693 C CB  . ASP E 74  ? 0.4744 0.7285 0.4014 0.2232  -0.1276 -0.1340 74  ASP E CB  
11694 C CG  . ASP E 74  ? 0.4934 0.7004 0.4181 0.2276  -0.1458 -0.1291 74  ASP E CG  
11695 O OD1 . ASP E 74  ? 0.4995 0.6775 0.4154 0.2130  -0.1441 -0.1103 74  ASP E OD1 
11696 O OD2 . ASP E 74  ? 0.5037 0.7023 0.4384 0.2457  -0.1601 -0.1439 74  ASP E OD2 
11697 N N   . LEU E 75  ? 0.4367 0.7914 0.4108 0.2276  -0.1049 -0.1476 75  LEU E N   
11698 C CA  . LEU E 75  ? 0.4202 0.8212 0.4155 0.2244  -0.0839 -0.1529 75  LEU E CA  
11699 C C   . LEU E 75  ? 0.4328 0.8629 0.4496 0.2443  -0.0823 -0.1753 75  LEU E C   
11700 O O   . LEU E 75  ? 0.4287 0.8861 0.4705 0.2405  -0.0704 -0.1803 75  LEU E O   
11701 C CB  . LEU E 75  ? 0.4022 0.8178 0.4170 0.2132  -0.0816 -0.1462 75  LEU E CB  
11702 C CG  . LEU E 75  ? 0.3855 0.7862 0.3870 0.1908  -0.0732 -0.1266 75  LEU E CG  
11703 C CD1 . LEU E 75  ? 0.3747 0.7875 0.3951 0.1831  -0.0760 -0.1258 75  LEU E CD1 
11704 C CD2 . LEU E 75  ? 0.3714 0.7906 0.3734 0.1794  -0.0490 -0.1187 75  LEU E CD2 
11705 N N   . GLY E 76  ? 0.5245 0.9384 0.5301 0.2596  -0.0929 -0.1879 76  GLY E N   
11706 C CA  . GLY E 76  ? 0.5236 0.9552 0.5440 0.2727  -0.0894 -0.2088 76  GLY E CA  
11707 C C   . GLY E 76  ? 0.5128 0.9739 0.5273 0.2664  -0.0628 -0.2095 76  GLY E C   
11708 O O   . GLY E 76  ? 0.5206 0.9793 0.5088 0.2596  -0.0528 -0.1994 76  GLY E O   
11709 N N   . ASN E 77  ? 0.5080 0.9932 0.5475 0.2674  -0.0514 -0.2189 77  ASN E N   
11710 C CA  . ASN E 77  ? 0.5218 1.0305 0.5573 0.2626  -0.0253 -0.2179 77  ASN E CA  
11711 C C   . ASN E 77  ? 0.5040 1.0215 0.5303 0.2433  -0.0044 -0.1939 77  ASN E C   
11712 O O   . ASN E 77  ? 0.5161 1.0342 0.5146 0.2396  0.0086  -0.1848 77  ASN E O   
11713 C CB  . ASN E 77  ? 0.5510 1.0507 0.5573 0.2750  -0.0287 -0.2300 77  ASN E CB  
11714 C CG  . ASN E 77  ? 0.5698 1.0562 0.5888 0.2932  -0.0508 -0.2537 77  ASN E CG  
11715 O OD1 . ASN E 77  ? 0.5706 1.0282 0.5784 0.3011  -0.0736 -0.2580 77  ASN E OD1 
11716 N ND2 . ASN E 77  ? 0.5880 1.0929 0.6336 0.2997  -0.0430 -0.2689 77  ASN E ND2 
11717 N N   . ALA E 78  ? 0.5056 1.0279 0.5565 0.2308  -0.0029 -0.1836 78  ALA E N   
11718 C CA  . ALA E 78  ? 0.4870 1.0134 0.5361 0.2112  0.0142  -0.1610 78  ALA E CA  
11719 C C   . ALA E 78  ? 0.4854 1.0329 0.5722 0.1990  0.0369  -0.1550 78  ALA E C   
11720 O O   . ALA E 78  ? 0.4724 1.0209 0.5649 0.1820  0.0520  -0.1361 78  ALA E O   
11721 C CB  . ALA E 78  ? 0.4648 0.9751 0.5116 0.2041  -0.0012 -0.1526 78  ALA E CB  
11722 N N   . ASN E 79  ? 0.4605 1.0227 0.5775 0.2073  0.0402  -0.1707 79  ASN E N   
11723 C CA  . ASN E 79  ? 0.4621 1.0432 0.6238 0.1974  0.0624  -0.1673 79  ASN E CA  
11724 C C   . ASN E 79  ? 0.4348 1.0143 0.6264 0.1827  0.0571  -0.1592 79  ASN E C   
11725 O O   . ASN E 79  ? 0.4311 1.0188 0.6528 0.1687  0.0784  -0.1473 79  ASN E O   
11726 C CB  . ASN E 79  ? 0.4811 1.0698 0.6329 0.1900  0.0953  -0.1517 79  ASN E CB  
11727 C CG  . ASN E 79  ? 0.5129 1.1007 0.6241 0.2042  0.0989  -0.1592 79  ASN E CG  
11728 O OD1 . ASN E 79  ? 0.5208 1.1042 0.6214 0.2198  0.0788  -0.1787 79  ASN E OD1 
11729 N ND2 . ASN E 79  ? 0.5355 1.1257 0.6240 0.1994  0.1238  -0.1442 79  ASN E ND2 
11730 N N   . LEU E 80  ? 0.4460 0.9093 0.7711 0.2341  -0.1124 -0.2104 80  LEU E N   
11731 C CA  . LEU E 80  ? 0.4356 0.9022 0.7761 0.2202  -0.1197 -0.2115 80  LEU E CA  
11732 C C   . LEU E 80  ? 0.4428 0.9369 0.8048 0.2203  -0.1279 -0.2139 80  LEU E C   
11733 O O   . LEU E 80  ? 0.4584 0.9459 0.8100 0.2325  -0.1383 -0.2169 80  LEU E O   
11734 C CB  . LEU E 80  ? 0.4381 0.8648 0.7544 0.2197  -0.1328 -0.2146 80  LEU E CB  
11735 C CG  . LEU E 80  ? 0.4451 0.8519 0.7526 0.2101  -0.1273 -0.2121 80  LEU E CG  
11736 C CD1 . LEU E 80  ? 0.4496 0.8777 0.7837 0.1936  -0.1233 -0.2118 80  LEU E CD1 
11737 C CD2 . LEU E 80  ? 0.4407 0.8442 0.7375 0.2144  -0.1121 -0.2079 80  LEU E CD2 
11738 N N   . SER E 81  ? 0.4237 0.9490 0.8171 0.2063  -0.1230 -0.2124 81  SER E N   
11739 C CA  . SER E 81  ? 0.4299 0.9834 0.8466 0.2028  -0.1319 -0.2152 81  SER E CA  
11740 C C   . SER E 81  ? 0.4248 0.9731 0.8488 0.1870  -0.1434 -0.2209 81  SER E C   
11741 O O   . SER E 81  ? 0.4123 0.9490 0.8377 0.1748  -0.1390 -0.2213 81  SER E O   
11742 C CB  . SER E 81  ? 0.4267 1.0242 0.8781 0.1978  -0.1181 -0.2094 81  SER E CB  
11743 O OG  . SER E 81  ? 0.4113 1.0174 0.8812 0.1824  -0.1039 -0.2048 81  SER E OG  
11744 N N   . GLY E 82  ? 0.4406 0.9976 0.8682 0.1881  -0.1581 -0.2254 82  GLY E N   
11745 C CA  . GLY E 82  ? 0.4414 0.9933 0.8712 0.1746  -0.1710 -0.2319 82  GLY E CA  
11746 C C   . GLY E 82  ? 0.4598 1.0028 0.8713 0.1855  -0.1882 -0.2344 82  GLY E C   
11747 O O   . GLY E 82  ? 0.4712 1.0244 0.8813 0.2001  -0.1898 -0.2319 82  GLY E O   
11748 N N   . GLN E 83  ? 0.4655 0.9900 0.8629 0.1785  -0.2002 -0.2387 83  GLN E N   
11749 C CA  . GLN E 83  ? 0.4844 1.0005 0.8634 0.1878  -0.2159 -0.2395 83  GLN E CA  
11750 C C   . GLN E 83  ? 0.4879 0.9607 0.8314 0.1928  -0.2219 -0.2368 83  GLN E C   
11751 O O   . GLN E 83  ? 0.4769 0.9324 0.8143 0.1820  -0.2187 -0.2380 83  GLN E O   
11752 C CB  . GLN E 83  ? 0.4924 1.0344 0.8892 0.1745  -0.2259 -0.2469 83  GLN E CB  
11753 C CG  . GLN E 83  ? 0.4856 1.0695 0.9238 0.1616  -0.2185 -0.2500 83  GLN E CG  
11754 C CD  . GLN E 83  ? 0.5010 1.1186 0.9550 0.1668  -0.2267 -0.2510 83  GLN E CD  
11755 O OE1 . GLN E 83  ? 0.5176 1.1286 0.9523 0.1778  -0.2394 -0.2510 83  GLN E OE1 
11756 N NE2 . GLN E 83  ? 0.4965 1.1520 0.9868 0.1595  -0.2188 -0.2504 83  GLN E NE2 
11757 N N   . LEU E 84  ? 0.4694 0.9254 0.7909 0.2091  -0.2300 -0.2320 84  LEU E N   
11758 C CA  . LEU E 84  ? 0.4761 0.8931 0.7658 0.2138  -0.2362 -0.2272 84  LEU E CA  
11759 C C   . LEU E 84  ? 0.4806 0.8971 0.7637 0.2017  -0.2453 -0.2312 84  LEU E C   
11760 O O   . LEU E 84  ? 0.4823 0.9280 0.7849 0.1909  -0.2490 -0.2389 84  LEU E O   
11761 C CB  . LEU E 84  ? 0.4959 0.8983 0.7683 0.2330  -0.2429 -0.2203 84  LEU E CB  
11762 C CG  . LEU E 84  ? 0.4969 0.8729 0.7577 0.2455  -0.2362 -0.2153 84  LEU E CG  
11763 C CD1 . LEU E 84  ? 0.4875 0.8855 0.7685 0.2469  -0.2250 -0.2191 84  LEU E CD1 
11764 C CD2 . LEU E 84  ? 0.5199 0.8792 0.7654 0.2628  -0.2441 -0.2085 84  LEU E CD2 
11765 N N   . VAL E 85  ? 0.4657 0.8486 0.7208 0.2036  -0.2489 -0.2261 85  VAL E N   
11766 C CA  . VAL E 85  ? 0.4706 0.8474 0.7138 0.1926  -0.2556 -0.2298 85  VAL E CA  
11767 C C   . VAL E 85  ? 0.4904 0.8446 0.7030 0.2051  -0.2648 -0.2207 85  VAL E C   
11768 O O   . VAL E 85  ? 0.4932 0.8206 0.6897 0.2169  -0.2629 -0.2103 85  VAL E O   
11769 C CB  . VAL E 85  ? 0.4536 0.8127 0.6940 0.1795  -0.2479 -0.2318 85  VAL E CB  
11770 C CG1 . VAL E 85  ? 0.4630 0.8100 0.6849 0.1703  -0.2548 -0.2353 85  VAL E CG1 
11771 C CG2 . VAL E 85  ? 0.4357 0.8205 0.7095 0.1664  -0.2381 -0.2397 85  VAL E CG2 
11772 N N   . MET E 86  ? 0.5575 0.9233 0.7632 0.2024  -0.2745 -0.2244 86  MET E N   
11773 C CA  . MET E 86  ? 0.5781 0.9269 0.7550 0.2144  -0.2826 -0.2145 86  MET E CA  
11774 C C   . MET E 86  ? 0.5755 0.8874 0.7259 0.2137  -0.2795 -0.2062 86  MET E C   
11775 O O   . MET E 86  ? 0.5908 0.8835 0.7181 0.2256  -0.2833 -0.1937 86  MET E O   
11776 C CB  . MET E 86  ? 0.5960 0.9685 0.7709 0.2110  -0.2930 -0.2219 86  MET E CB  
11777 C CG  . MET E 86  ? 0.5937 0.9663 0.7661 0.1933  -0.2935 -0.2335 86  MET E CG  
11778 S SD  . MET E 86  ? 0.6050 0.9432 0.7366 0.1960  -0.2952 -0.2256 86  MET E SD  
11779 C CE  . MET E 86  ? 0.6151 0.9686 0.7488 0.1782  -0.3001 -0.2444 86  MET E CE  
11780 N N   . GLN E 87  ? 0.5388 0.8416 0.6931 0.2001  -0.2724 -0.2119 87  GLN E N   
11781 C CA  . GLN E 87  ? 0.5361 0.8055 0.6659 0.1990  -0.2691 -0.2039 87  GLN E CA  
11782 C C   . GLN E 87  ? 0.5344 0.7771 0.6551 0.2113  -0.2649 -0.1897 87  GLN E C   
11783 O O   . GLN E 87  ? 0.5379 0.7525 0.6363 0.2135  -0.2638 -0.1792 87  GLN E O   
11784 C CB  . GLN E 87  ? 0.5173 0.7850 0.6565 0.1821  -0.2617 -0.2132 87  GLN E CB  
11785 C CG  . GLN E 87  ? 0.5261 0.7963 0.6557 0.1698  -0.2654 -0.2228 87  GLN E CG  
11786 C CD  . GLN E 87  ? 0.5281 0.8312 0.6845 0.1583  -0.2684 -0.2386 87  GLN E CD  
11787 O OE1 . GLN E 87  ? 0.5341 0.8610 0.7052 0.1647  -0.2731 -0.2397 87  GLN E OE1 
11788 N NE2 . GLN E 87  ? 0.5249 0.8288 0.6887 0.1408  -0.2653 -0.2509 87  GLN E NE2 
11789 N N   . LEU E 88  ? 0.5420 0.7923 0.6795 0.2190  -0.2624 -0.1894 88  LEU E N   
11790 C CA  . LEU E 88  ? 0.5429 0.7663 0.6739 0.2292  -0.2581 -0.1789 88  LEU E CA  
11791 C C   . LEU E 88  ? 0.5650 0.7660 0.6741 0.2411  -0.2640 -0.1639 88  LEU E C   
11792 O O   . LEU E 88  ? 0.5688 0.7428 0.6721 0.2477  -0.2609 -0.1544 88  LEU E O   
11793 C CB  . LEU E 88  ? 0.5401 0.7781 0.6921 0.2360  -0.2547 -0.1836 88  LEU E CB  
11794 C CG  . LEU E 88  ? 0.5178 0.7703 0.6904 0.2271  -0.2449 -0.1934 88  LEU E CG  
11795 C CD1 . LEU E 88  ? 0.5197 0.7867 0.7089 0.2364  -0.2414 -0.1966 88  LEU E CD1 
11796 C CD2 . LEU E 88  ? 0.5080 0.7331 0.6704 0.2225  -0.2375 -0.1895 88  LEU E CD2 
11797 N N   . GLY E 89  ? 0.5864 0.7983 0.6843 0.2439  -0.2719 -0.1614 89  GLY E N   
11798 C CA  . GLY E 89  ? 0.6082 0.8010 0.6848 0.2550  -0.2760 -0.1449 89  GLY E CA  
11799 C C   . GLY E 89  ? 0.6092 0.7783 0.6626 0.2504  -0.2739 -0.1356 89  GLY E C   
11800 O O   . GLY E 89  ? 0.6282 0.7834 0.6635 0.2588  -0.2763 -0.1199 89  GLY E O   
11801 N N   . GLN E 90  ? 0.6036 0.7687 0.6575 0.2376  -0.2688 -0.1435 90  GLN E N   
11802 C CA  . GLN E 90  ? 0.6039 0.7479 0.6356 0.2329  -0.2661 -0.1354 90  GLN E CA  
11803 C C   . GLN E 90  ? 0.6028 0.7147 0.6312 0.2335  -0.2589 -0.1235 90  GLN E C   
11804 O O   . GLN E 90  ? 0.6163 0.7108 0.6288 0.2285  -0.2549 -0.1167 90  GLN E O   
11805 C CB  . GLN E 90  ? 0.5966 0.7529 0.6296 0.2185  -0.2646 -0.1506 90  GLN E CB  
11806 C CG  . GLN E 90  ? 0.6065 0.7810 0.6275 0.2166  -0.2715 -0.1576 90  GLN E CG  
11807 C CD  . GLN E 90  ? 0.6062 0.8144 0.6496 0.2139  -0.2768 -0.1729 90  GLN E CD  
11808 O OE1 . GLN E 90  ? 0.5926 0.8158 0.6543 0.2008  -0.2747 -0.1885 90  GLN E OE1 
11809 N NE2 . GLN E 90  ? 0.6233 0.8439 0.6667 0.2260  -0.2833 -0.1675 90  GLN E NE2 
11810 N N   . LEU E 91  ? 0.5853 0.6893 0.6283 0.2392  -0.2570 -0.1216 91  LEU E N   
11811 C CA  . LEU E 91  ? 0.5885 0.6623 0.6307 0.2389  -0.2507 -0.1123 91  LEU E CA  
11812 C C   . LEU E 91  ? 0.6032 0.6569 0.6403 0.2498  -0.2530 -0.0956 91  LEU E C   
11813 O O   . LEU E 91  ? 0.6090 0.6589 0.6598 0.2563  -0.2536 -0.0973 91  LEU E O   
11814 C CB  . LEU E 91  ? 0.5795 0.6580 0.6427 0.2359  -0.2456 -0.1252 91  LEU E CB  
11815 C CG  . LEU E 91  ? 0.5691 0.6752 0.6443 0.2261  -0.2429 -0.1416 91  LEU E CG  
11816 C CD1 . LEU E 91  ? 0.5542 0.6734 0.6520 0.2271  -0.2381 -0.1529 91  LEU E CD1 
11817 C CD2 . LEU E 91  ? 0.5808 0.6732 0.6421 0.2098  -0.2308 -0.1391 91  LEU E CD2 
11818 N N   . PRO E 92  ? 0.6325 0.6732 0.6503 0.2521  -0.2536 -0.0787 92  PRO E N   
11819 C CA  . PRO E 92  ? 0.6570 0.6821 0.6726 0.2626  -0.2553 -0.0606 92  PRO E CA  
11820 C C   . PRO E 92  ? 0.6594 0.6563 0.6876 0.2629  -0.2515 -0.0554 92  PRO E C   
11821 O O   . PRO E 92  ? 0.6772 0.6669 0.7143 0.2723  -0.2539 -0.0494 92  PRO E O   
11822 C CB  . PRO E 92  ? 0.6692 0.6868 0.6617 0.2625  -0.2537 -0.0429 92  PRO E CB  
11823 C CG  . PRO E 92  ? 0.6501 0.6659 0.6340 0.2507  -0.2491 -0.0502 92  PRO E CG  
11824 C CD  . PRO E 92  ? 0.6370 0.6754 0.6348 0.2454  -0.2513 -0.0739 92  PRO E CD  
11825 N N   . ASN E 93  ? 0.6302 0.6113 0.6597 0.2530  -0.2457 -0.0581 93  ASN E N   
11826 C CA  . ASN E 93  ? 0.6339 0.5881 0.6749 0.2516  -0.2426 -0.0550 93  ASN E CA  
11827 C C   . ASN E 93  ? 0.6227 0.5838 0.6815 0.2520  -0.2426 -0.0749 93  ASN E C   
11828 O O   . ASN E 93  ? 0.6274 0.5681 0.6959 0.2511  -0.2409 -0.0764 93  ASN E O   
11829 C CB  . ASN E 93  ? 0.6301 0.5650 0.6635 0.2410  -0.2365 -0.0469 93  ASN E CB  
11830 C CG  . ASN E 93  ? 0.6430 0.5633 0.6628 0.2419  -0.2347 -0.0224 93  ASN E CG  
11831 O OD1 . ASN E 93  ? 0.6397 0.5636 0.6428 0.2371  -0.2313 -0.0156 93  ASN E OD1 
11832 N ND2 . ASN E 93  ? 0.6663 0.5709 0.6935 0.2488  -0.2362 -0.0085 93  ASN E ND2 
11833 N N   . LEU E 94  ? 0.6200 0.6106 0.6836 0.2530  -0.2441 -0.0903 94  LEU E N   
11834 C CA  . LEU E 94  ? 0.6079 0.6098 0.6880 0.2546  -0.2427 -0.1079 94  LEU E CA  
11835 C C   . LEU E 94  ? 0.6246 0.6132 0.7140 0.2654  -0.2460 -0.1061 94  LEU E C   
11836 O O   . LEU E 94  ? 0.6417 0.6375 0.7311 0.2751  -0.2510 -0.1000 94  LEU E O   
11837 C CB  . LEU E 94  ? 0.5953 0.6337 0.6811 0.2546  -0.2440 -0.1209 94  LEU E CB  
11838 C CG  . LEU E 94  ? 0.5837 0.6405 0.6867 0.2559  -0.2406 -0.1379 94  LEU E CG  
11839 C CD1 . LEU E 94  ? 0.5812 0.6296 0.6870 0.2479  -0.2327 -0.1445 94  LEU E CD1 
11840 C CD2 . LEU E 94  ? 0.5696 0.6636 0.6807 0.2543  -0.2417 -0.1478 94  LEU E CD2 
11841 N N   . GLN E 95  ? 0.6110 0.5811 0.7083 0.2641  -0.2434 -0.1118 95  GLN E N   
11842 C CA  . GLN E 95  ? 0.6343 0.5881 0.7410 0.2738  -0.2465 -0.1122 95  GLN E CA  
11843 C C   . GLN E 95  ? 0.6308 0.6038 0.7489 0.2800  -0.2459 -0.1308 95  GLN E C   
11844 O O   . GLN E 95  ? 0.6504 0.6239 0.7750 0.2917  -0.2496 -0.1315 95  GLN E O   
11845 C CB  . GLN E 95  ? 0.6438 0.5631 0.7528 0.2687  -0.2453 -0.1073 95  GLN E CB  
11846 C CG  . GLN E 95  ? 0.6506 0.5498 0.7503 0.2630  -0.2447 -0.0861 95  GLN E CG  
11847 C CD  . GLN E 95  ? 0.6595 0.5269 0.7650 0.2562  -0.2436 -0.0818 95  GLN E CD  
11848 O OE1 . GLN E 95  ? 0.6602 0.5207 0.7756 0.2554  -0.2439 -0.0968 95  GLN E OE1 
11849 N NE2 . GLN E 95  ? 0.6677 0.5173 0.7674 0.2512  -0.2421 -0.0614 95  GLN E NE2 
11850 N N   . TYR E 96  ? 0.5386 0.7092 0.6175 0.2466  -0.0526 -0.2517 96  TYR E N   
11851 C CA  . TYR E 96  ? 0.5296 0.7328 0.6197 0.2484  -0.0568 -0.2569 96  TYR E CA  
11852 C C   . TYR E 96  ? 0.5118 0.7448 0.6159 0.2469  -0.0634 -0.2572 96  TYR E C   
11853 O O   . TYR E 96  ? 0.4977 0.7367 0.6097 0.2391  -0.0614 -0.2551 96  TYR E O   
11854 C CB  . TYR E 96  ? 0.5251 0.7375 0.6205 0.2417  -0.0519 -0.2622 96  TYR E CB  
11855 C CG  . TYR E 96  ? 0.5473 0.7316 0.6300 0.2430  -0.0451 -0.2659 96  TYR E CG  
11856 C CD1 . TYR E 96  ? 0.5540 0.7118 0.6333 0.2388  -0.0400 -0.2639 96  TYR E CD1 
11857 C CD2 . TYR E 96  ? 0.5653 0.7473 0.6404 0.2487  -0.0412 -0.2715 96  TYR E CD2 
11858 C CE1 . TYR E 96  ? 0.5771 0.7080 0.6463 0.2390  -0.0327 -0.2686 96  TYR E CE1 
11859 C CE2 . TYR E 96  ? 0.5910 0.7426 0.6526 0.2493  -0.0330 -0.2761 96  TYR E CE2 
11860 C CZ  . TYR E 96  ? 0.5964 0.7230 0.6552 0.2437  -0.0295 -0.2752 96  TYR E CZ  
11861 O OH  . TYR E 96  ? 0.6249 0.7197 0.6713 0.2431  -0.0203 -0.2810 96  TYR E OH  
11862 N N   . LEU E 97  ? 0.5063 0.7589 0.6167 0.2552  -0.0699 -0.2595 97  LEU E N   
11863 C CA  . LEU E 97  ? 0.4915 0.7768 0.6205 0.2539  -0.0759 -0.2613 97  LEU E CA  
11864 C C   . LEU E 97  ? 0.4869 0.8026 0.6309 0.2550  -0.0723 -0.2620 97  LEU E C   
11865 O O   . LEU E 97  ? 0.4984 0.8220 0.6472 0.2655  -0.0737 -0.2620 97  LEU E O   
11866 C CB  . LEU E 97  ? 0.5014 0.7878 0.6300 0.2639  -0.0879 -0.2643 97  LEU E CB  
11867 C CG  . LEU E 97  ? 0.4887 0.8050 0.6379 0.2610  -0.0956 -0.2684 97  LEU E CG  
11868 C CD1 . LEU E 97  ? 0.4788 0.7830 0.6250 0.2495  -0.0876 -0.2677 97  LEU E CD1 
11869 C CD2 . LEU E 97  ? 0.5050 0.8224 0.6519 0.2713  -0.1124 -0.2731 97  LEU E CD2 
11870 N N   . GLU E 98  ? 0.4932 0.8252 0.6446 0.2461  -0.0662 -0.2618 98  GLU E N   
11871 C CA  . GLU E 98  ? 0.4949 0.8494 0.6537 0.2474  -0.0590 -0.2630 98  GLU E CA  
11872 C C   . GLU E 98  ? 0.4798 0.8685 0.6610 0.2421  -0.0584 -0.2599 98  GLU E C   
11873 O O   . GLU E 98  ? 0.4691 0.8675 0.6527 0.2341  -0.0543 -0.2582 98  GLU E O   
11874 C CB  . GLU E 98  ? 0.4993 0.8446 0.6441 0.2433  -0.0522 -0.2671 98  GLU E CB  
11875 C CG  . GLU E 98  ? 0.5116 0.8222 0.6386 0.2438  -0.0528 -0.2697 98  GLU E CG  
11876 C CD  . GLU E 98  ? 0.5360 0.8284 0.6518 0.2534  -0.0479 -0.2724 98  GLU E CD  
11877 O OE1 . GLU E 98  ? 0.5429 0.8505 0.6668 0.2616  -0.0442 -0.2716 98  GLU E OE1 
11878 O OE2 . GLU E 98  ? 0.5503 0.8126 0.6516 0.2534  -0.0458 -0.2745 98  GLU E OE2 
11879 N N   . LEU E 99  ? 0.4584 0.8675 0.6589 0.2471  -0.0624 -0.2582 99  LEU E N   
11880 C CA  . LEU E 99  ? 0.4471 0.8911 0.6747 0.2412  -0.0608 -0.2544 99  LEU E CA  
11881 C C   . LEU E 99  ? 0.4557 0.9236 0.6996 0.2474  -0.0507 -0.2512 99  LEU E C   
11882 O O   . LEU E 99  ? 0.4500 0.9495 0.7232 0.2441  -0.0493 -0.2462 99  LEU E O   
11883 C CB  . LEU E 99  ? 0.4420 0.8975 0.6874 0.2396  -0.0748 -0.2549 99  LEU E CB  
11884 C CG  . LEU E 99  ? 0.4332 0.8747 0.6718 0.2319  -0.0796 -0.2580 99  LEU E CG  
11885 C CD1 . LEU E 99  ? 0.4441 0.8516 0.6591 0.2397  -0.0877 -0.2631 99  LEU E CD1 
11886 C CD2 . LEU E 99  ? 0.4253 0.8963 0.6932 0.2242  -0.0874 -0.2589 99  LEU E CD2 
11887 N N   . TYR E 100 ? 0.5076 0.9599 0.7346 0.2562  -0.0418 -0.2538 100 TYR E N   
11888 C CA  . TYR E 100 ? 0.5226 0.9911 0.7632 0.2658  -0.0285 -0.2509 100 TYR E CA  
11889 C C   . TYR E 100 ? 0.5193 1.0122 0.7698 0.2602  -0.0149 -0.2487 100 TYR E C   
11890 O O   . TYR E 100 ? 0.5090 1.0014 0.7480 0.2504  -0.0149 -0.2505 100 TYR E O   
11891 C CB  . TYR E 100 ? 0.5469 0.9858 0.7616 0.2762  -0.0194 -0.2562 100 TYR E CB  
11892 C CG  . TYR E 100 ? 0.5517 0.9689 0.7343 0.2695  -0.0153 -0.2649 100 TYR E CG  
11893 C CD1 . TYR E 100 ? 0.5633 0.9891 0.7364 0.2688  -0.0011 -0.2689 100 TYR E CD1 
11894 C CD2 . TYR E 100 ? 0.5479 0.9377 0.7106 0.2644  -0.0255 -0.2690 100 TYR E CD2 
11895 C CE1 . TYR E 100 ? 0.5714 0.9819 0.7150 0.2631  -0.0003 -0.2783 100 TYR E CE1 
11896 C CE2 . TYR E 100 ? 0.5529 0.9289 0.6928 0.2582  -0.0236 -0.2767 100 TYR E CE2 
11897 C CZ  . TYR E 100 ? 0.5648 0.9527 0.6948 0.2576  -0.0127 -0.2822 100 TYR E CZ  
11898 O OH  . TYR E 100 ? 0.5736 0.9519 0.6798 0.2518  -0.0136 -0.2921 100 TYR E OH  
11899 N N   . SER E 101 ? 0.5203 1.0354 0.7943 0.2680  -0.0018 -0.2431 101 SER E N   
11900 C CA  . SER E 101 ? 0.5251 1.0617 0.8076 0.2659  0.0163  -0.2402 101 SER E CA  
11901 C C   . SER E 101 ? 0.5024 1.0623 0.8032 0.2512  0.0110  -0.2354 101 SER E C   
11902 O O   . SER E 101 ? 0.4991 1.0576 0.7825 0.2444  0.0161  -0.2373 101 SER E O   
11903 C CB  . SER E 101 ? 0.5454 1.0596 0.7873 0.2688  0.0293  -0.2497 101 SER E CB  
11904 O OG  . SER E 101 ? 0.5736 1.0649 0.8005 0.2820  0.0394  -0.2542 101 SER E OG  
11905 N N   . ASN E 102 ? 0.4853 1.0677 0.8223 0.2465  0.0005  -0.2288 102 ASN E N   
11906 C CA  . ASN E 102 ? 0.4684 1.0736 0.8285 0.2319  -0.0028 -0.2243 102 ASN E CA  
11907 C C   . ASN E 102 ? 0.4673 1.1101 0.8781 0.2299  -0.0043 -0.2155 102 ASN E C   
11908 O O   . ASN E 102 ? 0.4791 1.1310 0.9076 0.2415  -0.0024 -0.2112 102 ASN E O   
11909 C CB  . ASN E 102 ? 0.4533 1.0400 0.7989 0.2225  -0.0211 -0.2294 102 ASN E CB  
11910 C CG  . ASN E 102 ? 0.4505 1.0134 0.7611 0.2197  -0.0170 -0.2330 102 ASN E CG  
11911 O OD1 . ASN E 102 ? 0.4473 1.0221 0.7598 0.2138  -0.0065 -0.2289 102 ASN E OD1 
11912 N ND2 . ASN E 102 ? 0.4532 0.9847 0.7344 0.2243  -0.0253 -0.2394 102 ASN E ND2 
11913 N N   . ASN E 103 ? 0.3911 1.0573 0.8287 0.2149  -0.0073 -0.2120 103 ASN E N   
11914 C CA  . ASN E 103 ? 0.3899 1.0968 0.8814 0.2079  -0.0109 -0.2035 103 ASN E CA  
11915 C C   . ASN E 103 ? 0.3813 1.0934 0.8858 0.1962  -0.0388 -0.2081 103 ASN E C   
11916 O O   . ASN E 103 ? 0.3768 1.1188 0.9191 0.1801  -0.0457 -0.2053 103 ASN E O   
11917 C CB  . ASN E 103 ? 0.3879 1.1211 0.9052 0.1974  0.0083  -0.1965 103 ASN E CB  
11918 C CG  . ASN E 103 ? 0.3923 1.1704 0.9704 0.1931  0.0117  -0.1849 103 ASN E CG  
11919 O OD1 . ASN E 103 ? 0.4030 1.1924 1.0008 0.2059  0.0126  -0.1785 103 ASN E OD1 
11920 N ND2 . ASN E 103 ? 0.3858 1.1906 0.9975 0.1747  0.0145  -0.1811 103 ASN E ND2 
11921 N N   . ILE E 104 ? 0.4576 1.1396 0.9296 0.2031  -0.0548 -0.2161 104 ILE E N   
11922 C CA  . ILE E 104 ? 0.4554 1.1360 0.9295 0.1937  -0.0813 -0.2228 104 ILE E CA  
11923 C C   . ILE E 104 ? 0.4666 1.1767 0.9762 0.1953  -0.0986 -0.2156 104 ILE E C   
11924 O O   . ILE E 104 ? 0.4767 1.1871 0.9885 0.2124  -0.0944 -0.2088 104 ILE E O   
11925 C CB  . ILE E 104 ? 0.4559 1.0921 0.8815 0.2023  -0.0893 -0.2330 104 ILE E CB  
11926 C CG1 . ILE E 104 ? 0.4498 1.0584 0.8421 0.2052  -0.0697 -0.2349 104 ILE E CG1 
11927 C CG2 . ILE E 104 ? 0.4546 1.0848 0.8765 0.1906  -0.1113 -0.2426 104 ILE E CG2 
11928 C CD1 . ILE E 104 ? 0.4520 1.0183 0.8016 0.2134  -0.0745 -0.2424 104 ILE E CD1 
11929 N N   . THR E 105 ? 0.4244 1.1595 0.9629 0.1766  -0.1188 -0.2165 105 THR E N   
11930 C CA  . THR E 105 ? 0.4387 1.2063 1.0144 0.1731  -0.1404 -0.2076 105 THR E CA  
11931 C C   . THR E 105 ? 0.4521 1.2025 1.0032 0.1655  -0.1739 -0.2174 105 THR E C   
11932 O O   . THR E 105 ? 0.4491 1.1621 0.9566 0.1656  -0.1774 -0.2313 105 THR E O   
11933 C CB  . THR E 105 ? 0.4381 1.2526 1.0712 0.1531  -0.1385 -0.1986 105 THR E CB  
11934 O OG1 . THR E 105 ? 0.4550 1.3035 1.1270 0.1481  -0.1628 -0.1875 105 THR E OG1 
11935 C CG2 . THR E 105 ? 0.4325 1.2429 1.0624 0.1270  -0.1448 -0.2113 105 THR E CG2 
11936 N N   . GLY E 106 ? 0.4961 1.2741 1.0753 0.1590  -0.1990 -0.2088 106 GLY E N   
11937 C CA  . GLY E 106 ? 0.5195 1.2804 1.0709 0.1505  -0.2337 -0.2162 106 GLY E CA  
11938 C C   . GLY E 106 ? 0.5330 1.2754 1.0589 0.1759  -0.2416 -0.2109 106 GLY E C   
11939 O O   . GLY E 106 ? 0.5268 1.2762 1.0661 0.1984  -0.2228 -0.2000 106 GLY E O   
11940 N N   . THR E 107 ? 0.5306 1.2450 1.0158 0.1714  -0.2695 -0.2195 107 THR E N   
11941 C CA  . THR E 107 ? 0.5499 1.2443 1.0069 0.1938  -0.2810 -0.2147 107 THR E CA  
11942 C C   . THR E 107 ? 0.5407 1.1831 0.9435 0.2113  -0.2661 -0.2285 107 THR E C   
11943 O O   . THR E 107 ? 0.5244 1.1430 0.9072 0.2031  -0.2507 -0.2406 107 THR E O   
11944 C CB  . THR E 107 ? 0.5915 1.2836 1.0309 0.1786  -0.3218 -0.2132 107 THR E CB  
11945 O OG1 . THR E 107 ? 0.6121 1.2995 1.0404 0.2022  -0.3324 -0.2014 107 THR E OG1 
11946 C CG2 . THR E 107 ? 0.6095 1.2507 0.9866 0.1629  -0.3348 -0.2344 107 THR E CG2 
11947 N N   . ILE E 108 ? 0.5628 1.1857 0.9429 0.2349  -0.2690 -0.2239 108 ILE E N   
11948 C CA  . ILE E 108 ? 0.5601 1.1336 0.8903 0.2521  -0.2578 -0.2352 108 ILE E CA  
11949 C C   . ILE E 108 ? 0.6003 1.1262 0.8725 0.2402  -0.2804 -0.2405 108 ILE E C   
11950 O O   . ILE E 108 ? 0.6312 1.1684 0.9005 0.2421  -0.3099 -0.2336 108 ILE E O   
11951 C CB  . ILE E 108 ? 0.5633 1.1272 0.8916 0.2807  -0.2419 -0.2263 108 ILE E CB  
11952 C CG1 . ILE E 108 ? 0.5376 1.1079 0.8865 0.2862  -0.2062 -0.2243 108 ILE E CG1 
11953 C CG2 . ILE E 108 ? 0.5767 1.0892 0.8512 0.2972  -0.2433 -0.2354 108 ILE E CG2 
11954 C CD1 . ILE E 108 ? 0.5240 1.1405 0.9239 0.2726  -0.1985 -0.2154 108 ILE E CD1 
11955 N N   . PRO E 109 ? 0.6161 1.0861 0.8392 0.2276  -0.2665 -0.2508 109 PRO E N   
11956 C CA  . PRO E 109 ? 0.6630 1.0801 0.8250 0.2140  -0.2829 -0.2559 109 PRO E CA  
11957 C C   . PRO E 109 ? 0.6901 1.0721 0.8113 0.2370  -0.2878 -0.2524 109 PRO E C   
11958 O O   . PRO E 109 ? 0.6748 1.0322 0.7841 0.2557  -0.2642 -0.2533 109 PRO E O   
11959 C CB  . PRO E 109 ? 0.6753 1.0454 0.8061 0.1991  -0.2576 -0.2655 109 PRO E CB  
11960 C CG  . PRO E 109 ? 0.6195 1.0225 0.7960 0.2049  -0.2318 -0.2643 109 PRO E CG  
11961 C CD  . PRO E 109 ? 0.5856 1.0353 0.8039 0.2284  -0.2337 -0.2567 109 PRO E CD  
11962 N N   . GLU E 110 ? 0.7194 1.0990 0.8185 0.2344  -0.3197 -0.2476 110 GLU E N   
11963 C CA  . GLU E 110 ? 0.7540 1.0971 0.8090 0.2560  -0.3262 -0.2423 110 GLU E CA  
11964 C C   . GLU E 110 ? 0.7764 1.0411 0.7632 0.2546  -0.3046 -0.2511 110 GLU E C   
11965 O O   . GLU E 110 ? 0.8046 1.0331 0.7566 0.2748  -0.2990 -0.2471 110 GLU E O   
11966 C CB  . GLU E 110 ? 0.8045 1.1594 0.8436 0.2499  -0.3681 -0.2347 110 GLU E CB  
11967 C CG  . GLU E 110 ? 0.8553 1.1634 0.8338 0.2192  -0.3836 -0.2450 110 GLU E CG  
11968 C CD  . GLU E 110 ? 0.9132 1.2312 0.8694 0.2110  -0.4290 -0.2377 110 GLU E CD  
11969 O OE1 . GLU E 110 ? 0.9016 1.2865 0.9146 0.2211  -0.4527 -0.2238 110 GLU E OE1 
11970 O OE2 . GLU E 110 ? 0.9743 1.2329 0.8553 0.1946  -0.4408 -0.2452 110 GLU E OE2 
11971 N N   . GLN E 111 ? 0.7944 1.0316 0.7638 0.2320  -0.2903 -0.2615 111 GLN E N   
11972 C CA  . GLN E 111 ? 0.8347 1.0021 0.7500 0.2318  -0.2645 -0.2679 111 GLN E CA  
11973 C C   . GLN E 111 ? 0.8109 0.9766 0.7478 0.2506  -0.2327 -0.2670 111 GLN E C   
11974 O O   . GLN E 111 ? 0.8355 0.9484 0.7356 0.2539  -0.2105 -0.2696 111 GLN E O   
11975 C CB  . GLN E 111 ? 0.8504 0.9913 0.7466 0.2038  -0.2565 -0.2773 111 GLN E CB  
11976 C CG  . GLN E 111 ? 0.8997 1.0088 0.7435 0.1830  -0.2828 -0.2820 111 GLN E CG  
11977 C CD  . GLN E 111 ? 0.9457 1.0225 0.7368 0.1972  -0.3008 -0.2771 111 GLN E CD  
11978 O OE1 . GLN E 111 ? 0.9552 1.0626 0.7505 0.1961  -0.3361 -0.2715 111 GLN E OE1 
11979 N NE2 . GLN E 111 ? 0.9704 0.9857 0.7127 0.2105  -0.2765 -0.2776 111 GLN E NE2 
11980 N N   . LEU E 112 ? 0.7794 1.0002 0.7742 0.2619  -0.2293 -0.2632 112 LEU E N   
11981 C CA  . LEU E 112 ? 0.7528 0.9706 0.7631 0.2786  -0.2028 -0.2634 112 LEU E CA  
11982 C C   . LEU E 112 ? 0.7813 0.9643 0.7611 0.3009  -0.1993 -0.2593 112 LEU E C   
11983 O O   . LEU E 112 ? 0.7554 0.9214 0.7367 0.3115  -0.1764 -0.2608 112 LEU E O   
11984 C CB  . LEU E 112 ? 0.6742 0.9538 0.7457 0.2854  -0.1998 -0.2612 112 LEU E CB  
11985 C CG  . LEU E 112 ? 0.6319 0.9326 0.7328 0.2716  -0.1825 -0.2655 112 LEU E CG  
11986 C CD1 . LEU E 112 ? 0.6710 0.9567 0.7566 0.2463  -0.1866 -0.2689 112 LEU E CD1 
11987 C CD2 . LEU E 112 ? 0.5795 0.9420 0.7360 0.2768  -0.1835 -0.2622 112 LEU E CD2 
11988 N N   . GLY E 113 ? 0.7948 0.9664 0.7465 0.3074  -0.2221 -0.2534 113 GLY E N   
11989 C CA  . GLY E 113 ? 0.8283 0.9577 0.7422 0.3278  -0.2176 -0.2482 113 GLY E CA  
11990 C C   . GLY E 113 ? 0.8884 0.9485 0.7473 0.3228  -0.1978 -0.2524 113 GLY E C   
11991 O O   . GLY E 113 ? 0.9096 0.9307 0.7395 0.3394  -0.1869 -0.2482 113 GLY E O   
11992 N N   . ASN E 114 ? 0.9188 0.9613 0.7642 0.3012  -0.1904 -0.2595 114 ASN E N   
11993 C CA  . ASN E 114 ? 0.9208 0.8993 0.7208 0.2971  -0.1664 -0.2622 114 ASN E CA  
11994 C C   . ASN E 114 ? 0.8535 0.8306 0.6823 0.3016  -0.1358 -0.2634 114 ASN E C   
11995 O O   . ASN E 114 ? 0.8534 0.7818 0.6544 0.3016  -0.1131 -0.2630 114 ASN E O   
11996 C CB  . ASN E 114 ? 0.9331 0.8894 0.7066 0.2733  -0.1682 -0.2683 114 ASN E CB  
11997 C CG  . ASN E 114 ? 1.0022 0.9397 0.7273 0.2654  -0.1973 -0.2685 114 ASN E CG  
11998 O OD1 . ASN E 114 ? 1.0219 0.9818 0.7481 0.2768  -0.2223 -0.2623 114 ASN E OD1 
11999 N ND2 . ASN E 114 ? 1.0244 0.9196 0.7057 0.2457  -0.1945 -0.2752 114 ASN E ND2 
12000 N N   . LEU E 115 ? 0.9770 0.7932 0.6386 0.3986  -0.3410 -0.2752 115 LEU E N   
12001 C CA  . LEU E 115 ? 0.9710 0.7721 0.6295 0.3854  -0.3288 -0.2563 115 LEU E CA  
12002 C C   . LEU E 115 ? 0.9965 0.7667 0.6169 0.3951  -0.3354 -0.2330 115 LEU E C   
12003 O O   . LEU E 115 ? 0.9772 0.7407 0.6172 0.3924  -0.3444 -0.2341 115 LEU E O   
12004 C CB  . LEU E 115 ? 0.9189 0.7431 0.6361 0.3643  -0.3256 -0.2665 115 LEU E CB  
12005 C CG  . LEU E 115 ? 0.8827 0.7362 0.6403 0.3460  -0.3167 -0.2833 115 LEU E CG  
12006 C CD1 . LEU E 115 ? 0.8376 0.7124 0.6423 0.3238  -0.3095 -0.2898 115 LEU E CD1 
12007 C CD2 . LEU E 115 ? 0.9127 0.7504 0.6461 0.3417  -0.3017 -0.2760 115 LEU E CD2 
12008 N N   . THR E 116 ? 1.0229 0.7756 0.5899 0.4050  -0.3289 -0.2084 116 THR E N   
12009 C CA  . THR E 116 ? 1.0627 0.7883 0.5980 0.4093  -0.3320 -0.1757 116 THR E CA  
12010 C C   . THR E 116 ? 1.0360 0.7475 0.5992 0.3901  -0.3294 -0.1537 116 THR E C   
12011 O O   . THR E 116 ? 1.0530 0.7440 0.6210 0.3880  -0.3410 -0.1464 116 THR E O   
12012 C CB  . THR E 116 ? 1.1117 0.8290 0.5887 0.4220  -0.3186 -0.1465 116 THR E CB  
12013 O OG1 . THR E 116 ? 1.1508 0.8757 0.5950 0.4412  -0.3241 -0.1690 116 THR E OG1 
12014 C CG2 . THR E 116 ? 1.1542 0.8436 0.6060 0.4204  -0.3181 -0.1031 116 THR E CG2 
12015 N N   . GLU E 117 ? 1.0309 0.7511 0.6143 0.3767  -0.3165 -0.1443 117 GLU E N   
12016 C CA  . GLU E 117 ? 1.0104 0.7161 0.6203 0.3573  -0.3142 -0.1209 117 GLU E CA  
12017 C C   . GLU E 117 ? 0.9773 0.6889 0.6258 0.3459  -0.3241 -0.1488 117 GLU E C   
12018 O O   . GLU E 117 ? 0.9639 0.6633 0.6319 0.3300  -0.3250 -0.1360 117 GLU E O   
12019 C CB  . GLU E 117 ? 1.0131 0.7295 0.6371 0.3414  -0.2877 -0.0964 117 GLU E CB  
12020 C CG  . GLU E 117 ? 1.0245 0.7220 0.6603 0.3242  -0.2837 -0.0555 117 GLU E CG  
12021 C CD  . GLU E 117 ? 1.0584 0.7395 0.6571 0.3340  -0.2790 -0.0194 117 GLU E CD  
12022 O OE1 . GLU E 117 ? 1.0843 0.7681 0.6397 0.3567  -0.2793 -0.0269 117 GLU E OE1 
12023 O OE2 . GLU E 117 ? 1.0777 0.7429 0.6896 0.3176  -0.2761 0.0175  117 GLU E OE2 
12024 N N   . LEU E 118 ? 0.9647 0.6964 0.6251 0.3545  -0.3318 -0.1862 118 LEU E N   
12025 C CA  . LEU E 118 ? 0.9385 0.6836 0.6347 0.3475  -0.3376 -0.2122 118 LEU E CA  
12026 C C   . LEU E 118 ? 0.9415 0.6595 0.6386 0.3484  -0.3505 -0.2086 118 LEU E C   
12027 O O   . LEU E 118 ? 0.9749 0.6724 0.6535 0.3599  -0.3608 -0.2033 118 LEU E O   
12028 C CB  . LEU E 118 ? 0.9214 0.6998 0.6443 0.3575  -0.3397 -0.2450 118 LEU E CB  
12029 C CG  . LEU E 118 ? 0.8830 0.6974 0.6559 0.3442  -0.3337 -0.2623 118 LEU E CG  
12030 C CD1 . LEU E 118 ? 0.8686 0.6864 0.6474 0.3183  -0.3149 -0.2542 118 LEU E CD1 
12031 C CD2 . LEU E 118 ? 0.8576 0.7159 0.6674 0.3486  -0.3354 -0.2854 118 LEU E CD2 
12032 N N   . VAL E 119 ? 0.9264 0.6419 0.6416 0.3368  -0.3522 -0.2127 119 VAL E N   
12033 C CA  . VAL E 119 ? 0.9520 0.6368 0.6666 0.3383  -0.3672 -0.2138 119 VAL E CA  
12034 C C   . VAL E 119 ? 0.9394 0.6477 0.6807 0.3491  -0.3735 -0.2489 119 VAL E C   
12035 O O   . VAL E 119 ? 0.9647 0.6701 0.7085 0.3604  -0.3889 -0.2606 119 VAL E O   
12036 C CB  . VAL E 119 ? 0.9555 0.6119 0.6673 0.3181  -0.3671 -0.1838 119 VAL E CB  
12037 C CG1 . VAL E 119 ? 0.9796 0.6064 0.6946 0.3193  -0.3859 -0.1969 119 VAL E CG1 
12038 C CG2 . VAL E 119 ? 0.9816 0.6149 0.6767 0.3119  -0.3626 -0.1435 119 VAL E CG2 
12039 N N   . SER E 120 ? 0.9367 0.6876 0.7042 0.3293  -0.3499 -0.2546 120 SER E N   
12040 C CA  . SER E 120 ? 0.9017 0.6943 0.7021 0.3263  -0.3391 -0.2757 120 SER E CA  
12041 C C   . SER E 120 ? 0.8635 0.7071 0.6930 0.3199  -0.3224 -0.2884 120 SER E C   
12042 O O   . SER E 120 ? 0.8562 0.7026 0.6820 0.3038  -0.3094 -0.2789 120 SER E O   
12043 C CB  . SER E 120 ? 0.9020 0.6860 0.6967 0.3063  -0.3282 -0.2734 120 SER E CB  
12044 O OG  . SER E 120 ? 0.8775 0.7022 0.6944 0.3043  -0.3136 -0.2959 120 SER E OG  
12045 N N   . LEU E 121 ? 0.8292 0.7113 0.6894 0.3329  -0.3259 -0.3120 121 LEU E N   
12046 C CA  . LEU E 121 ? 0.8067 0.7376 0.7015 0.3267  -0.3152 -0.3302 121 LEU E CA  
12047 C C   . LEU E 121 ? 0.8047 0.7754 0.7285 0.3236  -0.3026 -0.3558 121 LEU E C   
12048 O O   . LEU E 121 ? 0.8200 0.8128 0.7652 0.3444  -0.3145 -0.3762 121 LEU E O   
12049 C CB  . LEU E 121 ? 0.8177 0.7604 0.7239 0.3492  -0.3361 -0.3393 121 LEU E CB  
12050 C CG  . LEU E 121 ? 0.8024 0.7798 0.7365 0.3420  -0.3321 -0.3531 121 LEU E CG  
12051 C CD1 . LEU E 121 ? 0.8267 0.7978 0.7544 0.3679  -0.3560 -0.3565 121 LEU E CD1 
12052 C CD2 . LEU E 121 ? 0.7892 0.8218 0.7735 0.3346  -0.3233 -0.3845 121 LEU E CD2 
12053 N N   . ASP E 122 ? 0.7961 0.7758 0.7175 0.2997  -0.2793 -0.3566 122 ASP E N   
12054 C CA  . ASP E 122 ? 0.8035 0.8186 0.7404 0.2961  -0.2620 -0.3813 122 ASP E CA  
12055 C C   . ASP E 122 ? 0.7879 0.8481 0.7580 0.2810  -0.2467 -0.4021 122 ASP E C   
12056 O O   . ASP E 122 ? 0.7814 0.8337 0.7371 0.2573  -0.2326 -0.3948 122 ASP E O   
12057 C CB  . ASP E 122 ? 0.8176 0.8033 0.7147 0.2820  -0.2499 -0.3690 122 ASP E CB  
12058 C CG  . ASP E 122 ? 0.8420 0.7871 0.7153 0.2965  -0.2667 -0.3582 122 ASP E CG  
12059 O OD1 . ASP E 122 ? 0.8478 0.7803 0.7291 0.3164  -0.2881 -0.3551 122 ASP E OD1 
12060 O OD2 . ASP E 122 ? 0.8622 0.7853 0.7059 0.2880  -0.2613 -0.3543 122 ASP E OD2 
12061 N N   . LEU E 123 ? 0.8326 0.8927 0.7384 0.4730  -0.2463 -0.1796 123 LEU E N   
12062 C CA  . LEU E 123 ? 0.8218 0.9042 0.7538 0.4724  -0.2447 -0.1837 123 LEU E CA  
12063 C C   . LEU E 123 ? 0.8172 0.9203 0.7705 0.4754  -0.2416 -0.1860 123 LEU E C   
12064 O O   . LEU E 123 ? 0.8113 0.9349 0.7920 0.4759  -0.2424 -0.1883 123 LEU E O   
12065 C CB  . LEU E 123 ? 0.8340 0.9116 0.7650 0.4749  -0.2575 -0.1893 123 LEU E CB  
12066 C CG  . LEU E 123 ? 0.8370 0.9031 0.7576 0.4738  -0.2580 -0.1882 123 LEU E CG  
12067 C CD1 . LEU E 123 ? 0.8366 0.8853 0.7343 0.4720  -0.2484 -0.1789 123 LEU E CD1 
12068 C CD2 . LEU E 123 ? 0.8601 0.9115 0.7670 0.4796  -0.2743 -0.1946 123 LEU E CD2 
12069 N N   . TYR E 124 ? 0.8395 0.9365 0.7811 0.4785  -0.2386 -0.1847 124 TYR E N   
12070 C CA  . TYR E 124 ? 0.8421 0.9543 0.7972 0.4849  -0.2351 -0.1862 124 TYR E CA  
12071 C C   . TYR E 124 ? 0.8265 0.9618 0.8055 0.4840  -0.2211 -0.1823 124 TYR E C   
12072 O O   . TYR E 124 ? 0.8142 0.9503 0.7939 0.4782  -0.2138 -0.1788 124 TYR E O   
12073 C CB  . TYR E 124 ? 0.8577 0.9514 0.7877 0.4902  -0.2370 -0.1866 124 TYR E CB  
12074 C CG  . TYR E 124 ? 0.8562 0.9375 0.7699 0.4880  -0.2311 -0.1828 124 TYR E CG  
12075 C CD1 . TYR E 124 ? 0.8494 0.9434 0.7710 0.4900  -0.2194 -0.1804 124 TYR E CD1 
12076 C CD2 . TYR E 124 ? 0.8634 0.9201 0.7552 0.4843  -0.2378 -0.1803 124 TYR E CD2 
12077 C CE1 . TYR E 124 ? 0.8511 0.9321 0.7565 0.4886  -0.2166 -0.1775 124 TYR E CE1 
12078 C CE2 . TYR E 124 ? 0.8635 0.9088 0.7441 0.4820  -0.2351 -0.1761 124 TYR E CE2 
12079 C CZ  . TYR E 124 ? 0.8578 0.9146 0.7441 0.4843  -0.2255 -0.1755 124 TYR E CZ  
12080 O OH  . TYR E 124 ? 0.8607 0.9046 0.7347 0.4827  -0.2252 -0.1718 124 TYR E OH  
12081 N N   . LEU E 125 ? 0.8248 0.9794 0.8242 0.4907  -0.2163 -0.1815 125 LEU E N   
12082 C CA  . LEU E 125 ? 0.8133 0.9919 0.8384 0.4919  -0.2012 -0.1758 125 LEU E CA  
12083 C C   . LEU E 125 ? 0.7955 0.9895 0.8479 0.4836  -0.1996 -0.1739 125 LEU E C   
12084 O O   . LEU E 125 ? 0.7836 0.9804 0.8375 0.4790  -0.1896 -0.1703 125 LEU E O   
12085 C CB  . LEU E 125 ? 0.8159 0.9847 0.8191 0.4943  -0.1904 -0.1729 125 LEU E CB  
12086 C CG  . LEU E 125 ? 0.8368 0.9972 0.8210 0.5064  -0.1882 -0.1737 125 LEU E CG  
12087 C CD1 . LEU E 125 ? 0.8468 0.9831 0.7963 0.5076  -0.1882 -0.1746 125 LEU E CD1 
12088 C CD2 . LEU E 125 ? 0.8378 1.0236 0.8476 0.5151  -0.1735 -0.1675 125 LEU E CD2 
12089 N N   . ASN E 126 ? 0.8390 1.0419 0.9127 0.4825  -0.2111 -0.1768 126 ASN E N   
12090 C CA  . ASN E 126 ? 0.8275 1.0422 0.9273 0.4759  -0.2145 -0.1768 126 ASN E CA  
12091 C C   . ASN E 126 ? 0.8289 1.0676 0.9703 0.4783  -0.2218 -0.1756 126 ASN E C   
12092 O O   . ASN E 126 ? 0.8360 1.0852 0.9878 0.4853  -0.2200 -0.1727 126 ASN E O   
12093 C CB  . ASN E 126 ? 0.8332 1.0231 0.9067 0.4713  -0.2275 -0.1831 126 ASN E CB  
12094 C CG  . ASN E 126 ? 0.8259 1.0011 0.8753 0.4669  -0.2176 -0.1803 126 ASN E CG  
12095 O OD1 . ASN E 126 ? 0.8125 0.9984 0.8769 0.4629  -0.2079 -0.1767 126 ASN E OD1 
12096 N ND2 . ASN E 126 ? 0.8353 0.9866 0.8497 0.4677  -0.2203 -0.1809 126 ASN E ND2 
12097 N N   . ASN E 127 ? 0.8503 1.0971 1.0169 0.4728  -0.2314 -0.1773 127 ASN E N   
12098 C CA  . ASN E 127 ? 0.8563 1.1251 1.0672 0.4730  -0.2434 -0.1760 127 ASN E CA  
12099 C C   . ASN E 127 ? 0.8671 1.1177 1.0683 0.4701  -0.2691 -0.1861 127 ASN E C   
12100 O O   . ASN E 127 ? 0.8705 1.1334 1.1070 0.4667  -0.2837 -0.1869 127 ASN E O   
12101 C CB  . ASN E 127 ? 0.8371 1.1357 1.0966 0.4695  -0.2332 -0.1671 127 ASN E CB  
12102 C CG  . ASN E 127 ? 0.8409 1.1708 1.1544 0.4720  -0.2372 -0.1590 127 ASN E CG  
12103 O OD1 . ASN E 127 ? 0.8363 1.1838 1.1938 0.4664  -0.2471 -0.1563 127 ASN E OD1 
12104 N ND2 . ASN E 127 ? 0.8446 1.1813 1.1570 0.4805  -0.2304 -0.1541 127 ASN E ND2 
12105 N N   . LEU E 128 ? 0.9030 1.1224 1.0559 0.4719  -0.2755 -0.1932 128 LEU E N   
12106 C CA  . LEU E 128 ? 0.9237 1.1201 1.0573 0.4718  -0.2985 -0.2025 128 LEU E CA  
12107 C C   . LEU E 128 ? 0.9370 1.1421 1.0915 0.4746  -0.3162 -0.2045 128 LEU E C   
12108 O O   . LEU E 128 ? 0.9377 1.1584 1.1057 0.4788  -0.3090 -0.1993 128 LEU E O   
12109 C CB  . LEU E 128 ? 0.9372 1.1002 1.0157 0.4745  -0.2973 -0.2061 128 LEU E CB  
12110 C CG  . LEU E 128 ? 0.9324 1.0853 0.9894 0.4716  -0.2806 -0.2024 128 LEU E CG  
12111 C CD1 . LEU E 128 ? 0.9308 1.0599 0.9453 0.4740  -0.2752 -0.2010 128 LEU E CD1 
12112 C CD2 . LEU E 128 ? 0.9356 1.0757 0.9868 0.4697  -0.2882 -0.2062 128 LEU E CD2 
12113 N N   . SER E 129 ? 0.9114 1.1042 1.0669 0.4731  -0.3402 -0.2119 129 SER E N   
12114 C CA  . SER E 129 ? 0.9278 1.1273 1.1045 0.4745  -0.3606 -0.2139 129 SER E CA  
12115 C C   . SER E 129 ? 0.9589 1.1219 1.0922 0.4777  -0.3828 -0.2247 129 SER E C   
12116 O O   . SER E 129 ? 0.9671 1.1007 1.0532 0.4803  -0.3791 -0.2289 129 SER E O   
12117 C CB  . SER E 129 ? 0.9226 1.1497 1.1591 0.4680  -0.3719 -0.2100 129 SER E CB  
12118 O OG  . SER E 129 ? 0.9364 1.1437 1.1655 0.4634  -0.3911 -0.2183 129 SER E OG  
12119 N N   . GLY E 130 ? 0.9809 1.1450 1.1297 0.4781  -0.4051 -0.2279 130 GLY E N   
12120 C CA  . GLY E 130 ? 1.0153 1.1436 1.1218 0.4824  -0.4266 -0.2378 130 GLY E CA  
12121 C C   . GLY E 130 ? 1.0232 1.1360 1.0905 0.4901  -0.4182 -0.2378 130 GLY E C   
12122 O O   . GLY E 130 ? 1.0043 1.1349 1.0813 0.4918  -0.3995 -0.2308 130 GLY E O   
12123 N N   . PRO E 131 ? 1.0203 1.0974 1.0411 0.4957  -0.4323 -0.2454 131 PRO E N   
12124 C CA  . PRO E 131 ? 1.0307 1.0922 1.0166 0.5030  -0.4262 -0.2447 131 PRO E CA  
12125 C C   . PRO E 131 ? 1.0222 1.0664 0.9687 0.5054  -0.4052 -0.2412 131 PRO E C   
12126 O O   . PRO E 131 ? 1.0074 1.0522 0.9525 0.5019  -0.3942 -0.2391 131 PRO E O   
12127 C CB  . PRO E 131 ? 1.0719 1.1027 1.0279 0.5084  -0.4513 -0.2533 131 PRO E CB  
12128 C CG  . PRO E 131 ? 1.0865 1.1022 1.0376 0.5056  -0.4660 -0.2595 131 PRO E CG  
12129 C CD  . PRO E 131 ? 1.0516 1.0976 1.0457 0.4970  -0.4538 -0.2544 131 PRO E CD  
12130 N N   . ILE E 132 ? 1.0184 1.0474 0.9353 0.5111  -0.4002 -0.2396 132 ILE E N   
12131 C CA  . ILE E 132 ? 1.0170 1.0256 0.8956 0.5133  -0.3841 -0.2348 132 ILE E CA  
12132 C C   . ILE E 132 ? 1.0528 1.0246 0.8849 0.5212  -0.3951 -0.2383 132 ILE E C   
12133 O O   . ILE E 132 ? 1.0759 1.0350 0.8924 0.5272  -0.4055 -0.2408 132 ILE E O   
12134 C CB  . ILE E 132 ? 1.0072 1.0212 0.8843 0.5144  -0.3716 -0.2293 132 ILE E CB  
12135 C CG1 . ILE E 132 ? 0.9762 1.0206 0.8888 0.5090  -0.3569 -0.2248 132 ILE E CG1 
12136 C CG2 . ILE E 132 ? 1.0141 1.0022 0.8513 0.5167  -0.3607 -0.2236 132 ILE E CG2 
12137 C CD1 . ILE E 132 ? 0.9688 1.0433 0.9264 0.5082  -0.3636 -0.2260 132 ILE E CD1 
12138 N N   . PRO E 133 ? 1.0339 0.9870 0.8418 0.5228  -0.3930 -0.2381 133 PRO E N   
12139 C CA  . PRO E 133 ? 1.0749 0.9907 0.8356 0.5330  -0.4040 -0.2414 133 PRO E CA  
12140 C C   . PRO E 133 ? 1.0908 0.9878 0.8186 0.5400  -0.3971 -0.2354 133 PRO E C   
12141 O O   . PRO E 133 ? 1.0710 0.9743 0.8000 0.5370  -0.3793 -0.2260 133 PRO E O   
12142 C CB  . PRO E 133 ? 1.0754 0.9775 0.8165 0.5341  -0.3946 -0.2380 133 PRO E CB  
12143 C CG  . PRO E 133 ? 1.0368 0.9711 0.8224 0.5233  -0.3863 -0.2369 133 PRO E CG  
12144 C CD  . PRO E 133 ? 1.0117 0.9787 0.8400 0.5164  -0.3855 -0.2369 133 PRO E CD  
12145 N N   . SER E 134 ? 1.1727 1.0451 0.8715 0.5494  -0.4128 -0.2408 134 SER E N   
12146 C CA  . SER E 134 ? 1.1932 1.0450 0.8584 0.5576  -0.4072 -0.2346 134 SER E CA  
12147 C C   . SER E 134 ? 1.2028 1.0320 0.8308 0.5632  -0.3898 -0.2232 134 SER E C   
12148 O O   . SER E 134 ? 1.2131 1.0297 0.8202 0.5681  -0.3806 -0.2139 134 SER E O   
12149 C CB  . SER E 134 ? 1.2359 1.0652 0.8771 0.5673  -0.4282 -0.2431 134 SER E CB  
12150 O OG  . SER E 134 ? 1.2704 1.0713 0.8785 0.5751  -0.4389 -0.2489 134 SER E OG  
12151 N N   . THR E 135 ? 1.1539 0.9783 0.7754 0.5629  -0.3847 -0.2223 135 THR E N   
12152 C CA  . THR E 135 ? 1.1628 0.9680 0.7524 0.5686  -0.3660 -0.2091 135 THR E CA  
12153 C C   . THR E 135 ? 1.1248 0.9500 0.7382 0.5588  -0.3448 -0.1955 135 THR E C   
12154 O O   . THR E 135 ? 1.1308 0.9426 0.7238 0.5624  -0.3281 -0.1809 135 THR E O   
12155 C CB  . THR E 135 ? 1.1746 0.9671 0.7493 0.5722  -0.3673 -0.2125 135 THR E CB  
12156 O OG1 . THR E 135 ? 1.1417 0.9630 0.7608 0.5604  -0.3733 -0.2206 135 THR E OG1 
12157 C CG2 . THR E 135 ? 1.2279 0.9852 0.7598 0.5862  -0.3865 -0.2228 135 THR E CG2 
12158 N N   . LEU E 136 ? 1.0949 0.9504 0.7506 0.5470  -0.3449 -0.1990 136 LEU E N   
12159 C CA  . LEU E 136 ? 1.0645 0.9347 0.7396 0.5382  -0.3279 -0.1876 136 LEU E CA  
12160 C C   . LEU E 136 ? 1.0775 0.9335 0.7359 0.5418  -0.3224 -0.1767 136 LEU E C   
12161 O O   . LEU E 136 ? 1.0607 0.9207 0.7287 0.5359  -0.3093 -0.1646 136 LEU E O   
12162 C CB  . LEU E 136 ? 1.0316 0.9329 0.7488 0.5279  -0.3300 -0.1945 136 LEU E CB  
12163 C CG  . LEU E 136 ? 1.0053 0.9270 0.7488 0.5205  -0.3253 -0.1974 136 LEU E CG  
12164 C CD1 . LEU E 136 ? 1.0126 0.9412 0.7683 0.5219  -0.3417 -0.2103 136 LEU E CD1 
12165 C CD2 . LEU E 136 ? 0.9729 0.9195 0.7485 0.5111  -0.3162 -0.1953 136 LEU E CD2 
12166 N N   . GLY E 137 ? 1.1356 0.9743 0.7706 0.5512  -0.3331 -0.1804 137 GLY E N   
12167 C CA  . GLY E 137 ? 1.1517 0.9750 0.7695 0.5558  -0.3277 -0.1688 137 GLY E CA  
12168 C C   . GLY E 137 ? 1.1707 0.9725 0.7598 0.5627  -0.3130 -0.1518 137 GLY E C   
12169 O O   . GLY E 137 ? 1.1820 0.9728 0.7622 0.5655  -0.3061 -0.1385 137 GLY E O   
12170 N N   . ARG E 138 ? 1.1481 0.9434 0.7237 0.5660  -0.3073 -0.1508 138 ARG E N   
12171 C CA  . ARG E 138 ? 1.1662 0.9428 0.7163 0.5734  -0.2898 -0.1325 138 ARG E CA  
12172 C C   . ARG E 138 ? 1.1352 0.9260 0.7130 0.5626  -0.2725 -0.1154 138 ARG E C   
12173 O O   . ARG E 138 ? 1.1479 0.9263 0.7129 0.5674  -0.2562 -0.0956 138 ARG E O   
12174 C CB  . ARG E 138 ? 1.1869 0.9488 0.7100 0.5822  -0.2898 -0.1379 138 ARG E CB  
12175 C CG  . ARG E 138 ? 1.2241 0.9667 0.7168 0.5936  -0.3100 -0.1552 138 ARG E CG  
12176 C CD  . ARG E 138 ? 1.2686 0.9781 0.7113 0.6099  -0.3049 -0.1519 138 ARG E CD  
12177 N NE  . ARG E 138 ? 1.2899 0.9876 0.7179 0.6149  -0.3264 -0.1724 138 ARG E NE  
12178 C CZ  . ARG E 138 ? 1.3019 0.9871 0.7136 0.6194  -0.3253 -0.1757 138 ARG E CZ  
12179 N NH1 . ARG E 138 ? 1.2937 0.9780 0.7011 0.6199  -0.3018 -0.1598 138 ARG E NH1 
12180 N NH2 . ARG E 138 ? 1.3241 0.9967 0.7252 0.6231  -0.3492 -0.1951 138 ARG E NH2 
12181 N N   . LEU E 139 ? 1.1376 0.9534 0.7530 0.5489  -0.2754 -0.1217 139 LEU E N   
12182 C CA  . LEU E 139 ? 1.1098 0.9380 0.7521 0.5382  -0.2625 -0.1074 139 LEU E CA  
12183 C C   . LEU E 139 ? 1.1122 0.9362 0.7630 0.5355  -0.2627 -0.0964 139 LEU E C   
12184 O O   . LEU E 139 ? 1.0947 0.9303 0.7675 0.5273  -0.2705 -0.1031 139 LEU E O   
12185 C CB  . LEU E 139 ? 1.0744 0.9276 0.7483 0.5265  -0.2660 -0.1193 139 LEU E CB  
12186 C CG  . LEU E 139 ? 1.0723 0.9331 0.7449 0.5284  -0.2740 -0.1365 139 LEU E CG  
12187 C CD1 . LEU E 139 ? 1.0374 0.9251 0.7451 0.5169  -0.2757 -0.1457 139 LEU E CD1 
12188 C CD2 . LEU E 139 ? 1.0865 0.9343 0.7375 0.5354  -0.2647 -0.1306 139 LEU E CD2 
12189 N N   . LYS E 140 ? 1.1368 0.9421 0.7683 0.5436  -0.2536 -0.0785 140 LYS E N   
12190 C CA  . LYS E 140 ? 1.1436 0.9421 0.7831 0.5420  -0.2540 -0.0656 140 LYS E CA  
12191 C C   . LYS E 140 ? 1.1170 0.9269 0.7918 0.5287  -0.2503 -0.0539 140 LYS E C   
12192 O O   . LYS E 140 ? 1.1180 0.9246 0.8056 0.5245  -0.2566 -0.0490 140 LYS E O   
12193 C CB  . LYS E 140 ? 1.1779 0.9551 0.7914 0.5543  -0.2424 -0.0459 140 LYS E CB  
12194 C CG  . LYS E 140 ? 1.2126 0.9728 0.7846 0.5694  -0.2477 -0.0573 140 LYS E CG  
12195 C CD  . LYS E 140 ? 1.2125 0.9766 0.7846 0.5687  -0.2680 -0.0795 140 LYS E CD  
12196 C CE  . LYS E 140 ? 1.2485 0.9950 0.7810 0.5833  -0.2766 -0.0918 140 LYS E CE  
12197 N NZ  . LYS E 140 ? 1.2878 1.0104 0.7893 0.5967  -0.2693 -0.0766 140 LYS E NZ  
12198 N N   . LYS E 141 ? 1.0519 0.8733 0.7416 0.5225  -0.2416 -0.0496 141 LYS E N   
12199 C CA  . LYS E 141 ? 1.0288 0.8599 0.7509 0.5101  -0.2401 -0.0391 141 LYS E CA  
12200 C C   . LYS E 141 ? 1.0031 0.8506 0.7424 0.5009  -0.2506 -0.0589 141 LYS E C   
12201 O O   . LYS E 141 ? 0.9870 0.8404 0.7495 0.4912  -0.2521 -0.0535 141 LYS E O   
12202 C CB  . LYS E 141 ? 1.0219 0.8563 0.7523 0.5089  -0.2235 -0.0202 141 LYS E CB  
12203 C CG  . LYS E 141 ? 1.0482 0.8673 0.7660 0.5182  -0.2092 0.0047  141 LYS E CG  
12204 C CD  . LYS E 141 ? 1.0472 0.8642 0.7943 0.5110  -0.2080 0.0292  141 LYS E CD  
12205 C CE  . LYS E 141 ? 1.0210 0.8521 0.8011 0.4991  -0.2047 0.0394  141 LYS E CE  
12206 N NZ  . LYS E 141 ? 1.0290 0.8573 0.8280 0.4992  -0.1900 0.0731  141 LYS E NZ  
12207 N N   . LEU E 142 ? 1.0305 0.8848 0.7593 0.5042  -0.2580 -0.0805 142 LEU E N   
12208 C CA  . LEU E 142 ? 1.0081 0.8796 0.7536 0.4972  -0.2651 -0.0975 142 LEU E CA  
12209 C C   . LEU E 142 ? 1.0085 0.8767 0.7645 0.4929  -0.2748 -0.0998 142 LEU E C   
12210 O O   . LEU E 142 ? 1.0273 0.8835 0.7731 0.4977  -0.2817 -0.1002 142 LEU E O   
12211 C CB  . LEU E 142 ? 1.0100 0.8894 0.7461 0.5025  -0.2718 -0.1171 142 LEU E CB  
12212 C CG  . LEU E 142 ? 0.9876 0.8878 0.7431 0.4969  -0.2761 -0.1326 142 LEU E CG  
12213 C CD1 . LEU E 142 ? 0.9677 0.8813 0.7339 0.4924  -0.2671 -0.1319 142 LEU E CD1 
12214 C CD2 . LEU E 142 ? 0.9954 0.9013 0.7470 0.5024  -0.2868 -0.1488 142 LEU E CD2 
12215 N N   . ARG E 143 ? 1.0085 0.8853 0.7825 0.4849  -0.2757 -0.1015 143 ARG E N   
12216 C CA  . ARG E 143 ? 1.0125 0.8831 0.7927 0.4820  -0.2859 -0.1057 143 ARG E CA  
12217 C C   . ARG E 143 ? 1.0017 0.8862 0.7858 0.4823  -0.2901 -0.1247 143 ARG E C   
12218 O O   . ARG E 143 ? 1.0127 0.8915 0.7925 0.4856  -0.2988 -0.1334 143 ARG E O   
12219 C CB  . ARG E 143 ? 1.0091 0.8725 0.8041 0.4738  -0.2862 -0.0905 143 ARG E CB  
12220 C CG  . ARG E 143 ? 1.0285 0.8724 0.8250 0.4733  -0.2901 -0.0726 143 ARG E CG  
12221 C CD  . ARG E 143 ? 1.0273 0.8637 0.8421 0.4642  -0.2967 -0.0616 143 ARG E CD  
12222 N NE  . ARG E 143 ? 1.0114 0.8576 0.8413 0.4585  -0.2868 -0.0476 143 ARG E NE  
12223 C CZ  . ARG E 143 ? 1.0032 0.8503 0.8494 0.4502  -0.2914 -0.0429 143 ARG E CZ  
12224 N NH1 . ARG E 143 ? 1.0119 0.8481 0.8580 0.4470  -0.3064 -0.0522 143 ARG E NH1 
12225 N NH2 . ARG E 143 ? 0.9889 0.8463 0.8495 0.4459  -0.2813 -0.0288 143 ARG E NH2 
12226 N N   . PHE E 144 ? 0.9736 0.8762 0.7660 0.4800  -0.2831 -0.1302 144 PHE E N   
12227 C CA  . PHE E 144 ? 0.9628 0.8808 0.7625 0.4806  -0.2843 -0.1447 144 PHE E CA  
12228 C C   . PHE E 144 ? 0.9517 0.8887 0.7558 0.4830  -0.2798 -0.1533 144 PHE E C   
12229 O O   . PHE E 144 ? 0.9418 0.8843 0.7485 0.4804  -0.2724 -0.1483 144 PHE E O   
12230 C CB  . PHE E 144 ? 0.9505 0.8721 0.7602 0.4747  -0.2811 -0.1417 144 PHE E CB  
12231 C CG  . PHE E 144 ? 0.9605 0.8625 0.7703 0.4700  -0.2862 -0.1286 144 PHE E CG  
12232 C CD1 . PHE E 144 ? 0.9781 0.8635 0.7817 0.4715  -0.2976 -0.1319 144 PHE E CD1 
12233 C CD2 . PHE E 144 ? 0.9544 0.8541 0.7717 0.4643  -0.2801 -0.1121 144 PHE E CD2 
12234 C CE1 . PHE E 144 ? 0.9896 0.8557 0.7965 0.4661  -0.3051 -0.1193 144 PHE E CE1 
12235 C CE2 . PHE E 144 ? 0.9638 0.8473 0.7874 0.4590  -0.2860 -0.0975 144 PHE E CE2 
12236 C CZ  . PHE E 144 ? 0.9815 0.8479 0.8008 0.4591  -0.2996 -0.1013 144 PHE E CZ  
12237 N N   . LEU E 145 ? 0.9581 0.9044 0.7642 0.4881  -0.2849 -0.1653 145 LEU E N   
12238 C CA  . LEU E 145 ? 0.9494 0.9145 0.7653 0.4899  -0.2839 -0.1735 145 LEU E CA  
12239 C C   . LEU E 145 ? 0.9416 0.9252 0.7731 0.4921  -0.2834 -0.1822 145 LEU E C   
12240 O O   . LEU E 145 ? 0.9539 0.9354 0.7828 0.4978  -0.2893 -0.1872 145 LEU E O   
12241 C CB  . LEU E 145 ? 0.9668 0.9244 0.7714 0.4957  -0.2922 -0.1768 145 LEU E CB  
12242 C CG  . LEU E 145 ? 0.9628 0.9353 0.7772 0.4975  -0.2953 -0.1847 145 LEU E CG  
12243 C CD1 . LEU E 145 ? 0.9807 0.9366 0.7745 0.5016  -0.2999 -0.1826 145 LEU E CD1 
12244 C CD2 . LEU E 145 ? 0.9663 0.9525 0.7943 0.5018  -0.3031 -0.1940 145 LEU E CD2 
12245 N N   . ARG E 146 ? 0.9125 0.9141 0.7600 0.4886  -0.2751 -0.1828 146 ARG E N   
12246 C CA  . ARG E 146 ? 0.9055 0.9262 0.7689 0.4916  -0.2711 -0.1880 146 ARG E CA  
12247 C C   . ARG E 146 ? 0.8914 0.9362 0.7783 0.4903  -0.2680 -0.1909 146 ARG E C   
12248 O O   . ARG E 146 ? 0.8769 0.9286 0.7715 0.4849  -0.2613 -0.1879 146 ARG E O   
12249 C CB  . ARG E 146 ? 0.8993 0.9183 0.7606 0.4897  -0.2637 -0.1847 146 ARG E CB  
12250 C CG  . ARG E 146 ? 0.9167 0.9109 0.7576 0.4915  -0.2699 -0.1828 146 ARG E CG  
12251 C CD  . ARG E 146 ? 0.9104 0.8957 0.7477 0.4853  -0.2664 -0.1757 146 ARG E CD  
12252 N NE  . ARG E 146 ? 0.9280 0.8866 0.7496 0.4846  -0.2755 -0.1713 146 ARG E NE  
12253 C CZ  . ARG E 146 ? 0.9261 0.8723 0.7469 0.4774  -0.2764 -0.1607 146 ARG E CZ  
12254 N NH1 . ARG E 146 ? 0.9079 0.8650 0.7391 0.4713  -0.2677 -0.1537 146 ARG E NH1 
12255 N NH2 . ARG E 146 ? 0.9441 0.8663 0.7551 0.4765  -0.2864 -0.1558 146 ARG E NH2 
12256 N N   . LEU E 147 ? 0.9200 1.0907 0.8601 0.5310  -0.2855 -0.1655 147 LEU E N   
12257 C CA  . LEU E 147 ? 0.8986 1.1107 0.8662 0.5228  -0.2876 -0.1646 147 LEU E CA  
12258 C C   . LEU E 147 ? 0.8863 1.1395 0.8969 0.5286  -0.2798 -0.1740 147 LEU E C   
12259 O O   . LEU E 147 ? 0.8775 1.1615 0.9137 0.5253  -0.2841 -0.1736 147 LEU E O   
12260 C CB  . LEU E 147 ? 0.9240 1.1260 0.8814 0.5229  -0.3098 -0.1552 147 LEU E CB  
12261 C CG  . LEU E 147 ? 0.9459 1.1094 0.8580 0.5169  -0.3228 -0.1460 147 LEU E CG  
12262 C CD1 . LEU E 147 ? 0.9591 1.1403 0.8693 0.5107  -0.3430 -0.1401 147 LEU E CD1 
12263 C CD2 . LEU E 147 ? 0.9399 1.0951 0.8342 0.5053  -0.3092 -0.1488 147 LEU E CD2 
12264 N N   . ASN E 148 ? 0.8920 1.1482 0.9111 0.5371  -0.2682 -0.1849 148 ASN E N   
12265 C CA  . ASN E 148 ? 0.8887 1.1803 0.9483 0.5449  -0.2622 -0.1971 148 ASN E CA  
12266 C C   . ASN E 148 ? 0.8498 1.1944 0.9337 0.5314  -0.2495 -0.1996 148 ASN E C   
12267 O O   . ASN E 148 ? 0.8241 1.1785 0.8984 0.5169  -0.2427 -0.1913 148 ASN E O   
12268 C CB  . ASN E 148 ? 0.9027 1.1861 0.9671 0.5578  -0.2517 -0.2131 148 ASN E CB  
12269 C CG  . ASN E 148 ? 0.8830 1.1721 0.9250 0.5507  -0.2372 -0.2181 148 ASN E CG  
12270 O OD1 . ASN E 148 ? 0.8490 1.1819 0.9004 0.5383  -0.2265 -0.2174 148 ASN E OD1 
12271 N ND2 . ASN E 148 ? 0.9054 1.1522 0.9201 0.5582  -0.2366 -0.2210 148 ASN E ND2 
12272 N N   . ASN E 149 ? 0.8492 1.2282 0.9696 0.5364  -0.2457 -0.2099 149 ASN E N   
12273 C CA  . ASN E 149 ? 0.8169 1.2480 0.9648 0.5242  -0.2343 -0.2117 149 ASN E CA  
12274 C C   . ASN E 149 ? 0.7990 1.2349 0.9460 0.5096  -0.2383 -0.1970 149 ASN E C   
12275 O O   . ASN E 149 ? 0.7705 1.2253 0.9198 0.4948  -0.2272 -0.1890 149 ASN E O   
12276 C CB  . ASN E 149 ? 0.7934 1.2568 0.9415 0.5173  -0.2166 -0.2176 149 ASN E CB  
12277 C CG  . ASN E 149 ? 0.7978 1.2963 0.9728 0.5262  -0.2067 -0.2398 149 ASN E CG  
12278 O OD1 . ASN E 149 ? 0.7802 1.3266 0.9838 0.5192  -0.1987 -0.2444 149 ASN E OD1 
12279 N ND2 . ASN E 149 ? 0.8231 1.2982 0.9917 0.5409  -0.2054 -0.2556 149 ASN E ND2 
12280 N N   . ASN E 150 ? 0.8770 1.2994 1.0260 0.5142  -0.2540 -0.1934 150 ASN E N   
12281 C CA  . ASN E 150 ? 0.8654 1.2945 1.0154 0.5028  -0.2595 -0.1853 150 ASN E CA  
12282 C C   . ASN E 150 ? 0.8761 1.3254 1.0512 0.5073  -0.2708 -0.1875 150 ASN E C   
12283 O O   . ASN E 150 ? 0.8903 1.3476 1.0849 0.5186  -0.2730 -0.1931 150 ASN E O   
12284 C CB  . ASN E 150 ? 0.8808 1.2705 0.9939 0.5022  -0.2712 -0.1781 150 ASN E CB  
12285 C CG  . ASN E 150 ? 0.8554 1.2421 0.9581 0.4892  -0.2584 -0.1732 150 ASN E CG  
12286 O OD1 . ASN E 150 ? 0.8333 1.2410 0.9539 0.4776  -0.2534 -0.1709 150 ASN E OD1 
12287 N ND2 . ASN E 150 ? 0.8589 1.2212 0.9377 0.4916  -0.2523 -0.1716 150 ASN E ND2 
12288 N N   . SER E 151 ? 0.8536 1.3149 1.0322 0.4987  -0.2777 -0.1844 151 SER E N   
12289 C CA  . SER E 151 ? 0.8633 1.3489 1.0638 0.5012  -0.2902 -0.1859 151 SER E CA  
12290 C C   . SER E 151 ? 0.8911 1.3617 1.0690 0.5043  -0.3139 -0.1798 151 SER E C   
12291 O O   . SER E 151 ? 0.8926 1.3909 1.0826 0.4996  -0.3248 -0.1814 151 SER E O   
12292 C CB  . SER E 151 ? 0.8321 1.3576 1.0629 0.4875  -0.2783 -0.1904 151 SER E CB  
12293 O OG  . SER E 151 ? 0.8402 1.3934 1.0961 0.4906  -0.2875 -0.1939 151 SER E OG  
12294 N N   . LEU E 152 ? 0.9487 1.3793 1.0932 0.5109  -0.3226 -0.1726 152 LEU E N   
12295 C CA  . LEU E 152 ? 0.9790 1.3955 1.0968 0.5113  -0.3465 -0.1631 152 LEU E CA  
12296 C C   . LEU E 152 ? 1.0096 1.4379 1.1457 0.5217  -0.3655 -0.1527 152 LEU E C   
12297 O O   . LEU E 152 ? 1.0166 1.4429 1.1785 0.5343  -0.3608 -0.1517 152 LEU E O   
12298 C CB  . LEU E 152 ? 0.9968 1.3645 1.0741 0.5145  -0.3488 -0.1562 152 LEU E CB  
12299 C CG  . LEU E 152 ? 0.9818 1.3349 1.0294 0.5024  -0.3432 -0.1602 152 LEU E CG  
12300 C CD1 . LEU E 152 ? 0.9420 1.3237 1.0169 0.4926  -0.3211 -0.1710 152 LEU E CD1 
12301 C CD2 . LEU E 152 ? 1.0062 1.3098 1.0200 0.5076  -0.3393 -0.1548 152 LEU E CD2 
12302 N N   . SER E 153 ? 0.9919 1.4370 1.1173 0.5153  -0.3878 -0.1446 153 SER E N   
12303 C CA  . SER E 153 ? 1.0212 1.4867 1.1678 0.5221  -0.4083 -0.1296 153 SER E CA  
12304 C C   . SER E 153 ? 1.0575 1.5197 1.1705 0.5141  -0.4357 -0.1113 153 SER E C   
12305 O O   . SER E 153 ? 1.0532 1.5235 1.1345 0.4973  -0.4403 -0.1189 153 SER E O   
12306 C CB  . SER E 153 ? 1.0029 1.5199 1.1853 0.5167  -0.4068 -0.1395 153 SER E CB  
12307 O OG  . SER E 153 ? 0.9897 1.5354 1.1579 0.4989  -0.4109 -0.1506 153 SER E OG  
12308 N N   . GLY E 154 ? 1.0278 1.4820 1.1507 0.5245  -0.4535 -0.0868 154 GLY E N   
12309 C CA  . GLY E 154 ? 1.0679 1.5236 1.1613 0.5147  -0.4814 -0.0623 154 GLY E CA  
12310 C C   . GLY E 154 ? 1.1036 1.5236 1.2051 0.5311  -0.4907 -0.0347 154 GLY E C   
12311 O O   . GLY E 154 ? 1.1061 1.5239 1.2547 0.5503  -0.4849 -0.0295 154 GLY E O   
12312 N N   . GLU E 155 ? 1.1304 1.5251 1.1882 0.5221  -0.5047 -0.0176 155 GLU E N   
12313 C CA  . GLU E 155 ? 1.1663 1.5240 1.2287 0.5357  -0.5133 0.0101  155 GLU E CA  
12314 C C   . GLU E 155 ? 1.1696 1.4769 1.1775 0.5294  -0.5055 0.0043  155 GLU E C   
12315 O O   . GLU E 155 ? 1.1574 1.4671 1.1198 0.5095  -0.5038 -0.0111 155 GLU E O   
12316 C CB  . GLU E 155 ? 1.2117 1.6001 1.2830 0.5289  -0.5464 0.0510  155 GLU E CB  
12317 C CG  . GLU E 155 ? 1.2496 1.6092 1.3483 0.5471  -0.5556 0.0860  155 GLU E CG  
12318 C CD  . GLU E 155 ? 1.2875 1.6921 1.4232 0.5456  -0.5859 0.1296  155 GLU E CD  
12319 O OE1 . GLU E 155 ? 1.3029 1.7494 1.4081 0.5198  -0.6087 0.1424  155 GLU E OE1 
12320 O OE2 . GLU E 155 ? 1.3038 1.7048 1.5012 0.5689  -0.5868 0.1518  155 GLU E OE2 
12321 N N   . ILE E 156 ? 1.1872 1.4491 1.2026 0.5461  -0.4998 0.0152  156 ILE E N   
12322 C CA  . ILE E 156 ? 1.1921 1.4025 1.1577 0.5415  -0.4915 0.0100  156 ILE E CA  
12323 C C   . ILE E 156 ? 1.2299 1.4407 1.1478 0.5206  -0.5163 0.0356  156 ILE E C   
12324 O O   . ILE E 156 ? 1.2692 1.4921 1.2040 0.5223  -0.5386 0.0714  156 ILE E O   
12325 C CB  . ILE E 156 ? 1.2049 1.3687 1.1932 0.5638  -0.4790 0.0141  156 ILE E CB  
12326 C CG1 . ILE E 156 ? 1.1693 1.3341 1.1961 0.5790  -0.4520 -0.0156 156 ILE E CG1 
12327 C CG2 . ILE E 156 ? 1.2167 1.3285 1.1504 0.5570  -0.4743 0.0134  156 ILE E CG2 
12328 C CD1 . ILE E 156 ? 1.1743 1.3702 1.2688 0.5949  -0.4544 -0.0083 156 ILE E CD1 
12329 N N   . PRO E 157 ? 1.2216 1.4231 1.0824 0.4990  -0.5133 0.0200  157 PRO E N   
12330 C CA  . PRO E 157 ? 1.2618 1.4606 1.0708 0.4750  -0.5343 0.0419  157 PRO E CA  
12331 C C   . PRO E 157 ? 1.2983 1.4494 1.1009 0.4858  -0.5392 0.0695  157 PRO E C   
12332 O O   . PRO E 157 ? 1.2864 1.3902 1.0965 0.5045  -0.5196 0.0579  157 PRO E O   
12333 C CB  . PRO E 157 ? 1.2403 1.4264 0.9957 0.4537  -0.5210 0.0112  157 PRO E CB  
12334 C CG  . PRO E 157 ? 1.1876 1.3762 0.9723 0.4674  -0.4957 -0.0217 157 PRO E CG  
12335 C CD  . PRO E 157 ? 1.1757 1.3805 1.0238 0.4925  -0.4917 -0.0171 157 PRO E CD  
12336 N N   . ARG E 158 ? 1.3448 1.5126 1.1346 0.4721  -0.5657 0.1074  158 ARG E N   
12337 C CA  . ARG E 158 ? 1.3834 1.5092 1.1672 0.4796  -0.5719 0.1380  158 ARG E CA  
12338 C C   . ARG E 158 ? 1.3838 1.4555 1.1044 0.4675  -0.5582 0.1211  158 ARG E C   
12339 O O   . ARG E 158 ? 1.4036 1.4267 1.1234 0.4801  -0.5532 0.1342  158 ARG E O   
12340 C CB  . ARG E 158 ? 1.4339 1.5994 1.2171 0.4630  -0.6048 0.1869  158 ARG E CB  
12341 C CG  . ARG E 158 ? 1.4604 1.6361 1.1676 0.4228  -0.6178 0.1924  158 ARG E CG  
12342 C CD  . ARG E 158 ? 1.5025 1.6376 1.1840 0.4200  -0.6240 0.2239  158 ARG E CD  
12343 N NE  . ARG E 158 ? 1.5202 1.6502 1.1219 0.3815  -0.6260 0.2156  158 ARG E NE  
12344 C CZ  . ARG E 158 ? 1.5455 1.6282 1.1078 0.3746  -0.6221 0.2260  158 ARG E CZ  
12345 N NH1 . ARG E 158 ? 1.5572 1.5923 1.1515 0.4038  -0.6167 0.2453  158 ARG E NH1 
12346 N NH2 . ARG E 158 ? 1.5608 1.6441 1.0516 0.3359  -0.6218 0.2143  158 ARG E NH2 
12347 N N   . SER E 159 ? 1.3639 1.4431 1.0352 0.4429  -0.5511 0.0923  159 SER E N   
12348 C CA  . SER E 159 ? 1.3656 1.3957 0.9777 0.4287  -0.5379 0.0767  159 SER E CA  
12349 C C   . SER E 159 ? 1.3388 1.3139 0.9653 0.4552  -0.5121 0.0572  159 SER E C   
12350 O O   . SER E 159 ? 1.3523 1.2767 0.9416 0.4516  -0.5040 0.0570  159 SER E O   
12351 C CB  . SER E 159 ? 1.3457 1.3987 0.9159 0.3989  -0.5318 0.0456  159 SER E CB  
12352 O OG  . SER E 159 ? 1.2981 1.3781 0.9061 0.4113  -0.5185 0.0175  159 SER E OG  
12353 N N   . LEU E 160 ? 1.3104 1.2976 0.9891 0.4791  -0.4983 0.0401  160 LEU E N   
12354 C CA  . LEU E 160 ? 1.2857 1.2311 0.9782 0.4999  -0.4731 0.0198  160 LEU E CA  
12355 C C   . LEU E 160 ? 1.3182 1.2220 1.0278 0.5183  -0.4734 0.0400  160 LEU E C   
12356 O O   . LEU E 160 ? 1.3057 1.1709 1.0171 0.5312  -0.4527 0.0228  160 LEU E O   
12357 C CB  . LEU E 160 ? 1.2431 1.2204 0.9883 0.5164  -0.4585 -0.0023 160 LEU E CB  
12358 C CG  . LEU E 160 ? 1.2056 1.2241 0.9455 0.5018  -0.4540 -0.0245 160 LEU E CG  
12359 C CD1 . LEU E 160 ? 1.1689 1.2208 0.9655 0.5179  -0.4407 -0.0409 160 LEU E CD1 
12360 C CD2 . LEU E 160 ? 1.1855 1.1773 0.8799 0.4878  -0.4388 -0.0449 160 LEU E CD2 
12361 N N   . THR E 161 ? 1.3524 1.2667 1.0784 0.5190  -0.4957 0.0767  161 THR E N   
12362 C CA  . THR E 161 ? 1.3872 1.2619 1.1348 0.5357  -0.4961 0.0996  161 THR E CA  
12363 C C   . THR E 161 ? 1.4211 1.2541 1.1098 0.5187  -0.5018 0.1152  161 THR E C   
12364 O O   . THR E 161 ? 1.4455 1.2350 1.1453 0.5319  -0.4960 0.1270  161 THR E O   
12365 C CB  . THR E 161 ? 1.4173 1.3260 1.2252 0.5476  -0.5164 0.1377  161 THR E CB  
12366 O OG1 . THR E 161 ? 1.4350 1.3916 1.2195 0.5235  -0.5431 0.1620  161 THR E OG1 
12367 C CG2 . THR E 161 ? 1.3884 1.3244 1.2646 0.5699  -0.5050 0.1209  161 THR E CG2 
12368 N N   . ALA E 162 ? 1.4246 1.2702 1.0532 0.4884  -0.5112 0.1138  162 ALA E N   
12369 C CA  . ALA E 162 ? 1.4585 1.2694 1.0277 0.4671  -0.5163 0.1277  162 ALA E CA  
12370 C C   . ALA E 162 ? 1.4352 1.1987 0.9557 0.4598  -0.4926 0.0936  162 ALA E C   
12371 O O   . ALA E 162 ? 1.4604 1.1924 0.9278 0.4397  -0.4934 0.1000  162 ALA E O   
12372 C CB  . ALA E 162 ? 1.4836 1.3400 1.0140 0.4323  -0.5396 0.1466  162 ALA E CB  
12373 N N   . VAL E 163 ? 1.4322 1.1936 0.9711 0.4739  -0.4715 0.0597  163 VAL E N   
12374 C CA  . VAL E 163 ? 1.4080 1.1332 0.9054 0.4658  -0.4499 0.0309  163 VAL E CA  
12375 C C   . VAL E 163 ? 1.4271 1.0917 0.9132 0.4771  -0.4380 0.0337  163 VAL E C   
12376 O O   . VAL E 163 ? 1.4436 1.0702 0.8789 0.4617  -0.4285 0.0250  163 VAL E O   
12377 C CB  . VAL E 163 ? 1.3627 1.1125 0.8895 0.4769  -0.4323 -0.0001 163 VAL E CB  
12378 C CG1 . VAL E 163 ? 1.3433 1.1059 0.9352 0.5066  -0.4269 -0.0008 163 VAL E CG1 
12379 C CG2 . VAL E 163 ? 1.3628 1.0779 0.8573 0.4718  -0.4097 -0.0242 163 VAL E CG2 
12380 N N   . LEU E 164 ? 1.4336 1.0886 0.9700 0.5032  -0.4362 0.0434  164 LEU E N   
12381 C CA  . LEU E 164 ? 1.4568 1.0588 0.9982 0.5171  -0.4248 0.0470  164 LEU E CA  
12382 C C   . LEU E 164 ? 1.4259 0.9977 0.9519 0.5220  -0.3973 0.0126  164 LEU E C   
12383 O O   . LEU E 164 ? 1.4425 0.9713 0.9715 0.5318  -0.3840 0.0094  164 LEU E O   
12384 C CB  . LEU E 164 ? 1.5048 1.0727 1.0040 0.5009  -0.4374 0.0753  164 LEU E CB  
12385 C CG  . LEU E 164 ? 1.5123 1.0468 0.9359 0.4734  -0.4331 0.0684  164 LEU E CG  
12386 C CD1 . LEU E 164 ? 1.5131 0.9881 0.9187 0.4808  -0.4105 0.0519  164 LEU E CD1 
12387 C CD2 . LEU E 164 ? 1.5591 1.0985 0.9515 0.4502  -0.4557 0.1034  164 LEU E CD2 
12388 N N   . THR E 165 ? 1.3776 0.9741 0.8918 0.5147  -0.3877 -0.0117 165 THR E N   
12389 C CA  . THR E 165 ? 1.3474 0.9250 0.8504 0.5174  -0.3631 -0.0393 165 THR E CA  
12390 C C   . THR E 165 ? 1.3089 0.9245 0.8636 0.5340  -0.3489 -0.0608 165 THR E C   
12391 O O   . THR E 165 ? 1.2882 0.8953 0.8454 0.5345  -0.3251 -0.0822 165 THR E O   
12392 C CB  . THR E 165 ? 1.3245 0.9040 0.7810 0.4864  -0.3542 -0.0497 165 THR E CB  
12393 O OG1 . THR E 165 ? 1.3612 0.9194 0.7715 0.4672  -0.3705 -0.0306 165 THR E OG1 
12394 C CG2 . THR E 165 ? 1.3051 0.8566 0.7448 0.4785  -0.3263 -0.0695 165 THR E CG2 
12395 N N   . LEU E 166 ? 1.3110 0.9734 0.9081 0.5411  -0.3597 -0.0559 166 LEU E N   
12396 C CA  . LEU E 166 ? 1.2643 0.9669 0.9107 0.5541  -0.3463 -0.0761 166 LEU E CA  
12397 C C   . LEU E 166 ? 1.2744 0.9586 0.9551 0.5718  -0.3284 -0.0895 166 LEU E C   
12398 O O   . LEU E 166 ? 1.3078 0.9784 1.0215 0.5843  -0.3338 -0.0764 166 LEU E O   
12399 C CB  . LEU E 166 ? 1.2599 1.0115 0.9468 0.5581  -0.3622 -0.0657 166 LEU E CB  
12400 C CG  . LEU E 166 ? 1.2255 1.0214 0.9049 0.5438  -0.3669 -0.0713 166 LEU E CG  
12401 C CD1 . LEU E 166 ? 1.1796 1.0089 0.8882 0.5487  -0.3467 -0.0961 166 LEU E CD1 
12402 C CD2 . LEU E 166 ? 1.2526 1.0279 0.8731 0.5218  -0.3705 -0.0687 166 LEU E CD2 
12403 N N   . GLN E 167 ? 1.3038 0.9912 0.9811 0.5713  -0.3057 -0.1153 167 GLN E N   
12404 C CA  . GLN E 167 ? 1.2850 0.9686 0.9979 0.5837  -0.2839 -0.1369 167 GLN E CA  
12405 C C   . GLN E 167 ? 1.2546 0.9949 1.0181 0.5916  -0.2751 -0.1552 167 GLN E C   
12406 O O   . GLN E 167 ? 1.2692 1.0159 1.0831 0.6048  -0.2666 -0.1645 167 GLN E O   
12407 C CB  . GLN E 167 ? 1.2769 0.9364 0.9535 0.5704  -0.2609 -0.1554 167 GLN E CB  
12408 C CG  . GLN E 167 ? 1.3081 0.9087 0.9353 0.5608  -0.2651 -0.1409 167 GLN E CG  
12409 C CD  . GLN E 167 ? 1.3372 0.8968 0.9701 0.5670  -0.2460 -0.1551 167 GLN E CD  
12410 O OE1 . GLN E 167 ? 1.3506 0.9175 1.0351 0.5803  -0.2360 -0.1661 167 GLN E OE1 
12411 N NE2 . GLN E 167 ? 1.3458 0.8673 0.9307 0.5500  -0.2369 -0.1557 167 GLN E NE2 
12412 N N   . VAL E 168 ? 1.1457 0.9279 0.9009 0.5827  -0.2755 -0.1602 168 VAL E N   
12413 C CA  . VAL E 168 ? 1.1136 0.9537 0.9120 0.5870  -0.2666 -0.1769 168 VAL E CA  
12414 C C   . VAL E 168 ? 1.0984 0.9737 0.9094 0.5832  -0.2857 -0.1608 168 VAL E C   
12415 O O   . VAL E 168 ? 1.0866 0.9614 0.8641 0.5695  -0.2958 -0.1486 168 VAL E O   
12416 C CB  . VAL E 168 ? 1.0761 0.9460 0.8604 0.5671  -0.2433 -0.1947 168 VAL E CB  
12417 C CG1 . VAL E 168 ? 1.0476 0.9794 0.8777 0.5712  -0.2333 -0.2120 168 VAL E CG1 
12418 C CG2 . VAL E 168 ? 1.0933 0.9301 0.8566 0.5596  -0.2227 -0.2093 168 VAL E CG2 
12419 N N   . LEU E 169 ? 1.1393 1.0451 1.0009 0.5938  -0.2887 -0.1628 169 LEU E N   
12420 C CA  . LEU E 169 ? 1.1266 1.0698 1.0059 0.5901  -0.3045 -0.1505 169 LEU E CA  
12421 C C   . LEU E 169 ? 1.1052 1.0977 1.0374 0.5973  -0.2934 -0.1679 169 LEU E C   
12422 O O   . LEU E 169 ? 1.1206 1.1101 1.0893 0.6105  -0.2819 -0.1813 169 LEU E O   
12423 C CB  . LEU E 169 ? 1.1660 1.0888 1.0505 0.5953  -0.3274 -0.1239 169 LEU E CB  
12424 C CG  . LEU E 169 ? 1.1653 1.1235 1.0669 0.5916  -0.3476 -0.1070 169 LEU E CG  
12425 C CD1 . LEU E 169 ? 1.1582 1.1565 1.1224 0.6038  -0.3443 -0.1136 169 LEU E CD1 
12426 C CD2 . LEU E 169 ? 1.1334 1.1147 1.0025 0.5726  -0.3498 -0.1099 169 LEU E CD2 
12427 N N   . ASP E 170 ? 1.0817 1.1191 1.0205 0.5874  -0.2949 -0.1691 170 ASP E N   
12428 C CA  . ASP E 170 ? 1.0614 1.1483 1.0482 0.5918  -0.2856 -0.1839 170 ASP E CA  
12429 C C   . ASP E 170 ? 1.0372 1.1618 1.0295 0.5804  -0.2954 -0.1748 170 ASP E C   
12430 O O   . ASP E 170 ? 1.0086 1.1461 0.9778 0.5655  -0.2914 -0.1741 170 ASP E O   
12431 C CB  . ASP E 170 ? 1.0354 1.1464 1.0262 0.5896  -0.2622 -0.2082 170 ASP E CB  
12432 C CG  . ASP E 170 ? 1.0217 1.1822 1.0632 0.5947  -0.2509 -0.2266 170 ASP E CG  
12433 O OD1 . ASP E 170 ? 1.0399 1.2040 1.1182 0.6044  -0.2591 -0.2224 170 ASP E OD1 
12434 O OD2 . ASP E 170 ? 0.9935 1.1929 1.0398 0.5885  -0.2340 -0.2441 170 ASP E OD2 
12435 N N   . LEU E 171 ? 0.6012 1.1614 1.4714 0.3435  -0.1271 -0.1680 171 LEU E N   
12436 C CA  . LEU E 171 ? 0.5856 1.1918 1.5290 0.3242  -0.1142 -0.1760 171 LEU E CA  
12437 C C   . LEU E 171 ? 0.5876 1.2333 1.5700 0.3460  -0.1009 -0.1616 171 LEU E C   
12438 O O   . LEU E 171 ? 0.5842 1.2774 1.6152 0.3358  -0.1031 -0.1657 171 LEU E O   
12439 C CB  . LEU E 171 ? 0.5857 1.2124 1.5377 0.2986  -0.1371 -0.1973 171 LEU E CB  
12440 C CG  . LEU E 171 ? 0.6024 1.2370 1.5199 0.3088  -0.1690 -0.2008 171 LEU E CG  
12441 C CD1 . LEU E 171 ? 0.6037 1.2921 1.5699 0.3198  -0.1734 -0.1967 171 LEU E CD1 
12442 C CD2 . LEU E 171 ? 0.6086 1.2332 1.5008 0.2790  -0.1908 -0.2213 171 LEU E CD2 
12443 N N   . SER E 172 ? 0.5962 1.2175 1.5452 0.3722  -0.0851 -0.1410 172 SER E N   
12444 C CA  . SER E 172 ? 0.6098 1.2616 1.5773 0.3921  -0.0662 -0.1227 172 SER E CA  
12445 C C   . SER E 172 ? 0.5964 1.2828 1.6321 0.3727  -0.0390 -0.1172 172 SER E C   
12446 O O   . SER E 172 ? 0.5819 1.2531 1.6398 0.3488  -0.0314 -0.1239 172 SER E O   
12447 C CB  . SER E 172 ? 0.6350 1.2462 1.5435 0.4255  -0.0561 -0.1046 172 SER E CB  
12448 O OG  . SER E 172 ? 0.6557 1.2315 1.4988 0.4431  -0.0832 -0.1083 172 SER E OG  
12449 N N   . ASN E 173 ? 0.5924 1.3264 1.6624 0.3838  -0.0244 -0.1040 173 ASN E N   
12450 C CA  . ASN E 173 ? 0.5869 1.3559 1.7177 0.3693  0.0033  -0.0934 173 ASN E CA  
12451 C C   . ASN E 173 ? 0.5680 1.3610 1.7614 0.3280  -0.0031 -0.1088 173 ASN E C   
12452 O O   . ASN E 173 ? 0.5615 1.3448 1.7880 0.3069  0.0131  -0.1074 173 ASN E O   
12453 C CB  . ASN E 173 ? 0.5926 1.3205 1.7020 0.3767  0.0271  -0.0799 173 ASN E CB  
12454 C CG  . ASN E 173 ? 0.6174 1.3235 1.6688 0.4175  0.0353  -0.0651 173 ASN E CG  
12455 O OD1 . ASN E 173 ? 0.6331 1.3751 1.6988 0.4370  0.0549  -0.0515 173 ASN E OD1 
12456 N ND2 . ASN E 173 ? 0.6246 1.2720 1.6102 0.4305  0.0203  -0.0684 173 ASN E ND2 
12457 N N   . ASN E 174 ? 0.5746 1.3957 1.7837 0.3168  -0.0285 -0.1240 174 ASN E N   
12458 C CA  . ASN E 174 ? 0.5637 1.4169 1.8369 0.2787  -0.0362 -0.1386 174 ASN E CA  
12459 C C   . ASN E 174 ? 0.5682 1.4719 1.8625 0.2766  -0.0602 -0.1439 174 ASN E C   
12460 O O   . ASN E 174 ? 0.5751 1.4683 1.8237 0.2973  -0.0814 -0.1480 174 ASN E O   
12461 C CB  . ASN E 174 ? 0.5522 1.3643 1.8185 0.2543  -0.0479 -0.1630 174 ASN E CB  
12462 C CG  . ASN E 174 ? 0.5520 1.3223 1.7495 0.2704  -0.0673 -0.1737 174 ASN E CG  
12463 O OD1 . ASN E 174 ? 0.5584 1.2952 1.7044 0.2969  -0.0601 -0.1604 174 ASN E OD1 
12464 N ND2 . ASN E 174 ? 0.5547 1.3194 1.7372 0.2501  -0.0921 -0.1952 174 ASN E ND2 
12465 N N   . PRO E 175 ? 0.5567 1.5137 1.9195 0.2510  -0.0598 -0.1428 175 PRO E N   
12466 C CA  . PRO E 175 ? 0.5648 1.5771 1.9525 0.2505  -0.0820 -0.1424 175 PRO E CA  
12467 C C   . PRO E 175 ? 0.5634 1.5658 1.9382 0.2325  -0.1194 -0.1684 175 PRO E C   
12468 O O   . PRO E 175 ? 0.5630 1.5874 1.9825 0.1962  -0.1334 -0.1826 175 PRO E O   
12469 C CB  . PRO E 175 ? 0.5668 1.6357 2.0334 0.2222  -0.0689 -0.1320 175 PRO E CB  
12470 C CG  . PRO E 175 ? 0.5583 1.5888 2.0417 0.1941  -0.0545 -0.1411 175 PRO E CG  
12471 C CD  . PRO E 175 ? 0.5538 1.5244 1.9754 0.2225  -0.0381 -0.1372 175 PRO E CD  
12472 N N   . LEU E 176 ? 0.5828 1.5502 1.8939 0.2561  -0.1370 -0.1751 176 LEU E N   
12473 C CA  . LEU E 176 ? 0.5851 1.5426 1.8754 0.2416  -0.1737 -0.1989 176 LEU E CA  
12474 C C   . LEU E 176 ? 0.6023 1.6036 1.9003 0.2526  -0.1994 -0.1917 176 LEU E C   
12475 O O   . LEU E 176 ? 0.6117 1.6468 1.9256 0.2770  -0.1865 -0.1686 176 LEU E O   
12476 C CB  . LEU E 176 ? 0.5837 1.4795 1.7998 0.2579  -0.1806 -0.2082 176 LEU E CB  
12477 C CG  . LEU E 176 ? 0.5932 1.4484 1.7649 0.2278  -0.2006 -0.2317 176 LEU E CG  
12478 C CD1 . LEU E 176 ? 0.5903 1.4393 1.7966 0.1900  -0.1856 -0.2447 176 LEU E CD1 
12479 C CD2 . LEU E 176 ? 0.5958 1.3905 1.6916 0.2437  -0.1994 -0.2321 176 LEU E CD2 
12480 N N   . THR E 177 ? 0.5941 1.5959 1.8804 0.2349  -0.2362 -0.2113 177 THR E N   
12481 C CA  . THR E 177 ? 0.6148 1.6548 1.9076 0.2423  -0.2657 -0.2049 177 THR E CA  
12482 C C   . THR E 177 ? 0.6291 1.6325 1.8565 0.2493  -0.3022 -0.2193 177 THR E C   
12483 O O   . THR E 177 ? 0.6265 1.5812 1.8079 0.2341  -0.3067 -0.2371 177 THR E O   
12484 C CB  . THR E 177 ? 0.6207 1.7130 1.9779 0.2033  -0.2808 -0.2104 177 THR E CB  
12485 O OG1 . THR E 177 ? 0.6219 1.6885 1.9658 0.1661  -0.3032 -0.2400 177 THR E OG1 
12486 C CG2 . THR E 177 ? 0.6099 1.7373 2.0326 0.1895  -0.2474 -0.1965 177 THR E CG2 
12487 N N   . GLY E 178 ? 0.6826 1.7044 1.8976 0.2703  -0.3261 -0.2079 178 GLY E N   
12488 C CA  . GLY E 178 ? 0.7050 1.6933 1.8569 0.2763  -0.3650 -0.2177 178 GLY E CA  
12489 C C   . GLY E 178 ? 0.7192 1.6633 1.8079 0.3203  -0.3620 -0.2047 178 GLY E C   
12490 O O   . GLY E 178 ? 0.7138 1.6523 1.8042 0.3480  -0.3290 -0.1884 178 GLY E O   
12491 N N   . ASP E 179 ? 0.7793 1.6875 1.8056 0.3245  -0.3987 -0.2117 179 ASP E N   
12492 C CA  . ASP E 179 ? 0.8033 1.6585 1.7581 0.3616  -0.4046 -0.2014 179 ASP E CA  
12493 C C   . ASP E 179 ? 0.7919 1.5910 1.6916 0.3544  -0.4015 -0.2134 179 ASP E C   
12494 O O   . ASP E 179 ? 0.8082 1.5917 1.6940 0.3134  -0.4012 -0.2281 179 ASP E O   
12495 C CB  . ASP E 179 ? 0.8470 1.6899 1.7605 0.3703  -0.4487 -0.1982 179 ASP E CB  
12496 C CG  . ASP E 179 ? 0.8699 1.7515 1.8188 0.4000  -0.4465 -0.1778 179 ASP E CG  
12497 O OD1 . ASP E 179 ? 0.8493 1.7899 1.8730 0.3969  -0.4206 -0.1700 179 ASP E OD1 
12498 O OD2 . ASP E 179 ? 0.9118 1.7647 1.8138 0.4259  -0.4705 -0.1689 179 ASP E OD2 
12499 N N   . ILE E 180 ? 0.8524 1.6047 1.7005 0.3869  -0.3900 -0.2011 180 ILE E N   
12500 C CA  . ILE E 180 ? 0.8688 1.5593 1.6535 0.3784  -0.3823 -0.2046 180 ILE E CA  
12501 C C   . ILE E 180 ? 0.9239 1.5692 1.6329 0.3589  -0.4200 -0.2113 180 ILE E C   
12502 O O   . ILE E 180 ? 0.9499 1.5749 1.6177 0.3819  -0.4519 -0.2042 180 ILE E O   
12503 C CB  . ILE E 180 ? 0.8597 1.5155 1.6132 0.4199  -0.3642 -0.1897 180 ILE E CB  
12504 C CG1 . ILE E 180 ? 0.8898 1.5318 1.6116 0.4546  -0.3778 -0.1743 180 ILE E CG1 
12505 C CG2 . ILE E 180 ? 0.8178 1.4990 1.6249 0.4225  -0.3170 -0.1821 180 ILE E CG2 
12506 C CD1 . ILE E 180 ? 0.9073 1.5057 1.5870 0.4896  -0.3541 -0.1583 180 ILE E CD1 
12507 N N   . PRO E 181 ? 0.9046 1.5325 1.5919 0.3173  -0.4177 -0.2246 181 PRO E N   
12508 C CA  . PRO E 181 ? 0.9602 1.5450 1.5703 0.2965  -0.4502 -0.2293 181 PRO E CA  
12509 C C   . PRO E 181 ? 0.9822 1.5040 1.5170 0.3147  -0.4544 -0.2169 181 PRO E C   
12510 O O   . PRO E 181 ? 0.9702 1.4759 1.5072 0.3283  -0.4259 -0.2102 181 PRO E O   
12511 C CB  . PRO E 181 ? 0.9732 1.5631 1.5895 0.2500  -0.4359 -0.2477 181 PRO E CB  
12512 C CG  . PRO E 181 ? 0.9292 1.5701 1.6327 0.2453  -0.4069 -0.2541 181 PRO E CG  
12513 C CD  . PRO E 181 ? 0.8885 1.5387 1.6233 0.2866  -0.3864 -0.2369 181 PRO E CD  
12514 N N   . VAL E 182 ? 1.0405 1.5241 1.5061 0.3144  -0.4931 -0.2124 182 VAL E N   
12515 C CA  . VAL E 182 ? 1.0718 1.4890 1.4558 0.3237  -0.5044 -0.2005 182 VAL E CA  
12516 C C   . VAL E 182 ? 1.1042 1.4923 1.4239 0.2824  -0.5290 -0.2059 182 VAL E C   
12517 O O   . VAL E 182 ? 1.1236 1.4572 1.3659 0.2838  -0.5565 -0.1950 182 VAL E O   
12518 C CB  . VAL E 182 ? 1.0684 1.4571 1.4220 0.3699  -0.5292 -0.1860 182 VAL E CB  
12519 C CG1 . VAL E 182 ? 1.0911 1.4074 1.3661 0.3839  -0.5346 -0.1729 182 VAL E CG1 
12520 C CG2 . VAL E 182 ? 1.0263 1.4638 1.4560 0.4085  -0.5067 -0.1835 182 VAL E CG2 
12521 N N   . ASN E 183 ? 1.0599 1.4823 1.4079 0.2442  -0.5194 -0.2227 183 ASN E N   
12522 C CA  . ASN E 183 ? 1.0894 1.4959 1.3818 0.2068  -0.5476 -0.2293 183 ASN E CA  
12523 C C   . ASN E 183 ? 1.1097 1.4728 1.3344 0.1836  -0.5447 -0.2248 183 ASN E C   
12524 O O   . ASN E 183 ? 1.1339 1.4512 1.2837 0.1801  -0.5770 -0.2126 183 ASN E O   
12525 C CB  . ASN E 183 ? 1.0824 1.5364 1.4222 0.1738  -0.5364 -0.2507 183 ASN E CB  
12526 C CG  . ASN E 183 ? 1.1115 1.5550 1.3968 0.1381  -0.5693 -0.2583 183 ASN E CG  
12527 O OD1 . ASN E 183 ? 1.1343 1.5370 1.3488 0.1379  -0.6027 -0.2460 183 ASN E OD1 
12528 N ND2 . ASN E 183 ? 1.1126 1.5889 1.4262 0.1064  -0.5605 -0.2786 183 ASN E ND2 
12529 N N   . GLY E 184 ? 1.1248 1.5020 1.3752 0.1668  -0.5077 -0.2333 184 GLY E N   
12530 C CA  . GLY E 184 ? 1.1371 1.4843 1.3311 0.1417  -0.5047 -0.2290 184 GLY E CA  
12531 C C   . GLY E 184 ? 1.1463 1.4688 1.3347 0.1587  -0.4848 -0.2148 184 GLY E C   
12532 O O   . GLY E 184 ? 1.1639 1.4448 1.2878 0.1511  -0.5004 -0.2003 184 GLY E O   
12533 N N   . SER E 185 ? 1.1230 1.4695 1.3775 0.1801  -0.4521 -0.2175 185 SER E N   
12534 C CA  . SER E 185 ? 1.1150 1.4429 1.3724 0.1940  -0.4296 -0.2055 185 SER E CA  
12535 C C   . SER E 185 ? 1.0929 1.4165 1.3806 0.2367  -0.4205 -0.1952 185 SER E C   
12536 O O   . SER E 185 ? 1.0860 1.3798 1.3556 0.2526  -0.4118 -0.1810 185 SER E O   
12537 C CB  . SER E 185 ? 1.1037 1.4632 1.4097 0.1736  -0.3919 -0.2185 185 SER E CB  
12538 O OG  . SER E 185 ? 1.0963 1.4433 1.4176 0.1907  -0.3697 -0.2064 185 SER E OG  
12539 N N   . PHE E 186 ? 1.1180 1.3074 1.5720 0.4889  -0.5457 0.0041  186 PHE E N   
12540 C CA  . PHE E 186 ? 1.1185 1.2886 1.5720 0.4862  -0.5444 0.0040  186 PHE E CA  
12541 C C   . PHE E 186 ? 1.1164 1.2829 1.5812 0.4860  -0.5392 0.0141  186 PHE E C   
12542 O O   . PHE E 186 ? 1.1177 1.2716 1.5823 0.4855  -0.5374 0.0146  186 PHE E O   
12543 C CB  . PHE E 186 ? 1.1202 1.2934 1.5697 0.4849  -0.5480 0.0037  186 PHE E CB  
12544 C CG  . PHE E 186 ? 1.1254 1.2938 1.5656 0.4844  -0.5551 -0.0081 186 PHE E CG  
12545 C CD1 . PHE E 186 ? 1.1282 1.3014 1.5633 0.4873  -0.5582 -0.0170 186 PHE E CD1 
12546 C CD2 . PHE E 186 ? 1.1284 1.2884 1.5671 0.4814  -0.5592 -0.0094 186 PHE E CD2 
12547 C CE1 . PHE E 186 ? 1.1349 1.3020 1.5633 0.4876  -0.5655 -0.0287 186 PHE E CE1 
12548 C CE2 . PHE E 186 ? 1.1348 1.2886 1.5686 0.4806  -0.5672 -0.0195 186 PHE E CE2 
12549 C CZ  . PHE E 186 ? 1.1386 1.2947 1.5672 0.4839  -0.5706 -0.0300 186 PHE E CZ  
12550 N N   . SER E 187 ? 1.1367 1.3152 1.6125 0.4869  -0.5371 0.0225  187 SER E N   
12551 C CA  . SER E 187 ? 1.1369 1.3102 1.6266 0.4868  -0.5334 0.0319  187 SER E CA  
12552 C C   . SER E 187 ? 1.1408 1.2910 1.6305 0.4867  -0.5331 0.0248  187 SER E C   
12553 O O   . SER E 187 ? 1.1441 1.2834 1.6398 0.4878  -0.5311 0.0270  187 SER E O   
12554 C CB  . SER E 187 ? 1.1346 1.3263 1.6393 0.4871  -0.5325 0.0440  187 SER E CB  
12555 O OG  . SER E 187 ? 1.1341 1.3311 1.6374 0.4873  -0.5345 0.0402  187 SER E OG  
12556 N N   . LEU E 188 ? 1.1030 1.2466 1.5859 0.4861  -0.5354 0.0156  188 LEU E N   
12557 C CA  . LEU E 188 ? 1.1073 1.2313 1.5890 0.4863  -0.5360 0.0079  188 LEU E CA  
12558 C C   . LEU E 188 ? 1.1095 1.2218 1.5775 0.4872  -0.5362 -0.0007 188 LEU E C   
12559 O O   . LEU E 188 ? 1.1137 1.2123 1.5790 0.4885  -0.5367 -0.0074 188 LEU E O   
12560 C CB  . LEU E 188 ? 1.1071 1.2315 1.5893 0.4853  -0.5385 0.0036  188 LEU E CB  
12561 C CG  . LEU E 188 ? 1.1048 1.2449 1.6014 0.4845  -0.5389 0.0136  188 LEU E CG  
12562 C CD1 . LEU E 188 ? 1.1005 1.2638 1.5920 0.4857  -0.5388 0.0168  188 LEU E CD1 
12563 C CD2 . LEU E 188 ? 1.1071 1.2401 1.6091 0.4832  -0.5416 0.0102  188 LEU E CD2 
12564 N N   . PHE E 189 ? 1.1075 1.2264 1.5683 0.4865  -0.5366 0.0001  189 PHE E N   
12565 C CA  . PHE E 189 ? 1.1095 1.2203 1.5603 0.4865  -0.5376 -0.0051 189 PHE E CA  
12566 C C   . PHE E 189 ? 1.1117 1.2196 1.5644 0.4889  -0.5344 -0.0003 189 PHE E C   
12567 O O   . PHE E 189 ? 1.1107 1.2254 1.5712 0.4899  -0.5320 0.0076  189 PHE E O   
12568 C CB  . PHE E 189 ? 1.1082 1.2267 1.5530 0.4842  -0.5413 -0.0064 189 PHE E CB  
12569 C CG  . PHE E 189 ? 1.1085 1.2287 1.5490 0.4838  -0.5448 -0.0138 189 PHE E CG  
12570 C CD1 . PHE E 189 ? 1.1086 1.2241 1.5502 0.4846  -0.5440 -0.0175 189 PHE E CD1 
12571 C CD2 . PHE E 189 ? 1.1099 1.2371 1.5459 0.4832  -0.5496 -0.0176 189 PHE E CD2 
12572 C CE1 . PHE E 189 ? 1.1091 1.2282 1.5469 0.4851  -0.5467 -0.0236 189 PHE E CE1 
12573 C CE2 . PHE E 189 ? 1.1118 1.2414 1.5435 0.4845  -0.5528 -0.0255 189 PHE E CE2 
12574 C CZ  . PHE E 189 ? 1.1109 1.2372 1.5433 0.4856  -0.5508 -0.0279 189 PHE E CZ  
12575 N N   . THR E 190 ? 1.1149 1.2151 1.5611 0.4906  -0.5344 -0.0044 190 THR E N   
12576 C CA  . THR E 190 ? 1.1185 1.2178 1.5649 0.4950  -0.5313 -0.0010 190 THR E CA  
12577 C C   . THR E 190 ? 1.1178 1.2227 1.5592 0.4938  -0.5323 0.0031  190 THR E C   
12578 O O   . THR E 190 ? 1.1164 1.2209 1.5540 0.4896  -0.5362 0.0007  190 THR E O   
12579 C CB  . THR E 190 ? 1.1249 1.2138 1.5690 0.5002  -0.5308 -0.0088 190 THR E CB  
12580 O OG1 . THR E 190 ? 1.1263 1.2139 1.5613 0.5006  -0.5323 -0.0127 190 THR E OG1 
12581 C CG2 . THR E 190 ? 1.1257 1.2073 1.5748 0.4988  -0.5328 -0.0143 190 THR E CG2 
12582 N N   . PRO E 191 ? 1.1196 1.2305 1.5626 0.4974  -0.5292 0.0100  191 PRO E N   
12583 C CA  . PRO E 191 ? 1.1188 1.2380 1.5606 0.4953  -0.5308 0.0173  191 PRO E CA  
12584 C C   . PRO E 191 ? 1.1208 1.2370 1.5573 0.4942  -0.5337 0.0146  191 PRO E C   
12585 O O   . PRO E 191 ? 1.1205 1.2432 1.5592 0.4909  -0.5366 0.0219  191 PRO E O   
12586 C CB  . PRO E 191 ? 1.1216 1.2487 1.5661 0.5018  -0.5259 0.0249  191 PRO E CB  
12587 C CG  . PRO E 191 ? 1.1221 1.2460 1.5720 0.5046  -0.5229 0.0236  191 PRO E CG  
12588 C CD  . PRO E 191 ? 1.1228 1.2347 1.5713 0.5034  -0.5248 0.0131  191 PRO E CD  
12589 N N   . ILE E 192 ? 1.1233 1.2309 1.5547 0.4966  -0.5337 0.0055  192 ILE E N   
12590 C CA  . ILE E 192 ? 1.1250 1.2316 1.5526 0.4955  -0.5365 0.0044  192 ILE E CA  
12591 C C   . ILE E 192 ? 1.1226 1.2250 1.5518 0.4878  -0.5424 0.0027  192 ILE E C   
12592 O O   . ILE E 192 ? 1.1243 1.2272 1.5546 0.4849  -0.5461 0.0057  192 ILE E O   
12593 C CB  . ILE E 192 ? 1.1289 1.2289 1.5505 0.5006  -0.5355 -0.0050 192 ILE E CB  
12594 C CG1 . ILE E 192 ? 1.1311 1.2340 1.5493 0.5006  -0.5376 -0.0036 192 ILE E CG1 
12595 C CG2 . ILE E 192 ? 1.1271 1.2167 1.5488 0.4977  -0.5371 -0.0142 192 ILE E CG2 
12596 C CD1 . ILE E 192 ? 1.1322 1.2491 1.5534 0.5020  -0.5369 0.0092  192 ILE E CD1 
12597 N N   . SER E 193 ? 1.1199 1.2193 1.5503 0.4851  -0.5437 -0.0020 193 SER E N   
12598 C CA  . SER E 193 ? 1.1198 1.2167 1.5509 0.4799  -0.5498 -0.0058 193 SER E CA  
12599 C C   . SER E 193 ? 1.1209 1.2236 1.5576 0.4757  -0.5547 0.0014  193 SER E C   
12600 O O   . SER E 193 ? 1.1242 1.2229 1.5629 0.4719  -0.5618 -0.0016 193 SER E O   
12601 C CB  . SER E 193 ? 1.1174 1.2148 1.5480 0.4799  -0.5497 -0.0117 193 SER E CB  
12602 O OG  . SER E 193 ? 1.1169 1.2093 1.5453 0.4829  -0.5463 -0.0167 193 SER E OG  
12603 N N   . PHE E 194 ? 1.1194 1.2310 1.5598 0.4766  -0.5518 0.0107  194 PHE E N   
12604 C CA  . PHE E 194 ? 1.1204 1.2392 1.5677 0.4722  -0.5569 0.0185  194 PHE E CA  
12605 C C   . PHE E 194 ? 1.1214 1.2482 1.5735 0.4729  -0.5551 0.0313  194 PHE E C   
12606 O O   . PHE E 194 ? 1.1212 1.2576 1.5799 0.4706  -0.5567 0.0409  194 PHE E O   
12607 C CB  . PHE E 194 ? 1.1175 1.2445 1.5666 0.4723  -0.5560 0.0200  194 PHE E CB  
12608 C CG  . PHE E 194 ? 1.1159 1.2407 1.5608 0.4737  -0.5556 0.0103  194 PHE E CG  
12609 C CD1 . PHE E 194 ? 1.1133 1.2359 1.5559 0.4780  -0.5487 0.0084  194 PHE E CD1 
12610 C CD2 . PHE E 194 ? 1.1183 1.2447 1.5626 0.4714  -0.5628 0.0034  194 PHE E CD2 
12611 C CE1 . PHE E 194 ? 1.1117 1.2354 1.5530 0.4789  -0.5485 0.0025  194 PHE E CE1 
12612 C CE2 . PHE E 194 ? 1.1170 1.2462 1.5577 0.4738  -0.5620 -0.0038 194 PHE E CE2 
12613 C CZ  . PHE E 194 ? 1.1130 1.2417 1.5529 0.4771  -0.5546 -0.0029 194 PHE E CZ  
12614 N N   . ALA E 195 ? 1.1228 1.2486 1.5719 0.4765  -0.5518 0.0324  195 ALA E N   
12615 C CA  . ALA E 195 ? 1.1242 1.2624 1.5774 0.4791  -0.5493 0.0456  195 ALA E CA  
12616 C C   . ALA E 195 ? 1.1268 1.2693 1.5913 0.4715  -0.5573 0.0562  195 ALA E C   
12617 O O   . ALA E 195 ? 1.1295 1.2618 1.5974 0.4655  -0.5650 0.0508  195 ALA E O   
12618 C CB  . ALA E 195 ? 1.1264 1.2652 1.5732 0.4857  -0.5449 0.0435  195 ALA E CB  
12619 N N   . ASN E 196 ? 1.1270 1.2852 1.5988 0.4722  -0.5559 0.0716  196 ASN E N   
12620 C CA  . ASN E 196 ? 1.1302 1.2954 1.6164 0.4645  -0.5637 0.0854  196 ASN E CA  
12621 C C   . ASN E 196 ? 1.1321 1.2891 1.6254 0.4557  -0.5736 0.0811  196 ASN E C   
12622 O O   . ASN E 196 ? 1.1374 1.2923 1.6434 0.4478  -0.5835 0.0869  196 ASN E O   
12623 C CB  . ASN E 196 ? 1.1340 1.2970 1.6247 0.4626  -0.5672 0.0890  196 ASN E CB  
12624 C CG  . ASN E 196 ? 1.1373 1.3155 1.6449 0.4575  -0.5719 0.1100  196 ASN E CG  
12625 O OD1 . ASN E 196 ? 1.1423 1.3134 1.6633 0.4480  -0.5824 0.1135  196 ASN E OD1 
12626 N ND2 . ASN E 196 ? 1.1359 1.3358 1.6439 0.4643  -0.5646 0.1244  196 ASN E ND2 
12627 N N   . THR E 197 ? 1.1291 1.2823 1.6153 0.4572  -0.5719 0.0709  197 THR E N   
12628 C CA  . THR E 197 ? 1.1318 1.2807 1.6226 0.4510  -0.5814 0.0651  197 THR E CA  
12629 C C   . THR E 197 ? 1.1274 1.2869 1.6161 0.4533  -0.5771 0.0676  197 THR E C   
12630 O O   . THR E 197 ? 1.1225 1.2836 1.6025 0.4601  -0.5675 0.0644  197 THR E O   
12631 C CB  . THR E 197 ? 1.1342 1.2677 1.6176 0.4510  -0.5858 0.0467  197 THR E CB  
12632 O OG1 . THR E 197 ? 1.1286 1.2623 1.6004 0.4572  -0.5774 0.0383  197 THR E OG1 
12633 C CG2 . THR E 197 ? 1.1374 1.2600 1.6205 0.4508  -0.5872 0.0431  197 THR E CG2 
12634 N N   . LYS E 198 ? 1.1301 1.2968 1.6285 0.4473  -0.5850 0.0737  198 LYS E N   
12635 C CA  . LYS E 198 ? 1.1272 1.3041 1.6248 0.4481  -0.5840 0.0744  198 LYS E CA  
12636 C C   . LYS E 198 ? 1.1209 1.3098 1.6161 0.4549  -0.5714 0.0850  198 LYS E C   
12637 O O   . LYS E 198 ? 1.1205 1.3154 1.6185 0.4575  -0.5664 0.0960  198 LYS E O   
12638 C CB  . LYS E 198 ? 1.1273 1.2974 1.6157 0.4501  -0.5859 0.0576  198 LYS E CB  
12639 C CG  . LYS E 198 ? 1.1343 1.2899 1.6214 0.4474  -0.5957 0.0436  198 LYS E CG  
12640 C CD  . LYS E 198 ? 1.1346 1.2903 1.6127 0.4509  -0.5971 0.0288  198 LYS E CD  
12641 C CE  . LYS E 198 ? 1.1262 1.2851 1.5953 0.4576  -0.5840 0.0285  198 LYS E CE  
12642 N NZ  . LYS E 198 ? 1.1231 1.2729 1.5893 0.4603  -0.5757 0.0310  198 LYS E NZ  
12643 N N   . LEU E 199 ? 1.1170 1.3107 1.6077 0.4586  -0.5666 0.0820  199 LEU E N   
12644 C CA  . LEU E 199 ? 1.1127 1.3150 1.6020 0.4659  -0.5553 0.0897  199 LEU E CA  
12645 C C   . LEU E 199 ? 1.1094 1.3111 1.5939 0.4694  -0.5512 0.0824  199 LEU E C   
12646 O O   . LEU E 199 ? 1.1076 1.3063 1.5888 0.4762  -0.5424 0.0813  199 LEU E O   
12647 C CB  . LEU E 199 ? 1.1123 1.3322 1.6113 0.4645  -0.5552 0.1064  199 LEU E CB  
12648 C CG  . LEU E 199 ? 1.1105 1.3396 1.6094 0.4737  -0.5438 0.1161  199 LEU E CG  
12649 C CD1 . LEU E 199 ? 1.1129 1.3394 1.6089 0.4783  -0.5402 0.1175  199 LEU E CD1 
12650 C CD2 . LEU E 199 ? 1.1096 1.3583 1.6185 0.4726  -0.5437 0.1327  199 LEU E CD2 
12651 N N   . GLU F 1   ? 0.3273 0.8629 1.1450 0.0130  -0.0474 -0.2558 1   GLU F N   
12652 C CA  . GLU F 1   ? 0.3279 0.8536 1.1761 -0.0288 -0.0375 -0.2063 1   GLU F CA  
12653 C C   . GLU F 1   ? 0.3310 0.7812 1.1685 -0.0300 -0.0358 -0.1708 1   GLU F C   
12654 O O   . GLU F 1   ? 0.3347 0.7672 1.1799 -0.0578 -0.0281 -0.1249 1   GLU F O   
12655 C CB  . GLU F 1   ? 0.3150 0.8851 1.1209 -0.0313 -0.0251 -0.1833 1   GLU F CB  
12656 C CG  . GLU F 1   ? 0.3240 0.9629 1.1482 -0.0485 -0.0221 -0.1980 1   GLU F CG  
12657 C CD  . GLU F 1   ? 0.3349 1.0001 1.1390 -0.0187 -0.0325 -0.2495 1   GLU F CD  
12658 O OE1 . GLU F 1   ? 0.3334 0.9697 1.1066 0.0174  -0.0416 -0.2762 1   GLU F OE1 
12659 O OE2 . GLU F 1   ? 0.3494 1.0629 1.1667 -0.0317 -0.0312 -0.2619 1   GLU F OE2 
12660 N N   . SER F 2   ? 0.3315 0.7403 1.1502 0.0016  -0.0429 -0.1928 2   SER F N   
12661 C CA  . SER F 2   ? 0.3328 0.6732 1.1372 0.0087  -0.0417 -0.1666 2   SER F CA  
12662 C C   . SER F 2   ? 0.3176 0.6482 1.0587 0.0192  -0.0312 -0.1314 2   SER F C   
12663 O O   . SER F 2   ? 0.3112 0.6792 1.0366 0.0047  -0.0240 -0.1115 2   SER F O   
12664 C CB  . SER F 2   ? 0.3510 0.6554 1.2222 -0.0299 -0.0439 -0.1392 2   SER F CB  
12665 O OG  . SER F 2   ? 0.3528 0.5947 1.2137 -0.0217 -0.0437 -0.1149 2   SER F OG  
12666 N N   . SER F 3   ? 0.3132 0.5956 1.0178 0.0443  -0.0297 -0.1250 3   SER F N   
12667 C CA  . SER F 3   ? 0.3008 0.5732 0.9482 0.0532  -0.0204 -0.0942 3   SER F CA  
12668 C C   . SER F 3   ? 0.3032 0.5227 0.9585 0.0410  -0.0191 -0.0544 3   SER F C   
12669 O O   . SER F 3   ? 0.3022 0.5261 0.9533 0.0187  -0.0151 -0.0161 3   SER F O   
12670 C CB  . SER F 3   ? 0.2933 0.5628 0.8763 0.0980  -0.0169 -0.1213 3   SER F CB  
12671 O OG  . SER F 3   ? 0.3012 0.5314 0.8923 0.1194  -0.0214 -0.1441 3   SER F OG  
12672 N N   . SER F 4   ? 0.3085 0.4805 0.9767 0.0555  -0.0228 -0.0631 4   SER F N   
12673 C CA  . SER F 4   ? 0.3080 0.4313 0.9717 0.0550  -0.0209 -0.0311 4   SER F CA  
12674 C C   . SER F 4   ? 0.2943 0.4231 0.8955 0.0662  -0.0121 -0.0110 4   SER F C   
12675 O O   . SER F 4   ? 0.2937 0.4217 0.8933 0.0454  -0.0110 0.0266  4   SER F O   
12676 C CB  . SER F 4   ? 0.3215 0.4266 1.0419 0.0182  -0.0261 0.0046  4   SER F CB  
12677 O OG  . SER F 4   ? 0.3195 0.3912 1.0273 0.0164  -0.0247 0.0408  4   SER F OG  
12678 N N   . SER F 5   ? 0.2869 0.4218 0.8349 0.1000  -0.0061 -0.0375 5   SER F N   
12679 C CA  . SER F 5   ? 0.2774 0.4192 0.7638 0.1126  0.0029  -0.0248 5   SER F CA  
12680 C C   . SER F 5   ? 0.2753 0.3807 0.7588 0.1035  0.0047  0.0113  5   SER F C   
12681 O O   . SER F 5   ? 0.2798 0.3468 0.7960 0.1015  0.0012  0.0186  5   SER F O   
12682 C CB  . SER F 5   ? 0.2800 0.4153 0.7050 0.1512  0.0097  -0.0563 5   SER F CB  
12683 O OG  . SER F 5   ? 0.3022 0.3937 0.7031 0.1573  0.0088  -0.0678 5   SER F OG  
12684 N N   . HIS F 6   ? 0.2698 0.3892 0.7137 0.0993  0.0096  0.0320  6   HIS F N   
12685 C CA  . HIS F 6   ? 0.2697 0.3672 0.7144 0.0843  0.0085  0.0689  6   HIS F CA  
12686 C C   . HIS F 6   ? 0.2647 0.3417 0.6569 0.1073  0.0171  0.0673  6   HIS F C   
12687 O O   . HIS F 6   ? 0.2623 0.3591 0.6040 0.1219  0.0245  0.0554  6   HIS F O   
12688 C CB  . HIS F 6   ? 0.2729 0.4041 0.7189 0.0556  0.0059  0.0980  6   HIS F CB  
12689 C CG  . HIS F 6   ? 0.2785 0.3893 0.7385 0.0362  0.0004  0.1377  6   HIS F CG  
12690 N ND1 . HIS F 6   ? 0.2761 0.3841 0.6947 0.0398  0.0029  0.1540  6   HIS F ND1 
12691 C CD2 . HIS F 6   ? 0.2896 0.3814 0.8001 0.0143  -0.0084 0.1636  6   HIS F CD2 
12692 C CE1 . HIS F 6   ? 0.2842 0.3760 0.7271 0.0215  -0.0053 0.1877  6   HIS F CE1 
12693 N NE2 . HIS F 6   ? 0.2931 0.3738 0.7907 0.0066  -0.0120 0.1953  6   HIS F NE2 
12694 N N   . SER F 7   ? 0.2668 0.3035 0.6690 0.1084  0.0165  0.0782  7   SER F N   
12695 C CA  . SER F 7   ? 0.2709 0.2859 0.6133 0.1157  0.0235  0.0777  7   SER F CA  
12696 C C   . SER F 7   ? 0.2635 0.2918 0.6159 0.1032  0.0204  0.1142  7   SER F C   
12697 O O   . SER F 7   ? 0.2662 0.2935 0.6593 0.0809  0.0101  0.1425  7   SER F O   
12698 C CB  . SER F 7   ? 0.2828 0.2612 0.6118 0.1109  0.0231  0.0688  7   SER F CB  
12699 O OG  . SER F 7   ? 0.2842 0.2483 0.5689 0.1137  0.0282  0.0696  7   SER F OG  
12700 N N   . GLU F 8   ? 0.2621 0.3012 0.5632 0.1140  0.0281  0.1111  8   GLU F N   
12701 C CA  . GLU F 8   ? 0.2650 0.3208 0.5470 0.0969  0.0240  0.1364  8   GLU F CA  
12702 C C   . GLU F 8   ? 0.2660 0.2922 0.5349 0.1020  0.0262  0.1449  8   GLU F C   
12703 O O   . GLU F 8   ? 0.2702 0.2715 0.5030 0.1162  0.0359  0.1186  8   GLU F O   
12704 C CB  . GLU F 8   ? 0.2669 0.3581 0.4995 0.1027  0.0302  0.1252  8   GLU F CB  
12705 C CG  . GLU F 8   ? 0.2655 0.3908 0.5132 0.0990  0.0291  0.1126  8   GLU F CG  
12706 C CD  . GLU F 8   ? 0.2700 0.4407 0.5016 0.0818  0.0277  0.1257  8   GLU F CD  
12707 O OE1 . GLU F 8   ? 0.2740 0.4537 0.4592 0.0870  0.0321  0.1282  8   GLU F OE1 
12708 O OE2 . GLU F 8   ? 0.2718 0.4688 0.5382 0.0625  0.0232  0.1333  8   GLU F OE2 
12709 N N   . ARG F 9   ? 0.2700 0.3002 0.5534 0.0814  0.0157  0.1742  9   ARG F N   
12710 C CA  . ARG F 9   ? 0.2742 0.2835 0.5448 0.0773  0.0153  0.1756  9   ARG F CA  
12711 C C   . ARG F 9   ? 0.2759 0.2798 0.4947 0.0955  0.0270  0.1615  9   ARG F C   
12712 O O   . ARG F 9   ? 0.2775 0.3025 0.4602 0.1049  0.0328  0.1542  9   ARG F O   
12713 C CB  . ARG F 9   ? 0.2812 0.3060 0.5692 0.0542  0.0004  0.2076  9   ARG F CB  
12714 C CG  . ARG F 9   ? 0.2854 0.3144 0.6217 0.0358  -0.0103 0.2223  9   ARG F CG  
12715 C CD  . ARG F 9   ? 0.2979 0.3435 0.6422 0.0156  -0.0244 0.2491  9   ARG F CD  
12716 N NE  . ARG F 9   ? 0.3081 0.3740 0.6735 -0.0005 -0.0321 0.2736  9   ARG F NE  
12717 C CZ  . ARG F 9   ? 0.3164 0.4104 0.6569 -0.0091 -0.0330 0.2941  9   ARG F CZ  
12718 N NH1 . ARG F 9   ? 0.3151 0.4224 0.6073 -0.0012 -0.0283 0.2926  9   ARG F NH1 
12719 N NH2 . ARG F 9   ? 0.3292 0.4404 0.6907 -0.0267 -0.0374 0.3146  9   ARG F NH2 
12720 N N   . ALA F 10  ? 0.2798 0.2593 0.4865 0.0946  0.0307  0.1494  10  ALA F N   
12721 C CA  . ALA F 10  ? 0.2859 0.2530 0.4469 0.1091  0.0426  0.1350  10  ALA F CA  
12722 C C   . ALA F 10  ? 0.2918 0.2773 0.4367 0.1061  0.0373  0.1590  10  ALA F C   
12723 O O   . ALA F 10  ? 0.2927 0.3040 0.4543 0.0864  0.0222  0.1818  10  ALA F O   
12724 C CB  . ALA F 10  ? 0.2891 0.2290 0.4478 0.1059  0.0470  0.1175  10  ALA F CB  
12725 N N   . GLY F 11  ? 0.3020 0.2762 0.4018 0.1177  0.0483  0.1445  11  GLY F N   
12726 C CA  . GLY F 11  ? 0.3137 0.3087 0.3795 0.1079  0.0424  0.1505  11  GLY F CA  
12727 C C   . GLY F 11  ? 0.3191 0.3064 0.4036 0.0931  0.0322  0.1642  11  GLY F C   
12728 O O   . GLY F 11  ? 0.3171 0.2747 0.4255 0.0967  0.0373  0.1602  11  GLY F O   
12729 N N   . GLY F 12  ? 0.3279 0.3451 0.4016 0.0767  0.0177  0.1800  12  GLY F N   
12730 C CA  . GLY F 12  ? 0.3372 0.3542 0.4209 0.0637  0.0054  0.1904  12  GLY F CA  
12731 C C   . GLY F 12  ? 0.3552 0.3712 0.3881 0.0678  0.0111  0.1738  12  GLY F C   
12732 O O   . GLY F 12  ? 0.3620 0.3845 0.3496 0.0789  0.0216  0.1593  12  GLY F O   
12733 N N   . ARG F 13  ? 0.3705 0.3784 0.4133 0.0591  0.0035  0.1746  13  ARG F N   
12734 C CA  . ARG F 13  ? 0.3912 0.3935 0.3905 0.0615  0.0083  0.1566  13  ARG F CA  
12735 C C   . ARG F 13  ? 0.4073 0.4479 0.3855 0.0470  -0.0112 0.1685  13  ARG F C   
12736 O O   . ARG F 13  ? 0.4054 0.4785 0.3791 0.0408  -0.0204 0.1861  13  ARG F O   
12737 C CB  . ARG F 13  ? 0.3960 0.3651 0.4175 0.0608  0.0142  0.1451  13  ARG F CB  
12738 C CG  . ARG F 13  ? 0.4213 0.3833 0.4056 0.0591  0.0164  0.1270  13  ARG F CG  
12739 C CD  . ARG F 13  ? 0.4269 0.3528 0.4371 0.0580  0.0268  0.1140  13  ARG F CD  
12740 N NE  . ARG F 13  ? 0.4264 0.3109 0.4248 0.0768  0.0544  0.0988  13  ARG F NE  
12741 C CZ  . ARG F 13  ? 0.4492 0.2998 0.4132 0.0862  0.0735  0.0776  13  ARG F CZ  
12742 N NH1 . ARG F 13  ? 0.4732 0.3250 0.4143 0.0774  0.0683  0.0662  13  ARG F NH1 
12743 N NH2 . ARG F 13  ? 0.4515 0.2647 0.4028 0.1054  0.0984  0.0674  13  ARG F NH2 
# 
